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Human Metabolome Database Version 2.5

 

Showing metabocard for Guanosine diphosphate (HMDB01201)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-23 12:05:30
Accession Number HMDB01201
Secondary Accession Numbers Not Available
Common Name Guanosine diphosphate
Description Guanosine 5'-(trihydrogen diphosphate). A guanine nucleotide containing two phosphate groups esterified to the sugar moiety. It is an ester of pyrophosphoric acid with the nucleoside guanosine. GDP consists of the pyrophosphate group, the pentose sugar ribose, and the nucleobase guanine. GDP is the product of GTP dephosphorylation by GTPases, e.g. the G-proteins that are involved in signal transduction.
Synonyms
  1. 5'-GDP
  2. Guanosine 5'-(trihydrogen pyrophosphate)
  3. Guanosine 5'-diphosphate
  4. Guanosine 5'-pyrophosphate
  5. GDP
  6. Guanosine mono(trihydrogen diphosphate)
  7. Guanosine pyrophosphate
  8. guanosine-5'-diphosphate
  9. guanosine-diphosphate
  10. ppG
Chemical IUPAC Name [[5-(2-amino-6-oxo-3H-purin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxyphosphonic acid
Chemical Formula C10H15N5O11P2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide diphosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-diol
  • primary amine
  • primary aromatic amine
  • oxo(het)arene
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Fructose and mannose metabolism
Application
Source
  • Endogenous
Average Molecular Weight 443.201
Monoisotopic Molecular Weight 443.024323
Isomeric SMILES NC1=NC2=C(N=CN2[C@@H]2O[C@H](COP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]2O)C(=O)N1
Canonical SMILES NC1=NC2=C(N=CN2C2OC(COP(O)(=O)OP(O)(O)=O)C(O)C2O)C(=O)N1
KEGG Compound ID C00035 Link Image
BioCyc ID GDP-4-DEHYDRO-6-DEOXY-D-MANNOSE Link Image
BiGG ID 33599 Link Image
Wikipedia Link GDP Link Image
NuGOwiki Link HMDB01201 Link Image
Metagene Link HMDB01201 Link Image
METLIN ID 6077 Link Image
PubChem Compound 8977 Link Image
PubChem Substance 8022983 Link Image
ChEBI ID 17552 Link Image
CAS Registry Number 146-91-8
InChI Identifier InChI=1/C10H15N5O11P2/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(25-9)1-24-28(22,23)26-27(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1
Synthesis Reference Edlin, Gordon; Donini, P. Synthesis of guanosine 5'-diphosphate, 2'-(or 3'-) diphosphate, and related nucleotides in a variety of physiological conditions. Journal of Biological Chemistry (1971), 246(13), 4371-3.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 4.44 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -3
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.51 [Predicted by ALOGPS]; -4.6 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID 1A4R Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • Extracellular
  • golgi apparatus
  • mitochondria
  • nucleus
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 18.0 +/- 8.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 15.0 +/- 2.0 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 1.86 +/- 0.027 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid CSF
Value 2.11 +/- 1.93 uM
Age Adult:>18 yrs old
Sex Both
Condition Rachialgia
Comments Not Available
References
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Biofluid CSF
Value 4.05 +/- 0.03 uM
Age Adult:>18 yrs old
Sex Both
Condition Subarachnoid hemorrhage
Comments Not Available
References
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Biofluid CSF
Value 0.99 +/- 1.32 uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Not Available
References
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Biofluid CSF
Value 2.55 +/- 1.62 uM
Age Adult:>18 yrs old
Sex Both
Condition Stroke
Comments Cerebral stroke
References
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Biofluid CSF
Value 2.59 +/- 1.77 uM
Age Adult:>18 yrs old
Sex Both
Condition Neuroinfection
Comments Not Available
References
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Associated Disorders
Condition References
Epilepsy
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Neuroinfection
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Rachialgia
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Stroke
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Subarachnoid hemorrhage
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Citric Acid Cycle SMP00057 Link Image map00020 Link Image
Gluconeogenesis SMP00128 Link Image map00010 Link Image
Purine Metabolism SMP00050 Link Image map00230 Link Image
General References
  1. Chantin C, Bonin B, Boulieu R, Bory C: Liquid-chromatographic study of purine metabolism abnormalities in purine nucleoside phosphorylase deficiency. Clin Chem. 1996 Feb;42(2):326-8. [PubMed Link Image]
  2. Wikipedia Link Image
Metabolic Enzymes
  1. Ectonucleoside triphosphate diphosphohydrolase 1
  2. Soluble calcium-activated nucleotidase 1
  3. Ectonucleoside triphosphate diphosphohydrolase 3
  4. Nucleoside diphosphate kinase, mitochondrial
  5. Ribonucleoside-diphosphate reductase large subunit
  6. Nucleoside diphosphate kinase A
  7. Nucleoside diphosphate kinase 7
  8. Ribonucleoside-diphosphate reductase subunit M2
  9. Nucleoside diphosphate kinase B
  10. Nucleoside diphosphate kinase 3
  11. Nucleoside diphosphate kinase 6
  12. Fucose-1-phosphate guanylyltransferase
  13. Alpha-1,3-mannosyltransferase ALG2
  14. Dolichol-phosphate mannosyltransferase
  15. GDP-mannose 4,6 dehydratase
  16. Galactoside 2-alpha-L-fucosyltransferase 2
  17. Galactoside 2-alpha-L-fucosyltransferase 1
  18. 6-phosphofructokinase type C
  19. 6-phosphofructokinase, liver type
  20. 6-phosphofructokinase, muscle type
  21. Pyruvate kinase isozymes M1/M2
  22. Pyruvate kinase isozymes R/L
  23. Ectonucleoside triphosphate diphosphohydrolase 4
  24. Ectonucleoside triphosphate diphosphohydrolase 6
  25. Ectonucleoside triphosphate diphosphohydrolase 5
  26. Adenylosuccinate synthetase isozyme 2
  27. Adenylosuccinate synthetase isozyme 1
  28. Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial
  29. Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial
  30. Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
  31. GDP-L-fucose synthase
  32. Guanylate kinase
  33. Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial
  34. Alpha-(1,3)-fucosyltransferase
  35. Rap guanine nucleotide exchange factor 2
  36. Polyribonucleotide nucleotidyltransferase 1, mitochondrial
  37. Rho guanine nucleotide exchange factor 1
  38. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
  39. Ras-related C3 botulinum toxin substrate 1
  40. Rho GDP-dissociation inhibitor 3
  41. Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
  42. Rab GDP dissociation inhibitor alpha
  43. Proto-oncogene DBL
  44. Cell division control protein 42 homolog
  45. Rab GDP dissociation inhibitor beta
  46. Rho GDP-dissociation inhibitor 1
  47. Rho GDP-dissociation inhibitor 2
  48. Ras-related C3 botulinum toxin substrate 2
  49. Elongation factor 1-alpha 1
  50. Elongation factor 1-alpha 2
  51. Vinexin
  52. GTPase HRas
  53. Rho-related GTP-binding protein RhoQ
  54. Guanine nucleotide-binding protein G(q) subunit alpha
  55. Guanine nucleotide-binding protein subunit alpha-11
  56. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-11
  57. Chitobiosyldiphosphodolichol beta-mannosyltransferase
  58. Guanine nucleotide-binding protein G(t) subunit alpha-1
  59. Uridine-cytidine kinase 2
  60. Protein ALEX
  61. Rap guanine nucleotide exchange factor 3
  62. Lysophosphatidic acid receptor 2
  63. Rap guanine nucleotide exchange factor 4
  64. Elongation factor 2
  65. Succinate-CoA ligase, ADP-forming, beta subunit
  66. ENTPD4 protein
  67. Mannose-1-phosphate guanyltransferase beta
  68. Mannose-1-phosphate guanyltransferase alpha
  69. Alpha-(1,3)-fucosyltransferase
  70. Alpha-(1,6)-fucosyltransferase
  71. Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
  72. Ribonucleoside-diphosphate reductase subunit M2 B
  73. Uridine-cytidine kinase-like 1
  74. Ectonucleoside triphosphate diphosphohydrolase 8
  75. Synembryn-B
  76. Rap guanine nucleotide exchange factor 6
  77. Neuroepithelial cell-transforming gene 1 protein
  78. Cell cycle progression protein 1
  79. Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein
  80. Dynamin-1-like protein
  81. Dedicator of cytokinesis protein 10
  82. Dedicator of cytokinesis protein 1
  83. Dedicator of cytokinesis protein 2
  84. Dedicator of cytokinesis protein 3
  85. Dedicator of cytokinesis protein 4
  86. Dedicator of cytokinesis protein 5
  87. Dedicator of cytokinesis protein 6
  88. Dedicator of cytokinesis protein 7
  89. Dedicator of cytokinesis protein 8
  90. Dynamin-1
  91. Dynamin-2
  92. Elongation factor G, mitochondrial
  93. Ribosome-releasing factor 2, mitochondrial
  94. Elongation factor Tu, mitochondrial
  95. Elongation factor Tu GTP-binding domain-containing protein 1
  96. GTPase-activating protein and VPS9 domain-containing protein 1
  97. Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
  98. Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2
  99. Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3
  100. Guanine nucleotide-binding protein subunit beta-4
  101. Guanine nucleotide-binding protein subunit beta-5
  102. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10
  103. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12
  104. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13
  105. Guanine nucleotide-binding protein G(T) subunit gamma-T1
  106. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3
  107. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-4
  108. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5
  109. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7
  110. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-8
  111. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-T2
  112. Guanine nucleotide-binding protein-like 1
  113. Probable E3 ubiquitin-protein ligase HERC1
  114. Eukaryotic translation initiation factor 5
  115. IQ motif and SEC7 domain-containing protein 1
  116. MAP kinase-activating death domain protein
  117. Guanine nucleotide exchange factor DBS
  118. Ras-related protein Rab-5A
  119. Ras-related protein Rab-5B
  120. Ran-binding protein 3
  121. Ral guanine nucleotide dissociation stimulator-like 2
  122. Ral guanine nucleotide dissociation stimulator-like 3
  123. Synembryn-A
  124. Ras and Rab interactor 1
  125. Ras and Rab interactor 2
  126. Ras and Rab interactor 3
  127. GTP-binding protein Rit1
  128. GTP-binding protein Rit2
  129. Rap guanine nucleotide exchange factor 5
  130. Ras-related GTP-binding protein A
  131. Ras-related GTP-binding protein B
  132. Ras-related GTP-binding protein C
  133. Ras-related GTP-binding protein D
  134. Secretion-regulating guanine nucleotide exchange factor
  135. T-lymphoma invasion and metastasis-inducing protein 2
  136. Protein XRP2
  137. Putative nucleoside diphosphate kinase
  138. Probable 7,8-dihydro-8-oxoguanine triphosphatase NUDT15
  139. Nucleoside diphosphate-linked moiety X motif 17
  140. Nucleoside diphosphate-linked moiety X motif 18
  141. Nucleoside diphosphate-linked moiety X motif 8, mitochondrial
  142. GDP-fucose protein O-fucosyltransferase 1
  143. Rho-related GTP-binding protein RhoU
  144. cDNA FLJ76131, highly similar to Homo sapiens non-metastatic cells 7, protein expressed in (nucleoside-diphosphate kinase) (NME7), transcript variant 1, mRNA (Non-metastatic cells 7, protein expressed in (Nucleoside-diphosphate kinase), isoform CRA_a)
  145. Uridine kinase
  146. Putative uncharacterized protein DKFZp761J1915 (Ectonucleoside triphosphate diphosphohydrolase 6 (Putative function), isoform CRA_a)
  147. Ectonucleoside triphosphate diphosphohydrolase 5
  148. Fucosyltransferase
  149. Alpha-(1,3)-fucosyltransferase
  150. Fucosyltransferase
  151. cDNA FLJ76814, highly similar to Homo sapiens dynamin 1-like (DNM1L), transcript variant 3, mRNA
  152. cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
  153. cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
  154. Adenylosuccinate synthetase
  155. Eukaryotic translation elongation factor 1 alpha 2
  156. EEF2 protein (Eukaryotic translation elongation factor 2, isoform CRA_a)
  157. GDP-fucose protein O-fucosyltransferase 2
  158. Guanine nucleotide-binding protein G(i) subunit alpha-1
  159. Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas
  160. Guanine nucleotide exchange factor VAV2
  161. Rho-guanine nucleotide exchange factor
  162. Ras guanyl-releasing protein 3
  163. Protein RCC2
  164. Protein very KIND
  165. Nucleoside diphosphate kinase
  166. Guanine nucleotide binding protein (G protein), gamma transducing activity polypeptide 1
  167. Abl interactor 1
  168. GTP-binding protein SAR1b
  169. Ras-GEF domain-containing family member 1A
  170. G-protein-signaling modulator 1
  171. GTP-binding protein GEM
  172. Rap guanine nucleotide exchange factor-like 1
  173. Guanine nucleotide binding protein-like 1
  174. Rho guanine nucleotide exchange factor 6
  175. Guanine nucleotide binding protein (G protein), alpha 13, isoform CRA_a
  176. cDNA, FLJ92996, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta polypeptide 1 (GNB1), mRNA
  177. Guanine nucleotide-binding protein subunit alpha-14
  178. PH and SEC7 domain-containing protein 4
  179. Rho guanine nucleotide exchange factor 9
  180. Guanine nucleotide-binding protein G(k) subunit alpha
  181. Epithelial cell-transforming sequence 2 oncogene-like
  182. cDNA, FLJ95645, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta 5(GNB5), transcript variant 1, mRNA
  183. Pleckstrin homology domain-containing family G member 6
  184. Guanine nucleotide-binding protein G(i) subunit alpha-2
  185. cDNA FLJ78228, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta 5(GNB5), transcript variant 1, mRNA
  186. Guanine nucleotide binding protein (G protein), beta polypeptide 1
  187. Guanine nucleotide-binding protein G(t) subunit alpha-2
  188. Rho guanine nucleotide exchange factor 37
  189. PH and SEC7 domain-containing protein 3
  190. PH and SEC7 domain-containing protein 1
  191. Guanine nucleotide-binding protein G(o) subunit alpha
  192. Ras-GEF domain-containing family member 1B
  193. Rho guanine nucleotide exchange factor 18
  194. ALS2 C-terminal-like protein
  195. Switch-associated protein 70
  196. Ras-specific guanine nucleotide-releasing factor RalGPS2
  197. FERM, RhoGEF and pleckstrin domain-containing protein 2
  198. Ral guanine nucleotide dissociation stimulator-like 1
  199. Guanine nucleotide-binding protein subunit alpha-13
  200. Vav-like protein C9orf100
  201. Probable guanine nucleotide exchange factor MCF2L2
  202. Rho guanine nucleotide exchange factor 7
  203. Guanine nucleotide binding protein (G protein), alpha 14
  204. Guanine nucleotide binding protein-like 1
  205. Guanine nucleotide binding protein (G protein), alpha activating activity polypeptide, olfactory type, isoform CRA_b
  206. Guanine nucleotide-binding protein subunit alpha-12
  207. Ras-specific guanine nucleotide-releasing factor RalGPS1
  208. Rho guanine nucleotide exchange factor 11
  209. cDNA FLJ76843, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), alpha 15 (Gq class) (GNA15), mRNA
  210. Growth factor receptor-bound protein 2
  211. Guanine nucleotide binding protein (G protein), beta polypeptide 1
  212. Rho guanine nucleotide exchange factor 10-like protein
  213. Guanine nucleotide binding protein (G protein), q polypeptide
  214. Protein SOLO
  215. Prolactin regulatory element-binding protein
  216. Rho guanine nucleotide exchange factor 4
  217. Not Available
  218. Guanine nucleotide exchange factor for Rab-3A
  219. cDNA FLJ77654, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta polypeptide 4 (GNB4), mRNA
  220. Guanine nucleotide binding protein-like 1
  221. Engulfment and cell motility protein 1
  222. GRB2-related adapter protein
  223. Guanine nucleotide-binding protein G(z) subunit alpha
  224. Engulfment and cell motility protein 3
  225. Guanine nucleotide exchange factor GEFT
  226. Differentially expressed in FDCP 6 homolog
  227. Alpha-catulin
  228. Guanine nucleotide binding protein (G protein), beta polypeptide 1
  229. IQ motif and SEC7 domain-containing protein 3
  230. Engulfment and cell motility protein 2
  231. Rho guanine nucleotide exchange factor 17
  232. Ras-GEF domain-containing family member 1C
  233. Rho guanine nucleotide exchange factor 12
  234. Ephexin-1
  235. Guanine nucleotide binding protein-like 1
  236. Guanine nucleotide-binding protein G(olf) subunit alpha
  237. Guanine nucleotide-binding protein subunit alpha-15
  238. Rho guanine nucleotide exchange factor 3
Enzyme 1 [top]
Enzyme 1 ID 5313
Enzyme 1 Name Ectonucleoside triphosphate diphosphohydrolase 1
Enzyme 1 Synonyms
  1. NTPDase 1
  2. Ecto-ATP diphosphohydrolase 1
  3. Ecto-ATPDase 1
  4. Ecto-ATPase 1
  5. Ecto-apyrase
  6. Lymphoid cell activation antigen
  7. CD39 antigen
Enzyme 1 Gene Name ENTPD1
Enzyme 1 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 1
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
Enzyme 1 Number of Residues 510
Enzyme 1 Molecular Weight 57964.1
Enzyme 1 Theoretical pI 6.29
Enzyme 1 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 1 General Function Involved in hydrolase activity
Enzyme 1 Specific Function In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation. Hydrolyzes ATP and ADP equally well
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 17-37 479-499
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 45580700 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P49961 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ENTP1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1533 bp
ATGGAAGATACAAAGGAGTCTAACGTGAAGACATTTTGCTCCAAGAATATCCTAGCCATC
CTTGGCTTCTCCTCTATCATAGCTGTGATAGCTTTGCTTGCTGTGGGGTTGACCCAGAAC
AAAGCATTGCCAGAAAACGTTAAGTATGGGATTGTGCTGGATGCGGGTTCTTCTCACACA
AGTTTATACATCTATAAGTGGCCAGCAGAAAAGGAGAATGACACAGGCGTGGTGCATCAA
GTAGAAGAATGCAGGGTTAAAGGTCCTGGAATCTCAAAATTTGTTCAGAAAGTAAATGAA
ATAGGCATTTACCTGACTGATTGCATGGAAAGAGCTAGGGAAGTGATTCCAAGGTCCCAG
CACCAAGAGACACCCGTTTACCTGGGAGCCACGGCAGGCATGCGGTTGCTCAGGATGGAA
AGTGAAGAGTTGGCAGACAGGGTTCTGGATGTGGTGGAGAGGAGCCTCAGCAACTACCCC
TTTGACTTCCAGGGTGCCAGGATCATTACTGGCCAAGAGGAAGGTGCCTATGGCTGGATT
ACTATCAACTATCTGCTGGGCAAATTCAGTCAGAAAACAAGGTGGTTCAGCATAGTCCCA
TATGAAACCAATAATCAGGAAACCTTTGGAGCTTTGGACCTTGGGGGAGCCTCTACACAA
GTCACTTTTGTACCCCAAAACCAGACTATCGAGTCCCCAGATAATGCTCTGCAATTTCGC
CTCTATGGCAAGGACTACAATGTCTACACACATAGCTTCTTGTGCTATGGGAAGGATCAG
GCACTCTGGCAGAAACTGGCCAAGGACATTCAGGTTGCAAGTAATGAAATTCTCAGGGAC
CCATGCTTTCATCCTGGATATAAGAAGGTAGTGAACGTAAGTGACCTTTACAAGACCCCC
TGCACCAAGAGATTTGAGATGACTCTTCCATTCCAGCAGTTTGAAATCCAGGGTATTGGA
AACTATCAACAATGCCATCAAAGCATCCTGGAGCTCTTCAACACCAGTTACTGCCCTTAC
TCCCAGTGTGCCTTCAATGGGATTTTCTTGCCACCACTCCAGGGGGATTTTGGGGCATTT
TCAGCTTTTTACTTTGTGATGAAGTTTTTAAACTTGACATCAGAGAAAGTCTCTCAGGAA
AAGGTGACTGAGATGATGAAAAAGTTCTGTGCTCAGCCTTGGGAGGAGATAAAAACATCT
TACGCTGGAGTAAAGGAGAAGTACCTGAGTGAATACTGCTTTTCTGGTACCTACATTCTC
TCCCTCCTTCTGCAAGGCTATCATTTCACAGCTGATTCCTGGGAGCACATCCATTTCATT
GGCAAGATCCAGGGCAGCGACGCCGGCTGGACTTTGGGCTACATGCTGAACCTGACCAAC
ATGATCCCAGCTGAGCAACCATTGTCCACACCTCTCTCCCACTCCACCTATGTCTTCCTC
ATGGTTCTATTCTCCCTGGTCCTTTTCACAGTGGCCATCATAGGCTTGCTTATCTTTCAC
AAGCCTTCATATTTCTGGAAAGATATGGTATAG
Enzyme 1 GenBank Gene ID NM_001776.5 Link Image
Enzyme 1 GeneCard ID ENTPD1 Link Image
Enzyme 1 GenAtlas ID ENTPD1 Link Image
Enzyme 1 HGNC ID HGNC:3363 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 10q24
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Maliszewski CR, Delespesse GJ, Schoenborn MA, Armitage RJ, Fanslow WC, Nakajima T, Baker E, Sutherland GR, Poindexter K, Birks C, et al.: The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. J Immunol. 1994 Oct 15;153(8):3574-83. [PubMed Link Image]
  2. Robson SC, Kaczmarek E, Siegel JB, Candinas D, Koziak K, Millan M, Hancock WW, Bach FH: Loss of ATP diphosphohydrolase activity with endothelial cell activation. J Exp Med. 1997 Jan 6;185(1):153-63. [PubMed Link Image]
  3. Matsumoto M, Sakurai Y, Kokubo T, Yagi H, Makita K, Matsui T, Titani K, Fujimura Y, Narita N: The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II. FEBS Lett. 1999 Jun 25;453(3):335-40. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  6. Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O: Purification and properties of human placental ATP diphosphohydrolase. Eur J Biochem. 1995 Nov 15;234(1):66-74. [PubMed Link Image]
  7. Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y: Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. Int J Hematol. 1998 Oct;68(3):297-310. [PubMed Link Image]
  8. Kaczmarek E, Koziak K, Sevigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC: Identification and characterization of CD39/vascular ATP diphosphohydrolase. J Biol Chem. 1996 Dec 20;271(51):33116-22. [PubMed Link Image]
  9. Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed Link Image]
  10. Koziak K, Kaczmarek E, Kittel A, Sevigny J, Blusztajn JK, Schulte Am Esch J 2nd, Imai M, Guckelberger O, Goepfert C, Qawi I, Robson SC: Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae. J Biol Chem. 2000 Jan 21;275(3):2057-62. [PubMed Link Image]
  11. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed Link Image]
  12. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5314
Enzyme 2 Name Soluble calcium-activated nucleotidase 1
Enzyme 2 Synonyms
  1. SCAN-1
  2. Apyrase homolog
  3. Putative MAPK-activating protein PM09
  4. Putative NF-kappa-B-activating protein 107
Enzyme 2 Gene Name CANT1
Enzyme 2 Protein Sequence >Soluble calcium-activated nucleotidase 1
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
Enzyme 2 Number of Residues 401
Enzyme 2 Molecular Weight 44839.2
Enzyme 2 Theoretical pI 5.98
Enzyme 2 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • ion binding
  • metal ion binding
  • pyrophosphatase activity
Process
Component
Enzyme 2 General Function Involved in calcium ion binding
Enzyme 2 Specific Function Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP
Enzyme 2 Pathways
Enzyme 2 Reactions
  • a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 45-62
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 229577440 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q8WVQ1 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CANT1_HUMAN Link Image
Enzyme 2 PDB ID 1S1D Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1206 bp
ATGCCCGTGCAGCTGTCTGAGCACCCGGAATGGAATGAGTCTATGCACTCCCTCCGGATC
AGTGTGGGGGGCCTTCCTGTGCTGGCGTCCATGACCAAGGCCGCGGACCCCCGCTTCCGC
CCCCGCTGGAAGGTGATCCTGACGTTCTTTGTGGGTGCTGCCATCCTCTGGCTGCTCTGC
TCCCACCGCCCGGCCCCCGGCAGGCCCCCCACCCACAATGCACACAACTGGAGGCTCGGC
CAGGCGCCCGCCAACTGGTACAATGACACCTACCCCCTGTCTCCCCCACAAAGGACACCG
GCTGGGATTCGGTATCGAATCGCAGTTATCGCAGACCTGGACACAGAGTCAAGGGCCCAA
GAGGAAAACACCTGGTTCAGTTACCTGAAAAAGGGCTACCTGACCCTGTCAGACAGTGGG
GACAAGGTGGCCGTGGAATGGGACAAAGACCATGGGGTCCTGGAGTCCCACCTGGCGGAG
AAGGGGAGAGGCATGGAGCTATCCGACCTGATTGTTTTCAATGGGAAACTCTACTCCGTG
GATGACCGGACGGGGGTCGTCTACCAGATCGAAGGCAGCAAAGCCGTGCCCTGGGTGATT
CTGTCCGACGGCGACGGCACCGTGGAGAAAGGCTTCAAGGCCGAATGGCTGGCAGTGAAG
GACGAGCGTCTGTACGTGGGCGGCCTGGGCAAGGAGTGGACGACCACTACGGGTGATGTG
GTGAACGAGAACCCGGAGTGGGTGAAGGTGGTGGGCTACAAGGGCAGCGTGGACCACGAG
AACTGGGTGTCCAACTACAACGCCCTGCGGGCTGCTGCCGGCATCCAGCCGCCAGGCTAC
CTCATCCATGAGTCTGCCTGCTGGAGTGACACGCTGCAGCGCTGGTTCTTCCTGCCGCGC
CGCGCCAGCCAGGAGCGCTACAGCGAGAAGGACGACGAGCGCAAGGGCGCCAACCTGCTG
CTGAGCGCCTCCCCTGACTTCGGCGACATCGCTGTGAGCCACGTCGGGGCGGTGGTCCCC
ACTCACGGCTTCTCGTCCTTCAAGTTCATCCCCAACACCGACGACCAGATCATTGTGGCC
CTCAAATCCGAGGAGGACAGCGGCAGAGTCGCCTCCTACATCATGGCCTTCACGCTGGAC
GGGCGCTTCCTGTTGCCGGAGACCAAGATCGGAAGCGTGAAATACGAAGGCATCGAGTTC
ATTTAA
Enzyme 2 GenBank Gene ID NM_001159772.1 Link Image
Enzyme 2 GeneCard ID CANT1 Link Image
Enzyme 2 GenAtlas ID CANT1 Link Image
Enzyme 2 HGNC ID HGNC:19721 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 17q25.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Smith TM, Hicks-Berger CA, Kim S, Kirley TL: Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases. Arch Biochem Biophys. 2002 Oct 1;406(1):105-15. [PubMed Link Image]
  2. Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S: Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003 May 22;22(21):3307-18. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Failer BU, Braun N, Zimmermann H: Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J Biol Chem. 2002 Oct 4;277(40):36978-86. Epub 2002 Aug 6. [PubMed Link Image]
  6. Yang M, Kirley TL: Site-directed mutagenesis of human soluble calcium-activated nucleotidase 1 (hSCAN-1): identification of residues essential for enzyme activity and the Ca(2+)-induced conformational change. Biochemistry. 2004 Jul 20;43(28):9185-94. [PubMed Link Image]
  7. Dai J, Liu J, Deng Y, Smith TM, Lu M: Structure and protein design of a human platelet function inhibitor. Cell. 2004 Mar 5;116(5):649-59. [PubMed Link Image]
  8. Huber C, Oules B, Bertoli M, Chami M, Fradin M, Alanay Y, Al-Gazali LI, Ausems MG, Bitoun P, Cavalcanti DP, Krebs A, Le Merrer M, Mortier G, Shafeghati Y, Superti-Furga A, Robertson SP, Le Goff C, Muda AO, Paterlini-Brechot P, Munnich A, Cormier-Daire V: Identification of CANT1 mutations in Desbuquois dysplasia. Am J Hum Genet. 2009 Nov;85(5):706-10. Epub 2009 Oct 22. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5318
Enzyme 3 Name Ectonucleoside triphosphate diphosphohydrolase 3
Enzyme 3 Synonyms
  1. NTPDase 3
  2. CD39 antigen-like 3
  3. Ecto-ATP diphosphohydrolase 3
  4. Ecto-ATPDase 3
  5. Ecto-ATPase 3
  6. Ecto-apyrase 3
  7. HB6
Enzyme 3 Gene Name ENTPD3
Enzyme 3 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 3
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
Enzyme 3 Number of Residues 529
Enzyme 3 Molecular Weight 59104.8
Enzyme 3 Theoretical pI 6.40
Enzyme 3 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 3 General Function Involved in hydrolase activity
Enzyme 3 Specific Function Has a threefold preference for the hydrolysis of ATP over ADP
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 23-43 486-506
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 13817037 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O75355 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ENTP3_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1590 bp
ATGTTCACTGTGCTGACCCGCCAACCATGTGAGCAAGCAGGCCTCAAGGCCCTCTACCGA
ACTCCAACCATCATTGCCTTGGTGGTCTTGCTTGTGAGTATTGTGGTACTTGTGAGTATC
ACTGTCATCCAGATCCACAAGCAAGAGGTCCTCCCTCCAGGACTGAAGTATGGTATTGTG
CTGGATGCCGGGTCTTCAAGAACCACAGTCTACGTGTATCAATGGCCAGCAGAAAAAGAG
AATAATACCGGAGTGGTCAGTCAAACCTTCAAATGTAGTGTGAAAGGCTCTGGAATCTCC
AGCTATGGAAATAACCCCCAAGATGTCCCCAGAGCCTTTGAGGAGTGTATGCAAAAAGTC
AAGGGGCAGGTTCCATCCCACCTCCACGGATCCACCCCCATTCACCTGGGAGCCACGGCT
GGGATGCGCTTGCTGAGGTTGCAAAATGAAACAGCAGCTAATGAAGTCCTTGAAAGCATC
CAAAGCTACTTCAAGTCCCAGCCCTTTGACTTTAGGGGTGCTCAAATCATTTCTGGGCAA
GAAGAAGGGGTATATGGATGGATTACAGCCAACTATTTAATGGGAAATTTCCTGGAGAAG
AACCTGTGGCACATGTGGGTGCACCCGCATGGAGTGGAAACCACGGGTGCCCTGGACTTA
GGTGGTGCCTCCACCCAAATATCCTTCGTGGCAGGAGAGAAGATGGATCTGAACACCAGC
GACATCATGCAGGTGTCCCTGTATGGCTACGTATACACGCTCTACACACACAGCTTCCAG
TGCTATGGCCGGAATGAGGCTGAGAAGAAGTTTCTGGCAATGCTCCTGCAGAATTCTCCT
ACCAAAAACCATCTCACCAATCCCTGTTACCCTCGGGATTATAGCATCAGCTTCACCATG
GGCCATGTATTTGATAGCCTGTGCACTGTGGACCAGAGGCCAGAAAGTTATAACCCCAAT
GATGTCATCACTTTTGAAGGAACTGGGGACCCATCTCTGTGTAAGGAGAAGGTGGCTTCC
ATATTTGACTTCAAAGCTTGCCATGATCAAGAAACCTGTTCTTTTGATGGGGTTTATCAG
CCAAAGATTAAAGGGCCATTTGTGGCTTTTGCAGGATTCTACTACACAGCCAGTGCTTTA
AATCTTTCAGGTAGCTTTTCCCTGGACACCTTCAACTCCAGCACCTGGAATTTCTGCTCA
CAGAATTGGAGTCAGCTCCCACTGCTGCTCCCCAAATTTGATGAGGTATATGCCCGCTCT
TACTGCTTCTCAGCCAACTACATCTACCACTTGTTTGTGAACGGTTACAAATTCACAGAG
GAGACTTGGCCCCAAATACACTTTGAAAAAGAAGTGGGGAATAGCAGCATAGCCTGGTCT
CTTGGCTACATGCTCAGCCTGACCAACCAGATCCCAGCTGAAAGCCCTCTGATCCGTCTG
CCCATAGAACCACCTGTCTTTGTGGGCACCCTCGCTTTCTTCACAGCGGCAGCCTTGCTG
TGTCTGGCATTTCTTGCATACCTGTGTTCAGCAACCAGAAGAAAGAGGCACTCCGAGCAT
GCCTTTGACCATGCAGTGGATTCTGACTGA
Enzyme 3 GenBank Gene ID AF034840 Link Image
Enzyme 3 GeneCard ID ENTPD3 Link Image
Enzyme 3 GenAtlas ID ENTPD3 Link Image
Enzyme 3 HGNC ID HGNC:3365 Link Image
Enzyme 3 Chromosome Location 3
Enzyme 3 Locus 3p21.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Chadwick BP, Frischauf AM: The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster. Genomics. 1998 Jun 15;50(3):357-67. [PubMed Link Image]
  2. Smith TM, Kirley TL: Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases1. Biochim Biophys Acta. 1998 Jul 28;1386(1):65-78. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Smith TM, Lewis Carl SA, Kirley TL: Mutagenesis of two conserved tryptophan residues of the E-type ATPases: inactivation and conversion of an ecto-apyrase to an ecto-NTPase. Biochemistry. 1999 May 4;38(18):5849-57. [PubMed Link Image]
  5. Yang F, Hicks-Berger CA, Smith TM, Kirley TL: Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: the importance of residues in the apyrase conserved regions. Biochemistry. 2001 Apr 3;40(13):3943-50. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5338
Enzyme 4 Name Nucleoside diphosphate kinase, mitochondrial
Enzyme 4 Synonyms
  1. NDK
  2. NDP kinase, mitochondrial
  3. Nucleoside diphosphate kinase D
  4. NDPKD
  5. nm23-H4
Enzyme 4 Gene Name NME4
Enzyme 4 Protein Sequence >Nucleoside diphosphate kinase, mitochondrial
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
Enzyme 4 Number of Residues 187
Enzyme 4 Molecular Weight 20658.5
Enzyme 4 Theoretical pI 10.75
Enzyme 4 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 4 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 4 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 14336697 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O00746 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name NDKM_HUMAN Link Image
Enzyme 4 PDB ID 1EHW Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >564 bp
ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCG
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
Enzyme 4 GenBank Gene ID AE006463 Link Image
Enzyme 4 GeneCard ID NME4 Link Image
Enzyme 4 GenAtlas ID NME4 Link Image
Enzyme 4 HGNC ID HGNC:7852 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 16p13.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Milon L, Rousseau-Merck MF, Munier A, Erent M, Lascu I, Capeau J, Lacombe ML: nm23-H4, a new member of the family of human nm23/nucleoside diphosphate kinase genes localised on chromosome 16p13. Hum Genet. 1997 Apr;99(4):550-7. [PubMed Link Image]
  2. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  3. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Milon L, Meyer P, Chiadmi M, Munier A, Johansson M, Karlsson A, Lascu I, Capeau J, Janin J, Lacombe ML: The human nm23-H4 gene product is a mitochondrial nucleoside diphosphate kinase. J Biol Chem. 2000 May 12;275(19):14264-72. [PubMed Link Image]
  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5340
Enzyme 5 Name Ribonucleoside-diphosphate reductase large subunit
Enzyme 5 Synonyms
  1. Ribonucleoside-diphosphate reductase subunit M1
  2. Ribonucleotide reductase large subunit
Enzyme 5 Gene Name RRM1
Enzyme 5 Protein Sequence >Ribonucleoside-diphosphate reductase large subunit
MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLA
AETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKST
LDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHK
EDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCAL
ISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIY
LEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLD
EVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNL
GTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKI
IDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGAL
EASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIA
PMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQII
ACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKL
TSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCS
LENRDECLMCGS
Enzyme 5 Number of Residues 792
Enzyme 5 Molecular Weight 90069.4
Enzyme 5 Theoretical pI 7.16
Enzyme 5 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH or CH2 groups
  • oxidoreductase activity, acting on CH or CH2 groups, disulfide as acceptor
  • protein binding
  • purine nucleoside binding
  • ribonucleoside-diphosphate reductase activity
Process
  • DNA metabolic process
  • DNA replication
  • cellular macromolecule metabolic process
  • macromolecule metabolic process
  • metabolic process
  • oxidation reduction
Component
  • macromolecular complex
  • protein complex
  • ribonucleoside-diphosphate reductase complex
Enzyme 5 General Function Involved in oxidation reduction
Enzyme 5 Specific Function Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides
Enzyme 5 Pathways
Enzyme 5 Reactions
  • 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin [RN:R04294]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 36065 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P23921 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name RIR1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >2379 bp
ATGCATGTGATCAAGCGAGATGGCCGCCAAGAACGAGTCATGTTTGACAAAATTACATCT
CGAATCCAGAAGCTTTGTTATGGACTCAATATGGATTTTGTTGATCCTGCTCAGATCACC
ATGAAAGTAATCCAAGGCTTGTACAGTGGGGTCACCACAGTGGAACTAGATACTTTGGCT
GCTGAAACAGCTGCAACCTTGACTACTAAGCACCCTGACTATGCTATCCTGGCAGCCAGG
ATCGCTGTCTCTAACTTGCACAAAGAAACAAAGAAAGTGTTCAGTGATGTGATGGAAGAC
CTCTATAACTACATAAATCCACATAATGGCAAACACTCTCCCATGGTGGCCAAGTCAACA
TTGGATATTGTTCTGGCCAATAAAGATCGCCTGAATTCTGCTATTATCTATGACCGAGAT
TTCTCTTACAATTACTTCGGCTTTAAGACGCTAGAGCGGTCTTATTTGTTGAAGATCAAT
GGAAAAGTGGCTGAAAGACCACAACATATGTTGATGAGAGTATCTGTTGGGATCCACAAA
GAAGACATTGATGCAGCAATTGAAACATATAATCTTCTTTCTGAGAGGTGGTTTACTCAT
GCTTCGCCCACTCTCTTCAATGCTGGTACCAACCGCCCACAACTTTCTAGCTGTTTTCTT
CTGAGTATGAAAGATGACAGCATTGAAGGCATTTATGACACTCTAAAGCAATGTGCATTG
ATTTCTAAGTCTGCTGGAGGAATTGGTGTTGCTGTGAGTTGTATTCGGGCTACTGGCAGC
TACATTGCTGGGACTAATGGCAATTCCAATGGCCTTGTACCGATGCTGAGAGTATATAAC
AACACAGCTCGATATGTGGATCAAGGTGGGAACAAGCGTCCTGGGGCATTTGCTATTTAC
CTGGAGCCTTGGCATTTAGACATCTTTGAATTCCTTGATTTAAAGAAGAACACAGGAAAG
GAAGAGCAGCGTGCCAGAGATCTTTTCTTTGCTCTTTGGATTCCGGATCTCTTCATGAAA
CGAGTGGAGACTAATCAGGACTGGTCTTTGATGTGTCCAAATGAGTGTCCTGGTCTGGAT
GAGGTTTGGGGAGAGGAATTTGAGAAACTATATGCAAGTTATGAGAAACAAGGTCGTGTC
CGCAAAGTTGTAAAAGCTCAGCAGCTTTGGTATGCCATCATTGAGTCTCAGACGGAAACA
GGCACCCCGTATATGCTCTACAAAGATTCCTGTAATCGAAAGAGCAACCAGCAGAACCTG
GGAACCATCAAATGCAGCAACCTGTGCACAGAAATAGTGGAGTACACCAGCAAAGATGAG
GTTGCTGTTTGTAATTTGGCTTCCCTGGCCCTGAATATGTATGTCACATCAGAACACACA
TACGACTTTAAGAAGTTGGCTGAAGTCACTAAAGTCGTTGTCCGAAACTTGAATAAAATT
ATTGATATAAACTACTATCCTGTACCAGAGGCATGCCTATCAAATAAACGCCATCGCCCC
ATTGGAATTGGGGTACAAGGTCTGGCAGATGCTTTTATCCTGATGAGATACCCTTTTGAG
AGTGCAGAAGCCCAGTTACTGAATAAGCAGATCTTTGAAACTATTTATTATGGTGCTCTG
GAAGCCAGCTGTGACCTTGCCAAGGAGCAGGGCCCATACGAAACCTATGAGGGCTCTCCA
GTTAGCAAAGGAATTCTTCAGTATGATATGTGGAATGTTACTCCTACAGACCTATGGGAC
TGGAAGGTTCTCAAGGAGAAGATTGCAAAGTATGGTATAAGAAACAGTTTACTTATTGCC
CCGATGCCTACAGCTTCCACTGCTCAGATCCTGGGGAATAATGAGTCCATTGAACCTTAC
ACCAGCAACATCTATACTCGCAGAGTCTTGTCAGGAGAATTTCAGATTGTAAATCCTCAC
TTATTGAAAGATCTTACCGAGCGGGGCCTATGGCATGAAGAGATGAAAAACCAGATTATT
GCATGCAATGGCTCTATTCAGAGCATACCAGAAATTCCTGATGACCTGAAGCAACTTTAT
AAAACTGTGTGGGAAATCTCTCAGAAAACTGTTCTCAAGATGGCAGCTGAGAGAGGTGCT
TTCATTGATCAAAGCCAATCTTTGAACATCCACATTGCTGAGCCTAACTATGGCAAACTC
ACTAGTATGCACTTCTACGGCTGGAAGCAGGGTTTGAAGACTGGGATGTATTATTTAAGG
ACGAGACCAGCAGCTAATCCAATCCAGTTCACTCTAAATAAGGAGAAGCTAAAAGATAAA
GAAAAGGTATCAAAAGAGGAAGAAGAGAAGGAGAGGAACACAGCAGCCATGGTGTGCTCT
TTGGAGAATAGAGATGAATGTCTGATGTGTGGATCCTGA
Enzyme 5 GenBank Gene ID X59543 Link Image
Enzyme 5 GeneCard ID RRM1 Link Image
Enzyme 5 GenAtlas ID RRM1 Link Image
Enzyme 5 HGNC ID HGNC:10451 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 11p15.5
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Parker NJ, Begley CG, Fox RM: Human M1 subunit of ribonucleotide reductase: cDNA sequence and expression in stimulated lymphocytes. Nucleic Acids Res. 1991 Jul 11;19(13):3741. [PubMed Link Image]
  2. Pavloff N, Rivard D, Masson S, Shen SH, Mes-Masson AM: Sequence analysis of the large and small subunits of human ribonucleotide reductase. DNA Seq. 1992;2(4):227-34. [PubMed Link Image]
  3. Bepler G, O'briant KC, Kim YC, Schreiber G, Pitterle DM: A 1.4-Mb high-resolution physical map and contig of chromosome segment 11p15.5 and genes in the LOH11A metastasis suppressor region. Genomics. 1999 Jan 15;55(2):164-75. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Parker NJ, Begley CG, Fox RM: Human R1 subunit of ribonucleotide reductase (RRM1): 5' flanking region of the gene. Genomics. 1994 Jan 1;19(1):91-6. [PubMed Link Image]
  6. Harrington JA, Spector T: Human ribonucleotide reductase. Activation and inhibition by analogs of ATP. Biochem Pharmacol. 1991 Jul 25;42(4):759-63. [PubMed Link Image]
  7. Xue L, Zhou B, Liu X, Qiu W, Jin Z, Yen Y: Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits. Cancer Res. 2003 Mar 1;63(5):980-6. [PubMed Link Image]
  8. Qiu W, Zhou B, Darwish D, Shao J, Yen Y: Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits. Biochem Biophys Res Commun. 2006 Feb 10;340(2):428-34. Epub 2005 Dec 15. [PubMed Link Image]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5341
Enzyme 6 Name Nucleoside diphosphate kinase A
Enzyme 6 Synonyms
  1. NDK A
  2. NDP kinase A
  3. Granzyme A-activated DNase
  4. GAAD
  5. Metastasis inhibition factor nm23
  6. Tumor metastatic process-associated protein
  7. nm23-H1
Enzyme 6 Gene Name NME1
Enzyme 6 Protein Sequence >Nucleoside diphosphate kinase A
MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
Enzyme 6 Number of Residues 152
Enzyme 6 Molecular Weight 17148.6
Enzyme 6 Theoretical pI 6.11
Enzyme 6 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 6 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 6 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein- coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination
Enzyme 6 Pathways
Enzyme 6 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 4557797 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P15531 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name NDKA_HUMAN Link Image
Enzyme 6 PDB ID 1JXV Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >459 bp
ATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAACCAGATGGGGTCCAGCGGGGTCTT
GTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGATTCCGCCTTGTTGGTCTGAAATTC
ATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTACGTTGACCTGAAGGACCGTCCATTC
TTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCGGTAGTTGCCATGGTCTGGGAGGGG
CTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGGGAGACCAACCCTGCAGACTCCAAG
CCTGGGACCATCCGTGGAGACTTCTGCATACAAGTTGGCAGGAACATTATACATGGCAGT
GATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTGTGGTTTCACCCTGAGGAACTGGTA
GATTACACGAGCTGTGCTCAGAACTGGATCTATGAATGA
Enzyme 6 GenBank Gene ID NM_000269.2 Link Image
Enzyme 6 GeneCard ID NME1 Link Image
Enzyme 6 GenAtlas ID NME1 Link Image
Enzyme 6 HGNC ID HGNC:7849 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 17q21.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Rosengard AM, Krutzsch HC, Shearn A, Biggs JR, Barker E, Margulies IM, King CR, Liotta LA, Steeg PS: Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development. Nature. 1989 Nov 9;342(6246):177-80. [PubMed Link Image]
  2. Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed Link Image]
  3. Wang L, Patel U, Ghosh L, Chen HC, Banerjee S: Mutation in the nm23 gene is associated with metastasis in colorectal cancer. Cancer Res. 1993 Feb 15;53(4):717-20. [PubMed Link Image]
  4. Dooley S, Seib T, Engel M, Theisinger B, Janz H, Piontek K, Zang KD, Welter C: Isolation and characterization of the human genomic locus coding for the putative metastasis control gene nm23-H1. Hum Genet. 1994 Jan;93(1):63-6. [PubMed Link Image]
  5. Ni X, Gu S, Dai J, Cheng H, Guo L, Li L, Ji C, Xie Y, Ying K, Mao Y: Isolation and characterization of a novel human NM23-H1B gene, a different transcript of NM23-H1. J Hum Genet. 2003;48(2):96-100. [PubMed Link Image]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  7. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed Link Image]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. Hailat N, Keim DR, Melhem RF, Zhu XX, Eckerskorn C, Brodeur GM, Reynolds CP, Seeger RC, Lottspeich F, Strahler JR, et al.: High levels of p19/nm23 protein in neuroblastoma are associated with advanced stage disease and with N-myc gene amplification. J Clin Invest. 1991 Jul;88(1):341-5. [PubMed Link Image]
  10. MacDonald NJ, Freije JM, Stracke ML, Manrow RE, Steeg PS: Site-directed mutagenesis of nm23-H1. Mutation of proline 96 or serine 120 abrogates its motility inhibitory activity upon transfection into human breast carcinoma cells. J Biol Chem. 1996 Oct 11;271(41):25107-16. [PubMed Link Image]
  11. Manda R, Kohno T, Matsuno Y, Takenoshita S, Kuwano H, Yokota J: Identification of genes (SPON2 and C20orf2) differentially expressed between cancerous and noncancerous lung cells by mRNA differential display. Genomics. 1999 Oct 1;61(1):5-14. [PubMed Link Image]
  12. Fan Z, Beresford PJ, Oh DY, Zhang D, Lieberman J: Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Cell. 2003 Mar 7;112(5):659-72. [PubMed Link Image]
  13. Valentijn LJ, Koster J, Versteeg R: Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene encodes a novel protein, NM23-LV. Genomics. 2006 Apr;87(4):483-9. Epub 2006 Jan 25. [PubMed Link Image]
  14. Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. Epub 2008 Sep 10. [PubMed Link Image]
  15. Garzia L, D'Angelo A, Amoresano A, Knauer SK, Cirulli C, Campanella C, Stauber RH, Steegborn C, Iolascon A, Zollo M: Phosphorylation of nm23-H1 by CKI induces its complex formation with h-prune and promotes cell motility. Oncogene. 2008 Mar 20;27(13):1853-64. Epub 2007 Oct 1. [PubMed Link Image]
  16. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  17. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  18. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  19. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  20. Min K, Song HK, Chang C, Kim SY, Lee KJ, Suh SW: Crystal structure of human nucleoside diphosphate kinase A, a metastasis suppressor. Proteins. 2002 Feb 15;46(3):340-2. [PubMed Link Image]
  21. Chen Y, Gallois-Montbrun S, Schneider B, Veron M, Morera S, Deville-Bonne D, Janin J: Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases. J Mol Biol. 2003 Sep 26;332(4):915-26. [PubMed Link Image]
  22. Chang CL, Zhu XX, Thoraval DH, Ungar D, Rawwas J, Hora N, Strahler JR, Hanash SM, Radany E: Nm23-H1 mutation in neuroblastoma. Nature. 1994 Aug 4;370(6488):335-6. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5342
Enzyme 7 Name Nucleoside diphosphate kinase 7
Enzyme 7 Synonyms
  1. NDK 7
  2. NDP kinase 7
  3. nm23-H7
Enzyme 7 Gene Name NME7
Enzyme 7 Protein Sequence >Nucleoside diphosphate kinase 7
MNHSERFVFIAEWYDPNASLLRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYDNLHLEDL
FIGNKVNVFSRQLVLIDYGDQYTARQLGSRKEKTLALIKPDAISKAGEIIEIINKAGFTI
TKLKMMMLSRKEALDFHVDHQSRPFFNELIQFITTGPIIAMEILRDDAICEWKRLLGPAN
SGVARTDASESIRALFGTDGIRNAAHGPDSFASAAREMELFFPSSGGCGPANTAKFTNCT
CCIVKPHAVSEGLLGKILMAIRDAGFEISAMQMFNMDRVNVEEFYEVYKGVVTEYHDMVT
EMYSGPCVAMEIQQNNATKTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLP
EDGLLEVQYFFKILDN
Enzyme 7 Number of Residues 376
Enzyme 7 Molecular Weight 42491.4
Enzyme 7 Theoretical pI 6.44
Enzyme 7 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 7 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 7 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate
Enzyme 7 Pathways
Enzyme 7 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 4960169 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9Y5B8 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name NDK7_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1131 bp
ATGAATCATAGTGAAAGATTCGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
Enzyme 7 GenBank Gene ID AF153191 Link Image
Enzyme 7 GeneCard ID NME7 Link Image
Enzyme 7 GenAtlas ID NME7 Link Image
Enzyme 7 HGNC ID HGNC:20461 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 1q24
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5343
Enzyme 8 Name Ribonucleoside-diphosphate reductase subunit M2
Enzyme 8 Synonyms
  1. Ribonucleotide reductase small chain
  2. Ribonucleotide reductase small subunit
Enzyme 8 Gene Name RRM2
Enzyme 8 Protein Sequence >Ribonucleoside-diphosphate reductase subunit M2
MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKT
KAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLK
PEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLI
DTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSF
ASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIE
QEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTN
FFEKRVGEYQRMGVMSSPTENSFTLDADF
Enzyme 8 Number of Residues 389
Enzyme 8 Molecular Weight 44877.2
Enzyme 8 Theoretical pI 5.05
Enzyme 8 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH or CH2 groups
  • oxidoreductase activity, acting on CH or CH2 groups, disulfide as acceptor
  • ribonucleoside-diphosphate reductase activity
  • transition metal ion binding
Process
  • cellular nitrogen compound metabolic process
  • deoxyribonucleoside diphosphate metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside diphosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • oxidation reduction
Component
Enzyme 8 General Function Involved in oxidoreductase activity
Enzyme 8 Specific Function Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling
Enzyme 8 Pathways
Enzyme 8 Reactions
  • 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin [RN:R04294]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 36155 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P31350 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name RIR2_HUMAN Link Image
Enzyme 8 PDB ID 1H0N Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1170 bp
ATGCTCTCCCTCCGTGTCCCGCTCGCGCCCATCACGGACCCGCAGCAGCTGCAGCTCTCG
CCGCTGAAGGGGCTCAGCTTGGTCGACAAGGAGAACACGCCGCCGGCCCTGAGCGGGACC
CGCGTCCTGGCCAGCAAGACCGCGAGGAGGATCTTCCAGGAGCCCACGGAGCCGAAAACT
AAAGCAGCTGCCCCCGGCGTGGAGGATGAGCCGCTGCTGAGAGAAAACCCCCGCCGCTTT
GTCATCTTCCCCATCGAGTACCATGATATCTGGCAGATGTATAAGAAGGCAGAGGCTTCC
TTTTGGACCGCCGAGGAGGTTGACCTCTCCAAGGACATTCAGCACTGGGAATCCCTGAAA
CCCGAGGAGAGATATTTTATATCCCATGTTCTGGCTTTCTTTGCAGCAAGCGATGGCATA
GTAAATGAAAACTTGGTGGAGCGATTTAGCCAAGAAGTTCAGATTACAGAAGCCCGCTGT
TTCTATGGCTTCCAAATTGCCATGGAAAACATACATTCTGAAATGTATAGTCTTCTTATT
GACACTTACATAAAAGATCCCAAAGAAAGGGAATTTCTCTTCAATGCCATTGAAACGATG
CCTTGTGTCAAGAAGAAGGCAGACTGGGCCTTGCGCTGGATTGGGGACAAAGAGGCTACC
TATGGTGAACGTGTTGTAGCCTTTGCTGCAGTGGAAGGCATTTTCTTTTCCGGTTCTTTT
GCGTCGATATTCTGGCTCAAGAAACGAGGACTGATGCCTGGCCTCACATTTTCTAATGAA
CTTATTAGCAGAGATGAGGGTTTACACTGTGATTTTGCTTGCCTGATGTTCAAACACCTG
GTACACAAACCATCGGAGGAGAGAGTAAGAGAAATAATTATCAATGCTGTTCGGATAGAA
CAGGAGTTCCTCACTGAGGCCTTGCCTGTGAAGCTCATTGGGATGAATTGCACTCTAATG
AAGCAATACATTGAGTTTGTGGCAGACAGACTTATGCTGGAACTGGGTTTTAGCAAGGTT
TTCAGAGTAGAGAACCCATTTGACTTTATGGAGAATATTTCACTGGAAGGAAAGACTAAC
TTCTTTGAGAAGAGAGTAGGCGAGTATCAGAGGATGGGAGTGATGTCAAGTCCAACAGAG
AATTCTTTTACCTTGGATGCTGACTTCTAA
Enzyme 8 GenBank Gene ID X59618 Link Image
Enzyme 8 GeneCard ID RRM2 Link Image
Enzyme 8 GenAtlas ID RRM2 Link Image
Enzyme 8 HGNC ID HGNC:10452 Link Image
Enzyme 8 Chromosome Location 2
Enzyme 8 Locus 2p25-p24
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Pavloff N, Rivard D, Masson S, Shen SH, Mes-Masson AM: Sequence analysis of the large and small subunits of human ribonucleotide reductase. DNA Seq. 1992;2(4):227-34. [PubMed Link Image]
  2. Zhou B, Yen Y: Characterization of the human ribonucleotide reductase M2 subunit gene; genomic structure and promoter analyses. Cytogenet Cell Genet. 2001;95(1-2):52-9. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  7. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  8. Tang LY, Deng N, Wang LS, Dai J, Wang ZL, Jiang XS, Li SJ, Li L, Sheng QH, Wu DQ, Li L, Zeng R: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction. Mol Cell Proteomics. 2007 Nov;6(11):1952-67. Epub 2007 Aug 12. [PubMed Link Image]
  9. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  10. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  11. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  12. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  13. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5344
Enzyme 9 Name Nucleoside diphosphate kinase B
Enzyme 9 Synonyms
  1. NDK B
  2. NDP kinase B
  3. C-myc purine-binding transcription factor PUF
  4. nm23-H2
Enzyme 9 Gene Name NME2
Enzyme 9 Protein Sequence >Nucleoside diphosphate kinase B
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
Enzyme 9 Number of Residues 152
Enzyme 9 Molecular Weight 17297.9
Enzyme 9 Theoretical pI 8.69
Enzyme 9 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 9 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 9 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically (PubMed:8392752)
Enzyme 9 Pathways
Enzyme 9 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 4467843 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P22392 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name NDKB_HUMAN Link Image
Enzyme 9 PDB ID 1NSK Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >459 bp
ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
Enzyme 9 GenBank Gene ID X58965 Link Image
Enzyme 9 GeneCard ID NME2 Link Image
Enzyme 9 GenAtlas ID NME2 Link Image
Enzyme 9 HGNC ID HGNC:7850 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 17q21.3
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Stahl JA, Leone A, Rosengard AM, Porter L, King CR, Steeg PS: Identification of a second human nm23 gene, nm23-H2. Cancer Res. 1991 Jan 1;51(1):445-9. [PubMed Link Image]
  2. Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed Link Image]
  3. Postel EH, Berberich SJ, Flint SJ, Ferrone CA: Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis. Science. 1993 Jul 23;261(5120):478-80. [PubMed Link Image]
  4. Valentijn LJ, Koster J, Versteeg R: Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene encodes a novel protein, NM23-LV. Genomics. 2006 Apr;87(4):483-9. Epub 2006 Jan 25. [PubMed Link Image]
  5. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Seifert M, Seib T, Engel M, Dooley S, Welter C: Characterization of the human nm23-H2 promoter region and localization of the microsatellite D17S396. Biochem Biophys Res Commun. 1995 Oct 24;215(3):910-4. [PubMed Link Image]
  8. Iwashita S, Fujii M, Mukai H, Ono Y, Miyamoto M: Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2. Biochem Biophys Res Commun. 2004 Aug 6;320(4):1063-8. [PubMed Link Image]
  9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  10. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  12. Webb PA, Perisic O, Mendola CE, Backer JM, Williams RL: The crystal structure of a human nucleoside diphosphate kinase, NM23-H2. J Mol Biol. 1995 Aug 25;251(4):574-87. [PubMed Link Image]
  13. Morera S, Lacombe ML, Xu Y, LeBras G, Janin J: X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution. Structure. 1995 Dec 15;3(12):1307-14. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5345
Enzyme 10 Name Nucleoside diphosphate kinase 3
Enzyme 10 Synonyms
  1. NDK 3
  2. NDP kinase 3
  3. DR-nm23
  4. Nucleoside diphosphate kinase C
  5. NDPKC
  6. nm23-H3
Enzyme 10 Gene Name NME3
Enzyme 10 Protein Sequence >Nucleoside diphosphate kinase 3
MICLVLTIFANLFPAACTGAHERTFLAVKPDGVQRRLVGEIVRRFERKGFKLVALKLVQA
SEELLREHYAELRERPFYGRLVKYMASGPVVAMVWQGLDVVRTSRALIGATNPADAPPGT
IRGDFCIEVGKNLIHGSDSVESARREIALWFRADELLCWEDSAGHWLYE
Enzyme 10 Number of Residues 169
Enzyme 10 Molecular Weight 19014.9
Enzyme 10 Theoretical pI 7.97
Enzyme 10 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 10 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 10 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Probably has a role in normal hematopoiesis by inhibition of granulocyte differentiation and induction of apoptosis
Enzyme 10 Pathways
Enzyme 10 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 14336763 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q13232 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name NDK3_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >510 bp
ATGATCTGCCTGGTGCTGACCATCTTCGCTAACCTCTTCCCCGCGGCCTGCACCGGCGCA
CACGAACGCACCTTCCTGGCCGTGAAGCCGGACGGCGTGCAGCGGCGGCTGGTGGGCGAG
ATTGTGCGGCGCTTCGAGAGGAAGGGCTTCAAGTTGGTGGCGCTGAAGCTGGTGCAGGCC
TCCGAGGAGCTGCTGCGTGAGCACTACGCCGAGCTGCGTGAACGCCCGTTCTACGGCCGC
CTTGTCAAGTATATGGCCTCCGGGCCGGTGGTGGCCATGGTTTGGCAGGGGCTGGACGTG
GTGCGCACCTCGCGGGCGCTCATCGGAGCCACGAACCCGGCCGACGCCCCGCCCGGCACC
ATCCGCGGGGATTTCTGCATCGAGGTTGGCAAGAACCTGATTCACGGCAGCGACTCGGTG
GAGAGTGCCCGCCGCGAGATCGCTCTCTGGTTCCGCGCAGACGAGCTCCTCTGCTGGGAG
GACAGCGCTGGGCACTGGCTGTATGAGTAG
Enzyme 10 GenBank Gene ID AE006639 Link Image
Enzyme 10 GeneCard ID NME3 Link Image
Enzyme 10 GenAtlas ID NME3 Link Image
Enzyme 10 HGNC ID HGNC:7851 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 16q13
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Venturelli D, Martinez R, Melotti P, Casella I, Peschle C, Cucco C, Spampinato G, Darzynkiewicz Z, Calabretta B: Overexpression of DR-nm23, a protein encoded by a member of the nm23 gene family, inhibits granulocyte differentiation and induces apoptosis in 32Dc13 myeloid cells. Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7435-9. [PubMed Link Image]
  2. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5346
Enzyme 11 Name Nucleoside diphosphate kinase 6
Enzyme 11 Synonyms
  1. NDK 6
  2. NDP kinase 6
  3. Inhibitor of p53-induced apoptosis-alpha
  4. IPIA-alpha
  5. nm23-H6
Enzyme 11 Gene Name NME6
Enzyme 11 Protein Sequence >Nucleoside diphosphate kinase 6
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA
Enzyme 11 Number of Residues 186
Enzyme 11 Molecular Weight 21142.0
Enzyme 11 Theoretical pI 8.49
Enzyme 11 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 11 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 11 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Inhibitor of p53-induced apoptosis
Enzyme 11 Pathways
Enzyme 11 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 3228530 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID O75414 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name NDK6_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >561 bp
ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA
Enzyme 11 GenBank Gene ID AF051941 Link Image
Enzyme 11 GeneCard ID NME6 Link Image
Enzyme 11 GenAtlas ID NME6 Link Image
Enzyme 11 HGNC ID HGNC:20567 Link Image
Enzyme 11 Chromosome Location 3
Enzyme 11 Locus 3p21
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Mehus JG, Deloukas P, Lambeth DO: NME6: a new member of the nm23/nucleoside diphosphate kinase gene family located on human chromosome 3p21.3. Hum Genet. 1999 Jun;104(6):454-9. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5486
Enzyme 12 Name Fucose-1-phosphate guanylyltransferase
Enzyme 12 Synonyms
  1. GDP-L-fucose diphosphorylase
  2. GDP-L-fucose pyrophosphorylase
Enzyme 12 Gene Name FPGT
Enzyme 12 Protein Sequence >Fucose-1-phosphate guanylyltransferase
MAAARDPPEVSLREATQRKLRRFSELRGKLVARGEFWDIVAITAADEKQELAYNQQLSEK
LKRKELPLGVQYHVFVDPAGAKIGNGGSTLCALQCLEKLYGDKWNSFTILLIHSGGYSQR
LPNASALGKIFTALPLGNPIYQMLELKLAMYIDFPLNMNPGILVTCADDIELYSIGEFEF
IRFDKPGFTALAHPSSLTIGTTHGVFVLDPFDDLKHRDLEYRSCHRFLHKPSIEKMYQFN
AVCRPGNFCQQDFAGGDIADLKLDSDYVYTDSLFYMDHKSAKMLLAFYEKIGTLSCEIDA
YGDFLQALGPGATVEYTRNTSNVIKEESELVEMRQRIFHLLKGTSLNVVVLNNSKFYHIG
TTEEYLFYFTSDNSLKSELGLQSITFSIFPDIPECSGKTSCIIQSILDSRCSVAPGSVVE
YSRLGPDVSVGENCIISGSYILTKAALPAHSFVCSLSLKMNRCLKYATMAFGVQDNLKKS
VKTLSDIKLLQFFGVCFLSCLDVWNLKVTEELFSGNKTCLSLWTARIFPVCSSLSDSVIT
SLKMLNAVKNKSAFSLNSYKLLSIEEMLIYKDVEDMITYREQIFLEISLKSSLM
Enzyme 12 Number of Residues 594
Enzyme 12 Molecular Weight 66598.1
Enzyme 12 Theoretical pI 6.44
Enzyme 12 GO Classification Not Available
Enzyme 12 General Function Involved in fucose-1-phosphate guanylyltransferase acti
Enzyme 12 Specific Function Catalyzes the formation of GDP-L-fucose from GTP and L- fucose-1-phosphate. Functions as a salvage pathway to reutilize L- fucose arising from the turnover of glycoproteins and glycolipids
Enzyme 12 Pathways
Enzyme 12 Reactions
  • GTP + beta-L-fucose 1-phosphate = diphosphate + GDP-L-fucose [RN:R01951]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 2582185 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID O14772 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name FPGT_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1785 bp
ATGGCAGCTGCTAGGGACCCTCCGGAAGTATCGCTGCGAGAAGCCACCCAGCGAAAATTG
CGGAGGTTTTCCGAGCTAAGAGGCAAACTTGTAGCACGTGGAGAATTCTGGGACATAGTT
GCAATAACAGCGGCTGATGAAAAACAGGAACTTGCTTACAACCAACAGCTGTCAGAAAAG
CTGAAAAGAAAGGAGTTACCCCTTGGAGTTCAATATCACGTTTTTGTGGATCCTGCTGGA
GCCAAAATTGGAAATGGAGGATCAACACTTTGTGCCCTTCAATGTTTGGAAAAGCTATAT
GGAGATAAATGGAATTCTTTTACCATCTTATTAATTCACTCTGGTGGCTACAGTCAACGA
CTTCCAAATGCAAGTGCTCTGGGAAAAATTTTCACTGCTTTACCTCTTGGTAACCCCATT
TATCAGATGCTAGAATTAAAGCTAGCCATGTACATTGATTTCCCCTTAAATATGAATCCT
GGAATTCTGGTTACCTGTGCAGATGATATTGAACTTTATAGTATTGGAGAATTTGAGTTT
ATTAGGTTTGACAAACCTGGCTTTACTGCTTTAGCTCATCCTTCTAGTTTGACGATAGGT
ACCACACATGGAGTATTTGTCTTAGATCCTTTTGATGATTTAAAACATAGAGACCTTGAA
TACAGGTCTTGCCATCGTTTCCTTCATAAGCCCAGCATAGAAAAGATGTATCAGTTTAAT
GCTGTGTGTAGACCTGGAAATTTTTGTCAACAGGACTTTGCTGGGGGTGACATTGCCGAT
CTTAAATTAGACTCTGACTATGTCTACACAGATAGCCTATTTTATATGGATCATAAATCA
GCAAAAATGTTACTTGCTTTTTATGAAAAAATAGGCACACTGAGCTGTGAAATAGATGCC
TATGGTGACTTTCTGCAGGCTTTGGGACCTGGAGCAACTGTGGAGTACACCAGAAACACA
TCACATGTCATTAAAGAAGAGTCAGAGTTGGTAGAAATGAGGCAGAGAATATTTCATCTT
CTTAAAGGAACATCACTAAATGTTGTTGTTCTTAATAACTCCAAATTTTATCACATTGGA
ACAACCGAAGAATATTTGTTTTACTTTACCTCAGATAACAGTTTAAAGTCAGAGCTCGGC
TTACAGTCCATAACTTTTAGTATCTTTCCAGATATACCAGAATGCTCTGGCAAAACATCC
TGTATCATTCAAAGCATACTGGATTCAAGATGTTCTGTGGCACCTGGCTCAGTTGTGGAG
TATTCCAGATTGGGGCCTGATGTTTCAGTTGGGGAAAACTGCATTATTAGTGGTTCTTAC
ATCCTAACAAAAGCTGCCCTCCCCGCACATTCTTTTGTATGTTCCTTAAGCTTAAAGATG
AATAGATGCTTAAAGTATGCAACTATGGCATTTGGAGTGCAAGACAACTTGAAAAAGAGT
GTGAAAACATTGTCAGATATAAAGTTACTTCAATTCTTTGGAGTCTGTTTCCTGTCATGC
TTAGATGTTTGGAATCTTAAAGTTACAGAGGAACTGTTCTCTGGTAACAAGACATGTCTG
AGTTTGTGGACTGCACGCATTTTCCCAGTTTGTTCTTCTTTGAGTGACTCAGTTATAACA
TCCCTAAAGATGTTAAATGCTGTTAAGAACAAGTCAGCATTCAGCCTGAATAGCTATAAG
TTGCTGTCCATTGAAGAAATGCTTATCTACAAAGATGTAGAAGATATGATAACTTACAGG
GAACAAATTTTTCTAGAAATCAGTTTAAAAAGCAGTTTGATGTAG
Enzyme 12 GenBank Gene ID AF017445 Link Image
Enzyme 12 GeneCard ID FPGT Link Image
Enzyme 12 GenAtlas ID FPGT Link Image
Enzyme 12 HGNC ID HGNC:3825 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 1p31.1
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Pastuszak I, Ketchum C, Hermanson G, Sjoberg EJ, Drake R, Elbein AD: GDP-L-fucose pyrophosphorylase. Purification, cDNA cloning, and properties of the enzyme. J Biol Chem. 1998 Nov 13;273(46):30165-74. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5620
Enzyme 13 Name Alpha-1,3-mannosyltransferase ALG2
Enzyme 13 Synonyms
  1. Asparagine-linked glycosylation protein 2 homolog
  2. GDP-Man:Man(1)GlcNAc(2)-PP-dolichol mannosyltransferase
Enzyme 13 Gene Name ALG2
Enzyme 13 Protein Sequence >Alpha-1,3-mannosyltransferase ALG2
MAEEQGRERDSVPKPSVLFLHPDLGVGGAERLVLDAALALQARGCSVKIWTAHYDPGHCF
AESRELPVRCAGDWLPRGLGWGGRGAAVCAYVRMVFLALYVLFLADEEFDVVVCDQVSAC
IPVFRLARRRKKILFYCHFPDLLLTKRDSFLKRLYRAPIDWIEEYTTGMADCILVNSQFT
AAVFKETFKSLSHIDPDVLYPSLNVTSFDSVVPEKLDDLVPKGKKFLLLSINRYERKKNL
TLALEALVQLRGRLTSQDWERVHLIVAGGYDERVLENVEHYQELKKMVQQSDLGQYVTFL
RSFSDKQKISLLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGF
LCEPDPVHFSEAIEKFIREPSLKATMGLAGRARVKEKFSPEAFTEQLYRYVTKLLV
Enzyme 13 Number of Residues 416
Enzyme 13 Molecular Weight 47091.1
Enzyme 13 Theoretical pI 7.05
Enzyme 13 GO Classification
Function
Process
  • biosynthetic process
  • metabolic process
Component
Enzyme 13 General Function Involved in biosynthetic process
Enzyme 13 Specific Function Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)- dolichol diphosphate
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • 85-105
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 44885912 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q9H553 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name ALG2_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1251 bp
ATGGCGGAGGAGCAGGGCCGGGAACGGGACTCGGTTCCCAAGCCGTCGGTGCTGTTCCTC
CACCCAGACCTGGGCGTGGGCGGCGCTGAGCGGCTGGTGTTGGACGCGGCGCTGGCGCTG
CAGGCGCGCGGGTGTAGCGTGAAGATCTGGACAGCGCACTACGACCCGGGCCACTGTTTC
GCCGAGAGCCGCGAGCTACCGGTGCGCTGTGCCGGGGACTGGCTGCCGCGAGGCCTGGGC
TGGGGCGGCCGCGGCGCCGCCGTCTGCGCCTACGTGCGCATGGTTTTCCTGGCGCTCTAC
GTGCTGTTCCTCGCCGACGAGGAGTTCGACGTGGTAGTGTGCGACCAGGTGTCTGCCTGT
ATCCCAGTGTTCAGGCTGGCTAGACGGCGGAAGAAGATCCTATTTTACTGTCACTTCCCA
GATCTGCTTCTCACCAAGAGAGATTCTTTTCTTAAACGACTATACAGGGCCCCAATTGAC
TGGATAGAGGAATACACCACAGGCATGGCAGACTGCATCTTAGTCAACAGCCAGTTCACA
GCTGCTGTTTTTAAGGAAACATTCAAGTCCCTGTCTCACATAGACCCTGATGTCCTCTAT
CCATCTCTAAATGTCACCAGCTTTGACTCAGTTGTTCCTGAAAAGCTGGATGACCTAGTC
CCCAAGGGGAAAAAATTCCTGCTGCTCTCCATCAACAGATACGAAAGGAAGAAAAATCTG
ACTTTGGCACTGGAAGCCCTAGTACAGCTGCGTGGAAGATTGACATCCCAAGATTGGGAG
AGGGTTCATCTGATCGTGGCAGGTGGTTATGACGAGAGAGTCCTGGAGAATGTGGAACAT
TATCAGGAATTGAAGAAAATGGTCCAACAGTCCGACCTTGGCCAGTATGTGACCTTCTTG
AGGTCTTTCTCAGACAAACAGAAAATCTCCCTCCTCCACAGCTGCACGTGTGTGCTTTAC
ACACCAAGCAATGAGCACTTTGGCATTGTCCCTCTGGAAGCCATGTACATGCAGTGCCCA
GTCATTGCTGTTAATTCGGGTGGACCCTTGGAGTCCATTGACCACAGTGTCACAGGGTTT
CTGTGTGAGCCTGACCCGGTGCACTTCTCAGAAGCAATAGAAAAGTTCATCCGTGAACCT
TCCTTAAAAGCCACCATGGGCCTGGCTGGAAGAGCCAGAGTGAAGGAAAAATTTTCCCCT
GAAGCATTTACAGAACAGCTCTACCGATATGTTACCAAACTGCTGGTATAA
Enzyme 13 GenBank Gene ID AB161356 Link Image
Enzyme 13 GeneCard ID ALG2 Link Image
Enzyme 13 GenAtlas ID ALG2 Link Image
Enzyme 13 HGNC ID HGNC:23159 Link Image
Enzyme 13 Chromosome Location 9
Enzyme 13 Locus 9q22.33
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Thiel C, Schwarz M, Peng J, Grzmil M, Hasilik M, Braulke T, Kohlschutter A, von Figura K, Lehle L, Korner C: A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis. J Biol Chem. 2003 Jun 20;278(25):22498-505. Epub 2003 Apr 8. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5621
Enzyme 14 Name Dolichol-phosphate mannosyltransferase
Enzyme 14 Synonyms
  1. Dolichol-phosphate mannose synthase
  2. DPM synthase
  3. Dolichyl-phosphate beta-D-mannosyltransferase
  4. Mannose-P-dolichol synthase
  5. MPD synthase
Enzyme 14 Gene Name DPM1
Enzyme 14 Protein Sequence >Dolichol-phosphate mannosyltransferase
MASLEVSRSPRRSRRELEVRSPRQNKYSVLLPTYNERENLPLIVWLLVKSFSESGINYEI
IIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLGTAYIHGMKHATGNYIIIMDAD
LSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFLTQILLRPGA
SDLTGSFRLYRKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESK
LGGNEIVSFLKGLLTLFATT
Enzyme 14 Number of Residues 260
Enzyme 14 Molecular Weight 29634.0
Enzyme 14 Theoretical pI 10.02
Enzyme 14 GO Classification Not Available
Enzyme 14 General Function Cell wall/membrane/envelope biogenesis
Enzyme 14 Specific Function Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O- mannosylation of proteins
Enzyme 14 Pathways
Enzyme 14 Reactions
  • GDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl phosphate [RN:R01009]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 4503363 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID O60762 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name DPM1_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >783 bp
ATGGCCTCCTTGGAAGTCAGTCGTAGTCCTCGCAGGTCTCGGCGGGAGCTGGAAGTGCGC
AGTCCACGACAGAACAAATATTCGGTGCTTTTACCTACCTACAACGAGCGCGAGAACCTG
CCGCTCATCGTGTGGCTGCTGGTGAAAAGCTTCTCCGAGAGTGGAATCAACTATGAAATT
ATAATCATAGATGATGGAAGCCCAGATGGAACAAGGGATGTTGCTGAACAGTTGGAGAAG
ATCTATGGGTCAGACAGAATTCTTCTAAGACCACGAGAGAAAAAGTTGGGACTAGGAACT
GCATATATTCATGGAATGAAACATGCCACAGGAAACTACATCATTATTATGGATGCTGAT
CTCTCACACCATCCAAAATTTATTCCTGAATTTATTAGGAAGCAAAAGGAGGGTAATTTT
GATATTGTCTCTGGAACTCGCTACAAAGGAAATGGAGGTGTATATGGCTGGGATTTGAAA
AGAAAAATAATCAGCCGTGGGGCCAATTTTTTAACTCAGATCTTGCTGAGACCAGGAGCA
TCTGATTTAACAGGAAGTTTCAGATTATACCGAAAAGAAGTTCTAGAGAAATTAATAGAA
AAATGTGTTTCTAAAGGCTACGTCTTCCAGATGGAGATGATTGTTCGGGCAAGACAGTTG
AATTATACTATTGGCGAGGTTCCAATATCATTTGTGGATCGTGTTTATGGTGAATCCAAG
TTGGGAGGAAATGAAATAGTATCTTTCTTGAAAGGATTATTGACTCTTTTTGCTACTACA
TAA
Enzyme 14 GenBank Gene ID NM_003859.1 Link Image
Enzyme 14 GeneCard ID DPM1 Link Image
Enzyme 14 GenAtlas ID DPM1 Link Image
Enzyme 14 HGNC ID HGNC:3005 Link Image
Enzyme 14 Chromosome Location 2
Enzyme 14 Locus 20q13.13
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Tomita S, Inoue N, Maeda Y, Ohishi K, Takeda J, Kinoshita T: A homologue of Saccharomyces cerevisiae Dpm1p is not sufficient for synthesis of dolichol-phosphate-mannose in mammalian cells. J Biol Chem. 1998 Apr 10;273(15):9249-54. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Colussi PA, Taron CH, Mack JC, Orlean P: Human and Saccharomyces cerevisiae dolichol phosphate mannose synthases represent two classes of the enzyme, but both function in Schizosaccharomyces pombe. Proc Natl Acad Sci U S A. 1997 Jul 22;94(15):7873-8. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  8. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  10. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  12. Kim S, Westphal V, Srikrishna G, Mehta DP, Peterson S, Filiano J, Karnes PS, Patterson MC, Freeze HH: Dolichol phosphate mannose synthase (DPM1) mutations define congenital disorder of glycosylation Ie (CDG-Ie) J Clin Invest. 2000 Jan;105(2):191-8. [PubMed Link Image]
  13. Imbach T, Schenk B, Schollen E, Burda P, Stutz A, Grunewald S, Bailie NM, King MD, Jaeken J, Matthijs G, Berger EG, Aebi M, Hennet T: Deficiency of dolichol-phosphate-mannose synthase-1 causes congenital disorder of glycosylation type Ie. J Clin Invest. 2000 Jan;105(2):233-9. [PubMed Link Image]
  14. Garcia-Silva MT, Matthijs G, Schollen E, Cabrera JC, Sanchez del Pozo J, Marti Herreros M, Simon R, Maties M, Martin Hernandez E, Hennet T, Briones P: Congenital disorder of glycosylation (CDG) type Ie. A new patient. J Inherit Metab Dis. 2004;27(5):591-600. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5622
Enzyme 15 Name GDP-mannose 4,6 dehydratase
Enzyme 15 Synonyms
  1. GDP-D-mannose dehydratase
  2. GMD
Enzyme 15 Gene Name GMDS
Enzyme 15 Protein Sequence >GDP-mannose 4,6 dehydratase
MAHAPARCPSARGSGDGEMGKPRNVALITGITGQDGSYLAEFLLEKGYEVHGIVRRSSSF
NTGRIEHLYKNPQAHIEGNMKLHYGDLTDSTCLVKIINEVKPTEIYNLGAQSHVKISFDL
AEYTADVDGVGTLRLLDAVKTCGLINSVKFYQASTSELYGKVQEIPQKETTPFYPRSPYG
AAKLYAYWIVVNFREAYNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQLECFSL
GNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVIATGEVHSVREFVEKSFLHIGKTIVWEG
KNENEVGRCKETGKVHVTVDLKYYRPTEVDFLQGDCTKAKQKLNWKPRVAFDELVREMVH
ADVELMRTNPNA
Enzyme 15 Number of Residues 372
Enzyme 15 Molecular Weight 41949.4
Enzyme 15 Theoretical pI 7.35
Enzyme 15 GO Classification
Function
  • GDP-mannose 4,6-dehydratase activity
  • binding
  • carbon-oxygen lyase activity
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • hydro-lyase activity
  • lyase activity
Process
  • GDP-mannose metabolic process
  • alcohol metabolic process
  • cellular metabolic process
  • hexose metabolic process
  • mannose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
  • cell part
  • intracellular
Enzyme 15 General Function Involved in catalytic activity
Enzyme 15 Specific Function Conversion of GDP-D-mannose to GDP-4-keto-6-D- deoxymannose
Enzyme 15 Pathways
Enzyme 15 Reactions
  • GDP-mannose = GDP-4-dehydro-6-deoxy-D-mannose + H2O [RN:R00888]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID O60547 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name GMDS_HUMAN Link Image
Enzyme 15 PDB ID 1T2A Link Image
Enzyme 15 PDB File Show
Enzyme 15 3D Structure
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1119 bp
ATGGCACACGCACCGGCACGCTGCCCCAGCGCCCGGGGCTCCGGGGACGGCGAGATGGGC
AAGCCCAGGAACGTGGCGCTCATCACCGGTATCACAGGCCAGGATGGTTCCTACCTGGCT
GAGTTCCTGCTGGAGAAAGGCTATGAGGTCCATGGAATTGTACGGCGGTCCAGTTCATTT
AATACGGGTCGAATTGAGCATCTGTATAAGAATCCCCAGGCTCACATTGAAGGAAACATG
AAGTTGCACTATGGCGATCTCACTGACAGTACCTGCCTTGTGAAGATCATTAATGAAGTA
AAGCCCACAGAGATCTACAACCTTGGAGCCCAGAGCCACGTCAAAATTTCCTTTGACCTC
GCTGAGTACACTGCGGACGTTGACGGAGTTGGCACTCTACGACTTCTAGATGCAGTTAAG
ACTTGTGGCCTTATCAACTCTGTGAAGTTCTACCAAGCCTCAACAAGTGAACTTTATGGG
AAAGTGCAGGAAATACCCCAGAAGGAGACCACCCCTTTCTATCCCCGGTCACCCTATGGG
GCAGCAAAACTCTATGCCTATTGGATTGTGGTGAACTTCCGTGAGGCGTATAATCTCTTT
GCAGTGAACGGCATTCTCTTCAATCATGAGAGTCCCAGAAGAGGAGCTAATTTCGTTACT
CGAAAAATTAGCCGGTCAGTAGCTAAGATTTACCTTGGACAACTGGAATGTTTCAGTTTG
GGAAATCTGGATGCCAAACGAGATTGGGGCCATGCCAAGGACTATGTGGAGGCTATGTGG
TTGATGTTGCAGAATGATGAGCCGGAGGACTTCGTTATAGCTACTGGGGAGGTCCATAGT
GTCCGGGAATTTGTCGAGAAATCATTCTTGCACATTGGAAAAACCATTGTGTGGGAAGGA
AAGAATGAAAATGAAGTGGGCAGATGTAAAGAGACCGGCAAAGTTCACGTGACTGTGGAT
CTCAAGTACTACCGGCCAACTGAAGTGGACTTTCTGCAGGGCGACTGCACCAAAGCGAAA
CAGAAGCTGAACTGGAAGCCCCGGGTCGCTTTCGATGAGCTGGTGAGGGAGATGGTGCAC
GCCGACGTGGAGCTCATGAGGACAAACCCCAATGCCTGA
Enzyme 15 GenBank Gene ID AF042377 Link Image
Enzyme 15 GeneCard ID GMDS Link Image
Enzyme 15 GenAtlas ID GMDS Link Image
Enzyme 15 HGNC ID HGNC:4369 Link Image
Enzyme 15 Chromosome Location 6
Enzyme 15 Locus 6p25
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Sullivan FX, Kumar R, Kriz R, Stahl M, Xu GY, Rouse J, Chang XJ, Boodhoo A, Potvin B, Cumming DA: Molecular cloning of human GDP-mannose 4,6-dehydratase and reconstitution of GDP-fucose biosynthesis in vitro. J Biol Chem. 1998 Apr 3;273(14):8193-202. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ohyama C, Smith PL, Angata K, Fukuda MN, Lowe JB, Fukuda M: Molecular cloning and expression of GDP-D-mannose-4,6-dehydratase, a key enzyme for fucose metabolism defective in Lec13 cells. J Biol Chem. 1998 Jun 5;273(23):14582-7. [PubMed Link Image]
  5. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5706
Enzyme 16 Name Galactoside 2-alpha-L-fucosyltransferase 2
Enzyme 16 Synonyms
  1. Alpha(1,2)FT 2
  2. Fucosyltransferase 2
  3. GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 2
  4. SE2
  5. Secretor blood group alpha-2-fucosyltransferase
  6. Secretor factor
  7. Se
Enzyme 16 Gene Name FUT2
Enzyme 16 Protein Sequence >Galactoside 2-alpha-L-fucosyltransferase 2
MLVVQMPFSFPMAHFILFVFTVSTIFHVQQRLAKIQAMWELPVQIPVLASTSKALGPSQL
RGMWTINAIGRLGNQMGEYATLYALAKMNGRPAFIPAQMHSTLAPIFRITLPVLHSATAS
RIPWQNYHLNDWMEEEYRHIPGEYVRFTGYPCSWTFYHHLRQEILQEFTLHDHVREEAQK
FLRGLQVNGSRPGTFVGVHVRRGDYVHVMPKVWKGVVADRRYLQQALDWFRARYSSLIFV
VTSNGMAWCRENIDTSHGDVVFAGDGIEGSPAKDFALLTQCNHTIMTIGTFGIWAAYLTG
GDTIYLANYTLPDSPFLKIFKPEAAFLPEWTGIAADLSPLLKH
Enzyme 16 Number of Residues 343
Enzyme 16 Molecular Weight 39016.8
Enzyme 16 Theoretical pI 8.73
Enzyme 16 GO Classification
Function
  • alpha(1,2)-fucosyltransferase activity
  • catalytic activity
  • fucosyltransferase activity
  • galactoside 2-alpha-L-fucosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
  • Golgi apparatus
  • cell part
  • intracellular membrane-bounded organelle
  • membrane
  • membrane-bounded organelle
  • organelle
Enzyme 16 General Function Involved in galactoside 2-alpha-L-fucosyltransferase activity
Enzyme 16 Specific Function Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble A and B antigen synthesis pathway. H and Se enzymes fucosylate the same acceptor substrates but exhibit different Km values
Enzyme 16 Pathways
  • Blood group glycolipid biosynthesis-neolactoseries (map00602 Link Image)
  • Globoside metabolism (map00603 Link Image)
  • Glycosphingolipid biosynthesis - lactoseries (map00601 Link Image)
Enzyme 16 Reactions
  • GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D- galactosyl-(1->4)-beta-D-glucosyl-(11)-ceramide = GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D- glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(11)- ceramide [RN:R04081]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • 15-28
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 60115832 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q10981 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name FUT2_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1032 bp
ATGCTGGTCGTTCAGATGCCTTTCTCCTTTCCCATGGCCCACTTCATCCTCTTTGTCTTT
ACGGTTTCCACTATATTTCACGTTCAGCAGCGGCTAGCGAAGATTCAAGCCATGTGGGAG
TTACCGGTGCAGATACCAGTGCTAGCCTCAACATCAAAGGCACTGGGACCCAGCCAGCTC
AGGGGGATGTGGACGATCAATGCAATAGGCCGCCTGGGGAACCAGATGGGCGAGTACGCC
ACACTGTACGCCCTGGCCAAGATGAACGGGCGGCCCGCCTTCATCCCGGCCCAGATGCAC
AGCACCCTGGCCCCCATCTTCAGAATCACCCTGCCGGTGCTGCACAGCGCCACGGCCAGC
AGGATCCCCTGGCAGAACTACCACCTGAACGACTGGATGGAGGAGGAATACCGCCACATC
CCGGGGGAGTACGTCCGCTTCACCGGCTACCCCTGCTCCTGGACCTTCTACCACCACCTC
CGCCAGGAGATCCTCCAGGAGTTCACCCTGCACGACCACGTGCGGGAGGAGGCCCAGAAG
TTCCTGCGGGGCCTGCAGGTGAACGGGAGCCGGCCGGGCACCTTTGTAGGGGTCCATGTT
CGCCGAGGGGACTATGTCCATGTCATGCCAAAAGTGTGGAAGGGGGTGGTGGCCGACCGG
CGATACCTACAGCAGGCCCTGGACTGGTTCCGAGCTCGCTACAGCTCCCTCATCTTCGTG
GTCACCAGTAATGGCATGGCCTGGTGTCGGGAGAACATTGACACCTCCCACAGTGATGTG
GTGTTTGCTGGCGATGGCATTGAGGGCTCACCTGCCAAAGATTTTGCTCTACTCACACAG
TGTAACCACACCATCATGACCATTGGGACGTTCGGGATCTGGGCCGCATACCTCACGGGC
GGAGACACCATCTACCTGGCCAATTACACCCTCCCCGACTCCCCTTTCCTCAAAATCTTT
AAGCCAGAGGCAGCCTTCCTGCCGGAGTGGACAGGGATTGCCGCAGACCTGTCCCCCTTA
CTCAAGCACTAA
Enzyme 16 GenBank Gene ID AY937240 Link Image
Enzyme 16 GeneCard ID FUT2 Link Image
Enzyme 16 GenAtlas ID FUT2 Link Image
Enzyme 16 HGNC ID HGNC:4013 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 19q13.3
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Kelly RJ, Rouquier S, Giorgi D, Lennon GG, Lowe JB: Sequence and expression of a candidate for the human Secretor blood group alpha(1,2)fucosyltransferase gene (FUT2). Homozygosity for an enzyme-inactivating nonsense mutation commonly correlates with the non-secretor phenotype. J Biol Chem. 1995 Mar 3;270(9):4640-9. [PubMed Link Image]
  2. Kudo T, Iwasaki H, Nishihara S, Shinya N, Ando T, Narimatsu I, Narimatsu H: Molecular genetic analysis of the human Lewis histo-blood group system. II. Secretor gene inactivation by a novel single missense mutation A385T in Japanese nonsecretor individuals. J Biol Chem. 1996 Apr 19;271(16):9830-7. [PubMed Link Image]
  3. Koda Y, Soejima M, Wang B, Kimura H: Structure and expression of the gene encoding secretor-type galactoside 2-alpha-L-fucosyltransferase (FUT2). Eur J Biochem. 1997 Jun 15;246(3):750-5. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Koda Y, Soejima M, Liu Y, Kimura H: Molecular basis for secretor type alpha(1,2)-fucosyltransferase gene deficiency in a Japanese population: a fusion gene generated by unequal crossover responsible for the enzyme deficiency. Am J Hum Genet. 1996 Aug;59(2):343-50. [PubMed Link Image]
  6. Liu Y, Koda Y, Soejima M, Pang H, Schlaphoff T, du Toit ED, Kimura H: Extensive polymorphism of the FUT2 gene in an African (Xhosa) population of South Africa. Hum Genet. 1998 Aug;103(2):204-10. [PubMed Link Image]
  7. Hazra A, Kraft P, Selhub J, Giovannucci EL, Thomas G, Hoover RN, Chanock SJ, Hunter DJ: Common variants of FUT2 are associated with plasma vitamin B12 levels. Nat Genet. 2008 Oct;40(10):1160-2. Epub 2008 Sep 7. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5707
Enzyme 17 Name Galactoside 2-alpha-L-fucosyltransferase 1
Enzyme 17 Synonyms
  1. Alpha(1,2)FT 1
  2. Blood group H alpha 2-fucosyltransferase
  3. Fucosyltransferase 1
  4. GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 1
Enzyme 17 Gene Name FUT1
Enzyme 17 Protein Sequence >Galactoside 2-alpha-L-fucosyltransferase 1
MWLRSHRQLCLAFLLVCVLSVIFFLHIHQDSFPHGLGLSILCPDRRLVTPPVAIFCLPGT
AMGPNASSSCPQHPASLSGTWTVYPNGRFGNQMGQYATLLALAQLNGRRAFILPAMHAAL
APVFRITLPVLAPEVDSRTPWRELQLHDWMSEEYADLRDPFLKLSGFPCSWTFFHHLREQ
IRREFTLHDHLREEAQSVLGQLRLGRTGDRPRTFVGVHVRRGDYLQVMPQRWKGVVGDSA
YLRQAMDWFRARHEAPVFVVTSNGMEWCKENIDTSQGDVTFAGDGQEATPWKDFALLTQC
NHTIMTIGTFGFWAAYLAGGDTVYLANFTLPDSEFLKIFKPEAAFLPEWVGINADLSPLW
TLAKP
Enzyme 17 Number of Residues 365
Enzyme 17 Molecular Weight 41251.1
Enzyme 17 Theoretical pI 7.38
Enzyme 17 GO Classification
Function
  • alpha(1,2)-fucosyltransferase activity
  • catalytic activity
  • fucosyltransferase activity
  • galactoside 2-alpha-L-fucosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
  • Golgi apparatus
  • cell part
  • intracellular membrane-bounded organelle
  • membrane
  • membrane-bounded organelle
  • organelle
Enzyme 17 General Function Involved in galactoside 2-alpha-L-fucosyltransferase activity
Enzyme 17 Specific Function Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble A and B antigen synthesis pathway. H and Se enzymes fucosylate the same acceptor substrates but exhibit different Km values
Enzyme 17 Pathways
  • Blood group glycolipid biosynthesis-neolactoseries (map00602 Link Image)
  • Globoside metabolism (map00603 Link Image)
  • Glycosphingolipid biosynthesis - lactoseries (map00601 Link Image)
Enzyme 17 Reactions
  • GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D- galactosyl-(1->4)-beta-D-glucosyl-(11)-ceramide = GDP + alpha-L-fucosyl-(1->2)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D- glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(11)- ceramide [RN:R04081]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • 9-25
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 2217925 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID P19526 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name FUT1_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1098 bp
ATGTGGCTCCGGAGCCATCGTCAGCTCTGCCTGGCCTTCCTGCTAGTCTGTGTCCTCTCT
GTAATCTTCTTCCTCCATATCCATCAAGACAGCTTTCCACATGGCCTAGGCCTGTCGATC
CTGTGTCCAGACCGCCGCCTGGTGACACCCCCAGTGGCCATCTTCTGCCTGCCGGGTACT
GCGATGGGCCCCAACGCCTCCTCTTCCTGTCCCCAGCACCCTGCTTCCCTCTCCGGCACC
TGGACTGTCTACCCCAATGGCCGGTTTGGTAATCAGATGGGACAGTATGCCACGCTGCTG
GCTCTGGCCCAGCTCAACGGCCGCCGGGCCTTTATCCTGCCTGCCATGCATGCCGCCCTG
GCCCCGGTATTCCGCATCACCCTGCCCGTGCTGGCCCCAGAAGTGGACAGCCGCACGCCG
TGGCGGGAGCTGCAGCTTCACGACTGGATGTCGGAGGAGTACGCGGACTTGAGAGATCCT
TTCCTGAAGCTCTCTGGCTTCCCCTGCTCTTGGACTTTCTTCCACCATCTCCGGGAACAG
ATCCGCAGAGAGTTCACCCTGCACGACCACCTTCGGGAAGAGGCGCAGAGTGTGCTGGGT
CAGCTCCGCCTGGGCCGCACAGGGGACCGCCCGCGCACCTTTGTCGGCGTCCACGTGCGC
CGTGGGGACTATCTGCAGGTTATGCCTCAGCGCTGGAAGGGTGTGGTGGGCGACAGCGCC
CACCTCCGGCAGGCCATGGACTGGTTCCGGGCACGGCACGAAGCCCCCGTTTTCGTGGTC
ACCAGCAACGGCATGGAGTGGTGTAAAGAAAACATCGACACCTCCCAGGGCGATGTGACG
TTTGCTGGCGATGGACAGGAGGCTACACCGTGGAAAGACTTTGCCCTGCTCACACAGTGC
AACCACACCATTATGACCATTGGCACCTTCGGCTTCTGGGCTGCCTACCTGGCTGGCGGA
GACACTGTCTACCTGGCCAACTTCACCCTGCCAGACTCTGAGTTCCTGAAGATCTTTAAG
CCGGAGGCGGCCTTCCTGCCCGAGTGGGTGGGCATTAATGCAGACTTGTCTCCACTCTGG
ACATTGGCTAAGCCTTGA
Enzyme 17 GenBank Gene ID AB004861 Link Image
Enzyme 17 GeneCard ID FUT1 Link Image
Enzyme 17 GenAtlas ID FUT1 Link Image
Enzyme 17 HGNC ID HGNC:4012 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 19q13.3
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Larsen RD, Ernst LK, Nair RP, Lowe JB: Molecular cloning, sequence, and expression of a human GDP-L-fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase cDNA that can form the H blood group antigen. Proc Natl Acad Sci U S A. 1990 Sep;87(17):6674-8. [PubMed Link Image]
  2. Wagner FF, Flegel WA: Polymorphism of the h allele and the population frequency of sporadic nonfunctional alleles. Transfusion. 1997 Mar;37(3):284-90. [PubMed Link Image]
  3. Kaneko M, Nishihara S, Shinya N, Kudo T, Iwasaki H, Seno T, Okubo Y, Narimatsu H: Wide variety of point mutations in the H gene of Bombay and para-Bombay individuals that inactivate H enzyme. Blood. 1997 Jul 15;90(2):839-49. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Kelly RJ, Ernst LK, Larsen RD, Bryant JG, Robinson JS, Lowe JB: Molecular basis for H blood group deficiency in Bombay (Oh) and para-Bombay individuals. Proc Natl Acad Sci U S A. 1994 Jun 21;91(13):5843-7. [PubMed Link Image]
  6. Koda Y, Soejima M, Johnson PH, Smart E, Kimura H: Missense mutation of FUT1 and deletion of FUT2 are responsible for Indian Bombay phenotype of ABO blood group system. Biochem Biophys Res Commun. 1997 Sep 8;238(1):21-5. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 6009
Enzyme 18 Name 6-phosphofructokinase type C
Enzyme 18 Synonyms
  1. 6-phosphofructokinase, platelet type
  2. Phosphofructo-1-kinase isozyme C
  3. PFK-C
  4. Phosphofructokinase 1
  5. Phosphohexokinase
Enzyme 18 Gene Name PFKP
Enzyme 18 Protein Sequence >6-phosphofructokinase type C
MDADDSRAPKGSLRKFLEHLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFI
YEGYQGMVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTREGRLKAACNLLQRGIT
NLCVIGGDGSLTGANLFRKEWSGLLEELARNGQIDKEAVQKYAYLNVVGMVGSIDNDFCG
TDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLP
ESPPEEGWEEQMCVKLSENRARKKRLNIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDT
RVTILGHVQRGGTPSAFDRILASRMGVEAVIALLEATPDTPACVVSLNGNHAVRLPLMEC
VQMTQDVQKAMDERRFQDAVRLRGRSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVINVGA
PAAGMNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWTDVGGWTGQGGSILGTK
RVLPGKYLEEIATQMRTHSINALLIIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVS
NNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGA
DAAYIFEEPFDIRDLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKG
VFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKEARGRGKKFTTDDSICVL
GISKRNVIFQPVAELKKQTDFEHRIPKEQWWLKLRPLMKILAKYKASYDVSDSGQLEHVQ
PWSV
Enzyme 18 Number of Residues 784
Enzyme 18 Molecular Weight 85595.4
Enzyme 18 Theoretical pI 7.60
Enzyme 18 GO Classification
Function
  • 6-phosphofructokinase activity
  • catalytic activity
  • phosphofructokinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
  • 6-phosphofructokinase complex
  • cell part
  • cytoplasm
  • intracellular part
  • macromolecular complex
  • protein complex
Enzyme 18 General Function Involved in 6-phosphofructokinase activity
Enzyme 18 Specific Function ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate
Enzyme 18 Pathways
Enzyme 18 Reactions
  • ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate [RN:R00756]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein Not Available
Enzyme 18 UniProtKB/Swiss-Prot ID Q01813 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name K6PP_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >2355 bp
ATGGACGCGGACGACTCCCGGGCCCCCAAGGGCTCCTTGCGGAAGTTCCTGGAGCACCTC
TCCGGGGCCGGCAAGGCCATCGGCGTGCTGACCAGCGGCGGGGATGCTCAAGGTATGAAC
GCTGCCGTCCGTGCCGTGGTGCGCATGGGTATCTACGTGGGGGCCAAGGTGTACTTCATC
TACGAGGGCTACCAGGGCATGGTGGACGGAGGCTCAAACATCGCAGAGGCCGACTGGGAG
AGTGTCTCCAGCATCCTGCAAGTGGGCGGGACGATCATTGGCAGTGCGCGGTGCCAGGCC
TTCCGCACGCGGGAAGGCCGCCTGAAGGCTGCTTGCAACCTGCTGCAGCGCGGCATCACC
AACCTGTGTGTGATCGGCGGGGACGGGAGCCTCACCGGGGCCAACCTCTTCCGGAAGGAG
TGGAGTGGGCTGCTGGAGGAGCTGGCCAGGAACGGCCAGATCGATAAGGAGGCCGTGCAG
AAGTACGCCTACCTCAACGTGGTGGGCATGGTGGGCTCCATCGACAATGATTTCTGCGGC
ACCGACATGACCATCGGCACGGACTCCGCCCTGCACAGGATCATCGAGGTCGTCGACGCC
ATCATGACCACGGCCCAGAGCCACCAGAGGACCTTCGTTCTGGAGGTGATGGGACGACAC
TGTGGGTACCTGGCCCTGGTGAGTGCCTTGGCCTGCGGTGCGGACTGGGTGTTCCTTCCA
GAATCTCCACCAGAGGAAGGCTGGGAGGAGCAGATGTGTGTCAAACTCTCGGAGAACCGT
GCCCGGAAAAAAAGGCTGAATATTATTATTGTGGCTGAAGGAGCAATTGATACCCAAAAT
AAACCCATCACCTCTGAGAAAATCAAAGAGCTTGTCGTCACGCAGCTGGGCTATGACACA
CGTGTGACCATCCTCGGGCACGTGCAGAGAGGAGGGACCCCTTCGGCATTCGACAGGATC
TTGGCCAGCCGCATGGGAGTGGAGGCAGTCATCGCCTTGCTAGAGGCCACCCCGGACACC
CCAGCTTGCGTCGTGTCACTGAACGGGAACCACGCCGTGCGCCTGCCGCTGATGGAGTGC
GTGCAGATGACTCAGGATGTGCAGAAGGCGATGGACGAGAGGAGATTTCAAGATGCGGTT
CGACTCCGAGGGAGGAGCTTTGCGGGCAACCTGAACACCTACAAGCGACTTGCCATCAAG
CTGCCGGATGATCAGATCCCAAAGACCAATTGCAACGTAGCTGTCATCAACGTGGGGGCA
CCCGCGGCTGGGATGAACGCGGCCGTACGCTCAGCTGTGCGCGTGGGCATTGCCGACGGC
CACAGGATGCTCGCCATCTATGATGGCTTTGACGGCTTCGCCAAGGGCCAGATCAAAGAA
ATCGGCTGGACAGATGTCGGGGGCTGGACCGGCCAAGGAGGCTCCATTCTTGGGACAAAA
CGCGTTCTCCCGGGGAAGTACTTGGAAGAGATCGCCACACAGATGCGCACGCACAGCATC
AACGCGCTGCTGATCATCGGTGGATTCGAGGCCTACCTGGGACTCCTGGAGCTGTCAGCC
GCCCGGGAGAAGCACGAGGAGTTCTGTGTCCCCATGGTCATGGTTCCCGCTACTGTGTCC
AACAATGTGCCGGGTTCCGATTTCAGCATCGGGGCAGACACCGCCCTGAACACTATCACC
GACACCTGCGACCGCATCAAGCAGTCCGCCAGCGGAACCAAGCGGCGCGTGTTCATCATC
GAGACCATGGGCGGCTACTGTGGCTACCTGGCCAACATGGGGGGGCTCGCGGCCGGAGCT
GATGCCGCATACATTTTCGAAGAGCCCTTCGACATCAGGGATCTGCAGTCCAACGTGGAG
CACCTGACGGAGAAAATGAAGACCACCATCCAGAGAGGCCTTGTGCTCAGAAATGAGAGC
TGCAGTGAAAACTACACCACCGACTTCATTTACCAGCTGTATTCAGAAGAGGGCAAAGGC
GTGTTTGACTGCAGGAAGAACGTGCTGGGTCACATGCAGCAGGGTGGGGCACCCTCTCCA
TTTGATAGAAACTTTGGAACCAAAATCTCTGCCAGAGCTATGGAGTGGATCACTGCAAAA
CTCAAGGAGGCCCGGGGCAGAGGAAAAAAATTTACCACCGATGATTCCATTTGTGTGCTG
GGAATAAGCAAAAGAAACGTTATTTTTCAACCTGTGGCAGAGCTGAAGAAGCAAACGGAT
TTTGAGCACAGGATTCCCAAAGAACAGTGGTGGCTCAAGCTACGGCCCCTCATGAAAATC
CTGGCCAAGTACAAGGCCAGCTATGACGTGTCGGACTCAGGCCAGCTGGAACATGTGCAG
CCCTGGAGTGTCTGA
Enzyme 18 GenBank Gene ID D25328 Link Image
Enzyme 18 GeneCard ID PFKP Link Image
Enzyme 18 GenAtlas ID PFKP Link Image
Enzyme 18 HGNC ID HGNC:8878 Link Image
Enzyme 18 Chromosome Location 1
Enzyme 18 Locus 10p15.3-p15.2
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Eto K, Sakura H, Yasuda K, Hayakawa T, Kawasaki E, Moriuchi R, Nagataki S, Yazaki Y, Kadowaki T: Cloning of a complete protein-coding sequence of human platelet-type phosphofructokinase isozyme from pancreatic islet. Biochem Biophys Res Commun. 1994 Feb 15;198(3):990-8. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Simpson CJ, Fothergill-Gilmore LA: Isolation and sequence of a cDNA encoding human platelet phosphofructokinase. Biochem Biophys Res Commun. 1991 Oct 15;180(1):197-203. [PubMed Link Image]
  6. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  7. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  8. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  9. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  10. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  11. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  12. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  13. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 6033
Enzyme 19 Name 6-phosphofructokinase, liver type
Enzyme 19 Synonyms
  1. Phosphofructo-1-kinase isozyme B
  2. PFK-B
  3. Phosphofructokinase 1
  4. Phosphohexokinase
Enzyme 19 Gene Name PFKL
Enzyme 19 Protein Sequence >6-phosphofructokinase, liver type
MAAVDLEKLRASGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVE
GGENIKQANWLSVSNIIQLGGTIIGSARCKAFTTREGRRAAAYNLVQHGITNLCVIGGDG
SLTGANIFRSEWGSLLEELVAEGKISETTARTYSHLNIAGLVGSIDNDFCGTDMTIGTDS
ALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWE
NFMCERLGETRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQ
RGGTPSAFDRILSSKMGMEAVMALLEATPDTPACVVTLSGNQSVRLPLMECVQMTKEVQK
AMDDKRFDEATQLRGGSFENNWNIYKLLAHQKPPKEKSNFSLAILNVGAPAAGMNAAVRS
AVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPKGQLESI
VENIRIYGIHALLVVGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLG
SDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFN
IHDLKVNVEHMTEKMKTDIQRGLVLRNEKCHDYYTTEFLYNLYSSEGKGVFDCRTNVLGH
LQQGGAPTPFDRNYGTKLGVKAMLWLSEKLREVYRKGRVFANAPDSACVIGLKKKAVAFS
PVTELKKDTDFEHRMPREQWWLSLRLMLKMLAQYRISMAAYVSGELEHVTRRTLSMDKGF
Enzyme 19 Number of Residues 780
Enzyme 19 Molecular Weight 85017.8
Enzyme 19 Theoretical pI 7.54
Enzyme 19 GO Classification
Function
  • 6-phosphofructokinase activity
  • catalytic activity
  • phosphofructokinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
  • 6-phosphofructokinase complex
  • cell part
  • cytoplasm
  • intracellular part
  • macromolecular complex
  • protein complex
Enzyme 19 General Function Involved in 6-phosphofructokinase activity
Enzyme 19 Specific Function ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate
Enzyme 19 Pathways
Enzyme 19 Reactions
  • ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate [RN:R00756]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 35431 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID P17858 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name K6PL_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >2343 bp
ATGGCCGCGGTGGACCTGGAGAAGCTGCGGGCGTCGGGCGCGGGCAAGGCCATCGGCGTC
CTGACCAGCGGCGGCGACCGGCAAGGCATGAACGCTGCTGTCCGGGCTGTGACGCGCATG
GGCATTTATGTGGGTGCCAAAGTCTTCCTCATCTACGAGGGCTATGAGGGCCTCGTGGAG
GGAGGTGAGAACATCAAGCAGGCCAACTGGCTGAGCGTCTCCAACATCATCCAGCTGGGC
GGCACTATCATTGGCAGCGCTCGCTCGAAGGCCTTTACCACCAGGGAGGGGCGCCGGGCA
GCGGCCTACAACCTGGTCCAGCACGGCATCACCAACCTGTGCGTCATCGGCGGGGATGGC
AGCCTCACAGGTGCCAACATCTTCCGCAGCGAGTGGGGCAGCCTGCTGGAGGAGCTGGTG
GCGGAAGGTAAGATCTCAGAGACTACAGCCTGGACCTACTCGCACCTGAACATCGCGGGC
CTAGTGGGCTCCATCGATAACGACTTCTGCGGCACCGACATGACCATCGGCACGGACTCG
GCCCTCCACCGCATCATGGAGGTCATCGATGCCATCACCACCACTGCCCAGAGCCACCAG
AGGACCTTCGTGCTGGAAGTGATGGGCCGGCACTGCGGGTACCTGGCGCTGGTATCTGCA
CTGGCCTCAGGGGCCGACTGGCTGTTCATCCCCGAGGCTCCACCCGAGGACGGCTGGGAG
AACTTCATGTGTGAGAGGCTGGGTGAGACTCGGAGCCGTGGGTCCCGACTGAACATCATC
ATCATCGCTGAGGGTGCCATTGACCGCAACGGGAAGCCCATCTCGTCCAGCTACGTGAAG
GACCTGGTGGTTCAGAGGCTGGGCTTCGACACCCGTGTAACTGTGCTGGGCCACGTGCAG
CGGGGAGGGACGCCCTCTGCCTTCGACCGGATCCTGAGCAGCAAGATGGGCATGGAGGCG
GTGATGGCGCTGCTGGAAGCCACGCCTGACACGCCGGCCTGCGTGGTCACCCTCTCGGGG
AACCAGTCAGTGCGGCTGCCCCTCATGGAGTGCGTGCAGATGACCAAGGAAGTGCAGAAA
GCCATGGATGACAAGAGGTTTGACGAGGCCACCCAGCTCCGTGGTGGGAGCTTCGAGAAC
AACTGGAACATTTACAAGCTCCTCACCCACCAGAAGCCCCCCAAGGAGAAGTCTAACTTC
TCCCTGGCCATCCTGAATGTGGGGGCCCCGGCGGCTGGCATGAATGCGGCCGTGCGCTCG
GCGGTGCGGACCGGCATCTCCCATGGACACACAGTATACGTGGTGCACGATGGCTTCGAA
GGCCTAGCCAAGGGTCAGGTGCAAGAAGTAGGCTGGCACGACGTGGCCGGCTGGTTGGGG
CGTGGTGGCTCCATGCTGGGGACCAAGAGGACCCTGCCCAAGGGCCAGCTGGAGTCCATT
GTGGAGAACATCCGCATCTATGGTATTCACGCCCTGCTGGTGGTCGGTGGGTTTGAGGCC
TATGAAGGGGTGCTGCAGCTGGTGGAGGCTCGCGGGCGCTACGAGGAGCTCTGCATCGTC
ATGTGTGTCATCCCAGCCACCATCAGCAACAACGTCCCTGGCACCGACTTCAGCCTGGGC
TCCGACACTGCTGTAAATGCCGCCATGGAGAGCTGTGACCGCATCAAACAGTCTGCCTCG
GGGACCAAGCGCCGTGTGTTCATCGTGGAGACCATGGGGGGTTACTGTGGCTACCTGGCC
ACCGTGACTGGCATTGCTGTGGGGGCCGACGCCGCCTACGTCTTCGAGGACCCTTTCAAC
ATCCACGACTTAAAGGTCAACGTGGAGCACATGACGGAGAAGATGAAGACAGACATTCAG
AGGGGCCTGGTGCTGCGGAACGAGAAGTGCCATGACTACTACACCACGGAGTTCCTGTAC
AACCTGTACTCATCAGAGGGCAAGGGCGTCTTCGACTGCAGGACCAATGTCCTGGGCCAC
CTGCAGCAGGGTGGCGCTCCAACCCCCTTTGACCGGAACTATGGGACCAAGCTGGGGGTG
AAGGCCATGCTGTGGTTGTCGGAGAAGCTGCGCGAGGTTTACCGCAAGGGACGGGTGTTC
GCCAATGCCCCAGACTCGGCCTGCGTGATCGGCCTGAAGAAGAAGGCGGTGGCCTTCAGC
CCCGTCACTGAGCTCAAGAAAGACACTGATTTCGAGCACCGCATGCCACGGGAGCAGTGG
TGGCTGAGCCTGCGGCTCATGCTGAAGATGCTGGCACAATACCGCATCAGTATGGCCGCC
TACGTGTCAGGGGAGCTGGAGCACGTGACCCGCCGCACCCTGAGCATGGACAAGGGCTTC
TGA
Enzyme 19 GenBank Gene ID X15573 Link Image
Enzyme 19 GeneCard ID PFKL Link Image
Enzyme 19 GenAtlas ID PFKL Link Image
Enzyme 19 HGNC ID HGNC:8876 Link Image
Enzyme 19 Chromosome Location 2
Enzyme 19 Locus 21q22.3
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Levanon D, Danciger E, Dafni N, Bernstein Y, Elson A, Moens W, Brandeis M, Groner Y: The primary structure of human liver type phosphofructokinase and its comparison with other types of PFK. DNA. 1989 Dec;8(10):733-43. [PubMed Link Image]
  2. Elson A, Levanon D, Brandeis M, Dafni N, Bernstein Y, Danciger E, Groner Y: The structure of the human liver-type phosphofructokinase gene. Genomics. 1990 May;7(1):47-56. [PubMed Link Image]
  3. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  6. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  7. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 6037
Enzyme 20 Name 6-phosphofructokinase, muscle type
Enzyme 20 Synonyms
  1. Phosphofructo-1-kinase isozyme A
  2. PFK-A
  3. Phosphofructokinase-M
  4. Phosphofructokinase 1
  5. Phosphohexokinase
Enzyme 20 Gene Name PFKM
Enzyme 20 Protein Sequence >6-phosphofructokinase, muscle type
MTHEEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVD
GGDHIKEATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAYNLVKRGITNLCVIGGDG
SLTGADTFRSEWSDLLSDLQKAGKITDEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDS
ALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWE
EHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQ
RGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTK
AMDEKKFDEALKLRGRSFMNNWEVYKLLAHVRPPVSKSGSHTVAVMNVGAPAAGMNAAVR
STVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQ
ISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSV
GADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPF
TIRDLQANVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLG
HMQQGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVF
QPVAELKDQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSDHAHLEHITRKRSGEAAV
Enzyme 20 Number of Residues 780
Enzyme 20 Molecular Weight 85181.9
Enzyme 20 Theoretical pI 8.07
Enzyme 20 GO Classification
Function
  • 6-phosphofructokinase activity
  • catalytic activity
  • phosphofructokinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
  • 6-phosphofructokinase complex
  • cell part
  • cytoplasm
  • intracellular part
  • macromolecular complex
  • protein complex
Enzyme 20 General Function Involved in 6-phosphofructokinase activity
Enzyme 20 Specific Function ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate
Enzyme 20 Pathways
Enzyme 20 Reactions
  • ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate [RN:R00756]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 189855 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P08237 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name K6PF_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >2343 bp
ATGACCCATGAAGAGCACCATGCAGCCAAAACCCTGGGGATTGGCAAAGCCATTGCTGTC
TTAACCTCTGGTGGAGATGCCCAAGGTATGAATGCTGCTGTCAGGGCTGTGGTTCGAGTT
GGTATCTTCACCGGTGCCCGTGTCTTCTTTGTCCATGAGGGTTATCAAGGCCTGGTGGAT
GGTGGAGATCACATCAAGGAAGCCACCTGGGAGAGCGTTTCGATGATGCTTCAGCTGGGA
GGCACGGTGATTGGAAGTGCCCGGTGCAAGGACTTTCGGGAACGAGAAGGACGACTCCGA
GCTGCCTACAACCTGGTGAAGCGTGGGATCACCAATCTCTGTGTCATTGGGGGTGATGGC
AGCCTCACTGGGGCTGACACCTTCCGTTCTGAGTGGAGTGACTTGTTGAGTGACCTCCAG
AAAGCAGGTAAGATCACAGATGAGGAGGCTACGAAGTCCAGCTACCTGAACATTGTGGGC
CTGGTTGGGTCAATTGACAATGACTTCTGTGGCACCGATATGACCATTGGCACTGACTCT
GCCCTGCATCGGATCATGGAAATTGTAGATGCCATCACTACCACTGCCCAGAGCCACCAG
AGGACATTTGTGTTAGAAGTAATGGGCCGCCACTGTGGATACCTGGCCCTTGTCACCTCT
CTGTCCTGTGGGGCCGACTGGGTTTTTATTCCTGAATGTCCACCAGATGACGACTGGGAG
GAACACCTTTGTCGCCGACTCAGCGAGACAAGGACCCGTGGTTCTCGTCTCAACATCATC
ATTGTGGCTGAGGGTGCAATTGACAAGAATGGAAAACCAATCACCTCAGAAGACATCAAG
AATCTGGTGGTTAAGCGTCTGGGATATGACACCCGGGTTACTGTCTTGGGGCATGTGCAG
AGGGGTGGGACGCCATCAGCCTTTGACAGAATTCTGGGCAGCAGGATGGGTGTGGAAGCA
GTGATGGCACTTTTGGAGGGGACCCCAGATACCCCAGCCTGTGTAGTGAGCCTCTCTGGT
AACCAGGCTGTGCGCCTGCCCCTCATGGAATGTGTCCAGGTGACCAAAGATGTGACCAAG
GCCATGGATGAGAAGAAATTTGACGAAGCCCTGAAGCTGAGAGGCCGGAGCTTCATGAAC
AACTGGGAGGTGTACAAGCTTCTAGCTCATGTCAGACCCCCGGTATCTAAGAGTGGTTCG
CACACAGTGGCTGTGATGAACGTGGGGGCTCCGGCTGCAGGCATGAATGCTGCTGTTCGC
TCCACTGTGAGGATTGGCCTTATCCAGGGCAACCGAGTGCTCGTTGTCCATGATGGTTTC
GAGGGCCTGGCCAAGGGGCAGATAGAGGAAGCTGGCTGGAGCTATGTTGGGGGCTGGACT
GGCCAAGGTGGCTCTAAACTTGGGACTAAAAGGACTCTACCCAAGAAGAGCTTTGAACAG
ATCAGTGCCAATATAACTAAGTTTAACATTCAGGGCCTTGTCATCATTGGGGGCTTTGAG
GCTTACACAGGGGGCCTGGAACTGATGGAGGGCAGGAAGCAGTTTGATGAGCTCTGCATC
CCATTTGTGGTCATTCCTGCTACAGTCTCCAACAATGTCCCTGGCTCAGACTTCAGCGTT
GGGGCTGACACAGCACTCAATACTATCTGCACAACCTGTGACCGCATCAAGCAGTCAGCA
GCTGGCACCAAGCGTCGGGTGTTTATCATTGAGACTATGGGTGGCTACTGTGGCTACCTG
GCTACCATGGCTGGACTGGCAGCTGGGGCCGATGCTGCCTACATTTTTGAGGAGCCCTTC
ACCATTCGAGACCTGCAGGCAAATGTTGAACATCTGGTGCAAAAGATGAAAACAACTGTG
AAAAGGGGCTTGGTGTTAAGGAATGAAAAGTGCAATGAGAACTATACCACTGACTTCATT
TTCAACCTGTACTCTGAGGAGGGGAAGGGCATCTTCGACAGCAGGAAGAATGTGCTTGGT
CACATGCAGCAGGGTGGGAGCCCAACCCCATTTGATAGGAATTTTGCCACTAAGATGGGC
GCCAAGGCTATGAACTGGATGTCTGGGAAAATCAAAGAGAGTTACCGTAATGGGCGGATC
TTTGCCAATACTCCAGATTCGGGCTGTGTTCTGGGGATGCGTAAGAGGGCTCTGGTCTTC
CAACCAGTGGCTGAGCTGAAGGACCAGACAGATTTTGAGCATCGAATCCCCAAGGAACAG
TGGTGGCTGAAACTGAGGCCCATCCTCAAAATCCTAGCCAAGTACGAGATTGACTTGGAC
ACTTCAGACCATGCCCACCTGGAGCACATCACCCGGAAGCGGTCCGGGGAAGCTGCCGTC
TAA
Enzyme 20 GenBank Gene ID M26066 Link Image
Enzyme 20 GeneCard ID PFKM Link Image
Enzyme 20 GenAtlas ID PFKM Link Image
Enzyme 20 HGNC ID HGNC:8877 Link Image
Enzyme 20 Chromosome Location 1
Enzyme 20 Locus 12q13.3
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Yamasaki T, Nakajima H, Kono N, Hotta K, Yamada K, Imai E, Kuwajima M, Noguchi T, Tanaka T, Tarui S: Structure of the entire human muscle phosphofructokinase-encoding gene: a two-promoter system. Gene. 1991 Aug 15;104(2):277-82. [PubMed Link Image]
  2. Sharma PM, Reddy GR, Vora S, Babior BM, McLachlan A: Cloning and expression of a human muscle phosphofructokinase cDNA. Gene. 1989 Apr 15;77(1):177-83. [PubMed Link Image]
  3. Nakajima H, Noguchi T, Yamasaki T, Kono N, Tanaka T, Tarui S: Cloning of human muscle phosphofructokinase cDNA. FEBS Lett. 1987 Oct 19;223(1):113-6. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Sharma PM, Reddy GR, Babior BM, McLachlan A: Alternative splicing of the transcript encoding the human muscle isoenzyme of phosphofructokinase. J Biol Chem. 1990 Jun 5;265(16):9006-10. [PubMed Link Image]
  6. Valdez BC, Chen Z, Sosa MG, Younathan ES, Chang SH: Human 6-phosphofructo-1-kinase gene has an additional intron upstream of start codon. Gene. 1989 Mar 15;76(1):167-9. [PubMed Link Image]
  7. Raben N, Sherman JB: Mutations in muscle phosphofructokinase gene. Hum Mutat. 1995;6(1):1-6. [PubMed Link Image]
  8. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  9. Tsujino S, Servidei S, Tonin P, Shanske S, Azan G, DiMauro S: Identification of three novel mutations in non-Ashkenazi Italian patients with muscle phosphofructokinase deficiency. Am J Hum Genet. 1994 May;54(5):812-9. [PubMed Link Image]
  10. Raben N, Exelbert R, Spiegel R, Sherman JB, Nakajima H, Plotz P, Heinisch J: Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency. Am J Hum Genet. 1995 Jan;56(1):131-41. [PubMed Link Image]
  11. Hamaguchi T, Nakajima H, Noguchi T, Nakagawa C, Kuwajima M, Kono N, Tarui S, Matsuzawa Y: Novel missense mutation (W686C) of the phosphofructokinase-M gene in a Japanese patient with a mild form of glycogenosis VII. Hum Mutat. 1996;8(3):273-5. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 6039
Enzyme 21 Name Pyruvate kinase isozymes M1/M2
Enzyme 21 Synonyms
  1. Cytosolic thyroid hormone-binding protein
  2. CTHBP
  3. Opa-interacting protein 3
  4. OIP-3
  5. Pyruvate kinase 2/3
  6. Pyruvate kinase muscle isozyme
  7. Thyroid hormone-binding protein 1
  8. THBP1
  9. Tumor M2-PK
  10. p58
Enzyme 21 Gene Name PKM2
Enzyme 21 Protein Sequence >Pyruvate kinase isozymes M1/M2
MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVET
LKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIR
TGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGL
ISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMV
FASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIE
IPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIM
LSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEAS
FKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQE
AWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP
Enzyme 21 Number of Residues 531
Enzyme 21 Molecular Weight 57936.4
Enzyme 21 Theoretical pI 7.94
Enzyme 21 GO Classification
Function
  • alkali metal ion binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • kinase activity
  • magnesium ion binding
  • metal ion binding
  • potassium ion binding
  • pyruvate kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 21 General Function Involved in magnesium ion binding
Enzyme 21 Specific Function Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival
Enzyme 21 Pathways
Enzyme 21 Reactions
  • ATP + pyruvate = ADP + phosphoenolpyruvate [RN:R00200]
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 33286418 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID P14618 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name KPYM_HUMAN Link Image
Enzyme 21 PDB ID 1F3X Link Image
Enzyme 21 PDB File Show
Enzyme 21 3D Structure
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1596 bp
ATGTCGAAGCCCCATAGTGAAGCCGGGACTGCCTTCATTCAGACCCAGCAGCTGCACGCA
GCCATGGCTGACACATTCCTGGAGCACATGTGCCGCCTGGACATTGATTCACCACCCATC
ACAGCCCGGAACACTGGCATCATCTGTACCATTGGCCCAGCTTCCCGATCAGTGGAGACG
TTGAAGGAGATGATTAAGTCTGGAATGAATGTGGCTCGTCTGAACTTCTCTCATGGAACT
CATGAGTACCATGCGGAGACCATCAAGAATGTGCGCACAGCCACGGAAAGCTTTGCTTCT
GACCCCATCCTCTACCGGCCCGTTGCTGTGGCTCTAGACACTAAAGGACCTGAGATCCGA
ACTGGGCTCATCAAGGGCAGCGGCACTGCAGAGGTGGAGCTGAAGAAGGGAGCCACTCTC
AAAATCACGCTGGATAACGCCTACATGGAAAAGTGTGACGAGAACATCCTGTGGCTGGAC
TACAAGAACATCTGCAAGGTGGTGGAAGTGGGCAGCAAGATCTACGTGGATGATGGGCTT
ATTTCTCTCCAGGTGAAGCAGAAAGGTGCCGACTTCCTGGTGACGGAGGTGGAAAATGGT
GGCTCCTTGGGCAGCAAGAAGGGTGTGAACCTTCCTGGGGCTGCTGTGGACTTGCCTGCT
GTGTCGGAGAAGGACATCCAGGATCTGAAGTTTGGGGTCGAGCAGGATGTTGATATGGTG
TTTGCGTCATTCATCCGCAAGGCATCTGATGTCCATGAAGTTAGGAAGGTCCTGGGAGAG
AAGGGAAAGAACATCAAGATTATCAGCAAAATCGAGAATCATGAGGGGGTTCGGAGGTTT
GATGAAATCCTGGAGGCCAGTGATGGGATCATGGTGGCTCGTGGTGATCTAGGCATTGAG
ATTCCTGCAGAGAAGGTCTTCCTTGCTCAGAAGATGATGATTGGACGGTGCAACCGAGCT
GGGAAGCCTGTCATCTGTGCTACTCAGATGCTGGAGAGCATGATCAAGAAGCCCCGCCCC
ACTCGGGCTGAAGGCAGTGATGTGGCCAATGCAGTCCTGGATGGAGCCGACTGCATCATG
CTGTCTGGAGAAACAGCCAAAGGGGACTATCCTCTGGAGGCTGTGCGCATGCAGCACCTG
ATTGCCCGTGAGGCAGAGGCTGCCATCTACCACTTGCAATTATTTGAGGAACTCCGCCGC
CTGGCGCCCATTACCAGCGACCCCACAGAAGCCACCGCCGTGGGTGCCGTGGAGGCCTCC
TTCAAGTGCTGCAGTGGGGCCATAATCGTCCTCACCAAGTCTGGCAGGTCTGCTCACCAG
GTGGCCAGATACCGCCCACGTGCCCCCATCATTGCTGTGACCCGGAATCCCCAGACAGCT
CGTCAGGCCCACCTGTACCGTGGCATCTTCCCTGTGCTGTGCAAGGACCCAGTCCAGGAG
GCCTGGGCTGAGGACGTGGACCTCCGGGTGAACTTTGCCATGAATGTTGGCAAGGCCCGA
GGCTTCTTCAAGAAGGGAGATGTGGTCATTGTGCTGACCGGATGGCGCCCTGGCTCCGGC
TTCACCAACACCATGCGTGTTGTTCCTGTGCCGTGA
Enzyme 21 GenBank Gene ID NM_002654.3 Link Image
Enzyme 21 GeneCard ID PKM2 Link Image
Enzyme 21 GenAtlas ID PKM2 Link Image
Enzyme 21 HGNC ID HGNC:9021 Link Image
Enzyme 21 Chromosome Location 1
Enzyme 21 Locus 15q22
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Tani K, Yoshida MC, Satoh H, Mitamura K, Noguchi T, Tanaka T, Fujii H, Miwa S: Human M2-type pyruvate kinase: cDNA cloning, chromosomal assignment and expression in hepatoma. Gene. 1988 Dec 20;73(2):509-16. [PubMed Link Image]
  2. Kato H, Fukuda T, Parkison C, McPhie P, Cheng SY: Cytosolic thyroid hormone-binding protein is a monomer of pyruvate kinase. Proc Natl Acad Sci U S A. 1989 Oct;86(20):7861-5. [PubMed Link Image]
  3. Takenaka M, Noguchi T, Sadahiro S, Hirai H, Yamada K, Matsuda T, Imai E, Tanaka T: Isolation and characterization of the human pyruvate kinase M gene. Eur J Biochem. 1991 May 23;198(1):101-6. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Ashizawa K, McPhie P, Lin KH, Cheng SY: An in vitro novel mechanism of regulating the activity of pyruvate kinase M2 by thyroid hormone and fructose 1, 6-bisphosphate. Biochemistry. 1991 Jul 23;30(29):7105-11. [PubMed Link Image]
  8. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  9. Williams JM, Chen GC, Zhu L, Rest RF: Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth. Mol Microbiol. 1998 Jan;27(1):171-86. [PubMed Link Image]
  10. Garcia-Gonzalo FR, Cruz C, Munoz P, Mazurek S, Eigenbrodt E, Ventura F, Bartrons R, Rosa JL: Interaction between HERC1 and M2-type pyruvate kinase. FEBS Lett. 2003 Mar 27;539(1-3):78-84. [PubMed Link Image]
  11. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  12. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  13. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  14. Stetak A, Veress R, Ovadi J, Csermely P, Keri G, Ullrich A: Nuclear translocation of the tumor marker pyruvate kinase M2 induces programmed cell death. Cancer Res. 2007 Feb 15;67(4):1602-8. [PubMed Link Image]
  15. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  16. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  17. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  18. Shimada N, Shinagawa T, Ishii S: Modulation of M2-type pyruvate kinase activity by the cytoplasmic PML tumor suppressor protein. Genes Cells. 2008 Mar;13(3):245-54. [PubMed Link Image]
  19. Lee J, Kim HK, Han YM, Kim J: Pyruvate kinase isozyme type M2 (PKM2) interacts and cooperates with Oct-4 in regulating transcription. Int J Biochem Cell Biol. 2008;40(5):1043-54. Epub 2007 Nov 29. [PubMed Link Image]
  20. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  21. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  22. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  23. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  24. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  25. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  26. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  27. Dombrauckas JD, Santarsiero BD, Mesecar AD: Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis. Biochemistry. 2005 Jul 12;44(27):9417-29. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 6041
Enzyme 22 Name Pyruvate kinase isozymes R/L
Enzyme 22 Synonyms
  1. Pyruvate kinase 1
  2. R-type/L-type pyruvate kinase
  3. Red cell/liver pyruvate kinase
Enzyme 22 Gene Name PKLR
Enzyme 22 Protein Sequence >Pyruvate kinase isozymes R/L
MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQ
LPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFS
HGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKG
SQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQV
ENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAA
LGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRC
NLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKM
QHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRS
AQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESG
KLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
Enzyme 22 Number of Residues 574
Enzyme 22 Molecular Weight 61829.6
Enzyme 22 Theoretical pI 7.83
Enzyme 22 GO Classification
Function
  • alkali metal ion binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • kinase activity
  • magnesium ion binding
  • metal ion binding
  • potassium ion binding
  • pyruvate kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 22 General Function Involved in magnesium ion binding
Enzyme 22 Specific Function Plays a key role in glycolysis
Enzyme 22 Pathways
Enzyme 22 Reactions
  • ATP + pyruvate = ADP + phosphoenolpyruvate [RN:R00200]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein Not Available
Enzyme 22 UniProtKB/Swiss-Prot ID P30613 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name KPYR_HUMAN Link Image
Enzyme 22 PDB ID 1LIU Link Image
Enzyme 22 PDB File Show
Enzyme 22 3D Structure
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1725 bp
ATGTCGATCCAGGAGAACATATCATCCCTGCAGCTTCGGTCATGGGTCTCTAAGTCCCAA
AGAGACTTAGCAAAGTCCATCCTGATTGGGGCTCCAGGAGGGCCAGCGGGGTATCTGCGG
CGGGCCAGTGTGGCCCAACTGACCCAGGAGCTGGGCACTGCCTTCTTCCAGCAGCAGCAG
CTGCCAGCTGCTATGGCAGACACCTTCCTGGAACACCTCTGCCTACTGGACATTGACTCC
GAGCCCGTGGCTGCTCGCAGTACCAGCATCATTGCCACCATCGGGCCAGCATCTCGCTCC
GTGGAGCGCCTCAAGGAGATGATCAAGGCCGGGATGAACATTGCGCGACTCAACTTCTCC
CACGGCTCCCACGAGTACCATGCTGAGTCCATCGCCAACGTCCGGGAGGCGGTGGAGAGC
TTTGCAGGTTCCCCACTCAGCTACCGGCCCGTGGCCATCGCCCTGGACACCAAGGGACCG
GAGATCCGCACTGGGATCCTGCAGGGGGGTCCAGAGTCGGAAGTGGAGCTGGTGAAGGGC
TCCCAGGTGCTGGTGACTGTGGACCCCGCGTTCCGGACGCGGGGGAACGCGAACACCGTG
TGGGTGGACTACCCCAATATTGTCCGGGTCGTGCCGGTGGGGGGCCGCATCTACATTGAC
GACGGGCTCATCTCCCTAGTGGTCCAGAAAATCGGCCCAGAGGGACTGGTGACCCAAGTG
GAGAACGGCGGCGTCCTGGGCAGCCGGAAGGGCGTGAACTTGCCAGGGGCCCAGGTGGAC
TTGCCCGGGCTGTCCGAGCAGGACGTCCGAGACCTGCGCTTCGGGGTGGAGCATGGGGTG
GACATCGTCTTTGCCTCCTTTGTGCGGAAAGCCAGCGACGTGGCTGCCGTCAGGGCTGCT
CTGGGTCCGGAAGGACACGGCATCAAGATCATCAGCAAAATTGAGAACCACGAAGGCGTG
AAGAGGTTTGATGAAATCCTGGAGGTGAGCGACGGCATCATGGTGGCACGGGGGGACCTA
GGCATCGAGATCCCAGCAGAGAAGGTTTTCCTGGCTCAGAAGATGATGATTGGGCGCTGC
AACTTGGCGGGCAAGCCTGTTGTCTGTGCCACACAGATGCTGGAGAGCATGATTACCAAG
CCCCGGCCAACGAGGGCAGAGACAAGCGATGTCGCCAATGCTGTGCTGGATGGGGCTGAC
TGCATCATGCTGTCAGGGGAGACTGCCAAGGGCAACTTCCCTGTGGAAGCGGTGAAGATG
CAGCATGCGATTGCCCGGGAGGCAGAGGCCGCAGTGTACCACCGGCAGCTGTTTGAGGAG
CTACGTCGGGCAGCGCCACTAAGCCGTGATCCCACTGAGGTCACCGCCATTGGTGCTGTG
GAGGCTGCCTTCAAGTGCTGTGCTGCTGCCATCATTGTGCTGACCACAACTGGCCGCTCA
GCCCAGCTTCTGTCTCGGTACCGACCTCGGGCAGCAGTCATTGCTGTCACCCGCTCTGCC
CAGGCTGCCCGCCAGGTCCACTTATGCCGAGGAGTCTTCCCCTTGCTTTACCGTGAACCT
CCAGAAGCCATCTGGGCAGATGATGTAGATCGCCGGGTGCAATTTGGCATTGAAAGTGGA
AAGCTCCGTGGCTTCCTCCGTGTTGGAGACCTGGTGATTGTGGTGACAGGCTGGCGACCT
GGCTCCGGCTACACCAACATCATGAGGGTGCTAAGCATATCCTGA
Enzyme 22 GenBank Gene ID AB015983 Link Image
Enzyme 22 GeneCard ID PKLR Link Image
Enzyme 22 GenAtlas ID PKLR Link Image
Enzyme 22 HGNC ID HGNC:9020 Link Image
Enzyme 22 Chromosome Location 1
Enzyme 22 Locus 1q21
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Kanno H, Fujii H, Hirono A, Miwa S: cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384----Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia. Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):8218-21. [PubMed Link Image]
  2. Tani K, Fujii H, Nagata S, Miwa S: Human liver type pyruvate kinase: complete amino acid sequence and the expression in mammalian cells. Proc Natl Acad Sci U S A. 1988 Mar;85(6):1792-5. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Tani K, Fujii H, Tsutsumi H, Sukegawa J, Toyoshima K, Yoshida MC, Noguchi T, Tanaka T, Miwa S: Human liver type pyruvate kinase: cDNA cloning and chromosomal assignment. Biochem Biophys Res Commun. 1987 Mar 13;143(2):431-8. [PubMed Link Image]
  5. Kanno H, Fujii H, Tsujino G, Miwa S: Molecular basis of impaired pyruvate kinase isozyme conversion in erythroid cells: a single amino acid substitution near the active site and decreased mRNA content of the R-type PK. Biochem Biophys Res Commun. 1993 Apr 15;192(1):46-52. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Beutler E, Baronciani L: Mutations in pyruvate kinase. Hum Mutat. 1996;7(1):1-6. [PubMed Link Image]
  8. Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase. Blood Cells Mol Dis. 1996;22(1):85-9. [PubMed Link Image]
  9. Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (1st update). Blood Cells Mol Dis. 1996;22(3):259-64. [PubMed Link Image]
  10. Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (2nd update). Blood Cells Mol Dis. 1998 Sep;24(3):273-9. [PubMed Link Image]
  11. Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (Third update). Blood Cells Mol Dis. 2000 Feb;26(1):47-53. [PubMed Link Image]
  12. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  13. Valentini G, Chiarelli LR, Fortin R, Dolzan M, Galizzi A, Abraham DJ, Wang C, Bianchi P, Zanella A, Mattevi A: Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia. J Biol Chem. 2002 Jun 28;277(26):23807-14. Epub 2002 Apr 17. [PubMed Link Image]
  14. Neubauer B, Lakomek M, Winkler H, Parke M, Hofferbert S, Schroter W: Point mutations in the L-type pyruvate kinase gene of two children with hemolytic anemia caused by pyruvate kinase deficiency. Blood. 1991 May 1;77(9):1871-5. [PubMed Link Image]
  15. Kanno H, Fujii H, Hirono A, Omine M, Miwa S: Identical point mutations of the R-type pyruvate kinase (PK) cDNA found in unrelated PK variants associated with hereditary hemolytic anemia. Blood. 1992 Mar 1;79(5):1347-50. [PubMed Link Image]
  16. Kanno H, Fujii H, Miwa S: Low substrate affinity of pyruvate kinase variant (PK Sapporo) caused by a single amino acid substitution (426 Arg-->Gln) associated with hereditary hemolytic anemia. Blood. 1993 May 1;81(9):2439-41. [PubMed Link Image]
  17. Baronciani L, Beutler E: Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia. Proc Natl Acad Sci U S A. 1993 May 1;90(9):4324-7. [PubMed Link Image]
  18. Kanno H, Ballas SK, Miwa S, Fujii H, Bowman HS: Molecular abnormality of erythrocyte pyruvate kinase deficiency in the Amish. Blood. 1994 Apr 15;83(8):2311-6. [PubMed Link Image]
  19. Lenzner C, Nurnberg P, Thiele BJ, Reis A, Brabec V, Sakalova A, Jacobasch G: Mutations in the pyruvate kinase L gene in patients with hereditary hemolytic anemia. Blood. 1994 May 15;83(10):2817-22. [PubMed Link Image]
  20. Baronciani L, Beutler E: Molecular study of pyruvate kinase deficient patients with hereditary nonspherocytic hemolytic anemia. J Clin Invest. 1995 Apr;95(4):1702-9. [PubMed Link Image]
  21. Beutler E, Westwood B, van Zwieten R, Roos D: G-->T transition at cDNA nt 110 (K37Q) in the PKLR (pyruvate kinase) gene is the molecular basis of a case of hereditary increase of red blood cell ATP. Hum Mutat. 1997;9(3):282-5. [PubMed Link Image]
  22. Zarza R, Alvarez R, Pujades A, Nomdedeu B, Carrera A, Estella J, Remacha A, Sanchez JM, Morey M, Cortes T, Perez Lungmus G, Bureo E, Vives Corrons JL: Molecular characterization of the PK-LR gene in pyruvate kinase deficient Spanish patients. Red Cell Pathology Group of the Spanish Society of Haematology (AEHH). Br J Haematol. 1998 Nov;103(2):377-82. [PubMed Link Image]
  23. Cohen-Solal M, Prehu C, Wajcman H, Poyart C, Bardakdjian-Michau J, Kister J, Prome D, Valentin C, Bachir D, Galacteros F: A new sickle cell disease phenotype associating Hb S trait, severe pyruvate kinase deficiency (PK Conakry), and an alpha2 globin gene variant (Hb Conakry). Br J Haematol. 1998 Dec;103(4):950-6. [PubMed Link Image]
  24. Pastore L, Della Morte R, Frisso G, Alfinito F, Vitale D, Calise RM, Ferraro F, Zagari A, Rotoli B, Salvatore F: Novel mutations and structural implications in R-type pyruvate kinase-deficient patients from Southern Italy. Hum Mutat. 1998;11(2):127-34. [PubMed Link Image]
  25. Zanella A, Bianchi P, Fermo E, Iurlo A, Zappa M, Vercellati C, Boschetti C, Baronciani L, Cotton F: Molecular characterization of the PK-LR gene in sixteen pyruvate kinase-deficient patients. Br J Haematol. 2001 Apr;113(1):43-8. [PubMed Link Image]
  26. van Wijk R, Huizinga EG, van Wesel AC, van Oirschot BA, Hadders MA, van Solinge WW: Fifteen novel mutations in PKLR associated with pyruvate kinase (PK) deficiency: structural implications of amino acid substitutions in PK. Hum Mutat. 2009 Mar;30(3):446-53. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 6159
Enzyme 23 Name Ectonucleoside triphosphate diphosphohydrolase 4
Enzyme 23 Synonyms
  1. NTPDase 4
  2. Lysosomal apyrase-like protein of 70 kDa
  3. Uridine-diphosphatase
  4. UDPase
Enzyme 23 Gene Name ENTPD4
Enzyme 23 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 4
MGRIGISCLFPASWHFSISPVGCPRILNTNLRQIMVISVLAAAVSLLYFSVVIIRNKYGR
LTRDKKFQRYLARVTDIEATDTNNPNVNYGIVVDCGSSGSRVFVYCWPRHNGNPHDLLDI
RQMRDKNRKPVVMKIKPGISEFATSPEKVSDYISPLLNFAAEHVPRAKHKETPLYILCTA
GMRILPESQQKAILEDLLTDIPVHFDFLFSDSHAEVISGKQEGVYAWIGINFVLGRFEHI
EDDDEAVVEVNIPGSESSEAIVRKRTAGILDMGGVSTQIAYEVPKTVSFASSQQEEVAKN
LLAEFNLGCDVHQTEHVYRVYVATFLGFGGNAARQRYEDRIFANTIQKNRLLGKQTGLTP
DMPYLDPCLPLDIKDEIQQNGQTIYLRGTGDFDLCRETIQPFMNKTNETQTSLNGVYQPP
IHFQNSEFYGFSEFYYCTEDVLRMGGDYNAAKFTKAAKDYCATKWSILRERFDRGLYASH
ADLHRLKYQCFKSAWMFEVFHRGFSFPVNYKSLKTALQVYDKEVQWTLGAILYRTRFLPL
RDIQQEAFRASHTHWRGVSFVYNHYLFSGCFLVVLLAILLYLLRLRRIHRRTPRSSSAAA
LWMEEGLPAQNAPGTL
Enzyme 23 Number of Residues 616
Enzyme 23 Molecular Weight 70254.8
Enzyme 23 Theoretical pI 8.39
Enzyme 23 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 23 General Function Involved in hydrolase activity
Enzyme 23 Specific Function Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent. The order of activity with different substrates is UDP >> GDP = CDP = TDP, AMP, ADP, ATP and UMP are not substrates. Preferred substrates for isoform 2 are CTP, UDP, CDP, GTP and GDP, while isoform 1 utilizes UTP and TTP
Enzyme 23 Pathways
Enzyme 23 Reactions
  • a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • 34-54 560-580
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 4758662 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q9Y227 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name ENTP4_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1851 bp
ATGGGGAGGATTGGCATCTCCTGTCTTTTTCCTGCTTCTTGGCATTTTAGCATATCTCCA
GTAGGGTGTCCTCGAATTCTGAATACCAATTTACGCCAAATTATGGTCATTAGTGTCCTG
GCTGCTGCTGTTTCACTTTTATATTTTTCTGTTGTCATAATCCGAAATAAGTATGGGCGA
CTAACCAGAGACAAGAAATTTCAAAGGTACCTGGCACGAGTTACCGACATTGAAGCTACA
GACACCAATAACCCCAATGTGAACTATGGGATCGTGGTGGACTGTGGTAGCAGTGGGTCT
CGAGTATTTGTTTACTGCTGGCCAAGGCATAATGGCAATCCACATGATCTGTTGGATATC
AGGCAAATGAGGGATAAAAACCGAAAGCCAGTGGTCATGAAGATAAAACCGGGCATTTCA
GAATTTGCTACCTCTCCAGAGAAAGTCAGTGATTACATTTCTCCACTTTTGAACTTTGCT
GCAGAGCATGTGCCACGGGCAAAACACAAAGAGACACCTCTCTACATTCTCTGCACGGCT
GGAATGAGAATCCTCCCCGAAAGCCAGCAGAAAGCTATTCTGGAAGACCTTCTGACCGAT
ATCCCCGTGCACTTTGACTTTCTGTTTTCTGACTCTCATGCAGAAGTAATTTCTGGGAAA
CAAGAAGGTGTGTATGCTTGGATTGGCATTAATTTTGTCCTTGGACGATTTGAGCATATT
GAAGATGATGATGAGGCCGTTGTGGAAGTTAACATTCCTGGAAGTGAAAGCAGCGAAGCC
ATTGTCCGTAAAAGGACAGCGGGCATTCTCGACATGGGCGGCGTGTCGACTCAGATAGCG
TACGAAGTCCCCAAAACTGTAAGCTTTGCGTCCTCACAGCAGGAAGAAGTAGCTAAAAAC
TTGTTAGCTGAATTTAACTTGGGATGTGATGTTCACCAAACTGAGCATGTGTATCGAGTC
TATGTGGCCACGTTTCTTGGGTTTGGTGGCAATGCTGCTCGACAGAGATACGAAGACAGA
ATATTTGCCAACACCATTCAAAAGAACAGGCTCCTGGGTAAACAGACTGGTCTGACTCCT
GATATGCCGTACTTGGACCCCTGCCTACCCCTAGACATTAAAGATGAAATCCAGCAAAAT
GGACAAACCATATACCTACGAGGGACTGGAGACTTTGACCTGTGTCGAGAGACTATCCAG
CCTTTCATGAATAAAACAAACGAGACCCAGACTTCCCTCAATGGGGTCTACCAGCCCCCA
ATTCACTTCCAGAACAGTGAATTCTATGGCTTCTCCGAATTCTACTACTGCACCGAGGAT
GTGTTACGAATGGGGGGAGACTACAATGCTGCTAAATTTACTAAAGCTGCAAAGGATTAT
TGTGCAACAAAGTGGTCCATTTTGCGGGAACGCTTTGACCGAGGACTGTACGCCTCTCAT
GCTGACCTCCACAGGCTTAAGTATCAGTGCTTCAAATCGGCCTGGATGTTTGAGGTGTTT
CATAGGGGCTTTTCGTTTCCTGTCAACTATAAAAGCTTAAAGACTGCCTTGCAAGTTTAC
GACAAGGAGGTTCAGTGGACCCTTGGAGCCATCCTCTACAGGACCCGCTTTCTACCATTA
AGAGACATCCAGCAGGAGGCCTTCCGAGCCAGTCACACCCACTGGCGGGGCGTTTCCTTT
GTCTACAACCACTACCTGTTCTCTGGCTGCTTCCTGGTGGTGCTGCTGGCCATCCTGCTG
TACCTGCTGCGGCTGCGGCGCATCCACAGGCGCACTCCCCGGAGCAGCTCGGCCGCCGCC
CTCTGGATGGAGGAGGGCCTTCCCGCCCAGAATGCCCCGGGGACCTTGTGA
Enzyme 23 GenBank Gene ID NM_004901.3 Link Image
Enzyme 23 GeneCard ID ENTPD4 Link Image
Enzyme 23 GenAtlas ID ENTPD4 Link Image
Enzyme 23 HGNC ID HGNC:14573 Link Image
Enzyme 23 Chromosome Location 8
Enzyme 23 Locus 8p21.3
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Wang TF, Guidotti G: Golgi localization and functional expression of human uridine diphosphatase. J Biol Chem. 1998 May 1;273(18):11392-9. [PubMed Link Image]
  2. Biederbick A, Rose S, Elsasser HP: A human intracellular apyrase-like protein, LALP70, localizes to lysosomal/autophagic vacuoles. J Cell Sci. 1999 Aug;112 ( Pt 15):2473-84. [PubMed Link Image]
  3. Biederbick A, Kosan C, Kunz J, Elsasser HP: First apyrase splice variants have different enzymatic properties. J Biol Chem. 2000 Jun 23;275(25):19018-24. [PubMed Link Image]
  4. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
  5. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 6160
Enzyme 24 Name Ectonucleoside triphosphate diphosphohydrolase 6
Enzyme 24 Synonyms
  1. NTPDase 6
  2. CD39 antigen-like 2
Enzyme 24 Gene Name ENTPD6
Enzyme 24 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 6
MKKGIRYETSRKTSYIFQQPQHGPWQTRMRKISNHGSLRVAKVAYPLGLCVGVFIYVAYI
KWHRATATQAFFSITRAAPGARWGQQAHSPLGTAADGHEVFYGIMFDAGSTGTRVHVFQF
TRPPRETPTLTHETFKALKPGLSAYADDVEKSAQGIRELLDVAKQDIPFDFWKATPLVLK
ATAGLRLLPGEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITINFLTGSLK
TPGGSSVGMLDLGGGSTQIAFLPRVEGTLQASPPGYLTALRMFNRTYKLYSYSYLGLGLM
SARLAILGGVEGQPAKDGKELVSPCLSPSFKGEWEHAEVTYRVSGQKAAASLHELCAARV
SEVLQNRVHRTEEVKHVDFYAFSYYYDLAAGVGLIDAEKGGSLVVGDFEIAAKYVCRTLE
TQPQSSPFSCMDLTYVSLLLQEFGFPRSKVLKLTRKIDNVETSWALGAIFHYIDSLNRQK
SPAS
Enzyme 24 Number of Residues 484
Enzyme 24 Molecular Weight 53246.7
Enzyme 24 Theoretical pI 9.52
Enzyme 24 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 24 General Function Involved in hydrolase activity
Enzyme 24 Specific Function Might support glycosylation reactions in the Golgi apparatus and, when released from cells, might catalyze the hydrolysis of extracellular nucleotides. Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent, there is no hydrolysis of nucleoside 5'-monophosphates. The order of activity with different substrates is GDP > IDP >> UDP = CDP >> ADP
Enzyme 24 Pathways
Enzyme 24 Reactions
  • a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • 40-60
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 3335098 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID O75354 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name ENTP6_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >1455 bp
ATGAAAAAAGGTATCCGTTATGAAACTTCCAGAAAAACGAGCTACATTTTTCAGCAGCCG
CAGCACGGTCCTTGGCAAACAAGGATGAGAAAAATATCCAACCACGGGAGCCTGCGGGTG
GCGAAGGTGGCATACCCCCTGGGGCTGTGTGTGGGCGTGTTCATCTATGTTGCCTACATC
AAGTGGCACCGGGCCACCGCCACCCAGGCCTTCTTCAGCATCACCAGGGCAGCCCCGGGG
GCCCGGTGGGGTCAGCAGGCCCACAGCCCCCTGGGGACAGCTGCAGACGGGCACGAGGTC
TTCTACGGGATCATGTTTGATGCAGGAAGCACTGGCACCCGAGTACACGTCTTCCAGTTC
ACCCGGCCCCCCAGAGAAACTCCCACGTTAACCCACGAAACCTTCAAAGCAGTGAAGCCA
GGTCTTTCTGCCTATGCTGATGATGTTGAAAAGAGCGCTCAGGGAATCCGGGAACTACTG
GATGTTGCTAAACAGGACATTCCGTTCGACTTCTGGAAGGCCACCCCTCTGGTCCTCAAG
GCCACAGCTGGCTTACGCCTGTTACCTGGAGAAAAGGCCCAGAAGTTACTGCAGAAGGTG
AAAGAAGTATTTAAAGCATCGCCTTTCCTTGTAGGGGATGACTGTGTTTCCATCATGAAC
GGAACAGATGAAGGCGTTTCGGCGTGGATCACCATCAACTTCCTGACAGGCAGCTTGAAA
ACTCCAGGAGGGAGCAGCGTGGGCATGCTGGACTTGGGCGGAGGATCCACTCAGATCGCC
TTCCTGCCACGCGTGGAGGGCACCCTGCAGGCCTCCCCACCCGGCTACCTGACGGCACTG
CGGATGTTTAACAGGACCTACAAGCTCTATTCCTACAGCTACCTCGGGCTCGGGCTGATG
TCGGCACGCCTGGCGATCCTGGGCGGCGTGGAGGGGCAGCCTGCTAAGGATGGAAAGGAG
TTGGTCAGCCCTTGCTTGTCTCCCAGTTTCAAAGGAGAGTGGGAACACGCAGAAGTCACG
TACAGGGTTTCAGGGCAGAAAGCAGCGGCAAGCCTGCACGAGCTGTGTGCTGCCAGAGTG
TCAGAGGTCCTTCAAAACAGAGTGCACAGGACGGAGGAAGTGAAGCATGTGGACTTCTAT
GCTTTCTCCTACTATTACGACCTTGCAGCTGGTGTGGGCCTCATAGATGCGGAGAAGGGA
GGCAGCCTGGTGGTGGGGGACTTCGAGATCGCAGCCAAGTACGTGTGTCGGACCCTGGAG
ACACAGCCGCAGAGCAGCCCCTTCTCATGCATGGACCTCACCTACGTCAGCCTGCTACTC
CAGGAGTTCGGCTTTCCCAGGAGCAAAGTGCTGAAGCTCACTCGGAAAATTGACAATGTT
GAGACCAGCTGGGCTCTGGGGGCCATTTTTCATTACATCGACTCCCTGAACAGACAGAAG
AGTCCAGCCTCATAG
Enzyme 24 GenBank Gene ID AF039916 Link Image
Enzyme 24 GeneCard ID ENTPD6 Link Image
Enzyme 24 GenAtlas ID ENTPD6 Link Image
Enzyme 24 HGNC ID HGNC:3368 Link Image
Enzyme 24 Chromosome Location 2
Enzyme 24 Locus 20p11.21
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Chadwick BP, Frischauf AM: The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster. Genomics. 1998 Jun 15;50(3):357-67. [PubMed Link Image]
  2. Ivanenkov VV, Murphy-Piedmonte DM, Kirley TL: Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function. Biochemistry. 2003 Oct 14;42(40):11726-35. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Yeung G, Mulero JJ, McGowan DW, Bajwa SS, Ford JE: CD39L2, a gene encoding a human nucleoside diphosphatase, predominantly expressed in the heart. Biochemistry. 2000 Oct 24;39(42):12916-23. [PubMed Link Image]
  7. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 6161
Enzyme 25 Name Ectonucleoside triphosphate diphosphohydrolase 5
Enzyme 25 Synonyms
  1. NTPDase 5
  2. CD39 antigen-like 4
  3. ER-UDPase
  4. Nucleoside diphosphatase
Enzyme 25 Gene Name ENTPD5
Enzyme 25 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 5
MATSWGTVFFMLVVSCVCSAVSHRNQQTWFEGIFLSSMCPINVSASTLYGIMFDAGSTGT
RIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHW
KKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTV
NFLTGQLHGHRQETVGTLDLGGASTQITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTH
SYLGFGLKAARLATLGALETEGTDGHTFRSACLPRWLEAEWIFGGVKYQYGGNQEGEVGF
EPCYAEVLRVVRGKLHQPEEVQRGSFYAFSYYYDRAVDTDMIDYEKGGILKVEDFERKAR
EVCDNLENFTSGSPFLCMDLSYITALLKDGFGFADSTVLQLTKKVNNIETGWALGATFHL
LQSLGISH
Enzyme 25 Number of Residues 428
Enzyme 25 Molecular Weight 47517.0
Enzyme 25 Theoretical pI 6.29
Enzyme 25 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 25 General Function Involved in hydrolase activity
Enzyme 25 Specific Function Likely to promote reglycosylation reactions involved in glycoproteins folding and quality control in the endoplasmic reticulum. Hydrolyzes UDP, GDP and IDP but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate
Enzyme 25 Pathways
Enzyme 25 Reactions
  • a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • 1-20
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 3335102 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID O75356 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name ENTP5_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >1287 bp
ATGGCCACTTCTTGGGGCACAGTCTTTTTCATGCTGGTGGTATCCTGTGTTTGCAGCGCT
GTCTCCCACAGGAACCAGCAGACTTGGTTTGAGGGTATCTTCCTGTCTTCCATGTGCCCC
ATCAATGTCAGCGCCAGCACCTTGTATGGAATTATGTTTGATGCAGGGAGCACTGGAACT
CGAATTCATGTTTACACCTTTGTGCAGAAAATGCCAGGACAGCTTCCAATTCTAGAAGGG
GAAGTTTTTGATTCTGTGAAGCCAGGACTTTCTGCTTTTGTAGATCAACCTAAGCAGGGT
GCTGAGACCGTTCAAGGGCTCTTAGAGGTGGCCAAAGACTCAATCCCCCGAAGTCACTGG
AAAAAGACCCCAGTGGTCCTAAAGGCAACAGCAGGACTACGCTTACTGCCAGAACACAAA
GCCAAGGCTCTGCTCTTTGAGGTAAAGGAGATCTTCAGGAAGTCACCTTTCCTGGTACCA
AAGGGCAGTGTTAGCATCATGGATGGATCCGACGAAGGCATATTAGCTTGGGTTACTGTG
AATTTTCTGACAGGTCAGCTGCATGGCCACAGACAGGAGACTGTGGGGACCTTGGACCTA
GGGGGAGCCTCCACCCAAATCACGTTCCTGCCCCAGTTTGAGAAAACTCTGGAACAAACT
CCTAGGGGCTACCTCACTTCCTTTGAGATGTTTAACAGCACTTATAAGCTCTATACACAT
AGTTACTTGGGATTTGGATTGAAAGCTGCAAGACTAGCAACCCTGGGAGCCCTGGAGACA
GAAGGGACTGATGGGCACACTTTCCGGAGTGCCTGTTTACCGAGATGGTTGGAAGCAGAG
TGGATCTTTGGGGGTGTGAAATACCAGTATGGTGGCAACCAAGAAGGGGAGGTGGGCTTT
GAGCCCTGCTATGCCGAAGTGCTGAGGGTGGTACGAGGAAAACTTCACCAGCCAGAGGAG
GTCCAGAGAGGTTCCTTCTATGCTTTCTCTTACTATTATGACCGAGCTGTTGACACAGAC
ATGATTGATTATGAAAAGGGGGGTATTTTAAAAGTTGAAGATTTTGAAAGAAAAGCCAGG
GAAGTGTGTGATAACTTGGAAAACTTCACCTCAGGCAGTCCTTTCCTGTGCATGGATCTC
AGCTACATCACAGCCCTGTTAAAGGATGGCTTTGGCTTTGCAGACAGCACAGTCTTACAG
CTCACAAAGAAAGTGAACAACATAGAGACGGGCTGGGCCTTGGGGGCCACCTTTCACCTG
TTGCAGTCTCTGGGCATCTCCCATTGA
Enzyme 25 GenBank Gene ID AF039918 Link Image
Enzyme 25 GeneCard ID ENTPD5 Link Image
Enzyme 25 GenAtlas ID ENTPD5 Link Image
Enzyme 25 HGNC ID HGNC:3367 Link Image
Enzyme 25 Chromosome Location 1
Enzyme 25 Locus 14q24
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Chadwick BP, Frischauf AM: The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster. Genomics. 1998 Jun 15;50(3):357-67. [PubMed Link Image]
  2. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  3. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 6162
Enzyme 26 Name Adenylosuccinate synthetase isozyme 2
Enzyme 26 Synonyms
  1. AMPSase 2
  2. AdSS 2
  3. Adenylosuccinate synthetase, acidic isozyme
  4. Adenylosuccinate synthetase, liver isozyme
  5. L-type adenylosuccinate synthetase
  6. IMP--aspartate ligase 2
Enzyme 26 Gene Name ADSS
Enzyme 26 Protein Sequence >Adenylosuccinate synthetase isozyme 2
MAFAETYPAASSLPNGDCGRPRARPGGNRVTVVLGAQWGDEGKGKVVDLLAQDADIVCRC
QGGNNAGHTVVVDSVEYDFHLLPSGIINPNVTAFIGNGVVIHLPGLFEEAEKNVQKGKGL
EGWEKRLIISDRAHIVFDFHQAADGIQEQQRQEQAGKNLGTTKKGIGPVYSSKAARSGLR
MCDLVSDFDGFSERFKVLANQYKSIYPTLEIDIEGELQKLKGYMEKIKPMVRDGVYFLYE
ALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGMPPQNVGEVYGVVKAY
TTRVGIGAFPTEQDNEIGELLQTRGREFGVTTGRKRRCGWLDLVLLKYAHMINGFTALAL
TKLDILDMFTEIKVGVAYKLDGEIIPHIPANQEVLNKVEVQYKTLPGWNTDISNARAFKE
LPVNAQNYVRFIEDELQIPVKWIGVGKSRESMIQLF
Enzyme 26 Number of Residues 456
Enzyme 26 Molecular Weight 50097.1
Enzyme 26 Theoretical pI 6.52
Enzyme 26 GO Classification
Function
  • GTP binding
  • adenylosuccinate synthase activity
  • binding
  • catalytic activity
  • cation binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • ion binding
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • magnesium ion binding
  • metal ion binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 26 General Function Involved in adenylosuccinate synthase activity
Enzyme 26 Specific Function Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP
Enzyme 26 Pathways
Enzyme 26 Reactions
  • GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP [RN:R01135]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 34577063 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P30520 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name PURA2_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >1371 bp
ATGGCGTTCGCCGAGACCTACCCGGCGGCATCCTCCCTGCCCAACGGCGATTGCGGCCGC
CCCAGGGCGCGGCCCGGAGGAAACCGGGTGACGGTGGTGCTCGGTGCGCAGTGGGGCGAC
GAAGGCAAAGGGAAGGTGGTGGACCTGCTGGCGCAGGACGCCGACATCGTGTGCCGCTGC
CAGGGAGGAAATAATGCTGGCCATACAGTTGTTGTGGATTCTGTGGAATATGATTTTCAT
CTCTTACCCAGTGGAATAATTAATCCAAATGTCACTGCATTCATTGGAAATGGTGTGGTA
ATTCATCTACCTGGATTGTTTGAAGAAGCAGAGAAAAATGTTCAAAAAGGAAAAGGACTA
GAAGGCTGGGAAAAAAGGCTTATTATATCTGACAGAGCTCATATTGTATTTGATTTTCAT
CAAGCAGCTGATGGTATCCAGGAACAACAGAGACAAGAACAAGCAGGAAAAAATTTGGGT
ACAACAAAAAAGGGCATTGGCCCAGTTTATTCGTCCAAAGCTGCTCGGAGTGGACTCAGG
ATGTGCGACCTTGTTTCTGACTTTGATGGCTTCTCTGAGAGGTTTAAAGTTCTAGCTAAC
CAATACAAATCTATATACCCCACTTTGGAAATAGACATTGAAGGTGAATTACAAAAACTC
AAGGGTTATATGGAAAAGATTAAACCAATGGTGAGAGATGGAGTTTATTTTCTATATGAG
GCCCTACATGGACCACCAAAGAAAATCTTGGTAGAAGGTGCAAATGCAGCACTATTAGAT
ATTGATTTTGGGACTTACCCTTTTGTAACCTCTTCAAATTGTACTGTTGGAGGTGTTTGT
ACTGGTTTGGGTATGCCACCTCAAAATGTTGGAGAAGTGTATGGAGTTGTGAAAGCTTAT
ACAACTAGAGTTGGTATTGGTGCCTTTCCTACAGAGCAAGACAATGAAATTGGAGAATTA
TTACAAACAAGGGGTAGAGAGTTTGGTGTAACTACTGGAAGGAAAAGAAGATGTGGCTGG
TTGGACCTCGTTTTGCTCAAATATGCTCATATGATCAATGGATTTACTGCGTTGGCACTT
ACCAAGTTGGATATTTTGGACATGTTTACGGAAATCAAAGTTGGAGTTGCTTACAAGTTA
GATGGTGAAATCATACCTCATATCCCAGCAAACCAAGAAGTCTTAAATAAAGTTGAAGTT
CAATATAAGACTCTCCCAGGATGGAACACAGACATATCAAATGCAAGGGCGTTTAAAGAA
CTACCTGTTAATGCACAAAACTATGTTCGATTTATTGAAGATGAGCTTCAAATTCCAGTT
AAGTGGATTGGTGTTGGTAAATCCAGAGAATCTATGATTCAACTCTTTTAA
Enzyme 26 GenBank Gene ID NM_001126 Link Image
Enzyme 26 GeneCard ID ADSS Link Image
Enzyme 26 GenAtlas ID ADSS Link Image
Enzyme 26 HGNC ID HGNC:292 Link Image
Enzyme 26 Chromosome Location 1
Enzyme 26 Locus 1cen-q12
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Powell SM, Zalkin H, Dixon JE: Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase. FEBS Lett. 1992 May 25;303(1):4-10. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 6166
Enzyme 27 Name Adenylosuccinate synthetase isozyme 1
Enzyme 27 Synonyms
  1. AMPSase 1
  2. AdSS 1
  3. Adenylosuccinate synthetase, basic isozyme
  4. Adenylosuccinate synthetase, muscle isozyme
  5. M-type adenylosuccinate synthetase
  6. IMP--aspartate ligase 1
Enzyme 27 Gene Name ADSSL1
Enzyme 27 Protein Sequence >Adenylosuccinate synthetase isozyme 1
MSGTRASNDRPPGAGGVKRGRLQQEAAATGSRVTVVLGAQWGDEGKGKVVDLLATDADII
SRCQGGNNAGHTVVVDGKEYDFHLLPSGIINTKAVSFIGNGVVIHLPGLFEEAEKNEKKG
LKDWEKRLIISDRAHLVFDFHQAVDGLQEVQRQAQEGKNIGTTKKGIGPTYSSKAARTGL
RICDLLSDFDEFSSRFKNLAHQHQSMFPTLEIDIEGQLKRLKGFAERIRPMVRDGVYFMY
EALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDVYGVVKA
YTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALA
LTKLDILDVLGEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWE
DLPPQAQNYIRFVENHVGVAVKWVGVGKSRESMIQLF
Enzyme 27 Number of Residues 457
Enzyme 27 Molecular Weight 50208.2
Enzyme 27 Theoretical pI 8.85
Enzyme 27 GO Classification
Function
  • GTP binding
  • adenylosuccinate synthase activity
  • binding
  • catalytic activity
  • cation binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • ion binding
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • magnesium ion binding
  • metal ion binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 27 General Function Involved in adenylosuccinate synthase activity
Enzyme 27 Specific Function Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP
Enzyme 27 Pathways
Enzyme 27 Reactions
  • GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP [RN:R01135]
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein Not Available
Enzyme 27 UniProtKB/Swiss-Prot ID Q8N142 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name PURA1_HUMAN Link Image
Enzyme 27 PDB ID 1MF1 Link Image
Enzyme 27 PDB File Show
Enzyme 27 3D Structure
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >1374 bp
ATGTCGGGGACCCGAGCCTCCAACGACCGGCCCCCCGGCGCAGGCGGCGTCAAGCGGGGG
CGGCTGCAGCAGGAGGCGGCGGCGACCGGCTCCCGCGTGACGGTGGTGCTGGGCGCGCAG
TGGGGGGACGAGGGCAAAGGCAAGGTGGTGGACCTGCTGGCCACGGACGCCGACATCATC
AGCCGCTGCCAGGGGGGCAACAACGCCGGCCACACGGTGGTGGTGGATGGGAAAGAGTAC
GACTTCCACCTGCTGCCCAGCGGCATCATCAACACCAAGGCCGTGTCCTTCATTGGCAAC
GGGGTGGTCATCCACTTGCCAGGCTTGTTTGAGGAAGCAGAGAAGAATGAAAAGAAAGGC
CTGAAGGACTGGGAGAAGAGGCTCATCATCTCTGACAGAGCCCACCTTGTGTTTGATTTT
CACCAGGCTGTCGACGGACTTCAGGAAGTGCAGCGCCAGGCACAAGAGGGGAAGAATATA
GGCACCACCAAGAAGGGAATCGGACCAACCTACTCTTCCAAAGCTGCCCGGACAGGCCTC
CGCATCTGCGACCTCCTGTCAGATTTTGATGAGTTTTCCTCCAGATTCAAGAACCTGGCC
CACCAGCACCAGTCGATGTTCCCCACCCTGGAAATAGACATTGAAGGCCAACTCAAAAGG
CTCAAGGGCTTTGCTGAGCGGATCAGACCCATGGTCCGAGATGGTGTTTACTTTATGTAT
GAGGCACTCCACGGCCCCCCCAAGAAGATCCTGGTGGAGGGTGCCAACGCCGCCCTCCTC
GACATTGACTTCGGGACCTACCCCTTTGTGACTTCATCCAACTGCACCGTGGGCGGTGTG
TGCACGGGCCTGGGCATCCCCCCGCAGAACATAGGTGACGTGTATGGCGTGGTGAAAGCC
TATACCACACGTGTGGGCATCGGGGCCTTCCCCACCGAGCAGATCAACGAGATTGGAGGC
CTGCTGCAGACCCGCGGCCACGAGTGGGGAGTGACCACAGGCAGGAAGAGGCGCTGCGGC
TGGCTCGACCTGATGATTCTAAGATATGCTCACATGGTCAACGGATTCACTGCGCTGGCC
CTGACGAAGCTGGACATCCTGGACGTACTGGGTGAGGTTAAAGTCGGTGTCTCATACAAG
CTGAACGGGAAAAGGATTCCCTATTTCCCAGCTAACCAGGAGATGCTTCAGAAGGTCGAA
GTTGAGTATGAAACGCTGCCTGGGTGGAAAGCAGACACCACAGGCGCCAGGAGGTGGGAG
GACCTGCCCCCACAGGCCCAGAACTACATCCGCTTTGTGGAGAATCACGTGGGAGTCGCA
GTCAAATGGGTTGGTGTTGGCAAGTCAAGAGAGTCGATGATCCAGCTGTTTTAG
Enzyme 27 GenBank Gene ID AY037159 Link Image
Enzyme 27 GeneCard ID ADSSL1 Link Image
Enzyme 27 GenAtlas ID ADSSL1 Link Image
Enzyme 27 HGNC ID HGNC:20093 Link Image
Enzyme 27 Chromosome Location 1
Enzyme 27 Locus 14q32.33
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Sun H, Li N, Wang X, Chen T, Shi L, Zhang L, Wang J, Wan T, Cao X: Molecular cloning and characterization of a novel muscle adenylosuccinate synthetase, AdSSL1, from human bone marrow stromal cells. Mol Cell Biochem. 2005 Jan;269(1-2):85-94. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 6171
Enzyme 28 Name Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial
Enzyme 28 Synonyms
  1. Succinyl-CoA synthetase subunit alpha
  2. SCS-alpha
Enzyme 28 Gene Name SUCLG1
Enzyme 28 Protein Sequence >Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial
MTATLAAAADIATMVSGSSGLAAARLLSRSFLLPQNGIRHCSYTASRQHLYVDKNTKIIC
QGFTGKQGTFHSQQALEYGTKLVGGTTPGKGGQTHLGLPVFNTVKEAKEQTGATASVIYV
PPPFAAAAINEAIEAEIPLVVCITEGIPQQDMVRVKHKLLRQEKTRLIGPNCPGVINPGE
CKIGIMPGHIHKKGRIGIVSRSGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFIDCL
EIFLNDSATEGIILIGEIGGNAEENAAEFLKQHNSGPNSKPVVSFIAGLTAPPGRRMGHA
GAIIAGGKGGAKEKISALQSAGVVVSMSPAQLGTTIYKEFEKRKML
Enzyme 28 Number of Residues 346
Enzyme 28 Molecular Weight 36249.5
Enzyme 28 Theoretical pI 9.04
Enzyme 28 GO Classification
Function
  • ATP citrate synthase activity
  • CoA-ligase activity
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-sulfur bonds
  • succinate-CoA ligase (ADP-forming) activity
  • succinate-CoA ligase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
Process
  • metabolic process
Component
Enzyme 28 General Function Involved in catalytic activity
Enzyme 28 Specific Function GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
Enzyme 28 Pathways
Enzyme 28 Reactions
  • GTP + succinate + CoA = GDP + phosphate + succinyl-CoA [RN:R00432]
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 109452591 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID P53597 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name SUCA_HUMAN Link Image
Enzyme 28 PDB ID 1EUC Link Image
Enzyme 28 PDB File Show
Enzyme 28 3D Structure
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >1041 bp
ATGACCGCAACCCTTGCCGCTGCCGCTGACATCGCTACCATGGTCTCCGGCAGCAGCGGC
CTCGCCGCCGCCCGTCTCCTGTCGCGCAGCTTCCTCCTGCCGCAGAATGGAATTCGGCAT
TGTTCCTACACAGCTTCTCGGCAACATCTCTATGTTGATAAAAATACAAAGATTATTTGC
CAGGGTTTCACTGGCAAACAGGGCACCTTTCACAGCCAGCAGGCATTGGAATATGGCACC
AAACTCGTTGGAGGAACCACTCCAGGGAAAGGAGGCCAGACACATCTGGGCTTACCTGTC
TTTAATACTGTGAAGGAGGCCAAAGAACAGACAGGAGCAACGGCTTCTGTCATTTATGTT
CCTCCGCCTTTTGCTGCTGCTGCCATTAATGAAGCTATTGAGGCAGAAATTCCCTTGGTT
GTGTGTATCACTGAAGGAATTCCCCAGCAGGACATGGTACGAGTCAAGCACAAACTGCTG
CGCCAGGAAAAGACAAGGCTAATTGGGCCCAACTGCCCTGGAGTCATCAATCCTGGAGAA
TGTAAAATTGGCATCATGCCTGGCCATATTCACAAAAAAGGAAGGATTGGCATTGTGTCC
AGATCTGGCACCCTGACTTATGAAGCAGTTCACCAAACAACGCAAGTTGGATTGGGGCAG
TCTTTGTGCGTTGGCATTGGAGGTGATCCTTTTAATGGAACAGATTTTATTGACTGCCTC
GAAATCTTTTTGAACGATTCTGCCACAGAAGGCATCATATTGATTGGTGAAATTGGTGGT
AATGCAGAAGAGAATGCTGCAGAATTTTTGAAGCAACATAATTCAGGTCCAAATTCCAAG
CCTGTAGTGTCCTTCATTGCTGGTTTAACTGCTCCTCCTGGGAGAAGAATGGGTCATGCC
GGGGCAATTATTGCTGGAGGAAAAGGTGGAGCTAAAGAGAAGATCTCTGCCCTTCAGAGT
GCAGGAGTTGTGGTCAGTATGTCTCCTGCACAGCTGGGAACCACGATCTACAAGGAATTT
GAAAAGAGGAAGATGCTATGA
Enzyme 28 GenBank Gene ID NM_003849.3 Link Image
Enzyme 28 GeneCard ID SUCLG1 Link Image
Enzyme 28 GenAtlas ID SUCLG1 Link Image
Enzyme 28 HGNC ID HGNC:11449 Link Image
Enzyme 28 Chromosome Location 2
Enzyme 28 Locus 2p11.2
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. James M, Man NT, Edwards YH, Morris GE: The molecular basis for cross-reaction of an anti-dystrophin antibody with alpha-actinin. Biochim Biophys Acta. 1997 Apr 12;1360(2):169-76. [PubMed Link Image]
  4. Ostergaard E, Christensen E, Kristensen E, Mogensen B, Duno M, Shoubridge EA, Wibrand F: Deficiency of the alpha subunit of succinate-coenzyme A ligase causes fatal infantile lactic acidosis with mitochondrial DNA depletion. Am J Hum Genet. 2007 Aug;81(2):383-7. Epub 2007 Jun 4. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 6173
Enzyme 29 Name Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial
Enzyme 29 Synonyms
  1. GTP-specific succinyl-CoA synthetase subunit beta
  2. Succinyl-CoA synthetase beta-G chain
  3. SCS-betaG
Enzyme 29 Gene Name SUCLG2
Enzyme 29 Protein Sequence >Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial
MASPVAAQAGKLLRALALRPRFLAAGSQAVQLTSRRWLNLQEYQSKKLMSDNGVRVQRFF
VADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPNVVGQLAKQM
IGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEV
AASNPELIFKEQIDIFEGIKDSQAQRMAENLGFVGPLKSQAADQITKLYNLFLKIDATQV
EVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAAKYDLKYIGLD
GNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKEAQVYQAFKLLTADPKVEAILV
NIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVQEAQKILNNSGLPITSAIDLED
AAKKAVASVAKK
Enzyme 29 Number of Residues 432
Enzyme 29 Molecular Weight 46510.2
Enzyme 29 Theoretical pI 6.18
Enzyme 29 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • purine nucleoside binding
Process
  • metabolic process
Component
Enzyme 29 General Function Involved in catalytic activity
Enzyme 29 Specific Function GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
Enzyme 29 Pathways
Enzyme 29 Reactions
  • GTP + succinate + CoA = GDP + phosphate + succinyl-CoA [RN:R00432]
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 157779135 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q96I99 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name SUCB2_HUMAN Link Image
Enzyme 29 PDB ID 1EUC Link Image
Enzyme 29 PDB File Show
Enzyme 29 3D Structure
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >1299 bp
ATGGCGTCCCCCGTAGCAGCGCAGGCCGGGAAGCTTCTGCGAGCCCTAGCGCTGCGGCCC
CGCTTCCTGGCGGCCGGGTCCCAGGCAGTTCAATTAACCTCCAGAAGATGGCTGAACCTG
CAGGAATACCAGAGCAAGAAACTGATGTCTGACAACGGAGTGAGAGTTCAAAGATTCTTT
GTAGCAGACACTGCAAATGAAGCTCTCGAGGCTGCTAAGAGACTAAATGCAAAAGAAATT
GTTTTAAAAGCCCAGATCTTAGCTGGAGGAAGAGGAAAAGGTGTCTTCAATAGTGGTTTG
AAAGGAGGTGTTCATTTAACAAAAGACCCTAATGTTGTGGGACAGCTGGCTAAACAGATG
ATTGGGTACAATCTAGCGACAAAACAAACTCCAAAAGAAGGTGTGAAAGTTAACAAGGTG
ATGGTTGCTGAAGCCTTGGATATTTCCAGAGAAACCTACCTGGCAATTCTGATGGACCGG
TCCTGCAATGGCCCCGTGCTGGTGGGCAGCCCCCAGGGGGGCGTCGACATTGAAGAGGTG
GCTGCTTCAAACCCGGAGCTCATTTTTAAGGAGCAAATTGACATTTTTGAAGGAATAAAG
GACAGCCAAGCTCAGCGGATGGCCGAAAATCTAGGCTTCGTTGGGCCTTTGAAAAGCCAG
GCTGCAGATCAAATTACGAAGCTGTATAATCTCTTCCTGAAAATTGATGCTACTCAGGTG
GAAGTGAATCCCTTTGGTGAAACTCCAGAAGGACAAGTTGTCTGTTTTGATGCCAAGATA
AACTTTGATGACAACGCAGAATTCCGACAAAAAGACATATTTGCTATGGACGACAAATCA
GAGAATGAGCCCATTGAAAATGAAGCTGCCAAATATGATCTAAAATACATAGGACTAGAT
GGGAACATTGCCTGCTTTGTGAATGGTGCTGGGCTCGCCATGGCTACTTGTGATATCATT
TTCCTTAATGGTGGGAAGCCAGCCAACTTCTTGGATCTTGGAGGTGGTGTAAAGGAAGCT
CAAGTATATCAAGCATTCAAATTGCTCACAGCTGATCCTAAGGTTGAAGCCATCCTTGTC
AATATATTTGGTGGTATCGTCAACTGTGCCATCATTGCCAATGGGATCACCAAAGCCTGC
CGGGAGCTAGAACTCAAGGTGCCCCTGGTGGTCCGGCTTGAAGGAACCAACGTCCAAGAG
GCCCAGAAGATACTCAACAACAGCGGACTCCCCATTACTTCAGCCATTGACCTGGAGGAT
GCAGCCAAGAAGGCTGTGGCCAGTGTGGCCAAGAAGTGA
Enzyme 29 GenBank Gene ID NM_003848.3 Link Image
Enzyme 29 GeneCard ID SUCLG2 Link Image
Enzyme 29 GenAtlas ID SUCLG2 Link Image
Enzyme 29 HGNC ID HGNC:11450 Link Image
Enzyme 29 Chromosome Location 3
Enzyme 29 Locus 3p14.1
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  2. Johnson JD, Mehus JG, Tews K, Milavetz BI, Lambeth DO: Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes. J Biol Chem. 1998 Oct 16;273(42):27580-6. [PubMed Link Image]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 6174
Enzyme 30 Name Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
Enzyme 30 Synonyms
  1. PEPCK-C
  2. Phosphoenolpyruvate carboxylase
Enzyme 30 Gene Name PCK1
Enzyme 30 Protein Sequence >Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
MPPQLQNGLNLSAKVVQGSLDSLPQAVREFLENNAELCQPDHIHICDGSEEENGRLLGQM
EEEGILRRLKKYDNCWLALTDPRDVARIESKTVIVTQEQRDTVPIPKTGLSQLGRWMSEE
DFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLSKIGIELTDSPYVVASMRIMTRMGTPV
LEAVGDGEFVKCLHSVGCPLPLQKPLVNNWPCNPELTLIAHLPDRREIISFGSGYGGNSL
LGKKCFALRMASRLAKEEGWLAEHMLILGITNPEGEKKYLAAAFPSACGKTNLAMMNPSL
PGWKVECVGDDIAWMKFDAQGHLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNV
AETSDGGVYWEGIDEPLASGVTITSWKNKEWSSEDGEPCAHPNSRFCTPASQCPIIDAAW
ESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKIIMHDPF
AMRPFFGYNFGKYLAHWLSMAQHPAAKLPKIFHVNWFRKDKEGKFLWPGFGENSRVLEWM
FNRIDGKASTKLTPIGYIPKEDALNLKGLGHINMMELFSISKEFWEKEVEDIEKYLEDQV
NADLPCEIEREILALKQRISQM
Enzyme 30 Number of Residues 622
Enzyme 30 Molecular Weight 69194.0
Enzyme 30 Theoretical pI 6.05
Enzyme 30 GO Classification
Function
  • GTP binding
  • binding
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • lyase activity
  • nucleotide binding
  • phosphoenolpyruvate carboxykinase activity
  • purine nucleotide binding
Process
  • alcohol metabolic process
  • gluconeogenesis
  • glucose metabolic process
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 30 General Function Involved in phosphoenolpyruvate carboxykinase activity
Enzyme 30 Specific Function Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle
Enzyme 30 Pathways
Enzyme 30 Reactions
  • GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2 [RN:R00431]
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 189945 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID P35558 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name PCKGC_HUMAN Link Image
Enzyme 30 PDB ID 1NHX Link Image
Enzyme 30 PDB File Show
Enzyme 30 3D Structure
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >1869 bp
ATGCCTCCTCAGCTGCAAAACGGCCTGAACCTCTCGGCCAAAGTTGTCCAGGGAAGCCTG
GACAGCCTGCCCCAGGCAGTGAGGGAGTTTCTCGAGAATAACGCTGAGCTGTGTCAGCCT
GATCACATCCACATCTGTGACGGCTCTGAGGAGGAGAATGGGCGGCTTCTGGGCCAGATG
GAGGAAGAGGGCATCCTCAGGCGGCTGAAGAAGTATGACAACTGCTGGTTGGCTCTCACT
GACCCCAGGGATGTGGCCAGGATCGAAAGCAAGACGGTTATCGTCACCCAAGAGCAAAGA
GACACAGTGCCCATCCCCAAAACAGGCCTCAGCCAGCTCGGTCGCTGGATGTCAGAGGAG
GATTTTGAGAAAGCGTTCAATGCCAGGTTCCCAGGGTGCATGAAAGGTCGCACCATGTAC
GTCATCCCATTCAGCATGGGGCCGCTGGGCTCACCTCTGTCGAAGATCGGCATCGAGCTG
ACGGATTCGCCCTACGTGGTGGCCAGCATGCGGATCATGACGCGGATGGGCACGCCCGTC
CTGGAAGCACTGGGCGATGGGGAGTTTGTCAAATGCCTCCATTCTGTGGGGTGCCCTCTG
CCTTTACAAAAGCCTTTGGTCAACAACTGGCCCTGCAACCCGGAGCTGACGCTCATCGCC
CACCTGCCTGACCGCAGAGAGATCATCTCCTTTGGCAGTGGGTACGGCGGGAACTCGCTG
CTCGGGAAGAAGTGCTTTGCTCTCAGGATGGCCAGCCGGCTGGCAGAGGAGGAAGGGTGG
CTGGCAGAGCACATGCTGATTCTGGGTATAACCAACCCTGAGGGTGAGAAGAAGTACCTG
GCGGCCGCATTTCCCAGCGCCTGCGGGAAGACCAACCTGGCCATGATGAACCCCAGCCTC
CCCGGGTGGAAGGTTGAGTGCGTCGGGGATGACATTGCCTGGATGAAGTTTGACGCACAA
GGTCATTTAAGGGCCATCAACCCAGAAAATGGCTTTTTCGGTGTCGCTCCTGGGACTTCA
GTGAAGACCAACCCCAATGCCATCAAGACCATCCAGAAGAACACAATCTTTACCAATGTG
GCCGAGACCAGCGACGGGGGCGTTTACTGGGAAGGCATTGATGAGCCGCTAGCTTCAGGC
GTCACCATCACGTCCTGGAAGAATAAGGAGTGGAGCTCAGAGGATGGGGAACCTTGTGCC
CACCCCAACTCGAGGTTCTGCACCCCTGCCAGCCAGTGCCCCATCATTGATGCTGCCTGG
GAGTCTCCGGAAGGTGTTCCCATTGAAGGCATTATCTTTGGAGGCCGTAGACCTGCTGGT
GTCCCTCTAGTCTATGAAGCTCTCAGCTGGCAACATGGAGTCTTTGTGGGGGCGGCCATG
AGATCAGAGGCCACAGCGGCTGCAGAACATAAAGGCAAAATCATCATGCATGACCCCTTT
GCCATGCGGCCCTTCTTTGGCTACAACTTCGGCAAATACCTGGCCCACTGGCTTAGCATG
GCCCAGCACCCAGCAGCCAAACTGCCCAAGATCTTCCATGTCAACTGGTTCCGGAAGGAC
AAGGAAGGCAAATTCCTCTGGCCAGGCTTTGGAGAGAACTCCAGGGTGCTGGAGTGGATG
TTCAACCGGATCGATGGAAAAGCCAGCACCAACGTCACGCCCATAGGCTACATCCCCAAG
GAGGATGCCCTGAACCTGAAAGGCCTGGGGCACATCAACATGATGGAGCTTTTCAGCATC
TCCAAGGAATTCTGGGACAAGGAGGTGGAAGACATCGAGAAGTATCTGGTGGATCAAGTC
AATGCCGACCTCCCCTGTGAAATCGAGAGAGAGATCCTTGCCTTGAAGCAAAGAATAAGC
CAGATGTAA
Enzyme 30 GenBank Gene ID L05144 Link Image
Enzyme 30 GeneCard ID PCK1 Link Image
Enzyme 30 GenAtlas ID PCK1 Link Image
Enzyme 30 HGNC ID HGNC:8724 Link Image
Enzyme 30 Chromosome Location 2
Enzyme 30 Locus 20q13.31
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Stoffel M, Xiang KS, Espinosa R 3rd, Cox NJ, Le Beau MM, Bell GI: cDNA sequence and localization of polymorphic human cytosolic phosphoenolpyruvate carboxykinase gene (PCK1) to chromosome 20, band q13.31: PCK1 is not tightly linked to maturity-onset diabetes of the young. Hum Mol Genet. 1993 Jan;2(1):1-4. [PubMed Link Image]
  2. Ting CN, Burgess DL, Chamberlain JS, Keith TP, Falls K, Meisler MH: Phosphoenolpyruvate carboxykinase (GTP): characterization of the human PCK1 gene and localization distal to MODY on chromosome 20. Genomics. 1993 Jun;16(3):698-706. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. O'Brien RM, Printz RL, Halmi N, Tiesinga JJ, Granner DK: Structural and functional analysis of the human phosphoenolpyruvate carboxykinase gene promoter. Biochim Biophys Acta. 1995 Dec 27;1264(3):284-8. [PubMed Link Image]
  7. Liu J, Hanson RW: Regulation of phosphoenolpyruvate carboxykinase (GTP) gene transcription. Mol Cell Biochem. 1991 May 29-Jun 12;104(1-2):89-100. [PubMed Link Image]
  8. Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL: Regulation of cellular metabolism by protein lysine acetylation. Science. 2010 Feb 19;327(5968):1000-4. [PubMed Link Image]
  9. Dunten P, Belunis C, Crowther R, Hollfelder K, Kammlott U, Levin W, Michel H, Ramsey GB, Swain A, Weber D, Wertheimer SJ: Crystal structure of human cytosolic phosphoenolpyruvate carboxykinase reveals a new GTP-binding site. J Mol Biol. 2002 Feb 15;316(2):257-64. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 6213
Enzyme 31 Name GDP-L-fucose synthase
Enzyme 31 Synonyms
  1. GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase
  2. Protein FX
  3. Red cell NADP(H)-binding protein
  4. Short-chain dehydrogenase/reductase family 4E member 1
Enzyme 31 Gene Name TSTA3
Enzyme 31 Protein Sequence >GDP-L-fucose synthase
MGEPQGSMRILVTGGSGLVGKAIQKVVADGAGLPGEDWVFVSSKDADLTDTAQTRALFEK
VQPTHVIHLAAMVGGLFRNIKYNLDFWRKNVHMNDNVLHSAFEVGARKVVSCLSTCIFPD
KTTYPIDETMIHNGPPHNSNFGYSYAKRMIDVQNRAYFQQYGCTFTAVIPTNVFGPHDNF
NIEDGHVLPGLIHKVHLAKSSGSALTVWGTGNPRRQFIYSLDLAQLFIWVLREYNEVEPI
ILSVGEEDEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSKLRTYLPDFRFTP
FKQAVKETCAWFTDNYEQARK
Enzyme 31 Number of Residues 321
Enzyme 31 Molecular Weight 35892.5
Enzyme 31 Theoretical pI 6.59
Enzyme 31 GO Classification
Function
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
Process
  • cellular metabolic process
  • metabolic process
Component
Enzyme 31 General Function Involved in catalytic activity
Enzyme 31 Specific Function Two step NADP-dependent conversion of GDP-4-dehydro-6- deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction
Enzyme 31 Pathways
Enzyme 31 Reactions
  • GDP-L-fucose + NADP+ = GDP-4-dehydro-6-deoxy-D-mannose + NADPH + H+ [RN:R05692]
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein Not Available
Enzyme 31 UniProtKB/Swiss-Prot ID Q13630 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name FCL_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >966 bp
ATGGGTGAACCCCAGGGATCCATGCGGATTCTAGTGACAGGGGGCTCTGGGCTGGTAGGC
AAAGCCATCCAGAAGGTGGTAGCAGATGGAGCTGGACTTCCTGGAGAGGACTGGGTGTTT
GTCTCCTCTAAAGACGCCGATCTCACGGATACAGCACAGACCCGCGCCCTGTTTGAGAAG
GTCCAACCCACACACGTCATCCATCTTGCTGCAATGGTGGGGGGCCTGTTCCGGAATATC
AAATACAATTTGGACTTCTGGAGGAAAAACGTGCACATGAACGACAACGTCCTGCACTCG
GCCTTTGAGGTGGGGGCCCGCAAGGTGGTGTCCTGCCTGTCCACCTGTATCTTCCCTGAC
AAGACGACCTACCCGATAGATGAGACCATGATCCACAATGGGCCTCCCCACAACAGCAAT
TTTGGGTACTCGTATGCCAAGAGGATGATCGACGTGCAGAACAGGGCCTACTTCCAGCAG
TACGGCTGCACCTTCACCGCTGTCATCCCCACCAACGTTTTCGGGCCCCACGACAACTTC
AACATCGAGGATGGCCACGTGCTGCCTGGCCTCATCCACAAGGTGCACCTGGCCAAGAGC
AGCGGCTCGGCCCTGACGGTGTGGGGTACAGGGAATCCGCGGAGGCAGTTCATATACTCG
CTGGACCTGGCCCAGCTCTTTATCTGGGTCCTGCGGGAGTACAATGAAGTGGAGCCCATC
ATCCTCTCCGTGGGCGAGGAAGATGAGGTCTCCATCAAGGAGGCAGCCGAGGCGGTGGTG
GAGGCCATGGACTTCCATGGGGAAGTCACCTTTGATACAACCAAGTCGGATGGGCAGTTT
AAGAAGACAGCCAGTAACAGCAAGCTGAGGACCTACCTGCCCGACTTCCGGTTCACACCC
TTCAAGCAGGCGGTGAAGGAGACCTGTGCTTGGTTCACTGACAACTACGAGCAGGCCCGG
AAGTGA
Enzyme 31 GenBank Gene ID U58766 Link Image
Enzyme 31 GeneCard ID TSTA3 Link Image
Enzyme 31 GenAtlas ID TSTA3 Link Image
Enzyme 31 HGNC ID HGNC:12390 Link Image
Enzyme 31 Chromosome Location 8
Enzyme 31 Locus 8q24.3
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Tonetti M, Sturla L, Bisso A, Benatti U, De Flora A: Synthesis of GDP-L-fucose by the human FX protein. J Biol Chem. 1996 Nov 1;271(44):27274-9. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Camardella L, Carratore V, Ciardiello MA, Damonte G, Benatti U, De Flora A: Primary structure of human erythrocyte nicotinamide adenine dinucleotide phosphate (NADP[H])-binding protein FX: identification with the mouse tum- transplantation antigen P35B. Blood. 1995 Jan 1;85(1):264-7. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 6218
Enzyme 32 Name Guanylate kinase
Enzyme 32 Synonyms
  1. GMP kinase
Enzyme 32 Gene Name GUK1
Enzyme 32 Protein Sequence >Guanylate kinase
MSGPRPVVLSGPSGAGKSTLLKRLLQEHSGIFGFSVSHTTRNPRPGEENGKDYYFVTREV
MQRDIAAGDFIEHAEFSGNLYGTSKVAVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYI
SVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMESSKEPGLFDVVIINDSLDQAYAE
LKEALSEEIKKAQRTGA
Enzyme 32 Number of Residues 197
Enzyme 32 Molecular Weight 21725.4
Enzyme 32 Theoretical pI 6.53
Enzyme 32 GO Classification
Function
  • catalytic activity
  • guanylate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleotide metabolic process
Component
Enzyme 32 General Function Involved in guanylate kinase activity
Enzyme 32 Specific Function Essential for recycling GMP and indirectly, cGMP
Enzyme 32 Pathways
Enzyme 32 Reactions
  • ATP + GMP = ADP + GDP [RN:R00332]
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 1196436 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID Q16774 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name KGUA_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >594 bp
ATGTCGGGCCCCAGGCCTGTGGTGCTGAGCGGGCCTTCGGGAGCTGGGAAGAGCACCCTG
CTGAAGAGGCTGCTCCAGGAGCACAGCGGCATCTTTGGCTTCAGCGTGTCCCATACCACG
AGGAACCCGAGGCCCGGCGAGGAGAACGGCAAAGATTACTACTTTGTAACCAGGGAGGTG
ATGCAGCGTGACATAGCAGCCGGCGACTTCATCGAGCATGCCGAGTTCTCGGGGAACCTG
TATGGCACGAGCAAGGTGGCGGTGCAGGCCGTGCAGGCCATGAACCGCATCTGTGTGCTG
GACGTGGACCTGCAGGGTGTGCGGAACATCAAGGCCACCGATCTGCGGCCCATCTACATC
TCTGTGCAGCCGCCTTCACTGCACGTGCTGGAGCAGCGGCTGCGGCAGCGCAACACTGAA
ACCGAGGAGAGCCTGGTGAAGCGGCTGGCTGCTGCCCAGGCCGACATGGAGAGCAGCAAG
GAGCCCGGCCTGTTTGATGTGGTCATCATTAACGACAGCCTGGACCAGGCCTACGCAGAG
CTGAAGGAGGCGCTCTCTGAGGAAATCAAGAAAGCTCAAAGGACCGGCGCCTGA
Enzyme 32 GenBank Gene ID L76200 Link Image
Enzyme 32 GeneCard ID GUK1 Link Image
Enzyme 32 GenAtlas ID GUK1 Link Image
Enzyme 32 HGNC ID HGNC:4693 Link Image
Enzyme 32 Chromosome Location 1
Enzyme 32 Locus 1q32-q41
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Fitzgibbon J, Katsanis N, Wells D, Delhanty J, Vallins W, Hunt DM: Human guanylate kinase (GUK1): cDNA sequence, expression and chromosomal localisation. FEBS Lett. 1996 May 6;385(3):185-8. [PubMed Link Image]
  2. Brady WA, Kokoris MS, Fitzgibbon M, Black ME: Cloning, characterization, and modeling of mouse and human guanylate kinases. J Biol Chem. 1996 Jul 12;271(28):16734-40. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 6259
Enzyme 33 Name Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial
Enzyme 33 Synonyms
  1. ATP-specific succinyl-CoA synthetase subunit beta
  2. Renal carcinoma antigen NY-REN-39
  3. Succinyl-CoA synthetase beta-A chain
  4. SCS-betaA
Enzyme 33 Gene Name SUCLA2
Enzyme 33 Protein Sequence >Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial
MAASMFYGRLVAVATLRNHRPRTAQRAAAQVLGSSGLFNNHGLQVQQQQQRNLSLHEYMS
MELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVK
IVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGP
VLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENM
VKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDER
DKDAAKANLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEA
FKLITSDKKVLAILVNIFGGIMRCDVIAQGIVMAVKDLEIKIPVVVRLQGTRVDDAKALI
ADSGLKILACDDLDEAARMVVKLSEIVTLAKQAHVDVKFQLPI
Enzyme 33 Number of Residues 463
Enzyme 33 Molecular Weight 50316.9
Enzyme 33 Theoretical pI 7.50
Enzyme 33 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • purine nucleoside binding
Process
  • metabolic process
Component
Enzyme 33 General Function Involved in catalytic activity
Enzyme 33 Specific Function ATP + succinate + CoA = ADP + phosphate + succinyl-CoA
Enzyme 33 Pathways
Enzyme 33 Reactions
  • ATP + succinate + CoA = ADP + phosphate + succinyl-CoA [RN:R00405]
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein Not Available
Enzyme 33 UniProtKB/Swiss-Prot ID Q9P2R7 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name SUCB1_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >1392 bp
ATGGCGGCCTCCATGTTCTACGGCAGGCTAGTGGCCGTGGCCACCCTTCGGAACCACCGG
CCTCGGACGGCCCAGCGGGCTGCTGCTCAGGTTCTGGGAAGTTCTGGATTGTTTAATAAC
CATGGACTCCAAGTACAGCAGCAACAGCAAAGGAATCTCTCACTACATGAATACATGAGT
ATGGAATTATTGCAAGAAGCTGGTGTCTCCGTTCCCAAAGGATATGTGGCAAAGTCACCA
GATGAAGCTTATGCAATTGCCAAAAAATTAGGTTCAAAAGATGTCGTGATAAAGGCACAG
GTTTTAGCTGGTGGTAGAGGAAAAGGAACATTTGAAAGTGGCCTCAAAGGAGGAGTGAAG
ATAGTTTTCTCTCCAGAAGAAGCAAAAGCTGTTTCTTCACAAATGATTGGGAAAAAATTG
TTTACCAAGCAAACGGGAGAAAAGGGCAGAATATGCAATCAAGTATTGGTCTGTGAGCGA
AAATATCCCAGGAGAGAATACTACTTTGCAATAACAATGGAAAGGTCATTTCAAGGTCCT
GTATTAATAGGAAGTTCACATGGTGGTGTCAACATTGAAGATGTTGCTGCTGAGTCTCCT
GAAGCAATAATTAAAGAACCTATTGATATTGAAGAAGGCATCAAAAAGGAACAAGCTCTC
CAGCTTGCACAGAAGATGGGATTTCCACCTAATATTGTGGAATCAGCAGCAGAAAACATG
GTCAAGCTTTACAGCCTTTTTCTGAAATACGATGCAACCATGATAGAAATAAATCCAATG
GTGGAAGATTCAGATGGAGCTGTATTGTGTATGGATGCAAAGATCAATTTTGACTCTAAT
TCAGCCTATCGCCAAAAGAAAATCTTTGATCTACAGGACTGGACCCAGGAAGATGAAAGG
GACAAAGATGCTGCTAAGGCAAATCTCAACTACATTGGCCTCGATGGAAATATAGGCTGC
CTAGTAAATGGTGCTGGTTTGGCTATGGCCACAATGGATATAATAAAACTTCATGGAGGG
ACTCCAGCCAACTTCCTTGATGTTGGTGGTGGTGCTACAGTCCATCAAGTAACAGAAGCA
TTTAAGCTTATCACTTCAGATAAAAAGGTACTGGCTATTCTGGTCAACATTTTTGGAGGA
ATCATGCGCTGTGATGTTATTGCACAGGGTATAGTCATGGCAGTAAAAGACTTGGAAATT
AAAATACCTGTTGTGGTACGGTTACAAGGTACACGAGTCGATGATGCTAAGGCACTGATA
GCGGACAGTGGACTTAAAATACTTGCTTGTGATGACTTGGATGAAGCTGCTAGAATGGTT
GTAAAGCTCTCTGAAATAGTGACCTTAGCGAAGCAAGCACATGTGGATGTGAAATTTCAG
TTGCCAATATGA
Enzyme 33 GenBank Gene ID AB035863 Link Image
Enzyme 33 GeneCard ID SUCLA2 Link Image
Enzyme 33 GenAtlas ID SUCLA2 Link Image
Enzyme 33 HGNC ID HGNC:11448 Link Image
Enzyme 33 Chromosome Location 1
Enzyme 33 Locus 13q12.2-q13.3
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Furuyama K, Sassa S: Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia. J Clin Invest. 2000 Mar;105(6):757-64. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Johnson JD, Mehus JG, Tews K, Milavetz BI, Lambeth DO: Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes. J Biol Chem. 1998 Oct 16;273(42):27580-6. [PubMed Link Image]
  6. Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed Link Image]
  7. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  8. Elpeleg O, Miller C, Hershkovitz E, Bitner-Glindzicz M, Bondi-Rubinstein G, Rahman S, Pagnamenta A, Eshhar S, Saada A: Deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomyopathy and mitochondrial DNA depletion. Am J Hum Genet. 2005 Jun;76(6):1081-6. Epub 2005 Apr 22. [PubMed Link Image]
  9. Ostergaard E, Hansen FJ, Sorensen N, Duno M, Vissing J, Larsen PL, Faeroe O, Thorgrimsson S, Wibrand F, Christensen E, Schwartz M: Mitochondrial encephalomyopathy with elevated methylmalonic acid is caused by SUCLA2 mutations. Brain. 2007 Mar;130(Pt 3):853-61. Epub 2007 Feb 7. [PubMed Link Image]
  10. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  11. Carrozzo R, Dionisi-Vici C, Steuerwald U, Lucioli S, Deodato F, Di Giandomenico S, Bertini E, Franke B, Kluijtmans LA, Meschini MC, Rizzo C, Piemonte F, Rodenburg R, Santer R, Santorelli FM, van Rooij A, Vermunt-de Koning D, Morava E, Wevers RA: SUCLA2 mutations are associated with mild methylmalonic aciduria, Leigh-like encephalomyopathy, dystonia and deafness. Brain. 2007 Mar;130(Pt 3):862-74. Epub 2007 Feb 14. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 6308
Enzyme 34 Name Alpha-(1,3)-fucosyltransferase
Enzyme 34 Synonyms
  1. Fucosyltransferase 5
  2. Fucosyltransferase V
  3. Fuc-TV
  4. FucT-V
  5. Galactoside 3-L-fucosyltransferase
Enzyme 34 Gene Name FUT5
Enzyme 34 Protein Sequence >Alpha-(1,3)-fucosyltransferase
MDPLGPAKPQWLWRRCLAGLLFQLLVAVCFFSYLRVSRDDATGSPRPGLMAVEPVTGAPN
GSRCQDSMATPAHPTLLILLWTWPFNTPVALPRCSEMVPGAADCNITADSSVYPQADAVI
VHHWDIMYNPSANLPPPTRPQGQRWIWFSMESPSNCRHLEALDGYFNLTMSYRSDSDIFT
PYGWLEPWSGQPAHPPLNLSAKTELVAWAVSNWKPDSARVRYYQSLQAHLKVDVYGRSHK
PLPKGTMMETLSRYKFYLAFENSLHPDYITEKLWRNALEAWAVPVVLGPSRSNYERFLPP
DAFIHVDDFQSPKDLARYLQELDKDHARYLSYFRWRETLRPRSFSWALAFCKACWKLQQE
SRYQTVRSIAAWFT
Enzyme 34 Number of Residues 374
Enzyme 34 Molecular Weight 43007.7
Enzyme 34 Theoretical pI 8.37
Enzyme 34 GO Classification
Function
  • catalytic activity
  • fucosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • membrane
Enzyme 34 General Function Involved in fucosyltransferase activity
Enzyme 34 Specific Function May catalyze alpha-1,3 glycosidic linkages involved in the expression of VIM-2, Lewis X/SSEA-1 and sialyl Lewis X antigens
Enzyme 34 Pathways
  • Glycosphingolipid biosynthesis - lactoseries (map00601 Link Image)
Enzyme 34 Reactions
  • GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-D-glucosaminyl-R = GDP + beta-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->4)]-N-acetyl-beta-D- glucosaminyl-R [RN:R04553]
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • 16-34
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 52485799 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q11128 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name FUT5_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >1125 bp
ATGGATCCCCTGGGCCCAGCCAAGCCACAGTGGCTGTGGCGCCGCTGTCTGGCCGGGCTG
CTGTTTCAGCTGCTGGTGGCTGTGTGTTTCTTCTCCTACCTGCGTGTGTCCCGAGACGAT
GCCACTGGATCCCCTAGGCCAGGGCTTATGGCAGTGGAACCTGTCACCGGGGCTCCCAAT
GGGTCCCGCTGCCAGGACAGCATGGCGACCCCTGCCCACCCCACCCTACTGATCCTGCTG
TGGACGTGGCCTTTTAACACACCCGTGGCTCTGCCCCGCTGCTCAGAGATGGTGCCCGGC
GCGGCCGACTGCAACATCACTGCCGACTCCAGTGTGTACCCACAGGCAGACGCGGTCATC
GTGCACCACTGGGATATCATGTACAACCCCAGTGCCAACCTCCCGCCCCCCACCAGGCCG
CAGGGGCAGCGCTGGATCTGGTTCAGCATGGAGTCCCCCAGCAACTGCCGGCACCTGGAA
GCCCTGGACGGATACTTCAATCTCACCATGTCCTACCGCAGCGACTCCGACATCTTCACG
CCCTACGGCTGGCTGGAGCCGTGGTCCGGCCAGCCTGCCCACCCACCGCTCAACCTCTCG
GCCAAGACCGAGCTGGTGGCCTGGGCGGTGTCCAACTGGAAGCCGGACTCGGCCAGGGTG
CGCTACTACCAGAGCCTGCAGGCTCATCTCAAGGTGGACGTGTACGGACGCTCCCACAAG
CCCCTGCCCAAGGGGACCATGATGGAGACGCTGTCCCGGTACAAGTTCTATCTGGCCTTC
GAGAACTCCTTGCACCCCGACTACATCACCGAGAAGCTGTGGAGGAACGCCCTGGAGGCC
TGGGCCGTGCCCGTGGTGCTGGGCCCCAGCAGAAGCAACTACGAGAGGTTCCTGCCACCC
GACGCCTTCATCCACGTGGACGACTTCCAGAGCCCCAAGGACCTGGCCCGGTACCTGCAG
GAGCTGGACAAGGACCACGCCCGCTACCTGAGCTACTTTCACTGGCGGGAGACGCTGCGG
CCTCGCTCCTTCAGCTGGGCACTGGCTTTCTGCAAGGCCTGCTGGAAGCTGCAGCAGGAA
TCTAGGTACCAGACGGTGCGCAGCATAGCGGCTTGGTTCACCTGA
Enzyme 34 GenBank Gene ID NM_002034.2 Link Image
Enzyme 34 GeneCard ID FUT5 Link Image
Enzyme 34 GenAtlas ID FUT5 Link Image
Enzyme 34 HGNC ID HGNC:4016 Link Image
Enzyme 34 Chromosome Location 1
Enzyme 34 Locus 19p13.3
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Weston BW, Nair RP, Larsen RD, Lowe JB: Isolation of a novel human alpha (1,3)fucosyltransferase gene and molecular comparison to the human Lewis blood group alpha (1,3/1,4)fucosyltransferase gene. Syntenic, homologous, nonallelic genes encoding enzymes with distinct acceptor substrate specificities. J Biol Chem. 1992 Feb 25;267(6):4152-60. [PubMed Link Image]
  2. Cameron HS, Szczepaniak D, Weston BW: Expression of human chromosome 19p alpha(1,3)-fucosyltransferase genes in normal tissues. Alternative splicing, polyadenylation, and isoforms. J Biol Chem. 1995 Aug 25;270(34):20112-22. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 6417
Enzyme 35 Name Rap guanine nucleotide exchange factor 2
Enzyme 35 Synonyms
  1. Neural RAP guanine nucleotide exchange protein
  2. nRap GEP
  3. PDZ domain-containing guanine nucleotide exchange factor 1
  4. PDZ-GEF1
  5. RA-GEF
Enzyme 35 Gene Name RAPGEF2
Enzyme 35 Protein Sequence >Rap guanine nucleotide exchange factor 2
MKPLAIPANHGVMGQQEKHSLPADFTKLHLTDSLHPQVTHVSSSHSGCSITSDSGSSSLS
DIYQATESEAGDMDLSGLPETAVDSEDDDDEEDIERASDPLMSRDIVRDCLEKDPIDRTD
DDIEQLLEFMHQLPAFANMTMSVRRELCAVMVFAVVERAGTIVLNDGEELDSWSVILNGS
VEVTYPDGKAEILCMGNSFGVSPTMDKEYMKGVMRTKVDDCQFVCIAQQDYCRILNQVEK
NMQKVEEEGEIVMVKEHRELDRTGTRKGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLL
TYRTFLSSPMEVGKKLLEWFNDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENN
LEREKMGGHLRLLNIACAAKAKRRLMTLTKPSREAPLPFILLGGSEKGFGIFVDSVDSGS
KATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVFKELLTRLSEE
KRNGAPHLPKIGDIKKASRYSIPDLAVDVEQVIGLEKVNKKSKANTVGGRNKLKKILDKT
RISILPQKPYNDIGIGQSQDDSIVGLRQTKHIPTALPVSGTLSSSNPDLLQSHHRILDFS
ATPDLPDQVLRVFKADQQSRYIMISKDTTAKEVVIQAIREFAVTATPDQYSLCEVSVTPE
GVIKQRRLPDQLSKLADRIQLSGRYYLKNNMETETLCSDEDAQELLRESQISLLQLSTVE
VATQLSMRNFELFRNIEPTEYIDDLFKLRSKTSCANLKRFEEVINQETFWVASEILRETN
QLKRMKIIKHFIKIALHCRECKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDL
QDLFDPSRNMAKYRNVLNSQNLQPPIIPLFPVIKKDLTFLHEGNDSKVDGLVNFEKLRMI
AKEIRHVGRMASVNMDPALMFRTRKKKWRSLGSLSQGSTNATVLDVAQTGGHKKRVRRSS
FLNAKKLYEDAQMARKVKQYLSNLELEMDEESLQTLSLQCEPATNTLPKNPGDKKPVKSE
TSPVAPRAGSQQKAQSLPQPQQQPPPAHKINQGLQVPAVSLYPSRKKVPVKDLPPFGINS
PQALKKILSLSEEGSLERHKKQAEDTISNASSQLSSPPTSPQSSPRKGYTLAPSGTVDNF
SDSGHSEISSRSSIVSNSSFDSVPVSLHDERRQRHSVSIVETNLGMGRMERRTMIEPDQY
SLGSYAPMSEGRGLYATATVISSPSTEELSQDQGDRASLDAADSGRGSWTSCSSGSHDNI
QTIQHQRSWETLPFGHTHFDYSGDPAGLWASSSHMDQIMFSDHSTKYNRQNQSRESLEQA
QSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSIEAESSSLTSVTTEETKPVPMPAHIAV
ASSTTKGLIARKEGRYREPPPTPPGYIGIPITDFPEGHSHPARKPPDYNVALQRSRMVAR
SSDTAGPSSVQQPHGHPTSSRPVNKPQWHKPNESDPRLAPYQSQGFSTEEDEDEQVSAV
Enzyme 35 Number of Residues 1499
Enzyme 35 Molecular Weight 167415.5
Enzyme 35 Theoretical pI 6.64
Enzyme 35 GO Classification
Function
  • GTPase regulator activity
  • binding
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • protein binding
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 35 General Function Involved in protein binding
Enzyme 35 Specific Function Guanine nucleotide exchange factor (GEF) for Rap1A, Rap1B and Rap2B GTPases. Does not interact with cAMP or cGMP
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions Not Available
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 7657261 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID Q9Y4G8 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name RPGF2_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >4500 bp
ATGAAACCACTAGCAATCCCAGCTAACCATGGAGTTATGGGCCAGCAGGAGAAACACTCA
CTTCCTGCAGATTTCACAAAACTGCATCTTACTGACAGTCTCCACCCACAGGTGACCCAC
GTTTCTTCTAGCCATTCAGGATGTAGTATCACTAGTGATTCTGGGAGCAGCAGTCTTTCT
GATATCTACCAGGCCACAGAAAGCGAGGCTGGTGATATGGACCTGAGTGGGTTGCCAGAA
ACAGCAGTGGATTCCGAAGACGACGACGATGAAGAAGACATTGAGAGAGCATCAGATCCT
CTGATGAGCAGGGACATTGTGAGAGACTGCCTAGAGAAGGACCCAATTGACCGGACAGAT
GATGACATTGAACAACTCTTGGAATTTATGCACCAGTTGCCTGCTTTTGCCAATATGACA
ATGTCAGTGAGGCGAGAACTCTGTGCTGTGATGGTGTTCGCAGTGGTGGAAAGAGCAGGG
ACCATAGTGTTAAATGATGGTGAAGAGCTGGACTCCTGGTCAGTGATTCTCAATGGATCT
GTGGAAGTGACTTATCCAGATGGAAAAGCAGAAATACTGTGCATGGGAAATAGTTTTGGT
GTCTCTCCTACCATGGACAAAGAATACATGAAAGGAGTGATGAGAACAAAGGTGGATGAC
TGCCAGTTTGTCTGCATAGCCCAGCAAGATTACTGCCGTATTCTCAATCAAGTAGAAAAG
AACATGCAAAAAGTTGAAGAGGAAGGAGAGATTGTTATGGTGAAAGAACACCGAGAACTT
GATCGAACTGGAACAAGAAAGGGACACATTGTCATCAAGGGTACCTCAGAAAGGTTAACA
ATGCATTTGGTGGAAGAGCATTCAGTAGTAGATCCAACATTCATAGAAGACTTTCTGTTG
ACCTATAGGACTTTTCTTTCTAGCCCAATGGAAGTGGGCAAAAAGTTATTGGAGTGGTTT
AATGACCCGAGCCTCAGGGATAAGGTTACACGGGTAGTATTATTGTGGGTAAATAATCAC
TTCAATGACTTTGAAGGAGATCCTGCAATGACTCGATTTTTAGAAGAATTTGAAAACAAT
CTGGAAAGAGAGAAAATGGGTGGACACCTAAGGCTGTTGAATATCGCGTGTGCTGCTAAA
GCAAAAAGAAGATTGATGACGTTAACAAAACCATCCCGAGAAGCTCCTTTGCCTTTTATC
TTACTTGGAGGCTCTGAGAAGGGATTTGGAATCTTTGTTGACAGTGTAGATTCAGGTAGC
AAAGCAACTGAAGCAGGCTTGAAACGGGGGGATCAGATATTAGAAGTAAATGGCCAAAAC
TTTGAAAACATTCAGCTGTCAAAAGCTATGGAAATTCTTAGAAATAACACACATTTATCT
ATCACTGTGAAAACCAATTTATTTGTATTTAAAGAACTTCTAACAAGATTGTCAGAAGAG
AAAAGAAATGGTGCCCCCCACCTTCCTAAAATTGGTGACATTAAAAAGGCCAGTCGCTAC
TCCATTCCAGATCTTGCTGTAGATGTAGAACAGGTGATAGGACTTGAAAAAGTGAACAAA
AAAAGTAAAGCCAACACTGTGGGAGGAAGGAACAAGCTGAAAAAGATACTCGACAAGACT
CGGATCAGTATCTTGCCACAGAAACCATACAATGATATTGGGATTGGTCAGTCTCAAGAT
GACAGCATAGTAGGATTAAGGCAGACAAAGCACATCCCAACTGCATTGCCTGTCAGTGGA
ACCTTATCATCCAGTAATCCTGATTTATTGCAGTCACATCATCGCATTTTAGACTTCAGT
GCTACTCCTGACTTGCCAGATCAAGTGCTAAGGGTTTTTAAGGCTGATCAGCAAAGCCGC
TACATCATGATCAGTAAGGACACTACAGCAAAGGAAGTGGTCATTCAGGCTATCAGGGAG
TTTGCTGTTACTGCCACCCCGGATCAATATTCACTATGTGAGGTCTCTGTCACACCTGAG
GGAGTAATCAAACAAAGAAGACTTCCAGATCAGCTTTCCAAACTTGCAGACAGAATACAA
CTGAGTGGAAGGTATTATCTGAAAAACAACATGGAAACAGAAACTCTTTGTTCAGATGAA
GATGCTCAGGAGTTGTTGAGAGAGAGTCAAATTTCCCTCCTTCAGCTCAGCACTGTGGAA
GTTGCAACACAGCTCTCTATGCGAAATTTTGAACTCTTTCGCAACATTGAACCTACTGAA
TATATAGATGATTTATTTAAACTCAGATCAAAAACCAGCTGTGCCAACCTGAAGAGATTT
GAAGAAGTCATTAACCAGGAAACATTTTGGGTAGCATCTGAAATTCTCAGAGAAACAAAC
CAGCTGAAGAGGATGAAGATCATTAAGCATTTCATCAAGATAGCACTGCACTGTAGGGAA
TGCAAGAATTTTAACTCAATGTTTGCAATCATCAGTGGCCTAAACCTGGCACCAGTGGCA
AGACTGCGAACGACCTGGGAGAAACTTCCCAATAAATACGAAAAACTATTTCAAGATCTC
CAAGACCTGTTTGATCCTTCCAGAAACATGGCAAAATATCGTAATGTTCTCAATAGTCAA
AATCTACAACCTCCCATAATCCCTCTATTCCCAGTTATCAAAAAGGATCTCACCTTCCTT
CACGAAGGAAATGACTCAAAAGTAGACGGGCTGGTCAATTTTGAGAAGCTAAGGATGATT
GCAAAAGAAATTCGTCACGTTGGCCGAATGGCTTCAGTGAACATGGACCCTGCCCTCATG
TTCAGGACTCGGAAGAAGAAATGGCGGAGTTTGGGGTCTCTCAGCCAGGGTAGTACAAAT
GCAACAGTGCTAGATGTTGCTCAGACAGGTGGTCATAAAAAGCGGGTACGTCGTAGTTCC
TTTCTCAATGCCAAAAAGCTTTATGAAGATGCCCAAATGGCTCGAAAAGTGAAGCAGTAC
CTTTCCAATTTGGAGCTAGAAATGGACGAGGAGAGTCTTCAGACATTATCTCTGCAGTGT
GAGCCAGCAACCAACACATTGCCTAAGAATCCTGGTGACAAAAAGCCTGTCAAATCCGAG
ACCTCTCCAGTAGCTCCAAGGGCAGGGTCACAACAGAAAGCTCAGTCCCTGCCACAGCCC
CAGCAGCAGCCACCACCAGCACATAAAATCAACCAGGGACTACAGGTTCCCGCCGTGTCC
CTTTATCCTTCACGGAAGAAAGTGCCCGTAAAGGATCTCCCACCTTTTGGCATAAACTCT
CCACAAGCTTTAAAAAAAATTCTTTCTTTGTCTGAAGAAGGAAGTTTGGAACGTCACAAG
AAACAGGCTGAAGATACAATATCAAATGCATCTTCGCAGCTTTCTTCTCCTCCTACTTCT
CCACAGAGTTCTCCAAGGAAAGGCTATACTTTGGCTCCCAGTGGTACTGTGGATAATTTT
TCAGATTCTGGTCACAGTGAAATTTCTTCACGATCCAGTATTGTTAGCAATTCGTCTTTT
GACTCAGTGCCAGTCTCACTGCACGATGAGAGGCGCCAGAGGCATTCTGTCAGCATCGTG
GAAACAAACCTAGGGATGGGCAGGATGGAGAGGCGGACCATGATTGAACCTGATCAGTAT
AGCTTGGGGTCCTATGCACCAATGTCCGAGGGCCGAGGCTTATATGCTACAGCTACAGTA
ATTTCTTCTCCAAGCACAGAGGAACTTTCCCAGGATCAGGGGGATCGCGCGTCACTTGAT
GCTGCTGACAGTGGCCGTGGGAGCTGGACGTCATGCTCAAGTGGCTCCCATGATAATATA
CAGACGATCCAGCACCAGAGAAGCTGGGAGACTCTTCCATTCGGGCATACTCACTTTGAT
TATTCAGGGGATCCTGCAGGTTTATGGGCATCAAGCAGCCATATGGACCAAATTATGTTT
TCTGATCATAGCACAAAGTATAACAGGCAAAATCAAAGTAGAGAGAGCCTTGAACAAGCC
CAGTCCCGAGCAAGCTGGGCGTCTTCCACAGGTTACTGGGGAGAAGACTCAGAAGGTGAC
ACAGGCACAATAAAGCGGAGGGGTGGAAAGGATGTTTCCATTGAAGCCGAAAGCAGTAGC
CTAACGTCTGTGACTACGGAAGAAACCAAGCCTGTCCCCATGCCTGCCCACATAGCTGTG
GCATCAAGTACTACAAAGGGGCTCATTGCACGAAAGGAGGGCAGGTATCGAGAGCCCCCG
CCCACCCCTCCCGGCTACATTGGAATTCCCATTACTGACTTTCCAGAAGGGCACTCCCAT
CCAGCCAGGAAACCGCCGGACTACAACGTGGCCCTTCAGAGATCGCGGATGGTCGCACGA
TCCTCCGACACAGCTGGGCCTTCATCCGTACAGCAGCCACATGGGCATCCCACCAGCAGC
AGGCCTGTGAACAAACCTCAGTGGCATAAACCGAACGAGTCTGACCCGCGCCTCGCCCCC
TATCAGTCCCAAGGGTTTTCCACCGAGGAGGATGAAGATGAACAAGTTTCTGCTGTTTGA
Enzyme 35 GenBank Gene ID NM_014247.2 Link Image
Enzyme 35 GeneCard ID RAPGEF2 Link Image
Enzyme 35 GenAtlas ID RAPGEF2 Link Image
Enzyme 35 HGNC ID HGNC:16854 Link Image
Enzyme 35 Chromosome Location 4
Enzyme 35 Locus 4q32.1
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
  2. Ohtsuka T, Hata Y, Ide N, Yasuda T, Inoue E, Inoue T, Mizoguchi A, Takai Y: nRap GEP: a novel neural GDP/GTP exchange protein for rap1 small G protein that interacts with synaptic scaffolding molecule (S-SCAM). Biochem Biophys Res Commun. 1999 Nov;265(1):38-44. [PubMed Link Image]
  3. de Rooij J, Boenink NM, van Triest M, Cool RH, Wittinghofer A, Bos JL: PDZ-GEF1, a guanine nucleotide exchange factor specific for Rap1 and Rap2. J Biol Chem. 1999 Dec 31;274(53):38125-30. [PubMed Link Image]
  4. Rebhun JF, Castro AF, Quilliam LA: Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction. J Biol Chem. 2000 Nov 10;275(45):34901-8. [PubMed Link Image]
  5. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  6. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 6586
Enzyme 36 Name Polyribonucleotide nucleotidyltransferase 1, mitochondrial
Enzyme 36 Synonyms
  1. 3'-5' RNA exonuclease OLD35
  2. PNPase old-35
  3. Polynucleotide phosphorylase 1
  4. PNPase 1
  5. Polynucleotide phosphorylase-like protein
Enzyme 36 Gene Name PNPT1
Enzyme 36 Protein Sequence >Polyribonucleotide nucleotidyltransferase 1, mitochondrial
MAACRYCCSCLRLRPLSDGPFLLPRRDRALTQLQVRALWSSAGSRAVAVDLGNRKLEISS
GKLARFADGSAVVQSGDTAVMVTAVSKTKPSPSQFMPLVVDYRQKAAAAGRIPTNYLRRE
IGTSDKEILTSRIIDRSIRPLFPAGYFYDTQVLCNLLAVDGVNEPDVLAINGASVALSLS
DIPWNGPVGAVRIGIIDGEYVVNPTRKEMSSSTLNLVVAGAPKSQIVMLEASAENILQQD
FCHAIKVGVKYTQQIIQGIQQLVKETGVTKRTPQKLFTPSPEIVKYTHKLAMERLYAVFT
DYEHDKVSRDEAVNKIRLDTEEQLKEKFPEADPYEIIESFNVVAKEVFRSIVLNEYKRCD
GRDLTSLRNVSCEVDMFKTLHGSALFQRGQTQVLCTVTFDSLESGIKSDQVITAINGIKD
KNFMLHYEFPPYATNEIGKVTGLNRRELGHGALAEKALYPVIPRDFPFTIRVTSEVLESN
GSSSMASACGGSLALMDSGVPISSAVAGVAIGLVTKTDPEKGEIEDYRLLTDILGIEDYN
GDMDFKIAGTNKGITALQADIKLPGIPIKIVMEAIQQASVAKKEILQIMNKTISKPRASR
KENGPVVETVQVPLSKRAKFVGPGGYNLKKLQAETGVTISQVDEETFSVFAPTPSAMHEA
RDFITEICKDDQEQQLEFGAVYTATITEIRDTGVMVKLYPNMTAVLLHNTQLDQRKIKHP
TALGLEVGQEIQVKYFGRDPADGRMRLSRKVLQSPATTVVRTLNDRSSIVMGEPISQSSS
NSQ
Enzyme 36 Number of Residues 783
Enzyme 36 Molecular Weight 85949.8
Enzyme 36 Theoretical pI 7.86
Enzyme 36 GO Classification
Function
  • 3'-5' exonuclease activity
  • 3'-5'-exoribonuclease activity
  • RNA binding
  • binding
  • catalytic activity
  • exonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • polyribonucleotide nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • RNA catabolic process
  • RNA metabolic process
  • RNA processing
  • cellular macromolecule metabolic process
  • mRNA catabolic process
  • macromolecule metabolic process
  • metabolic process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • mitochondrion
  • organelle
Enzyme 36 General Function Involved in 3'-5'-exoribonuclease activity
Enzyme 36 Specific Function Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3'- to 5'-direction
Enzyme 36 Pathways
Enzyme 36 Reactions
  • RNAn+1 + phosphate = RNAn + a nucleoside diphosphate [RN:R07282]
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 62988884 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q8TCS8 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name PNPT1_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >2352 bp
ATGGCGGCCTGCAGGTACTGCTGCTCGTGCCTCCGGCTCCGGCCCCTGAGCGATGGTCCT
TTCCTTCTGCCACGGCGGGATCGGGCACTCACCCAGTTGCAAGTGCGAGCACTATGGAGT
AGCGCAGGGTCTCGAGCTGTGGCCGTGGACTTAGGCAACAGGAAATTAGAAATATCTTCT
GGAAAGCTGGCCAGATTTGCAGATGGCTCTGCTGTAGTACAGTCAGGTGACACTGCAGTA
ATGGTCACAGCGGTCAGTAAAACAAAACCTTCCCCTTCCCAGTTTATGCCTTTGGTGGTT
GACTACAGACAAAAAGCTGCTGCAGCAGGTAGAATTCCCACAAACTATCTGAGAAGAGAG
ATTGGTACTTCTGATAAAGAAATTCTAACAAGTCGAATAATAGATCGTTCAATTAGACCG
CTCTTTCCAGCTGGCTACTTCTATGATACACAGGTTCTGTGTAATCTGTTAGCAGTAGAT
GGTGTAAATGAGCCTGATGTCCTAGCAATTAATGGCGCTTCCGTAGCCCTCTCATTATCA
GATATTCCTTGGAATGGACCTGTTGGGGCAGTACGAATAGGAATAATTGATGGAGAATAT
GTTGTTAACCCAACAAGAAAAGAAATGTCTTCTAGTACTTTAAATTTAGTGGTTGCTGGA
GCACCTAAAAGTCAGATTGTCATGTTGGAAGCCTCTGCAGAGAACATTTTACAGCAGGAC
TTTTGCCATGCTATCAAAGTGGGAGTGAAATATACCCAACAAATAATTCAGGGCATTCAG
CAGTTGGTAAAAGAAACTGGTGTTACCAAGAGGACACCTCAGAAGTTATTTACCCCTTCG
CCAGAGATTGTGAAATATACTCATAAACTTGCTATGGAGAGACTCTATGCAGTTTTTACA
GATTACGAGCATGACAAAGTTTCCAGAGATGAAGCTGTTAACAAAATAAGATTAGATACG
GAGGAACAACTAAAAGAAAAATTTCCAGAAGCCGATCCATATGAAATAATAGAATCCTTC
AATGTTGTTGCAAAGGAAGTTTTTAGAAGTATTGTTTTGAATGAATACAAAAGGTGCGAT
GGTCGGGATTTGACTTCACTTAGGAATGTAAGTTGTGAGGTAGATATGTTTAAAACCCTT
CATGGATCAGCATTATTTCAAAGAGGACAAACACAGGTGCTTTGTACCGTTACATTTGAT
TCATTAGAATCTGGTATTAAGTCAGATCAAGTTATAACAGCTATAAATGGGATAAAAGAT
AAAAATTTCATGCTGCACTACGAGTTTCCTCCTTATGCAACTAATGAAATTGGCAAAGTC
ACTGGTTTAAATAGAAGAGAACTTGGGCATGGTGCTCTTGCTGAGAAAGCTTTGTATCCT
GTTATTCCCCGAGATTTTCCTTTCACCATAAGAGTTACATCTGAAGTCCTAGAGTCAAAT
GGGTCATCTTCTATGGCATCTGCATGTGGCGGAAGTTTAGCATTAATGGATTCAGGGGTT
CCAATTTCATCTGCTGTTGCAGGCGTAGCAATAGGATTGGTCACCAAAACCGATCCTGAG
AAGGGTGAAATAGAAGATTATCGTTTGCTGACAGATATTTTGGGAATTGAAGATTACAAT
GGTGACATGGACTTCAAAATAGCTGGCACTAATAAAGGAATAACTGCATTACAGGCTGAT
ATTAAATTACCTGGAATACCAATAAAAATTGTGATGGAGGCTATTCAACAAGCTTCAGTG
GCAAAAAAGGAGATATTACAGATCATGAACAAAACTATTTCAAAACCTCGAGCATCTAGA
AAAGAAAATGGACCTGTTGTAGAAACTGTTCAGGTTCCATTATCAAAACGAGCAAAATTT
GTTGGACCTGGTGGCTATAACTTAAAAAAACTTCAGGCTGAAACAGGTGTAACTATTAGT
CAGGTGGATGAAGAAACGTTTTCTGTATTTGCACCAACACCCAGTGCTATGCATGAGGCA
AGAGACTTCATTACTGAAATCTGCAAGGATGATCAGGAGCAGCAATTAGAATTTGGAGCA
GTATATACCGCCACAATAACTGAAATCAGAGATACTGGTGTAATGGTAAAATTATATCCA
AATATGACTGCGGTACTGCTTCATAACACACAACTTGATCAACGAAAGATTAAACATCCT
ACTGCCCTAGGATTAGAAGTTGGCCAAGAAATTCAGGTGAAATACTTTGGACGTGACCCA
GCCGATGGAAGAATGAGGCTTTCTCGAAAAGTGCTTCAGTCGCCAGCTACAACCGTGGTC
AGAACTTTGAATGACAGAAGTAGTATTGTAATGGGAGAACCTATTTCACAGTCATCATCT
AATTCTCAGTGA
Enzyme 36 GenBank Gene ID AC015982 Link Image
Enzyme 36 GeneCard ID PNPT1 Link Image
Enzyme 36 GenAtlas ID PNPT1 Link Image
Enzyme 36 HGNC ID HGNC:23166 Link Image
Enzyme 36 Chromosome Location 2
Enzyme 36 Locus 2p15
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Raijmakers R, Egberts WV, van Venrooij WJ, Pruijn GJ: Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring. J Mol Biol. 2002 Nov 1;323(4):653-63. [PubMed Link Image]
  2. Leszczyniecka M, Kang DC, Sarkar D, Su ZZ, Holmes M, Valerie K, Fisher PB: Identification and cloning of human polynucleotide phosphorylase, hPNPase old-35, in the context of terminal differentiation and cellular senescence. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16636-41. Epub 2002 Dec 9. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  6. Piwowarski J, Grzechnik P, Dziembowski A, Dmochowska A, Minczuk M, Stepien PP: Human polynucleotide phosphorylase, hPNPase, is localized in mitochondria. J Mol Biol. 2003 Jun 20;329(5):853-7. [PubMed Link Image]
  7. French SW, Dawson DW, Chen HW, Rainey RN, Sievers SA, Balatoni CE, Wong L, Troke JJ, Nguyen MT, Koehler CM, Teitell MA: The TCL1 oncoprotein binds the RNase PH domains of the PNPase exoribonuclease without affecting its RNA degrading activity. Cancer Lett. 2007 Apr 18;248(2):198-210. Epub 2006 Aug 28. [PubMed Link Image]
  8. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  9. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  10. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 7002
Enzyme 37 Name Rho guanine nucleotide exchange factor 1
Enzyme 37 Synonyms
  1. 115 kDa guanine nucleotide exchange factor
  2. p115-RhoGEF
  3. p115RhoGEF
  4. Sub1.5
Enzyme 37 Gene Name ARHGEF1
Enzyme 37 Protein Sequence >Rho guanine nucleotide exchange factor 1
MEDFARGAASPGPSRPGLVPVSIIGAEDEDFENELETNSEEQNSQFQSLEQVKRRPAHLM
ALLQHVALQFEPGPLLCCLHADMLGSLGPKEAKKAFLDFYHSFLEKTAVLRVPVPPNVAF
ELDRTRADLISEDVQRRFVQEVVQSQQVAVGRQLEDFRSKRLMGMTPWEQELAQLEAWVG
RDRASYEARERHVAERLLMHLEEMQHTISTDEEKSAAVVNAIGLYMRHLGVRTKSGDKKS
GRNFFRKKVMGNRRSDEPAKTKKGLSSILDAARWNRGEPQVPDFRHLKAEVDAEKPGATD
RKGGVGMPSRDRNIGAPGQDTPGVSLHPLSLDSPDREPGADAPLELGDSSPQGPMSLESL
APPESTDEGAETESPEPGDEGEPGRSGLELEPEEPPGWRELVPPDTLHSLPKSQVKRQEV
ISELLVTEAAHVRMLRVLHDLFFQPMAECLFFPLEELQNIFPSLDELIEVHSLFLDRLMK
RRQESGYLIEEIGDVLLARFDGAEGSWFQKISSRFCSRQSFALEQLKAKQRKDPRFCAFV
QEAESRPRCRRLQLKDMIPTEMQRLTKYPLLLQSIGQNTEEPTEREKVELAAECCREILH
HVNQAVRDMEDLLRLKDYQRRLDLSHLRQSSDPMLSEFKNLDITKKKLVHEGPLTWRVTK
DKAVEVHVLLLDDLLLLLQRQDERLLLKSHSRTLTPTPDGKTMLRPVLRLTSAMTREVAT
DHKAFYVLFTWDQEAQIYELVAQTVSERKNWCALITETAGSLKVPAPASRPKPRPSPSST
REPLLSSSENGNGGRETSPADARTERILSDLLPFCRPGPEGQLAATALRKVLSLKQLLFP
AEEDNGAGPPRDGDGVPGGGPLSPARTQEIQENLLSLEETMKQLEELEEEFCRLRPLLSQ
LGGNSVPQPGCT
Enzyme 37 Number of Residues 912
Enzyme 37 Molecular Weight 102434.3
Enzyme 37 Theoretical pI 5.37
Enzyme 37 GO Classification
Function
  • GTPase regulator activity
  • Ras guanyl-nucleotide exchange factor activity
  • Rho guanyl-nucleotide exchange factor activity
  • enzyme regulator activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
  • biological regulation
  • regulation of Ras protein signal transduction
  • regulation of Rho protein signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
Component
  • cell part
  • cytoplasm
  • intracellular
  • intracellular part
Enzyme 37 General Function Involved in GTPase activator activity
Enzyme 37 Specific Function Seems to play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13) subunits. Acts as GTPase-activating protein (GAP) for GNA12 and GNA13, and as guanine nucleotide exchange factor (GEF) for RhoA GTPase. Activated G alpha 13/GNA13 stimulates the RhoGEF activity through interaction with the RGS-like domain. This GEF activity is inhibited by binding to activated GNA12
Enzyme 37 Pathways Not Available
Enzyme 37 Reactions Not Available
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • None
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 15011972 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q92888 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name ARHG1_HUMAN Link Image
Enzyme 37 PDB ID 1SHZ Link Image
Enzyme 37 PDB File Show
Enzyme 37 3D Structure
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >2739 bp
ATGGAAGACTTCGCCCGAGGGGCGGCCTCCCCAGGCCCCTCCCGGCCTGGCCTGGTTCCC
GTCAGCATCATCGGGGCTGAGGATGAGGATTTTGAGAACGAGCTGGAGACAAACTCAGAA
GAGCAAAACAGCCAGTTCCAGAGCCTGGAGCAGGTGAAGCGGCGCCCAGCCCACCTCATG
GCCCTCCTGCAGCACGTGGCCCTGCAGTTTGAGCCAGGACCCCTGCTTTGCTGTCTGCAT
GCCGACATGCTGGGCTCACTGGGCCCCAAGGAGGCCAAGAAGGCCTTCCTGGACTTCTAC
CACAGCTTCCTGGAGAAGACAGCGGTTCTCCGGGTGCCGGTCCCTCCCAACGTCGCCTTT
GAACTTGACCGCACTAGGGCTGACCTCATCTCCGAGGATGTCCAGCGGCGGTTCGTGCAG
GAGGTGGTGCAAAGCCAGCAGGTAGCCGTGGGCCGGCAGCTGGAGGACTTCCGTTCCAAG
CGGCTCATGGGCATGACGCCCTGGGAGCAGGAGCTGGCCCAGCTGGAGGCTTGGGTTGGG
CGGGACCGAGCCAGCTACGAGGCCCGGGAGCGGCACGTGGCGGAGCGGCTGCTCATGCAC
CTGGAGGAGATGCAACATACCATCTCTACCGACGAAGAAAAGAGTGCTGCCGTGGTCAAC
GCCATTGGCCTGTACATGCGCCACCTTGGGGTGCGGACCAAGAGTGGAGACAAGAAGTCG
GGGAGGAACTTCTTCCGGAAAAAGGTGATGGGGAACCGGCGGTCGGACGAGCCTGCCAAG
ACCAAGAAGGGGCTGAGCAGCATCCTGGATGCCGCCCGCTGGAACCGGGGAGAGCCCCAG
GTTCCAGATTTTCGACACCTCAAAGCAGAGGTTGATGCCGAGAAGCCAGGTGCTACAGAC
CGGAAGGGAGGCGTGGGGATGCCCTCTCGGGACCGGAATATCGGGGCTCCTGGGCAGGAC
ACCCCTGGAGTCTCTCTGCACCCTCTGTCCCTGGACAGCCCAGACCGGGAACCAGGTGCT
GACGCCCCCCTGGAGCTGGGGGACTCATCCCCGCAGGGCCCAATGAGCCTGGAGTCCTTG
GCGCCCCCAGAGAGTACCGACGAGGGGGCCGAAACCGAGAGCCCCGAGCCTGGAGATGAG
GGGGAGCCGGGGCGGTCGGGACTGGAGCTTGAACCAGAAGAGCCTCCCGGCTGGCGGGAA
CTCGTCCCCCCAGACACCCTGCACAGCCTGCCCAAGAGCCAGGTGAAGCGGCAGGAGGTC
ATCAGCGAGCTGCTGGTGACAGAGGCGGCCCACGTGCGCATGCTGCGGGTGCTGCACGAC
CTCTTCTTCCAGCCCATGGCAGAATGCCTGTTCTTCCCCTTGGAGGAGCTGCAGAACATC
TTCCCCAGCCTGGACGAGCTCATCGAGGTGCATTCCCTGTTCCTCGATCGCCTGATGAAG
CGGAGGCAGGAGAGTGGCTACCTCATCGAGGAGATCGGAGACGTGCTGCTGGCCCGGTTT
GATGGTGCTGAGGGCTCCTGGTTCCAGAAAATCTCCTCCCGCTTCTGCAGCCGCCAGTCA
TTTGCCTTAGAGCAGCTCAAAGCCAAGCAACGCAAGGACCCTCGGTTCTGTGCCTTCGTG
CAGGAAGCTGAGAGCCGCCCGCGGTGCCGCCGCCTGCAGCTGAAGGACATGATCCCCACG
GAGATGCAGCGGCTGACCAAGTACCCCCTGCTCCTGCAGAGCATCGGGCAGAACACAGAA
GAGCCCACAGAACGGGAGAAAGTGGAGCTGGCAGCCGAGTGCTGCCGGGAAATTCTACAC
CACGTCAACCAAGCCGTGCGTGACATGGAGGACCTGCTGAGGCTCAAGGACTATCAGCGG
CGCCTGGACTTGTCCCACCTTCGGCAGAGCAGCGACCCTATGCTGAGCGAGTTCAAGAAC
CTGGACATCACCAAGAAGAAATTGGTCCACGAGGGCCCACTGACGTGGCGGGTGACTAAG
GACAAGGCAGTGGAGGTGCATGTGCTGCTGCTGGACGACCTGCTGCTGCTGCTCCAGCGC
CAGGACGAGCGGCTGCTGCTCAAGTCCCATAGCCGGACACTGACGCCCACGCCCGATGGC
AAGACCATGCTGCGGCCCGTGCTGCGGCTCACCTCCGCCATGACCCGCGAGGTGGCCACC
GATCACAAAGCCTTCTACGTCCTTTTTACCTGGGACCAGGAGGCCCAGATATACGAGCTG
GTGGCACAGACTGTGTCGGAGCGGAAAAACTGGTGTGCTCTCATCACTGAGACTGCCGGA
TCCCTGAAAGTCCCTGCCCCTGCCTCTCGCCCTAAGCCCCGGCCCAGCCCGAGCAGCACC
CGAGAACCCCTCCTCAGCAGCTCTGAGAACGGCAATGGTGGCCGAGAGACGTCTCCAGCT
GATGCCCGGACCGAGAGAATCCTCAGTGACCTCCTGCCCTTCTGCAGACCAGGCCCCGAG
GGCCAGCTCGCTGCCACGGCCCTTCGGAAAGTGCTGTCCCTGAAGCAGCTTCTGTTTCCG
GCGGAGGAAGACAATGGGGCGGGGCCTCCTCGAGATGGGGATGGGGTCCCAGGGGGCGGC
CCCCTGAGCCCAGCACGGACCCAGGAAATCCAGGAGAACCTGCTCAGCTTGGAGGAGACC
ATGAAGCAGCTGGAGGAGTTGGAGGAGGAATTTTGCCGCCTGAGACCCCTCCTGTCTCAG
CTTGGGGGGAACTCTGTCCCCCAGCCTGGCTGCACTTGA
Enzyme 37 GenBank Gene ID NM_004706.3 Link Image
Enzyme 37 GeneCard ID ARHGEF1 Link Image
Enzyme 37 GenAtlas ID Not Available
Enzyme 37 HGNC ID Not Available
Enzyme 37 Chromosome Location 1
Enzyme 37 Locus 19q13.13
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Hart MJ, Sharma S, elMasry N, Qiu RG, McCabe P, Polakis P, Bollag G: Identification of a novel guanine nucleotide exchange factor for the Rho GTPase. J Biol Chem. 1996 Oct 11;271(41):25452-8. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Aasheim HC, Pedeutour F, Smeland EB: Characterization, expression and chromosomal localization of a human gene homologous to the mouse Lsc oncogene, with strongest expression in hematopoetic tissues. Oncogene. 1997 Apr 10;14(14):1747-52. [PubMed Link Image]
  4. Kozasa T, Jiang X, Hart MJ, Sternweis PM, Singer WD, Gilman AG, Bollag G, Sternweis PC: p115 RhoGEF, a GTPase activating protein for Galpha12 and Galpha13. Science. 1998 Jun 26;280(5372):2109-11. [PubMed Link Image]
  5. Hart MJ, Jiang X, Kozasa T, Roscoe W, Singer WD, Gilman AG, Sternweis PC, Bollag G: Direct stimulation of the guanine nucleotide exchange activity of p115 RhoGEF by Galpha13. Science. 1998 Jun 26;280(5372):2112-4. [PubMed Link Image]
  6. Bhattacharyya R, Wedegaertner PB: Galpha 13 requires palmitoylation for plasma membrane localization, Rho-dependent signaling, and promotion of p115-RhoGEF membrane binding. J Biol Chem. 2000 May 19;275(20):14992-9. [PubMed Link Image]
  7. Park B, Nguyen NT, Dutt P, Merdek KD, Bashar M, Sterpetti P, Tosolini A, Testa JR, Toksoz D: Association of Lbc Rho guanine nucleotide exchange factor with alpha-catenin-related protein, alpha-catulin/CTNNAL1, supports serum response factor activation. J Biol Chem. 2002 Nov 22;277(47):45361-70. Epub 2002 Sep 20. [PubMed Link Image]
  8. Holinstat M, Mehta D, Kozasa T, Minshall RD, Malik AB: Protein kinase Calpha-induced p115RhoGEF phosphorylation signals endothelial cytoskeletal rearrangement. J Biol Chem. 2003 Aug 1;278(31):28793-8. Epub 2003 May 16. [PubMed Link Image]
  9. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  10. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  11. Chen Z, Wells CD, Sternweis PC, Sprang SR: Structure of the rgRGS domain of p115RhoGEF. Nat Struct Biol. 2001 Sep;8(9):805-9. [PubMed Link Image]
  12. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 7120
Enzyme 38 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
Enzyme 38 Synonyms
  1. G gamma-I
Enzyme 38 Gene Name GNG2
Enzyme 38 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL
Enzyme 38 Number of Residues 71
Enzyme 38 Molecular Weight 7850.0
Enzyme 38 Theoretical pI 8.22
Enzyme 38 GO Classification
Function
  • molecular transducer activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • extrinsic to membrane
  • extrinsic to plasma membrane
  • heterotrimeric G-protein complex
  • membrane part
Enzyme 38 General Function Involved in signal transducer activity
Enzyme 38 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions Not Available
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 20147633 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID P59768 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name GBG2_HUMAN Link Image
Enzyme 38 PDB ID 1GP2 Link Image
Enzyme 38 PDB File Show
Enzyme 38 3D Structure
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >216 bp
ATGGCCAGCAACAACACCGCCAGCATAGCACAAGCCAGGAAGCTGGTAGAGCAGCTTAAG
ATGGAAGCCAATATCGACAGGATAAAGGTGTCCAAGGCAGCTGCAGATTTGATGGCCTAC
TGTGAAGCACATGCCAAGGAAGACCCCCTCCTGACCCCTGTTCCGGCTTCAGAAAACCCG
TTTAGGGAGAAGAAGTTTTTCTGTGCCATCCTTTAA
Enzyme 38 GenBank Gene ID AF493870 Link Image
Enzyme 38 GeneCard ID GNG2 Link Image
Enzyme 38 GenAtlas ID GNG2 Link Image
Enzyme 38 HGNC ID HGNC:4404 Link Image
Enzyme 38 Chromosome Location 1
Enzyme 38 Locus 14q21
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Modarressi MH, Taylor KE, Wolfe J: Cloning, characterization, and mapping of the gene encoding the human G protein gamma 2 subunit. Biochem Biophys Res Commun. 2000 Jun 7;272(2):610-5. [PubMed Link Image]
  2. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 7131
Enzyme 39 Name Ras-related C3 botulinum toxin substrate 1
Enzyme 39 Synonyms
  1. Cell migration-inducing gene 5 protein
  2. Ras-like protein TC25
  3. p21-Rac1
Enzyme 39 Gene Name RAC1
Enzyme 39 Protein Sequence >Ras-related C3 botulinum toxin substrate 1
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAG
QEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLR
DDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPP
PVKKRKRKCLLL
Enzyme 39 Number of Residues 192
Enzyme 39 Molecular Weight 21449.9
Enzyme 39 Theoretical pI 8.65
Enzyme 39 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 39 General Function Involved in GTP binding
Enzyme 39 Specific Function Isoform B has an accelerated GEF-independent GDP/GTP exchange and an impaired GTP hydrolysis, which is restored partially by GTPase-activating proteins. It is able to bind to the GTPase-binding domain of PAK but not full-length PAK in a GTP- dependent manner, suggesting that the insertion does not completely abolish effector interaction
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions Not Available
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein Not Available
Enzyme 39 UniProtKB/Swiss-Prot ID P63000 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name RAC1_HUMAN Link Image
Enzyme 39 PDB ID 1I4L Link Image
Enzyme 39 PDB File Show
Enzyme 39 3D Structure
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >579 bp
ATGCAGGCCATCAAGTGTGTGGTGGTGGGAGACGGAGCTGTAGGTAAAACTTGCCTACTG
ATCAGTTACACAACCAATGCATTTCCTGGAGAATATATCCCTACTGTCTTTGACAATTAT
TCTGCCAATGTTATGGTAGATGGAAAACCGGTGAATCTGGGCTTATGGGATACAGCTGGA
CAAGAAGATTATGACAGATTACGCCCCCTATCCTATCCGCAAACAGATGTGTTCTTAATT
TGCTTTTCCCTTGTGAGTCCTGCATCATTTGAAAATGTCCGTGCAAAGTGGTATCCTGAG
GTGCGGCACCACTGTCCCAACACTCCCATCATCCTAGTGGGAACTAAACTTGATCTTAGG
GATGATAAAGACACGATCGAGAAACTGAAGGAGAAGAAGCTGACTCCCATCACCTATCCG
CAGGGTCTAGCCATGGCTAAGGAGATTGGTGCTGTAAAATACCTGGAGTGCTCGGCGCTC
ACACAGCGAGGCCTCAAGACAGTGTTTGACGAAGCGATCCGAGCAGTCCTCTGCCCGCCT
CCCGTGAAGAAGAGGAAGAGAAAATGCCTGCTGTTGTAA
Enzyme 39 GenBank Gene ID M29870 Link Image
Enzyme 39 GeneCard ID RAC1 Link Image
Enzyme 39 GenAtlas ID RAC1 Link Image
Enzyme 39 HGNC ID HGNC:9801 Link Image
Enzyme 39 Chromosome Location 7
Enzyme 39 Locus 7p22
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Didsbury J, Weber RF, Bokoch GM, Evans T, Snyderman R: rac, a novel ras-related family of proteins that are botulinum toxin substrates. J Biol Chem. 1989 Oct 5;264(28):16378-82. [PubMed Link Image]
  2. Drivas GT, Shih A, Coutavas E, Rush MG, D'Eustachio P: Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line. Mol Cell Biol. 1990 Apr;10(4):1793-8. [PubMed Link Image]
  3. Matos P, Skaug J, Marques B, Beck S, Verissimo F, Gespach C, Boavida MG, Scherer SW, Jordan P: Small GTPase Rac1: structure, localization, and expression of the human gene. Biochem Biophys Res Commun. 2000 Nov 2;277(3):741-51. [PubMed Link Image]
  4. Jordan P, Brazao R, Boavida MG, Gespach C, Chastre E: Cloning of a novel human Rac1b splice variant with increased expression in colorectal tumors. Oncogene. 1999 Nov 18;18(48):6835-9. [PubMed Link Image]
  5. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Kinsella BT, Erdman RA, Maltese WA: Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA. J Biol Chem. 1991 May 25;266(15):9786-94. [PubMed Link Image]
  8. Ridley AJ, Paterson HF, Johnston CL, Diekmann D, Hall A: The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell. 1992 Aug 7;70(3):401-10. [PubMed Link Image]
  9. Jullien-Flores V, Dorseuil O, Romero F, Letourneur F, Saragosti S, Berger R, Tavitian A, Gacon G, Camonis JH: Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity. J Biol Chem. 1995 Sep 22;270(38):22473-7. [PubMed Link Image]
  10. Ren Y, Li R, Zheng Y, Busch H: Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases. J Biol Chem. 1998 Dec 25;273(52):34954-60. [PubMed Link Image]
  11. Nishihara H, Kobayashi S, Hashimoto Y, Ohba F, Mochizuki N, Kurata T, Nagashima K, Matsuda M: Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins. Biochim Biophys Acta. 1999 Nov 11;1452(2):179-87. [PubMed Link Image]
  12. Johansson A, Driessens M, Aspenstrom P: The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1. J Cell Sci. 2000 Sep;113 ( Pt 18):3267-75. [PubMed Link Image]
  13. Miki H, Yamaguchi H, Suetsugu S, Takenawa T: IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature. 2000 Dec 7;408(6813):732-5. [PubMed Link Image]
  14. Vikis HG, Li W, He Z, Guan KL: The semaphorin receptor plexin-B1 specifically interacts with active Rac in a ligand-dependent manner. Proc Natl Acad Sci U S A. 2000 Nov 7;97(23):12457-62. [PubMed Link Image]
  15. Noda Y, Takeya R, Ohno S, Naito S, Ito T, Sumimoto H: Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C. Genes Cells. 2001 Feb;6(2):107-19. [PubMed Link Image]
  16. Welch HC, Coadwell WJ, Ellson CD, Ferguson GJ, Andrews SR, Erdjument-Bromage H, Tempst P, Hawkins PT, Stephens LR: P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-nucleotide exchange factor for Rac. Cell. 2002 Mar 22;108(6):809-21. [PubMed Link Image]
  17. Brugnera E, Haney L, Grimsley C, Lu M, Walk SF, Tosello-Trampont AC, Macara IG, Madhani H, Fink GR, Ravichandran KS: Unconventional Rac-GEF activity is mediated through the Dock180-ELMO complex. Nat Cell Biol. 2002 Aug;4(8):574-82. [PubMed Link Image]
  18. Takeya R, Ueno N, Kami K, Taura M, Kohjima M, Izaki T, Nunoi H, Sumimoto H: Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases. J Biol Chem. 2003 Jul 4;278(27):25234-46. Epub 2003 Apr 25. [PubMed Link Image]
  19. Masuda-Robens JM, Kutney SN, Qi H, Chou MM: The TRE17 oncogene encodes a component of a novel effector pathway for Rho GTPases Cdc42 and Rac1 and stimulates actin remodeling. Mol Cell Biol. 2003 Mar;23(6):2151-61. [PubMed Link Image]
  20. Li W, Guan KL: The Down syndrome cell adhesion molecule (DSCAM) interacts with and activates Pak. J Biol Chem. 2004 Jul 30;279(31):32824-31. Epub 2004 May 28. [PubMed Link Image]
  21. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed Link Image]
  22. Watabe-Uchida M, John KA, Janas JA, Newey SE, Van Aelst L: The Rac activator DOCK7 regulates neuronal polarity through local phosphorylation of stathmin/Op18. Neuron. 2006 Sep 21;51(6):727-39. [PubMed Link Image]
  23. Oka T, Ihara S, Fukui Y: Cooperation of DEF6 with activated Rac in regulating cell morphology. J Biol Chem. 2007 Jan 19;282(3):2011-8. Epub 2006 Nov 22. [PubMed Link Image]
  24. Millard TH, Dawson J, Machesky LM: Characterisation of IRTKS, a novel IRSp53/MIM family actin regulator with distinct filament bundling properties. J Cell Sci. 2007 May 1;120(Pt 9):1663-72. Epub 2007 Apr 12. [PubMed Link Image]
  25. Lores P, Visvikis O, Luna R, Lemichez E, Gacon G: The SWI/SNF protein BAF60b is ubiquitinated through a signalling process involving Rac GTPase and the RING finger protein Unkempt. FEBS J. 2010 Mar;277(6):1453-64. Epub 2010 Feb 8. [PubMed Link Image]
  26. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  27. Worby CA, Mattoo S, Kruger RP, Corbeil LB, Koller A, Mendez JC, Zekarias B, Lazar C, Dixon JE: The fic domain: regulation of cell signaling by adenylylation. Mol Cell. 2009 Apr 10;34(1):93-103. [PubMed Link Image]
  28. Yarbrough ML, Li Y, Kinch LN, Grishin NV, Ball HL, Orth K: AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science. 2009 Jan 9;323(5911):269-72. Epub 2008 Nov 27. [PubMed Link Image]
  29. Frasa MA, Maximiano FC, Smolarczyk K, Francis RE, Betson ME, Lozano E, Goldenring J, Seabra MC, Rak A, Ahmadian MR, Braga VM: Armus is a Rac1 effector that inactivates Rab7 and regulates E-cadherin degradation. Curr Biol. 2010 Feb 9;20(3):198-208. Epub 2010 Jan 28. [PubMed Link Image]
  30. Hirshberg M, Stockley RW, Dodson G, Webb MR: The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue. Nat Struct Biol. 1997 Feb;4(2):147-52. [PubMed Link Image]
  31. Lapouge K, Smith SJ, Walker PA, Gamblin SJ, Smerdon SJ, Rittinger K: Structure of the TPR domain of p67phox in complex with Rac.GTP. Mol Cell. 2000 Oct;6(4):899-907. [PubMed Link Image]
  32. Worthylake DK, Rossman KL, Sondek J: Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1. Nature. 2000 Dec 7;408(6813):682-8. [PubMed Link Image]
  33. Stebbins CE, Galan JE: Modulation of host signaling by a bacterial mimic: structure of the Salmonella effector SptP bound to Rac1. Mol Cell. 2000 Dec;6(6):1449-60. [PubMed Link Image]
  34. Wurtele M, Wolf E, Pederson KJ, Buchwald G, Ahmadian MR, Barbieri JT, Wittinghofer A: How the Pseudomonas aeruginosa ExoS toxin downregulates Rac. Nat Struct Biol. 2001 Jan;8(1):23-6. [PubMed Link Image]
  35. Grizot S, Faure J, Fieschi F, Vignais PV, Dagher MC, Pebay-Peyroula E: Crystal structure of the Rac1-RhoGDI complex involved in nadph oxidase activation. Biochemistry. 2001 Aug 28;40(34):10007-13. [PubMed Link Image]
  36. Tarricone C, Xiao B, Justin N, Walker PA, Rittinger K, Gamblin SJ, Smerdon SJ: The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways. Nature. 2001 May 10;411(6834):215-9. [PubMed Link Image]
  37. Fiegen D, Haeusler LC, Blumenstein L, Herbrand U, Dvorsky R, Vetter IR, Ahmadian MR: Alternative splicing of Rac1 generates Rac1b, a self-activating GTPase. J Biol Chem. 2004 Feb 6;279(6):4743-9. Epub 2003 Nov 18. [PubMed Link Image]
  38. Prehna G, Ivanov MI, Bliska JB, Stebbins CE: Yersinia virulence depends on mimicry of host Rho-family nucleotide dissociation inhibitors. Cell. 2006 Sep 8;126(5):869-80. [PubMed Link Image]
  39. Jezyk MR, Snyder JT, Gershberg S, Worthylake DK, Harden TK, Sondek J: Crystal structure of Rac1 bound to its effector phospholipase C-beta2. Nat Struct Mol Biol. 2006 Dec;13(12):1135-40. Epub 2006 Nov 19. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 7133
Enzyme 40 Name Rho GDP-dissociation inhibitor 3
Enzyme 40 Synonyms
  1. Rho GDI 3
  2. Rho-GDI gamma
Enzyme 40 Gene Name ARHGDIG
Enzyme 40 Protein Sequence >Rho GDP-dissociation inhibitor 3
MLGLDACELGAQLLELLRLALCARVLLADKEGGPPAVDEVLDEAVPEYRAPGRKSLLEIR
QLDPDDRSLAKYKRVLLGPLPPAVDPSLPNVQVTRLTLLSEQAPGPVVMDLTGDLAVLKD
QVFVLKEGVDYRVKISFKVHREIVSGLKCLHHTYRRGLRVDKTVYMVGSYGPSAQEYEFV
TPVEEAPRGALVRGPYLVVSLFTDDDRTHHLSWEWGLCICQDWKD
Enzyme 40 Number of Residues 225
Enzyme 40 Molecular Weight 25097.8
Enzyme 40 Theoretical pI 5.37
Enzyme 40 GO Classification
Function
  • GDP-dissociation inhibitor activity
  • GTPase regulator activity
  • Rho GDP-dissociation inhibitor activity
  • enzyme regulator activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 40 General Function Involved in Rho GDP-dissociation inhibitor activity
Enzyme 40 Specific Function Inhibits GDP/GTP exchange reaction of RhoB. Interacts specifically with the GDP- and GTP-bound forms of post- translationally processed Rhob and Rhog proteins, both of which show a growth-regulated expression in mammalian cells. Stimulates the release of the GDP-bound but not the GTP-bound RhoB protein. Also inhibits the GDP/GTP exchange of RhoB but shows less ability to inhibit the dissociation of prebound GTP
Enzyme 40 Pathways Not Available
Enzyme 40 Reactions Not Available
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 82941188 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID Q99819 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name GDIR3_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >678 bp
ATGCTGGGCCTGGACGCGTGCGAGCTGGGGGCGCAGCTGCTGGAGCTGCTCCGGCTGGCG
CTGTGCGCCCGAGTCCTCCTGGCTGACAAGGAGGGTGGGCCGCCGGCAGTGGACGAGGTG
TTGGATGAGGCTGTGCCCGAGTACCGGGCGCCGGGGAGGAAGAGCCTCTTGGAGATCCGG
CAGCTGGACCCGGACGACAGGAGCCTGGCCAAGTACAAGCGGGTGCTGCTGGGGCCCCTG
CCACCGGCCGTGGACCCAAGCCTGCCCAATGTGCAGGTGACCAGGCTGACACTCCTGTCG
GAACAGGCTCCGGGGCCCGTCGTCATGGATCTCACAGGGGACCTGGCTGTTCTGAAGGAC
CAGGTGTTTGTCCTGAAGGAAGGTGTTGATTACAGAGTGAAGATCTCCTTCAAGGTCCAC
AGGGAGATTGTCAGCGGCCTCAAGTGTCTGCACCACACCTACCGCCGGGGCCTGCGCGTG
GACAAGACCGTCTACATGGTGGGCAGCTATGGCCCGAGCGCCCAGGAGTATGAGTTTGTG
ACTCCGGTGGAGGAAGCGCCGAGGGGTGCGCTGGTGCGGGGCCCCTATCTGGTGGTGTCC
CTCTTCACCGACGATGACAGGACGCACCACCTGTCCTGGGAGTGGGGTCTCTGCATCTGC
CAGGACTGGAAGGACTGA
Enzyme 40 GenBank Gene ID AB127078 Link Image
Enzyme 40 GeneCard ID ARHGDIG Link Image
Enzyme 40 GenAtlas ID ARHGDIG Link Image
Enzyme 40 HGNC ID HGNC:680 Link Image
Enzyme 40 Chromosome Location 1
Enzyme 40 Locus 16p13.3
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Adra CN, Manor D, Ko JL, Zhu S, Horiuchi T, Van Aelst L, Cerione RA, Lim B: RhoGDIgamma: a GDP-dissociation inhibitor for Rho proteins with preferential expression in brain and pancreas. Proc Natl Acad Sci U S A. 1997 Apr 29;94(9):4279-84. [PubMed Link Image]
  2. Adra CN, Iyengar AR, Syed FA, Kanaan IN, Rilo HL, Yu W, Kheraj R, Lin SR, Horiuchi T, Khan S, Weremowicz S, Lim B, Morton CC, Higgs DR: Human ARHGDIG, a GDP-dissociation inhibitor for Rho proteins: genomic structure, sequence, expression analysis, and mapping to chromosome 16p13.3. Genomics. 1998 Oct 1;53(1):104-9. [PubMed Link Image]
  3. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  4. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 7134
Enzyme 41 Name Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Enzyme 41 Synonyms
  1. Adenylate cyclase-stimulating G alpha protein
Enzyme 41 Gene Name GNAS
Enzyme 41 Protein Sequence >Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQM
RILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELA
NPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLD
KIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFND
VTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEK
VLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCY
PHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL
Enzyme 41 Number of Residues 394
Enzyme 41 Molecular Weight 45664.2
Enzyme 41 Theoretical pI 5.56
Enzyme 41 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • molecular transducer activity
  • nucleotide binding
  • purine nucleotide binding
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • biological regulation
  • cell surface receptor linked signaling pathway
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 41 General Function Involved in signal transducer activity
Enzyme 41 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(s) protein is involved in hormonal regulation of adenylate cyclase:it activates the cyclase in response to beta-adrenergic stimuli
Enzyme 41 Pathways Not Available
Enzyme 41 Reactions Not Available
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 31915 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID P63092 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name GNAS2_HUMAN Link Image
Enzyme 41 PDB ID 1U0H Link Image
Enzyme 41 PDB File Show
Enzyme 41 3D Structure
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >1185 bp
ATGGGCTGCCTCGGGAACAGTAAGACCGAGGACCAGCGCAACGAGGAGAAGGCGCAGCGT
GAGGCCAACAAAAAGATCGAGAAGCAGCTGCAGAAGGACAAGCAGGTCTACCGGGCCACG
CACCGCCTGCTGCTGCTGGGTGCTGGAGAATCTGGTAAAAGCACCATTGTGAAGCAGATG
AGGATCCTGCATGTTAATGGGTTTAATGGAGAGGGCGGCGAAGAGGACCCGCAGGCTGCA
AGGAGCAACAGCGATGGTGAGAAGGCAACCAAAGTGCAGGACATCAAAAACAACCTGAAA
GAGGCGATTGAAACCATTGTGGCCGCCATGAGCAACCTGGTGCCCCCCGTGGAGCTGGCC
AACCCCGAGAACCAGTTCAGAGTGGACTACATCCTGAGTGTGATGAACGTGCCTGACTTT
GACTTCCCTCCCGAATTCTATGAGCATGCCAAGGCTCTGTGGGAGGATGAAGGAGTGCGT
GCCTGCTACGAACGCTCCAACGAGTACCAGCTGATTGACTGTGCCCAGTACTTCCTGGAC
AAGATCGACGTGATCAAGCAGGCTGACTATGTGCCGAGCGATCAGGACCTGCTTCGCTGC
CGTGTCCTGACTTCTGGAATCTTTGAGACCAAGTTCCAGGTGGACAAAGTCAACTTCCAC
ATGTTTGACGTGGGTGGCCAGCGCGATGAACGCCGCAAGTGGATCCAGTGCTTCAACGAT
GTGACTGCCATCATCTTCGTGGTGGCCAGCAGCAGCTACAACATGGTCATCCGGGAGGAC
AACCAGACCAACCGCCTGCAGGAGGCTCTGAACCTCTTCAAGAGCATCTGGAACAACAGA
TGGCTGCGCACCATCTCTGTGATCCTGTTCCTCAACAAGCAAGATCTGCTCGCTGAGAAA
GTCCTTGCTGGGAAATCGAAGATTGAGGACTACTTTCCAGAATTTGCTCGCTACACTACT
CCTGAGGATGCTACTCCCGAGCCCGGAGAGGACCCACGCGTGACCCGGGCCAAGTACTTC
ATTCGAGATGAGTTTCTGAGGATCAGCACTGCCAGTGGAGATGGGCGTCACTACTGCTAC
CCTCATTTCACCTGCGCTGTGGACACTGAGAACATCCGCCGTGTGTTCAACGACTGCCGT
GACATCATTCAGCGCATGCACCTTCGTCAGTACGAGCTGCTCTAA
Enzyme 41 GenBank Gene ID X04408 Link Image
Enzyme 41 GeneCard ID GNAS Link Image
Enzyme 41 GenAtlas ID GNAS Link Image
Enzyme 41 HGNC ID HGNC:4392 Link Image
Enzyme 41 Chromosome Location 2
Enzyme 41 Locus 20q13.3
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Mattera R, Codina J, Crozat A, Kidd V, Woo SL, Birnbaumer L: Identification by molecular cloning of two forms of the alpha-subunit of the human liver stimulatory (GS) regulatory component of adenylyl cyclase. FEBS Lett. 1986 Sep 29;206(1):36-42. [PubMed Link Image]
  2. Harris BA: Complete cDNA sequence of a human stimulatory GTP-binding protein alpha subunit. Nucleic Acids Res. 1988 Apr 25;16(8):3585. [PubMed Link Image]
  3. Kozasa T, Itoh H, Tsukamoto T, Kaziro Y: Isolation and characterization of the human Gs alpha gene. Proc Natl Acad Sci U S A. 1988 Apr;85(7):2081-5. [PubMed Link Image]
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Bray P, Carter A, Simons C, Guo V, Puckett C, Kamholz J, Spiegel A, Nirenberg M: Human cDNA clones for four species of G alpha s signal transduction protein. Proc Natl Acad Sci U S A. 1986 Dec;83(23):8893-7. [PubMed Link Image]
  7. Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed Link Image]
  8. Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. Epub 2008 Sep 10. [PubMed Link Image]
  9. Miric A, Vechio JD, Levine MA: Heterogeneous mutations in the gene encoding the alpha-subunit of the stimulatory G protein of adenylyl cyclase in Albright hereditary osteodystrophy. J Clin Endocrinol Metab. 1993 Jun;76(6):1560-8. [PubMed Link Image]
  10. Schwindinger WF, Francomano CA, Levine MA: Identification of a mutation in the gene encoding the alpha subunit of the stimulatory G protein of adenylyl cyclase in McCune-Albright syndrome. Proc Natl Acad Sci U S A. 1992 Jun 1;89(11):5152-6. [PubMed Link Image]
  11. Weinstein LS, Shenker A, Gejman PV, Merino MJ, Friedman E, Spiegel AM: Activating mutations of the stimulatory G protein in the McCune-Albright syndrome. N Engl J Med. 1991 Dec 12;325(24):1688-95. [PubMed Link Image]
  12. Landis CA, Masters SB, Spada A, Pace AM, Bourne HR, Vallar L: GTPase inhibiting mutations activate the alpha chain of Gs and stimulate adenylyl cyclase in human pituitary tumours. Nature. 1989 Aug 31;340(6236):692-6. [PubMed Link Image]
  13. Schwindinger WF, Miric A, Zimmerman D, Levine MA: A novel Gs alpha mutant in a patient with Albright hereditary osteodystrophy uncouples cell surface receptors from adenylyl cyclase. J Biol Chem. 1994 Oct 14;269(41):25387-91. [PubMed Link Image]
  14. Iiri T, Herzmark P, Nakamoto JM, van Dop C, Bourne HR: Rapid GDP release from Gs alpha in patients with gain and loss of endocrine function. Nature. 1994 Sep 8;371(6493):164-8. [PubMed Link Image]
  15. Gorelov VN, Dumon K, Barteneva NS, Palm D, Roher HD, Goretzki PE: Overexpression of Gs alpha subunit in thyroid tumors bearing a mutated Gs alpha gene. J Cancer Res Clin Oncol. 1995;121(4):219-24. [PubMed Link Image]
  16. Williamson EA, Ince PG, Harrison D, Kendall-Taylor P, Harris PE: G-protein mutations in human pituitary adrenocorticotrophic hormone-secreting adenomas. Eur J Clin Invest. 1995 Feb;25(2):128-31. [PubMed Link Image]
  17. Yang I, Park S, Ryu M, Woo J, Kim S, Kim J, Kim Y, Choi Y: Characteristics of gsp-positive growth hormone-secreting pituitary tumors in Korean acromegalic patients. Eur J Endocrinol. 1996 Jun;134(6):720-6. [PubMed Link Image]
  18. Farfel Z, Iiri T, Shapira H, Roitman A, Mouallem M, Bourne HR: Pseudohypoparathyroidism, a novel mutation in the betagamma-contact region of Gsalpha impairs receptor stimulation. J Biol Chem. 1996 Aug 16;271(33):19653-5. [PubMed Link Image]
  19. Candeliere GA, Roughley PJ, Glorieux FH: Polymerase chain reaction-based technique for the selective enrichment and analysis of mosaic arg201 mutations in G alpha s from patients with fibrous dysplasia of bone. Bone. 1997 Aug;21(2):201-6. [PubMed Link Image]
  20. Warner DR, Gejman PV, Collins RM, Weinstein LS: A novel mutation adjacent to the switch III domain of G(S alpha) in a patient with pseudohypoparathyroidism. Mol Endocrinol. 1997 Oct;11(11):1718-27. [PubMed Link Image]
  21. Iiri T, Farfel Z, Bourne HR: Conditional activation defect of a human Gsalpha mutant. Proc Natl Acad Sci U S A. 1997 May 27;94(11):5656-61. [PubMed Link Image]
  22. Warner DR, Weng G, Yu S, Matalon R, Weinstein LS: A novel mutation in the switch 3 region of Gsalpha in a patient with Albright hereditary osteodystrophy impairs GDP binding and receptor activation. J Biol Chem. 1998 Sep 11;273(37):23976-83. [PubMed Link Image]
  23. Riminucci M, Fisher LW, Majolagbe A, Corsi A, Lala R, De Sanctis C, Robey PG, Bianco P: A novel GNAS1 mutation, R201G, in McCune-albright syndrome. J Bone Miner Res. 1999 Nov;14(11):1987-9. [PubMed Link Image]
  24. Warner DR, Weinstein LS: A mutation in the heterotrimeric stimulatory guanine nucleotide binding protein alpha-subunit with impaired receptor-mediated activation because of elevated GTPase activity. Proc Natl Acad Sci U S A. 1999 Apr 13;96(8):4268-72. [PubMed Link Image]
  25. Liu J, Litman D, Rosenberg MJ, Yu S, Biesecker LG, Weinstein LS: A GNAS1 imprinting defect in pseudohypoparathyroidism type IB. J Clin Invest. 2000 Nov;106(9):1167-74. [PubMed Link Image]
  26. Bastepe M, Lane AH, Juppner H: Paternal uniparental isodisomy of chromosome 20q--and the resulting changes in GNAS1 methylation--as a plausible cause of pseudohypoparathyroidism. Am J Hum Genet. 2001 May;68(5):1283-9. Epub 2001 Apr 9. [PubMed Link Image]
  27. Wu WI, Schwindinger WF, Aparicio LF, Levine MA: Selective resistance to parathyroid hormone caused by a novel uncoupling mutation in the carboxyl terminus of G alpha(s). A cause of pseudohypoparathyroidism type Ib. J Biol Chem. 2001 Jan 5;276(1):165-71. [PubMed Link Image]
  28. Ishikawa Y, Tajima T, Nakae J, Nagashima T, Satoh K, Okuhara K, Fujieda K: Two mutations of the Gsalpha gene in two Japanese patients with sporadic pseudohypoparathyroidism type Ia. J Hum Genet. 2001;46(7):426-30. [PubMed Link Image]
  29. Ahrens W, Hiort O, Staedt P, Kirschner T, Marschke C, Kruse K: Analysis of the GNAS1 gene in Albright's hereditary osteodystrophy. J Clin Endocrinol Metab. 2001 Oct;86(10):4630-4. [PubMed Link Image]
  30. Linglart A, Carel JC, Garabedian M, Le T, Mallet E, Kottler ML: GNAS1 lesions in pseudohypoparathyroidism Ia and Ic: genotype phenotype relationship and evidence of the maternal transmission of the hormonal resistance. J Clin Endocrinol Metab. 2002 Jan;87(1):189-97. [PubMed Link Image]
  31. Lim SH, Poh LK, Cowell CT, Tey BH, Loke KY: Mutational analysis of the GNAS1 exons encoding the stimulatory G protein in five patients with pseudohypoparathyroidism type 1a. J Pediatr Endocrinol Metab. 2002 Mar;15(3):259-68. [PubMed Link Image]
  32. Jan de Beur S, Ding C, Germain-Lee E, Cho J, Maret A, Levine MA: Discordance between genetic and epigenetic defects in pseudohypoparathyroidism type 1b revealed by inconsistent loss of maternal imprinting at GNAS1. Am J Hum Genet. 2003 Aug;73(2):314-22. Epub 2003 Jul 11. [PubMed Link Image]
  33. Rickard SJ, Wilson LC: Analysis of GNAS1 and overlapping transcripts identifies the parental origin of mutations in patients with sporadic Albright hereditary osteodystrophy and reveals a model system in which to observe the effects of splicing mutations on translated and untranslated messenger RNA. Am J Hum Genet. 2003 Apr;72(4):961-74. Epub 2003 Mar 6. [PubMed Link Image]
  34. Pohlenz J, Ahrens W, Hiort O: A new heterozygous mutation (L338N) in the human Gsalpha (GNAS1) gene as a cause for congenital hypothyroidism in Albright's hereditary osteodystrophy. Eur J Endocrinol. 2003 Apr;148(4):463-8. [PubMed Link Image]
  35. Fragoso MC, Domenice S, Latronico AC, Martin RM, Pereira MA, Zerbini MC, Lucon AM, Mendonca BB: Cushing's syndrome secondary to adrenocorticotropin-independent macronodular adrenocortical hyperplasia due to activating mutations of GNAS1 gene. J Clin Endocrinol Metab. 2003 May;88(5):2147-51. [PubMed Link Image]
  36. Bastepe M, Frohlich LF, Hendy GN, Indridason OS, Josse RG, Koshiyama H, Korkko J, Nakamoto JM, Rosenbloom AL, Slyper AH, Sugimoto T, Tsatsoulis A, Crawford JD, Juppner H: Autosomal dominant pseudohypoparathyroidism type Ib is associated with a heterozygous microdeletion that likely disrupts a putative imprinting control element of GNAS. J Clin Invest. 2003 Oct;112(8):1255-63. [PubMed Link Image]
  37. Chan I, Hamada T, Hardman C, McGrath JA, Child FJ: Progressive osseous heteroplasia resulting from a new mutation in the GNAS1 gene. Clin Exp Dermatol. 2004 Jan;29(1):77-80. [PubMed Link Image]
  38. Linglart A, Gensure RC, Olney RC, Juppner H, Bastepe M: A novel STX16 deletion in autosomal dominant pseudohypoparathyroidism type Ib redefines the boundaries of a cis-acting imprinting control element of GNAS. Am J Hum Genet. 2005 May;76(5):804-14. Epub 2005 Mar 30. [PubMed Link Image]
  39. Riepe FG, Ahrens W, Krone N, Folster-Holst R, Brasch J, Sippell WG, Hiort O, Partsch CJ: Early manifestation of calcinosis cutis in pseudohypoparathyroidism type Ia associated with a novel mutation in the GNAS gene. Eur J Endocrinol. 2005 Apr;152(4):515-9. [PubMed Link Image]
  40. Bastepe M, Frohlich LF, Linglart A, Abu-Zahra HS, Tojo K, Ward LM, Juppner H: Deletion of the NESP55 differentially methylated region causes loss of maternal GNAS imprints and pseudohypoparathyroidism type Ib. Nat Genet. 2005 Jan;37(1):25-7. Epub 2004 Dec 12. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 7135
Enzyme 42 Name Rab GDP dissociation inhibitor alpha
Enzyme 42 Synonyms
  1. Rab GDI alpha
  2. Guanosine diphosphate dissociation inhibitor 1
  3. GDI-1
  4. Oligophrenin-2
  5. Protein XAP-4
Enzyme 42 Gene Name GDI1
Enzyme 42 Protein Sequence >Rab GDP dissociation inhibitor alpha
MDEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDRNPYYGGESSSITPLEELYKRFQLLE
GPPESMGRGRDWNVDLIPKFLMANGQLVKMLLYTEVTRYLDFKVVEGSFVYKGGKIYKVP
STETEALASNLMGMFEKRRFRKFLVFVANFDENDPKTFEGVDPQTTSMRDVYRKFDLGQD
VIDFTGHALALYRTDDYLDQPCLETVNRIKLYSESLARYGKSPYLYPLYGLGELPQGFAR
LSAIYGGTYMLNKPVDDIIMENGKVVGVKSEGEVARCKQLICDPSYIPDRVRKAGQVIRI
ICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISYAHNVAAQGKYIAIASTTVETT
DPEKEVEPALELLEPIDQKFVAISDLYEPIDDGCESQVFCSCSYDATTHFETTCNDIKDI
YKRMAGTAFDFENMKRKQNDVFGEAEQ
Enzyme 42 Number of Residues 447
Enzyme 42 Molecular Weight 50582.3
Enzyme 42 Theoretical pI 4.75
Enzyme 42 GO Classification
Function
  • GDP-dissociation inhibitor activity
  • GTPase regulator activity
  • Rab GDP-dissociation inhibitor activity
  • enzyme regulator activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
  • biological regulation
  • establishment of localization
  • protein transport
  • regulation of GTP catabolic process
  • regulation of GTPase activity
  • regulation of biological process
  • regulation of cellular metabolic process
  • regulation of metabolic process
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • regulation of nucleotide catabolic process
  • regulation of nucleotide metabolic process
  • regulation of purine nucleotide catabolic process
  • transport
Component
Enzyme 42 General Function Involved in regulation of GTPase activity
Enzyme 42 Specific Function Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions Not Available
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 695585 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID P31150 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name GDIA_HUMAN Link Image
Enzyme 42 PDB ID 1GND Link Image
Enzyme 42 PDB File Show
Enzyme 42 3D Structure
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >1344 bp
ATGGACGAGGAATACGATGTGATCGTGCTGGGGACCGGTCTCACCGAATGCATCCTGTCG
GGCATCATGTCTGTGAACGGGAAGAAGGTGCTGCACATGGACCGGAACCCCTACTACGGG
GGCGAGAGCTCCTCCATCACACCCCTGGAGGAGCTGTATAAGCGTTTTCAGTTGCTGGAG
GGGCCCCCTGAGTCGATGGGCCGAGGCCGAGACTGGAATGTTGACCTGATTCCCAAATTC
CTCATGGCTAACGGGCAGCTGGTAAAGATGCTACTGTATACAGAGGTGACTCGCTACCTG
GACTTCAAGGTGGTGGAGGGCAGCTTTGTCTACAAGGGGGGCAAGATCTACAAAGTGCCG
TCCACTGAGACTGAGGCCTTGGCTTCCAATCTGATGGGCATGTTTGAGAAACGGCGCTTC
CGCAAGTTCCTGGTGTTTGTGGCAAACTTCGATGAGAATGACCCCAAGACCTTTGAGGGC
GTTGACCCCCAGACTACCAGCATGCGTGACGTCTACCGGAAGTTTGATCTGGGCCAGGAT
GTCATCGATTTCACTGGCCATGCCCTGGCGCTCTACCGCACTGATGACTACCTGGACCAG
CCCTGCCTTGAGACCGTCAACCGCATCAAGTTGTACAGTGAGTCCCTGGCCCGGTATGGC
AAGAGCCCATATTTATACCCGCTCTACGGCTTGGGCGAGCTGCCCCAGGGTTTTGCAAGA
TTGAGTGCCATCTATGGGGGGACATATATGCTGAACAAACCTGTGGATGACATCATCATG
GAGAACGGCAAGGTGGTGGGCGTGAAGTCTGAGGGAGAGGTGGCCCGCTGCAAGCAGCTG
ATCTGTGACCCCAGCTACATCCCGGACCGTGTGCGGAAGGCTGGCCAGGTTATCCGCATC
ATCTGTATCCTTAGCCACCCCATCAAGAACACCAACGACGCCAACTCCTGCCAAATAATC
ATCCCCCAGAACCAGGTCAACAGGAAGTCAGACATCTACGTGTGCATGATCTCCTATGCA
CACAACGTGGCGGCCCAGGGCAAGTACATAGCTATTGCCAGCACTACTGTGGAGACCACG
GACCCTGAAAAGGAGGTGGAGCCGGCTCTGGAGCTGTTGGAGCCCATTGACCAGAAGTTT
GTGGCTATCAGTGACTTGTATGAGCCCATTGATGATGGTTGTGAGAGCCAGGTGTTCTGT
TCCTGCTCCTACGATGCCACCACACACTTTGAGACAACCTGCAACGACATCAAAGACATC
TACAAACGCATGGCTGGCACGGCCTTTGACTTTGAGAACATGAAGCGCAAACAGAACGAC
GTCTTTGGAGAAGCTGAGCAGTGA
Enzyme 42 GenBank Gene ID X79353 Link Image
Enzyme 42 GeneCard ID GDI1 Link Image
Enzyme 42 GenAtlas ID GDI1 Link Image
Enzyme 42 HGNC ID HGNC:4226 Link Image
Enzyme 42 Chromosome Location Not Available
Enzyme 42 Locus Not Available
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Sedlacek Z, Konecki DS, Korn B, Klauck SM, Poustka A: Evolutionary conservation and genomic organization of XAP-4, an Xq28 located gene coding for a human rab GDP-dissociation inhibitor (GDI). Mamm Genome. 1994 Oct;5(10):633-9. [PubMed Link Image]
  2. Nishimura N, Goji J, Nakamura H, Orita S, Takai Y, Sano K: Cloning of a brain-type isoform of human Rab GDI and its expression in human neuroblastoma cell lines and tumor specimens. Cancer Res. 1995 Nov 15;55(22):5445-50. [PubMed Link Image]
  3. Chen EY, Zollo M, Mazzarella R, Ciccodicola A, Chen CN, Zuo L, Heiner C, Burough F, Repetto M, Schlessinger D, D'Urso M: Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci. Hum Mol Genet. 1996 May;5(5):659-68. [PubMed Link Image]
  4. Kitano T, Schwarz C, Nickel B, Paabo S: Gene diversity patterns at 10 X-chromosomal loci in humans and chimpanzees. Mol Biol Evol. 2003 Aug;20(8):1281-9. Epub 2003 May 30. [PubMed Link Image]
  5. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. Electrophoresis. 1992 Dec;13(12):960-9. [PubMed Link Image]
  8. Bachner D, Sedlacek Z, Korn B, Hameister H, Poustka A: Expression patterns of two human genes coding for different rab GDP-dissociation inhibitors (GDIs), extremely conserved proteins involved in cellular transport. Hum Mol Genet. 1995 Apr;4(4):701-8. [PubMed Link Image]
  9. Li X, Bu X, Lu B, Avraham H, Flavell RA, Lim B: The hematopoiesis-specific GTP-binding protein RhoH is GTPase deficient and modulates activities of other Rho GTPases by an inhibitory function. Mol Cell Biol. 2002 Feb;22(4):1158-71. [PubMed Link Image]
  10. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  11. D'Adamo P, Menegon A, Lo Nigro C, Grasso M, Gulisano M, Tamanini F, Bienvenu T, Gedeon AK, Oostra B, Wu SK, Tandon A, Valtorta F, Balch WE, Chelly J, Toniolo D: Mutations in GDI1 are responsible for X-linked non-specific mental retardation. Nat Genet. 1998 Jun;19(2):134-9. [PubMed Link Image]
  12. Bienvenu T, des Portes V, Saint Martin A, McDonell N, Billuart P, Carrie A, Vinet MC, Couvert P, Toniolo D, Ropers HH, Moraine C, van Bokhoven H, Fryns JP, Kahn A, Beldjord C, Chelly J: Non-specific X-linked semidominant mental retardation by mutations in a Rab GDP-dissociation inhibitor. Hum Mol Genet. 1998 Aug;7(8):1311-5. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 7136
Enzyme 43 Name Proto-oncogene DBL
Enzyme 43 Synonyms
  1. Proto-oncogene MCF-2
  2. MCF2-transforming protein
  3. DBL-transforming protein
Enzyme 43 Gene Name MCF2
Enzyme 43 Protein Sequence >Proto-oncogene DBL
MAEANPRRGKMRFRRNAASFPGNLHLVLVLRPTSFLQRTFTDIGFWFSQEDFMLKLPVVM
LSSVSDLLTYIDDKQLTPELGGTLQYCHSEWIIFRNAIENFALTVKEMAQMLQSFGTELA
ETELPDDIPSIEEILAIRAERYHLLKNDITAVTKEGKILLTNLEVPDTEGAVSSRLECHR
QISGDWQTINKLLTQVHDMETAFDGFWEKHQLKMEQYLQLWKFEQDFQQLVTEVEFLLNQ
QAELADVTGTIAQVKQKIKKLENLDENSQELLSKAQFVILHGHKLAANHHYALDLICQRC
NELRYLSDILVNEIKAKRIQLSRTFKMHKLLQQARQCCDEGECLLANQEIDKFQSKEDAQ
KALQDIENFLEMALPFINYEPETLQYEFDVILSPELKVQMKTIQLKLENIRSIFENQQAG
FRNLADKHVRPIQFVVPTPENLVTSGTPFFSSKQGKKTWRQNQSNLKIEVVPDCQEKRSS
GPSSSLDNGNSLDVLKNHVLNELIQTERVYVRELYTVLLGYRAEMDNPEMFDLMPPLLRN
KKDILFGNMAEIYEFHNDIFLSSLENCAHAPERVGPCFLERKDDFQMYAKYCQNKPRSET
IWRKYSECAFFQECQRKLKHRLRLDSYLLKPVQRITKYQLLLKELLKYSKDCEGSALLKK
ALDAMLDLLKSVNDSMHQIAINGYIGNLNELGKMIMQGGFSVWIGHKKGATKMKDLARFK
PMQRHLFLYEKAIVFCKRRVESGEGSDRYPSYSFKHCWKMDEVGITEYVKGDNRKFEIWY
GEKEEVYIVQASNVDVKMTWLKEIRNILLKQQELLTVKKRKQQDQLTERDKFQISLQQND
EKQQGAFISTEETELEHTSTVVEVCEAIASVQAEANTVWTEASQSAEISEEPAEWSSNYF
YPTYDENEEENRPLMRPVSEMALLY
Enzyme 43 Number of Residues 925
Enzyme 43 Molecular Weight 107672.4
Enzyme 43 Theoretical pI 5.87
Enzyme 43 GO Classification
Function
  • GTPase regulator activity
  • Ras guanyl-nucleotide exchange factor activity
  • Rho guanyl-nucleotide exchange factor activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
  • biological regulation
  • intracellular signaling pathway
  • regulation of Ras protein signal transduction
  • regulation of Rho protein signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signaling
  • signaling pathway
Component
  • cell part
  • intracellular
Enzyme 43 General Function Involved in protein binding
Enzyme 43 Specific Function Guanine nucleotide exchange factor (GEF) that modulates the Rho family of GTPases. Promotes the conversion of some member of the Rho family GTPase from the GDP-bound to the GTP-bound form. Isoform 1 exhibits no activity toward RHOA, RAC1 or CDC42. Isoform 2 exhibits decreased GEF activity toward CDC42. Isoform 3 exhibits a weak but significant activity toward RAC1 and CDC42. Isoform 4 exhibits significant activity toward RHOA and CDC42. The truncated DBL oncogene is active toward RHOA, RAC1 and CDC42
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions Not Available
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 153791325 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID P10911 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name MCF2_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >2778 bp
ATGGCAGAAGCAAATCCCCGGAGAGGCAAGATGAGGTTCAGAAGGAATGCGGCTTCCTTC
CCTGGGAACTTGCACTTGGTTTTGGTTTTACGTCCTACCAGCTTTCTTCAACGAACGTTC
ACAGACATTGGATTTTGGTTTAGTCAGGAGGATTTTATGCTTAAATTACCAGTTGTTATG
CTGAGCTCAGTTAGTGATTTGCTGACATACATTGATGACAAGCAATTAACCCCTGAGTTA
GGCGGCACCTTGCAGTACTGCCACAGTGAATGGATCATCTTCAGAAATGCTATAGAAAAT
TTTGCCCTCACAGTGAAAGAAATGGCTCAGATGTTACAGTCCTTTGGAACTGAACTGGCT
GAGACAGAACTACCAGATGATATTCCCTCAATAGAAGAAATTCTGGCAATTCGTGCTGAA
AGGTATCATCTGTTGAAGAATGATATTACAGCTGTAACCAAAGAAGGAAAAATTCTGCTA
ACAAATCTGGAAGTGCCTGACACTGAAGGAGCTGTCAGTTCAAGACTAGAATGTCATCGG
CAAATAAGTGGTGACTGGCAAACTATTAATAAGTTGCTGACTCAAGTACATGATATGGAA
ACAGCTTTTGATGGATTTTGGGAAAAACATCAATTAAAAATGGAGCAGTATCTGCAACTA
TGGAAGTTTGAGCAGGATTTTCAACAGCTTGTGACTGAAGTTGAATTTCTATTAAACCAA
CAAGCAGAACTGGCTGATGTAACAGGGACTATAGCTCAAGTAAAACAAAAAATAAAAAAA
TTGGAAAACTTAGATGAAAATTCTCAGGAGCTATTATCAAAGGCCCAGTTTGTGATATTA
CATGGACACAAGCTTGCAGCAAATCACCATTATGCACTTGATTTAATCTGCCAGAGGTGC
AATGAGCTACGTTACCTTTCTGATATTTTGGTTAATGAGATAAAAGCAAAACGGATACAA
CTCAGCAGGACCTTCAAAATGCATAAACTCCTACAGCAGGCTCGTCAATGCTGTGATGAA
GGGGAATGTCTTCTAGCTAATCAGGAAATAGATAAGTTTCAGTCTAAAGAAGATGCTCAG
AAAGCTCTCCAAGACATTGAAAATTTTCTTGAAATGGCTCTACCCTTTATAAATTATGAA
CCTGAAACACTGCAGTATGAATTTGATGTAATATTATCTCCTGAGCTTAAGGTTCAAATG
AAGACTATACAACTCAAGCTTGAAAACATTCGAAGTATATTTGAGAACCAGCAGGCTGGT
TTCAGGAACCTGGCAGATAAGCATGTGAGGCCAATCCAATTTGTGGTACCCACACCTGAA
AATTTGGTCACATCTGGGACACCATTTTTTTCATCTAAACAAGGGAAGAAGACTTGGAGA
CAAAATCAGAGCAACTTAAAAATTGAAGTGGTGCCTGATTGTCAGGAGAAGAGAAGTTCT
GGTCCATCCTCCAGTTTGGACAATGGCAATAGCTTGGATGTTTTAAAGAACCACGTACTA
AATGAACTGATACAGACTGAGAGAGTTTATGTTCGAGAACTGTATACTGTTTTGTTGGGT
TATAGAGCGGAGATGGATAATCCAGAGATGTTTGATCTTATGCCACCTCTCCTGAGAAAT
AAAAAGGACATTCTCTTTGGAAACATGGCAGAAATATATGAATTCCATAACGACATTTTC
TTGAGCAGCCTGGAAAATTGTGCTCATGCTCCAGAAAGAGTGGGACCTTGTTTCCTGGAA
AGGAAGGATGATTTTCAGATGTATGCAAAATATTGTCAGAATAAGCCCAGATCAGAAACA
ATTTGGAGGAAGTATTCAGAATGCGCATTTTTCCAGGAATGTCAAAGAAAGTTAAAACAC
AGACTTAGACTGGATTCCTATTTACTCAAACCAGTGCAACGAATCACTAAATATCAGTTA
TTGTTGAAGGAGCTATTAAAATATAGCAAAGACTGTGAAGGATCTGCTCTGTTGAAGAAG
GCACTCGATGCAATGCTGGATTTACTGAAGTCAGTTAATGATTCTATGCATCAGATTGCA
ATAAATGGCTATATTGGAAACTTAAATGAACTGGGCAAGATGATAATGCAAGGTGGATTC
AGCGTTTGGATAGGGCACAAGAAAGGTGCTACAAAAATGAAGGATTTGGCTAGATTCAAA
CCAATGCAGCGACACCTTTTCTTGTATGAAAAAGCCATTGTTTTTTGCAAAAGGCGTGTT
GAAAGTGGAGAAGGCTCTGACAGATACCCGTCATACAGTTTTAAACACTGTTGGAAAATG
GATGAAGTTGGAATCACTGAATATGTAAAAGGTGATAACCGCAAGTTTGAAATCTGGTAT
GGTGAAAAGGAAGAAGTTTATATTGTCCAGGCTTCTAATGTAGATGTGAAGATGACGTGG
CTAAAAGAAATAAGAAATATTTTGTTGAAGCAGCAGGAACTTTTGACAGTTAAAAAAAGA
AAGCAACAGGATCAATTAACAGAACGGGATAAGTTTCAGATTTCTCTTCAGCAGAATGAT
GAAAAGCAACAGGGAGCTTTTATAAGTACTGAGGAAACTGAATTGGAACACACCAGCACT
GTGGTGGAGGTCTGTGAGGCAATTGCGTCAGTTCAGGCAGAAGCAAATACAGTTTGGACT
GAGGCATCACAATCTGCAGAAATCTCTGAAGAACCTGCGGAATGGTCAAGCAACTATTTC
TACCCTACTTATGATGAAAATGAAGAAGAAAATAGGCCCCTCATGAGACCTGTGTCGGAG
ATGGCTCTCCTATATTGA
Enzyme 43 GenBank Gene ID NM_005369.4 Link Image
Enzyme 43 GeneCard ID MCF2 Link Image
Enzyme 43 GenAtlas ID Not Available
Enzyme 43 HGNC ID Not Available
Enzyme 43 Chromosome Location Not Available
Enzyme 43 Locus Not Available
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Ron D, Tronick SR, Aaronson SA, Eva A: Molecular cloning and characterization of the human dbl proto-oncogene: evidence that its overexpression is sufficient to transform NIH/3T3 cells. EMBO J. 1988 Aug;7(8):2465-73. [PubMed Link Image]
  2. Komai K, Okayama R, Kitagawa M, Yagi H, Chihara K, Shiozawa S: Alternative splicing variants of the human DBL (MCF-2) proto-oncogene. Biochem Biophys Res Commun. 2002 Dec 6;299(3):455-8. [PubMed Link Image]
  3. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  4. Eva A, Vecchio G, Rao CD, Tronick SR, Aaronson SA: The predicted DBL oncogene product defines a distinct class of transforming proteins. Proc Natl Acad Sci U S A. 1988 Apr;85(7):2061-5. [PubMed Link Image]
  5. Noguchi T, Galland F, Batoz M, Mattei MG, Birnbaum D: Activation of a mcf.2 oncogene by deletion of amino-terminal coding sequences. Oncogene. 1988 Dec;3(6):709-15. [PubMed Link Image]
  6. Ron D, Zannini M, Lewis M, Wickner RB, Hunt LT, Graziani G, Tronick SR, Aaronson SA, Eva A: A region of proto-dbl essential for its transforming activity shows sequence similarity to a yeast cell cycle gene, CDC24, and the human breakpoint cluster gene, bcr. New Biol. 1991 Apr;3(4):372-9. [PubMed Link Image]
  7. Hart MJ, Eva A, Zangrilli D, Aaronson SA, Evans T, Cerione RA, Zheng Y: Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product. J Biol Chem. 1994 Jan 7;269(1):62-5. [PubMed Link Image]
  8. Ueda S, Kataoka T, Satoh T: Role of the Sec14-like domain of Dbl family exchange factors in the regulation of Rho family GTPases in different subcellular sites. Cell Signal. 2004 Aug;16(8):899-906. [PubMed Link Image]
  9. Kostenko EV, Olabisi OO, Sahay S, Rodriguez PL, Whitehead IP: Ccpg1, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs. Mol Cell Biol. 2006 Dec;26(23):8964-75. Epub 2006 Sep 25. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 7137
Enzyme 44 Name Cell division control protein 42 homolog
Enzyme 44 Synonyms
  1. G25K GTP-binding protein
Enzyme 44 Gene Name CDC42
Enzyme 44 Protein Sequence >Cell division control protein 42 homolog
MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAG
QEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLR
DDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQRGLKNVFDEAILAALEPP
ETQPKRKCCIF
Enzyme 44 Number of Residues 191
Enzyme 44 Molecular Weight 21310.4
Enzyme 44 Theoretical pI 5.83
Enzyme 44 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 44 General Function Involved in GTP binding
Enzyme 44 Specific Function Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Causes the formation of thin, actin-rich surface projections called filopodia
Enzyme 44 Pathways Not Available
Enzyme 44 Reactions Not Available
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 182857 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID P60953 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name CDC42_HUMAN Link Image
Enzyme 44 PDB ID 1GRN Link Image
Enzyme 44 PDB File Show
Enzyme 44 3D Structure
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence >576 bp
ATGCAGACAATTAAGTGTGTTGTTGTGGGCGATGGTGCTGTTGGTAAAACATGTCTCCTG
ATATCCTACACAACAAACAAATTTCCATCGGAATATGTACCGACTGTTTTTGACAACTAT
GCAGTCACAGTTATGATTGGTGGAGAACCATATACTCTTGGACTTTTTGATACTGCAGGG
CAAGAGGATTATGACAGATTACGACCGCTGAGTTATCCACAAACAGATGTATTTCTAGTC
TGTTTTTCAGTGGTCTCTCCATCTTCATTTGAAAACGTGAAAGAAAAGTGGGTGCCTGAG
ATAACTCACCACTGTCCAAAGACTCCTTTCTTGCTTGTTGGGACTCAAATTGATCTCAGA
GATGACCCCTCTACTATTGAGAAACTTGCCAAGAACAAACAGAAGCCTATCACTCCAGAG
ACTGCTGAAAAGCTGGCCCGTGACCTGAAGGCTGTCAAGTATGTGGAGTGTTCTGCACTT
ACACAGAGAGGTCTGAAGAATGTGTTTGATGAGGCTATCCTAGCTGCCCTCGAGCCTCCG
GAAACTCAACCCAAAAGGAAGTGCTGTATATTCTAA
Enzyme 44 GenBank Gene ID M35543 Link Image
Enzyme 44 GeneCard ID CDC42 Link Image
Enzyme 44 GenAtlas ID CDC42 Link Image
Enzyme 44 HGNC ID HGNC:1736 Link Image
Enzyme 44 Chromosome Location 1
Enzyme 44 Locus 1p36.1
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References
  1. Munemitsu S, Innis MA, Clark R, McCormick F, Ullrich A, Polakis P: Molecular cloning and expression of a G25K cDNA, the human homolog of the yeast cell cycle gene CDC42. Mol Cell Biol. 1990 Nov;10(11):5977-82. [PubMed Link Image]
  2. Shinjo K, Koland JG, Hart MJ, Narasimhan V, Johnson DI, Evans T, Cerione RA: Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42. Proc Natl Acad Sci U S A. 1990 Dec;87(24):9853-7. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Kwong CH, Malech HL, Rotrosen D, Leto TL: Regulation of the human neutrophil NADPH oxidase by rho-related G-proteins. Biochemistry. 1993 Jun 1;32(21):5711-7. [PubMed Link Image]
  6. Polakis PG, Snyderman R, Evans T: Characterization of G25K, a GTP-binding protein containing a novel putative nucleotide binding domain. Biochem Biophys Res Commun. 1989 Apr 14;160(1):25-32. [PubMed Link Image]
  7. Yamane HK, Farnsworth CC, Xie HY, Evans T, Howald WN, Gelb MH, Glomset JA, Clarke S, Fung BK: Membrane-binding domain of the small G protein G25K contains an S-(all-trans-geranylgeranyl)cysteine methyl ester at its carboxyl terminus. Proc Natl Acad Sci U S A. 1991 Jan 1;88(1):286-90. [PubMed Link Image]
  8. Joberty G, Perlungher RR, Macara IG: The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins. Mol Cell Biol. 1999 Oct;19(10):6585-97. [PubMed Link Image]
  9. Eisenmann KM, McCarthy JB, Simpson MA, Keely PJ, Guan JL, Tachibana K, Lim L, Manser E, Furcht LT, Iida J: Melanoma chondroitin sulphate proteoglycan regulates cell spreading through Cdc42, Ack-1 and p130cas. Nat Cell Biol. 1999 Dec;1(8):507-13. [PubMed Link Image]
  10. Pirone DM, Fukuhara S, Gutkind JS, Burbelo PD: SPECs, small binding proteins for Cdc42. J Biol Chem. 2000 Jul 28;275(30):22650-6. [PubMed Link Image]
  11. Johansson A, Driessens M, Aspenstrom P: The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1. J Cell Sci. 2000 Sep;113 ( Pt 18):3267-75. [PubMed Link Image]
  12. Miki H, Yamaguchi H, Suetsugu S, Takenawa T: IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature. 2000 Dec 7;408(6813):732-5. [PubMed Link Image]
  13. Noda Y, Takeya R, Ohno S, Naito S, Ito T, Sumimoto H: Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C. Genes Cells. 2001 Feb;6(2):107-19. [PubMed Link Image]
  14. Meller N, Irani-Tehrani M, Kiosses WB, Del Pozo MA, Schwartz MA: Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho proteins. Nat Cell Biol. 2002 Sep;4(9):639-47. [PubMed Link Image]
  15. Masuda-Robens JM, Kutney SN, Qi H, Chou MM: The TRE17 oncogene encodes a component of a novel effector pathway for Rho GTPases Cdc42 and Rac1 and stimulates actin remodeling. Mol Cell Biol. 2003 Mar;23(6):2151-61. [PubMed Link Image]
  16. Worby CA, Mattoo S, Kruger RP, Corbeil LB, Koller A, Mendez JC, Zekarias B, Lazar C, Dixon JE: The fic domain: regulation of cell signaling by adenylylation. Mol Cell. 2009 Apr 10;34(1):93-103. [PubMed Link Image]
  17. Yarbrough ML, Li Y, Kinch LN, Grishin NV, Ball HL, Orth K: AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science. 2009 Jan 9;323(5911):269-72. Epub 2008 Nov 27. [PubMed Link Image]
  18. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  19. Feltham JL, Dotsch V, Raza S, Manor D, Cerione RA, Sutcliffe MJ, Wagner G, Oswald RE: Definition of the switch surface in the solution structure of Cdc42Hs. Biochemistry. 1997 Jul 22;36(29):8755-66. [PubMed Link Image]
  20. Guo W, Sutcliffe MJ, Cerione RA, Oswald RE: Identification of the binding surface on Cdc42Hs for p21-activated kinase. Biochemistry. 1998 Oct 6;37(40):14030-7. [PubMed Link Image]
  21. Rittinger K, Walker PA, Eccleston JF, Nurmahomed K, Owen D, Laue E, Gamblin SJ, Smerdon SJ: Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP. Nature. 1997 Aug 14;388(6643):693-7. [PubMed Link Image]
  22. Rudolph MG, Wittinghofer A, Vetter IR: Nucleotide binding to the G12V-mutant of Cdc42 investigated by X-ray diffraction and fluorescence spectroscopy: two different nucleotide states in one crystal. Protein Sci. 1999 Apr;8(4):778-87. [PubMed Link Image]
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 7138
Enzyme 45 Name Rab GDP dissociation inhibitor beta
Enzyme 45 Synonyms
  1. Rab GDI beta
  2. Guanosine diphosphate dissociation inhibitor 2
  3. GDI-2
Enzyme 45 Gene Name GDI2
Enzyme 45 Protein Sequence >Rab GDP dissociation inhibitor beta
MNEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDRNPYYGGESASITPLEDLYKRFKIPG
SPPESMGRGRDWNVDLIPKFLMANGQLVKMLLYTEVTRYLDFKVTEGSFVYKGGKIYKVP
STEAEALASSLMGLFEKRRFRKFLVYVANFDEKDPRTFEGIDPKKTTMRDVYKKFDLGQD
VIDFTGHALALYRTDDYLDQPCYETINRIKLYSESLARYGKSPYLYPLYGLGELPQGFAR
LSAIYGGTYMLNKPIEEIIVQNGKVIGVKSEGEIARCKQLICDPSYVKDRVEKVGQVIRV
ICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISFAHNVAAQGKYIAIVSTTVETK
EPEKEIRPALELLEPIEQKFVSISDLLVPKDLGTESQIFISRTYDATTHFETTCDDIKNI
YKRMTGSEFDFEEMKRKKNDIYGED
Enzyme 45 Number of Residues 445
Enzyme 45 Molecular Weight 50662.8
Enzyme 45 Theoretical pI 6.39
Enzyme 45 GO Classification
Function
  • GDP-dissociation inhibitor activity
  • GTPase regulator activity
  • Rab GDP-dissociation inhibitor activity
  • enzyme regulator activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
  • biological regulation
  • establishment of localization
  • protein transport
  • regulation of GTP catabolic process
  • regulation of GTPase activity
  • regulation of biological process
  • regulation of cellular metabolic process
  • regulation of metabolic process
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • regulation of nucleotide catabolic process
  • regulation of nucleotide metabolic process
  • regulation of purine nucleotide catabolic process
  • transport
Component
Enzyme 45 General Function Involved in regulation of GTPase activity
Enzyme 45 Specific Function Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them
Enzyme 45 Pathways Not Available
Enzyme 45 Reactions Not Available
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 6598323 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID P50395 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name GDIB_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >1338 bp
ATGAATGAGGAGTACGACGTGATCGTGCTGGGCACCGGCCTGACGGAATGTATCCTGTCA
GGTATAATGTCAGTGAATGGCAAGAAAGTTCTTCATATGGATCGAAACCCTTACTACGGA
GGAGAGAGTGCATCTATAACACCATTGGAAGATTTATACAAAAGATTTAAAATACCAGGA
TCACCACCCGAGTCAATGGGGAGAGGAAGAGACTGGAATGTTGACTTGATTCCCAAGTTC
CTTATGGCTAATGGTCAGCTGGTTAAGATGCTGCTTTATACAGAGGTAACTCGCTATCTG
GATTTTAAAGTGACTGAAGGGAGCTTTGTCTATAAGGGTGGAAAAATCTACAAGGTTCCT
TCCACTGAAGCAGAAGCCCTGGCATCTAGCCTAATGGGATTGTTTGAAAAACGTCGCTTC
AGGAAATTCCTAGTGTATGTTGCCAACTTCGATGAAAAAGATCCAAGAACTTTTGAAGGC
ATTGATCCTAAGAAGACCACAATGCGAGATGTGTATAAGAAATTTGATTTGGGTCAAGAC
GTTATAGATTTTACTGGTCATGCTCTTGCACTTTACAGAACTGATGATTACTTAGATCAA
CCGTGTTATGAAACCATTAATAGAATTAAACTTTACAGTGAATCTTTGGCAAGATATGGC
AAAAGCCCATACCTTTATCCACTCTATGGCCTTGGAGAACTGCCCCAAGGATTTGCAAGG
CTAAGTGCTATTTATGGAGGTACCTATATGCTGAATAAACCCATTGAAGAAATCATTGTA
CAGAATGGAAAAGTAATTGGTGTAAAATCTGAAGGAGAAATTGCTCGCTGTAAGCAGCTC
ATCTGTGACCCCAGCTACGTAAAAGATCGGGTAGAAAAAGTGGGCCAGGTGATCAGAGTT
ATTTGCATCCTCAGCCACCCCATCAAGAACACCAATGATGCCAACTCCTGCCAGATCATT
ATTCCACAGAACCAAGTCAATCGAAAGTCAGATATCTACGTCTGCATGATCTCCTTTGCG
CACAATGTAGCAGCACAAGGGAAGTACATTGCTATAGTTAGTACAACTGTGGAAACCAAG
GAGCCTGAGAAGGAAATCAGACCAGCTTTGGAGCTCTTGGAACCAATTGAACAGAAATTT
GTTAGCATCAGTGACCTCCTGGTACCAAAAGACTTGGGAACAGAAAGCCAGATCTTTATT
TCCCGCACATATGATGCCACCACTCATTTTGAGACAACGTGTGATGACATTAAAAACATC
TATAAGAGGATGACAGGATCAGAGTTTGACTTTGAGGAAATGAAGCGCAAGAAGAATGAC
ATCTATGGGGAAGACTAA
Enzyme 45 GenBank Gene ID NM_001494.3 Link Image
Enzyme 45 GeneCard ID GDI2 Link Image
Enzyme 45 GenAtlas ID GDI2 Link Image
Enzyme 45 HGNC ID HGNC:4227 Link Image
Enzyme 45 Chromosome Location 1
Enzyme 45 Locus 10p15
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References
  1. Sedlacek Z, Munstermann E, Mincheva A, Lichter P, Poustka A: The human rab GDI beta gene with long retroposon-rich introns maps to 10p15 and its pseudogene to 7p11-p13. Mamm Genome. 1998 Jan;9(1):78-80. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Caillol N, Pasqualini E, Lloubes R, Lombardo D: Impairment of bile salt-dependent lipase secretion in human pancreatic tumoral SOJ-6 cells. J Cell Biochem. 2000 Sep 14;79(4):628-47. [PubMed Link Image]
  4. Bachner D, Sedlacek Z, Korn B, Hameister H, Poustka A: Expression patterns of two human genes coding for different rab GDP-dissociation inhibitors (GDIs), extremely conserved proteins involved in cellular transport. Hum Mol Genet. 1995 Apr;4(4):701-8. [PubMed Link Image]
  5. Li X, Bu X, Lu B, Avraham H, Flavell RA, Lim B: The hematopoiesis-specific GTP-binding protein RhoH is GTPase deficient and modulates activities of other Rho GTPases by an inhibitory function. Mol Cell Biol. 2002 Feb;22(4):1158-71. [PubMed Link Image]
  6. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 7139
Enzyme 46 Name Rho GDP-dissociation inhibitor 1
Enzyme 46 Synonyms
  1. Rho GDI 1
  2. Rho-GDI alpha
Enzyme 46 Gene Name ARHGDIA
Enzyme 46 Protein Sequence >Rho GDP-dissociation inhibitor 1
MAEQEPTAEQLAQIAAENEEDEHSVNYKPPAQKSIQEIQELDKDDESLRKYKEALLGRVA
VSADPNVPNVVVTGLTLVCSSAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNR
EIVSGMKYIQHTYRKGVKIDKTDYMVGSYGPRAEEYEFLTPVEEAPKGMLARGSYSIKSR
FTDDDKTDHLSWEWNLTIKKDWKD
Enzyme 46 Number of Residues 204
Enzyme 46 Molecular Weight 23206.9
Enzyme 46 Theoretical pI 4.74
Enzyme 46 GO Classification
Function
  • GDP-dissociation inhibitor activity
  • GTPase regulator activity
  • Rho GDP-dissociation inhibitor activity
  • enzyme regulator activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 46 General Function Involved in GTPase activator activity
Enzyme 46 Specific Function Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 20379028 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID P52565 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name GDIR1_HUMAN Link Image
Enzyme 46 PDB ID 1HH4 Link Image
Enzyme 46 PDB File Show
Enzyme 46 3D Structure
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >615 bp
ATGGCTGAGCAGGAGCCCACAGCCGAGCAGCTGGCCCAGATTGCAGCGGAGAACGAGGAG
GATGAGCACTCGGTCAACTACAAGCCCCCGGCCCAGAAGAGCATCCAGGAGATCCAGGAG
CTGGACAAGGACGACGAGAGCCTGCGAAAGTACAAGGAGGCCCTGCTGGGCCGCGTGGCC
GTTTCCGCAGACCCCAACGTCCCCAACGTCGTGGTGACTGGCCTGACCCTGGTGTGCAGC
TCGGCCCCGGGCCCCCTGGAGCTGGACCTGACGGGCGACCTGGAGAGCTTCAAGAAGCAG
TCGTTTGTGCTGAAGGAGGGTGTGGAGTACCGGATAAAAATCTCTTTCCGGGTTAACCGA
GAGATAGTGTCCGGCATGAAGTACATCCAGCATACGTACAGGAAAGGCGTCAAGATTGAC
AAGACTGACTACATGGTAGGCAGCTATGGGCCCCGGGCCGAGGAGTACGAGTTCCTGACC
CCCGTGGAGGAGGCACCCAAGGGTATGCTGGCCCGGGGCAGCTACAGCATCAAGTCCCGC
TTCACAGACGACGACAAGACCGACCACCTGTCCTGGGAGTGGAATCTCACCATCAAGAAG
GACTGGAAGGACTGA
Enzyme 46 GenBank Gene ID AF498926 Link Image
Enzyme 46 GeneCard ID ARHGDIA Link Image
Enzyme 46 GenAtlas ID Not Available
Enzyme 46 HGNC ID Not Available
Enzyme 46 Chromosome Location 1
Enzyme 46 Locus 17q25.3
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Leffers H, Nielsen MS, Andersen AH, Honore B, Madsen P, Vandekerckhove J, Celis JE: Identification of two human Rho GDP dissociation inhibitor proteins whose overexpression leads to disruption of the actin cytoskeleton. Exp Cell Res. 1993 Dec;209(2):165-74. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Kwong CH, Malech HL, Rotrosen D, Leto TL: Regulation of the human neutrophil NADPH oxidase by rho-related G-proteins. Biochemistry. 1993 Jun 1;32(21):5711-7. [PubMed Link Image]
  5. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed Link Image]
  6. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  8. Keep NH, Barnes M, Barsukov I, Badii R, Lian LY, Segal AW, Moody PC, Roberts GC: A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm. Structure. 1997 May 15;5(5):623-33. [PubMed Link Image]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 7140
Enzyme 47 Name Rho GDP-dissociation inhibitor 2
Enzyme 47 Synonyms
  1. Rho GDI 2
  2. Ly-GDI
  3. Rho-GDI beta
Enzyme 47 Gene Name ARHGDIB
Enzyme 47 Protein Sequence >Rho GDP-dissociation inhibitor 2
MTEKAPEPHVEEDDDDELDSKLNYKPPPQKSLKELQEMDKDDESLIKYKKTLLGDGPVVT
DPKAPNVVVTRLTLVCESAPGPITMDLTGDLEALKKETIVLKEGSEYRVKIHFKVNRDIV
SGLKYVQHTYRTGVKVDKATFMVGSYGPRPEEYEFLTPVEEAPKGMLARGTYHNKSFFTD
DDKQDHLSWEWNLSIKKEWTE
Enzyme 47 Number of Residues 201
Enzyme 47 Molecular Weight 22987.9
Enzyme 47 Theoretical pI 4.84
Enzyme 47 GO Classification
Function
  • GDP-dissociation inhibitor activity
  • GTPase regulator activity
  • Rho GDP-dissociation inhibitor activity
  • enzyme regulator activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 47 General Function Involved in GTPase activator activity
Enzyme 47 Specific Function Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them
Enzyme 47 Pathways Not Available
Enzyme 47 Reactions Not Available
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 197692331 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID P52566 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name GDIR2_HUMAN Link Image
Enzyme 47 PDB ID 1DS6 Link Image
Enzyme 47 PDB File Show
Enzyme 47 3D Structure
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence >606 bp
ATGACTGAAAAAGCCCCAGAGCCACATGTGGAGGAGGATGACGATGATGAGCTGGACAGC
AAGCTCAATTATAAGCCTCCACCACAGAAGTCCCTGAAAGAGCTGCAGGAAATGGACAAA
GATGATGAGAGTCTAATTAAGTACAAGAAAACGCTGCTGGGAGATGGTCCTGTGGTGACA
GATCCGAAAGCCCCCAATGTCGTTGTCACCCGGCTCACCCTGGTTTGTGAGAGTGCCCCG
GGACCAATCACCATGGACCTTACTGGAGATCTGGAAGCCCTCAAAAAGGAAACCATTGTG
TTAAAGGAAGGTTCTGAATATAGAGTCAAAATTCACTTCAAAGTGAACAGGGATATTGTG
TCAGGCCTGAAATACGTTCAGCACACCTACAGGACTGGGGTGAAAGTGGATAAAGCAACA
TTTATGGTTGGCAGCTATGGACCTCGGCCTGAGGAGTATGAGTTCCTCACTCCAGTTGAG
GAGGCTCCCAAGGGCATGCTGGCGCGAGGCACGTACCACAACAAGTCCTTCTTCACCGAC
GATGACAAGCAAGACCACCTCAGCTGGGAGTGGAACCTGTCGATTAAGAAGGAGTGGACA
GAATAA
Enzyme 47 GenBank Gene ID AB451315 Link Image
Enzyme 47 GeneCard ID ARHGDIB Link Image
Enzyme 47 GenAtlas ID Not Available
Enzyme 47 HGNC ID Not Available
Enzyme 47 Chromosome Location 1
Enzyme 47 Locus 12p12.3
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References
  1. Scherle P, Behrens T, Staudt LM: Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein, is expressed preferentially in lymphocytes. Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7568-72. [PubMed Link Image]
  2. Leffers H, Nielsen MS, Andersen AH, Honore B, Madsen P, Vandekerckhove J, Celis JE: Identification of two human Rho GDP dissociation inhibitor proteins whose overexpression leads to disruption of the actin cytoskeleton. Exp Cell Res. 1993 Dec;209(2):165-74. [PubMed Link Image]
  3. Lelias JM, Adra CN, Wulf GM, Guillemot JC, Khagad M, Caput D, Lim B: cDNA cloning of a human mRNA preferentially expressed in hematopoietic cells and with homology to a GDP-dissociation inhibitor for the rho GTP-binding proteins. Proc Natl Acad Sci U S A. 1993 Feb 15;90(4):1479-83. [PubMed Link Image]
  4. Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Aebersold R, Leavitt J: Sequence analysis of proteins separated by polyacrylamide gel electrophoresis: towards an integrated protein database. Electrophoresis. 1990 Jul;11(7):517-27. [PubMed Link Image]
  7. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  8. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  10. Scheffzek K, Stephan I, Jensen ON, Illenberger D, Gierschik P: The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI. Nat Struct Biol. 2000 Feb;7(2):122-6. [PubMed Link Image]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 7141
Enzyme 48 Name Ras-related C3 botulinum toxin substrate 2
Enzyme 48 Synonyms
  1. GX
  2. Small G protein
  3. p21-Rac2
Enzyme 48 Gene Name RAC2
Enzyme 48 Protein Sequence >Ras-related C3 botulinum toxin substrate 2
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDSKPVNLGLWDTAG
QEDYDRLRPLSYPQTDVFLICFSLVSPASYENVRAKWFPEVRHHCPSTPIILVGTKLDLR
DDKDTIEKLKEKKLAPITYPQGLALAKEIDSVKYLECSALTQRGLKTVFDEAIRAVLCPQ
PTRQQKRACSLL
Enzyme 48 Number of Residues 192
Enzyme 48 Molecular Weight 21428.6
Enzyme 48 Theoretical pI 7.70
Enzyme 48 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 48 General Function Involved in GTP binding
Enzyme 48 Specific Function Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. Augments the production of reactive oxygen species (ROS) by NADPH oxidase
Enzyme 48 Pathways Not Available
Enzyme 48 Reactions Not Available
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein Not Available
Enzyme 48 UniProtKB/Swiss-Prot ID P15153 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name RAC2_HUMAN Link Image
Enzyme 48 PDB ID 1DS6 Link Image
Enzyme 48 PDB File Show
Enzyme 48 3D Structure
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence >579 bp
ATGCAGGCCATCAAGTGTGTGGTGGTGGGAGATGGGGCCGTGGGCAAGACCTGCCTTCTC
ATCAGCTACACCACCAACGCCTTTCCCGGAGAGTACATCCCCACCGTGTTTGACAACTAT
TCAGCCAATGTGATGGTGGACAGCAAGCCAGTGAACCTGGGGCTGTGGGACACTGCTGGG
CAGGAGGACTACGACCGTCTCCGGCCGCTCTCCTATCCACAGACGGACGTCTTCCTCATC
TGCTTCTCCCTCGTCAGCCCAGCCTCTTATGAGAACGTCCGCGCCAAGTGGTTCCCAGAA
GTGCGGCACCACTGCCCCAGCACACCCATCATCCTGGTGGGCACCAAGCTGGACCTGCGG
GACGACAAGGACACCATCGAGAAACTGAAGGAGAAGAAGCTGGCTCCCATCACCTACCCG
CAGGGCCTGGCACTGGCCAAGGAGATTGACTCGGTGAAATACCTGGAGTGCTCAGCCCTC
ACCCAGAGAGGCCTGAAAACCGTGTTCGACGAGGCCATCCGGGCCGTGCTGTGCCCTCAG
CCCACGCGGCAGCAGAAGCGCGCCTGCAGCCTCCTCTAG
Enzyme 48 GenBank Gene ID M29871 Link Image
Enzyme 48 GeneCard ID RAC2 Link Image
Enzyme 48 GenAtlas ID RAC2 Link Image
Enzyme 48 HGNC ID HGNC:9802 Link Image
Enzyme 48 Chromosome Location 2
Enzyme 48 Locus 22q13.1
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References
  1. Didsbury J, Weber RF, Bokoch GM, Evans T, Snyderman R: rac, a novel ras-related family of proteins that are botulinum toxin substrates. J Biol Chem. 1989 Oct 5;264(28):16378-82. [PubMed Link Image]
  2. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  3. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Mizuno T, Kaibuchi K, Ando S, Musha T, Hiraoka K, Takaishi K, Asada M, Nunoi H, Matsuda I, Takai Y: Regulation of the superoxide-generating NADPH oxidase by a small GTP-binding protein and its stimulatory and inhibitory GDP/GTP exchange proteins. J Biol Chem. 1992 May 25;267(15):10215-8. [PubMed Link Image]
  6. Knaus UG, Heyworth PG, Evans T, Curnutte JT, Bokoch GM: Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2. Science. 1991 Dec 6;254(5037):1512-5. [PubMed Link Image]
  7. Reibel L, Dorseuil O, Stancou R, Bertoglio J, Gacon G: A hemopoietic specific gene encoding a small GTP binding protein is overexpressed during T cell activation. Biochem Biophys Res Commun. 1991 Mar 15;175(2):451-8. [PubMed Link Image]
  8. Kwong CH, Malech HL, Rotrosen D, Leto TL: Regulation of the human neutrophil NADPH oxidase by rho-related G-proteins. Biochemistry. 1993 Jun 1;32(21):5711-7. [PubMed Link Image]
  9. Kinsella BT, Erdman RA, Maltese WA: Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA. J Biol Chem. 1991 May 25;266(15):9786-94. [PubMed Link Image]
  10. Nishihara H, Kobayashi S, Hashimoto Y, Ohba F, Mochizuki N, Kurata T, Nagashima K, Matsuda M: Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins. Biochim Biophys Acta. 1999 Nov 11;1452(2):179-87. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  12. Scheffzek K, Stephan I, Jensen ON, Illenberger D, Gierschik P: The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI. Nat Struct Biol. 2000 Feb;7(2):122-6. [PubMed Link Image]
  13. Ambruso DR, Knall C, Abell AN, Panepinto J, Kurkchubasche A, Thurman G, Gonzalez-Aller C, Hiester A, deBoer M, Harbeck RJ, Oyer R, Johnson GL, Roos D: Human neutrophil immunodeficiency syndrome is associated with an inhibitory Rac2 mutation. Proc Natl Acad Sci U S A. 2000 Apr 25;97(9):4654-9. [PubMed Link Image]
  14. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 7272
Enzyme 49 Name Elongation factor 1-alpha 1
Enzyme 49 Synonyms
  1. EF-1-alpha-1
  2. Elongation factor Tu
  3. EF-Tu
  4. Eukaryotic elongation factor 1 A-1
  5. eEF1A-1
  6. Leukocyte receptor cluster member 7
Enzyme 49 Gene Name EEF1A1
Enzyme 49 Protein Sequence >Elongation factor 1-alpha 1
MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVL
DKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGV
GEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKK
IGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTR
PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALS
EALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPV
LDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPP
LGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK
Enzyme 49 Number of Residues 462
Enzyme 49 Molecular Weight 50140.6
Enzyme 49 Theoretical pI 9.50
Enzyme 49 GO Classification
Function
  • GTP binding
  • GTPase activity
  • RNA binding
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleic acid binding
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • translation elongation factor activity
  • translation factor activity, nucleic acid binding
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • translational elongation
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 49 General Function Involved in GTPase activity
Enzyme 49 Specific Function This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis
Enzyme 49 Pathways Not Available
Enzyme 49 Reactions Not Available
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • None
Enzyme 49 Transmembrane Regions
  • None
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 31098 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID P68104 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name EF1A1_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >1389 bp
ATGGGAAAGGAAAAGACTCATATCAACATTGTCGTCATTGGACACGTAGATTCGGGCAAG
TCCACCACTACTGGCCATCTGATCTATAAATGCGGTGGCATCGACAAAAGAACCATTGAA
AAATTTGAGAAGGAGGCTGCTGAGATGGGAAAGGGCTCCTTCAAGTATGCCTGGGTCTTG
GATAAACTGAAAGCTGAGCGTGAACGTGGTATCACCATTGATATCTCCTTGTGGAAATTT
GAGACCAGCAAGTACTATGTGACTATCATTGATGCCCCAGGACACAGAGACTTTATCAAA
AACATGATTACAGGGACATCTCAGGCTGACTGTGCTGTCCTGATTGTTGCTGCTGGTGTT
GGTGAATTTGAAGCTGGTATCTCCAAGAATGGGCAGACCCGAGAGCATGCCCTTCTGGCT
TACACACTGGGTGTGAAACAACTAATTGTCGGTGTTAACAAAATGGATTCCACTGAGCCA
CCCTACAGCCAGAAGAGATATGAGGAAATTGTTAAGGAAGTCAGCACTTACATTAAGAAA
ATTGGCTACAACCCCGACACAGTAGCATTTGTGCCAATTTCTGGTTGGAATGGTGACAAC
ATGCTGGAGCCAAGTGCTAACATGCCTTGGTTCAAGGGATGGAAAGTCACCCGTAAGGAT
GGCAATGCCAGTGGAACCACGCTGCTTGAGGCTCTGGACTGCATCCTACCACCAACTCGT
CCAACTGACAAGCCCTTGCGCCTGCCTCTCCAGGATGTCTACAAAATTGGTGGTATTGGT
ACTGTTCCTGTTGGCCGAGTGGAGACTGGTGTTCTCAAACCCGGTATGGTGGTCACCTTT
GCTCCAGTCAACGTTACAACGGAAGTAAAATCTGTCGAAATGCACCATGAAGCTTTGAGT
GAAGCTCTTCCTGGGGACAATGTGGGCTTCAATGTCAAGAATGTGTCTGTCAAGGATGTT
CGTCGTGGCAACGTTGCTGGTGACAGCAAAAATGACCCACCAATGGAAGCAGCTGGCTTC
ACTGCTCAGGTGATTATCCTGAACCATCCAGGCCAAATAAGCGCCGGCTATGCCCCTGTA
TTGGATTGCCACACGGCTCACATTGCATGCAAGTTTGCTGAGCTGAAGGAAAAGATTGAT
CGCCGTTCTGGTAAAAAGCTGGAAGATGGCCCTAAATTCTTGAAGTCTGGTGATGCTGCC
ATTGTTGATATGGTTCCTGGCAAGCCCATGTGTGTTGAGAGCTTCTCAGACTATCCACCT
TTGGGTCGCTTTGCTGTTCGTGATATGAGACAGACAGTTGCGGTGGGTGTCATCAAAGCA
GTGGACAAGAAGGCTGCTGGAGCTGGCAAGGTCACCAAGTCTGCCCAGAAAGCTCAGAAG
GCTAAATGA
Enzyme 49 GenBank Gene ID X03558 Link Image
Enzyme 49 GeneCard ID EEF1A1 Link Image
Enzyme 49 GenAtlas ID EEF1A1 Link Image
Enzyme 49 HGNC ID HGNC:3189 Link Image
Enzyme 49 Chromosome Location 6
Enzyme 49 Locus 6q14.1
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References
  1. Brands JH, Maassen JA, van Hemert FJ, Amons R, Moller W: The primary structure of the alpha subunit of human elongation factor 1. Structural aspects of guanine-nucleotide-binding sites. Eur J Biochem. 1986 Feb 17;155(1):167-71. [PubMed Link Image]
  2. Uetsuki T, Naito A, Nagata S, Kaziro Y: Isolation and characterization of the human chromosomal gene for polypeptide chain elongation factor-1 alpha. J Biol Chem. 1989 Apr 5;264(10):5791-8. [PubMed Link Image]
  3. Madsen HO, Poulsen K, Dahl O, Clark BF, Hjorth JP: Retropseudogenes constitute the major part of the human elongation factor 1 alpha gene family. Nucleic Acids Res. 1990 Mar 25;18(6):1513-6. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Rao TR, Slobin LI: Structure of the amino-terminal end of mammalian elongation factor Tu. Nucleic Acids Res. 1986 Mar 11;14(5):2409. [PubMed Link Image]
  6. Ann DK, Wu MM, Huang T, Carlson DM, Wu R: Retinol-regulated gene expression in human tracheobronchial epithelial cells. Enhanced expression of elongation factor EF-1 alpha. J Biol Chem. 1988 Mar 15;263(8):3546-9. [PubMed Link Image]
  7. Whiteheart SW, Shenbagamurthi P, Chen L, Cotter RJ, Hart GW: Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha. J Biol Chem. 1989 Aug 25;264(24):14334-41. [PubMed Link Image]
  8. Bohnsack MT, Regener K, Schwappach B, Saffrich R, Paraskeva E, Hartmann E, Gorlich D: Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm. EMBO J. 2002 Nov 15;21(22):6205-15. [PubMed Link Image]
  9. Calado A, Treichel N, Muller EC, Otto A, Kutay U: Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA. EMBO J. 2002 Nov 15;21(22):6216-24. [PubMed Link Image]
  10. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  11. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed Link Image]
  12. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  13. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  14. Guzzo CM, Yang DC: Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro. Biochem Biophys Res Commun. 2008 Jan 25;365(4):718-23. Epub 2007 Nov 20. [PubMed Link Image]
  15. Yang YF, Chou MY, Fan CY, Chen SF, Lyu PC, Liu CC, Tseng TL: The possible interaction of CDA14 and protein elongation factor 1alpha. Biochim Biophys Acta. 2008 Feb;1784(2):312-8. Epub 2007 Oct 17. [PubMed Link Image]
  16. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 7276
Enzyme 50 Name Elongation factor 1-alpha 2
Enzyme 50 Synonyms
  1. EF-1-alpha-2
  2. Eukaryotic elongation factor 1 A-2
  3. eEF1A-2
  4. Statin-S1
Enzyme 50 Gene Name EEF1A2
Enzyme 50 Protein Sequence >Elongation factor 1-alpha 2
MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVL
DKLKAERERGITIDISLWKFETTKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGV
GEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPAYSEKRYDEIVKEVSAYIKK
IGYNPATVPFVPISGWHGDNMLEPSPNMPWFKGWKVERKEGNASGVSLLEALDTILPPTR
PTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALS
EALPGDNVGFNVKNVSVKDIRRGNVCGDSKSDPPQEAAQFTSQVIILNHPGQISAGYSPV
IDCHTAHIACKFAELKEKIDRRSGKKLEDNPKSLKSGDAAIVEMVPGKPMCVESFSQYPP
LGRFAVRDMRQTVAVGVIKNVEKKSGGAGKVTKSAQKAQKAGK
Enzyme 50 Number of Residues 463
Enzyme 50 Molecular Weight 50469.9
Enzyme 50 Theoretical pI 9.50
Enzyme 50 GO Classification
Function
  • GTP binding
  • GTPase activity
  • RNA binding
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleic acid binding
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • translation elongation factor activity
  • translation factor activity, nucleic acid binding
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • translational elongation
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 50 General Function Involved in GTPase activity
Enzyme 50 Specific Function This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis
Enzyme 50 Pathways Not Available
Enzyme 50 Reactions Not Available
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • None
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 38456 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID Q05639 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name EF1A2_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence >1392 bp
ATGGGCAAGGAGAAGACCCACATCAACATCGTGGTCATCGGCCACGTGGACTCCGGAAAG
TCCACCACCACGGGCCACCTCATCTACAAATGCGGAGGTATTGACAAAAGGACCATTGAG
AAGTTCGAGAAGGAGGCGGCTGAGATGGGGAAGGGATCCTTCAAGTATGCCTGGGTGCTG
GACAAGCTGAAGGCGGAGCGTGAGCGCGGCATCACCATCGACATCTCCCTCTGGAAGTTC
GAGACCACCAAGTACTACATCACCATCATCGATGCCCCCGGCCACCGCGACTTCATCAAG
AACATGATCACGGGTACATCCCAGGCGGACTGCGCAGTGCTGATCGTGGCGGCGGGCGTG
GGCGAGTTCGAGGCGGGCATCTCCAAGAATGGGCAGACGCGGGAGCATGCCCTGCTGGCC
TACACGCTGGGTGTGAAGCAGCTCATCGTGGGCGTGAACAAAATGGACTCCACAGAGCCG
GCCTACAGCGAGAAGCGCTACGACGAGATCGTCAAGGAAGTCAGCGCCTACATCAAGAAG
ATCGGCTACAACCCGGCCACCGTGCCCTTTGTGCCCATCTCCGGCTGGCACGGCGACAAC
ATGCTGGAGCCCTCCCCCAACATGCCGTGGTTCAAGGGCTGGAAGGTGGAGCGTAAGGAG
GGCAACGCAAGCGGCGTGTCCCTGCTGGAGGCCCTGGACACCATCCTGCCCCCCACGCGC
CCCACGGACAAGCCCCTGCGCCTGCCGCTGCAGGACGTGTACAAGATTGGCGGCATTGGC
ACGGTGCCCGTGGGCCGGGTGGAGACCGGCATCCTGCGGCCGGGCATGGTGGTGACCTTT
GCGCCAGTGAACATCACCACTGAGGTGAAGTCAGTGGAGATGCACCACGAGGCTCTGAGC
GAAGCTCTGCCCGGCGACAACGTCGGCTTCAATGTGAAGAACGTGTCGGTGAAGGACATC
CGGCGGGGCAACGTGTGTGGGGACAGCAAGTCTGACCCGCCGCAGGAGGCTGCTCAGTTC
ACCTCCCAGGTCATCATCCTGAACCACCCGGGGCAGATTAGCGCCGGCTACTCCCCGGTC
ATCGACTGCCACACAGCCCACATCGCCTGCAAGTTTGCGGAGCTGAAGGAGAAGATTGAC
CGGCGCTCTGGCAAGAAGCTGGAGGACAACCCCAAGTCCCTGAAGTCTGGAGACGCGGCC
ATCGTGGAGATGGTGCCGGGAAAGCCCATGTGTGTGGAGAGCTTCTCCCAGTACCCGCCT
CTCGGCCGCTTCGCCGTGCGCGACATGAGGCAGACGGTGGCCGTAGGCGTCATCAAGAAC
GTGGAAAAGAAGAGCGGCGGCGCCGGCAAGGTCACCAAGTCGGCGCAGAAGGCGCAGAAG
GCGGGCAAGTGA
Enzyme 50 GenBank Gene ID X70940 Link Image
Enzyme 50 GeneCard ID EEF1A2 Link Image
Enzyme 50 GenAtlas ID EEF1A2 Link Image
Enzyme 50 HGNC ID HGNC:3192 Link Image
Enzyme 50 Chromosome Location 2
Enzyme 50 Locus 20q13.3
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 General References
  1. Knudsen SM, Frydenberg J, Clark BF, Leffers H: Tissue-dependent variation in the expression of elongation factor-1 alpha isoforms: isolation and characterisation of a cDNA encoding a novel variant of human elongation-factor 1 alpha. Eur J Biochem. 1993 Aug 1;215(3):549-54. [PubMed Link Image]
  2. Bischoff C, Kahns S, Lund A, Jorgensen HF, Praestegaard M, Clark BF, Leffers H: The human elongation factor 1 A-2 gene (EEF1A2): complete sequence and characterization of gene structure and promoter activity. Genomics. 2000 Aug 15;68(1):63-70. [PubMed Link Image]
  3. Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7. [PubMed Link Image]
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Lee S, Ann DK, Wang E: Cloning of human and mouse brain cDNAs coding for S1, the second member of the mammalian elongation factor-1 alpha gene family: analysis of a possible evolutionary pathway. Biochem Biophys Res Commun. 1994 Sep 30;203(3):1371-7. [PubMed Link Image]
  7. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  8. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  9. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  10. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  12. Dai S, Crawford F, Marrack P, Kappler JW: The structure of HLA-DR52c: comparison to other HLA-DRB3 alleles. Proc Natl Acad Sci U S A. 2008 Aug 19;105(33):11893-7. Epub 2008 Aug 12. [PubMed Link Image]
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 7342
Enzyme 51 Name Vinexin
Enzyme 51 Synonyms
  1. SH3-containing adapter molecule 1
  2. SCAM-1
  3. Sorbin and SH3 domain-containing protein 3
Enzyme 51 Gene Name SORBS3
Enzyme 51 Protein Sequence >Vinexin
MQGPPRSLRAGLSLDDFIPGHLQSHIGSSSRGTRVPVIRNGGSNTLNFQFHDPAPRTVCN
GGYTPRRDASQHPDPAWYQTWPGPGSKPSASTKIPASQHTQNWSATWTKDSKRRDKRWVK
YEGIGPVDESGMPIAPRSSVDRPRDWYRRMFQQIHRKMPDLQLDWTFEEPPRDPRHLGAQ
QRPAHRPGPATSSSGRSWDHSEELPRSTFNYRPGAFSTVLQPSNQVLRRREKVDNVWTEE
SWNQFLQELETGQRPKKPLVDDPGEKPSQPIEVLLERELAELSAELDKDLRAIETRLPSP
KSSPAPRRAPEQRPPAGPASAWSSSYPHAPYLGSARSLSPHKMADGGSPFLGRRDFVYPS
STRDPSASNGGGSPARREEKKRKAARLKFDFQAQSPKELTLQKGDIVYIHKEVDKNWLEG
EHHGRLGIFPANYVEVLPADEIPKPIKPPTYQVLEYGEAVAQYTFKGDLEVELSFRKGEH
ICLIRKVNENWYEGRITGTGRQGIFPASYVQVSREPRLRLCDDGPQLPTSPRLTAAARSA
RHPSSPSALRSPADPTDLGGQTSPRRTGFSFPTQEPRPQTQNLGTPGPALSHSRGPSHPL
DLGTSSPNTSQIHWTPYRAMYQYRPQNEDELELREGDRVDVMQQCDDGWFVGVSRRTQKF
GTFPGNYVAPV
Enzyme 51 Number of Residues 671
Enzyme 51 Molecular Weight 75328.4
Enzyme 51 Theoretical pI 9.87
Enzyme 51 GO Classification Not Available
Enzyme 51 General Function Involved in structural constituent of cytoskeleton
Enzyme 51 Specific Function Vinexin alpha isoform promotes up-regulation of actin stress fiber formation. Vinexin beta isoform plays a role in cell spreading and enhances the activation of JNK/SAPK in response to EGF stimulation by using its third SH3 domain
Enzyme 51 Pathways Not Available
Enzyme 51 Reactions Not Available
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • None
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 155030230 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID O60504 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name VINEX_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence >2016 bp
ATGCAGGGCCCACCCCGCAGCCTCCGCGCTGGGCTCAGCCTGGACGACTTCATCCCTGGC
CACCTCCAGTCCCACATAGGGTCTTCCTCCCGGGGGACACGGGTGCCCGTGATCCGGAAT
GGTGGCTCCAACACCCTTAATTTCCAGTTCCACGACCCCGCGCCCAGGACTGTGTGCAAT
GGGGGCTACACACCAAGACGAGATGCTTCCCAGCACCCGGACCCTGCGTGGTATCAGACC
TGGCCAGGCCCTGGGAGCAAGCCCTCTGCAAGCACAAAGATCCCTGCCTCCCAGCACACC
CAGAACTGGTCAGCCACGTGGACCAAGGACAGCAAGCGTCGGGACAAGCGCTGGGTCAAG
TACGAGGGAATCGGGCCCGTGGACGAGAGCGGCATGCCCATTGCCCCCCGATCCAGCGTT
GACAGACCCAGAGACTGGTACCGGAGAATGTTCCAGCAGATTCACCGGAAAATGCCAGAC
TTGCAGCTGGACTGGACCTTCGAGGAGCCACCCAGAGACCCCAGGCATCTAGGAGCCCAG
CAAAGACCTGCCCACAGGCCCGGCCCGGCAACATCTTCCAGTGGAAGAAGCTGGGACCAC
TCTGAAGAGTTACCTAGAAGCACCTTCAACTACAGACCTGGAGCATTCTCCACTGTGCTG
CAGCCCTCAAATCAGGTGCTCAGACGCCGGGAAAAAGTAGACAATGTCTGGACGGAAGAG
TCCTGGAACCAGTTTCTGCAGGAACTAGAGACTGGGCAGAGGCCCAAGAAACCGCTGGTG
GACGACCCTGGTGAGAAGCCCTCCCAGCCCATTGAGGTGCTGCTGGAGAGAGAGCTGGCC
GAGCTGAGCGCCGAGCTGGACAAGGACCTGCGGGCAATTGAGACCCGACTGCCGTCCCCC
AAGAGCTCGCCGGCGCCCCGACGGGCCCCGGAGCAGCGGCCCCCGGCCGGCCCGGCCTCA
GCCTGGAGCTCCAGCTACCCACATGCACCTTACCTGGGTTCCGCCCGGTCCCTGAGTCCC
CACAAAATGGCTGATGGAGGAAGCCCCTTCCTAGGTCGGAGGGACTTTGTCTACCCTTCC
TCAACCCGAGACCCTAGTGCCTCTAACGGAGGGGGCAGCCCAGCCAGGAGGGAAGAGAAG
AAGAGAAAGGCCGCCAGGCTCAAGTTTGACTTCCAGGCGCAGTCCCCCAAGGAGCTGACT
CTGCAGAAGGGTGACATTGTCTACATCCACAAGGAGGTGGACAAGAACTGGCTGGAGGGA
GAGCACCACGGCCGCCTGGGCATCTTCCCTGCTAATTATGTGGAGGTGCTGCCCGCAGAT
GAGATCCCTAAGCCCATCAAGCCCCCGACCTACCAGGTGCTGGAGTATGGAGAGGCTGTG
GCCCAGTACACCTTCAAGGGGGACCTGGAGGTGGAGCTGTCCTTCCGCAAGGGAGAGCAC
ATCTGCCTGATCCGCAAGGTGAACGAGAACTGGTACGAGGGACGCATCACGGGCACGGGG
CGCCAAGGCATATTCCCTGCCAGCTACGTGCAGGTGTCTCGTGAACCCCGGCTCCGGCTC
TGTGACGACGGCCCCCAGCTCCCCACGTCTCCCCGCCTGACCGCTGCCGCCCGCTCAGCC
CGTCACCCCAGCTCCCCCTCAGCCCTGCGCAGCCCAGCTGACCCCATCGACTTGGGGGGA
CAGACCTCCCCCCGTCGCACTGGCTTCTCCTTCCCCACCCAGGAGCCTAGACCCCAGACC
CAGAATCTTGGCACCCCTGGTCCAGCTCTGTCCCACTCTCGAGGTCCCAGCCATCCCCTG
GACCTGGGGACCTCCTCTCCTAACACCTCTCAGATACACTGGACCCCGTACCGGGCGATG
TACCAGTACAGGCCCCAGAACGAAGACGAGCTGGAGCTGCGCGAGGGGGACAGGGTGGAT
GTCATGCAGCAGTGTGACGATGGCTGGTTTGTGGGTGTCTCCCGGAGGACCCAGAAATTC
GGAACGTTCCCTGGAAATTACGTTGCCCCGGTGTGA
Enzyme 51 GenBank Gene ID NM_005775.4 Link Image
Enzyme 51 GeneCard ID SORBS3 Link Image
Enzyme 51 GenAtlas ID SORBS3 Link Image
Enzyme 51 HGNC ID HGNC:30907 Link Image
Enzyme 51 Chromosome Location 8
Enzyme 51 Locus 8p21.3
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 General References
  1. Kioka N, Sakata S, Kawauchi T, Amachi T, Akiyama SK, Okazaki K, Yaen C, Yamada KM, Aota S: Vinexin: a novel vinculin-binding protein with multiple SH3 domains enhances actin cytoskeletal organization. J Cell Biol. 1999 Jan 11;144(1):59-69. [PubMed Link Image]
  2. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Akamatsu M, Aota S, Suwa A, Ueda K, Amachi T, Yamada KM, Akiyama SK, Kioka N: Vinexin forms a signaling complex with Sos and modulates epidermal growth factor-induced c-Jun N-terminal kinase/stress-activated protein kinase activities. J Biol Chem. 1999 Dec 10;274(50):35933-7. [PubMed Link Image]
  5. Townson SM, Dobrzycka KM, Lee AV, Air M, Deng W, Kang K, Jiang S, Kioka N, Michaelis K, Oesterreich S: SAFB2, a new scaffold attachment factor homolog and estrogen receptor corepressor. J Biol Chem. 2003 May 30;278(22):20059-68. Epub 2003 Mar 26. [PubMed Link Image]
  6. Martens N, Wery M, Wang P, Braet F, Gertler A, Hooghe R, Vandenhaute J, Hooghe-Peters EL: The suppressor of cytokine signaling (SOCS)-7 interacts with the actin cytoskeleton through vinexin. Exp Cell Res. 2004 Aug 1;298(1):239-48. [PubMed Link Image]
  7. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  8. Paternotte N, Zhang J, Vandenbroere I, Backers K, Blero D, Kioka N, Vanderwinden JM, Pirson I, Erneux C: SHIP2 interaction with the cytoskeletal protein Vinexin. FEBS J. 2005 Dec;272(23):6052-66. [PubMed Link Image]
  9. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  10. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  11. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  12. Ito H, Atsuzawa K, Sudo K, Di Stefano P, Iwamoto I, Morishita R, Takei S, Semba R, Defilippi P, Asano T, Usuda N, Nagata K: Characterization of a multidomain adaptor protein, p140Cap, as part of a pre-synaptic complex. J Neurochem. 2008 Oct;107(1):61-72. Epub 2008 Jul 24. [PubMed Link Image]
  13. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  14. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  15. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  16. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  17. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  18. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 7383
Enzyme 52 Name GTPase HRas
Enzyme 52 Synonyms
  1. H-Ras-1
  2. Ha-Ras
  3. Transforming protein p21
  4. c-H-ras
  5. p21ras
  6. GTPase HRas, N-terminally processed
Enzyme 52 Gene Name HRAS
Enzyme 52 Protein Sequence >GTPase HRas
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG
QEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL
AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPG
CMSCKCVLS
Enzyme 52 Number of Residues 189
Enzyme 52 Molecular Weight 21298.0
Enzyme 52 Theoretical pI 4.94
Enzyme 52 GO Classification
Function
  • GTP binding
  • GTPase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
  • membrane
Enzyme 52 General Function Involved in GTP binding
Enzyme 52 Specific Function Ras proteins bind GDP/GTP and possess intrinsic GTPase activity
Enzyme 52 Pathways Not Available
Enzyme 52 Reactions Not Available
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • None
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein 20147725 Link Image
Enzyme 52 UniProtKB/Swiss-Prot ID P01112 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name RASH_HUMAN Link Image
Enzyme 52 PDB ID 4Q21 Link Image
Enzyme 52 PDB File Show
Enzyme 52 3D Structure
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence >570 bp
ATGACGGAATATAAGCTGGTGGTGGTGGGCGCCGGCGGTGTGGGCAAGAGTGCGCTGACC
ATCCAGCTGATCCAGAACCATTTTGTGGACGAATACGACCCCACTATAGAGGATTCCTAC
CGGAAGCAGGTGGTCATTGATGGGGAGACGTGCCTGTTGGACATCCTGGATACCGCCGGC
CAGGAGGAGTACAGCGCCATGCGGGACCAGTACATGCGCACCGGGGAGGGCTTCCTGTGT
GTGTTTGCCATCAACAACACCAAGTCTTTTGAGGACATCCACCAGTACAGGGAGCAGATC
AAACGGGTGAAGGACTCGGATGACGTGCCCATGGTGCTGGTGGGGAACAAGTGTGACCTG
GCTGCACGCACTGTGGAATCTCGGCAGGCTCAGGACCTCGCCCGAAGCTACGGCATCCCC
TACATCGAGACCTCGGCCAAGACCCGGCAGGGAGTGGAGGATGCCTTCTACACGTTGGTG
CGTGAGATCCGGCAGCACAAGCTGCGGAAGCTGAACCCTCCTGATGAGAGTGGCCCCGGC
TGCATGAGCTGCAAGTGTGTGCTCTCCTGA
Enzyme 52 GenBank Gene ID AF493916 Link Image
Enzyme 52 GeneCard ID HRAS Link Image
Enzyme 52 GenAtlas ID HRAS Link Image
Enzyme 52 HGNC ID HGNC:5173 Link Image
Enzyme 52 Chromosome Location 1
Enzyme 52 Locus 11p15.5
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 General References
  1. Capon DJ, Chen EY, Levinson AD, Seeburg PH, Goeddel DV: Complete nucleotide sequences of the T24 human bladder carcinoma oncogene and its normal homologue. Nature. 1983 Mar 3;302(5903):33-7. [PubMed Link Image]
  2. Reddy EP: Nucleotide sequence analysis of the T24 human bladder carcinoma oncogene. Science. 1983 Jun 3;220(4601):1061-3. [PubMed Link Image]
  3. Sekiya T, Fushimi M, Hori H, Hirohashi S, Nishimura S, Sugimura T: Molecular cloning and the total nucleotide sequence of the human c-Ha-ras-1 gene activated in a melanoma from a Japanese patient. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4771-5. [PubMed Link Image]
  4. Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Tabin CJ, Bradley SM, Bargmann CI, Weinberg RA, Papageorge AG, Scolnick EM, Dhar R, Lowy DR, Chang EH: Mechanism of activation of a human oncogene. Nature. 1982 Nov 11;300(5888):143-9. [PubMed Link Image]
  7. Honkawa H, Masahashi W, Hashimoto S, Hashimoto-Gotoh T: Identification of the principal promoter sequence of the c-H-ras transforming oncogene: deletion analysis of the 5'-flanking region by focus formation assay. Mol Cell Biol. 1987 Aug;7(8):2933-40. [PubMed Link Image]
  8. Low A, Sprinzl M, Faulhammer HG: Affinity labeling of c-H-ras p21 consensus elements with periodate-oxidized GDP and GTP. Eur J Biochem. 1993 Jul 15;215(2):473-9. [PubMed Link Image]
  9. Feig LA, Pan BT, Roberts TM, Cooper GM: Isolation of ras GTP-binding mutants using an in situ colony-binding assay. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4607-11. [PubMed Link Image]
  10. Lacal JC, Anderson PS, Aaronson SA: Deletion mutants of Harvey ras p21 protein reveal the absolute requirement of at least two distant regions for GTP-binding and transforming activities. EMBO J. 1986 Apr;5(4):679-87. [PubMed Link Image]
  11. Hancock JF, Magee AI, Childs JE, Marshall CJ: All ras proteins are polyisoprenylated but only some are palmitoylated. Cell. 1989 Jun 30;57(7):1167-77. [PubMed Link Image]
  12. Dudler T, Gelb MH: Palmitoylation of Ha-Ras facilitates membrane binding, activation of downstream effectors, and meiotic maturation in Xenopus oocytes. J Biol Chem. 1996 May 10;271(19):11541-7. [PubMed Link Image]
  13. Lander HM, Hajjar DP, Hempstead BL, Mirza UA, Chait BT, Campbell S, Quilliam LA: A molecular redox switch on p21(ras). Structural basis for the nitric oxide-p21(ras) interaction. J Biol Chem. 1997 Feb 14;272(7):4323-6. [PubMed Link Image]
  14. Song C, Hu CD, Masago M, Kariyai K, Yamawaki-Kataoka Y, Shibatohge M, Wu D, Satoh T, Kataoka T: Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras. J Biol Chem. 2001 Jan 26;276(4):2752-7. Epub 2000 Oct 5. [PubMed Link Image]
  15. Topham MK, Prescott SM: Diacylglycerol kinase zeta regulates Ras activation by a novel mechanism. J Cell Biol. 2001 Mar 19;152(6):1135-43. [PubMed Link Image]
  16. Swarthout JT, Lobo S, Farh L, Croke MR, Greentree WK, Deschenes RJ, Linder ME: DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H- and N-Ras. J Biol Chem. 2005 Sep 2;280(35):31141-8. Epub 2005 Jul 6. [PubMed Link Image]
  17. Rocks O, Peyker A, Kahms M, Verveer PJ, Koerner C, Lumbierres M, Kuhlmann J, Waldmann H, Wittinghofer A, Bastiaens PI: An acylation cycle regulates localization and activity of palmitoylated Ras isoforms. Science. 2005 Mar 18;307(5716):1746-52. Epub 2005 Feb 10. [PubMed Link Image]
  18. Pan F, Sun L, Kardian DB, Whartenby KA, Pardoll DM, Liu JO: Feedback inhibition of calcineurin and Ras by a dual inhibitory protein Carabin. Nature. 2007 Jan 25;445(7126):433-6. Epub 2007 Jan 17. [PubMed Link Image]
  19. de Vos AM, Tong L, Milburn MV, Matias PM, Jancarik J, Noguchi S, Nishimura S, Miura K, Ohtsuka E, Kim SH: Three-dimensional structure of an oncogene protein: catalytic domain of human c-H-ras p21. Science. 1988 Feb 19;239(4842):888-93. [PubMed Link Image]
  20. Pai EF, Kabsch W, Krengel U, Holmes KC, John J, Wittinghofer A: Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. Nature. 1989 Sep 21;341(6239):209-14. [PubMed Link Image]
  21. Pai EF, Krengel U, Petsko GA, Goody RS, Kabsch W, Wittinghofer A: Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 1990 Aug;9(8):2351-9. [PubMed Link Image]
  22. Tong LA, de Vos AM, Milburn MV, Kim SH: Crystal structures at 2.2 A resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP. J Mol Biol. 1991 Feb 5;217(3):503-16. [PubMed Link Image]
  23. Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED: Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy. Biochemistry. 1994 Mar 29;33(12):3515-31. [PubMed Link Image]
  24. Scheffzek K, Ahmadian MR, Kabsch W, Wiesmuller L, Lautwein A, Schmitz F, Wittinghofer A: The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science. 1997 Jul 18;277(5324):333-8. [PubMed Link Image]
  25. Scheidig AJ, Burmester C, Goody RS: The pre-hydrolysis state of p21(ras) in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins. Structure. 1999 Nov 15;7(11):1311-24. [PubMed Link Image]
  26. Hall BE, Bar-Sagi D, Nassar N: The structural basis for the transition from Ras-GTP to Ras-GDP. Proc Natl Acad Sci U S A. 2002 Sep 17;99(19):12138-42. Epub 2002 Sep 4. [PubMed Link Image]
  27. Williams JG, Pappu K, Campbell SL: Structural and biochemical studies of p21Ras S-nitrosylation and nitric oxide-mediated guanine nucleotide exchange. Proc Natl Acad Sci U S A. 2003 May 27;100(11):6376-81. Epub 2003 May 9. [PubMed Link Image]
  28. Buhrman G, Wink G, Mattos C: Transformation efficiency of RasQ61 mutants linked to structural features of the switch regions in the presence of Raf. Structure. 2007 Dec;15(12):1618-29. [PubMed Link Image]
  29. Stieglitz B, Bee C, Schwarz D, Yildiz O, Moshnikova A, Khokhlatchev A, Herrmann C: Novel type of Ras effector interaction established between tumour suppressor NORE1A and Ras switch II. EMBO J. 2008 Jul 23;27(14):1995-2005. Epub 2008 Jul 3. [PubMed Link Image]
  30. Sakai E, Rikimaru K, Ueda M, Matsumoto Y, Ishii N, Enomoto S, Yamamoto H, Tsuchida N: The p53 tumor-suppressor gene and ras oncogene mutations in oral squamous-cell carcinoma. Int J Cancer. 1992 Dec 2;52(6):867-72. [PubMed Link Image]
  31. Nikiforova MN, Lynch RA, Biddinger PW, Alexander EK, Dorn GW 2nd, Tallini G, Kroll TG, Nikiforov YE: RAS point mutations and PAX8-PPAR gamma rearrangement in thyroid tumors: evidence for distinct molecular pathways in thyroid follicular carcinoma. J Clin Endocrinol Metab. 2003 May;88(5):2318-26. [PubMed Link Image]
  32. Aoki Y, Niihori T, Kawame H, Kurosawa K, Ohashi H, Tanaka Y, Filocamo M, Kato K, Suzuki Y, Kure S, Matsubara Y: Germline mutations in HRAS proto-oncogene cause Costello syndrome. Nat Genet. 2005 Oct;37(10):1038-40. Epub 2005 Sep 18. [PubMed Link Image]
  33. Gripp KW, Lin AE, Stabley DL, Nicholson L, Scott CI Jr, Doyle D, Aoki Y, Matsubara Y, Zackai EH, Lapunzina P, Gonzalez-Meneses A, Holbrook J, Agresta CA, Gonzalez IL, Sol-Church K: HRAS mutation analysis in Costello syndrome: genotype and phenotype correlation. Am J Med Genet A. 2006 Jan 1;140(1):1-7. [PubMed Link Image]
  34. Kerr B, Delrue MA, Sigaudy S, Perveen R, Marche M, Burgelin I, Stef M, Tang B, Eden OB, O'Sullivan J, De Sandre-Giovannoli A, Reardon W, Brewer C, Bennett C, Quarell O, M'Cann E, Donnai D, Stewart F, Hennekam R, Cave H, Verloes A, Philip N, Lacombe D, Levy N, Arveiler B, Black G: Genotype-phenotype correlation in Costello syndrome: HRAS mutation analysis in 43 cases. J Med Genet. 2006 May;43(5):401-5. Epub 2006 Jan 27. [PubMed Link Image]
  35. Zampino G, Pantaleoni F, Carta C, Cobellis G, Vasta I, Neri C, Pogna EA, De Feo E, Delogu A, Sarkozy A, Atzeri F, Selicorni A, Rauen KA, Cytrynbaum CS, Weksberg R, Dallapiccola B, Ballabio A, Gelb BD, Neri G, Tartaglia M: Diversity, parental germline origin, and phenotypic spectrum of de novo HRAS missense changes in Costello syndrome. Hum Mutat. 2007 Mar;28(3):265-72. [PubMed Link Image]
  36. van der Burgt I, Kupsky W, Stassou S, Nadroo A, Barroso C, Diem A, Kratz CP, Dvorsky R, Ahmadian MR, Zenker M: Myopathy caused by HRAS germline mutations: implications for disturbed myogenic differentiation in the presence of constitutive HRas activation. J Med Genet. 2007 Jul;44(7):459-62. Epub 2007 Apr 5. [PubMed Link Image]
  37. Gripp KW, Innes AM, Axelrad ME, Gillan TL, Parboosingh JS, Davies C, Leonard NJ, Lapointe M, Doyle D, Catalano S, Nicholson L, Stabley DL, Sol-Church K: Costello syndrome associated with novel germline HRAS mutations: an attenuated phenotype? Am J Med Genet A. 2008 Mar 15;146A(6):683-90. [PubMed Link Image]
Enzyme 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 7391
Enzyme 53 Name Rho-related GTP-binding protein RhoQ
Enzyme 53 Synonyms
  1. Ras-like protein TC10
  2. Ras-like protein family member 7A
Enzyme 53 Gene Name RHOQ
Enzyme 53 Protein Sequence >Rho-related GTP-binding protein RhoQ
MAHGPGALMLKCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVSVTVGGKQYLLG
LYDTAGQEDYDRLRPLSYPMTDVFLICFSVVNPASFQNVKEEWVPELKEYAPNVPFLLIG
TQIDLRDDPKTLARLNDMKEKPICVEQGQKLAKEIGACCYVECSALTQKGLKTVFDEAII
AILTPKKHTVKKRIGSRCINCCLIT
Enzyme 53 Number of Residues 205
Enzyme 53 Molecular Weight 22659.3
Enzyme 53 Theoretical pI 6.25
Enzyme 53 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 53 General Function Involved in GTP binding
Enzyme 53 Specific Function Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. May play a role in CFTR trafficking to the plasma membrane. Causes the formation of thin, actin-rich surface projections called filopodia
Enzyme 53 Pathways Not Available
Enzyme 53 Reactions Not Available
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • None
Enzyme 53 Transmembrane Regions
  • None
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein 62822285 Link Image
Enzyme 53 UniProtKB/Swiss-Prot ID P17081 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name RHOQ_HUMAN Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence >618 bp
ATGGCTCACGGGCCCGGCGCGCTGATGCTCAAGTGCGTGGTGGTCGGCGACGGGGCGGTG
GGCAAGACGTGCCTACTCATGAGCTATGCCAACGACGCCTTCCCGGAGGAGTACGTGCCC
ACCGTCTTCGACCACTACGCAGTCAGCGTCACCGTGGGGGGCAAGCAGTACCTCCTAGGA
CTCTATGACACGGCCGGACAGGAAGACTATGACCGTCTGAGGCCTTTATCTTACCCAATG
ACCGATGTCTTCCTTATATGCTTCTCGGTGGTAAATCCAGCCTCATTTCAAAATGTGAAA
GAGGAGTGGGTACCGGAACTTAAGGAATACGCACCAAATGTACCCTTTTTATTAATAGGA
ACTCAGATTGATCTCCGAGATGACCCCAAAACTTTAGCAAGACTGAATGATATGAAAGAA
AAACCTATATGTGTGGAACAAGGACAGAAACTAGCAAAAGAGATAGGAGCATGCTGCTAT
GTGGAATGTTCAGCTTTAACCCAGAAGGGATTGAAGACTGTTTTTGATGAGGCTATCATA
GCCATTTTAACTCCAAAGAAACACACTGTAAAAAAAAGAATAGGATCAAGATGTATAAAC
TGTTGTTTAATTACGTGA
Enzyme 53 GenBank Gene ID AC018682 Link Image
Enzyme 53 GeneCard ID RHOQ Link Image
Enzyme 53 GenAtlas ID RHOQ Link Image
Enzyme 53 HGNC ID HGNC:17736 Link Image
Enzyme 53 Chromosome Location 2
Enzyme 53 Locus 2p21
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 General References
  1. Drivas GT, Shih A, Coutavas E, Rush MG, D'Eustachio P: Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line. Mol Cell Biol. 1990 Apr;10(4):1793-8. [PubMed Link Image]
  2. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Joberty G, Perlungher RR, Macara IG: The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins. Mol Cell Biol. 1999 Oct;19(10):6585-97. [PubMed Link Image]
  5. Joberty G, Petersen C, Gao L, Macara IG: The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42. Nat Cell Biol. 2000 Aug;2(8):531-9. [PubMed Link Image]
  6. Neudauer CL, Joberty G, Macara IG: PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10. Biochem Biophys Res Commun. 2001 Jan 19;280(2):541-7. [PubMed Link Image]
  7. Cheng J, Wang H, Guggino WB: Regulation of cystic fibrosis transmembrane regulator trafficking and protein expression by a Rho family small GTPase TC10. J Biol Chem. 2005 Feb 4;280(5):3731-9. Epub 2004 Nov 15. [PubMed Link Image]
Enzyme 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 7480
Enzyme 54 Name Guanine nucleotide-binding protein G(q) subunit alpha
Enzyme 54 Synonyms
  1. Guanine nucleotide-binding protein alpha-q
Enzyme 54 Gene Name GNAQ
Enzyme 54 Protein Sequence >Guanine nucleotide-binding protein G(q) subunit alpha
MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMR
IIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEK
VSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPAYLPTQQDVL
RVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLV
ESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQR
DAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
Enzyme 54 Number of Residues 359
Enzyme 54 Molecular Weight 42141.7
Enzyme 54 Theoretical pI 5.37
Enzyme 54 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • molecular transducer activity
  • nucleotide binding
  • purine nucleotide binding
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • biological regulation
  • cell surface receptor linked signaling pathway
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • post-translational protein modification
  • protein amino acid ADP-ribosylation
  • protein modification process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 54 General Function Involved in signal transducer activity
Enzyme 54 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems
Enzyme 54 Pathways Not Available
Enzyme 54 Reactions Not Available
Enzyme 54 Pfam Domain Function
Enzyme 54 Signals
  • None
Enzyme 54 Transmembrane Regions
  • None
Enzyme 54 Essentiality Not Available
Enzyme 54 GenBank ID Protein 1181671 Link Image
Enzyme 54 UniProtKB/Swiss-Prot ID P50148 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name GNAQ_HUMAN Link Image
Enzyme 54 PDB ID Not Available
Enzyme 54 Cellular Location Not Available
Enzyme 54 Gene Sequence >1080 bp
ATGACTCTGGAGTCCATCATGGCGTGCTGCCTGAGCGAGGAGGCCAAGGAAGCCCGGCGG
ATCAACGACGAGATCGAGCGGCACGTCCGCAGGGACAAGCGGGACGCCCGCCGGGAGCTC
AAGCTGCTGCTGCTCGGGACAGGAGAGAGTGGCAAGAGTACGTTTATCAAGCAGATGAGA
ATCATCCATGGGTCAGGATACTCTGATGAAGATAAAAGGGGCTTCACCAAGCTGGTGTAT
CAGAACATCTTCACGGCCATGCAGGCCATGATCAGAGCCATGGACACACTCAAGATCCCA
TACAAGTATGAGCACAATAAGGCTCATGCACAATTAGTTCGAGAAGTTGATGTGGAGAAG
GTGTCTGCTTTTGAGAATCCATATGTAGATGCAATAAAGAGTTTATGGAATGATCCTGGA
ATCCAGGAATGCTATGATAGACGACGAGAATATCAATTATCTGACTCTACCAAATACTAT
CTTAATGACTTGGACCGCGTAGCTGACCCTGCCTACCTGCCTACGCAACAAGATGTGCTT
AGAGTTCGAGTCCCCACCACAGGGATCATCGAATACCCCTTTGACTTACAAAGTGTCATT
TTCAGAATGGTCGATGTAGGGGGCCAAAGGTCAGAGAGAAGAAAATGGATACACTGCTTT
GAAAATGTCACCTCTATCATGTTTCTAGTAGCGCTTAGTGAATATGATCAAGTTCTCGTG
GAGTCAGACAATGAGAACCGAATGGAGGAAAGCAAGGCTCTCTTTAGAACAATTATCACA
TACCCCTGGTTCCAGAACTCCTCGGTTATTCTGTTCTTAAACAAGAAAGATCTTCTAGAG
GAGAAAATCATGTATTCCCATCTAGTCGACTACTTCCCAGAATATGATGGACCCCAGAGA
GATGCCCAGGCAGCCCGAGAATTCATTCTGAAGATGTTCGTGGACCTGAACCCAGACAGT
GACAAAATTATCTACTCCCACTTCACGTGCGCCACAGACACCGAGAATATCCGCTTTGTC
TTTGCTGCCGTCAAGGACACCATCCTCCAGTTGAACCTGAAGGAGTACAATCTGGTCTAA
Enzyme 54 GenBank Gene ID U40038 Link Image
Enzyme 54 GeneCard ID GNAQ Link Image
Enzyme 54 GenAtlas ID GNAQ Link Image
Enzyme 54 HGNC ID HGNC:4390 Link Image
Enzyme 54 Chromosome Location 9
Enzyme 54 Locus 9q21
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 General References
  1. Dong Q, Shenker A, Way J, Haddad BR, Lin K, Hughes MR, McBride OW, Spiegel AM, Battey J: Molecular cloning of human G alpha q cDNA and chromosomal localization of the G alpha q gene (GNAQ) and a processed pseudogene. Genomics. 1995 Dec 10;30(3):470-75. [PubMed Link Image]
  2. Chen B, Leverette RD, Schwinn DA, Kwatra MM: Human G(alpha q): cDNA and tissue distribution. Biochim Biophys Acta. 1996 Jun 11;1281(2):125-8. [PubMed Link Image]
  3. Johnson GJ, Leis LA, Dunlop PC: Specificity of G alpha q and G alpha 11 gene expression in platelets and erythrocytes. Expressions of cellular differentiation and species differences. Biochem J. 1996 Sep 15;318 ( Pt 3):1023-31. [PubMed Link Image]
  4. Gabbeta J, Dhanasekaran N, Rao AK: G alpha q cDNA sequence from human platelets. Thromb Res. 1998 Jul 1;91(1):29-32. [PubMed Link Image]
  5. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Lesch KP, Manji HK: Signal-transducing G proteins and antidepressant drugs: evidence for modulation of alpha subunit gene expression in rat brain. Biol Psychiatry. 1992 Oct 1;32(7):549-79. [PubMed Link Image]
  8. Thomas CP, Dunn MJ, Mattera R: Ca2+ signalling in K562 human erythroleukaemia cells: effect of dimethyl sulphoxide and role of G-proteins in thrombin- and thromboxane A2-activated pathways. Biochem J. 1995 Nov 15;312 ( Pt 1):151-8. [PubMed Link Image]
  9. Rochdi MD, Watier V, La Madeleine C, Nakata H, Kozasa T, Parent JL: Regulation of GTP-binding protein alpha q (Galpha q) signaling by the ezrin-radixin-moesin-binding phosphoprotein-50 (EBP50). J Biol Chem. 2002 Oct 25;277(43):40751-9. Epub 2002 Aug 21. [PubMed Link Image]
  10. Yeh JC, Otte LA, Frangos JA: Regulation of G protein-coupled receptor activities by the platelet-endothelial cell adhesion molecule, PECAM-1. Biochemistry. 2008 Aug 26;47(34):9029-39. Epub 2008 Aug 2. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 7482
Enzyme 55 Name Guanine nucleotide-binding protein subunit alpha-11
Enzyme 55 Synonyms
  1. G alpha-11
  2. G-protein subunit alpha-11
  3. Guanine nucleotide-binding protein G(y) subunit alpha
Enzyme 55 Gene Name GNA11
Enzyme 55 Protein Sequence >Guanine nucleotide-binding protein subunit alpha-11
MTLESMMACCLSDEVKESKRINAEIEKQLRRDKRDARRELKLLLLGTGESGKSTFIKQMR
IIHGAGYSEEDKRGFTKLVYQNIFTAMQAMIRAMETLKILYKYEQNKANALLIREVDVEK
VTTFEHQYVSAIKTLWEDPGIQECYDRRREYQLSDSAKYYLTDVDRIATLGYLPTQQDVL
RVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLV
ESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEDKILYSHLVDYFPEFDGPQR
DAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
Enzyme 55 Number of Residues 359
Enzyme 55 Molecular Weight 42122.9
Enzyme 55 Theoretical pI 5.38
Enzyme 55 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • molecular transducer activity
  • nucleotide binding
  • purine nucleotide binding
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • biological regulation
  • cell surface receptor linked signaling pathway
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • post-translational protein modification
  • protein amino acid ADP-ribosylation
  • protein modification process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 55 General Function Involved in signal transducer activity
Enzyme 55 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C
Enzyme 55 Pathways Not Available
Enzyme 55 Reactions Not Available
Enzyme 55 Pfam Domain Function
Enzyme 55 Signals
  • None
Enzyme 55 Transmembrane Regions
  • None
Enzyme 55 Essentiality Not Available
Enzyme 55 GenBank ID Protein 3289982 Link Image
Enzyme 55 UniProtKB/Swiss-Prot ID P29992 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name GNA11_HUMAN Link Image
Enzyme 55 PDB ID Not Available
Enzyme 55 Cellular Location Not Available
Enzyme 55 Gene Sequence >1080 bp
ATGACTCTGGAGTCCATGATGGCGTGTTGCCTGAGCGATGAGGTGAAGGAGTCCAAGCGG
ATCAACGCCGAGATCGAGAAGCAGCTGCGGCGGGACAAGCGCGACGCCCGGCGCGAGCTC
AAGCTGCTGCTGCTCGGCACGGGCGAGAGCGGGAAGAGCACGTTCATCAAGCAGATGCGC
ATCATCCACGGCGCCGGCTACTCGGAGGAGGACAAGCGCGGCTTCACCAAGCTCGTCTAC
CAGAACATCTTCACCGCCATGCAGGCCATGATCCGGGCCATGGAGACGCTCAAGATCCTC
TACAAGTACGAGCAGAACAAGGCCAATGCGCTCCTGATCCGGGAGGTGGACGTGGAGAAG
GTGACCACCTTCGAGCATCAGTACGTCAGTGCCATCAAGACCCTGTGGGAGGACCCGGGC
ATCCAGGAATGCTACGACCGCAGGCGCGAGTACCAGCTCTCCGACTCTGCCAAGTACTAC
CTGACCGACGTTGACCGCATCGCCACCTTGGGCTACCTGCCCACCCAGCAGGACGTGCTG
CGGGTCCGCGTGCCCACCACCGGCATCATCGAGTACCCTTTCGACCTGGAGAACATCATC
TTCCGGATGGTGGATGTGGGGGGCCAGCGGTCGGAGCGGAGGAAGTGGATCCACTGCTTT
GAGAACGTGACATCCATCATGTTTCTCGTCGCCCTCAGCGAATACGACCAAGTCCTGGTG
GAGTCGGACAACGAGAACCGGATGGAGGAGAGCAAAGCCCTGTTCCGGACCATCATCACC
TACCCCTGGTTCCAGAACTCCTCCGTCATCCTCTTCCTCAACAAGAAGGACCTGCTGGAG
GACAAGATCCTGTACTCGCACCTGGTGGACTACTTCCCCGAGTTCGATGGTCCCCAGCGG
GACGCCCAGGCGGCGCGGGAGTTCATCCTGAAGATGTTCGTGGACCTGAACCCCGACAGC
GACAAGATCATCTACTCACACTTCACGTGTGCCACCGACACGGAGAACATCCGCTTCGTG
TTCGCGGCCGTGAAGGACACCATCCTGCAGCTCAACCTCAAGGAGTACAACCTGGTCTGA
Enzyme 55 GenBank Gene ID AC005262 Link Image
Enzyme 55 GeneCard ID GNA11 Link Image
Enzyme 55 GenAtlas ID GNA11 Link Image
Enzyme 55 HGNC ID HGNC:4379 Link Image
Enzyme 55 Chromosome Location 1
Enzyme 55 Locus 19p13.3
Enzyme 55 SNPs SNPJam Report Link Image
Enzyme 55 General References
  1. Jiang M, Pandey S, Tran VT, Fong HK: Guanine nucleotide-binding regulatory proteins in retinal pigment epithelial cells. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3907-11. [PubMed Link Image]
  2. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Thomas CP, Dunn MJ, Mattera R: Ca2+ signalling in K562 human erythroleukaemia cells: effect of dimethyl sulphoxide and role of G-proteins in thrombin- and thromboxane A2-activated pathways. Biochem J. 1995 Nov 15;312 ( Pt 1):151-8. [PubMed Link Image]
Enzyme 55 Metabolite References Not Available
Enzyme 56 [top]
Enzyme 56 ID 7684
Enzyme 56 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-11
Enzyme 56 Synonyms Not Available
Enzyme 56 Gene Name GNG11
Enzyme 56 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-11
MPALHIEDLPEKEKLKMEVEQLRKEVKLQRQQVSKCSEEIKNYIEERSGEDPLVKGIPED
KNPFKEKGSCVIS
Enzyme 56 Number of Residues 73
Enzyme 56 Molecular Weight 8480.7
Enzyme 56 Theoretical pI 5.23
Enzyme 56 GO Classification
Function
  • molecular transducer activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • extrinsic to membrane
  • extrinsic to plasma membrane
  • heterotrimeric G-protein complex
  • membrane part
Enzyme 56 General Function Involved in signal transducer activity
Enzyme 56 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Enzyme 56 Pathways Not Available
Enzyme 56 Reactions Not Available
Enzyme 56 Pfam Domain Function
Enzyme 56 Signals
  • None
Enzyme 56 Transmembrane Regions
  • None
Enzyme 56 Essentiality Not Available
Enzyme 56 GenBank ID Protein 41393495 Link Image
Enzyme 56 UniProtKB/Swiss-Prot ID P61952 Link Image
Enzyme 56 UniProtKB/Swiss-Prot Entry Name GBG11_HUMAN Link Image
Enzyme 56 PDB ID Not Available
Enzyme 56 Cellular Location Not Available
Enzyme 56 Gene Sequence >222 bp
ATGCCTGCCCTTCACATCGAAGATTTGCCAGAGAAGGAAAAACTGAAAATGGAAGTTGAG
CAGCTTCGCAAAGAAGTGAAGTTGCAGAGACAACAAGTGTCTAAATGTTCTGAAGAAATA
AAGAACTATATTGAAGAACGTTCTGGAGAGGATCCTCTAGTAAAGGGAATTCCAGAAGAC
AAGAACCCCTTTAAAGAAAAAGGCAGCTGTGTTATTTCATAA
Enzyme 56 GenBank Gene ID AC002076 Link Image
Enzyme 56 GeneCard ID GNG11 Link Image
Enzyme 56 GenAtlas ID GNG11 Link Image
Enzyme 56 HGNC ID HGNC:4403 Link Image
Enzyme 56 Chromosome Location 7
Enzyme 56 Locus 7q21
Enzyme 56 SNPs SNPJam Report Link Image
Enzyme 56 General References
  1. Ray K, Kunsch C, Bonner LM, Robishaw JD: Isolation of cDNA clones encoding eight different human G protein gamma subunits, including three novel forms designated the gamma 4, gamma 10, and gamma 11 subunits. J Biol Chem. 1995 Sep 15;270(37):21765-71. [PubMed Link Image]
  2. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 56 Metabolite References Not Available
Enzyme 57 [top]
Enzyme 57 ID 7852
Enzyme 57 Name Chitobiosyldiphosphodolichol beta-mannosyltransferase
Enzyme 57 Synonyms
  1. Asparagine-linked glycosylation protein 1 homolog
  2. Beta-1,4-mannosyltransferase
  3. GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase
  4. GDP-mannose-dolichol diphosphochitobiose mannosyltransferase
  5. Mannosyltransferase-1
  6. MT-1
  7. hMat-1
Enzyme 57 Gene Name ALG1
Enzyme 57 Protein Sequence >Chitobiosyldiphosphodolichol beta-mannosyltransferase
MAASCLVLLALCLLLPLLLLGGWKRWRRGRAARHVVAVVLGDVGRSPRMQYHALSLAMHG
FSVTLLGFCNSKPHDELLQNNRIQIVGLTELQSLAVGPRVFQYGVKVVLQAMYLLWKLMW
REPGAYIFLQNPPGLPSIAVCWFVGCLCGSKLVIDWHNYGYSIMGLVHGPNHPLVLLAKW
YEKFFGRLSHLNLCVTNAMREDLADNWHIRAVTVYDKPASFFKETPLDLQHRLFMKLGSM
HSPFRARSEPEDPVTERSAFTERDAGSGLVTRLRERPALLVSSTSWTEDEDFSILLAALE
KFEQLTLDGHNLPSLVCVITGKGPLREYYSRLIHQKHFQHIQVCTPWLEAEDYPLLLGSA
DLGVCLHTSSSGLDLPMKVVDMFGCCLPVCAVNFKCLHELVKHEENGLVFEDSEELAAQL
QMLFSNFPDPAGKLNQFRKNLRESQQLRWDESWVQTVLPLVMDT
Enzyme 57 Number of Residues 464
Enzyme 57 Molecular Weight 52517.7
Enzyme 57 Theoretical pI 7.24
Enzyme 57 GO Classification
Function
Process
  • biosynthetic process
  • metabolic process
Component
Enzyme 57 General Function Involved in biosynthetic process
Enzyme 57 Specific Function Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER
Enzyme 57 Pathways
Enzyme 57 Reactions
  • GDP-mannose + chitobiosyldiphosphodolichol = GDP + beta-(1->4)-D-mannosylchitobiosyldiphosphodolichol [RN:R04502 R05972]
Enzyme 57 Pfam Domain Function
Enzyme 57 Signals
  • None
Enzyme 57 Transmembrane Regions
  • 3-23
Enzyme 57 Essentiality Not Available
Enzyme 57 GenBank ID Protein 6970470 Link Image
Enzyme 57 UniProtKB/Swiss-Prot ID Q9BT22 Link Image
Enzyme 57 UniProtKB/Swiss-Prot Entry Name ALG1_HUMAN Link Image
Enzyme 57 PDB ID Not Available
Enzyme 57 Cellular Location Not Available
Enzyme 57 Gene Sequence >1395 bp
ATGGCGGCCTCATGCTTGGTCCTGCTGGCGCTGTGTCTGCTGCTGCCGCTGCTGCTGCTG
GGAGGATGGAAGCGCTGGCGCCGGGGGCGGGCGGCCCGGCATGTAGTAGCGGTGGTGCTG
GGCGACGTGGGCCGCAGCCCCCGTATGCAGTACCACGCGCTGTCGTTGGCCATGCACGGC
TTCTCGGTGACCCTCCTGGGGTTCTGCAACTCCAAACCCCATGATGAGCTCTTGCAGAAC
AACAGAATTCAGATTGTGGGGTTGACAGAACTTCAGAGTCTTGCAGTTGGGCCCCGAGTT
TTCCAGTACGGAGTCAAAGTTGTACTTCAGGCTATGTACTTGCTGTGGAAGTTGATGTGG
AGGGAGCCAGGTGCCTATATCTTTCTCCAGAACCCCCCAGGTCTGCCTAGCATTGCTGTC
TGCTGGTTCGTGGGCTGCCTTTGTGGAAGCAAGCTCGTCATTGACTGGCACAACTATGGC
TACTCCATCATGGGTCTGGTGCATGGCCCCAACCATCCCCTCGTTCTGCTGGCCAAGTGG
TACGAGAAGTTCTTTGGGCGCCTGTCCCACCTGAACCTGTGTGTTACCAATGCTATGCGA
GAAGACCTGGCGGATAACTGGCACATCAGGGCTGTGACCGTCTACGACAAGCCCGCATCT
TTCTTTAAAGAGACACCTCTGGACCTGCAGCACCGGCTCTTCATGAAGCTGGGCAGCATG
CACTCTCCGTTCAGGGCCCGCTCAGAACCTGAGGACCCAGTCACGGAGCGGTCGGCCTTC
ACGGAGCGGGATGCTGGGAGCGGGCTGGTGACGCGTCTCCGTGAGCGGCCAGCCCTGCTG
GTCAGCAGCACGAGCTGGACAGAGGACGAAGACTTCTCCATCCTGCTGGCAGCTTTAGAA
AAGTTTGAACAACTGACTCTTGATGGACACAACCTTCCTTCTCTCGTCTGTGTGATAACA
GGCAAAGGGCCTCTGAGGGAGTATTATAGCCGCCTCATCCACCAGAAGCACTTCCAGCAC
ATCCAGGTCTGCACCCCCTGGCTGGAGGCCGAGGACTACCCCCTGCTTCTAGGGTCGGCG
GACCTGGGTGTCTGTCTGCACACGTCCTCCAGTGGCCTGGACCTGCCCATGAAGGTGGTG
GACATGTTCGGGTGCTGTTTGCCTGTGTGTGCTGTGAACTTCAAGTGTTTACATGAGCTG
GTGAAACATGAAGAAAATGGCCTGGTCTTTGAGGACTCAGAGGAACTGGCAGCTCAGCTG
CAGATGCTTTTCTCAAACTTTCCTGATCCTGCGGGCAAGCTAAACCAGTTCCGGAAGAAC
CTGCGGGAGTCGCAGCAGCTCCGATGGGATGAGAGCTGGGTGCAGACTGTGCTCCCTTTG
GTTATGGACACATAA
Enzyme 57 GenBank Gene ID AB019038 Link Image
Enzyme 57 GeneCard ID ALG1 Link Image
Enzyme 57 GenAtlas ID ALG1 Link Image
Enzyme 57 HGNC ID HGNC:18294 Link Image
Enzyme 57 Chromosome Location 1
Enzyme 57 Locus 16p13.3
Enzyme 57 SNPs SNPJam Report Link Image
Enzyme 57 General References
  1. Takahashi T, Honda R, Nishikawa Y: Cloning of the human cDNA which can complement the defect of the yeast mannosyltransferase I-deficient mutant alg 1. Glycobiology. 2000 Mar;10(3):321-7. [PubMed Link Image]
  2. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  5. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  6. Schwarz M, Thiel C, Lubbehusen J, Dorland B, de Koning T, von Figura K, Lehle L, Korner C: Deficiency of GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase causes congenital disorder of glycosylation type Ik. Am J Hum Genet. 2004 Mar;74(3):472-81. Epub 2004 Feb 16. [PubMed Link Image]
  7. Kranz C, Denecke J, Lehle L, Sohlbach K, Jeske S, Meinhardt F, Rossi R, Gudowius S, Marquardt T: Congenital disorder of glycosylation type Ik (CDG-Ik): a defect of mannosyltransferase I. Am J Hum Genet. 2004 Mar;74(3):545-51. Epub 2004 Feb 17. [PubMed Link Image]
  8. Grubenmann CE, Frank CG, Hulsmeier AJ, Schollen E, Matthijs G, Mayatepek E, Berger EG, Aebi M, Hennet T: Deficiency of the first mannosylation step in the N-glycosylation pathway causes congenital disorder of glycosylation type Ik. Hum Mol Genet. 2004 Mar 1;13(5):535-42. Epub 2004 Jan 6. [PubMed Link Image]
Enzyme 57 Metabolite References Not Available
Enzyme 58 [top]
Enzyme 58 ID 7906
Enzyme 58 Name Guanine nucleotide-binding protein G(t) subunit alpha-1
Enzyme 58 Synonyms
  1. Transducin alpha-1 chain
Enzyme 58 Gene Name GNAT1
Enzyme 58 Protein Sequence >Guanine nucleotide-binding protein G(t) subunit alpha-1
MGAGASAEEKHSRELEKKLKEDAEKDARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLE
ECLEFIAIIYGNTLQSILAIVRAMTTLNIQYGDSARQDDARKLMHMADTIEEGTMPKEMS
DIIQRLWKDSGIQACFERASEYQLNDSAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGI
IETQFSFKDLNFRMFDVGGQRSERKKWIHCFEGVTCIIFIAALSAYDMVLVEDDEVNRMH
ESLHLFNSICNHRYFATTSIVLFLNKKDVFFEKIKKAHLSICFPDYDGPNTYEDAGNYIK
VQFLELNMRRDVKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF
Enzyme 58 Number of Residues 350
Enzyme 58 Molecular Weight 40040.4
Enzyme 58 Theoretical pI 5.32
Enzyme 58 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • molecular transducer activity
  • nucleotide binding
  • purine nucleotide binding
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • biological regulation
  • cell surface receptor linked signaling pathway
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 58 General Function Involved in signal transducer activity
Enzyme 58 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase
Enzyme 58 Pathways Not Available
Enzyme 58 Reactions Not Available
Enzyme 58 Pfam Domain Function
Enzyme 58 Signals
  • None
Enzyme 58 Transmembrane Regions
  • None
Enzyme 58 Essentiality Not Available
Enzyme 58 GenBank ID Protein 31865 Link Image
Enzyme 58 UniProtKB/Swiss-Prot ID P11488 Link Image
Enzyme 58 UniProtKB/Swiss-Prot Entry Name GNAT1_HUMAN Link Image
Enzyme 58 PDB ID 1TND Link Image
Enzyme 58 PDB File Show
Enzyme 58 3D Structure
Enzyme 58 Cellular Location Not Available
Enzyme 58 Gene Sequence >1053 bp
ATGGGGGCTGGGGCCAGTGCTGAGGAGAAGCACTCCAGGGAGCTGGAAAAGAAGCTGAAA
GAGGACGCTGAGAAGGATGCTCGAACCGTGAAGCTGCTGCTTCTGGGTGCCGGTGAGTCC
GGGAAGAGCACCATCGTCAAGCAGATGAAGATTATCCACCAGGACGGGTACTCGCTGGAA
GAGTGCCTCGAGTTTATCGCCATCATCTACGGCAACACGTTGCAGTCCATCCTGGCCATC
GTACGCGCCATGACCACACTCAACATCCAGTACGGAGACTCTGCACGCCAGGACGACGCC
CGGAAGCTGATGCACATGGCAGACACTATCGAGGAGGGCACGATGCCCAAGGAGATGTCG
GACATCATCCAGCGGCTGTGGAAGGACTCCGGTATCCAGGCCTGTTTTGAGCGCGCCTCG
GAGTACCAGCTCAACGACTCGGCGGGCTACTACCTCTCCGACCTGGAGCGCCTGGTAACC
CCGGGCTACGTGCCCACCGAGCAGGACGTGCTGCGCTCGCGAGTCAAGACCACTGGCATC
ATCGAGACGCAGTTCTCCTTCAAGGATCTCAACTTCCGGATGTTCGATGTGGGCGGGCAG
CGCTCGGAGCCGAAGAAGTGGATCCACTGCTTCGAGGGCGTGACCTGCATCATCTTCATC
GCGGCGCTGACCGCGTACGACATGGTGCTAGTGGAGGACGACGAAGTGAACCGCATGCAC
GAGAGCCTGCACCTGTTCAACAGCATCTGCAACCACCGCTACTTCGCCACGACGTCCATC
GTGCTCTTCCTTAACAAGAAGGACGTCTTCTTCGAGAAGGTCAAGAAGGCGCACCTCAGC
ATCTGTTTCCCGGACTACGATGGACCCAACACCTACGAGGACGCCGGCAACTACATCAAG
GTGCAGTTCCTCGAGCTCAACATGCGGCGCGACGTGAAGGAGATCTATTCCCACATGACG
TGCGCCACCGACACGCAGAACGTCAAATTCTGCTTCGACGCTGTCACCGACATCATCATC
AAGGAGAACCTCAAAGACTGTGGCCTCTTCTGA
Enzyme 58 GenBank Gene ID X15088 Link Image
Enzyme 58 GeneCard ID GNAT1 Link Image
Enzyme 58 GenAtlas ID GNAT1 Link Image
Enzyme 58 HGNC ID HGNC:4393 Link Image
Enzyme 58 Chromosome Location 3
Enzyme 58 Locus 3p21
Enzyme 58 SNPs SNPJam Report Link Image
Enzyme 58 General References
  1. Fong SL: Characterization of the human rod transducin alpha-subunit gene. Nucleic Acids Res. 1992 Jun 11;20(11):2865-70. [PubMed Link Image]
  2. Lerea CL, Bunt-Milam AH, Hurley JB: Alpha transducin is present in blue-, green-, and red-sensitive cone photoreceptors in the human retina. Neuron. 1989 Sep;3(3):367-76. [PubMed Link Image]
  3. Van Dop C, Medynski DC, Apone LM: Nucleotide sequence for a cDNA encoding the alpha subunit of retinal transducin (GNAT1) isolated from the human eye. Nucleic Acids Res. 1989 Jun 26;17(12):4887. [PubMed Link Image]
  4. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Bell MW, Desai N, Guo XX, Ghalayini AJ: Tyrosine phosphorylation of the alpha subunit of transducin and its association with Src in photoreceptor rod outer segments. J Neurochem. 2000 Nov;75(5):2006-19. [PubMed Link Image]
  7. Dryja TP, Hahn LB, Reboul T, Arnaud B: Missense mutation in the gene encoding the alpha subunit of rod transducin in the Nougaret form of congenital stationary night blindness. Nat Genet. 1996 Jul;13(3):358-60. [PubMed Link Image]
Enzyme 58 Metabolite References Not Available
Enzyme 59 [top]
Enzyme 59 ID 8075
Enzyme 59 Name Uridine-cytidine kinase 2
Enzyme 59 Synonyms
  1. UCK 2
  2. Cytidine monophosphokinase 2
  3. Testis-specific protein TSA903
  4. Uridine monophosphokinase 2
Enzyme 59 Gene Name UCK2
Enzyme 59 Protein Sequence >Uridine-cytidine kinase 2
MAGDSEQTLQNHQQPNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQNEVDYRQKQVVILS
QDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELILKTLKEITEGKTVQIPVYDFVSHSRK
EETVTVYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ
ILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNGGPSKRQTNG
CLNGYTPSRKRQASESSSRPH
Enzyme 59 Number of Residues 261
Enzyme 59 Molecular Weight 29298.9
Enzyme 59 Theoretical pI 6.68
Enzyme 59 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolic process
Component
Enzyme 59 General Function Involved in ATP binding
Enzyme 59 Specific Function Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and N(4)-anisoylcytidine
Enzyme 59 Pathways
Enzyme 59 Reactions
  • ATP + uridine = ADP + UMP [RN:R00964]
Enzyme 59 Pfam Domain Function
Enzyme 59 Signals
  • None
Enzyme 59 Transmembrane Regions
  • None
Enzyme 59 Essentiality Not Available
Enzyme 59 GenBank ID Protein 18699734 Link Image
Enzyme 59 UniProtKB/Swiss-Prot ID Q9BZX2 Link Image
Enzyme 59 UniProtKB/Swiss-Prot Entry Name UCK2_HUMAN Link Image
Enzyme 59 PDB ID 1XRJ Link Image
Enzyme 59 PDB File Show
Enzyme 59 3D Structure
Enzyme 59 Cellular Location Not Available
Enzyme 59 Gene Sequence >786 bp
ATGGCCGGGGACAGCGAGCAGACCCTGCAGAACCACCAGCAGCCCAACGGCGGCGAGCCC
TTCCTTATAGGCGTCAGCGGGGGAACAGCTAGCGGCAAGTCTTCCGTGTGTGCTAAGATC
GTGCAGCTCCTGGGGCAGAATGAGGTGGACTATCGCCAGAAGCAGGTGGTCATCCTGAGC
CAGGATAGCTTCTACCGTGTCCTTACCTCGGAGCAGAAGGCCAAAGCCCTGAAGGGCCAG
TTCAACTTTGACCACCCGGATGCCTTTGACAATGAACTCATTCTCAAAACACTCAAAGAA
ATCACTGAAGGGAAAACAGTCCAGATCCCCGTGTATGACTTTGTCTCCCATTCCCGGAAG
GAGGAGACAGTTACTGTCTATCCCGCAGACGTGGTGCTCTTTGAAGGGATCCTGGCCTTC
TACTCCCAGGAGGTACGAGACCTGTTCCAGATGAAGCTTTTTGTGGATACAGATGCGGAC
ACCCGGCTCTCACGCAGAGTATTAAGGGACATCAGCGAGAGAGGCAGGGATCTTGAGCAG
ATTTTATCTCAGTACATTACGTTCGTCAAGCCTGCCTTTGAGGAATTCTGCTTGCCAACA
AAGAAGTATGCTGATGTGATCATCCCTAGAGGTGCAGATAATCTGGTGGCCATCAACCTC
ATCGTGCAGCACATCCAGGACATCCTGAATGGAGGGCCCTCCAAACGGCAGACCAATGGC
TGTCTCAACGGCTACACCCCTTCACGCAAGAGGCAGGCATCGGAGTCCAGCAGCAGGCCG
CATTGA
Enzyme 59 GenBank Gene ID NM_012474.3 Link Image
Enzyme 59 GeneCard ID UCK2 Link Image
Enzyme 59 GenAtlas ID UCK2 Link Image
Enzyme 59 HGNC ID HGNC:12562 Link Image
Enzyme 59 Chromosome Location 1
Enzyme 59 Locus 1q23
Enzyme 59 SNPs SNPJam Report Link Image
Enzyme 59 General References
  1. Ozaki K, Kuroki T, Hayashi S, Nakamura Y: Isolation of three testis-specific genes (TSA303, TSA806, TSA903) by a differential mRNA display method. Genomics. 1996 Sep 1;36(2):316-9. [PubMed Link Image]
  2. Van Rompay AR, Norda A, Linden K, Johansson M, Karlsson A: Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases. Mol Pharmacol. 2001 May;59(5):1181-6. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Koizumi K, Shimamoto Y, Azuma A, Wataya Y, Matsuda A, Sasaki T, Fukushima M: Cloning and expression of uridine/cytidine kinase cDNA from human fibrosarcoma cells. Int J Mol Med. 2001 Sep;8(3):273-8. [PubMed Link Image]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  8. Suzuki NN, Koizumi K, Fukushima M, Matsuda A, Inagaki F: Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase. Structure. 2004 May;12(5):751-64. [PubMed Link Image]
  9. Appleby TC, Larson G, Cheney IW, Walker H, Wu JZ, Zhong W, Hong Z, Yao N: Structure of human uridine-cytidine kinase 2 determined by SIRAS using a rotating-anode X-ray generator and a single samarium derivative. Acta Crystallogr D Biol Crystallogr. 2005 Mar;61(Pt 3):278-84. Epub 2005 Feb 24. [PubMed Link Image]
Enzyme 59 Metabolite References Not Available
Enzyme 60 [top]
Enzyme 60 ID 8236
Enzyme 60 Name Protein ALEX
Enzyme 60 Synonyms
  1. Alternative gene product encoded by XL-exon
Enzyme 60 Gene Name GNAS
Enzyme 60 Protein Sequence >Protein ALEX
MMARPVDPQRSPDPTFRSSTRHSGKLEPMEATAHLLRKQCPSRLNSPAWEASGLHWSSLD
SPVGSMQALRPSAQHSWSPEPSVVPDQAWEDTALHQKKLCPLSLTSLPREAAVNFSYRSQ
TLLQEAQVLQGSPELLPRSPKPSGLQRLAPEEATALPLRRLCHLSLMEKDLGTTAHPRGF
PELSHKSTAAASSRQSRPRVRSASLPPRTRLPSGSQAPSAAHPKRLSDLLLTSRAAAPGW
RSPDPRSRLAAPPLGSTTLPSTWTAPQSRLTARPSRSPEPQIRESEQRDPQLRRKQQRWK
EPLMPRREEKYPLRGTDPLPPGQPQRIPLPGQPLQPQPILTPGQPQKIPTPGQHQPILTP
GHSQPIPTPGQPLPPQPIPTPGRPLTPQPIPTPGRPLTPQPIQMPGRPLRLPPPLRLLRP
GQPMSPQLRQTQGLPLPQPLLPPGQPKSAGRPLQPLPPGPDARSISDPPAPRSRLPIRLL
RGLLARLPGGASPRAAAAAACTTMKGWPAATMTPAETSPTMGPPDASAGFSIGEIAAAES
PSATYSATFSCKPSGAASVDLRVPSPKPRALSRSRRYPWRRSADRCAKKPWRSGPRSAQR
RNAVSSSTNNSRTKRWATCVRTACCF
Enzyme 60 Number of Residues 626
Enzyme 60 Molecular Weight 67947.1
Enzyme 60 Theoretical pI 12.07
Enzyme 60 GO Classification Not Available
Enzyme 60 General Function Not Available
Enzyme 60 Specific Function May inhibit the adenylyl cyclase-stimulating activity of guanine nucleotide-binding protein G(s) subunit alpha which is produced from the same locus in a different open reading frame
Enzyme 60 Pathways Not Available
Enzyme 60 Reactions Not Available
Enzyme 60 Pfam Domain Function Not Available
Enzyme 60 Signals
  • None
Enzyme 60 Transmembrane Regions
  • None
Enzyme 60 Essentiality Not Available
Enzyme 60 GenBank ID Protein 117938768 Link Image
Enzyme 60 UniProtKB/Swiss-Prot ID P84996 Link Image
Enzyme 60 UniProtKB/Swiss-Prot Entry Name ALEX_HUMAN Link Image
Enzyme 60 PDB ID Not Available
Enzyme 60 Cellular Location Not Available
Enzyme 60 Gene Sequence >1881 bp
ATGATGGCGAGGCCTGTGGACCCCCAGAGGTCTCCAGACCCAACTTTCAGGTCCTCAACC
CGGCATTCAGGGAAGCTGGAGCCCATGGAAGCTACAGCCCACCTCCTGAGGAAGCAATGC
CCTTCGAGGCTGAACAGCCCAGCTTGGGAGGCTTCTGGCCTACACTGGAGCAGCCTGGAT
TCCCCAGTGGGGTCCATGCAGGCCTTGAGGCCTTCGGCCCAGCACTCATGGAGCCCGGAG
CCTTCAGTGGTGCCAGACCAGGCCTGGGAGGATACAGCCCTCCACCAGAAGAAGCTATGC
CCTTTGAGTTTGACCAGCCTGCCCAGAGAGGCTGCAGTCAACTTCTCTTACAGGTCCCAG
ACCTTGCTCCAGGAGGCCCAGGTGCTGCAGGGGTCCCCGGAGCTCCTCCCGAGGAGCCCC
AAGCCCTCAGGCCTGCAAAGGCTGGCTCCAGAGGAGGCTACAGCCCTCCCCCTGAGGAGA
CTATGCCATTTGAGCTTGATGGAGAAGGATTTGGGGACGACAGCCCACCCCCGGGGCTTT
CCCGAGTTATCGCACAAGTCGACGGCAGCAGCCAGTTCGCGGCAGTCGCGGCCTCGAGTG
CGGTCCGCCTCACTCCCGCCGCGAACGCGCCTCCCCTCTGGGTCCCAGGCGCCATCGGCA
GCCCATCCCAAGAGGCTGTCAGACCTCCTTCTAACTTCACGGGCAGCAGCCCCTGGATGG
AGATCTCCGGACCCCCGTTCGAGATTGGCAGCGCCCCCGCTGGGGTCGACGACACTCCCG
TCAACATGGACAGCCCCCCAATCGCGCTTGACGGCCCGCCCATCAAGGTCTCCGGAGCCC
CAGATAAGAGAGAGCGAGCAGAGAGACCCCCAGTTGAGGAGGAAGCAGCAGAGATGGAAG
GAGCCGCTGATGCCGCGGAGGGAGGAAAAGTACCCTCTCCGGGGTACGGATCCCCTGCCG
CCGGGGCAGCCTCAGCGGATACCGCTGCCAGGGCAGCCCCTGCAGCCCCAGCCGATCCTG
ACTCCGGGGCAACCCCAGAAGATCCCGACTCCGGGACAGCACCAGCCGATCCTGACTCCG
GGGCATTCGCAGCCGATCCCGACTCCGGGGCAGCCCCTGCCGCCCCAGCCGATCCCGACT
CCGGGGCGGCCCCTGACGCCCCAGCCGATCCCGACTCCGGGGCGGCCCCTGACGCCCCAG
CCGATCCAGATGCCGGGGCGGCCCCTGAGGCTCCCGCCGCCCCTGCGGCTGCTGAGACCC
GGGCAGCCCATGTCGCCCCAGCTGCGCCAGACGCAGGGGCTCCCACTGCCCCAGCCGCTT
CTGCCACCCGGGCAGCCCAAGTCCGCCGGGCGGCCTCTGCAGCCCCTGCCTCCGGGGCCA
GACGCAAGATCCATCTCAGACCCCCCAGCCCCGAGATCCAGGCTGCCGATCCGCCTACTC
CGCGGCCTACTCGCGCGTCTGCCTGGCGGGGCAAGTCCGAGAGCAGCCGCGGCCGCCGCG
TGTACTACGATGAAGGGGTGGCCAGCAGCGACGATGACTCCAGCGGAGACGAGTCCGACG
ATGGGACCTCCGGATGCCTCCGCTGGTTTCAGCATCGGCGAAATCGCCGCCGCCGAAAGC
CCCAGCGCAACTTACTCCGCAACTTTCTCGTGCAAGCCTTCGGGGGCTGCTTCGGTCGAT
CTGAGAGTCCCCAGCCCAAAGCCTCGCGCTCTCTCAAGGTCAAGAAGGTACCCCTGGCGG
AGAAGCGCAGACAGATGCGCAAAGAAGCCCTGGAGAAGCGGGCCCAGAAGCGCGCAGAGA
AGAAACGCAGTAAGCTCATCGACAAACAACTCCAGGACGAAAAGATGGGCTACATGTGTA
CGCACCGCCTGCTGCTTCTAG
Enzyme 60 GenBank Gene ID NM_001077490.1 Link Image
Enzyme 60 GeneCard ID GNAS Link Image
Enzyme 60 GenAtlas ID GNAS Link Image
Enzyme 60 HGNC ID HGNC:4392 Link Image
Enzyme 60 Chromosome Location 2
Enzyme 60 Locus 20q13.3
Enzyme 60 SNPs SNPJam Report Link Image
Enzyme 60 General References
  1. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  2. Freson K, Jaeken J, Van Helvoirt M, de Zegher F, Wittevrongel C, Thys C, Hoylaerts MF, Vermylen J, Van Geet C: Functional polymorphisms in the paternally expressed XLalphas and its cofactor ALEX decrease their mutual interaction and enhance receptor-mediated cAMP formation. Hum Mol Genet. 2003 May 15;12(10):1121-30. [PubMed Link Image]
  3. Abramowitz J, Grenet D, Birnbaumer M, Torres HN, Birnbaumer L: XLalphas, the extra-long form of the alpha-subunit of the Gs G protein, is significantly longer than suspected, and so is its companion Alex. Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8366-71. Epub 2004 May 17. [PubMed Link Image]
  4. Liu J, Litman D, Rosenberg MJ, Yu S, Biesecker LG, Weinstein LS: A GNAS1 imprinting defect in pseudohypoparathyroidism type IB. J Clin Invest. 2000 Nov;106(9):1167-74. [PubMed Link Image]
  5. Bastepe M, Lane AH, Juppner H: Paternal uniparental isodisomy of chromosome 20q--and the resulting changes in GNAS1 methylation--as a plausible cause of pseudohypoparathyroidism. Am J Hum Genet. 2001 May;68(5):1283-9. Epub 2001 Apr 9. [PubMed Link Image]
  6. Wu WI, Schwindinger WF, Aparicio LF, Levine MA: Selective resistance to parathyroid hormone caused by a novel uncoupling mutation in the carboxyl terminus of G alpha(s). A cause of pseudohypoparathyroidism type Ib. J Biol Chem. 2001 Jan 5;276(1):165-71. [PubMed Link Image]
  7. Jan de Beur S, Ding C, Germain-Lee E, Cho J, Maret A, Levine MA: Discordance between genetic and epigenetic defects in pseudohypoparathyroidism type 1b revealed by inconsistent loss of maternal imprinting at GNAS1. Am J Hum Genet. 2003 Aug;73(2):314-22. Epub 2003 Jul 11. [PubMed Link Image]
  8. Fragoso MC, Domenice S, Latronico AC, Martin RM, Pereira MA, Zerbini MC, Lucon AM, Mendonca BB: Cushing's syndrome secondary to adrenocorticotropin-independent macronodular adrenocortical hyperplasia due to activating mutations of GNAS1 gene. J Clin Endocrinol Metab. 2003 May;88(5):2147-51. [PubMed Link Image]
  9. Bastepe M, Frohlich LF, Hendy GN, Indridason OS, Josse RG, Koshiyama H, Korkko J, Nakamoto JM, Rosenbloom AL, Slyper AH, Sugimoto T, Tsatsoulis A, Crawford JD, Juppner H: Autosomal dominant pseudohypoparathyroidism type Ib is associated with a heterozygous microdeletion that likely disrupts a putative imprinting control element of GNAS. J Clin Invest. 2003 Oct;112(8):1255-63. [PubMed Link Image]
  10. Linglart A, Gensure RC, Olney RC, Juppner H, Bastepe M: A novel STX16 deletion in autosomal dominant pseudohypoparathyroidism type Ib redefines the boundaries of a cis-acting imprinting control element of GNAS. Am J Hum Genet. 2005 May;76(5):804-14. Epub 2005 Mar 30. [PubMed Link Image]
  11. Bastepe M, Frohlich LF, Linglart A, Abu-Zahra HS, Tojo K, Ward LM, Juppner H: Deletion of the NESP55 differentially methylated region causes loss of maternal GNAS imprints and pseudohypoparathyroidism type Ib. Nat Genet. 2005 Jan;37(1):25-7. Epub 2004 Dec 12. [PubMed Link Image]
  12. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 60 Metabolite References Not Available
Enzyme 61 [top]
Enzyme 61 ID 8268
Enzyme 61 Name Rap guanine nucleotide exchange factor 3
Enzyme 61 Synonyms
  1. Exchange factor directly activated by cAMP 1
  2. Exchange protein directly activated by cAMP 1
  3. EPAC 1
  4. Rap1 guanine-nucleotide-exchange factor directly activated by cAMP
  5. cAMP-regulated guanine nucleotide exchange factor I
  6. cAMP-GEFI
Enzyme 61 Gene Name RAPGEF3
Enzyme 61 Protein Sequence >Rap guanine nucleotide exchange factor 3
MKVGWPGESCWQVGLAVEDSPALGAPRVGALPDVVPEGTLLNMVLRRMHRPRSCSYQLLL
EHQRPSCIQGLRWTPLTNSEESLDFSESLEQASTERVLRAGRQLHRHLLATCPNLIRDRK
YHLRLYRQCCSGRELVDGILALGLGVHSRSQVVGICQVLLDEGALCHVKHDWAFQDRDAQ
FYRFPGPEPEPVGTHEMEEELAEAVALLSQRGPDALLTVALRKPPGQRTDEELDLIFEEL
LHIKAVAHLSNSVKRELAAVLLFEPHSKAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKGL
VTTLHEGDDFGQLALVNDAPRAATIILREDNCHFLRVDKQDFNRIIKDVEAKTMRLEEHG
KVVLVLERASQGAGPSRPPTPGRNRYTVMSGTPEKILELLLEAMGPDSSAHDPTETFLSD
FLLTHRVFMPSAQLCAALLHHFHVEPAGGSEQERSTYVCNKRQQILRLVSQWVALYGSML
HTDPVATSFLQKLSDLVGRDTRLSNLLREQWPERRRCHRLENGCGNASPQMKARNLPVWL
PNQDEPLPGSSCAIQVGDKVPYDICRPDHSVLTLQLPVTASVREVMAALAQEDGWTKGQV
LVKVNSAGDAIGLQPDARGVATSLGLNERLFVVNPQEVHELIPHPDQLGPTVGSAEGLDL
VSAKDLAGQLTDHDWSLFNSIHQVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVAT
ELCLCPVPGPRAQLLRKFIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKV
RKLYSALERLLDPSWNHRVYRLALAKLSPPVIPFMPLLLKDMTFIHEGNHTLVENLINFE
KMRMMARAARMLHHCRSHNPVPLSPLRSRVSHLHEDSQVARISTCSEQSLSTRSPASTWA
YVQQLKVIDNQRELSRLSRELEP
Enzyme 61 Number of Residues 923
Enzyme 61 Molecular Weight 103651.0
Enzyme 61 Theoretical pI 7.49
Enzyme 61 GO Classification
Function
  • GTPase regulator activity
  • cAMP-dependent protein kinase regulator activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • kinase regulator activity
  • nucleoside-triphosphatase regulator activity
  • protein kinase regulator activity
Process
  • biological regulation
  • intracellular signal transduction
  • intracellular signaling pathway
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular metabolic process
  • regulation of cellular process
  • regulation of cellular protein metabolic process
  • regulation of metabolic process
  • regulation of protein amino acid phosphorylation
  • regulation of protein modification process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • signaling
  • signaling pathway
  • small GTPase mediated signal transduction
Component
  • cAMP-dependent protein kinase complex
  • cell part
  • intracellular
  • macromolecular complex
  • protein complex
Enzyme 61 General Function Involved in cAMP-dependent protein kinase regulator activity
Enzyme 61 Specific Function Guanine nucleotide exchange factor (GEF) for RAP1A and RAP2A small GTPases that is activated by binding cAMP
Enzyme 61 Pathways Not Available
Enzyme 61 Reactions Not Available
Enzyme 61 Pfam Domain Function
Enzyme 61 Signals
  • None
Enzyme 61 Transmembrane Regions
  • None
Enzyme 61 Essentiality Not Available
Enzyme 61 GenBank ID Protein 148747859 Link Image
Enzyme 61 UniProtKB/Swiss-Prot ID O95398 Link Image
Enzyme 61 UniProtKB/Swiss-Prot Entry Name RPGF3_HUMAN Link Image
Enzyme 61 PDB ID Not Available
Enzyme 61 Cellular Location Not Available
Enzyme 61 Gene Sequence >2772 bp
ATGAAGGTGGGCTGGCCAGGTGAGAGCTGCTGGCAGGTGGGCCTGGCTGTGGAGGATAGC
CCAGCTCTGGGAGCACCGCGGGTGGGAGCCCTCCCTGACGTGGTGCCGGAGGGGACACTA
CTCAACATGGTGTTGAGAAGGATGCACCGGCCCCGAAGCTGCTCCTACCAGCTGCTGCTG
GAGCACCAGCGTCCGAGCTGCATCCAGGGGCTGCGCTGGACACCACTCACCAACAGCGAG
GAGTCCCTGGATTTCAGCGAGAGCCTGGAGCAGGCCTCCACAGAGCGGGTGCTCAGGGCT
GGGAGGCAGCTGCATCGGCATCTGCTGGCCACCTGCCCAAACCTCATCCGAGACCGGAAG
TACCACCTTAGGCTCTATCGGCAGTGCTGCTCTGGCCGGGAGCTGGTGGATGGGATCTTG
GCCCTGGGACTTGGGGTCCATTCCCGGAGCCAAGTTGTGGGAATCTGCCAGGTGCTGCTG
GATGAAGGTGCCCTCTGCCATGTGAAACACGACTGGGCCTTCCAGGACCGAGATGCCCAA
TTCTACCGGTTCCCCGGGCCCGAGCCCGAGCCCGTGGGAACTCATGAGATGGAGGAGGAG
TTGGCCGAAGCTGTGGCCCTGCTCTCCCAGCGGGGGCCTGACGCCCTGCTCACTGTGGCA
CTTCGAAAGCCCCCAGGTCAGCGCACGGATGAAGAGCTGGACCTCATCTTTGAGGAGCTG
CTGCACATCAAGGCTGTGGCCCACCTCTCCAACTCGGTGAAGCGAGAATTAGCGGCTGTT
CTGCTCTTTGAACCACACAGCAAGGCAGGGACCGTGTTGTTCAGCCAGGGGGACAAGGGC
ACTTCGTGGTACATTATCTGGAAGGGATCTGTCAACGTGGTGACCCATGGCAAGGGGCTG
GTGACCACCCTGCATGAGGGAGATGATTTTGGACAGCTGGCTCTGGTGAATGATGCACCC
CGGGCAGCCACCATCATCCTGCGAGAAGACAACTGTCATTTCCTGCGTGTGGACAAGCAG
GACTTCAACCGTATCATCAAGGATGTGGAGGCAAAGACCATGCGGCTGGAAGAACATGGC
AAAGTGGTGCTGGTGCTGGAGAGAGCCTCTCAGGGCGCCGGCCCTTCCCGACCCCCAACC
CCAGGCAGGAACCGGTATACAGTGATGTCTGGCACCCCAGAGAAGATCCTAGAGCTTCTG
TTGGAGGCCATGGGACCAGATTCCAGTGCTCATGACCCAACAGAGACATTCCTCAGCGAC
TTCCTCCTGACCCACAGGGTCTTCATGCCCAGCGCCCAACTCTGCGCTGCCCTTCTGCAC
CACTTCCATGTGGAGCCTGCGGGTGGCAGCGAGCAGGAGCGCAGCACCTACGTCTGCAAC
AAGAGGCAGCAGATCTTGCGGCTGGTCAGCCAGTGGGTGGCCCTGTATGGCTCCATGCTC
CACACTGACCCTGTGGCCACCAGCTTCCTCCAGAAACTCTCAGACCTGGTGGGCAGGGAC
ACCCGACTCAGCAACCTGCTGAGGGAGCAGTGGCCAGAGAGGCGGCGATGCCACAGGTTG
GAGAATGGCTGTGGGAATGCATCTCCTCAGATGAAGGCCCGGAACTTGCCTGTTTGGCTC
CCCAACCAGGACGAGCCCCTTCCTGGCAGCAGCTGTGCCATCCAAGTTGGGGATAAAGTC
CCCTATGACATCTGCCGGCCAGACCACTCAGTGTTGACCCTGCAGCTGCCTGTGACAGCC
TCCGTGAGAGAGGTGATGGCAGCGTTGGCCCAGGAGGATGGCTGGACCAAGGGGCAGGTG
CTGGTGAAGGTCAATTCTGCAGGTGATGCCATTGGCCTGCAGCCAGATGCCCGTGGTGTG
GCCACATCTCTGGGGCTCAATGAGCGTCTCTTTGTTGTCAACCCACAGGAAGTGCATGAG
CTGATCCCACACCCTGACCAGCTGGGGCCCACTGTGGGCTCTGCTGAGGGGCTGGACCTG
GTGAGTGCCAAGGACCTGGCAGGCCAGCTGACGGACCACGACTGGAGCCTCTTCAACAGT
ATCCACCAGGTGGAGCTGATCCACTATGTGCTGGGCCCCCAGCATCTGCGGGATGTCACC
ACCGCCAACCTGGAGCGCTTCATGCGCCGCTTCAATGAGCTGCAGTACTGGGTGGCCACC
GAGCTGTGTCTCTGCCCCGTGCCCGGCCCCCGGGCCCAGCTGCTCAGGAAGTTCATTAAG
CTGGCGGCCCACCTCAAGGAGCAGAAGAATCTCAATTCCTTCTTTGCCGTCATGTTTGGC
CTCAGCAACTCGGCCATCAGCCGCCTAGCCCACACCTGGGAGCGGCTGCCTCACAAAGTC
CGGAAGCTGTACTCCGCCCTCGAGAGGCTGCTGGATCCCTCATGGAACCACCGGGTATAC
CGACTGGCCCTCGCCAAGCTCTCCCCTCCTGTCATCCCCTTCATGCCCCTTCTTCTCAAA
GACATGACCTTCATTCATGAGGGAAACCACACACTAGTGGAGAATCTCATCAACTTTGAG
AAGATGAGAATGATGGCCAGAGCCGCGCGGATGCTGCACCACTGCCGAAGCCACAACCCT
GTGCCTCTCTCACCACTCAGAAGCCGAGTTTCCCACCTCCACGAGGACAGCCAGGTGGCG
AGGATTTCCACATGCTCGGAGCAGTCCCTGAGCACCCGGAGTCCAGCCAGCACCTGGGCT
TATGTCCAGCAGCTGAAGGTCATTGACAACCAGCGGGAACTCTCCCGCCTCTCCCGAGAG
CTGGAGCCATGA
Enzyme 61 GenBank Gene ID NM_001098531.2 Link Image
Enzyme 61 GeneCard ID RAPGEF3 Link Image
Enzyme 61 GenAtlas ID RAPGEF3 Link Image
Enzyme 61 HGNC ID HGNC:16629 Link Image
Enzyme 61 Chromosome Location 1
Enzyme 61 Locus 12q13.1
Enzyme 61 SNPs SNPJam Report Link Image
Enzyme 61 General References
  1. Kawasaki H, Springett GM, Mochizuki N, Toki S, Nakaya M, Matsuda M, Housman DE, Graybiel AM: A family of cAMP-binding proteins that directly activate Rap1. Science. 1998 Dec 18;282(5397):2275-9. [PubMed Link Image]
  2. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. de Rooij J, Zwartkruis FJ, Verheijen MH, Cool RH, Nijman SM, Wittinghofer A, Bos JL: Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP. Nature. 1998 Dec 3;396(6710):474-7. [PubMed Link Image]
  5. de Rooij J, Rehmann H, van Triest M, Cool RH, Wittinghofer A, Bos JL: Mechanism of regulation of the Epac family of cAMP-dependent RapGEFs. J Biol Chem. 2000 Jul 7;275(27):20829-36. [PubMed Link Image]
  6. Rehmann H, Prakash B, Wolf E, Rueppel A, de Rooij J, Bos JL, Wittinghofer A: Structure and regulation of the cAMP-binding domains of Epac2. Nat Struct Biol. 2003 Jan;10(1):26-32. [PubMed Link Image]
Enzyme 61 Metabolite References Not Available
Enzyme 62 [top]
Enzyme 62 ID 8354
Enzyme 62 Name Lysophosphatidic acid receptor 2
Enzyme 62 Synonyms
  1. LPA receptor 2
  2. LPA-2
  3. Lysophosphatidic acid receptor Edg-4
Enzyme 62 Gene Name LPAR2
Enzyme 62 Protein Sequence >Lysophosphatidic acid receptor 2
MVIMGQCYYNETIGFFYNNSGKELSSHWRPKDVVVVALGLTVSVLVLLTNLLVIAAIASN
RRFHQPIYYLLGNLAAADLFAGVAYLFLMFHTGPRTARLSLEGWFLRQGLLDTSLTASVA
TLLAIAVERHRSVMAVQLHSRLPRGRVVMLIVGVWVAALGLGLLPAHSWHCLCALDRCSR
MAPLLSRSYLAVWALSSLLVFLLMVAVYTRIFFYVRRRVQRMAEHVSCHPRYRETTLSLV
KTVVIILGAFVVCWTPGQVVLLLDGLGCESCNVLAVEKYFLLLAEANSLVNAAVYSCRDA
EMRRTFRRLLCCACLRQSTRESVHYTSSAQGGASTRIMLPENGHPLMDSTL
Enzyme 62 Number of Residues 351
Enzyme 62 Molecular Weight 39083.8
Enzyme 62 Theoretical pI 9.42
Enzyme 62 GO Classification
Function
  • G-protein coupled receptor activity
  • bioactive lipid receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 62 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 62 Specific Function Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. Seems to be coupled to the G(i)/G(o), G(12)/G(13), and G(q) families of heteromeric G proteins. Plays a key role in phospholipase C-beta (PLC-beta) signaling pathway. Stimulates phospholipase C (PLC) activity in a manner that is independent of RALA activation
Enzyme 62 Pathways Not Available
Enzyme 62 Reactions Not Available
Enzyme 62 Pfam Domain Function
Enzyme 62 Signals
  • None
Enzyme 62 Transmembrane Regions
  • 34-54 70-90 104-126 147-167 189-209 243-263 280-297
Enzyme 62 Essentiality Not Available
Enzyme 62 GenBank ID Protein 2213635 Link Image
Enzyme 62 UniProtKB/Swiss-Prot ID Q9HBW0 Link Image
Enzyme 62 UniProtKB/Swiss-Prot Entry Name LPAR2_HUMAN Link Image
Enzyme 62 PDB ID Not Available
Enzyme 62 Cellular Location Not Available
Enzyme 62 Gene Sequence >1056 bp
ATGGTCATCATGGGCCAGTGCTACTACAACGAGACCATCGGCTTCTTCTATAACAACAGT
GGCAAAGAGCTCAGCTCCCACTGGCGGCCCAAGGATGTGGTCGTGGTGGCACTGGGGCTG
ACCGTCAGCGTGCTGGTGCTGCTGACCAATCTGCTGGTCATAGCAGCCATCGCCTCCAAC
CGCCGCTTCCACCAGCCCATCTACTACCTGCTCGGCAATCTGGCCGCGGCTGACCTCTTC
GCGGGCGTGGCCTACCTCTTCCTCATGTTCCACACTGGTCCCCGCACAGCCCGACTTTCA
CTTGAGGGCTGGTTCCTGCGGCAGGGCTTGCTGGACACAAGCCTCACTGCGTCGGTGGCC
ACACTGCTGGCCATCGCCGTGGAGCGGCACCGCAGTGTGATGGCCGTGCAGCTGCACAGC
CGCCTGCCCCGTGGCCGCGTGGTCATGCTCATTGTGGGCGTGTGGGTGGCTGCCCTGGGC
CTGGGGCTGCTGCCTGCCCACTCCTGGCACTGCCTCTGTGCCCTGGACCGCTGCTCACGC
ATGGCACCCCTGCTCAGCCGCTCCTATTTGGCCGTCTGGGCTCTGTCGAGCCTGCTTGTC
TTCCTGCTCATGGTGGCTGTGTACACCCGCATTTTCTTCTACGTGCGGCGGCGAGTGCAG
CGCATGGCAGAGCATGTCAGCTGCCACCCCCGCTACCGAGAGACCACGCTCAGCCTGGTC
AAGACTGTTGTCATCATCCTGGGGGCGTTCGTGGTCTGCTGGACACCAGGCCAGGTGGTA
CTGCTCCTGGATGGTTTAGGCTGTGAGTCCTGCAATGTCCTGGCTGTAGAAAAGTACTTC
CTACTGTTGGCCGAGGCCAACTCACTGGTCAATGCTGCTGTGTACTCTTGCCGAGATGCT
GAGATGCGCCGCACCTTCCGCCGCCTTCTCTGCTGCGCGTGCCTCCGCCAGTCCACCCGC
GAGTCTGTCCACTATACATCCTCTGCCCAGGGAGGTGCCAGCACTCGCATCATGCTTCCC
GAGAACGGCCACCCACTGATGGACTCCACCCTTTAG
Enzyme 62 GenBank Gene ID AC002306 Link Image
Enzyme 62 GeneCard ID LPAR2 Link Image
Enzyme 62 GenAtlas ID LPAR2 Link Image
Enzyme 62 HGNC ID HGNC:3168 Link Image
Enzyme 62 Chromosome Location 1
Enzyme 62 Locus 19p12
Enzyme 62 SNPs SNPJam Report Link Image
Enzyme 62 General References
  1. An S, Bleu T, Hallmark OG, Goetzl EJ: Characterization of a novel subtype of human G protein-coupled receptor for lysophosphatidic acid. J Biol Chem. 1998 Apr 3;273(14):7906-10. [PubMed Link Image]
  2. Bandoh K, Aoki J, Taira A, Tsujimoto M, Arai H, Inoue K: Lysophosphatidic acid (LPA) receptors of the EDG family are differentially activated by LPA species. Structure-activity relationship of cloned LPA receptors. FEBS Lett. 2000 Jul 28;478(1-2):159-65. [PubMed Link Image]
  3. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Contos JJ, Ishii I, Chun J: Lysophosphatidic acid receptors. Mol Pharmacol. 2000 Dec;58(6):1188-96. [PubMed Link Image]
  6. Contos JJ, Chun J: Genomic characterization of the lysophosphatidic acid receptor gene, lp(A2)/Edg4, and identification of a frameshift mutation in a previously characterized cDNA. Genomics. 2000 Mar 1;64(2):155-69. [PubMed Link Image]
  7. Oh YS, Jo NW, Choi JW, Kim HS, Seo SW, Kang KO, Hwang JI, Heo K, Kim SH, Kim YH, Kim IH, Kim JH, Banno Y, Ryu SH, Suh PG: NHERF2 specifically interacts with LPA2 receptor and defines the specificity and efficiency of receptor-mediated phospholipase C-beta3 activation. Mol Cell Biol. 2004 Jun;24(11):5069-79. [PubMed Link Image]
  8. Zhang H, Wang D, Sun H, Hall RA, Yun CC: MAGI-3 regulates LPA-induced activation of Erk and RhoA. Cell Signal. 2007 Feb;19(2):261-8. Epub 2006 Aug 9. [PubMed Link Image]
  9. Aziziyeh AI, Li TT, Pape C, Pampillo M, Chidiac P, Possmayer F, Babwah AV, Bhattacharya M: Dual regulation of lysophosphatidic acid (LPA1) receptor signalling by Ral and GRK. Cell Signal. 2009 Jul;21(7):1207-17. Epub 2009 Mar 21. [PubMed Link Image]
Enzyme 62 Metabolite References Not Available
Enzyme 63 [top]
Enzyme 63 ID 8453
Enzyme 63 Name Rap guanine nucleotide exchange factor 4
Enzyme 63 Synonyms
  1. Exchange factor directly activated by cAMP 2
  2. Exchange protein directly activated by cAMP 2
  3. EPAC 2
  4. cAMP-regulated guanine nucleotide exchange factor II
  5. cAMP-GEFII
Enzyme 63 Gene Name RAPGEF4
Enzyme 63 Protein Sequence >Rap guanine nucleotide exchange factor 4
MVAAHAAHSSSSAEWIACLDKRPLERSSEDVDIIFTRLKEVKAFEKFHPNLLHQICLCGY
YENLEKGITLFRQGDIGTNWYAVLAGSLDVKVSETSSHQDAVTICTLGIGTAFGESILDN
TPRHATIVTRESSELLRIEQKDFKALWEKYRQYMAGLLAPPYGVMETGSNNDRIPDKENT
PLIEPHVPLRPANTITKVPSEKILRAGKILRNAILSRAPHMIRDRKYHLKTYRQCCVGTE
LVDWMMQQTPCVHSRTQAVGMWQVLLEDGVLNHVDQEHHFQDKYLFYRFLDDEHEDAPLP
TEEEKKECDEELQDTMLLLSQMGPDAHMRMILRKPPGQRTVDDLEIIYEELLHIKALSHL
STTVKRELAGVLIFESHAKGGTVLFNQGEEGTSWYIILKGSVNVVIYGKGVVCTLHEGDD
FGKLALVNDAPRAASIVLREDNCHFLRVDKEDFNRILRDVEANTVRLKEHDQDVLVLEKV
PAGNRASNQGNSQPQQKYTVMSGTPEKILEHFLETIRLEATLNEATDSVLNDFIMMHCVF
MPNTQLCPALVAHYHAQPSQGTEQEKMDYALNNKRRVIRLVLQWAAMYGDLLQEDDVSMA
FLEEFYVSVSDDARMIAALKEQLPELEKIVKQISEDAKAPQKKHKVLLQQFNTGDERAQK
RQPIRGSDEVLFKVYCMDHTYTTIRVPVATSVKEVISAVADKLGSGEGLIIVKMSSGGEK
VVLKPNDVSVFTTLTINGRLFACPREQFDSLTPLPEQEGPTVGTVGTFELMSSKDLAYQM
TIYDWELFNCVHELELIYHTFGRHNFKKTTANLDLFLRRFNEIQFWVVTEICLCSQLSKR
VQLLKKFIKIAAHCKEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLM
DPSRNHRAYRLTVAKLEPPLIPFMPLLIKDMTFTHEGNKTFIDNLVNFEKMRMIANTART
VRYYRSQPFNPDAAQANKNHQDVRSYVRQLNVIDNQRTLSQMSHRLEPRRP
Enzyme 63 Number of Residues 1011
Enzyme 63 Molecular Weight 115520.7
Enzyme 63 Theoretical pI 6.83
Enzyme 63 GO Classification
Function
  • GTPase regulator activity
  • cAMP-dependent protein kinase regulator activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • kinase regulator activity
  • nucleoside-triphosphatase regulator activity
  • protein kinase regulator activity
Process
  • biological regulation
  • intracellular signal transduction
  • intracellular signaling pathway
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular metabolic process
  • regulation of cellular process
  • regulation of cellular protein metabolic process
  • regulation of metabolic process
  • regulation of protein amino acid phosphorylation
  • regulation of protein modification process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • signaling
  • signaling pathway
  • small GTPase mediated signal transduction
Component
  • cAMP-dependent protein kinase complex
  • cell part
  • intracellular
  • macromolecular complex
  • protein complex
Enzyme 63 General Function Involved in cAMP-dependent protein kinase regulator activity
Enzyme 63 Specific Function Guanine nucleotide exchange factor (GEF) for RAP1A, RAP1B and RAP2A small GTPases that is activated by binding cAMP. Seems not to activate RAB3A. Involved in cAMP-dependent, PKA- independent exocytosis through interaction with RIMS2
Enzyme 63 Pathways Not Available
Enzyme 63 Reactions Not Available
Enzyme 63 Pfam Domain Function
Enzyme 63 Signals
  • None
Enzyme 63 Transmembrane Regions
  • None
Enzyme 63 Essentiality Not Available
Enzyme 63 GenBank ID Protein 17061825 Link Image
Enzyme 63 UniProtKB/Swiss-Prot ID Q8WZA2 Link Image
Enzyme 63 UniProtKB/Swiss-Prot Entry Name RPGF4_HUMAN Link Image
Enzyme 63 PDB ID Not Available
Enzyme 63 Cellular Location Not Available
Enzyme 63 Gene Sequence >3036 bp
ATGGTCGCTGCGCACGCTGCCCATTCTTCCTCCTCTGCCGAGTGGATCGCCTGCCTGGAT
AAAAGACCACTGGAGCGATCCAGCGAAGATGTGGATATAATCTTCACTCGACTGAAAGAA
GTTAAAGCTTTTGAGAAATTTCACCCAAATCTCCTTCATCAGATTTGCTTATGTGGTTAT
TATGAGAATCTGGAAAAGGGAATAACATTATTTCGCCAGGGTGATATTGGAACAAACTGG
TATGCTGTCCTGGCAGGGTCTTTGGATGTTAAAGTATCTGAGACCAGCAGTCACCAGGAT
GCTGTGACCATCTGTACCCTGGGAATTGGGACGGCCTTTGGAGAGTCCATTCTGGACAAC
ACACCCCGCCATGCAACCATCGTTACCAGGGAGAGCAGTGAATTGCTCCGCATCGAGCAG
AAGGACTTCAAGGCACTATGGGAGAAATATCGACAGTATATGGCAGGACTTCTGGCTCCT
CCTTATGGTGTTATGGAAACGGGCTCTAACAATGACAGGATTCCTGACAAGGAGAACACA
CCTCTCATTGAACCTCACGTTCCTCTTCGTCCTGCTAACACCATTACCAAGGTCCCTTCA
GAGAAGATCCTCAGAGCTGGAAAAATTTTACGAAATGCCATTCTCTCTCGAGCACCTCAC
ATGATAAGAGATAGAAAATACCACCTAAAGACATACAGACAATGCTGTGTGGGAACTGAA
CTGGTGGACTGGATGATGCAGCAGACACCATGTGTTCACTCCCGGACTCAAGCTGTTGGC
ATGTGGCAAGTCCTGTTAGAAGATGGTGTTCTCAACCACGTGGACCAGGAGCACCATTTC
CAAGACAAATATTTATTCTATCGATTTCTGGATGATGAGCACGAGGATGCCCCTTTGCCT
ACTGAGGAGGAGAAGAAGGAGTGTGATGAGGAGCTCCAGGACACCATGCTGCTGCTGTCA
CAGATGGGCCCCGACGCCCACATGAGGATGATCCTTCGCAAACCACCTGGCCAGAGGACT
GTGGATGACCTAGAGATTATCTATGAGGAGCTTCTTCATATTAAAGCCTTATCCCATCTT
TCTACCACAGTGAAACGAGAGTTAGCAGGTGTTCTCATTTTTGAGTCTCACGCCAAAGGA
GGGACTGTGTTGTTTAACCAGGGGGAAGAAGGTACCTCCTGGTACATTATTCTAAAAGGA
TCAGTGAATGTAGTCATTTACGGCAAGGGTGTGGTCTGCACCCTGCATGAAGGAGATGAC
TTCGGCAAGTTAGCACTAGTGAATGATGCCCCACGAGCTGCCTCTATCGTCTTACGAGAA
GATAACTGCCATTTCTTAAGAGTAGACAAGGAGGATTTCAACCGGATCCTAAGGGACGTG
GAGGCGAATACAGTCAGACTTAAAGAACATGACCAAGATGTCTTGGTGCTGGAGAAGGTC
CCAGCAGGGAACAGAGCTTCTAATCAAGGAAACTCACAGCCTCAGCAAAAGTATACTGTG
ATGTCAGGAACACCTGAAAAAATTTTAGAGCATTTTCTAGAAACAATACGCCTTGAGGCA
ACTTTAAATGAAGCAACAGATTCTGTTTTAAATGACTTTATTATGATGCACTGTGTTTTT
ATGCCAAATACCCAGCTTTGCCCGGCACTGGTGGCCCACTACCACGCACAGCCTTCACAA
GGTACAGAACAGGAGAAAATGGATTATGCCCTCAACAATAAGAGGCGAGTCATCCGCCTG
GTTCTACAGTGGGCTGCCATGTATGGAGACCTCCTGCAAGAGGATGACGTGTCTATGGCC
TTCCTGGAGGAGTTTTATGTATCTGTATCAGATGATGCCCGGATGATTGCTGCCCTCAAG
GAGCAACTGCCAGAGTTGGAGAAGATTGTCAAGCAAATCTCAGAAGATGCAAAGGCACCA
CAAAAGAAGCACAAGGTTCTTTTGCAACAGTTCAATACGGGCGATGAGAGAGCCCAGAAG
CGCCAGCCTATCCGCGGCTCTGATGAAGTTCTGTTTAAGGTCTATTGCATGGACCACACC
TACACAACCATTCGGGTGCCAGTGGCCACTTCGGTGAAGGAAGTCATCAGTGCAGTTGCC
GACAAGCTGGGCTCCGGGGAGGGCCTGATCATAGTCAAGATGAGTTCCGGAGGAGAAAAG
GTGGTGCTCAAACCTAATGATGTTTCAGTATTTACGACGCTCACCATTAATGGACGCCTG
TTTGCTTGCCCGCGAGAGCAATTCGATTCACTGACTCCCTTACCAGAACAGGAAGGCCCA
ACTGTTGGAACAGTGGGAACTTTTGAACTGATGAGCTCCAAAGATTTAGCATACCAGATG
ACAATTTATGATTGGGAACTCTTCAACTGCGTGCATGAGCTGGAGCTAATCTATCACACA
TTTGGAAGGCATAATTTTAAAAAGACCACAGCAAACTTGGATTTGTTCCTGAGGAGATTT
AATGAAATTCAGTTTTGGGTCGTCACTGAGATCTGCCTTTGTTCTCAGCTCAGCAAGCGT
GTTCAGCTATTAAAAAAATTTATTAAGATAGCAGCCCACTGTAAGGAGTATAAAAATCTG
AATTCCTTTTTTGCCATCGTCATGGGACTAAGTAACGTTGCTGTGAGCCGCTTGGCACTA
ACGTGGGAGAAACTGCCAAGCAAGTTCAAGAAGTTCTATGCGGAGTTTGAAAGTTTAATG
GACCCTTCAAGGAACCACAGGGCCTACAGGCTGACAGTAGCTAAGCTGGAACCTCCTCTC
ATCCCCTTCATGCCTTTGCTCATTAAAGATATGACATTTACTCATGAGGGGAACAAGACG
TTCATTGACAATCTAGTAAACTTTGAAAAAATGCGCATGATTGCAAATACGGCCAGAACA
GTGAGATACTACAGGAGCCAACCCTTCAATCCTGATGCAGCTCAAGCTAATAAGAACCAT
CAGGATGTCCGGAGTTATGTACGGCAATTAAATGTGATTGACAACCAGAGAACTTTATCA
CAGATGTCACACAGATTAGAGCCTCGTCGACCATAG
Enzyme 63 GenBank Gene ID AB027471 Link Image
Enzyme 63 GeneCard ID RAPGEF4 Link Image
Enzyme 63 GenAtlas ID RAPGEF4 Link Image
Enzyme 63 HGNC ID HGNC:16626 Link Image
Enzyme 63 Chromosome Location 2
Enzyme 63 Locus 2q31-q32
Enzyme 63 SNPs SNPJam Report Link Image
Enzyme 63 General References
  1. Kawasaki H, Springett GM, Mochizuki N, Toki S, Nakaya M, Matsuda M, Housman DE, Graybiel AM: A family of cAMP-binding proteins that directly activate Rap1. Science. 1998 Dec 18;282(5397):2275-9. [PubMed Link Image]
  2. Ueno H, Shibasaki T, Iwanaga T, Takahashi K, Yokoyama Y, Liu LM, Yokoi N, Ozaki N, Matsukura S, Yano H, Seino S: Characterization of the gene EPAC2: structure, chromosomal localization, tissue expression, and identification of the liver-specific isoform. Genomics. 2001 Nov;78(1-2):91-8. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. de Rooij J, Rehmann H, van Triest M, Cool RH, Wittinghofer A, Bos JL: Mechanism of regulation of the Epac family of cAMP-dependent RapGEFs. J Biol Chem. 2000 Jul 7;275(27):20829-36. [PubMed Link Image]
Enzyme 63 Metabolite References Not Available
Enzyme 64 [top]
Enzyme 64 ID 8457
Enzyme 64 Name Elongation factor 2
Enzyme 64 Synonyms
  1. EF-2
Enzyme 64 Gene Name EEF2
Enzyme 64 Protein Sequence >Elongation factor 2
MVNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTR
KDEQERCITIKSTAISLFYELSENDLNFIKQSKDGAGFLINLIDSPGHVDFSSEVTAALR
VTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQR
IVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKG
EGQLGPAERAKKVEDMMKKLWGDRYFDPANGKFSKSATSPEGKKLPRTFCQLILDPIFKV
FDAIMNFKKEETAKLIEKLDIKLDSEDKDKEGKPLLKAVMRRWLPAGDALLQMITIHLPS
PVTAQKYRCELLYEGPPDDEAAMGIKSCDPKGPLMMYISKMVPTSDKGRFYAFGRVFSGL
VSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLV
KTGTITTFEHAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEE
SGEHIIAGAGELHLEICLKDLEEDHACIPIKKSDPVVSYRETVSEESNVLCLSKSPNKHN
RLYMKARPFPDGLAEDIDKGEVSARQELKQRARYLAEKYEWDVAEARKIWCFGPDGTGPN
ILTDITKGVQYLNEIKDSVVAGFQWATKEGALCEENMRGVRFDVHDVTLHADAIHRGGGQ
IIPTARRCLYASVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVAGTP
MFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDNSSRPSQVVAETRK
RKGLKEGIPALDNFLDKL
Enzyme 64 Number of Residues 858
Enzyme 64 Molecular Weight 95337.4
Enzyme 64 Theoretical pI 6.82
Enzyme 64 GO Classification
Function
  • GTP binding
  • GTPase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
Process
Component
Enzyme 64 General Function Involved in GTPase activity
Enzyme 64 Specific Function This protein promotes the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site of the ribosome
Enzyme 64 Pathways Not Available
Enzyme 64 Reactions Not Available
Enzyme 64 Pfam Domain Function
Enzyme 64 Signals
  • None
Enzyme 64 Transmembrane Regions
  • None
Enzyme 64 Essentiality Not Available
Enzyme 64 GenBank ID Protein 60685056 Link Image
Enzyme 64 UniProtKB/Swiss-Prot ID P13639 Link Image
Enzyme 64 UniProtKB/Swiss-Prot Entry Name EF2_HUMAN Link Image
Enzyme 64 PDB ID Not Available
Enzyme 64 Cellular Location Not Available
Enzyme 64 Gene Sequence >2577 bp
ATGGTGAACTTCACGGTAGACCAGATCCGCGCCATCATGGACAAGAAGGCCAACATCCGC
AACATGTCTGTCATCGCCCACGTGGACCATGGCAAGTCCACGCTGACAGACTCCCTGGTG
TGCAAGGCGGGCATCATCGCCTCGGCCCGGGCCGGGGAGACACGCTTCACTGATACCCGG
AAGGACGAGCAGGAGCGTTGCATCACCATCAAGTCAACTGCCATCTCCCTCTTCTACGAG
CTCTCGGAGAATGACTTGAACTTCATCAAGCAGAGCAAGGACGGTGCCGGCTTCCTCATC
AACCTCATTGACTCCCCCGGGCATGTCGACTTCTCCTCGGAGGTGACTGCTGCCCTCCGA
GTCACCGATGGCGCATTGGTGGTGGTGGACTGCGTGTCAGGCGTGTGCGTGCAGACGGAG
ACAGTGCTGCGGCAGGCCATTGCCGAGCGCATCAAGCCTGTGCTGATGATGAACAAGATG
GACCGCGCCCTGCTGGAGCTGCAGCTGGAGCCCGAGGAGCTCTACCAGACTTTCCAGCGC
ATCGTGGAGAACGTGAACGTCATCATCTCCACCTACGGCGAGGGCGAGAGCGGCCCCATG
GGCAACATCATGATCGATCCTGTCCTCGGTACCGTGGGCTTTGGGTCTGGCCTCCACGGG
TGGGCCTTCACCCTGAAGCAGTTTGCCGAGATGTATGTGGCCAAGTTCGCCGCCAAGGGG
GAGGGCCAGTTGGGGCCTGCCGAGCGGGCCAAGAAAGTAGAGGACATGATGAAGAAGCTG
TGGGGTGACAGGTACTTTGACCCAGCCAACGGCAAGTTCAGCAAGTCAGCCACCAGCCCC
GAAGGGAAGAAGCTGCCACGCACCTTCTGCCAGCTGATCCTGGACCCCATCTTCAAGGTG
TTTGATGCGATCATGAATTTCAAGAAAGAGGAGACAGCAAAACTGATAGAGAAACTGGAC
ATCAAACTGGACAGCGAGGACAAGGACAAAGAAGGCAAACCCCTGCTGAAGGCTGTGATG
CGCCGCTGGCTGCCTGCCGGAGACGCCTTGTTGCAGATGATCACCATCCACCTGCCCTCC
CCTGTGACGGCCCAGAAGTACCGCTGCGAGCTCCTGTACGAGGGGCCCCCGGACGACGAG
GCTGCCATGGGCATTAAAAGCTGTGACCCCAAAGGCCCTCTTATGATGTATATTTCCAAA
ATGGTGCCAACCTCCGACAAAGGTCGGTTCTACGCCTTTGGACGAGTCTTCTCGGGGCTG
GTCTCCACTGGCCTGAAGGTCAGGATCATGGGGCCCAACTATACCCCTGGGAAGAAGGAG
GACCTCTACCTGAAGCCAATCCAGAGAACAATCTTGATGATGGGCCGCTACGTGGAGCCC
ATCGAGGATGTGCCTTGTGGGAACATTGTGGGCCTCGTGGGCGTGGACCAGTTCCTGGTG
AAGACGGGCACCATCACCACCTTCGAGCACGCGCACAACATGCGGGTGATGAAGTTCAGC
GTCAGCCCTGTTGTCAGAGTGGCCGTGGAGGCCAAGAACCCGGCTGACCTGCCCAAGCTG
GTGGAGGGGCTGAAGCGGCTGGCCAAGTCCGACCCCATGGTGCAGTGCATCATCGAGGAG
TCGGGAGAGCATATCATCGCGGGCGCCGGCGAGCTGCACCTGGAGATCTGCCTGAAGGAC
CTGGAGGAGGACCACGCCTGCATCCCCATCAAGAAATCTGACCCGGTCGTCTCGTACCGC
GAGACGGTCAGTGAAGAGTCGAACGTGCTCTGCCTCTCCAAGTCCCCCAACAAGCACAAC
CGGCTGTACATGAAGGCGCGGCCCTTCCCCGACGGCCTGGCCGAGGACATCGATAAAGGC
GAGGTGTCCGCCCGTCAGGAGCTCAAGCAGCGGGCGCGCTACCTGGCCGAGAAGTACGAG
TGGGACGTGGCTGAGGCCCGCAAGATCTGGTGCTTTGGGCCCGACGGCACCGGCCCCAAC
ATCCTCACCGACATCACCAAGGGTGTGCAGTACCTCAACGAGATCAAGGACAGTGTGGTG
GCCGGCTTCCAGTGGGCCACCAAGGAGGGCGCACTGTGTGAGGAGAACATGCGGGGTGTG
CGCTTCGACGTCCACGACGTCACCCTGCACGCCGATGCCATCCACCGCGGAGGGGGCCAG
ATCATCCCCACAGCACGGCGCTGCCTCTATGCCAGTGTGCTGACCGCCCAGCCACGCCTC
ATGGAGCCCATCTACCTTGTGGAGATCCAGTGTCCAGAGCAGGTGGTCGGTGGCATCTAC
GGGGTTTTGAACAGGAAGCGGGGCCACGTGTTCGAGGAGTCCCAGGTGGCCGGCACCCCC
ATGTTTGTGGTCAAGGCCTATCTGCCCGTCAACGAGTCCTTTGGCTTCACCGCTGACCTG
AGGTCCAACACGGGCGGCCAGGCGTTCCCCCAGTGTGTGTTTGACCACTGGCAGATCCTG
CCCGGAGACCCCTTCGACAACAGCAGCCGCCCCAGCCAGGTGGTGGCGGAGACCCGCAAG
CGCAAGGGCCTGAAAGAAGGCATCCCTGCCCTGGACAACTTCCTGGACAAATTGTAG
Enzyme 64 GenBank Gene ID AY942181 Link Image
Enzyme 64 GeneCard ID EEF2 Link Image
Enzyme 64 GenAtlas ID EEF2 Link Image
Enzyme 64 HGNC ID HGNC:3214 Link Image
Enzyme 64 Chromosome Location 1
Enzyme 64 Locus 19pter-q12
Enzyme 64 SNPs SNPJam Report Link Image
Enzyme 64 General References
  1. Rapp G, Klaudiny J, Hagendorff G, Luck MR, Scheit KH: Complete sequence of the coding region of human elongation factor 2 (EF-2) by enzymatic amplification of cDNA from human ovarian granulosa cells. Biol Chem Hoppe Seyler. 1989 Oct;370(10):1071-5. [PubMed Link Image]
  2. Hanes J, Freudenstein J, Rapp G, Scheit KH: Construction of a plasmid containing the complete coding region of human elongation factor 2. Biol Chem Hoppe Seyler. 1992 Apr;373(4):201-4. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Rapp G, Mucha J, Einspanier R, Luck M, Scheit KH: Cloning and sequence analysis of a cDNA from human ovarian granulosa cells encoding the C-terminal part of human elongation factor 2. Biol Chem Hoppe Seyler. 1988 Apr;369(4):247-50. [PubMed Link Image]
  5. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  6. Kim JE, Tannenbaum SR, White FM: Global phosphoproteome of HT-29 human colon adenocarcinoma cells. J Proteome Res. 2005 Jul-Aug;4(4):1339-46. [PubMed Link Image]
  7. Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J: Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC. Proteomics. 2005 Sep;5(14):3589-99. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  9. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  10. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  11. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  12. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  13. Yamashita A, Izumi N, Kashima I, Ohnishi T, Saari B, Katsuhata Y, Muramatsu R, Morita T, Iwamatsu A, Hachiya T, Kurata R, Hirano H, Anderson P, Ohno S: SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate remodeling of the mRNA surveillance complex during nonsense-mediated mRNA decay. Genes Dev. 2009 May 1;23(9):1091-105. [PubMed Link Image]
  14. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 64 Metabolite References Not Available
Enzyme 65 [top]
Enzyme 65 ID 8557
Enzyme 65 Name Succinate-CoA ligase, ADP-forming, beta subunit
Enzyme 65 Synonyms Not Available
Enzyme 65 Gene Name SUCLA2
Enzyme 65 Protein Sequence >Succinate-CoA ligase, ADP-forming, beta subunit
MAASMFYGRLVAVATLRNHRPRTAQRAAAQVLGSSGLFNNHGLQVQQQQQRNLSLHEYMS
MELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVK
IVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGP
VLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENM
VKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDER
DKDAAKANLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEA
FKLITSDKKVLAILVNIFGGIMRCDVIAQGIVMAVKDLEIKIPVVVRLQGTRVDDAKALI
ADSGLKILACDDLDEAARMVVKLSEIVTLAKQAHVDVKFQLPI
Enzyme 65 Number of Residues 463
Enzyme 65 Molecular Weight 50318
Enzyme 65 Theoretical pI 7.50
Enzyme 65 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 65 General Function Energy production and conversion
Enzyme 65 Specific Function Not Available
Enzyme 65 Pathways Not Available
Enzyme 65 Reactions Not Available
Enzyme 65 Pfam Domain Function
Enzyme 65 Signals Not Available
Enzyme 65 Transmembrane Regions Not Available
Enzyme 65 Essentiality Not Available
Enzyme 65 GenBank ID Protein 55957259 Link Image
Enzyme 65 UniProtKB/Swiss-Prot ID Q5T9Q4 Link Image
Enzyme 65 UniProtKB/Swiss-Prot Entry Name Q5T9Q4_HUMAN Link Image
Enzyme 65 PDB ID Not Available
Enzyme 65 Cellular Location Not Available
Enzyme 65 Gene Sequence >1326 bp
ATGGCGGCCTCCATGTTCTACGGCAGGCTAGTGGCCGTGGCCACCCTTCGGAACCACCGG
CCTCGGACGGCCCAGCAACAGCAAAGGAATCTCTCACTACATGAATACATGAGTATGGAA
TTATTGCAAGAAGCTGGTGTCTCCGTTCCCAAAGGATATGTGGCAAAGTCACCAGATGAA
GCTTATGCAATTGCCAAAAAATTAGGTTCAAAAGATGTCGTGATAAAGGCACAGGTTTTA
GCTGGTGGTAGAGGAAAAGGAACATTTGAAAGTGGCCTCAAAGGAGGAGTGAAGATAGTT
TTCTCTCCAGAAGAAGCAAAAGCTGTTTCTTCACAAATGATTGGGAAAAAATTGTTTACC
AAGCAAACGGGAGAAAAGGGCAGAATATGCAATCAAGTATTGGTCTGTGAGCGAAAATAT
CCCAGGAGAGAATACTACTTTGCAATAACAATGGAAAGGTCATTTCAAGGTCCTGTATTA
ATAGGAAGTTCACATGGTGGTGTCAACATTGAAGATGTTGCTGCTGAGTCTCCTGAAGCA
ATAATTAAAGAACCTATTGATATTGAAGAAGGCATCAAAAAGGAACAAGCTCTCCAGCTT
GCACAGAAGATGGGATTTCCACCTAATATTGTGGAATCAGCAGCAGAAAACATGGTCAAG
CTTTACAGCCTTTTTCTGAAATACGATGCAACCATGATAGAAATAAATCCAATGGTGGAA
GATTCAGATGGAGCTGTATTGTGTATGGATGCAAAGATCAATTTTGACTCTAATTCAGCC
TATCGCCAAAAGAAAATCTTTGATCTACAGGACTGGACCCAGGAAGATGAAAGGGACAAA
GATGCTGCTAAGGCAAATCTCAACTACATTGGCCTCGATGGAAATATAGGCTGCCTAGTA
AATGGTGCTGGTTTGGCTATGGCCACAATGGATATAATAAAACTTCATGGAGGGACTCCA
GCCAACTTCCTTGATGTTGGTGGTGGTGCTACAGTCCATCAAGTAACAGAAGCATTTAAG
CTTATCACTTCAGATAAAAAGGTACTGGCTATTCTGGTCAACATTTTTGGAGGAATCATG
CGCTGTGATGTTATTGCACAGGGTATAGTCATGGCAGTAAAAGACTTGGAAATTAAAATA
CCTGTTGTGGTACGGTTACAAGGTACACGAGTCGATGATGCTAAGGCACTGATAGCGGAC
AGTGGACTTAAAATACTTGCTTGTGATGACTTGGATGAAGCTGCTAGAATGGTTGTAAAG
CTCTCTGAAATAGTGACCTTAGCGAAGCAAGCACATGTGGATGTGAAATTTCAGTTGCCA
ATATGA
Enzyme 65 GenBank Gene ID AL157369 Link Image
Enzyme 65 GeneCard ID SUCLA2 Link Image
Enzyme 65 GenAtlas ID SUCLA2 Link Image
Enzyme 65 HGNC ID HGNC:11448 Link Image
Enzyme 65 Chromosome Location 13
Enzyme 65 Locus 13q12.2-q13.3
Enzyme 65 SNPs SNPJam Report Link Image
Enzyme 65 General References Not Available
Enzyme 65 Metabolite References Not Available
Enzyme 66 [top]
Enzyme 66 ID 8772
Enzyme 66 Name ENTPD4 protein
Enzyme 66 Synonyms Not Available
Enzyme 66 Gene Name ENTPD4
Enzyme 66 Protein Sequence >ENTPD4 protein
MGRIGISCLFPASWHFSISPVGCPRILNTNLRQIMVISVLAAAVSLLYFSVVIIRNKYGR
LTRDKKFQRYLARVTDIEATDTNNPNVNYGIVVDCGSSGSRVFVYCWPRHNGNPHDLLDI
RQMRDKNRKPVVMKIKPGISEFATSPEKVSDYISPLLNFAAEHVPRAKHKETPLYILCTA
GMRILPESQQKAILEDLLTDIPVHFDFLFSDSHAEVISGKQEGVYAWIGINFVLGRFEHI
EDDDEAVVEVNIPGSESSEAIVRKRTAGILDMGGVSTQIAYEVPKTEEVAKNLLAEFNLG
CDVHQTEHVYRVYVATFLGFGGNAARQRYEDRIFANTIQKNRLLGKQTGLTPDMPYLDPC
LPLDIKDEIQQNGQTIYLRGTGDFDLCRETIQPFMNKTNETQTSLNGVYQPPIHFQNSEF
YGFSEFYYCTEDVLRMGGDYNAAKFTKAAKDYCATKWSILRERFDRGLYASHADLHRLKY
QCFKSAWMFEVFHRGFSFPVNYKSLKTALQVYDKEVQWTLGAILYRTRFLPLRKIGMLII
PCSGGCPKLCCAVWQPPPYGATKHLQCAAWN
Enzyme 66 Number of Residues 571
Enzyme 66 Molecular Weight 64852.9
Enzyme 66 Theoretical pI 8.13
Enzyme 66 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 66 General Function Involved in hydrolase activity
Enzyme 66 Specific Function Not Available
Enzyme 66 Pathways Not Available
Enzyme 66 Reactions Not Available
Enzyme 66 Pfam Domain Function
Enzyme 66 Signals
  • None
Enzyme 66 Transmembrane Regions
  • None
Enzyme 66 Essentiality Not Available
Enzyme 66 GenBank ID Protein 21759777 Link Image
Enzyme 66 UniProtKB/Swiss-Prot ID Q8NE73 Link Image
Enzyme 66 UniProtKB/Swiss-Prot Entry Name Q8NE73_HUMAN Link Image
Enzyme 66 PDB ID Not Available
Enzyme 66 Cellular Location Not Available
Enzyme 66 Gene Sequence >1716 bp
ATGGGGAGGATTGGCATCTCCTGTCTTTTTCCTGCTTCTTGGCATTTTAGCATATCTCCA
GTAGGGTGTCCTCGAATTCTGAATACCAATTTACGCCAAATTATGGTCATTAGTGTCCTG
GCTGCTGCTGTTTCACTTTTATATTTTTCTGTTGTCATAATCCGAAATAAGTATGGGCGA
CTAACCAGAGACAAGAAATTTCAAAGGTACCTGGCACGAGTTACCGACATTGAAGCTACA
GACACCAATAACCCCAATGTGAACTATGGGATCGTGGTGGACTGTGGTAGCAGTGGGTCT
CGAGTATTTGTTTACTGCTGGCCAAGGCATAATGGCAATCCACATGATCTGTTGGATATC
AGGCAAATGAGGGATAAAAACCGAAAGCCAGTGGTCATGAAGATAAAACCGGGCATTTCA
GAATTTGCTACCTCTCCAGAGAAAGTCAGTGATTACATTTCTCCACTTTTGAACTTTGCT
GCAGAGCATGTGCCACGGGCAAAACACAAAGAGACACCTCTCTACATTCTCTGCACGGCT
GGAATGAGAATCCTCCCCGAAAGCCAGCAGAAAGCTATTCTGGAAGACCTTCTGACCGAT
ATCCCCGTGCACTTTGACTTTCTGTTTTCTGACTCTCATGCAGAAGTAATTTCTGGGAAA
CAAGAAGGTGTGTATGCTTGGATTGGCATTAATTTTGTCCTTGGACGATTTGAGCATATT
GAAGATGATGATGAGGCCGTTGTGGAAGTTAACATTCCTGGAAGTGAAAGCAGCGAAGCC
ATTGTCCGTAAAAGGACAGCGGGCATTCTCGACATGGGCGGCGTGTCGACTCAGATAGCG
TACGAAGTCCCCAAAACTGAAGAAGTAGCTAAAAACTTGTTAGCTGAATTTAACTTGGGA
TGTGATGTTCACCAAACTGAGCATGTGTATCGAGTCTATGTGGCCACGTTTCTTGGGTTT
GGTGGCAATGCTGCTCGACAGAGATACGAAGACAGAATATTTGCCAACACCATTCAAAAG
AACAGGCTCCTGGGTAAACAGACTGGTCTGACTCCTGATATGCCGTACTTGGACCCCTGC
CTACCCCTAGACATTAAAGATGAAATCCAGCAAAATGGACAAACCATATACCTACGAGGG
ACTGGAGACTTTGACCTGTGTCGAGAGACTATCCAGCCTTTCATGAATAAAACAAACGAG
ACCCAGACTTCCCTCAATGGGGTCTACCAGCCCCCAATTCACTTCCAGAACAGTGAATTC
TATGGCTTCTCCGAATTCTACTACTGCACCGAGGATGTGTTACGAATGGGGGGAGACTAC
AATGCTGCTAAATTTACTAAAGCTGCAAAGGATTATTGTGCAACAAAGTGGTCCATTTTG
CGGGAACGCTTTGACCGAGGACTGTACGCCTCTCATGCTGACCTCCACAGGCTTAAGTAT
CAGTGCTTCAAATCGGCCTGGATGTTTGAGGTGTTTCATAGGGGCTTTTCGTTTCCTGTC
AACTATAAAAGCTTAAAGACTGCCTTGCAAGTTTACGACAAGGAGGTTCAGTGGACCCTT
GGAGCCATCCTCTACAGGACCCGCTTTCTACCATTAAGGAAAATAGGGATGCTGATAATA
CCTTGCTCAGGGGGTTGTCCAAAGCTGTGTTGTGCAGTATGGCAGCCACCACCATATGGG
GCCACCAAACACTTGCAATGTGCTGCTTGGAATTGA
Enzyme 66 GenBank Gene ID BC034477 Link Image
Enzyme 66 GeneCard ID ENTPD4 Link Image
Enzyme 66 GenAtlas ID ENTPD4 Link Image
Enzyme 66 HGNC ID HGNC:14573 Link Image
Enzyme 66 Chromosome Location 8
Enzyme 66 Locus 8p21.3
Enzyme 66 SNPs SNPJam Report Link Image
Enzyme 66 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 66 Metabolite References Not Available
Enzyme 67 [top]
Enzyme 67 ID 9324
Enzyme 67 Name Mannose-1-phosphate guanyltransferase beta
Enzyme 67 Synonyms
  1. GDP-mannose pyrophosphorylase B
  2. GTP-mannose-1-phosphate guanylyltransferase beta
Enzyme 67 Gene Name GMPPB
Enzyme 67 Protein Sequence >Mannose-1-phosphate guanyltransferase beta
MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQVL
EKEMKAQEQRLGIRISMSHEEEPLGTAGPLALARDLLSETADPFFVLNSDVICDFPFQAM
VQFHRHHGQEGSILVTKVEEPSKYGVVVCEADTGRIHRFVEKPQVFVSNKINAGMYILSP
AVLQRIQLQPTSIEKEVFPIMAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFLQSLRQKQ
PERLCSGPGIVGNVLVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVLRDARIRSH
SWLESCIVGWRCRVGQWVRMENVTVLGEDVIVNDELYLNGASVLPHKSIGESVPEPRIIM
Enzyme 67 Number of Residues 360
Enzyme 67 Molecular Weight 39834.1
Enzyme 67 Theoretical pI 6.59
Enzyme 67 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • metabolic process
Component
Enzyme 67 General Function Involved in transferase activity
Enzyme 67 Specific Function GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose
Enzyme 67 Pathways
Enzyme 67 Reactions
  • GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose [RN:R00885]
Enzyme 67 Pfam Domain Function
Enzyme 67 Signals
  • None
Enzyme 67 Transmembrane Regions
  • None
Enzyme 67 Essentiality Not Available
Enzyme 67 GenBank ID Protein 5052351 Link Image
Enzyme 67 UniProtKB/Swiss-Prot ID Q9Y5P6 Link Image
Enzyme 67 UniProtKB/Swiss-Prot Entry Name GMPPB_HUMAN Link Image
Enzyme 67 PDB ID Not Available
Enzyme 67 Cellular Location Not Available
Enzyme 67 Gene Sequence >1083 bp
ATGAAGGCACTGATCTTAGTGGGGGGCTATGGGACGCGGCTACGGCCGCTGACGCTGAGC
ACCCCGAAGCCACTGGTGGACTTCTGCAATAAGCCCATCTTGCTGCACCAAGTGGAGGCG
CTAGCCGCGGCAGGCGTGGACCACGTGATCCTGGCCGTGAGCTACATGTCGCAGGTGCTG
GAGAAGGAAATGAAGGCACAGGAGCAGAGGCTGGGAATCCGAATCTCCATGTCCCATGAA
GAGGAGCCTTTGGGGACAGCTGGGCCCCTGGCGCTGGCCCGTGACCTACTCTCTGAGACT
GCAGACCCTTTCTTCGTCCTCAACAGTGACGTGATCTGCGATTTCCCCTTCCAAGCCATG
GTGCAGTTCCACCGGCACCATGGCCAGGAGGGCTCCATCCTGGTGACCAAGGTGGAGGAA
CCCTCCAAGTACGGTGTGGTGGTGTGTGAGGCTGACACAGGCCGCATTCACCGGTTCGTG
GAGAAGCCACAGGTGTTTGTGTCCAATAAGATCAACGCAGGCATGTACATCCTGAGCCCT
GCAGTGCTGCGGCGCATCCAGCTGCAGCCTACGTCCATTGAGAAGGAGGTCTTCCCCATT
ATGGCCAAGGAGGGGCAGCTATATGCCATGGAGTTACAGGGCTTCTGGATGGACATTGGG
CAGCCCAAGGACTTCCTCACTGGCATGTGCCTCTTCCTGCAGTCACTGAGGCAGAAGCAG
CCTGAGCGGCTGTGCTCAGGCCCTGGCATTGTGGGCAACGTGCTGGTGGACCCAAGTGCC
CGCATCGGCCAGAACTGCAGCATTGGCCCCAATGTGAGCCTGGGACCTGGCGTGGTGGTC
GAAGATGGTGTGTGTATCCGGCGGTGCACGGTGCTGCGGGATGCCCGGATCCGTTCCCAT
TCCTGGCTTGAGTCCTGCATTGTGGGCTGGCGCTGCCGCGTGGGTCAGTGGGTACGCATG
GAGAACGTGACAGTGCTGGGTGAGGACGTCATAGTTAATGATGAGCTCTACCTCAACGGA
GCCAGCGTGCTGCCCCACAAGTCTATTGGCGAGTCAGTGCCAGAGCCTCGTATCATCATG
TGA
Enzyme 67 GenBank Gene ID AF135421 Link Image
Enzyme 67 GeneCard ID GMPPB Link Image
Enzyme 67 GenAtlas ID GMPPB Link Image
Enzyme 67 HGNC ID HGNC:22932 Link Image
Enzyme 67 Chromosome Location 3
Enzyme 67 Locus 3p21.31
Enzyme 67 SNPs SNPJam Report Link Image
Enzyme 67 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 67 Metabolite References Not Available
Enzyme 68 [top]
Enzyme 68 ID 9325
Enzyme 68 Name Mannose-1-phosphate guanyltransferase alpha
Enzyme 68 Synonyms
  1. GDP-mannose pyrophosphorylase A
  2. GTP-mannose-1-phosphate guanylyltransferase alpha
Enzyme 68 Gene Name GMPPA
Enzyme 68 Protein Sequence >Mannose-1-phosphate guanyltransferase alpha
MLKAVILIGGPQKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGFYQ
PDEPLTQFLEAAQQEFNLPVRYLQEFAPLGTGGGLYHFRDQILAGSPEAFFVLNADVCSD
FPLSAMLEAHRRQRHPFLLLGTTANRTQSLNYGCIVENPQTHEVLHYVEKPSTFISDIIN
CGIYLFSPEALKPLRDVFQRNQQDGQLEDSPGLWPGAGTIRLEQDVFSALAGQGQIYVHL
TDGIWSQIKSAGSALYASRLYLSRYQDTHPERLAKHTPGGPWIRGNVYIHPTAKVAPSAV
LGPNVSIGKGVTVGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARVEGTPSDP
NPNDPRARMDSESLFKDGKLLPAITILGCRVRIPAEVLILNSIVLPHKELSRSFTNQIIL
Enzyme 68 Number of Residues 420
Enzyme 68 Molecular Weight 46290.8
Enzyme 68 Theoretical pI 7.23
Enzyme 68 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • metabolic process
Component
Enzyme 68 General Function Involved in transferase activity
Enzyme 68 Specific Function GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose
Enzyme 68 Pathways Not Available
Enzyme 68 Reactions
  • GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose [RN:R00885]
Enzyme 68 Pfam Domain Function
Enzyme 68 Signals
  • None
Enzyme 68 Transmembrane Regions
  • None
Enzyme 68 Essentiality Not Available
Enzyme 68 GenBank ID Protein 62822505 Link Image
Enzyme 68 UniProtKB/Swiss-Prot ID Q96IJ6 Link Image
Enzyme 68 UniProtKB/Swiss-Prot Entry Name GMPPA_HUMAN Link Image
Enzyme 68 PDB ID Not Available
Enzyme 68 Cellular Location Not Available
Enzyme 68 Gene Sequence >1263 bp
ATGCTCAAAGCGGTGATCCTGATTGGAGGCCCTCAAAAGGGAACTCGCTTCAGACCTTTG
TCTTTTGAGGTGCCCAAACCATTGTTTCCTGTGGCAGGGGTCCCTATGATCCAACACCAT
ATTGAAGCCTGTGCCCAGGTCCCTGGAATGCAGGAGATTCTGCTCATTGGCTTCTACCAA
CCTGATGAGCCCCTCACCCAGTTCCTAGAAGCCGCCCAGCAGGAGTTTAACCTTCCAGTC
AGGTACCTGCAGGAATTTGCCCCCCTAGGCACAGGGGGTGGTCTTTACCATTTTCGAGAC
CAGATCCTGGCTGGGAGCCCCGAGGCATTCTTCGTGCTCAATGCTGATGTCTGCTCCGAC
TTCCCCTTGAGTGCTATGTTGGAAGCCCACCGACGCCAGCGTCACCCTTTCTTACTCCTT
GGCACTACGGCTAACAGGACGCAATCCCTCAACTACGGCTGCATCGTTGAGAATCCACAG
ACACACGAGGTATTGCACTATGTGGAGAAACCCAGCACATTTATCAGTGACATCATCAAC
TGCGGCATCTACCTCTTTTCTCCTGAAGCCTTGAAGCCTCTTCGGGATGTCTTCCAGCGT
AATCAGCAGGATGGGCAATTGGAGGACTCACCAGGCTTGTGGCCAGGGGCAGGTACCATC
CGCCTAGAGCAGGATGTGTTTTCAGCCCTGGCAGGGCAGGGCCAGATATACGTGCATCTC
ACTGATGGTATCTGGAGTCAGATCAAGTCCGCAGGTTCAGCCCTCTACGCCTCCCGCCTC
TACCTGAGCCGATACCAGGACACTCACCCAGAACGGCTGGCCAAGCACACCCCAGGGGGC
CCATGGATCCGAGGGAATGTGTACATCCACCCGACCGCCAAGGTGGCCCCCTCGGCTGTG
CTGGGCCCCAACGTCTCCATCGGGAAGGGGGTGACCGTGGGTGAGGGTGTGCGGCTCCGG
GAGAGCATCGTCCTCCATGGAGCCACTTTGCAGGAGCACACGTGTGTTCTGCATAGCATC
GTGGGCTGGGGGAGCACCGTGGGACGCTGGGCCCGCGTGGAGGGTACCCCCAGTGACCCT
AACCCCAACGATCCCCGAGCCCGCATGGACAGTGAGAGCCTCTTCAAGGACGGGAAGCTG
CTGCCTGCTATCACCATCCTGGGCTGCCGAGTCCGGATCCCTGCCGAGGTGCTCATCCTG
AACTCGATTGTTCTGCCACACAAGGAGCTGAGCCGAAGCTTCACCAACCAGATCATCCTC
TGA
Enzyme 68 GenBank Gene ID AC053503 Link Image
Enzyme 68 GeneCard ID GMPPA Link Image
Enzyme 68 GenAtlas ID GMPPA Link Image
Enzyme 68 HGNC ID HGNC:22923 Link Image
Enzyme 68 Chromosome Location 2
Enzyme 68 Locus 2q35
Enzyme 68 SNPs SNPJam Report Link Image
Enzyme 68 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 68 Metabolite References Not Available
Enzyme 69 [top]
Enzyme 69 ID 11509
Enzyme 69 Name Alpha-(1,3)-fucosyltransferase
Enzyme 69 Synonyms
  1. Fucosyltransferase 9
  2. Fucosyltransferase IX
  3. Fuc-TIX
  4. FucT-IX
  5. Galactoside 3-L-fucosyltransferase
Enzyme 69 Gene Name FUT9
Enzyme 69 Protein Sequence >Alpha-(1,3)-fucosyltransferase
MTSTSKGILRPFLIVCIILGCFMACLLIYIKPTNSWIFSPMESASSVLKMKNFFSTKTDY
FNETTILVWVWPFGQTFDLTSCQAMFNIQGCHLTTDRSLYNKSHAVLIHHRDISWDLTNL
PQQARPPFQKWIWMNLESPTHTPQKSGIEHLFNLTLTYRRDSDIQVPYGFLTVSTNPFVF
EVPSKEKLVCWVVSNWNPEHARVKYYNELSKSIEIHTYGQAFGEYVNDKNLIPTISACKF
YLSFENSIHKDYITEKLYNAFLAGSVPVVLGPSRENYENYIPADSFIHVEDYNSPSELAK
YLKEVDKNNKLYLSYFNWRKDFTVNLPRFWESHACLACDHVKRHQEYKSVGNLEKWFWN
Enzyme 69 Number of Residues 359
Enzyme 69 Molecular Weight 42040.7
Enzyme 69 Theoretical pI 7.77
Enzyme 69 GO Classification
Function
  • catalytic activity
  • fucosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • membrane
Enzyme 69 General Function Involved in fucosyltransferase activity
Enzyme 69 Specific Function Transfers a fucose to lacto-N-neotetraose but not to either alpha2,3-sialyl lacto-N-neotetraose or lacto-N-tetraose. Can catalyze the last step in the biosynthesis of Lewis antigen, the addition of a fucose to precursor polysaccharides
Enzyme 69 Pathways Not Available
Enzyme 69 Reactions Not Available
Enzyme 69 Pfam Domain Function
Enzyme 69 Signals
  • None
Enzyme 69 Transmembrane Regions
  • 12-32
Enzyme 69 Essentiality Not Available
Enzyme 69 GenBank ID Protein 5139693 Link Image
Enzyme 69 UniProtKB/Swiss-Prot ID Q9Y231 Link Image
Enzyme 69 UniProtKB/Swiss-Prot Entry Name FUT9_HUMAN Link Image
Enzyme 69 PDB ID Not Available
Enzyme 69 Cellular Location Not Available
Enzyme 69 Gene Sequence >1080 bp
ATGACATCAACATCCAAAGGAATTCTTCGCCCATTTTTAATTGTCTGCATTATCCTGGGC
TGTTTCATGGCATGTCTTCTCATTTACATCAAACCTACCAACAGCTGGATCTTCAGTCCA
ATGGAATCAGCCAGCTCTGTGCTGAAAATGAAAAACTTCTTTTCCACCAAAACTGATTAT
TTTAATGAAACTACTATTCTGGTGTGGGTGTGGCCATTTGGGCAGACCTTTGACCTTACA
TCCTGCCAAGCAATGTTCAACATCCAAGGATGCCATCTCACAACGGACCGTTCACTGTAC
AACAAATCCCATGCAGTTCTGATCCATCACCGAGACATCAGTTGGGATCTGACAAATTTA
CCTCAGCAAGCTAGGCCACCCTTCCAGAAATGGATTTGGATGAATTTGGAATCACCAACT
CACACTCCCCAAAAGAGTGGCATTGAGCACTTGTTTAACCTGACTCTGACTTACCGCCGT
GATTCAGATATCCAAGTGCCTTATGGCTTCTTGACGGTAAGCACAAATCCCTTCGTGTTT
GAAGTGCCAAGCAAAGAGAAATTGGTGTGCTGGGTTGTGAGTAACTGGAACCCTGAGCAT
GCCAGAGTCAAGTATTACAATGAGCTAAGCAAAAGCATTGAAATCCATACCTACGGGCAA
GCATTTGGAGAATATGTCAATGATAAAAATTTGATTCCTACCATATCTGCTTGTAAATTT
TATCTTTCCTTTGAAAATTCAATCCACAAGGATTACATCACGGAAAAGCTATACAATGCT
TTTCTGGCTGGCTCTGTACCTGTTGTTCTGGGACCATCTAGGGAAAACTATGAGAATTAT
ATTCCAGCAGATTCATTCATTCATGTGGAAGATTATAACTCTCCCAGTGAGCTAGCAAAG
TATCTGAAGGAAGTCGACAAAAACAATAAGTTATACCTTAGTTACTTTAACTGGAGGAAG
GATTTCACTGTAAATCTTCCACGATTTTGGGAATCACATGCATGTTTGGCTTGCGATCAT
GTGAAAAGGCATCAAGAATATAAGTCTGTTGGTAATTTAGAGAAATGGTTTTGGAATTAA
Enzyme 69 GenBank Gene ID AB023021 Link Image
Enzyme 69 GeneCard ID FUT9 Link Image
Enzyme 69 GenAtlas ID FUT9 Link Image
Enzyme 69 HGNC ID HGNC:4020 Link Image
Enzyme 69 Chromosome Location 6
Enzyme 69 Locus 6q16
Enzyme 69 SNPs SNPJam Report Link Image
Enzyme 69 General References
  1. Kaneko M, Kudo T, Iwasaki H, Ikehara Y, Nishihara S, Nakagawa S, Sasaki K, Shiina T, Inoko H, Saitou N, Narimatsu H: Alpha1,3-fucosyltransferase IX (Fuc-TIX) is very highly conserved between human and mouse; molecular cloning, characterization and tissue distribution of human Fuc-TIX. FEBS Lett. 1999 Jun 11;452(3):237-42. [PubMed Link Image]
  2. Cailleau-Thomas A, Coullin P, Candelier JJ, Balanzino L, Mennesson B, Oriol R, Mollicone R: FUT4 and FUT9 genes are expressed early in human embryogenesis. Glycobiology. 2000 Aug;10(8):789-802. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 69 Metabolite References Not Available
Enzyme 70 [top]
Enzyme 70 ID 11524
Enzyme 70 Name Alpha-(1,6)-fucosyltransferase
Enzyme 70 Synonyms
  1. alpha1-6FucT
  2. Fucosyltransferase 8
  3. GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase
  4. GDP-fucose--glycoprotein fucosyltransferase
  5. Glycoprotein 6-alpha-L-fucosyltransferase
Enzyme 70 Gene Name FUT8
Enzyme 70 Protein Sequence >Alpha-(1,6)-fucosyltransferase
MRPWTGSWRWIMLILFAWGTLLFYIGGHLVRDNDHPDHSSRELSKILAKLERLKQQNEDL
RRMAESLRIPEGPIDQGPAIGRVRVLEEQLVKAKEQIENYKKQTRNGLGKDHEILRRRIE
NGAKELWFFLQSELKKLKNLEGNELQRHADEFLLDLGHHERSIMTDLYYLSQTDGAGDWR
EKEAKDLTELVQRRITYLQNPKDCSKAKKLVCNINKGCGYGCQLHHVVYCFMIAYGTQRT
LILESQNWRYATGGWETVFRPVSETCTDRSGISTGHWSGEVKDKNVQVVELPIVDSLHPR
PPYLPLAVPEDLADRLVRVHGDPAVWWVSQFVKYLIRPQPWLEKEIEEATKKLGFKHPVI
GVHVRRTDKVGTEAAFHPIEEYMVHVEEHFQLLARRMQVDKKRVYLATDDPSLLKEAKTK
YPNYEFISDNSISWSAGLHNRYTENSLRGVILDIHFLSQADFLVCTFSSQVCRVAYEIMQ
TLHPDASANFHSLDDIYYFGGQNAHNQIAIYAHQPRTADEIPMEPGDIIGVAGNHWDGYS
KGVNRKLGRTGLYPSYKVREKIETVKYPTYPEAEK
Enzyme 70 Number of Residues 575
Enzyme 70 Molecular Weight 66515.3
Enzyme 70 Theoretical pI 7.72
Enzyme 70 GO Classification
Function
  • alpha(1,6)-fucosyltransferase activity
  • catalytic activity
  • fucosyltransferase activity
  • glycoprotein 6-alpha-L-fucosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein amino acid glycosylation in Golgi
  • protein modification process
Component
  • Golgi cisterna membrane
  • Golgi membrane
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
  • organelle membrane
Enzyme 70 General Function Involved in glycoprotein 6-alpha-L-fucosyltransferase activity
Enzyme 70 Specific Function Catalyzes the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue, next to the peptide chains in N-glycans
Enzyme 70 Pathways
Enzyme 70 Reactions
  • GDP-beta-L-fucose + N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N- acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D- mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D- glucosaminyl}asparagine = GDP + N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N- acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D- mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L- fucosyl-(1->6)]-N-acetyl-beta-D-glucosaminyl}asparagine [RN:R05988]
Enzyme 70 Pfam Domain Function Not Available
Enzyme 70 Signals
  • None
Enzyme 70 Transmembrane Regions
  • 10-30
Enzyme 70 Essentiality Not Available
Enzyme 70 GenBank ID Protein 30410724 Link Image
Enzyme 70 UniProtKB/Swiss-Prot ID Q9BYC5 Link Image
Enzyme 70 UniProtKB/Swiss-Prot Entry Name FUT8_HUMAN Link Image
Enzyme 70 PDB ID Not Available
Enzyme 70 Cellular Location Not Available
Enzyme 70 Gene Sequence >1728 bp
ATGCGGCCATGGACTGGTTCCTGGCGTTGGATTATGCTCATTCTTTTTGCCTGGGGGACC
TTGCTGTTTTATATAGGTGGTCACTTGGTACGAGATAATGACCATCCTGATCACTCTAGC
CGAGAACTGTCCAAGATTCTGGCAAAGCTTGAACGCTTAAAACAACAGAATGAAGACTTG
AGGCGAATGGCCGAATCTCTCCGGATACCAGAAGGCCCTATTGATCAGGGGCCAGCTATA
GGAAGAGTACGCGTTTTAGAAGAGCAGCTTGTTAAGGCCAAAGAACAGATTGAAAATTAC
AAGAAACAGACCAGAAATGGTCTGGGGAAGGATCATGAAATCCTGAGGAGGAGGATTGAA
AATGGAGCTAAAGAGCTCTGGTTTTTCCTACAGAGTGAATTGAAGAAATTAAAGAACTTA
GAAGGAAATGAACTCCAAAGACATGCAGATGAATTTCTTTTGGATTTAGGACATCATGAA
AGGTCTATAATGACGGATCTATACTACCTCAGTCAGACAGATGGAGCAGGTGATTGGCGG
GAAAAAGAGGCCAAAGATCTGACAGAACTGGTTCAGCGGAGAATAACATATCTTCAGAAT
CCCAAGGACTGCAGCAAAGCCAAAAAGCTGGTGTGTAATATCAACAAAGGCTGTGGCTAT
GGCTGTCAGCTCCATCATGTGGTCTACTGCTTCATGATTGCATATGGCACCCAGCGAACA
CTCATCTTGGAATCTCAGAATTGGCGCTATGCTACTGGTGGATGGGAGACTGTATTTAGG
CCTGTAAGTGAGACATGCACAGACAGATCTGGCATCTCCACTGGACACTGGTCAGGTGAA
GTGAAGGACAAAAATGTTCAAGTGGTCGAGCTTCCCATTGTAGACAGTCTTCATCCCCGT
CCTCCATATTTACCCTTGGCTGTACCAGAAGACCTCGCAGATCGACTTGTACGAGTGCAT
GGTGACCCTGCAGTGTGGTGGGTGTCTCAGTTTGTCAAATACTTGATCCGCCCACAGCCT
TGGCTAGAAAAAGAAATAGAAGAAGCCACCAAGAAGCTTGGCTTCAAACATCCAGTTATT
GGAGTCCATGTCAGACGCACAGACAAAGTGGGAACAGAAGCTGCCTTCCATCCCATTGAA
GAGTACATGGTGCATGTTGAAGAACATTTTCAGCTTCTTGCACGCAGAATGCAAGTGGAC
AAAAAAAGAGTGTATTTGGCCACAGATGACCCTTCTTTATTAAAGGAGGCAAAAACAAAG
TACCCCAATTATGAATTTATTAGTGATAACTCTATTTCCTGGTCAGCTGGACTGCACAAT
CGATACACAGAAAATTCACTTCGTGGAGTGATCCTGGATATACATTTTCTCTCTCAGGCA
GACTTCCTAGTGTGTACTTTTTCATCCCAGGTCTGTCGAGTTGCTTATGAAATTATGCAA
ACACTACATCCTGATGCCTCTGCAAACTTCCATTCTTTAGATGACATCTACTATTTTGGG
GGCCAGAATGCCCACAATCAAATTGCCATTTATGCTCACCAACCCCGAACTGCAGATGAA
ATTCCCATGGAACCTGGAGATATCATTGGTGTGGCTGGAAATCATTGGGATGGCTATTCT
AAAGGTGTCAACAGGAAATTGGGAAGGACGGGCCTATATCCCTCCTACAAAGTTCGAGAG
AAGATAGAAACGGTCAAGTACCCCACATATCCTGAGGCTGAGAAATAA
Enzyme 70 GenBank Gene ID NM_178154.1 Link Image
Enzyme 70 GeneCard ID FUT8 Link Image
Enzyme 70 GenAtlas ID FUT8 Link Image
Enzyme 70 HGNC ID HGNC:4019 Link Image
Enzyme 70 Chromosome Location 1
Enzyme 70 Locus 14q24.3
Enzyme 70 SNPs SNPJam Report Link Image
Enzyme 70 General References
  1. Yanagidani S, Uozumi N, Ihara Y, Miyoshi E, Yamaguchi N, Taniguchi N: Purification and cDNA cloning of GDP-L-Fuc:N-acetyl-beta-D-glucosaminide:alpha1-6 fucosyltransferase (alpha1-6 FucT) from human gastric cancer MKN45 cells. J Biochem. 1997 Mar;121(3):626-32. [PubMed Link Image]
  2. Yamaguchi Y, Ikeda Y, Takahashi T, Ihara H, Tanaka T, Sasho C, Uozumi N, Yanagidani S, Inoue S, Fujii J, Taniguchi N: Genomic structure and promoter analysis of the human alpha1, 6-fucosyltransferase gene (FUT8). Glycobiology. 2000 Jun;10(6):637-43. [PubMed Link Image]
  3. Takahashi T, Ikeda Y, Tateishi A, Yamaguchi Y, Ishikawa M, Taniguchi N: A sequence motif involved in the donor substrate binding by alpha1,6-fucosyltransferase: the role of the conserved arginine residues. Glycobiology. 2000 May;10(5):503-10. [PubMed Link Image]
Enzyme 70 Metabolite References Not Available
Enzyme 71 [top]
Enzyme 71 ID 12965
Enzyme 71 Name Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
Enzyme 71 Synonyms
  1. P-Rex1
  2. PtdIns(3,4,5)-dependent Rac exchanger 1
Enzyme 71 Gene Name PREX1
Enzyme 71 Protein Sequence >Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
MEAPSGSEPGGDGAGDCAHPDPRAPGAAAPSSGPGPCAAARESERQLRLRLCVLNEILGT
ERDYVGTLRFLQSAFLHRIRQNVADSVEKGLTEENVKVLFSNIEDILEVHKDFLAALEYC
LHPEPQSQHELGNVFLKFKDKFCVYEEYCSNHEKALRLLVELNKIPTVRAFLLSCMLLGG
RKTTDIPLEGYLLSPIQRICKYPLLLKELAKRTPGKHPDHPAVQSALQAMKTVCSNINET
KRQMEKLEALEQLQSHIEGWEGSNLTDICTQLLLQGTLLKISAGNIQERAFFLFDNLLVY
CKRKSRVTGSKKSTKRTKSINGSLYIFRGRINTEVMEVENVEDGTADYHSNGYTVTNGWK
IHNTAKNKWFVCMAKTAEEKQKWLDAIIREREQRESLKLGMERDAYVMIAEKGEKLYHMM
MNKKVNLIKDRRRKLSTVPKCFLGNEFVAWLLEIGEISKTEEGVNLGQALLENGIIHHVS
DKHQFKNEQVMYRFRYDDGTYKARSELEDIMSKGVRLYCRLHSLYTPVIKDRDYHLKTYK
SVLPGSKLVDWLLAQGDCQTREEAVALGVGLCNNGFMHHVLEKSEFRDESQYFRFHADEE
MEGTSSKNKQLRNDFKLVENILAKRLLILPQEEDYGFDIEEKNKAVVVKSVQRGSLAEVA
GLQVGRKIYSINEDLVFLRPFSEVESILNQSFCSRRPLRLLVATKAKEIIKIPDQPDTLC
FQIRGAAPPYVYAVGRGSEAMAAGLCAGQCILKVNGSNVMNDGAPEVLEHFQAFRSRREE
ALGLYQWIYHTHEDAQEARASQEASTEDPSGEQAQEEDQADSAFPLLSLGPRLSLCEDSP
MVTLTVDNVHLEHGVVYEYVSTAGVRCHVLEKIVEPRGCFGLTAKILEAFAANDSVFVEN
CRRLMALSSAIVTMPHFEFRNICDTKLESIGQRIACYQEFAAQLKSRVSPPFKQAPLEPH
PLCGLDFCPTNCHINLMEVSYPKTTPSVGRSFSIRFGRKPSLIGLDPEQGHLNPMSYTQH
CITTMAAPSWKCLPAAEGDPQGQGLHDGSFGPASGTLGQEDRGLSFLLKQEDREIQDAYL
QLFTKLDVALKEMKQYVTQINRLLSTITEPTSGGSCDASLAEEASSLPLVSEESEMDRSD
HGGIKKVCFKVAEEDQEDSGHDTMSYRDSYSECNSNRDSVLSYTSVRSNSSYLGSDEMGS
GDELPCDMRIPSDKQDKLHGCLEHLFNQVDSINALLKGPVMSRAFEETKHFPMNHSLQEF
KQKEECTIRGRSLIQISIQEDPWNLPNSIKTLVDNIQRYVEDGKNQLLLALLKCTDTELQ
LRRDAIFCQALVAAVCTFSKQLLAALGYRYNNNGEYEESSRDASRKWLEQVAATGVLLHC
QSLLSPATVKEERTMLEDIWVTLSELDNVTFSFKQLDENYVANTNVFYHIEGSRQALKVI
FYLDSYHFSKLPSRLEGGASLRLHTALFTKVLENVEGLPSPGSQAAEDLQQDINAQSLEK
VQQYYRKLRAFYLERSNLPTDASTTAVKIDQLIRPINALDELCRLMKSFVHPKPGAAGSV
GAGLIPISSELCYRLGACQMVMCGTGMQRSTLSVSLEQAAILARSHGLLPKCIMQATDIM
RKQGPRVEILAKNLRVKDQMPQGAPRLYRLCQPPVDGDL
Enzyme 71 Number of Residues 1659
Enzyme 71 Molecular Weight 186201.7
Enzyme 71 Theoretical pI 6.40
Enzyme 71 GO Classification
Function
  • GTPase regulator activity
  • Ras guanyl-nucleotide exchange factor activity
  • Rho guanyl-nucleotide exchange factor activity
  • binding
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • protein binding
  • small GTPase regulator activity
Process
  • biological regulation
  • intracellular signaling pathway
  • regulation of Ras protein signal transduction
  • regulation of Rho protein signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signaling
  • signaling pathway
Component
  • cell part
  • intracellular
Enzyme 71 General Function Involved in intracellular signaling pathway
Enzyme 71 Specific Function Functions as a RAC guanine nucleotide exchange factor (GEF), which activates the Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol-3,4,5-triphosphate and the beta gamma subunits of heterotrimeric G protein. May function downstream of heterotrimeric G proteins in neutrophils
Enzyme 71 Pathways Not Available
Enzyme 71 Reactions Not Available
Enzyme 71 Pfam Domain Function
Enzyme 71 Signals
  • None
Enzyme 71 Transmembrane Regions
  • None
Enzyme 71 Essentiality Not Available
Enzyme 71 GenBank ID Protein 34452732 Link Image
Enzyme 71 UniProtKB/Swiss-Prot ID Q8TCU6 Link Image
Enzyme 71 UniProtKB/Swiss-Prot Entry Name PREX1_HUMAN Link Image
Enzyme 71 PDB ID Not Available
Enzyme 71 Cellular Location Not Available
Enzyme 71 Gene Sequence >4980 bp
ATGGAGGCGCCCAGCGGCAGCGAGCCCGGCGGCGACGGGGCCGGGGACTGCGCCCACCCG
GACCCCCGGGCCCCTGGCGCCGCGGCGCCCAGCTCCGGCCCCGGCCCGTGCGCGGCCGCC
CGGGAGTCCGAGCGCCAGCTGCGCCTCCGCCTCTGCGTCCTCAACGAGATCTTGGGCACC
GAGAGGGACTACGTGGGCACCTTGCGCTTCTTGCAGTCGGCATTCCTGCATCGCATCCGG
CAGAACGTGGCCGACTCAGTGGAGAAGGGCCTCACGGAGGAGAATGTCAAGGTCCTGTTC
TCGAACATCGAAGACATCCTGGAAGTTCATAAGGATTTCTTGGCCGCCTTGGAGTATTGT
TTACACCCGGAGCCGCAGTCTCAGCATGAACTTGGGAATGTTTTCTTAAAATTCAAGGAC
AAGTTCTGCGTGTACGAGGAGTATTGCAGCAACCATGAGAAAGCCCTGAGGCTGCTGGTG
GAGCTGAACAAGATCCCTACCGTGCGCGCCTTCCTTTTGAGCTGCATGCTTCTGGGAGGC
CGGAAGACCACGGACATCCCTTTGGAAGGCTACCTGTTGTCTCCGATCCAGAGGATCTGC
AAGTACCCGCTCCTCCTTAAGGAGCTGGCCAAGAGGACTCCCGGCAAGCACCCAGACCAC
CCCGCGGTCCAGAGTGCCCTGCAGGCCATGAAGACCGTTTGCTCCAACATCAATGAGACC
AAGCGGCAGATGGAGAAGCTGGAAGCCCTGGAGCAGCTGCAGTCCCACATCGAAGGCTGG
GAGGGTTCCAACCTCACAGACATCTGCACTCAGCTCCTCCTGCAAGGGACTTTGTTAAAG
ATCTCTGCGGGCAACATCCAGGAAAGGGCCTTCTTCCTCTTCGACAACCTTCTCGTCTAC
TGCAAGCGGAAATCCAGGGTCACCGGGAGCAAGAAGTCCACCAAGAGGACCAAATCCATC
AACGGCTCCCTCTACATCTTCAGGGGTCGAATCAACACTGAAGTCATGGAGGTGGAGAAT
GTGGAAGATGGGACAGCGGATTACCATAGCAACGGCTATACCGTCACCAACGGCTGGAAG
ATCCACAACACGGCCAAGAATAAGTGGTTTGTCTGCATGGCCAAGACGGCAGAGGAGAAG
CAGAAGTGGCTGGATGCCATCATCCGCGAGCGGGAGCAGCGCGAGAGCCTGAAGCTGGGC
ATGGAGCGTGATGCCTACGTCATGATTGCGGAGAAGGGGGAGAAGCTGTACCACATGATG
ATGAACAAGAAGGTGAACCTCATCAAGGACCGCCGGAGAAAGCTGAGCACTGTCCCCAAG
TGCTTTCTTGGCAATGAGTTCGTTGCCTGGCTCCTAGAAATTGGTGAAATCAGCAAGACG
GAAGAAGGAGTCAACTTGGGCCAAGCCCTGTTGGAGAATGGCATCATCCACCATGTTTCC
GACAAGCACCAGTTCAAGAATGAGCAGGTGATGTATCGCTTCCGCTACGACGATGGCACC
TACAAGGCCCGAAGTGAGCTGGAGGACATCATGTCCAAGGGTGTGAGGCTTTACTGCCGT
CTTCACAGCCTCTACACCCCGGTGATCAAAGACCGTGATTACCACCTGAAGACCTACAAG
TCAGTGCTTCCCGGGAGCAAGCTGGTGGACTGGCTGCTGGCTCAGGGAGACTGCCAGACT
CGGGAGGAGGCAGTGGCGCTCGGCGTGGGTCTGTGCAACAATGGCTTCATGCACCACGTG
CTGGAGAAGAGCGAGTTCAGGGATGAGTCCCAGTACTTCCGCTTTCATGCTGACGAGGAG
ATGGAGGGGACCAGCAGCAAGAACAAACAGCTTCGCAACGACTTCAAGCTGGTGGAGAAC
ATTCTGGCCAAGCGCCTGCTGATCCTGCCCCAGGAGGAGGACTATGGCTTTGACATCGAG
GAGAAGAACAAGGCTGTGGTGGTGAAGTCCGTCCAGAGGGGCTCGCTGGCTGAGGTGGCT
GGCCTGCAGGTGGGGAGGAAGATCTACTCCATCAATGAGGACCTGGTGTTCCTGCGGCCG
TTTTCAGAGGTGGAGTCCATCCTCAACCAGTCCTTCTGCTCCCGCCGCCCTCTGCGCCTC
CTGGTGGCCACGAAGGCCAAAGAGATCATCAAAATCCCCGACCAGCCGGACACACTGTGC
TTCCAGATTCGTGGAGCTGCCCCACCGTACGTCTATGCTGTGGGGAGAGGCTCTGAGGCC
ATGGCTGCAGGGCTCTGTGCTGGTCAGTGCATTCTGAAGGTCAATGGCAGCAACGTGATG
AACGATGGTGCCCCTGAGGTCCTGGAGCACTTCCAGGCATTCCGGAGTCGGCGCGAAGAG
GCCCTGGGCCTGTACCAGTGGATCTACCACACCCATGAGGATGCCCAGGAAGCACGAGCC
AGTCAGGAGGCCTCCACTGAGGACCCCAGTGGCGAGCAGGCCCAGGAGGAAGACCAGGCT
GATTCAGCCTTCCCACTGCTGTCCCTGGGTCCCCGGCTGAGCCTGTGTGAGGACAGCCCC
ATGGTCACCCTGACTGTGGACAACGTGCACCTGGAACACGGCGTGGTGTATGAGTATGTG
AGCACGGCAGGCGTCAGGTGCCATGTGCTGGAGAAGATCGTGGAGCCCCGCGGCTGCTTC
GGCCTCACCGCCAAGATCCTCGAGGCCTTTGCTGCCAATGACAGCGTCTTCGTGGAGAAC
TGCAGGCGGCTCATGGCCCTGAGCAGCGCCATCGTGACCATGCCCCACTTTGAGTTCCGC
AACATCTGTGACACCAAGCTGGAGAGCATTGGCCAGAGGATTGCCTGCTACCAGGAGTTT
GCAGCCCAACTGAAGAGCAGGGTCAGCCCACCCTTCAAACAAGCCCCCCTGGAGCCCCAC
CCGCTGTGTGGCCTGGACTTCTGCCCCACCAATTGCCACATCAACCTCATGGAAGTGTCC
TACCCCAAGACCACCCCCTCAGTGGGCAGGTCCTTCAGCATCCGCTTTGGACGCAAACCC
TCCCTCATCGGCCTTGACCCGGAGCAAGGCCACCTGAACCCCATGTCGTACACCCAGCAC
TGCATCACCACCATGGCTGCTCCCTCCTGGAAGTGCTTGCCTGCTGCAGAGGGTGATCCC
CAAGGCCAGGGTCTCCATGATGGCAGCTTCGGGCCAGCCAGTGGGACCCTTGGTCAGGAA
GACCGGGGCCTCAGCTTCCTACTCAAGCAGGAGGACCGTGAGATCCAGGATGCCTACCTG
CAGCTCTTCACCAAGCTGGATGTGGCCCTGAAGGAGATGAAGCAATATGTCACCCAGATC
AACAGGCTGCTGTCCACCATCACAGAGCCCACCTCGGGTGGGTCCTGCGACGCATCCTTG
GCTGAGGAGGCCTCCTCCCTGCCCCTGGTCAGTGAAGAGAGCGAGATGGACAGGAGTGAC
CATGGGGGCATCAAGAAGGTGTGCTTCAAGGTGGCCGAGGAGGACCAGGAGGACTCAGGC
CACGACACCATGAGTTATCGCGACTCCTACAGCGAGTGTAACAGCAATCGAGACTCGGTC
CTGTCCTACACCAGCGTGAGAAGTAACAGCTCCTACTTGGGCAGCGACGAGATGGGGTCT
GGAGATGAGCTGCCCTGTGACATGCGGATCCCATCTGACAAGCAGGACAAGCTTCATGGC
TGCCTGGAGCACCTCTTTAACCAGGTGGACTCCATCAATGCTCTCCTCAAGGGGCCAGTC
ATGAGCCGGGCTTTCGAAGAGACCAAGCATTTCCCTATGAACCACAGCTTACAAGAGTTT
AAACAGAAAGAAGAGTGTACAATCCGTGGCCGGAGCCTGATCCAGATTAGCATCCAGGAG
GACCCCTGGAACCTCCCCAACTCCATCAAGACCCTGGTGGACAACATTCAGAGATATGTG
GAAGATGGGAAGAACCAGCTGCTCCTGGCCTTGCTGAAGTGCACAGACACGGAGCTGCAG
CTGCGCAGAGACGCGATCTTCTGCCAGGCCCTGGTGGCCGCCGTGTGCACCTTCTCCGAG
CAGCTGCTGGCGGCCCTGGGCTACCGCTACAACAACAATGGCGAGTACGAGGAGAGCAGC
CGCGACGCCAGCCGCAAGTGGCTGGAGCAGGTGGCGGCCACGGGCGTCCTGCTGCACTGC
CAGTCCCTGCTCTCGCCAGCCACAGTGAAGGAGGAACGGACCATGCTGGAGGACATCTGG
GTGACGCTGTCAGAGCTGGACAATGTCACCTTCTCCTTTAAGCAGCTGGACGAGAACTAT
GTGGCCAACACCAACGTCTTCTACCACATTGAGGGCAGCCGGCAGGCGCTGAAGGTCATC
TTCTACCTCGACAGCTACCACTTCTCCAAGCTGCCCTCCCGCCTGGAGGGTGGGGCCAGC
CTGAGGCTGCACACAGCGCTGTTCACGAAAGTGCTGGAGAACGTGGAGGGGCTGCCTTCT
CCAGGCAGCCAGGCCGCGGAGGATTTGCAGCAGGACATCAACGCGCAGTCCCTGGAGAAA
GTTCAGCAGTATTACCGCAAACTCAGGGCATTTTACCTGGAGCGGTCTAACCTGCCCACG
GATGCCAGCACCACGGCGGTAAAGATAGACCAGCTGATCCGCCCCATCAATGCCCTGGAT
GAGCTCTGCCGCCTCATGAAGTCCTTTGTCCACCCAAAGCCTGGTGCTGCTGGGAGTGTG
GGCGCCGGCCTCATCCCCATCTCCTCGGAGCTCTGCTACCGCCTGGGGGCCTGCCAGATG
GTCATGTGTGGCACAGGCATGCAGAGGAGCACCCTGAGCGTGTCCCTGGAGCAGGCGGCC
ATCTTGGCACGGAGCCACGGGTTGCTGCCCAAGTGCATCATGCAGGCCACGGACATCATG
CGGAAGCAGGGCCCAAGGGTGGAGATTCTGGCCAAAAACCTGCGAGTCAAGGACCAGATG
CCCCAGGGTGCTCCGCGCCTCTACCGCCTCTGCCAGCCGCCGGTGGATGGGGACCTCTGA
Enzyme 71 GenBank Gene ID NM_020820.3 Link Image
Enzyme 71 GeneCard ID PREX1 Link Image
Enzyme 71 GenAtlas ID PREX1 Link Image
Enzyme 71 HGNC ID HGNC:32594 Link Image
Enzyme 71 Chromosome Location 2
Enzyme 71 Locus 20q13.13
Enzyme 71 SNPs SNPJam Report Link Image
Enzyme 71 General References
  1. Welch HC, Coadwell WJ, Ellson CD, Ferguson GJ, Andrews SR, Erdjument-Bromage H, Tempst P, Hawkins PT, Stephens LR: P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-nucleotide exchange factor for Rac. Cell. 2002 Mar 22;108(6):809-21. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  4. Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Feb 28;7(1):65-73. [PubMed Link Image]
  5. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  8. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
Enzyme 71 Metabolite References Not Available
Enzyme 72 [top]
Enzyme 72 ID 13094
Enzyme 72 Name Ribonucleoside-diphosphate reductase subunit M2 B
Enzyme 72 Synonyms
  1. TP53-inducible ribonucleotide reductase M2 B
  2. p53-inducible ribonucleotide reductase small subunit 2-like protein
  3. p53R2
Enzyme 72 Gene Name RRM2B
Enzyme 72 Protein Sequence >Ribonucleoside-diphosphate reductase subunit M2 B
MGDPERPEAAGLDQDERSSSDTNESEIKSNEEPLLRKSSRRFVIFPIQYPDIWKMYKQAQ
ASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEA
RCFYGFQILIENVHSEMYSLLIDTYIRDPKKREFLFNAIETMPYVKKKADWALRWIADRK
STFGERVVAFAAVEGVFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQ
YLVNKPSEERVREIIVDAVKIEQEFLTEALPVGLIGMNCILMKQYIEFVADRLLVELGFS
KVFQAENPFDFMENISLEGKTNFFEKRVSEYQRFAVMAETTDNVFTLDADF
Enzyme 72 Number of Residues 351
Enzyme 72 Molecular Weight 40736.1
Enzyme 72 Theoretical pI 4.61
Enzyme 72 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH or CH2 groups
  • oxidoreductase activity, acting on CH or CH2 groups, disulfide as acceptor
  • ribonucleoside-diphosphate reductase activity
  • transition metal ion binding
Process
  • cellular nitrogen compound metabolic process
  • deoxyribonucleoside diphosphate metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside diphosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • oxidation reduction
Component
Enzyme 72 General Function Involved in oxidoreductase activity
Enzyme 72 Specific Function Plays a pivotal role in cell survival by repairing damaged DNA in a p53/TP53-dependent manner. Supplies deoxyribonucleotides for DNA repair in cells arrested at G1 or G2. Contains an iron-tyrosyl free radical center required for catalysis. Forms an active ribonucleotide reductase (RNR) complex with RRM1 which is expressed both in resting and proliferating cells in response to DNA damage
Enzyme 72 Pathways
Enzyme 72 Reactions
  • 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin [RN:R04294]
Enzyme 72 Pfam Domain Function
Enzyme 72 Signals
  • None
Enzyme 72 Transmembrane Regions
  • None
Enzyme 72 Essentiality Not Available
Enzyme 72 GenBank ID Protein Not Available
Enzyme 72 UniProtKB/Swiss-Prot ID Q7LG56 Link Image
Enzyme 72 UniProtKB/Swiss-Prot Entry Name RIR2B_HUMAN Link Image
Enzyme 72 PDB ID Not Available
Enzyme 72 Cellular Location Not Available
Enzyme 72 Gene Sequence >1056 bp
ATGGGCGACCCGGAAAGGCCGGAAGCGGCCGGGCTGGATCAGGATGAGAGATCATCTTCA
GACACCAACGAAAGTGAAATAAAGTCAAATGAAGAGCCACTCCTAAGAAAGAGTTCTCGC
CGGTTTGTCATCTTTCCAATCCAGTACCCTGATATTTGGAAAATGTATAAACAGGCACAG
GCTTCCTTCTGGACAGCAGAAGAGGTCGACTTATCAAAGGATCTCCCTCACTGGAACAAG
CTTAAAGCAGATGAGAAGTACTTCATCTCTCACATCTTAGCCTTTTTTGCAGCCAGTGAT
GGAATTGTAAATGAAAATTTGGTGGAGCGCTTTAGTCAGGAGGTGCAGGTTCCAGAGGCT
CGCTGTTTCTATGGCTTTCAAATTCTCATCGAGAATGTTCACTCAGAGATGTACAGTTTG
CTGATAGACACTTACATCAGAGATCCCAAGAAAAGGGAATTTTTATTTAATGCAATTGAA
ACCATGCCCTATGTTAAGAAAAAAGCAGATTGGGCCTTGCGATGGATAGCAGATAGAAAA
TCTACTTTTGGGGAAAGAGTGGTGGCCTTTGCTGCTGTAGAAGGAGTTTTCTTCTCAGGA
TCTTTTGCTGCTATATTCTGGCTAAAGAAGAGAGGTCTTATGCCAGGACTCACTTTTTCC
AATGAACTCATCAGCAGAGATGAAGGACTTCACTGTGACTTTGCTTGCCTGATGTTCCAA
TACTTAGTAAATAAGCCTTCAGAAGAAAGGGTCAGGGAGATCATTGTTGATGCTGTCAAA
ATTGAGCAGGAGTTTTTAACAGAAGCCTTGCCAGTTGGCCTCATTGGAATGAATTGCATT
TTGATGAAACAGTACATTGAGTTTGTAGCTGACAGATTACTTGTGGAACTTGGATTCTCA
AAGGTTTTTCAGGCAGAAAATCCTTTTGATTTTATGGAAAACATTTCTTTAGAAGGAAAA
ACAAATTTCTTTGAGAAACGAGTTTCAGAGTATCAGCGTTTTGCAGTTATGGCAGAAACC
ACAGATAACGTCTTCACCTTGGATGCAGATTTTTAA
Enzyme 72 GenBank Gene ID AB036063 Link Image
Enzyme 72 GeneCard ID RRM2B Link Image
Enzyme 72 GenAtlas ID RRM2B Link Image
Enzyme 72 HGNC ID HGNC:17296 Link Image
Enzyme 72 Chromosome Location 8
Enzyme 72 Locus 8q23.1
Enzyme 72 SNPs SNPJam Report Link Image
Enzyme 72 General References
  1. Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y: A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage. Nature. 2000 Mar 2;404(6773):42-9. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L: Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells. J Biol Chem. 2001 Nov 2;276(44):40647-51. Epub 2001 Aug 21. [PubMed Link Image]
  6. Yamaguchi T, Matsuda K, Sagiya Y, Iwadate M, Fujino MA, Nakamura Y, Arakawa H: p53R2-dependent pathway for DNA synthesis in a p53-regulated cell cycle checkpoint. Cancer Res. 2001 Nov 15;61(22):8256-62. [PubMed Link Image]
  7. Xue L, Zhou B, Liu X, Qiu W, Jin Z, Yen Y: Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits. Cancer Res. 2003 Mar 1;63(5):980-6. [PubMed Link Image]
  8. Zhou B, Liu X, Mo X, Xue L, Darwish D, Qiu W, Shih J, Hwu EB, Luh F, Yen Y: The human ribonucleotide reductase subunit hRRM2 complements p53R2 in response to UV-induced DNA repair in cells with mutant p53. Cancer Res. 2003 Oct 15;63(20):6583-94. [PubMed Link Image]
  9. Qiu W, Zhou B, Darwish D, Shao J, Yen Y: Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits. Biochem Biophys Res Commun. 2006 Feb 10;340(2):428-34. Epub 2005 Dec 15. [PubMed Link Image]
  10. Tyynismaa H, Ylikallio E, Patel M, Molnar MJ, Haller RG, Suomalainen A: A heterozygous truncating mutation in RRM2B causes autosomal-dominant progressive external ophthalmoplegia with multiple mtDNA deletions. Am J Hum Genet. 2009 Aug;85(2):290-5. Epub 2009 Aug 6. [PubMed Link Image]
  11. Smith P, Zhou B, Ho N, Yuan YC, Su L, Tsai SC, Yen Y: 2.6 A X-ray crystal structure of human p53R2, a p53-inducible ribonucleotide reductase . Biochemistry. 2009 Nov 24;48(46):11134-41. [PubMed Link Image]
  12. Bourdon A, Minai L, Serre V, Jais JP, Sarzi E, Aubert S, Chretien D, de Lonlay P, Paquis-Flucklinger V, Arakawa H, Nakamura Y, Munnich A, Rotig A: Mutation of RRM2B, encoding p53-controlled ribonucleotide reductase (p53R2), causes severe mitochondrial DNA depletion. Nat Genet. 2007 Jun;39(6):776-80. Epub 2007 May 7. [PubMed Link Image]
  13. Bornstein B, Area E, Flanigan KM, Ganesh J, Jayakar P, Swoboda KJ, Coku J, Naini A, Shanske S, Tanji K, Hirano M, DiMauro S: Mitochondrial DNA depletion syndrome due to mutations in the RRM2B gene. Neuromuscul Disord. 2008 Jun;18(6):453-9. Epub 2008 May 27. [PubMed Link Image]
Enzyme 72 Metabolite References Not Available
Enzyme 73 [top]
Enzyme 73 ID 13098
Enzyme 73 Name Uridine-cytidine kinase-like 1
Enzyme 73 Synonyms Not Available
Enzyme 73 Gene Name UCKL1
Enzyme 73 Protein Sequence >Uridine-cytidine kinase-like 1
MAAPPARADADPSPTSPPTARDTPGRQAEKSETACEDRSNAESLDRLLPPVGTGRSPRKR
TTSQCKSEPPLLRTSKRTIYTAGRPPWYNEHGTQSKEAFAIGLGGGSASGKTTVARMIIE
ALDVPWVVLLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV
PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRR
DISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQL
EERELSVRAALASAHQCHPLPRTLSVLKSTPQVRGMHTIIRDKETSRDEFIFYSKRLMRL
LIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIG
TILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIF
LLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTDAVPDGSD
EEEVAYTG
Enzyme 73 Number of Residues 548
Enzyme 73 Molecular Weight 61140.4
Enzyme 73 Theoretical pI 7.40
Enzyme 73 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolic process
Component
Enzyme 73 General Function Involved in ATP binding
Enzyme 73 Specific Function May contribute to UTP accumulation needed for blast transformation and proliferation
Enzyme 73 Pathways
Enzyme 73 Reactions
  • ATP + uridine = ADP + UMP [RN:R00964]
Enzyme 73 Pfam Domain Function
Enzyme 73 Signals
  • None
Enzyme 73 Transmembrane Regions
  • None
Enzyme 73 Essentiality Not Available
Enzyme 73 GenBank ID Protein 57863312 Link Image
Enzyme 73 UniProtKB/Swiss-Prot ID Q9NWZ5 Link Image
Enzyme 73 UniProtKB/Swiss-Prot Entry Name UCKL1_HUMAN Link Image
Enzyme 73 PDB ID Not Available
Enzyme 73 Cellular Location Not Available
Enzyme 73 Gene Sequence >1647 bp
ATGGCTGCGCCCCCGGCCCGCGCGGACGCTGATCCTTCGCCCACGTCGCCACCTACGGCC
CGAGACACACCAGGCCGGCAGGCTGAGAAAAGCGAGACCGCGTGCGAGGACCGCAGCAAT
GCAGAGTCCCTGGACAGGCTCCTGCCACCTGTGGGCACTGGGCGCTCTCCCCGGAAGCGG
ACCACCAGCCAGTGCAAGTCAGAGCCTCCCCTGCTGCGTACAAGCAAGCGTACCATCTAC
ACCGCCGGGCGGCCGCCCTGGTACAATGAACACGGCACGCAATCCAAAGAGGCCTTCGCC
ATCGGCTTGGGAGGCGGCAGTGCCTCTGGGAAGACCACTGTGGCCAGAATGATCATCGAG
GCCCTGGATGTGCCCTGGGTGGTCTTGCTGTCCATGGACTCCTTCTACAAGGTGCTGACT
GAGCAGCAGCAGGAACAGGCCGCACACAACAACTTCAACTTCGACCACCCAGATGCCTTT
GACTTCGACCTCATCATTTCCACCCTCAAGAAGCTGAAGCAGGGGAAGAGTGTCAAGGTG
CCCATTTATGACTTCACCACGCACAGCCGGAAGAAGGACTGGAAAACACTGTATGGTGCA
AACGTCATCATCTTTGAGGGCATCATGGCCTTTGCTGACAAGACACTGTTGGAGCTCCTG
GACATGAAGATCTTTGTGGACACAGACTCCGACATCCGCCTGGTACGGCGGCTGCGCCGG
GACATCAGTGAGCGCGGCCGGGACATCGAGGGTGTCATCAAGCAGTACAACAAGTTTGTC
AAGCCCTCCTTCGACCAGTACATCCAGCCCACCATGCGCCTGGCAGACATCGTGGTCCCC
AGAGGGAGCGGCAACACGGTGGCCATCGACCTGATTGTGCAGCACGTGCACAGCCAGCTG
GAGGAGCGTGAACTCAGCGTCAGGGCTGCGCTGGCCTCGGCACACCAGTGCCACCCGCTG
CCCCGGACGCTGAGCGTCCTGAAGAGCACGCCGCAGGTACGGGGCATGCACACCATCATC
AGGGACAAGGAGACCAGTCGCGACGAGTTCATCTTCTACTCCAAGAGACTGATGCGGCTG
CTCATCGAGCACGCGCTCTCCTTCCTGCCCTTTCAGGACTGCGTCGTACAGACCCCGCAG
GGGCAGGACTATGCGGGCAAGTGCTATGCGGGGAAGCAGATCACCGGTGTGTCCATTCTG
CGCGCCGGTGAAACCATGGAGCCCGCGCTGCGCGCTGTGTGCAAAGACGTGCGCATCGGC
ACCATCCTCATCCAGACCAACCAGCTTACCGGGGAGCCCGAGCTCCACTACCTGAGGCTG
CCCAAGGACATCAGCGATGACCACGTGATCCTCATGGACTGCACCGTGTCCACGGGCGCG
GCGGCCATGATGGCAGTGCGCGTGCTCCTGGACCACGACGTGCCTGAGGACAAGATCTTT
TTGCTGTCGCTGCTCATGGCAGAGATGGGCGTGCACTCAGTGGCCTATGCATTTCCGCGA
GTGAGAATCATCACCACGGCGGTGGACAAGCGGGTCAATGACCTTTTCCGCATCATCCCA
GGCATTGGGAACTTTGGCGACCGCTACTTTGGGACAGACGCGGTCCCCGATGGCAGTGAC
GAGGAGGAAGTGGCCTACACGGGTTAG
Enzyme 73 GenBank Gene ID NM_017859.3 Link Image
Enzyme 73 GeneCard ID UCKL1 Link Image
Enzyme 73 GenAtlas ID UCKL1 Link Image
Enzyme 73 HGNC ID HGNC:15938 Link Image
Enzyme 73 Chromosome Location 2
Enzyme 73 Locus 20q13.33
Enzyme 73 SNPs SNPJam Report Link Image
Enzyme 73 General References
  1. Kashuba E, Kashuba V, Sandalova T, Klein G, Szekely L: Epstein-Barr virus encoded nuclear protein EBNA-3 binds a novel human uridine kinase/uracil phosphoribosyltransferase. BMC Cell Biol. 2002 Aug 29;3:23. Epub 2002 Aug 29. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Fortier JM, Kornbluth J: NK lytic-associated molecule, involved in NK cytotoxic function, is an E3 ligase. J Immunol. 2006 Jun 1;176(11):6454-63. [PubMed Link Image]
  6. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  7. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  8. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 73 Metabolite References Not Available
Enzyme 74 [top]
Enzyme 74 ID 13379
Enzyme 74 Name Ectonucleoside triphosphate diphosphohydrolase 8
Enzyme 74 Synonyms
  1. E-NTPDase 8
  2. NTPDase 8
  3. NTPDase8
Enzyme 74 Gene Name ENTPD8
Enzyme 74 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 8
MGLSRKEQVFLALLGASGVSGLTALILLLVEATSVLLPTDIKFGIVFDAGSSHTSLFLYQ
WLANKENGTGVVSQALACQVEGPGISSYTSNAAQAGESLQGCLEEALVLIPEAQHRKTPT
FLGATAGMRLLSRKNSSQARDIFAAVTQVLGRSPVDFWGAELLAGQAEGAFGWITVNYGL
GTLVKYSFTGEWIQPPEEMLVGALDMGGASTQITFVPGGPILDKSTQADFRLYGSDYSVY
THSYLCFGRDQMLSRLLVGLVQSRPAALLRHPCYLSGYQTTLALGPLYESPCVHATPPLS
LPQNLTVEGTGNPGACVSAIRELFNFSSCQGQEDCAFDGVYQPPLRGQFYAFSNFYYTFH
FLNLTSRQPLSTVNATIWEFCQRPWKLVEASYPGQDRWLRDYCASGLYILTLLHEGYGFS
EETWPSLEFRKQAGGVDIGWTLGYMLNLTGMIPADAPAQWRAESYGVWVAKVVFMVLALV
AVVGAALVQLFWLQD
Enzyme 74 Number of Residues 495
Enzyme 74 Molecular Weight 53903.1
Enzyme 74 Theoretical pI 4.96
Enzyme 74 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 74 General Function Involved in hydrolase activity
Enzyme 74 Specific Function Canalicular ectonucleoside NTPDase responsible for the main hepatic NTPDase activity. Ectonucleoside NTPDases catalyze the hydrolyzis of gamma- and beta-phosphate residues of nucleotides, playing a central role in concentration of extracellular nucleotides. Has activity toward ATP, ADP, UTP and UDP, but not toward AMP
Enzyme 74 Pathways
Enzyme 74 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
Enzyme 74 Pfam Domain Function
Enzyme 74 Signals
  • None
Enzyme 74 Transmembrane Regions
  • 9-29 472-492
Enzyme 74 Essentiality Not Available
Enzyme 74 GenBank ID Protein 110431368 Link Image
Enzyme 74 UniProtKB/Swiss-Prot ID Q5MY95 Link Image
Enzyme 74 UniProtKB/Swiss-Prot Entry Name ENTP8_HUMAN Link Image
Enzyme 74 PDB ID Not Available
Enzyme 74 Cellular Location Not Available
Enzyme 74 Gene Sequence >1488 bp
ATGGGGCTGTCCCGGAAGGAGCAGGTCTTCTTGGCCCTGCTGGGGGCCTCGGGGGTCTCA
GGCCTCACGGCACTCATTCTCCTCCTGGTGGAGGCCACCAGCGTGCTCCTGCCCACAGAC
ATCAAGTTTGGGATCGTGTTTGATGCGGGCTCCTCCCACACGTCCCTCTTCCTGTATCAG
TGGCTGGCGAACAAGGAGAATGGCACGGGTGTGGTCAGCCAGGCCCTGGCCTGCCAGGTG
GAAGGGCCTGGAATCTCCTCCTACACTTCTAATGCTGCACAGGCTGGTGAGAGCCTGCAG
GGCTGCTTGGAGGAGGCGCTGGTGCTGATCCCAGAGGCCCAGCATCGGAAAACACCCACG
TTCCTGGGGGCCACGGCTGGCATGAGGTTGCTCAGCCGGAAGAACAGCTCTCAGGCCAGG
GACATCTTTGCAGCAGTCACCCAGGTCCTGGGCCGGTCTCCCGTGGACTTTTGGGGTGCC
GAGCTCCTGGCCGGGCAGGCCGAAGGTGCCTTTGGTTGGATCACTGTCAACTACGGCTTG
GGGACGCTGGTCAAGTACTCCTTCACTGGAGAATGGATCCAGCCTCCGGAGGAGATGCTG
GTGGGTGCCCTGGACATGGGAGGGGCCTCCACCCAGATCACGTTCGTGCCTGGGGGCCCC
ATCTTGGACAAGAGCACCCAGGCCGATTTTCGCCTCTACGGCTCCGACTACAGCGTCTAC
ACTCACAGCTACCTGTGCTTTGGACGGGACCAGATGCTGAGCAGGCTCCTCGTGGGGCTG
GTACAGAGCCGCCCGGCTGCCCTGCTCCGTCACCCGTGCTACCTCAGCGGCTACCAGACC
ACACTGGCCCTGGGCCCGCTGTATGAGTCACCCTGTGTCCACGCCACGCCCCCGCTGAGC
CTCCCCCAGAACCTCACAGTTGAAGGGACAGGCAACCCTGGAGCCTGCGTCTCAGCCATC
CGGGAACTTTTCAACTTCTCCAGCTGCCAGGGCCAGGAGGACTGCGCCTTTGACGGGGTC
TACCAGCCCCCGCTGCGGGGCCAGTTCTATGCCTTCTCCAACTTCTACTACACCTTCCAC
TTCCTGAACCTCACCTCCAGGCAGCCCCTGAGCACGGTCAACGCCACCATCTGGGAGTTT
TGCCAGAGGCCCTGGAAACTGGTGGAGGCCAGCTACCCTGGGCAGGACCGCTGGCTGCGG
GACTACTGTGCCTCAGGCCTGTACATCCTCACCCTCCTGCACGAGGGCTACGGGTTCAGC
GAGGAGACCTGGCCCAGCCTCGAGTTCCGAAAGCAGGCGGGCGGTGTGGACATTGGCTGG
ACACTGGGCTACATGCTGAACCTGACCGGGATGATCCCGGCCGATGCGCCGGCTCAGTGG
CGGGCAGAGAGCTACGGCGTCTGGGTGGCCAAAGTGGTGTTCATGGTGCTGGCCCTGGTG
GCGGTGGTGGGGGCTGCCTTGGTCCAGCTCTTCTGGTTGCAGGACTAG
Enzyme 74 GenBank Gene ID NM_001033113.1 Link Image
Enzyme 74 GeneCard ID ENTPD8 Link Image
Enzyme 74 GenAtlas ID ENTPD8 Link Image
Enzyme 74 HGNC ID HGNC:24860 Link Image
Enzyme 74 Chromosome Location 9
Enzyme 74 Locus 9q34.3
Enzyme 74 SNPs SNPJam Report Link Image
Enzyme 74 General References
  1. Knowles AF, Li C: Molecular cloning and characterization of expressed human ecto-nucleoside triphosphate diphosphohydrolase 8 (E-NTPDase 8) and its soluble extracellular domain. Biochemistry. 2006 Jun 13;45(23):7323-33. [PubMed Link Image]
  2. Fausther M, Lecka J, Kukulski F, Levesque SA, Pelletier J, Zimmermann H, Dranoff JA, Sevigny J: Cloning, purification, and identification of the liver canalicular ecto-ATPase as NTPDase8. Am J Physiol Gastrointest Liver Physiol. 2007 Mar;292(3):G785-95. Epub 2006 Nov 9. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Levesque SA, Lavoie EG, Lecka J, Bigonnesse F, Sevigny J: Specificity of the ecto-ATPase inhibitor ARL 67156 on human and mouse ectonucleotidases. Br J Pharmacol. 2007 Sep;152(1):141-50. Epub 2007 Jul 2. [PubMed Link Image]
Enzyme 74 Metabolite References Not Available
Enzyme 75 [top]
Enzyme 75 ID 13877
Enzyme 75 Name Synembryn-B
Enzyme 75 Synonyms
  1. Brain synembrin
  2. hSyn
  3. Protein Ric-8B
Enzyme 75 Gene Name RIC8B
Enzyme 75 Protein Sequence >Synembryn-B
MDEERALYIVRAGEAGAIERVLRDYSDKHRATFKFESTDEDKRKKLCEGIFKVLIKDIPT
TCQVSCLEVLRILSRDKKVLVPVTTKENMQILLRLAKLNELDDSLEKVSEFPVIVESLKC
LCNIVFNSQMAQQLSLELNLAAKLCNLLRKCKDRKFINDIKCFDLRLLFLLSLLHTDIRS
QLRYELQGLPLLTQILESAFSIKWTDEYESAIDHNGPPLSPQETDCAIEALKALFNVTVD
SWKVHKESDSHQFRVMAAVLRHCLLIVGPTEDKTEELHSNAVNLLSNVPVSCLDVLICPL
THEETAQEATTLDELPSNKTAEKETVLKNNTMVYNGMNMEAIHVLLNFMEKRIDKGSSYR
EGLTPVLSLLTECSRAHRNIRKFLKDQVLPPLRDVTNRPEVGSTVRNKLVRLMTHVDLGV
KQIAAEFLFVLCKERVDSLLKYTGYGNAAGLLAARGLLAGGRGDNWYSEDEDTDTEEYKN
AKPKEELLKPMGLKPDGTITPLEEALNQYSVIEETSSDTD
Enzyme 75 Number of Residues 520
Enzyme 75 Molecular Weight 58824.1
Enzyme 75 Theoretical pI 5.45
Enzyme 75 GO Classification
Function
  • binding
Process
Component
Enzyme 75 General Function Involved in binding
Enzyme 75 Specific Function Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins by exchanging bound GDP for free GTP. Able to potentiate G(olf)-alpha- dependent cAMP accumulation suggesting that it may be an important component for odorant signal transduction
Enzyme 75 Pathways Not Available
Enzyme 75 Reactions Not Available
Enzyme 75 Pfam Domain Function
Enzyme 75 Signals
  • None
Enzyme 75 Transmembrane Regions
  • None
Enzyme 75 Essentiality Not Available
Enzyme 75 GenBank ID Protein 124375842 Link Image
Enzyme 75 UniProtKB/Swiss-Prot ID Q9NVN3 Link Image
Enzyme 75 UniProtKB/Swiss-Prot Entry Name RIC8B_HUMAN Link Image
Enzyme 75 PDB ID Not Available
Enzyme 75 Cellular Location Not Available
Enzyme 75 Gene Sequence >1563 bp
ATGGATGAGGAGCGCGCCCTCTACATCGTCCGGGCCGGCGAAGCAGGGGCTATCGAGCGG
GTCCTGAGGGATTACAGCGACAAGCATAGGGCTACTTTCAAATTTGAATCAACAGATGAA
GATAAAAGAAAGAAACTCTGTGAAGGCATATTTAAAGTCCTTATAAAGGACATCCCAACA
ACATGTCAAGTGTCCTGCCTGGAAGTACTCCGCATTCTCTCCAGAGACAAAAAGGTTTTA
GTTCCTGTGACAACTAAGGAAAATATGCAGATACTGCTGCGACTAGCCAAGCTAAATGAG
TTAGATGATTCTTTGGAGAAAGTATCAGAGTTCCCAGTTATTGTGGAGTCATTAAAATGT
CTGTGTAATATAGTGTTCAACAGTCAGATGGCACAGCAGCTCAGCCTGGAACTTAATCTT
GCTGCAAAGCTCTGTAACCTCCTGAGAAAGTGCAAGGACCGGAAATTTATCAATGACATT
AAGTGCTTTGACTTGCGCTTGCTCTTCCTTCTGTCACTTTTGCACACCGACATCAGGTCA
CAATTGCGCTATGAGCTCCAGGGACTACCGCTGCTAACGCAGATCTTGGAAAGTGCCTTT
AGCATCAAGTGGACCGATGAGTATGAATCGGCCATAGACCATAATGGACCTCCTCTCTCA
CCTCAGGAGACAGACTGTGCCATTGAGGCCCTCAAAGCTCTCTTCAATGTGACGGTAGAC
AGTTGGAAGGTGCATAAAGAGAGTGATTCTCATCAGTTCCGTGTAATGGCAGCTGTCCTT
CGTCATTGTTTACTAATCGTAGGTCCAACTGAAGACAAAACAGAAGAGCTACACAGCAAT
GCAGTCAACCTTTTAAGCAATGTTCCAGTCTCTTGTTTGGATGTTCTCATTTGTCCGTTA
ACCCATGAAGAAACAGCCCAAGAGGCAACGACTCTAGATGAACTGCCCAGTAATAAAACA
GCTGAGAAAGAAACAGTTTTGAAAAACAATACCATGGTATACAATGGTATGAATATGGAG
GCCATTCATGTTTTACTGAATTTTATGGAGAAGAGAATAGACAAGGGAAGCAGCTATAGA
GAGGGTCTAACTCCAGTTCTCAGCTTATTAACCGAATGTTCCCGAGCCCATCGAAACATC
CGAAAATTTCTCAAAGATCAGGTTTTACCACCGTTGAGGGATGTGACAAATCGACCTGAA
GTTGGCTCAACTGTGAGAAATAAGCTGGTGCGCCTCATGACACATGTTGACCTTGGAGTC
AAGCAAATTGCTGCTGAATTCCTTTTTGTCCTTTGCAAAGAGAGAGTGGATAGTCTGCTG
AAATACACTGGCTATGGGAATGCTGCAGGACTGTTGGCGGCCAGGGGCCTCTTGGCTGGA
GGAAGAGGAGATAATTGGTACTCAGAGGATGAGGACACAGACACTGAAGAATACAAAAAT
GCAAAACCAAAAGAGGAGTTGCTTAAACCAATGGGACTAAAACCTGATGGGACAATAACG
CCTTTGGAGGAAGCACTCAACCAGTACTCTGTCATCGAAGAGACCAGCTCTGACACAGAC
TAA
Enzyme 75 GenBank Gene ID BC132689 Link Image
Enzyme 75 GeneCard ID RIC8B Link Image
Enzyme 75 GenAtlas ID RIC8B Link Image
Enzyme 75 HGNC ID HGNC:25555 Link Image
Enzyme 75 Chromosome Location 1
Enzyme 75 Locus 12q23.3
Enzyme 75 SNPs SNPJam Report Link Image
Enzyme 75 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Klattenhoff C, Montecino M, Soto X, Guzman L, Romo X, Garcia MA, Mellstrom B, Naranjo JR, Hinrichs MV, Olate J: Human brain synembryn interacts with Gsalpha and Gqalpha and is translocated to the plasma membrane in response to isoproterenol and carbachol. J Cell Physiol. 2003 May;195(2):151-7. [PubMed Link Image]
  5. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 75 Metabolite References Not Available
Enzyme 76 [top]
Enzyme 76 ID 13881
Enzyme 76 Name Rap guanine nucleotide exchange factor 6
Enzyme 76 Synonyms
  1. PDZ domain-containing guanine nucleotide exchange factor 2
  2. PDZ-GEF2
  3. RA-GEF-2
Enzyme 76 Gene Name RAPGEF6
Enzyme 76 Protein Sequence >Rap guanine nucleotide exchange factor 6
MNSPVDPGARQALRKKPPERTPEDLNTIYSYLHGMEILSNLREHQLRLMSARARYERYSG
NQVLFCSETIARCWYILLSGSVLVKGSMVLPPCSFGKQFGGKRGCDCLVLEPSEMIVVEN
AKDNEDSILQREIPARQSRRRFRKINYKGERQTITDDVEVNSYLSLPADLTKMHLTENPH
PQVTHVSSSQSGCSIASDSGSSSLSDIYQATESEVGDVDLTRLPEGPVDSEDDEEEDEEI
DRTDPLQGRDLVRECLEKEPADKTDDDIEQLLEFMHQLPAFANMTMSVRRELCSVMIFEV
VEQAGAIILEDGQELDSWYVILNGTVEISHPDGKVENLFMGNSFGITPTLDKQYMHGIVR
TKVDDCQFVCIAQQDYWRILNHVEKNTHKVEEEGEIVMVHEHRELDRSGTRKGHIVIKAT
PERLIMHLIEEHSIVDPTYIEDFLLTYRTFLESPLDVGIKLLEWFKIDSLRDKVTRIVLL
WVNNHFNDFEGDPAMTRFLEEFEKNLEDTKMNGHLRLLNIACAAKAKWRQVVLQKASRES
PLQFSLNGGSEKGFGIFVEGVEPGSEAADSGLKRGDQIMEVNGQNFENITFMKAVEILRN
NTHLALTVKTNIFVFKELPFRTEQEKSGVPHIPKIAKKKSNRHSIQHVPGDIEQTSQEKG
SKKVKANTASGGRNKIRKILDKTRFSILPPKLFSDGGLSQSQDDSIVGTRHCRHSLAIMP
IPGTLSSSSPDLLQPTTSMLDFSNPSDIPDQVIRVFKVDQQSCYIIISKDTTAKEVVFHA
VHEFGLTGASDTYSLCEVSVTPEGVIKQRRLPDQFSKLADRIQLNGRYYLKNNMETETLC
SDEDAQELVKESQLSMLQLSTIEVATQLSMRDFDLFRNIEPTEYIDDLFKLNSKTGNTHL
KRFEDIVNQETFWVASEILTEANQLKRMKIIKHFIKIALHCRECKNFNSMFAIISGLNLA
SVARLRGTWEKLPSKYEKHLQDLQDIFDPSRNMAKYRNILSSQSMQPPIIPLFPVVKKDM
TFLHEGNDSKVDGLVNFEKLRMISKEIRQVVRMTSANMDPAMMFRQRSLSQGSTNSNMLD
VQGGAHKKRARRSSLLNAKKLYEDAQMARKVKQYLSSLDVETDEEKFQMMSLQWEPAYGT
LTKNLSEKRSAKSSEMSPVPMRSAGQTTKAHLHQPHRVSQVLQVPAVNLHPIRKKGQTKD
PALNTSLPQKVLGTTEEISGKKHTEDTISVASSLHSSPPASPQGSPHKGYTLIPSAKSDN
LSDSSHSEISSRSSIVSNCSVDSMSAALQDERCSSQALAVPESTGALEKTEHASGIGDHS
QHGPGWTLLKPSLIKCLAVSSSVSNEEISQEHIIIEAADSGRGSWTSCSSSSHDNFQSLP
NPKSWDFLNSYRHTHLDDPIAEVEPTDSEPYSCSKSCSRTCGQCKGSLERKSWTSSSSLS
DTYEPNYGTVKRRVLESTPAESSEGLDPKDATDPVYKTVTSSTEKGLIVYCVTSPKKDDR
YREPPPTPPGYLGISLADLKEGPHTHLKPPDYSVAVQRSKMMHNSLSRLPPASLSSNLVA
CVPSKIVTQPQRHNLQPFHPKLGDVTDADSEADENEQVSAV
Enzyme 76 Number of Residues 1601
Enzyme 76 Molecular Weight 179405.2
Enzyme 76 Theoretical pI 6.40
Enzyme 76 GO Classification
Function
  • GTPase regulator activity
  • binding
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • protein binding
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 76 General Function Involved in protein binding
Enzyme 76 Specific Function Guanine nucleotide exchange factor (GEF) for Rap1A, Rap2A and M-Ras GTPases. Does not interact with cAMP
Enzyme 76 Pathways Not Available
Enzyme 76 Reactions Not Available
Enzyme 76 Pfam Domain Function
Enzyme 76 Signals
  • None
Enzyme 76 Transmembrane Regions
  • None
Enzyme 76 Essentiality Not Available
Enzyme 76 GenBank ID Protein 256600194 Link Image
Enzyme 76 UniProtKB/Swiss-Prot ID Q8TEU7 Link Image
Enzyme 76 UniProtKB/Swiss-Prot Entry Name RPGF6_HUMAN Link Image
Enzyme 76 PDB ID Not Available
Enzyme 76 Cellular Location Not Available
Enzyme 76 Gene Sequence >4806 bp
ATGAACTCACCCGTGGACCCTGGCGCTAGGCAGGCGTTGAGGAAGAAGCCACCCGAGCGG
ACTCCCGAGGACTTAAATACTATTTATTCTTATCTTCATGGAATGGAAATATTATCAAAT
CTCAGGGAACATCAGCTTAGATTAATGTCTGCAAGAGCACGCTATGAGAGATACAGTGGC
AATCAGGTTCTCTTTTGTTCAGAAACGATTGCCAGATGTTGGTATATCCTACTTTCTGGA
TCTGTGCTTGTGAAAGGCTCCATGGTCTTGCCTCCTTGCAGTTTTGGTAAGCAGTTTGGA
GGAAAAAGAGGATGTGATTGTCTTGTATTAGAGCCTTCAGAAATGATTGTGGTAGAGAAT
GCCAAAGATAATGAAGATAGTATTCTACAAAGAGAAATTCCTGCCAGACAATCCCGAAGA
AGATTTCGGAAAATTAACTATAAAGGAGAGCGCCAAACCATTACTGATGATGTGGAGGTT
AACAGCTATCTTTCTCTTCCAGCTGATCTTACCAAGATGCATCTCACAGAAAACCCTCAT
CCACAGGTGACTCATGTGTCTTCTAGTCAGTCTGGTTGTAGCATTGCCAGTGACTCTGGA
AGCAGCAGTTTATCTGATATCTATCAGGCTACGGAGAGTGAGGTAGGAGATGTAGATTTG
ACACGTCTTCCAGAAGGACCTGTTGATTCTGAGGATGACGAAGAGGAAGATGAAGAGATT
GATCGAACAGATCCATTGCAGGGGCGAGATCTTGTTCGAGAATGTCTTGAAAAAGAACCT
GCAGACAAAACTGATGATGACATTGAACAATTGCTGGAGTTTATGCACCAGCTCCCTGCA
TTTGCAAACATGACCATGTCTGTAAGGAGAGAACTCTGCTCAGTGATGATTTTTGAAGTG
GTAGAGCAGGCTGGAGCTATTATTCTTGAAGATGGGCAAGAGCTTGACTCATGGTATGTT
ATTTTAAACGGCACTGTGGAAATCAGTCATCCAGATGGAAAAGTTGAAAATTTGTTTATG
GGAAATAGTTTTGGAATTACTCCCACTCTGGATAAGCAGTACATGCATGGAATTGTCAGG
ACTAAAGTAGATGATTGTCAGTTTGTCTGCATAGCCCAGCAAGATTATTGGAGAATTTTA
AACCATGTGGAAAAAAATACCCATAAAGTTGAGGAAGAGGGAGAAATTGTTATGGTACAT
GAGCATCGGGAACTAGACCGGAGTGGAACCAGGAAAGGACACATTGTGATCAAGGCAACA
CCTGAGCGTCTCATAATGCATTTAATAGAAGAACATTCCATCGTGGATCCAACTTATATA
GAAGATTTTCTATTAACTTACAGGACATTTCTTGAAAGTCCTTTGGATGTTGGGATCAAA
CTATTGGAATGGTTTAAGATCGACAGCTTAAGAGATAAGGTGACACGGATTGTATTATTA
TGGGTAAATAATCATTTTAATGATTTTGAAGGTGACCCTGCTATGACTCGATTTCTAGAG
GAATTTGAAAAAAATCTGGAAGATACAAAGATGAATGGTCATCTCCGGTTATTGAATATT
GCCTGTGCTGCAAAGGCTAAGTGGAGACAGGTTGTGCTGCAAAAGGCTTCCCGCGAGTCC
CCTCTACAATTCAGCCTTAATGGAGGGAGTGAGAAGGGATTTGGTATTTTTGTTGAAGGA
GTAGAACCTGGTAGCAAAGCTGCTGATTCAGGACTGAAACGTGGTGATCAGATTATGGAA
GTAAATGGACAAAACTTTGAGAATATTACATTTATGAAAGCCGTTGAAATTTTGAGGAAT
AATACTCATCTTGCACTTACTGTGAAGACCAACATTTTTGTGTTCAAAGAGTTACTTTTT
AGGACTGAACAAGAGAAATCTGGTGTTCCTCATATTCCCAAAATTGCTGAAAAAAAAAGT
AATCGCCATTCTATCCAGCATGTGCCAGGAGATATTGAACAGACATCACAGGAGAAAGGA
AGTAAGAAAGTTAAAGCAAATACTGTTTCAGGTGGAAGAAACAAAATCAGGAAGATTTTG
GATAAAACACGATTTAGTATCTTGCCTCCAAAGCTATTTAGTGATGGAGGCCTAAGCCAA
TCACAAGATGACAGCATTGTGGGAACAAGGCACTGTAGGCATAGTCTGGCTATAATGCCC
ATCCCTGGAACACTCTCATCCAGCAGCCCTGATCTCCTGCAGCCTACCACCAGTATGTTG
GATTTTTCCAATCCTTCAGATATCCCTGATCAAGTTATAAGAGTTTTCAAAGTGGATCAG
CAAAGTTGCTACATTATCATCAGTAAAGACACCACAGCTAAAGAAGTAGTTTTTCATGCT
GTTCATGAATTTGGTTTGACCGGTGCATCCGACACATATTCTCTCTGTGAAGTTTCTGTT
ACTCCTGAGGGTGTCATAAAACAGAGAAGACTTCCAGATCAGTTCTCCAAATTAGCTGAT
AGAATTCAACTCAATGGAAGGTATTACTTAAAAAATAACATGGAAACAGAAACCTTATGT
TCAGATGAAGATGCTCAAGAACTAGTTAAGGAAAGCCAGCTATCCATGCTGCAGCTCAGT
ACCATTGAGGTGGCCACCCAGCTGTCAATGAGGGACTTTGATTTGTTTCGTAATATTGAA
CCGACTGAGTACATCGATGACCTTTTTAAGTTAAATTCCAAAACAGGAAATACTCATTTG
AAGAGGTTTGAGGACATTGTAAACCAAGAGACATTCTGGGTTGCCTCAGAAATTTTAACT
GAAGCAAATCAGCTCAAACGAATGAAGATTATTAAGCATTTTATTAAAATTGCACTTCAT
TGTCGAGAATGTAAGAACTTCAATTCCATGTTTGCAATAATAAGTGGCTTGAACCTGGCA
TCTGTAGCAAGACTCAGAGGAACTTGGGAAAAGTTACCAAGCAAATACGAGAAACATCTT
CAAGATCTACAAGACATTTTTGATCCATCTAGAAACATGGCAAAGTATAGAAATATTCTT
AGTAGTCAAAGTATGCAGCCTCCAATTATTCCACTCTTCCCTGTTGTCAAGAAAGATATG
ACATTTCTACATGAAGGAAATGACTCCAAAGTAGATGGTTTAGTAAACTTTGAGAAGTTA
AGAATGATTTCCAAGGAAATCCGCCAAGTTGTTCGAATGACTTCTGCTAACATGGACCCA
GCTATGATGTTTCGACAGAGGTCACTGAGTCAAGGAAGCACAAATTCAAACATGCTGGAT
GTTCAGGGAGGTGCTCACAAAAAAAGGGCACGCCGCAGCTCTCTGCTTAATGCCAAGAAG
CTATATGAGGATGCCCAAATGGCAAGGAAGGTGAAGCAGTATCTTTCCAGTCTCGATGTA
GAGACAGATGAGGAGAAGTTCCAGATGATGTCATTACAGTGGGAGCCTGCATATGGTACC
TTGACCAAGAATTTAAGTGAGAAAAGATCAGCCAAATCATCTGAAATGTCTCCAGTGCCT
ATGAGGTCAGCTGGCCAAACAACTAAAGCCCACTTGCATCAACCCCACAGAGTAAGCCAG
GTGCTTCAGGTGCCAGCTGTTAATTTGCACCCCATCAGGAAGAAGGGACAAACAAAAGAC
CCTGCACTGAATACAAGTTTACCTCAGAAAGTTTTAGGAACAACTGAAGAAATAAGTGGT
AAGAAGCATACAGAAGACACTATTTCTGTGGCGTCATCTTTACATTCTAGTCCTCCTGCA
TCTCCTCAAGGCTCCCCTCACAAAGGTTACACACTTATTCCATCAGCTAAATCTGACAAC
TTGTCTGACTCCAGCCATAGTGAGATTTCTTCACGGTCCAGCATCGTGAGCAATTGTTCT
GTTGACTCCATGTCTGCAGCTCTACAGGATGAACGGTGTTCCTCTCAGGCCCTGGCAGTC
CCTGAATCCACTGGGGCATTGGAAAAGACAGAGCACGCTTCAGGGATAGGAGATCATAGT
CAACATGGCCCTGGGTGGACACTCTTGAAGCCATCTCTAATCAAGTGTTTAGCTGTCTCA
TCGTCTGTGAGCAATGAAGAGATTTCTCAAGAGCATATCATTATAGAAGCAGCTGACAGT
GGTCGTGGAAGTTGGACTTCGTGTTCAAGCAGCTCCCATGACAACTTCCAAAGCCTTCCA
AACCCAAAAAGCTGGGATTTTTTGAACTCTTACAGACATACCCATTTGGATGACCCCATT
GCTGAAGTTGAACCCACTGACTCTGAGCCCTATTCCTGTTCTAAAAGCTGCTCTAGAACT
TGTGGGCAGTGTAAAGGAAGCCTAGAGAGAAAGAGTTGGACCTCCTCCAGTTCTCTGTCT
GACACGTATGAACCAAACTATGGGACAGTTAAACAGAGAGTATTGGAGAGCACCCCAGCT
GAGTCATCTGAAGGCTTGGACCCCAAGGATGCCACTGACCCAGTTTATAAAACTGTCACT
TCAAGTACAGAAAAGGGCTTGATTGTGTACTGTGTCACCTCACCCAAGAAGGACGATAGG
TATAGGGAGCCACCTCCCACTCCTCCAGGATATTTGGGGATTTCTTTAGCGGACCTAAAG
GAAGGACCCCACACACACCTAAAACCTCCAGATTATAGTGTGGCAGTGCAGAGGTCAAAG
ATGATGCATAACAGCCTCTCTAGACTGCCACCAGCTTCTCTCAGTAGCAACCTCGTGGCC
TGTGTTCCATCGAAGATTGTAACTCAGCCTCAGAGGCATAATTTGCAGCCATTCCATCCT
AAACTAGGAGATGTGACTGATGCAGATAGCGAAGCAGATGAAAATGAACAAGTTTCAGCA
GTCTAG
Enzyme 76 GenBank Gene ID NM_016340.5 Link Image
Enzyme 76 GeneCard ID RAPGEF6 Link Image
Enzyme 76 GenAtlas ID RAPGEF6 Link Image
Enzyme 76 HGNC ID HGNC:20655 Link Image
Enzyme 76 Chromosome Location 5
Enzyme 76 Locus 5q31.1
Enzyme 76 SNPs SNPJam Report Link Image
Enzyme 76 General References
  1. Kuiperij HB, de Rooij J, Rehmann H, van Triest M, Wittinghofer A, Bos JL, Zwartkruis FJ: Characterisation of PDZ-GEFs, a family of guanine nucleotide exchange factors specific for Rap1 and Rap2. Biochim Biophys Acta. 2003 Feb 17;1593(2-3):141-9. [PubMed Link Image]
  2. Gao X, Satoh T, Liao Y, Song C, Hu CD, Kariya Ki K, Kataoka T: Identification and characterization of RA-GEF-2, a Rap guanine nucleotide exchange factor that serves as a downstream target of M-Ras. J Biol Chem. 2001 Nov 9;276(45):42219-25. Epub 2001 Aug 27. [PubMed Link Image]
  3. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  4. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  5. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  9. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 76 Metabolite References Not Available
Enzyme 77 [top]
Enzyme 77 ID 14023
Enzyme 77 Name Neuroepithelial cell-transforming gene 1 protein
Enzyme 77 Synonyms
  1. Proto-oncogene p65 Net1
  2. Rho guanine nucleotide exchange factor 8
Enzyme 77 Gene Name NET1
Enzyme 77 Protein Sequence >Neuroepithelial cell-transforming gene 1 protein
MEPELAAQKQPRPRRRSRRASGLSTEGATGPSADTSGSELDGRCSLRRGSSFTFLTPGPN
WDFTLKRKRREKDDDVVSLSSLDLKEPSNKRVRPLARVTSLANLISPVRNGAVRRFGQTI
QSFTLRGDHRSPASAQKFSSRSTVPTPAKRRSSALWSEMLDITMKESLTTREIRRQEAIY
EMSRGEQDLIEDLKLARKAYHDPMLKLSIMSEEELTHIFGDLDSYIPLHEDLLTRIGEAT
KPDGTVEQIGHILVSWLPRLNAYRGYCSNQLAAKALLDQKKQDPRVQDFLQRCLESPFSR
KLDLWSFLDIPRSRLVKYPLLLKEILKHTPKEHPDVQLLEDAILIIQGVLSDINLKKGES
ECQYYIDKLEYLDEKQRDPRIEASKVLLCHGELRSKSGHKLYIFLFQDILVLTRPVTRNE
RHSYQVYRQPIPVQELVLEDLQDGDVRMGGSFRGAFSNSEKAKNIFRIRFHDPSPAQSHT
LQANDVFHKQQWFNCIRAAIAPFQSAGSPPELQGLPELHEECEGNHPSARKLTAQRRAST
VSSVTQVEVDENAYRCGSGMQMAEDSKSLKTHQTQPGIRRARDKALSGGKRKETLV
Enzyme 77 Number of Residues 596
Enzyme 77 Molecular Weight 67739.3
Enzyme 77 Theoretical pI 9.70
Enzyme 77 GO Classification
Function
  • GTPase regulator activity
  • Ras guanyl-nucleotide exchange factor activity
  • Rho guanyl-nucleotide exchange factor activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
  • biological regulation
  • intracellular signaling pathway
  • regulation of Ras protein signal transduction
  • regulation of Rho protein signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signaling
  • signaling pathway
Component
  • cell part
  • intracellular
Enzyme 77 General Function Involved in Rho guanyl-nucleotide exchange factor activity
Enzyme 77 Specific Function Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase. May be involved in activation of the SAPK/JNK pathway
Enzyme 77 Pathways Not Available
Enzyme 77 Reactions Not Available
Enzyme 77 Pfam Domain Function
Enzyme 77 Signals
  • None
Enzyme 77 Transmembrane Regions
  • None
Enzyme 77 Essentiality Not Available
Enzyme 77 GenBank ID Protein 114145479 Link Image
Enzyme 77 UniProtKB/Swiss-Prot ID Q7Z628 Link Image
Enzyme 77 UniProtKB/Swiss-Prot Entry Name ARHG8_HUMAN Link Image
Enzyme 77 PDB ID Not Available
Enzyme 77 Cellular Location Not Available
Enzyme 77 Gene Sequence >1791 bp
ATGGAGCCCGAGCTGGCGGCTCAGAAGCAGCCTCGACCGCGGAGGCGAAGCCGCCGGGCC
TCTGGGCTCAGCACGGAGGGAGCGACGGGGCCTTCGGCCGACACCTCCGGGTCGGAGCTG
GACGGGAGATGTTCCCTTCGGAGAGGCAGCTCCTTCACATTCTTAACACCTGGCCCCAAC
TGGGACTTCACTTTGAAAAGAAAACGCAGAGAGAAAGATGATGATGTTGTAAGCCTTAGC
AGCCTTGATCTGAAGGAGCCAAGCAATAAAAGAGTTCGACCTCTGGCTCGTGTCACGTCC
TTGGCAAATTTAATCTCTCCTGTAAGAAATGGAGCTGTCAGACGTTTTGGTCAAACAATA
CAGTCATTTACCCTTCGTGGTGACCACAGATCCCCAGCCTCTGCCCAGAAGTTTTCTAGC
AGGTCAACAGTCCCAACACCCGCCAAGAGAAGGAGCAGTGCACTGTGGTCAGAGATGCTG
GACATCACCATGAAGGAGTCTCTCACCACCAGGGAGATCAGACGGCAGGAGGCAATATAT
GAAATGTCCCGAGGTGAACAGGATTTAATTGAGGATCTCAAACTTGCAAGAAAGGCCTAC
CATGACCCCATGTTAAAGTTGTCCATCATGTCAGAAGAGGAACTCACACATATATTTGGT
GATCTGGACTCTTACATACCTCTGCATGAAGATTTGTTGACAAGAATAGGAGAAGCAACC
AAGCCTGATGGAACAGTGGAGCAGATTGGTCACATTCTCGTGAGCTGGTTACCGCGCTTG
AATGCCTACAGAGGTTACTGTAGTAACCAGCTGGCAGCCAAAGCTCTTCTTGATCAAAAG
AAACAGGATCCAAGAGTCCAAGACTTCCTCCAGCGATGTCTCGAGTCTCCCTTCAGTCGA
AAACTAGATCTTTGGAGTTTCCTAGATATCCCTCGAAGTCGCCTAGTCAAATACCCTTTA
CTGTTAAAAGAAATTCTTAAACACACTCCAAAAGAGCACCCTGATGTTCAGCTTCTGGAG
GATGCTATATTGATAATACAGGGAGTCCTCTCTGATATCAACTTGAAGAAAGGTGAATCC
GAGTGCCAGTATTACATCGACAAGCTGGAGTACCTGGATGAAAAGCAGAGGGACCCCAGA
ATCGAAGCGAGCAAAGTGCTGCTGTGCCATGGGGAGCTGCGGAGCAAGAGTGGACATAAA
CTTTACATTTTCCTGTTTCAAGACATCTTGGTTCTGACTCGGCCCGTCACACGGAACGAA
CGGCACTCTTACCAGGTTTACCGGCAGCCAATCCCAGTCCAAGAGCTAGTCCTAGAAGAC
CTGCAGGATGGAGATGTGAGAATGGGAGGCTCCTTTCGAGGAGCTTTCAGTAACTCAGAG
AAAGCTAAAAATATCTTTAGAATTCGCTTCCATGACCCCTCTCCAGCCCAGTCTCACACT
CTGCAAGCCAATGACGTGTTCCACAAGCAGCAGTGGTTCAACTGTATTCGAGCGGCCATT
GCCCCCTTCCAGTCGGCAGGCAGTCCACCTGAGCTGCAGGGCCTGCCGGAGCTGCACGAA
GAGTGTGAGGGGAACCACCCCTCTGCGAGGAAACTCACAGCCCAGAGGAGGGCATCCACA
GTTTCCAGTGTTACTCAGGTAGAAGTTGATGAAAACGCTTACAGATGTGGCTCTGGCATG
CAGATGGCAGAGGACAGCAAGAGCTTAAAGACACACCAGACACAGCCCGGCATCCGAAGA
GCGAGGGACAAAGCCCTTTCTGGTGGCAAACGGAAAGAGACTTTGGTGTAG
Enzyme 77 GenBank Gene ID NM_001047160.1 Link Image
Enzyme 77 GeneCard ID NET1 Link Image
Enzyme 77 GenAtlas ID NET1 Link Image
Enzyme 77 HGNC ID HGNC:14592 Link Image
Enzyme 77 Chromosome Location 1
Enzyme 77 Locus 10p15
Enzyme 77 SNPs SNPJam Report Link Image
Enzyme 77 General References
  1. Chan AM, Takai S, Yamada K, Miki T: Isolation of a novel oncogene, NET1, from neuroepithelioma cells by expression cDNA cloning. Oncogene. 1996 Mar 21;12(6):1259-66. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Shen X, Li J, Hu PP, Waddell D, Zhang J, Wang XF: The activity of guanine exchange factor NET1 is essential for transforming growth factor-beta-mediated stress fiber formation. J Biol Chem. 2001 May 4;276(18):15362-8. Epub 2001 Feb 2. [PubMed Link Image]
  4. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  5. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  6. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 77 Metabolite References Not Available
Enzyme 78 [top]
Enzyme 78 ID 14038
Enzyme 78 Name Cell cycle progression protein 1
Enzyme 78 Synonyms
  1. Cell cycle progression restoration protein 8
Enzyme 78 Gene Name CCPG1
Enzyme 78 Protein Sequence >Cell cycle progression protein 1
MSENSSDSDSSCGWTVISHEGSDIEMLNSVTPTDSCEPAPECSSLEQEELQALQIEQGES
SQNGTVLMEETAYPALEETSSTIEAEEQKIPEDSIYIGTASDDSDIVTLEPPKLEEIGNQ
EVVIVEEAQSSEDFNMGSSSSSQYTFCQPETVFSSQPSDDESSSDETSNQPSPAFRRRRA
RKKTVSASESEDRLVAEQETEPSKELSKRQFSSGLNKCVILALVIAISMGFGHFYGTIQI
QKRQQLVRKIHEDELNDMKDYLSQCQQEQESFIDYKSLKENLARCWTLTEAEKMSFETQK
TNLATENQYLRVSLEKEEKALSSLQEELNKLREQIRILEDKGTSTELVKENQKLKQHLEE
EKQKKHSFLSQRETLLTEAKMLKRELERERLVTTALRGELQQLSGSQLHGKSDSPNVYTE
KKEIAILRERLTELERKLTFEQQRSDLWERLYVEAKDQNGKQGTDGKKKGGRGSHRAKNK
SKETFLGSVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTT
KNIFDEKGNKRFGATKEAAEKPRTVFSDYLHPQYKAPTENHHNRGPTMQNDGRKEKPVHF
KEFRKNTNSKKCSPGHDCRENSHSFRKACSGVFDCAQQESMSLFNTVVNPIRMDEFRQII
QRYMLKELDTFCHWNELDQFINKFFLNGVFIHDQKLFTDFVNDVKDYLRNMKEYEVDNDG
VFEKLDEYIYRHFFGHTFSPPYGPRSVYIKPCHYSSL
Enzyme 78 Number of Residues 757
Enzyme 78 Molecular Weight 87339.7
Enzyme 78 Theoretical pI 5.78
Enzyme 78 GO Classification Not Available
Enzyme 78 General Function Replication, recombination and repair
Enzyme 78 Specific Function Acts as an assembly platform for Rho protein signaling complexes. Limits guanine nucleotide exchange activity of MCF2L toward RHOA, which results in an inhibition of both its transcriptional activation ability and its transforming activity. Does not inhibit activity of MCF2L toward CDC42, or activity of MCF2 toward either RHOA or CDC42. May be involved in cell cycle regulation
Enzyme 78 Pathways Not Available
Enzyme 78 Reactions Not Available
Enzyme 78 Pfam Domain Function Not Available
Enzyme 78 Signals
  • None
Enzyme 78 Transmembrane Regions
  • 218-238
Enzyme 78 Essentiality Not Available
Enzyme 78 GenBank ID Protein 75677585 Link Image
Enzyme 78 UniProtKB/Swiss-Prot ID Q9ULG6 Link Image
Enzyme 78 UniProtKB/Swiss-Prot Entry Name CCPG1_HUMAN Link Image
Enzyme 78 PDB ID Not Available
Enzyme 78 Cellular Location Not Available
Enzyme 78 Gene Sequence >2274 bp
ATGTCTGAAAATTCCAGTGACAGTGATTCATCTTGTGGTTGGACTGTCATCAGTCATGAG
GGGTCAGATATAGAAATGTTGAATTCTGTGACCCCCACTGACAGCTGTGAGCCCGCCCCA
GAATGTTCATCTTTAGAGCAAGAGGAGCTTCAAGCATTGCAGATAGAGCAAGGAGAAAGC
AGCCAAAATGGCACAGTGCTTATGGAAGAAACTGCTTATCCAGCTTTGGAGGAAACCAGC
TCAACAATTGAGGCAGAGGAACAAAAGATACCCGAAGACAGTATCTATATTGGAACTGCC
AGTGATGATTCTGATATTGTTACCCTTGAGCCACCTAAGTTAGAAGAAATTGGAAATCAA
GAAGTTGTCATTGTTGAAGAAGCACAGAGTTCAGAAGACTTTAACATGGGCTCTTCCTCT
AGCAGCCAGTATACTTTCTGTCAGCCAGAAACTGTATTTTCATCTCAGCCTAGTGACGAT
GAATCAAGTAGTGATGAAACCAGTAATCAGCCCAGTCCTGCCTTTAGACGACGCCGTGCT
AGGAAGAAGACCGTTTCTGCTTCAGAATCTGAAGACCGGCTAGTTGCTGAACAAGAAACT
GAACCTTCTAAGGAGTTGAGTAAACGTCAGTTCAGTAGTGGTCTCAATAAGTGTGTTATA
CTTGCTTTGGTGATTGCAATCAGCATGGGATTTGGCCATTTCTATGGCACAATTCAGATT
CAGAAGCGTCAACAGTTAGTCAGAAAGATACATGAAGATGAATTGAATGATATGAAGGAT
TATCTTTCCCAGTGTCAACAGGAACAAGAATCTTTTATAGATTATAAGTCATTGAAAGAA
AATCTTGCAAGGTGTTGGACACTTACTGAAGCAGAGAAGATGTCCTTTGAAACTCAGAAA
ACGAACCTTGCTACAGAAAATCAGTATTTAAGAGTATCCTTGGAGAAGGAAGAAAAAGCC
TTATCCTCATTACAGGAAGAGTTAAACAAACTAAGAGAACAGATTAGAATATTGGAAGAT
AAAGGGACAAGTACTGAATTAGTTAAAGAAAATCAGAAACTTAAGCAGCATTTGGAAGAG
GAAAAGCAGAAAAAACACAGCTTTCTTAGTCAAAGGGAGACTCTGTTGACAGAAGCAAAG
ATGCTAAAGAGAGAACTGGAGAGAGAACGACTAGTAACTACGGCTTTAAGGGGGGAACTC
CAGCAGTTAAGTGGTAGTCAGTTACATGGCAAGTCAGATTCTCCCAATGTATATACTGAA
AAAAAGGAAATAGCAATCTTACGGGAAAGACTCACTGAGCTGGAACGGAAGCTAACCTTC
GAACAGCAGCGTTCTGATTTGTGGGAAAGATTGTATGTTGAGGCAAAAGATCAAAATGGA
AAACAAGGAACAGATGGAAAAAAGAAAGGGGGCAGAGGAAGCCACAGGGCTAAAAATAAG
TCAAAGGAAACATTTTTGGGTTCAGTTAAGGAAACATTTGATGCCATGAAGAATTCTACC
AAGGAGTTTGTAAGGCATCATAAAGAGAAAATTAAGCAGGCTAAAGAAGCTGTGAAGGAA
AATCTGAAAAAATTCTCAGATTCAGTTAAATCCACTTTCAGACACTTTAAAGATACCACC
AAGAATATCTTTGATGAAAAGGGTAATAAAAGATTTGGTGCTACAAAAGAAGCAGCTGAA
AAACCAAGAACAGTTTTTAGTGACTATTTACATCCACAGTATAAGGCACCTACAGAAAAC
CATCATAATAGAGGCCCTACTATGCAAAATGATGGAAGGAAAGAAAAGCCAGTTCACTTT
AAAGAATTCAGAAAAAATACAAATTCAAAGAAATGCAGTCCTGGGCATGATTGTAGAGAA
AATTCTCATTCTTTCAGAAAGGCTTGTTCTGGTGTATTTGATTGTGCTCAACAAGAGTCC
ATGAGCCTTTTTAACACAGTGGTGAATCCTATAAGGATGGATGAATTTAGACAGATAATT
CAAAGGTACATGTTAAAAGAACTGGATACTTTTTGTCACTGGAACGAACTTGATCAGTTC
ATCAATAAGTTTTTCCTAAACGGTGTCTTTATACATGATCAGAAGCTCTTCACTGACTTT
GTTAATGATGTTAAAGATTATCTTAGAAACATGAAGGAATATGAAGTAGATAATGATGGA
GTATTTGAGAAGTTGGATGAATATATATATAGACACTTCTTTGGTCACACTTTTTCCCCT
CCATATGGACCCAGGTCGGTTTACATAAAACCGTGTCATTACAGTAGTTTGTAA
Enzyme 78 GenBank Gene ID NM_004748.3 Link Image
Enzyme 78 GeneCard ID CCPG1 Link Image
Enzyme 78 GenAtlas ID CCPG1 Link Image
Enzyme 78 HGNC ID HGNC:24227 Link Image
Enzyme 78 Chromosome Location 1
Enzyme 78 Locus 15q21.1
Enzyme 78 SNPs SNPJam Report Link Image
Enzyme 78 General References
  1. Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Oct 29;6(5):337-45. [PubMed Link Image]
  2. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Edwards MC, Liegeois N, Horecka J, DePinho RA, Sprague GF Jr, Tyers M, Elledge SJ: Human CPR (cell cycle progression restoration) genes impart a Far- phenotype on yeast cells. Genetics. 1997 Nov;147(3):1063-76. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
Enzyme 78 Metabolite References Not Available
Enzyme 79 [top]
Enzyme 79 ID 14055
Enzyme 79 Name Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein
Enzyme 79 Synonyms
  1. P-Rex2
  2. PtdIns(3,4,5)-dependent Rac exchanger 2
  3. DEP domain-containing protein 2
Enzyme 79 Gene Name PREX2
Enzyme 79 Protein Sequence >Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein
MSEDSRGDSRAESAKDLEKQLRLRVCVLSELQKTERDYVGTLEFLVSAFLHRMNQCAASK
VDKNVTEETVKMLFSNIEDILAVHKEFLKVVEECLHPEPNAQQEVGTCFLHFKDKFRIYD
EYCSNHEKAQKLLLELNKIRTIRTFLLNCMLLGGRKNTDVPLEGYLVTPIQRICKYPLIL
KELLKRTPRKHSDYAAVMEALQAMKAVCSNINEAKRQMEKLEVLEEWQSHIEGWEGSNIT
DTCTEMLMCGVLLKISSGNIQERVFFLFDNLLVYCKRKHRRLKNSKASTDGHRYLFRGRI
NTEVMEVENVDDGTADFHSSGHIVVNGWKIHNTAKNKWFVCMAKTPEEKHEWFEAILKER
ERRKGLKLGMEQDTWVMISEQGEKLYKMMCRQGNLIKDRKRKLTTFPKCFLGSEFVSWLL
EIGEIHRPEEGVHLGQALLENGIIHHVTDKHQFKPEQMLYRFRYDDGTFYPRNEMQDVIS
KGVRLYCRLHSLFTPVIRDKDYHLRTYKSVVMANKLIDWLIAQGDCRTREEAMIFGVGLC
DNGFMHHVLEKSEFKDEPLLFRFFSDEEMEGSNMKHRLMKHDLKVVENVIAKSLLIKSNE
GSYGFGLEDKNKVPIIKLVEKGSNAEMAGMEVGKKIFAINGDLVFMRPFNEVDCFLKSCL
NSRKPLRVLVSTKPRETVKIPDSADGLGFQIRGFGPSVVHAVGRGTVAAAAGLHPGQCII
KVNGINVSKETHASVIAHVTACRKYRRPTKQDSIQWVYNSIESAQEDLQKSHSKPPGDEA
GDAFDCKVEEVIDKFNTMAIIDGKKEHVSLTVDNVHLEYGVVYEYDSTAGIKCNVVEKMI
EPKGFFSLTAKILEALAKSDEHFVQNCTSLNSLNEVIPTDLQSKFSALCSERIEHLCQRI
SSYKKFSRVLKNRAWPTFKQAKSKISPLHSSDFCPTNCHVNVMEVSYPKTSTSLGSAFGV
QLDSRKHNSHDKENKSSEQGKLSPMVYIQHTITTMAAPSGLSLGQQDGHGLRYLLKEEDL
ETQDIYQKLLGKLQTALKEVEMCVCQIDDLLSSITYSPKLERKTSEGIIPTDSDNEKGER
NSKRVCFNVAGDEQEDSGHDTISNRDSYSDCNSNRNSIASFTSICSSQCSSYFHSDEMDS
GDELPLSVRISHDKQDKIHSCLEHLFSQVDSITNLLKGQAVVRAFDQTKYLTPGRGLQEF
QQEMEPKLSCPKRLRLHIKQDPWNLPSSVRTLAQNIRKFVEEVKCRLLLALLEYSDSETQ
LRRDMVFCQTLVATVCAFSEQLMAALNQMFDNSKENEMETWEASRRWLDQIANAGVLFHF
QSLLSPNLTDEQAMLEDTLVALFDLEKVSFYFKPSEEEPLVANVPLTYQAEGSRQALKVY
FYIDSYHFEQLPQRLKNGGGFKIHPVLFAQALESMEGYYYRDNVSVEEFQAQINAASLEK
VKQYNQKLRAFYLDKSNSPPNSTSKAAYVDKLMRPLNALDELYRLVASFIRSKRTAACAN
TACSASGVGLLSVSSELCNRLGACHIIMCSSGVHRCTLSVTLEQAIILARSHGLPPRYIM
QATDVMRKQGARVQNTAKNLGVRDRTPQSAPRLYKLCEPPPPAGEE
Enzyme 79 Number of Residues 1606
Enzyme 79 Molecular Weight 182620.5
Enzyme 79 Theoretical pI 7.46
Enzyme 79 GO Classification
Function
  • GTPase regulator activity
  • Ras guanyl-nucleotide exchange factor activity
  • Rho guanyl-nucleotide exchange factor activity
  • binding
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • protein binding
  • small GTPase regulator activity
Process
  • biological regulation
  • intracellular signaling pathway
  • regulation of Ras protein signal transduction
  • regulation of Rho protein signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signaling
  • signaling pathway
Component
  • cell part
  • intracellular
Enzyme 79 General Function Involved in intracellular signaling pathway
Enzyme 79 Specific Function Functions as a RAC1 guanine nucleotide exchange factor (GEF), activating Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol-3,4,5-triphosphate and the beta gamma subunits of heterotrimeric G protein. Mediates the activation of RAC1 in a PI3K-dependent manner. May be an important mediator of Rac signaling, acting directly downstream of both G protein- coupled receptors and phosphoinositide 3-kinase
Enzyme 79 Pathways Not Available
Enzyme 79 Reactions Not Available
Enzyme 79 Pfam Domain Function
Enzyme 79 Signals
  • None
Enzyme 79 Transmembrane Regions
  • None
Enzyme 79 Essentiality Not Available
Enzyme 79 GenBank ID Protein 47578115 Link Image
Enzyme 79 UniProtKB/Swiss-Prot ID Q70Z35 Link Image
Enzyme 79 UniProtKB/Swiss-Prot Entry Name PREX2_HUMAN Link Image
Enzyme 79 PDB ID Not Available
Enzyme 79 Cellular Location Not Available
Enzyme 79 Gene Sequence >4821 bp
ATGAGCGAGGACAGCCGCGGAGACAGCCGCGCCGAGAGCGCCAAGGACCTGGAGAAGCAG
CTTCGCCTGCGCGTGTGCGTGCTCAGCGAGCTCCAGAAGACCGAGCGGGACTATGTGGGC
ACGCTGGAGTTCCTGGTGTCGGCATTCTTACACAGAATGAACCAGTGTGCAGCATCAAAA
GTTGACAAAAATGTGACAGAAGAAACAGTGAAGATGTTGTTCTCAAACATTGAAGACATC
CTTGCAGTACATAAAGAATTCTTAAAAGTCGTGGAAGAATGCTTACACCCCGAACCTAAT
GCTCAACAAGAAGTGGGAACCTGCTTTCTTCACTTTAAAGACAAGTTTCGTATCTATGAT
GAATATTGTAGTAACCATGAGAAGGCACAAAAATTACTTCTTGAACTCAACAAAATAAGA
ACAATCCGGACATTTCTTTTGAACTGCATGCTGCTTGGAGGACGGAAGAACACAGATGTT
CCCTTGGAAGGATATTTAGTAACACCAATACAAAGAATATGCAAGTACCCTCTTATTTTG
AAGGAGTTGCTGAAGCGGACTCCACGGAAACACAGTGACTATGCAGCAGTGATGGAAGCC
CTCCAAGCCATGAAAGCTGTCTGTTCCAACATAAACGAGGCCAAGAGACAGATGGAGAAG
TTAGAAGTTTTAGAGGAATGGCAGTCTCACATTGAAGGCTGGGAGGGGTCCAACATCACT
GACACCTGCACTGAAATGCTAATGTGTGGAGTCTTACTGAAAATTTCTTCTGGAAATATT
CAAGAACGGGTGTTTTTTCTTTTCGATAATCTTTTGGTGTACTGCAAAAGAAAACACAGA
CGGTTGAAGAACAGCAAGGCATCTACAGATGGACATCGGTACCTTTTTCGTGGCCGGATC
AACACGGAGGTGATGGAAGTGGAGAATGTGGATGATGGCACCGCTGATTTCCATAGCAGT
GGACACATTGTTGTTAATGGATGGAAGATACATAACACAGCAAAAAATAAATGGTTTGTT
TGTATGGCAAAAACACCTGAAGAGAAGCATGAATGGTTTGAAGCTATTTTGAAAGAAAGA
GAACGGCGGAAAGGTTTAAAATTAGGAATGGAGCAAGATACCTGGGTCATGATCTCTGAA
CAGGGTGAGAAACTTTATAAAATGATGTGCAGACAAGGAAATCTGATCAAAGACCGAAAG
AGAAAACTGACTACGTTCCCTAAATGCTTTCTTGGAAGCGAATTTGTGTCATGGCTGTTG
GAAATTGGAGAGATTCACAGGCCTGAGGAAGGCGTGCACTTGGGACAAGCATTATTAGAA
AATGGAATCATTCACCATGTTACTGATAAACATCAATTCAAACCAGAACAGATGTTATAT
AGATTTCGCTATGATGATGGAACATTTTATCCAAGAAATGAGATGCAGGACGTGATTTCA
AAGGGTGTAAGATTATATTGTCGTCTTCATAGCCTTTTTACTCCAGTGATAAGAGATAAA
GATTACCATTTAAGGACCTACAAATCTGTGGTCATGGCCAACAAACTGATAGACTGGTTA
ATTGCACAGGGAGATTGCCGCACCAGAGAAGAGGCAATGATATTTGGCGTTGGACTCTGT
GACAATGGATTTATGCACCATGTCCTTGAAAAAAGCGAATTCAAAGATGAACCCCTACTT
TTCCGTTTTTTTTCGGATGAGGAAATGGAGGGATCAAATATGAAACATCGACTTATGAAA
CATGACTTAAAAGTTGTGGAAAATGTTATAGCTAAGTCATTATTGATTAAATCCAATGAA
GGCAGCTATGGCTTTGGATTAGAAGACAAAAATAAAGTTCCAATAATAAAGTTGGTAGAA
AAGGGATCTAATGCTGAGATGGCTGGCATGGAAGTCGGGAAAAAGATTTTTGCTATTAAT
GGTGACCTAGTTTTTATGAGACCTTTCAATGAAGTGGATTGCTTCCTGAAATCGTGTTTA
AACAGCAGAAAACCTCTAAGAGTTCTTGTGAGCACAAAGCCAAGAGAGACAGTGAAAATT
CCAGATTCAGCTGATGGACTTGGCTTCCAGATCCGGGGATTTGGCCCTTCTGTTGTGCAT
GCTGTAGGAAGAGGAACTGTGGCTGCAGCAGCTGGTCTTCACCCTGGACAGTGCATTATC
AAGGTGAATGGAATCAATGTCAGCAAAGAGACACATGCCAGTGTCATTGCACACGTTACA
GCCTGCAGGAAGTACAGGCGGCCAACGAAGCAAGATTCCATACAATGGGTTTATAATAGC
ATTGAGAGTGCTCAAGAAGACCTTCAAAAATCTCACTCCAAGCCCCCTGGAGATGAAGCA
GGGGATGCTTTTGACTGTAAAGTAGAAGAGGTTATTGACAAATTCAACACTATGGCCATC
ATTGATGGGAAGAAGGAGCATGTGAGTCTGACAGTGGACAATGTCCACCTGGAATATGGT
GTCGTGTATGAGTACGACAGCACAGCTGGCATCAAGTGCAATGTGGTGGAAAAGATGATT
GAGCCCAAAGGTTTCTTCAGCTTAACTGCCAAGATTCTTGAAGCCCTGGCTAAAAGTGAT
GAGCATTTTGTACAAAACTGTACCAGCCTAAATTCTCTAAATGAAGTGATTCCTACTGAC
CTTCAGAGTAAATTCAGTGCCCTTTGCAGTGAAAGAATTGAACACCTATGTCAGAGAATA
TCCAGTTATAAAAAGTTTTCTCGTGTACTGAAGAATAGGGCCTGGCCTACTTTTAAACAG
GCCAAATCTAAAATCTCCCCACTGCACAGCAGTGATTTCTGCCCTACCAACTGCCATGTC
AATGTGATGGAAGTTTCTTATCCCAAAACATCAACCTCTTTGGGAAGTGCATTTGGTGTT
CAGTTGGATAGCAGGAAGCATAATTCTCATGATAAAGAAAACAAATCTTCGGAGCAAGGG
AAACTGAGCCCTATGGTGTACATTCAGCACACCATCACAACCATGGCGGCCCCTTCAGGT
CTGTCTCTGGGACAGCAGGATGGCCATGGTCTCAGGTATCTGCTAAAAGAAGAAGACTTA
GAAACCCAAGACATCTATCAGAAACTGCTGGGCAAACTTCAGACTGCACTGAAAGAGGTG
GAGATGTGTGTTTGTCAAATAGATGACCTTCTGTCTTCAATAACATATTCTCCTAAATTA
GAACGTAAGACATCAGAGGGCATAATACCAACAGACAGTGACAATGAGAAGGGAGAAAGA
AACAGCAAACGGGTATGTTTTAATGTAGCAGGAGATGAACAGGAAGATTCTGGTCATGAC
ACCATCAGCAACAGAGACTCTTACAGTGACTGCAACAGCAATAGGAATTCCATCGCCTCC
TTCACCAGCATCTGCAGCAGCCAGTGCAGCTCGTATTTCCACAGTGATGAAATGGACTCA
GGTGATGAACTTCCCTTAAGTGTTCGCATATCTCATGATAAACAGGACAAGATACATAGT
TGCCTTGAGCATCTTTTCAGCCAGGTGGATTCAATTACCAATCTCCTAAAAGGGCAGGCT
GTTGTGAGGGCCTTTGACCAAACCAAGTATCTCACTCCAGGCCGAGGATTGCAAGAATTT
CAACAGGAAATGGAACCAAAGCTGAGTTGTCCAAAAAGGCTACGGCTTCATATCAAGCAA
GATCCTTGGAATCTTCCCAGCAGCGTCCGGACTCTTGCTCAGAACATCAGGAAATTTGTT
GAAGAGGTAAAGTGTAGGCTACTCCTGGCTCTTCTTGAATATTCAGATAGTGAGACACAG
CTCCGTAGAGACATGGTTTTCTGCCAGACTCTTGTGGCCACTGTCTGTGCCTTCTCTGAG
CAGCTCATGGCGGCCTTGAACCAGATGTTTGACAACAGCAAGGAAAATGAGATGGAAACT
TGGGAAGCCAGCAGGAGGTGGCTGGACCAGATAGCGAATGCAGGTGTTCTTTTTCACTTT
CAGTCACTTCTGTCACCAAACTTGACAGATGAACAAGCCATGTTAGAAGATACACTGGTT
GCACTATTTGATTTGGAAAAGGTTTCCTTTTACTTTAAACCATCAGAAGAGGAACCTCTG
GTTGCAAATGTTCCTCTTACATATCAAGCAGAAGGAAGTCGGCAAGCTCTGAAAGTTTAC
TTCTACATTGATAGTTATCATTTTGAACAACTTCCTCAACGGCTGAAAAATGGAGGAGGG
TTTAAAATTCATCCTGTTCTTTTTGCACAAGCACTAGAGAGCATGGAAGGATATTATTAC
AGAGACAATGTTTCTGTGGAAGAATTTCAAGCTCAGATAAATGCAGCCTCACTGGAAAAG
GTCAAACAGTACAACCAGAAGCTCAGGGCATTCTACTTGGACAAGTCAAATTCACCACCA
AACTCCACATCCAAAGCTGCCTATGTAGATAAGCTAATGAGGCCTCTCAACGCTTTGGAT
GAACTTTACCGACTGGTAGCCTCGTTTATCAGATCCAAGCGCACAGCTGCCTGTGCAAAC
ACAGCTTGCAGTGCTTCTGGGGTTGGACTGCTGTCAGTTTCCTCGGAGCTGTGCAACAGG
CTGGGCGCCTGCCACATCATCATGTGCAGCAGCGGTGTGCATCGGTGCACCCTGAGCGTG
ACGCTGGAGCAAGCCATCATTCTGGCCAGAAGCCACGGACTGCCACCTCGTTACATCATG
CAGGCTACAGATGTGATGCGGAAGCAGGGAGCAAGAGTTCAGAACACAGCGAAGAATTTG
GGAGTCAGAGACCGGACTCCACAGTCTGCACCAAGGCTGTACAAGCTGTGCGAGCCACCT
CCCCCAGCTGGAGAAGAATGA
Enzyme 79 GenBank Gene ID NM_024870.2 Link Image
Enzyme 79 GeneCard ID PREX2 Link Image
Enzyme 79 GenAtlas ID PREX2 Link Image
Enzyme 79 HGNC ID HGNC:22950 Link Image
Enzyme 79 Chromosome Location 8
Enzyme 79 Locus 8q13.2
Enzyme 79 SNPs SNPJam Report Link Image
Enzyme 79 General References
  1. Donald S, Hill K, Lecureuil C, Barnouin R, Krugmann S, John Coadwell W, Andrews SR, Walker SA, Hawkins PT, Stephens LR, Welch HC: P-Rex2, a new guanine-nucleotide exchange factor for Rac. FEBS Lett. 2004 Aug 13;572(1-3):172-6. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed Link Image]
  4. Rosenfeldt H, Vazquez-Prado J, Gutkind JS: P-REX2, a novel PI-3-kinase sensitive Rac exchange factor. FEBS Lett. 2004 Aug 13;572(1-3):167-71. [PubMed Link Image]
  5. Joseph RE, Norris FA: Substrate specificity and recognition is conferred by the pleckstrin homology domain of the Dbl family guanine nucleotide exchange factor P-Rex2. J Biol Chem. 2005 Jul 29;280(30):27508-12. Epub 2005 May 16. [PubMed Link Image]
  6. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 79 Metabolite References Not Available
Enzyme 80 [top]
Enzyme 80 ID 14061
Enzyme 80 Name Dynamin-1-like protein
Enzyme 80 Synonyms
  1. Dnm1p/Vps1p-like protein
  2. DVLP
  3. Dynamin family member proline-rich carboxyl-terminal domain less
  4. Dymple
  5. Dynamin-like protein
  6. Dynamin-like protein 4
  7. Dynamin-like protein IV
  8. HdynIV
  9. Dynamin-related protein 1
Enzyme 80 Gene Name DNM1L
Enzyme 80 Protein Sequence >Dynamin-1-like protein
MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTR
RPLILQLVHVSQEDKRKTTGEENGVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISG
NNKGVSPEPIHLKIFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSI
ILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLG
IIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDC
LPELKTRINVLAAQYQSLLNSYGEPVDDKSATLLQLITKFATEYCNTIEGTAKYIETSEL
CGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQ
IKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTCLLRKRLPVTN
EMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRRNRLARELPSAVSRDKSSKVPSAL
APASQEPSPAASAEADGKLIQDSRRETKNVASGGGGVGDGVQEPTTGNWRGMLKTSKAEE
LLAEEKSKPIPIMPASPQKGHAVNLLDVPVPVARKLSAREQRDCEVIERLIKSYFLIVRK
NIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKAL
QGASQIIAEIRETHLW
Enzyme 80 Number of Residues 736
Enzyme 80 Molecular Weight 81876.4
Enzyme 80 Theoretical pI 6.80
Enzyme 80 GO Classification
Function
  • GTP binding
  • GTPase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
Process
Component
Enzyme 80 General Function Involved in GTP binding
Enzyme 80 Specific Function Isoform 1 and isoform 4 inhibit peroxisomal division when overexpressed
Enzyme 80 Pathways Not Available
Enzyme 80 Reactions
  • GTP + H2O = GDP + phosphate [RN:R00335]
Enzyme 80 Pfam Domain Function
Enzyme 80 Signals
  • None
Enzyme 80 Transmembrane Regions
  • None
Enzyme 80 Essentiality Not Available
Enzyme 80 GenBank ID Protein Not Available
Enzyme 80 UniProtKB/Swiss-Prot ID O00429 Link Image
Enzyme 80 UniProtKB/Swiss-Prot Entry Name DNM1L_HUMAN Link Image
Enzyme 80 PDB ID Not Available
Enzyme 80 Cellular Location Not Available
Enzyme 80 Gene Sequence >2211 bp
ATGGAGGCGCTAATTCCTGTCATAAACAAGCTCCAGGACGTCTTCAACACGGTGGGCGCC
GACATCATCCAGCTGCCTCAAATCGTCGTAGTGGGAACGCAGAGCAGCGGAAAGAGCTCA
GTGCTAGAAAGCCTGGTGGGGAGGGACCTGCTTCCCAGAGGTACTGGAATTGTCACCCGG
AGACCTCTCATTCTGCAACTGGTCCATGTTTCACAAGAAGATAAACGGAAAACAACAGGA
GAAGAAAATGGGGTGGAAGCAGAAGAATGGGGTAAATTTCTTCACACCAAAAATAAGCTT
TACACGGATTTTGATGAAATTCGACAAGAAATTGAAAATGAAACAGAAAGAATTTCAGGA
AATAATAAGGGAGTAAGCCCTGAACCAATTCATCTTAAGATTTTTTCACCCAACGTTGTC
AATTTGACACTTGTGGATTTGCCAGGAATGACCAAGGTGCCTGTAGGTGATCAACCTAAG
GATATTGAGCTTCAAATCAGAGAGCTCATTCTTCGGTTCATCAGTAATCCTAATTCCATT
ATCCTCGCTGTCACTGCTGCTAATACAGATATGGCAACATCAGAGGCACTTAAAATTTCA
AGAGAGGTAGATCCAGATGGTCGCAGAACCCTAGCTGTAATCACTAAACTTGATCTCATG
GATGCGGGTACTGATGCCATGGATGTATTGATGGGAAGGGTTATTCCAGTCAAACTTGGA
ATAATTGGAGTAGTTAACAGGAGCCAGCTAGATATTAACAACAAGAAGAGTGTAACTGAT
TCAATCCGTGATGAGTATGCTTTTCTTCAAAAGAAATATCCATCTCTGGCCAATAGAAAT
GGAACAAAGTATCTTGCTAGGACTCTAAACAGGTTACTGATGCATCACATCAGAGATTGT
TTACCAGAGTTGAAAACAAGAATAAATGTTCTAGCTGCTCAGTATCAGTCTCTTCTAAAT
AGCTACGGTGAACCCGTGGATGATAAAAGTGCTACTTTACTCCAACTTATTACCAAATTT
GCCACAGAATATTGTAACACTATTGAAGGAACTGCAAAATATATTGAAACTTCGGAGCTA
TGCGGTGGTGCTAGAATTTGTTATATTTTCCATGAGACTTTTGGGCGAACCTTAGAATCT
GTTGATCCACTTGGTGGCCTTAACACTATTGACATTTTGACTGCCATTAGAAATGCTACT
GGTCCTCGTCCTGCTTTATTTGTGCCTGAGGTTTCATTTGAGTTACTGGTGAAGCGGCAA
ATCAAACGTCTAGAAGAGCCCAGCCTCCGCTGTGTGGAACTGGTTCATGAGGAAATGCAA
AGGATCATTCAGCACTGTAGCAATTACAGTACACAGGAATTGTTACGATTTCCTAAACTT
CATGATGCCATAGTTGAAGTGGTGACTTGTCTTCTTCGTAAAAGGTTGCCTGTTACAAAT
GAAATGGTCCATAACTTAGTGGCAATTGAACTGGCTTATATCAACACAAAACATCCAGAC
TTTGCTGATGCTTGTGGGCTAATGAACAATAATATAGAGGAACAAAGGAGAAACAGGCTA
GCCAGAGAATTACCTTCAGCTGTATCACGAGACAAGTCTTCTAAAGTTCCAAGTGCTTTG
GCACCTGCCTCCCAGGAGCCCTCCCCCGCTGCTTCTGCTGAGGCTGATGGCAAGTTAATT
CAGGACAGCAGAAGAGAAACTAAAAATGTTGCATCTGGAGGTGGTGGGGTTGGAGATGGT
GTTCAAGAACCAACCACAGGCAACTGGAGAGGAATGCTGAAAACTTCAAAAGCTGAAGAG
TTATTAGCAGAAGAAAAATCAAAACCCATTCCAATTATGCCAGCCAGTCCACAAAAAGGT
CATGCCGTGAACCTGCTAGATGTGCCAGTTCCTGTTGCACGAAAACTATCTGCTCGGGAA
CAGCGAGATTGTGAGGTTATTGAACGACTCATTAAATCATATTTTCTCATTGTCAGAAAG
AATATTCAAGACAGTGTGCCAAAGGCAGTAATGCATTTTTTGGTTAATCATGTGAAAGAC
ACTCTTCAGAGTGAGCTAGTAGGCCAGCTGTATAAATCATCCTTATTGGATGATCTTCTG
ACAGAATCTGAGGACATGGCACAGCGCAGGAAAGAAGCAGCTGATATGCTAAAGGCATTA
CAAGGAGCCAGTCAAATTATTGCTGAAATCCGGGAGACTCATCTTTGGTGA
Enzyme 80 GenBank Gene ID AB006965 Link Image
Enzyme 80 GeneCard ID DNM1L Link Image
Enzyme 80 GenAtlas ID DNM1L Link Image
Enzyme 80 HGNC ID HGNC:2973 Link Image
Enzyme 80 Chromosome Location 1
Enzyme 80 Locus 12p11.21
Enzyme 80 SNPs SNPJam Report Link Image
Enzyme 80 General References
  1. Shin HW, Shinotsuka C, Torii S, Murakami K, Nakayama K: Identification and subcellular localization of a novel mammalian dynamin-related protein homologous to yeast Vps1p and Dnm1p. J Biochem. 1997 Sep;122(3):525-30. [PubMed Link Image]
  2. Hong YR, Chen CH, Cheng DS, Howng SL, Chow CC: Human dynamin-like protein interacts with the glycogen synthase kinase 3beta. Biochem Biophys Res Commun. 1998 Aug 28;249(3):697-703. [PubMed Link Image]
  3. Imoto M, Tachibana I, Urrutia R: Identification and functional characterization of a novel human protein highly related to the yeast dynamin-like GTPase Vps1p. J Cell Sci. 1998 May;111 ( Pt 10):1341-9. [PubMed Link Image]
  4. Chen CH, Howng SL, Hwang SL, Chou CK, Liao CH, Hong YR: Differential expression of four human dynamin-like protein variants in brain tumors. DNA Cell Biol. 2000 Mar;19(3):189-94. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
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  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Kamimoto T, Nagai Y, Onogi H, Muro Y, Wakabayashi T, Hagiwara M: Dymple, a novel dynamin-like high molecular weight GTPase lacking a proline-rich carboxyl-terminal domain in mammalian cells. J Biol Chem. 1998 Jan 9;273(2):1044-51. [PubMed Link Image]
  9. Yoon Y, Pitts KR, Dahan S, McNiven MA: A novel dynamin-like protein associates with cytoplasmic vesicles and tubules of the endoplasmic reticulum in mammalian cells. J Cell Biol. 1998 Feb 23;140(4):779-93. [PubMed Link Image]
  10. Smirnova E, Shurland DL, Ryazantsev SN, van der Bliek AM: A human dynamin-related protein controls the distribution of mitochondria. J Cell Biol. 1998 Oct 19;143(2):351-8. [PubMed Link Image]
  11. Shin HW, Takatsu H, Mukai H, Munekata E, Murakami K, Nakayama K: Intermolecular and interdomain interactions of a dynamin-related GTP-binding protein, Dnm1p/Vps1p-like protein. J Biol Chem. 1999 Jan 29;274(5):2780-5. [PubMed Link Image]
  12. Smirnova E, Griparic L, Shurland DL, van der Bliek AM: Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells. Mol Biol Cell. 2001 Aug;12(8):2245-56. [PubMed Link Image]
  13. Koch A, Thiemann M, Grabenbauer M, Yoon Y, McNiven MA, Schrader M: Dynamin-like protein 1 is involved in peroxisomal fission. J Biol Chem. 2003 Mar 7;278(10):8597-605. Epub 2002 Dec 23. [PubMed Link Image]
  14. Li X, Gould SJ: The dynamin-like GTPase DLP1 is essential for peroxisome division and is recruited to peroxisomes in part by PEX11. J Biol Chem. 2003 May 9;278(19):17012-20. Epub 2003 Mar 4. [PubMed Link Image]
  15. Zhu PP, Patterson A, Stadler J, Seeburg DP, Sheng M, Blackstone C: Intra- and intermolecular domain interactions of the C-terminal GTPase effector domain of the multimeric dynamin-like GTPase Drp1. J Biol Chem. 2004 Aug 20;279(34):35967-74. Epub 2004 Jun 18. [PubMed Link Image]
  16. Yonashiro R, Ishido S, Kyo S, Fukuda T, Goto E, Matsuki Y, Ohmura-Hoshino M, Sada K, Hotta H, Yamamura H, Inatome R, Yanagi S: A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics. EMBO J. 2006 Aug 9;25(15):3618-26. Epub 2006 Jul 27. [PubMed Link Image]
  17. Nakamura N, Kimura Y, Tokuda M, Honda S, Hirose S: MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology. EMBO Rep. 2006 Oct;7(10):1019-22. Epub 2006 Aug 25. [PubMed Link Image]
  18. Parone PA, James DI, Da Cruz S, Mattenberger Y, Donze O, Barja F, Martinou JC: Inhibiting the mitochondrial fission machinery does not prevent Bax/Bak-dependent apoptosis. Mol Cell Biol. 2006 Oct;26(20):7397-408. [PubMed Link Image]
  19. Taguchi N, Ishihara N, Jofuku A, Oka T, Mihara K: Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission. J Biol Chem. 2007 Apr 13;282(15):11521-9. Epub 2007 Feb 14. [PubMed Link Image]
  20. Chang CR, Blackstone C: Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology. J Biol Chem. 2007 Jul 27;282(30):21583-7. Epub 2007 Jun 6. [PubMed Link Image]
  21. Karbowski M, Neutzner A, Youle RJ: The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division. J Cell Biol. 2007 Jul 2;178(1):71-84. [PubMed Link Image]
  22. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  23. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  24. Han XJ, Lu YF, Li SA, Kaitsuka T, Sato Y, Tomizawa K, Nairn AC, Takei K, Matsui H, Matsushita M: CaM kinase I alpha-induced phosphorylation of Drp1 regulates mitochondrial morphology. J Cell Biol. 2008 Aug 11;182(3):573-85. [PubMed Link Image]
  25. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
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  29. Figueroa-Romero C, Iniguez-Lluhi JA, Stadler J, Chang CR, Arnoult D, Keller PJ, Hong Y, Blackstone C, Feldman EL: SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity cycle. FASEB J. 2009 Nov;23(11):3917-27. Epub 2009 Jul 28. [PubMed Link Image]
  30. Zunino R, Braschi E, Xu L, McBride HM: Translocation of SenP5 from the nucleoli to the mitochondria modulates DRP1-dependent fission during mitosis. J Biol Chem. 2009 Jun 26;284(26):17783-95. Epub 2009 May 1. [PubMed Link Image]
  31. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
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Enzyme 80 Metabolite References Not Available
Enzyme 81 [top]
Enzyme 81 ID 14062
Enzyme 81 Name Dedicator of cytokinesis protein 10
Enzyme 81 Synonyms
  1. Zizimin-3
Enzyme 81 Gene Name DOCK10
Enzyme 81 Protein Sequence >Dedicator of cytokinesis protein 10
MAGERTRRFTRSLLRPGQAAELRHSAASAAAVAVSSRQQQRQEKPRLLEPLDYETVIEEL
EKTYRNDPLQDLLFFPSDDFSAATVSWDIRTLYSTVPEDAEHKAENLLVKEACKFYSSQW
HVVNYKYEQYSGDIRQLPRAEYKPEKLPSHSFEIDHEDADKDEDTTSHSSSKGGGGAGGT
GVFKSGWLYKGNFNSTVNNTVTVRSFKKRYFQLTQLPDNSYIMNFYKDEKISKEPKGCIF
LDSCTGVVQNNRLRKYAFELKMNDLTYFVLAAETESDMDEWIHTLNRILQISPEGPLQGR
RSTELTDLGLDSLDNSVTCECTPEETDSSENNLHADFAKYLTETEDTVKTTRNMERLNLF
SLDPDIDTLKLQKKDLLEPESVIKPFEEKAAKRIMIICKALNSNLQGCVTENENDPITNI
EPFFVSVALYDLRDSRKISADFHVDLNHAAVRQMLLGASVALENGNIDTITPRQSEEPHI
KGLPEEWLKFPKQAVFSVSNPHSEIVLVAKIEKVLMGNIASGAEPYIKNPDSNKYAQKIL
KSNRQFCSKLGKYRMPFAWAVRYVFKDNQGNVDRDSRFSPLFRQESSKISTEDLVKLVSD
YRRADRISKMQTIPGSLDIAVDNVPLEHPDCVTSSFIPVKPFNMMAQTEPTVEVEEFVYD
STKYCRPYRVYKNQIYIYPKHLKYDSQKCFNKARNITVCIEFKNSDEESAKPLKCIYGKP
GGPLFTSAAYTAVLHHSQNPDFSDEVKIELPTQLHEKHHILFSFYHVTCDINAKANAKKK
EALETSVGYAWLPLMKHDQIASQEYNIPIATSLPPNYLSFQDSASHGGSDIKWVDGGKPL
FKVSTFVVSTVNTQDPHVNAFFQECQKREKDMSQSPTSNFIRSCKNLLNVEKIHAIMSFL
PIILNQLFKVLVQNEEDEITTTVTRVLTDIVAKCHEEQLDHSVQSYIKFVFKTRACKERT
VHEELAKNVTGLLKSNDSTTVKHVLEHSWFFFAIILKSMAQHLIDTNKIQLPRPQRFPES
YQNELDNLVMVLSDHVIWKYKDALEETRRANHSVARFLKRCFTFMDRGYVFKMVNNYISM
FSSGDFQTLCQYKFDFLQEVCQHEHFIPLCLPIRSANIPDPLTPSESTQELHASDMPEYS
VTNEFCRKHFLIGILLREVGFALQEDQDVRHLALAVLKNLMAKHSFDDRYRERKQAQIAS
LYMPLYGMLLDNMPRIYLKDLYPFTVNTSNQGSRDDLSTNGGFQSQTAIKHANSVDTSFS
KDVLNSIAAFSSIAISTVNHADSRASLASLDSNPSTNEKSSEKTDNCEKVPRPLSLIGST
LRFDKLDQAETRSLLMCFLHIMKTISDETLIAYWQRAPSPEVSDFFSILEVCLQNFRYLG
KRNIIRKIAAAFKFVQSTQNNGTLKGSNPSCQTSGLLSQWMHSTSSHEGHKQHRSQTLPI
IRGKNALSNPKLLQMLDNTMTSNSNEIDIVHHVDTEANIATEVCLTILDLLSLFTQTHQR
QLQQCDCQNSLMKRVFDTYMLFFQVNQSATALKHVFASLRLFVCKFPSAFFQGPADLCGS
FCYEVLKCCNHRSRSTQTEASALLYFFMRKNFEFNKQKSIVRSHLQLIKAVSQLIADAGI
GGSRFQHSLAITNNFANGDKQMKNSNFPAEVKDLTKRIRTVLMATAQMKEHEKDPEMLVD
LQYSLANSYASTPELRRTWLESMAKIHARNGDLSEAAMCYIHIAALIAEYLKRKGYWKVE
KICTASLLSEDTHPCDSNSLLTTPSGGSMFSMGWPAFLSITPNIKEEGAMKEDSGMQDTP
YNENILVEQLYMCVEFLWKSERYELIADVNKPIIAVFEKQRDFKKLSDLYYDIHRSYLKV
AEVVNSEKRLFGRYYRVAFYGQGFFEEEEGKEYIYKEPKLTGLSEISQRLLKLYADKFGA
DNVKIIQDSNKVNPKDLDPKYAYIQVTYVTPFFEEKEIEDRKTDFEMHHNINRFVFETPF
TLSGKKHGGVAEQCKRRTILTTSHLFPYVKKRIQVISQSSTELNPIEVAIDEMSKKVSEL
NQLCTMEEVDMIRLQLKLQGSVSVKVNAGPMAYARAFLEETNAKKYPDNQVKLLKEIFRQ
FADACGQALDVNERLIKEDQLEYQEELRSHYKDMLSELSTVMNEQITGRDDLSKRGVDQT
CTRVISKATPALPTVSISSSAEV
Enzyme 81 Number of Residues 2183
Enzyme 81 Molecular Weight 249310.2
Enzyme 81 Theoretical pI 6.93
Enzyme 81 GO Classification
Function
  • GTP binding
  • GTPase binding
  • GTPase regulator activity
  • binding
  • enzyme binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
Process
Component
Enzyme 81 General Function Involved in guanyl-nucleotide exchange factor activity
Enzyme 81 Specific Function Potential guanine nucleotide exchange factor (GEF). GEF proteins activate some small GTPases by exchanging bound GDP for free GTP
Enzyme 81 Pathways Not Available
Enzyme 81 Reactions Not Available
Enzyme 81 Pfam Domain Function
Enzyme 81 Signals
  • None
Enzyme 81 Transmembrane Regions
  • None
Enzyme 81 Essentiality Not Available
Enzyme 81 GenBank ID Protein 154146189 Link Image
Enzyme 81 UniProtKB/Swiss-Prot ID Q96BY6 Link Image
Enzyme 81 UniProtKB/Swiss-Prot Entry Name DOC10_HUMAN Link Image
Enzyme 81 PDB ID Not Available
Enzyme 81 Cellular Location Not Available
Enzyme 81 Gene Sequence >6561 bp
ATGGCCGGTGAGCGGACCCGCAGGTTCACCCGGAGCCTGTTGAGACCTGGGCAGGCGGCC
GAGCTCCGGCACAGCGCCGCGTCCGCCGCCGCGGTGGCAGTCAGCAGCCGGCAGCAGCAG
CGGCAAGAAAAGCCTAGGCTTCTCGAGCCTTTGGATTATGAGACTGTCATTGAAGAACTT
GAAAAGACCTACCGGAATGATCCTCTTCAAGATCTCTTGTTCTTCCCCAGTGATGACTTT
TCAGCAGCCACAGTTTCCTGGGATATCCGCACGTTGTACTCAACAGTACCTGAAGATGCA
GAGCACAAGGCAGAAAATTTACTGGTTAAGGAGGCTTGTAAATTTTATAGTTCCCAGTGG
CATGTGGTAAACTACAAATATGAACAATATTCTGGAGACATTCGACAGCTACCCCGAGCA
GAATACAAACCAGAGAAGCTTCCTTCACATTCCTTTGAGATTGACCATGAAGATGCTGAT
AAGGATGAAGATACCACTTCCCACTCGTCTTCCAAGGGGGGTGGAGGAGCGGGAGGAACT
GGTGTTTTCAAGTCCGGCTGGCTCTACAAGGGGAATTTTAACAGCACCGTGAACAACACC
GTTACTGTTCGGTCATTCAAAAAGCGCTACTTCCAGCTGACTCAGTTACCAGATAACTCC
TACATTATGAACTTTTACAAAGATGAGAAAATATCCAAAGAACCCAAAGGATGCATCTTT
TTGGATTCCTGTACAGGAGTGGTGCAGAATAACAGACTAAGAAAATATGCCTTTGAATTG
AAAATGAATGATCTGACCTATTTTGTGCTGGCAGCTGAAACAGAGTCAGATATGGATGAA
TGGATCCACACCCTCAACCGCATTCTGCAAATCAGTCCTGAGGGGCCCCTCCAAGGGAGG
AGGAGCACAGAGCTCACTGATCTGGGTCTGGATTCGCTGGATAATTCTGTAACTTGTGAA
TGCACGCCAGAGGAAACAGATTCTTCAGAGAACAACCTACACGCAGACTTTGCAAAGTAC
CTCACAGAAACAGAAGATACTGTAAAAACAACTCGAAACATGGAGAGGCTAAATCTGTTC
TCTCTAGATCCAGACATAGATACCTTGAAACTTCAAAAAAAAGATCTCTTGGAACCTGAG
TCTGTGATCAAACCATTTGAAGAAAAAGCTGCCAAGAGAATCATGATCATCTGTAAAGCC
CTCAACTCAAATCTTCAGGGATGTGTTACGGAGAATGAAAATGATCCGATAACGAATATT
GAGCCTTTTTTTGTGAGTGTGGCACTTTATGACCTCAGAGACAGCAGGAAGATTTCTGCT
GATTTTCATGTGGATCTAAACCATGCTGCTGTCAGACAGATGCTCTTGGGGGCTTCTGTG
GCTTTGGAAAATGGCAACATCGACACCATCACTCCAAGACAATCAGAAGAACCTCACATC
AAGGGACTTCCAGAGGAATGGCTAAAATTTCCAAAGCAGGCTGTATTTTCTGTAAGCAAT
CCACATTCTGAAATTGTTTTGGTGGCCAAAATCGAAAAAGTCTTGATGGGAAACATTGCA
AGTGGTGCCGAACCTTATATTAAGAACCCAGACTCCAACAAGTATGCACAAAAGATACTA
AAATCCAACAGACAATTCTGCAGCAAATTGGGAAAATACCGTATGCCTTTTGCTTGGGCA
GTAAGATCAGTATTTAAGGACAACCAGGGAAATGTGGACAGAGACTCAAGATTTTCACCA
TTGTTTAGACAAGAAAGTAGCAAGATTTCAACTGAGGACCTAGTTAAACTAGTATCAGAT
TATAGAAGGGCCGACAGAATAAGCAAAATGCAGACCATTCCTGGAAGCCTGGATATTGCT
GTTGACAACGTTCCCTTGGAGCATCCAAATTGTGTAACATCGTCCTTTATCCCTGTCAAG
CCTTTCAACATGATGGCTCAAACAGAACCCACAGTGGAGGTGGAAGAATTTGTTTACGAT
TCAACAAAGTATTGTCGGCCTTACAGAGTATATAAAAATCAAATTTATATTTACCCCAAA
CACCTCAAGTATGATAGCCAGAAATGCTTCAACAAGGCACGGAATATAACTGTGTGCATT
GAATTCAAAAATTCAGATGAAGAAAGTGCCAAGCCCCTGAAGTGTATTTATGGAAAACCT
GGAGGGCCCCTCTTCACCTCAGCCGCCTACACAGCAGTTCTGCACCACTCTCAGAATCCG
GATTTCTCAGATGAGGTGAAAATTGAGCTACCAACACAACTCCATGAGAAACACCATATT
TTGTTTTCTTTTTATCACGTCACCTGTGACATCAATGCAAAAGCTAATGCCAAAAAGAAG
GAGGCTCTGGAAACGTCAGTTGGATATGCTTGGCTTCCTCTGATGAAACACGATCAGATA
GCTTCTCAAGAGTACAACATCCCAATAGCAACAAGTCTGCCTCCTAATTATTTAAGCTTT
CAAGATTCTGCAAGTGGAAAGCATGGTGGGAGTGACATTAAATGGGTTGATGGTGGCAAA
CCACTTTTCAAAGTGTCGACATTTGTTGTATCAACAGTAAATACTCAGGATCCACATGTG
AATGCATTTTTCCAAGAGTGCCAAAAAAGAGAGAAAGATATGTCTCAGTCACCTACCTCA
AATTTCATCCGCTCTTGTAAGAACTTATTGAATGTGGAAAAGATTCATGCAATCATGAGT
TTTCTGCCTATAATTTTGAATCAGCTCTTCAAAGTTCTGGTACAGAATGAGGAAGATGAA
ATAACTACAACTGTCACCAGGGTTCTGACCGACATTGTGGCCAAGTGCCATGAGGAGCAG
CTGGATCATTCTGTCCAGTCATATATTAAGTTCGTGTTCAAGACCAGGGCATGCAAGGAG
AGGACTGTACATGAGGAACTGGCTAAAAATGTGACTGGTCTTTTGAAATCAAATGACTCA
ACAACAGTAAAGCATGTCCTAAAGCATTCCTGGTTCTTCTTTGCAATTATCCTAAAATCG
ATGGCACAGCACTTGATTGACACAAATAAAATCCAGCTTCCCCGGCCTCAGAGATTTCCT
GAATCTTACCAAAATGAATTGGACAATCTTGTCATGGTCCTATCCGACCATGTGATTTGG
AAATACAAGGATGCACTTGAAGAAACAAGAAGGGCAAACCACAGCGTTGCCAGATTTCTC
AAGCGCTGCTTTACATTTATGGACCGAGGGTATGTGTTTAAGATGGTCAACAATTACATC
AGCATGTTCTCCTCCGGTGACCTTAAGACCTTGTGCCAGTATAAATTTGATTTTCTTCAA
GAAGTATGTCAACATGAACACTTTATCCCTTTGTGTCTGCCCATAAGATCAGCAAACATT
CCAGATCCTTTGACACCTTCAGAATCGACTCAAGAGTTACATGCATCAGATATGCCTGAA
TATTCAGTCACAAATGAATTTTGTCGCAAACACTTCTTAATCGGAATTCTGCTCCGAGAA
GTTGGCTTTGCCCTGCAGGAAGACCAAGATGTCAGACACTTAGCTTTAGCTGTCCTAAAA
AATCTAATGGCTAAGCATTCATTTGATGATCGATACAGAGAGCCAAGAAAGCAGGCCCAG
ATAGCAAGTTTATACATGCCCCTGTACGGCATGCTCCTGGACAATATGCCAAGGATTTAT
CTGAAGGACCTGTATCCTTTTACTGTCAATACATCTAATCAGGGGTCTAGAGATGATCTA
AGCACCAATGGAGGATTTCAAAGCCAGACAGCTATCAAACATGCAAACTCTGTGGATACA
TCATTTTCTAAAGATGTTTTAAATTCCATAGCAGCATTTTCATCAATAGCTATTTCTACA
GTAAACCATGCTGACTCCAGAGCATCTTTAGCAAGTCTTGACTCCAATCCAAGTACCAAT
GAGAAGAGCAGTGAGAAGACGGACAACTGTGAAAAGATCCCAAGACCCTTGTCTTTGATT
GGCTCAACTCTTCGATTTGACAAGTTAGATCAAGCAGAAACCAGGAGTCTCCTGATGTGT
TTTCTTCACATTATGAAAACGATTTCGTACGAGACTCTGATTGCCTACTGGCAGAGAGCT
CCCAGCCCAGAGGTGTCCGACTTCTTCAGCATCTTGGACGTTTGTCTTCAAAATTTCAGA
TACCTAGGAAAACGCAACATAATAAGAAAAATTGCTGCTGCATTTAAATTTGTGCAGTCC
ACCCAGAACAATGGAACTCTCAAAGGATCCAATCCTTCCTGCCAGACATCAGGTCTCTTG
TCACAATGGATGCACTCCACTTCCAGTCATGAAGGCCATAAGCAGCACAGATCACAAACT
TTACCTATAATTCGAGGCAAAAATGCACTTTCTAACCCCAAACTCTTACAGATGTTAGAC
AATACCATGACCAGCAACTCCAATGAAATAGACATCGTGCATCATGTAGACACTGAGGCC
AATATAGCTACGGAGGTTTGCCTCACTATTCTGGACCTGTTATCCCTCTTCACACAGACT
CATCAGAGACAACTCCAACAATGTGACTGTCAAAATTCATTGATGAAAAGGGTCTTTGAT
ACCTACATGCTCTTTTTCCAAGTCAATCAGTCAGCCACAGCGCTGAAGCATGTGTTTGCC
TCCTTGAGACTGTTTGTATGCAAGTTTCCTTCAGCGTTCTTTCAAGGGCCTGCTGACCTC
TGTGGATCATTCTGTTACGAAGTCCTAAAATGCTGTAACCACAGGTCACGGTCAACTCAG
ACAGAAGCCTCAGCCCTTCTGTACTTTTTCATGAGGAAGAATTTTGAATTTAACAAGCAG
AAGTCAATTGTCCGGTCCCACTTACAACTCATCAAAGCTGTGAGCCAGTTAATAGCCGAT
GCTGGGATTGGAGGCTCTCGGTTTCAACATTCGCTTGCAATTACCAATAATTTCGCCAAT
GGAGATAAGCAAATGAAAAACAGCAATTTCCCAGCAGAGGTGAAGGACCTGACTAAGCGT
ATAAGGACTGTTTTGATGGCCACAGCTCAGATGAAGGAGCACGAGAAGGACCCCGAGATG
CTGGTGGATCTCCAGTACAGCCTGGCAAACTCCTACGCAAGCACTCCTGAACTACGCAGG
ACCTGGCTGGAAAGTATGGCCAAGATTCATGCCAGAAACGGAGATTTATCTGAGGCTGCC
ATGTGTTACATCCATATTGCTGCTCTCATTGCAGAGTATCTGAAAAGAAAGGGTTACTGG
AAAGTGGAAAAGATTTGCACAGCATCCCTGCTCTCGGAGGATACCCACCCCTGTGATAGC
AACTCATTACTAACAACTCCCAGTGGAGGAAGCATGTTCTCTATGGGATGGCCAGCTTTT
TTGAGCATTACACCAAACATTAAGGAAGAAGGAGCGATGAAAGAGGATTCTGGAATGCAA
GATACACCATACAATGAGAATATCCTGGTGGAGCAGCTATACATGTGTGTGGAGTTTCTC
TGGAAGTCTGAGCGATATGAACTCATTGCTGATGTCAACAAGCCCATCATTGCTGTCTTT
GAGAAACAACGAGACTTCAAAAAATTGTCAGATCTCTACTACGACATTCATCGGTCATAT
CTGAAAGTGGCAGAGGTGGTGAATTCGGAGAAGCGGCTGTTTGGTCGCTACTATCGTGTG
GCATTTTATGGGCAGGGCTTTTTTGAAGAAGAAGAAGGTAAAGAGTATATTTATAAAGAG
CCTAAGCTGACAGGTCTGTCCGAGATTTCCCAAAGATTACTCAAGCTCTATGCAGATAAA
TTTGGAGCAGACAATGTGAAGATAATCCAGGATTCCAACAAGGTAAACCCCAAGGATTTG
GACCCCAAATATGCCTACATCCAGGTGACCTATGTGACGCCGTTCTTTGAGGAAAAGGAA
ATCGAAGACCGGAAGACAGATTTCGAAATGCACCACAACATCAACCGCTTTGTCTTCGAG
ACACCCTTCACGCTGTCGGGCAAGAAGCACGGTGGGGTGGCGGAGCAGTGCAAGCGGCGG
ACGATCCTGACAACGAGTCACCTGTTCCCCTACGTGAAGAAGAGAATACAAGTAATTAGC
CAATCGAGCACAGAACTGAATCCAATTGAAGTGGCAATTGACGAGATGTCCAAGAAGGTT
TCTGAGCTTAATCAGCTTTGCACAATGGAAGAAGTGGACATGATCAGACTGCAGCTCAAA
CTGCAAGGAAGTGTCAGCGTGAAGGTTAATGCTGGGCCAATGGCCTATGCACGAGCTTTT
CTTGAAGAAACCAATGCAAAGAAGTACCCTGACAACCAAGTAAAGCTTTTGAAGGAGATC
TTCAGGCAATTTGCAGATGCATGTGGGCAGGCCCTTGACGTGAATGAGCGCCTCATCAAA
GAGGACCAGCTGGAGTACCAGGAAGAACTGAGGTCCCACTACAAGGACATGCTCAGCGAA
CTCTCCACAGTCATGAATGAGCAGATTACGGGCAGGGACGACCTGTCAAAGCGCGGAGTG
GACCAAACCTGCACTCGAGTAATTAGCAAAGCAACTCCGGCCCTACCCACGGTCTCCATC
TCATCTAGTGCTGAAGTCTGA
Enzyme 81 GenBank Gene ID Not Available
Enzyme 81 GeneCard ID DOCK10 Link Image
Enzyme 81 GenAtlas ID DOCK10 Link Image
Enzyme 81 HGNC ID HGNC:23479 Link Image
Enzyme 81 Chromosome Location 2
Enzyme 81 Locus 2q36.2
Enzyme 81 SNPs SNPJam Report Link Image
Enzyme 81 General References
  1. Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Jun 30;5(3):169-76. [PubMed Link Image]
  2. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Cote JF, Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J Cell Sci. 2002 Dec 15;115(Pt 24):4901-13. [PubMed Link Image]
  7. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  8. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  9. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  10. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 81 Metabolite References Not Available
Enzyme 82 [top]
Enzyme 82 ID 14064
Enzyme 82 Name Dedicator of cytokinesis protein 1
Enzyme 82 Synonyms
  1. 180 kDa protein downstream of CRK
  2. DOCK180
Enzyme 82 Gene Name DOCK1
Enzyme 82 Protein Sequence >Dedicator of cytokinesis protein 1
MTRWVPTKREEKYGVAFYNYDARGADELSLQIGDTVHILETYEGWYRGYTLRKKSKKGIF
PASYIHLKEAIVEGKGQHETVIPGDLPLIQEVTTTLREWSTIWRQLYVQDNREMFRSVRH
MIYDLIEWRSQILSGTLPQDELKELKKKVTAKIDYGNRILDLDLVVRDEDGNILDPELTS
TISLFRAHEIASKQVEERLQEEKSQKQNIDINRQAKFAATPSLALFVNLKNVVCKIGEDA
EVLMSLYDPVESKFISENYLVRWSSSGLPKDIDRLHNLRAVFTDLGSKDLKREKISFVCQ
IVRVGRMELRDNNTRKLTSGLRRPFGVAVMDVTDIINGKVDDEDKQHFIPFQPVAGENDF
LQTVINKVIAAKEVNHKGQGLWVTLKLLPGDIHQIRKEFPHLVDRTTAVARKTGFPEIIM
PGDVRNDIYVTLVQGDFDKGSKTTAKNVEVTVSVYDEDGKRLEHVIFPGAGDEAISEYKS
VIYYQVKQPRWFETVKVAIPIEDVNRSHLRFTFRHRSSQDSKDKSEKIFALAFVKLMRYD
GTTLRDGEHDLIVYKAEAKKLEDAATYLSLPSTKAELEEKGHSATGKSMQSLGSCTISKD
SFQISTLVCSTKLTQNVDLLGLLKWRSNTSLLQQNLRQLMKVDGGEVVKFLQDTLDALFN
IMMENSESETFDTLVFDALVFIIGLIADRKFQHFNPVLETYIKKHFSATLAYTKLTKVLK
NYVDGAEKPGVNEQLYKAMKALESIFKFIVRSRILFNQLYENKGEADFVESLLQLFRSIN
DMMSSMSDQTVRVKGAALKYLPTIVNDVKLVFDPKELSKMFTEFILNVPMGLLTIQKLYC
LIEIVHSDLFTQHDCREILLPMMTDQLKYHLERQEDLEACCQLLSHILEVLYRKDVGPTQ
RHVQIIMEKLLRTVNRTVISMGRDSELIGNFVACMTAILRQMEDYHYAHLIKTFGKMRTD
VVDFLMETFIMFKNLIGKNVYPFDWVIMNMVQNKVFLRAINQYADMLNKKFLDQANFELQ
LWNNYFHLAVAFLTQESLQLENFSSAKRAKILNKYGDMRRQIGFEIRDMWYNLGQHKIKF
IPEMVGPILEMTLIPETELRKATIPIFFDMMQCEFHSTRSFQMFENEIITKLDHEVEGGR
GDEQYKVLFDKILLEHCRKHKYLAKTGETFVKLVVRLMERLLDYRTIMHDENKENRMSCT
VNVLNFYKEIEREEMYIRYLYKLCDLHKECDNYTEAAYTLLLHAKLLKWSEDVCVAHLTQ
RDGYQATTQGQLKEQLYQEIIHYFDKGKMWEEAIALGKELAEQYENEMFDYEQLSELLKK
QAQFYENIVKVIRPKPDYFAVGYYGQGFPTFLRGKVFIYRGKEYERREDFEARLLTQFPN
AEKMKTTSPPGDDIKNSPGQYIQCFTVKPKLDLPPKFHRPVSEQIVSFYRVNEVQRFEYS
RPIRKGEKNPDNEFANMWIERTIYTTAYKLPGILRWFEVKSVFMVEISPLENAIETMQLT
NDKINSMVQQHLDDPSLPINPLSMLLNGIVDPAVMGGFANYEKAFFTDRYLQEHPEAHEK
IEKLKDLIAWQIPFLAEGIRIHGDKVTEALRPFHERMEACFKQLKEKVEKEYGVRIMPSS
LDDRRGSRPRSMVRSFTMPSSSRPLSVASVSSLSSDSTPSRPGSDGFALEPLLPKKMHSR
SQDKLDKDDLEKEKKDKKKEKRNSKHQEIFEKEFKPTDISLQQSEAVILSETISPLRPQR
PKSQVMNVIGSERRFSVSPSSPSSQQTPPPVTPRAKLSFSMQSSLELNGMTGADVADVPP
PLPLKGSVADYGNLMENQDLLGSPTPPPPPPHQRHLPPPLPSKTPPPPPPKTTRKQASVD
SGIVQ
Enzyme 82 Number of Residues 1865
Enzyme 82 Molecular Weight 215344.1
Enzyme 82 Theoretical pI 7.61
Enzyme 82 GO Classification
Function
  • GTP binding
  • GTPase binding
  • GTPase regulator activity
  • binding
  • enzyme binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
Process
Component
Enzyme 82 General Function Involved in guanyl-nucleotide exchange factor activity
Enzyme 82 Specific Function Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Functions as a guanine nucleotide exchange factor (GEF), which activates Rac Rho small GTPases by exchanging bound GDP for free GTP. Its GEF activity may be enhanced by ELMO1
Enzyme 82 Pathways Not Available
Enzyme 82 Reactions Not Available
Enzyme 82 Pfam Domain Function
Enzyme 82 Signals
  • None
Enzyme 82 Transmembrane Regions
  • None
Enzyme 82 Essentiality Not Available
Enzyme 82 GenBank ID Protein 122889127 Link Image
Enzyme 82 UniProtKB/Swiss-Prot ID Q14185 Link Image
Enzyme 82 UniProtKB/Swiss-Prot Entry Name DOCK1_HUMAN Link Image
Enzyme 82 PDB ID Not Available
Enzyme 82 Cellular Location Not Available
Enzyme 82 Gene Sequence >5598 bp
ATGACGCGCTGGGTGCCCACCAAGCGCGAGGAGAAGTACGGCGTGGCTTTTTATAACTAT
GATGCCAGAGGAGCGGATGAACTTTCTTTACAGATCGGAGACACTGTGCACATCTTAGAA
ACATATGAAGGGTGGTACCGAGGTTACACGTTACGAAAAAAGTCTAAGAAGGGTATATTT
CCTGCTTCATATATTCATCTTAAAGAAGCGATAGTTGAAGGAAAAGGGCAACATGAAACA
GTCATCCCGGGTGACCTCCCCCTCATCCAGGAAGTCACCACGACACTCCGAGAGTGGTCC
ACCATCTGGAGGCAGCTCTACGTGCAAGATAACAGGGAGATGTTTCGAAGTGTGCGGCAC
ATGATCTATGACCTTATTGAATGGCGATCACAAATTCTTTCTGGAACTCTGCCTCAGGAT
GAACTCAAAGAACTGAAGAAGAAGGTCACAGCCAAAATTGATTATGGAAACAGAATTCTA
GATTTGGACCTGGTGGTTAGAGATGAAGATGGGAATATTTTGGATCCAGAATTAACTAGC
ACGATTAGTCTCTTCAGAGCTCATGAAATAGCTTCTAAACAAGTGGAGGAAAGGTTACAA
GAGGAAAAATCTCAAAAGCAGAACATAGATATTAACAGACAAGCCAAGTTTGCTGCAACC
CCTTCTCTGGCCTTGTTTGTGAACCTCAAAAATGTGGTTTGTAAAATAGGAGAAGATGCT
GAAGTCCTCATGTCTCTATATGACCCTGTGGAGTCCAAATTCATCAGTGAGAACTACCTG
GTTCGCTGGTCCAGTTCAGGATTACCTAAAGACATAGACAGATTACATAATTTGCGAGCC
GTGTTTACTGACCTCGGAAGCAAAGACCTGAAAAGGGAGAAAATCAGTTTTGTCTGTCAG
ATTGTTCGCGTGGGTCGCATGGAGCTGAGGGACAACAACACCAGGAAACTGACCTCGGGG
TTGCGGCGACCTTTTGGAGTGGCTGTGATGGATGTAACAGATATAATAAATGGAAAAGTA
GATGATGAAGATAAGCAGCATTTCATTCCCTTTCAGCCGGTGGCAGGGGAGAATGACTTC
CTTCAGACTGTTATAAACAAAGTCATCGCTGCCAAAGAAGTCAACCACAAGGGGCAGGGT
TTGTGGGTAACATTGAAATTACTTCCTGGAGATATCCATCAGATCCGAAAAGAGTTTCCG
CATTTAGTGGACAGGACCACAGCTGTGGCTCGAAAAACAGGGTTTCCGGAGATAATCATG
CCTGGTGATGTTCGAAATGATATCTATGTAACATTAGTTCAAGGAGATTTTGATAAAGGA
AGCAAAACAACAGCGAAGAACGTGGAGGTCACGGTGTCTGTGTACGATGAGGATGGGAAA
CGATTAGAGCATGTGATTTTCCCGGGTGCTGGTGATGAAGCGATTTCAGAGTACAAATCT
GTGATTTACTACCAAGTAAAGCAGCCACGCTGGTTTGAGACTGTTAAGGTGGCCATTCCC
ATCGAGGACGTTAACCGCAGTCACCTTCGGTTTACCTTCCGCCACAGGTCATCACAGGAC
TCTAAGGATAAATCTGAGAAAATATTTGCACTAGCATTTGTCAAGCTGATGAGATACGAT
GGTACCACCCTGCGAGACGGAGAGCACGATCTTATCGTCTATAAGGCCGAAGCAAAGAAG
CTGGAAGATGCTGCCACGTACTTGAGTCTGCCCTCCACGAAGGCAGAGTTGGAAGAAAAG
GGCCACTCGGCCACCGGCAAGAGCATGCAGAGCCTTGGGAGCTGCACCATTAGCAAGGAC
TCCTTCCAGATCTCCACGCTCGTGTGCTCCACCAAACTGACTCAGAACGTGGACCTTCTG
GGGCTCTTGAAATGGCGCTCCAACACCAGCCTGCTGCAGCAGAACTTGAGGCAGCTGATG
AAAGTCGATGGTGGTGAAGTAGTGAAGTTTCTTCAGGACACGTTGGATGCCCTCTTCAAC
ATCATGATGGAGAACTCAGAGAGTGAGACTTTTGACACGTTAGTCTTTGATGCTCTGGTA
TTTATCATTGGACTGATTGCTGATAGAAAATTTCAGCATTTTAATCCTGTTTTGGAAACT
TACATTAAGAAACACTTTAGTGCAACGTTAGCCTACACGAAGTTGACAAAAGTGTTGAAG
AACTACGTGGACGGTGCTGAGAAGCCGGGAGTAAATGAGCAGCTGTACAAAGCCATGAAA
GCGCTAGAATCCATCTTCAAGTTCATCGTGCGCTCCAGGATCCTGTTCAATCAACTGTAT
GAAAACAAGGGAGAGGCTGACTTCGTGGAATCTTTGCTGCAGCTCTTCAGGTCCATCAAT
GACATGATGAGCAGCATGTCAGACCAGACCGTCCGGGTGAAGGGGGCAGCACTGAAATAC
TTACCAACGATCGTCAACGATGTGAAATTGGTGTTTGATCCCAAAGAGCTCAGCAAAATG
TTTACTGAATTCATCCTCAATGTTCCCATGGGCTTGCTGACCATCCAGAAACTCTACTGC
TTGATCGAAATCGTCCACAGTGACCTCTTCACACAGCATGACTGCAGAGAGATCCTGCTT
CCCATGATGACCGATCAGCTCAAGTACCATCTGGAGAGACAGGAGGACCTGGAGGCCTGC
TGTCAGCTGCTCAGCCACATCCTGGAGGTGCTGTACAGGAAGGACGTGGGGCCAACCCAG
AGGCACGTCCAGATTATCATGGAGAAACTTCTCCGGACCGTGAACCGAACCGTCATTTCC
ATGGGACGAGATTCTGAACTCATTGGAAACTTCGTGGCTTGCATGACAGCTATTTTACGA
CAAATGGAAGATTACCATTATGCCCACTTGATCAAGACTTTTGGGAAAATGAGGACTGAT
GTGGTAGATTTCCTAATGGAAACATTCATCATGTTTAAGAACCTCATTGGAAAGAACGTT
TACCCCTTCGACTGGGTGATCATGAACATGGTGCAAAATAAAGTCTTCCTGCGAGCAATT
AATCAGTATGCAGATATGCTGAACAAAAAATTTCTGGATCAAGCCAACTTTGAGCTACAG
CTGTGGAACAACTACTTTCACCTGGCTGTTGCTTTCCTTACTCAAGAGTCCCTGCAACTG
GAGAATTTTTCAAGTGCCAAGAGAGCCAAAATCCTTAACAAGTACGGAGATATGAGGAGA
CAGATTGGCTTTGAAATCAGAGACATGTGGTACAACCTTGGTCAACACAAGATAAAGTTC
ATTCCAGAAATGGTGGGCCCAATATTAGAAATGACATTAATTCCCGAGACGGAGCTGCGC
AAAGCCACCATCCCCATCTTCTTTGATATGATGCAGTGTGAATTCCATTCGACCCGAAGC
TTCCAAATGTTTGAAAATGAGATCATCACCAAGCTGGATCATGAAGTCGAAGGAGGCAGA
GGAGACGAACAGTACAAAGTGTTATTTGATAAAATCCTTCTGGAACACTGCAGGAAGCAC
AAATACCTCGCCAAAACAGGAGAAACTTTTGTAAAACTCGTTGTGCGCTTAATGGAAAGG
CTTTTGGATTATAGAACCATCATGCACGACGAGAACAAAGAAAACCGCATGAGCTGCACC
GTCAATGTGCTGAATTTCTACAAAGAAATTGAAAGAGAAGAAATGTATATAAGGTATTTG
TACAAGCTCTGTGACCTGCACAAGGAGTGTGATAACTACACCGAAGCGGCTTACACCTTG
CTTCTCCATGCAAAGCTTCTTAAGTGGTCGGAGGATGTGTGTGTGGCCCACCTCACCCAG
CGGGACGGGTACCAGGCCACCACGCAGGGACAGCTGAAGGAGCAGCTCTACCAGGAAATC
ATCCACTACTTCGACAAAGGCAAGATGTGGGAGGAGGCCATTGCCTTGGGCAAGGAGCTA
GCCGAGCAGTATGAGAACGAAATGTTTGATTATGAGCAACTCAGCGAATTGCTGAAAAAA
CAGGCTCAGTTTTATGAAAACATCGTCAAAGTGATCAGGCCCAAGCCTGACTATTTTGCT
GTTGGCTACTACGGACAAGGGTTCCCCACATTCCTGCGGGGAAAAGTTTTCATTTACCGA
GGGAAAGAGTATGAGCGCCGGGAAGATTTTGAGGCTCGGCTCTTAACTCAGTTTCCAAAC
GCCGAGAAAATGAAGACAACATCTCCACCAGGCGACGATATTAAAAACTCTCCTGGCCAG
TATATTCAGTGCTTCACAGTGAAGCCCAAACTCGATCTGCCTCCTAAGTTTCACAGGCCA
GTGTCAGAGCAGATTGTAAGTTTTTACAGGGTGAACGAGGTCCAGCGATTTGAATATTCT
CGGCCAATCCGGAAGGGAGAGAAAAACCCAGACAATGAATTTGCGAATATGTGGATCGAG
AGAACCATATATACAACTGCATATAAATTACCTGGAATTTTAAGGTGGTTTGAGGTCAAG
TCTGTTTTCATGGTGGAAATCAGCCCCCTGGAGAATGCCATTGAGACCATGCAGCTGACG
AACGACAAGATCAACAGCATGGTGCAGCAGCACCTGGATGACCCCAGCCTGCCCATCAAC
CCGCTCTCCATGCTCCTGAACGGCATCGTGGACCCAGCTGTCATGGGGGGCTTCGCAAAC
TACGAAAAGGCCTTCTTTACAGACCGGTACCTGCAGGAGCACCCTGAGGCCCATGAAAAG
ATCGAGAAGCTCAAGGACCTGATTGCTTGGCAGATTCCTTTTCTGGCCGAAGGGATCAGA
ATCCATGGAGACAAAGTCACGGAGGCACTGAGGCCGTTCCACGAGAGGATGGAGGCCTGT
TTCAAACAGCTGAAGGAAAAGGTGGAGAAAGAGTACGGCGTCCGAATCATGCCCTCAAGT
CTGGATGATAGAAGAGGCAGCCGCCCCCGGTCCATGGTGCGGTCCTTCACGATGCCTTCC
TCATCCCGCCCTCTGTCTGTGGCCTCTGTCTCTTCCCTCTCATCGGACAGCACCCCTTCC
AGACCAGGCTCCGACGGGTTTGCCCTGGAGCCTCTCCTGCCAAAGAAAATGCACTCCAGG
TCCCAGGACAAGCTGGACAAGGATGACCTGGAGAAGGAGAAGAAGGACAAGAAGAAGGAA
AAAAGGAACAGCAAACATCAAGAGATATTTGAGAAAGAATTTAAACCCACCGACATTTCC
CTGCAGCAGTCTGAGGCTGTGATCCTTTCGGAAACGATAAGTCCCCTGCGGCCCCAGAGA
CCGAAGAGCCAGGTGATGAACGTCATTGGAAGCGAAAGGCGCTTCTCGGTGTCCCCCTCG
TCACCGTCCTCCCAGCAAACACCCCCTCCAGTTACACCAAGGGCCAAGCTCAGCTTCAGC
ATGCAGTCGAGCTTGGAGCTGAACGGCATGACGGGGGCGGACGTGGCCGATGTCCCACCC
CCTCTGCCTCTCAAAGGCAGCGTGGCAGATTACGGGAATTTGATGGAAAACCAGGACTTG
CTGGGCTCGCCAACACCTCCACCTCCCCCTCCACACCAGAGGCATCTGCCACCTCCACTG
CCCAGCAAAACTCCGCCTCCTCCCCCTCCAAAGACAACTCGCAAGCAGGCATCGGTGGAC
TCCGGGATCGTGCAGTGA
Enzyme 82 GenBank Gene ID AL157711 Link Image
Enzyme 82 GeneCard ID DOCK1 Link Image
Enzyme 82 GenAtlas ID DOCK1 Link Image
Enzyme 82 HGNC ID HGNC:2987 Link Image
Enzyme 82 Chromosome Location 1
Enzyme 82 Locus 10q26.13-q26.3
Enzyme 82 SNPs SNPJam Report Link Image
Enzyme 82 General References
  1. Hasegawa H, Kiyokawa E, Tanaka S, Nagashima K, Gotoh N, Shibuya M, Kurata T, Matsuda M: DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane. Mol Cell Biol. 1996 Apr;16(4):1770-6. [PubMed Link Image]
  2. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  3. Matsuda M, Ota S, Tanimura R, Nakamura H, Matuoka K, Takenawa T, Nagashima K, Kurata T: Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins. J Biol Chem. 1996 Jun 14;271(24):14468-72. [PubMed Link Image]
  4. Kiyokawa E, Hashimoto Y, Kobayashi S, Sugimura H, Kurata T, Matsuda M: Activation of Rac1 by a Crk SH3-binding protein, DOCK180. Genes Dev. 1998 Nov 1;12(21):3331-6. [PubMed Link Image]
  5. Tu Y, Kucik DF, Wu C: Identification and kinetic analysis of the interaction between Nck-2 and DOCK180. FEBS Lett. 2001 Mar 2;491(3):193-9. [PubMed Link Image]
  6. Kobayashi S, Shirai T, Kiyokawa E, Mochizuki N, Matsuda M, Fukui Y: Membrane recruitment of DOCK180 by binding to PtdIns(3,4,5)P3. Biochem J. 2001 Feb 15;354(Pt 1):73-8. [PubMed Link Image]
  7. Brugnera E, Haney L, Grimsley C, Lu M, Walk SF, Tosello-Trampont AC, Macara IG, Madhani H, Fink GR, Ravichandran KS: Unconventional Rac-GEF activity is mediated through the Dock180-ELMO complex. Nat Cell Biol. 2002 Aug;4(8):574-82. [PubMed Link Image]
  8. Cote JF, Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J Cell Sci. 2002 Dec 15;115(Pt 24):4901-13. [PubMed Link Image]
  9. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  10. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  11. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
Enzyme 82 Metabolite References Not Available
Enzyme 83 [top]
Enzyme 83 ID 14065
Enzyme 83 Name Dedicator of cytokinesis protein 2
Enzyme 83 Synonyms Not Available
Enzyme 83 Gene Name DOCK2
Enzyme 83 Protein Sequence >Dedicator of cytokinesis protein 2
MAPWRKADKERHGVAIYNFQGSGAPQLSLQIGDVVRIQETCGDWYRGYLIKHKMLQGIFP
KSFIHIKEVTVEKRRNTENIIPAEIPLAQEVTTTLWEWGSIWKQLYVASKKERFLQVQSM
MYDLMEWRSQLLSGTLPKDELKELKQKVTSKIDYGNKILELDLIVRDEDGNILDPDNTSV
ISLFHAHEEATDKITERIKEEMSKDQPDYAMYSRISSSPTHSLYVFVRNFVCRIGEDAEL
FMSLYDPNKQTVISENYLVRWGSRGFPKEIEMLNNLKVVFTDLGNKDLNRDKIYLICQIV
RVGKMDLKDTGAKKCTQGLRRPFGVAVMDITDIIKGKAESDEEKQHFIPFHPVTAENDFL
HSLLGKVIASKGDSGGQGLWVTMKMLVGDIIQIRKDYPHLVDRTTVVARKLGFPEIIMPG
DVRNDIYITLLQGDFDKYNKTTQRNVEVIMCVCAEDGKTLPNAICVGAGDKPMNEYRSVV
YYQVKQPRWMETVKVAVPIEDMQRIHLRFMFRHRSSLESKDKGEKNFAMSYVKLMKEDGT
TLHDGFHDLVVLKGDSKKMEDASAYLTLPSYRHHVENKGATLSRSSSSVGGLSVSSRDVF
SISTLVCSTKLTQNVGLLGLLKWRMKPQLLQENLEKLKIVDGEEVVKFLQDTLDALFNIM
MEHSQSDEYDILVFDALIYIIGLIADRKFQHFNTVLEAYIQQHFSATLAYKKLMTVLKTY
LDTSSRGEQCEPILRTLKALEYVFKFIVRSRTLFSQLYEGKEQMEFEESMRRLFESINNL
MKSQYKTTILLQVAALKYIPSVLHDVEMVFDAKLLSQLLYEFYTCIPPVKLQKQKVQSMN
EIVQSNLFKKQECRDILLPVITKELKELLEQKDDMQHQVLERKYCVELLNSILEVLSYQD
AAFTYHHIQEIMVQLLRTVNRTVITMGRDHILISHFVACMTAILNQMGDQHYSFYIETFQ
TSSELVDFLMETFIMFKDLIGKNVYPGDWMAMSMVQNRVFLRAINKFAETMNQKFLEHTN
FEFQLWNNYFHLAVAFITQDSLQLEQFSHAKYNKILNKYGDMRRLIGFSIRDMWYKLGQN
KICFIPGMVGPILEMTLIPEAELRKATIPIFFDMMLCEYQRSGDFKKFENEIILKLDHEV
EGGRGDEQYMQLLESILMECAAEHPTIAKSVENFVNLVKGLLEKLLDYRGVMTDESKDNR
MSCTVNLLNFYKDNNREEMYIRYLYKLRDLHLDCDNYTEAAYTLLLHTWLLKWSDEQCAS
QVMQTGQQHPQTHRQLKETLYETIIGYFDKGKMWEEAISLCKELAEQYEMEIFDYELLSQ
NLIQQAKFYESIMKILRPKPDYFAVGYYGQGFPSFLRNKVFIYRGKEYERREDFQMQLMT
QFPNAEKMNTTSAPGDDVKNAPGQYIQCFTVQPVLDEHPRFKNKPVPDQIINFYKSNYVQ
RFHYSRPVRRGTVDPENEFASMWIERTSFVTAYKLPGILRWFEVVHMSQTTISPLENAIE
TMSTANEKILMMINQYQSDETLPINPLSMLLNGIVDPAVMGGFAKYEKAFFTEEYVRDHP
EDQDKLTHLKDLIAWQIPFLGAGIKIHEKRVSDNLRPFHDRMEECFKNLKMKVEKEYGVR
EMPDFDDRRVGRPRSMLRSYRQMSIISLASMNSDCSTPSKPTSESFDLELASPKTPRVEQ
EEPISPGSTLPEVKLRRSKKRTKRSSVVFADEKAAAESDLKRLSRKHEFMSDTNLSEHAA
IPLKASVLSQMSFASQSMPTIPALALSVAGIPGLDEANTSPRLSQTFLQLSDGDKKTLTR
KKVNQFFKTMLASKSAEEGKQIPDSLSTDL
Enzyme 83 Number of Residues 1830
Enzyme 83 Molecular Weight 211946.7
Enzyme 83 Theoretical pI 6.87
Enzyme 83 GO Classification
Function
  • GTP binding
  • GTPase binding
  • GTPase regulator activity
  • binding
  • cation binding
  • electron carrier activity
  • enzyme binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • guanyl-nucleotide exchange factor activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
  • transition metal ion binding
Process
Component
Enzyme 83 General Function Involved in iron ion binding
Enzyme 83 Specific Function Involved in cytoskeletal rearrangements required for lymphocyte migration in response of chemokines. Activates RAC1 and RAC2 small GTPases, probably by functioning as a guanine nucleotide exchange factor (GEF), which exchanges bound GDP for free GTP. May also participate in IL2 transcriptional activation via the activation of RAC2
Enzyme 83 Pathways Not Available
Enzyme 83 Reactions Not Available
Enzyme 83 Pfam Domain Function
Enzyme 83 Signals
  • None
Enzyme 83 Transmembrane Regions
  • None
Enzyme 83 Essentiality Not Available
Enzyme 83 GenBank ID Protein 31377468 Link Image
Enzyme 83 UniProtKB/Swiss-Prot ID Q92608 Link Image
Enzyme 83 UniProtKB/Swiss-Prot Entry Name DOCK2_HUMAN Link Image
Enzyme 83 PDB ID Not Available
Enzyme 83 Cellular Location Not Available
Enzyme 83 Gene Sequence >5493 bp
ATGGCCCCCTGGCGCAAAGCTGACAAGGAGCGGCACGGCGTGGCCATATACAACTTCCAA
GGCAGCGGAGCCCCCCAGCTCTCCCTGCAGATCGGCGATGTGGTGCGAATACAGGAGACG
TGTGGAGACTGGTATAGGGGATACCTCATAAAGCACAAAATGTTACAGGGCATTTTTCCT
AAGTCATTTATCCACATCAAGGAAGTGACAGTTGAGAAAAGAAGAAATACTGAGAACATC
ATTCCTGCAGAAATTCCTCTGGCACAAGAAGTGACAACGACACTTTGGGAATGGGGAAGC
ATCTGGAAACAACTCTATGTGGCCAGCAAAAAGGAGCGTTTTCTCCAGGTGCAGTCCATG
ATGTACGATCTGATGGAGTGGAGGTCCCAGCTTCTCTCAGGAACCTTACCCAAGGATGAG
CTGAAGGAACTGAAGCAGAAAGTCACGTCCAAAATTGACTATGGCAACAAAATCCTTGAG
CTTGATTTGATTGTCAGAGATGAAGACGGAAATATCTTGGACCCTGATAATACCAGTGTC
ATCAGCTTGTTCCATGCACATGAGGAAGCAACTGATAAAATCACAGAGCGTATCAAAGAA
GAAATGTCAAAAGACCAGCCAGATTATGCAATGTATTCCCGGATCTCCTCATCCCCCACC
CATAGCCTCTATGTGTTTGTGAGAAACTTTGTGTGCAGAATTGGGGAAGATGCTGAGCTC
TTCATGTCTCTCTACGACCCCAACAAGCAAACGGTCATAAGTGAGAACTACCTAGTGCGA
TGGGGCAGCCGGGGCTTCCCTAAGGAGATTGAGATGCTCAACAATCTGAAGGTGGTCTTC
ACGGATCTTGGAAACAAAGACCTCAACAGGGATAAAATTTACTTGATTTGTCAAATAGTC
CGGGTCGGCAAGATGGATCTTAAGGATACTGGTGCAAAGAAGTGCACGCAGGGACTGAGG
AGGCCCTTTGGGGTGGCAGTTATGGATATAACAGACATCATCAAGGGGAAAGCAGAGAGT
GATGAAGAAAAGCAGCACTTCATTCCTTTTCACCCGGTTACAGCTGAGAATGACTTCCTA
CACAGCCTGCTGGGCAAAGTCATAGCCTCCAAGGGGGACAGTGGAGGGCAAGGCCTCTGG
GTGACCATGAAGATGCTGGTGGGTGACATCATTCAGATTCGCAAGGACTATCCACACCTG
GTGGACAGGACCACCGTGGTGGCCAGGAAGCTGGGATTCCCAGAGATCATCATGCCAGGG
GATGTCAGGAACGACATCTACATTACTCTCTTACAAGGTGACTTTGACAAGTACAACAAG
ACCACACAGAGGAATGTGGAAGTCATCATGTGTGTGTGCGCGGAGGATGGCAAAACGCTG
CCTAATGCAATTTGCGTGGGAGCAGGGGACAAGCCCATGAATGAGTATCGCTCCGTTGTG
TACTATCAAGTCAAACAGCCACGCTGGATGGAAACAGTCAAGGTGGCTGTCCCTATTGAA
GACATGCAGAGGATCCATCTGCGATTCATGTTTCGACATCGGTCATCTCTGGAATCTAAA
GATAAAGGAGAAAAGAACTTTGCCATGTCCTATGTGAAGCTGATGAAAGAAGATGGGACT
ACTCTACACGATGGATTCCATGACTTAGTTGTCCTCAAGGGGGACAGCAAGAAGATGGAG
GATGCCAGCGCATACCTGACCCTTCCTTCTTATCGACACCATGTGGAAAACAAGGGGGCC
ACGCTGAGCAGGAGCTCCAGCAGTGTTGGGGGGCTTTCTGTCAGCTCCCGGGATGTGTTC
TCCATTTCCACCCTGGTGTGCTCCACAAAGCTCACTCAGAATGTGGGCTTGCTGGGTTTG
CTGAAGTGGCGTATGAAGCCTCAACTGCTACAGGAGAATTTAGAAAAGTTGAAGATTGTG
GATGGAGAGGAAGTGGTGAAGTTTCTCCAGGATACTCTGGATGCCCTCTTCAACATCATG
ATGGAGCATTCTCAAAGTGATGAATATGACATCCTCGTCTTTGATGCCTTGATTTACATA
ATAGGACTCATTGCAGACCGGAAATTTCAGCATTTCAACACCGTTCTGGAGGCTTACATC
CAACAGCATTTCAGTGCGACCTTGGCTTACAAGAAATTGATGACAGTGCTGAAGACTTAC
TTGGATACCTCCAGCAGAGGGGAGCAATGTGAGCCAATCCTAAGAACGCTGAAGGCTTTG
GAATATGTGTTCAAGTTCATTGTTCGGTCGAGGACATTATTTTCACAGCTTTATGAAGGC
AAAGAACAGATGGAGTTTGAAGAATCCATGAGACGGCTCTTTGAATCCATCAACAATCTG
ATGAAAAGTCAATACAAAACTACCATCCTTTTGCAGGTGGCGGCTTTGAAATACATCCCA
TCTGTCCTGCATGATGTAGAAATGGTCTTTGATGCGAAGTTACTCAGCCAACTCCTGTAT
GAGTTCTACACCTGCATCCCTCCTGTGAAACTCCAGAAGCAGAAAGTACAGTCTATGAAT
GAGATAGTCCAGAGCAACCTCTTTAAAAAGCAAGAATGCCGGGACATTCTGCTTCCTGTC
ATCACCAAAGAGCTGAAGGAGCTGCTGGAGCAGAAGGATGACATGCAACACCAGGTCCTG
GAGAGGAAGTACTGCGTTGAATTGCTCAACAGCATCTTGGAAGTCCTTAGCTACCAGGAT
GCGGCCTTCACCTACCACCATATCCAGGAGATCATGGTCCAGCTGCTGCGGACAGTGAAC
CGGACAGTCATCACCATGGGCCGGGATCACATTCTGATTAGTCACTTTGTGGCATGTATG
ACAGCCATCTTAAACCAGATGGGTGACCAGCACTACTCCTTCTACATTGAGACCTTCCAG
ACCAGCTCTGAACTTGTGGACTTCTTGATGGAGACCTTCATCATGTTCAAGGACCTCATT
GGAAAGAACGTGTACCCTGGAGACTGGATGGCCATGAGCATGGTTCAAAACAGGGTCTTC
CTGAGAGCTATCAACAAGTTTGCAGAAACCATGAACCAGAAGTTCCTAGAACACACGAAC
TTTGAGTTCCAGCTGTGGAACAACTATTTTCATCTGGCAGTGGCTTTTATCACCCAGGAT
TCTCTGCAGCTGGAGCAGTTCTCACACGCCAAATACAACAAAATCCTGAATAAGTATGGG
GACATGAGACGGCTAATTGGCTTCTCCATCCGTGATATGTGGTACAAGCTTGGTCAGAAC
AAAATCTGCTTCATCCCAGGCATGGTAGGACCTATATTAGAGATGACACTTATCCCTGAG
GCTGAGCTCCGGAAAGCCACCATACCAATCTTCTTCGACATGATGCTGTGTGAATATCAA
AGAAGTGGGGATTTCAAAAAGTTTGAAAACGAAATCATCCTGAAGCTGGACCACGAGGTA
GAAGGGGGCCGAGGCGACGAGCAGTACATGCAGCTCCTGGAGTCAATCCTGATGGAATGT
GCTGCAGAGCACCCAACCATTGCCAAGTCGGTGGAGAACTTCGTGAACCTGGTCAAAGGC
CTCCTGGAGAAGCTGCTGGATTACCGGGGTGTGATGACAGATGAGAGCAAAGACAACCGC
ATGAGCTGCACCGTGAACCTGCTGAATTTCTACAAAGATAACAACAGGGAGGAGATGTAC
ATAAGGTACCTGTACAAACTCCGCGATCTTCACCTGGACTGTGACAATTACACAGAGGCT
GCCTACACGCTCCTTCTCCACACCTGGCTTCTCAAGTGGTCGGATGAGCAGTGTGCATCA
CAGGTCATGCAGACAGGCCAGCAGCACCCCCAGACACACCGGCAGCTGAAGGAGACGCTC
TACGAGACCATCATAGGCTACTTTGACAAAGGAAAGATGTGGGAAGAGGCCATAAGTCTG
TGCAAGGAGCTGGCGGAACAGTACGAGATGGAGATCTTTGACTATGAGCTGCTCAGCCAG
AACCTGATCCAGCAGGCAAAATTCTATGAAAGCATCATGAAAATCCTCAGGCCCAAACCA
GACTACTTTGCTGTTGGATACTACGGCCAGGGATTCCCCTCCTTCCTGCGGAACAAAGTG
TTCATCTACCGCGGGAAGGAATATGAGCGAAGAGAAGATTTCCAGATGCAGCTGATGACC
CAGTTCCCCAATGCAGAGAAGATGAACACCACCTCTGCCCCGGGAGATGATGTGAAGAAT
GCCCCAGGCCAGTATATCCAGTGCTTCACTGTCCAGCCTGTCTTGGATGAACATCCCAGG
TTCAAGAATAAGCCAGTGCCTGACCAGATTATAAACTTCTACAAATCCAACTACGTGCAA
AGGTTCCACTACTCCCGGCCCGTGCGCAGGGGGACCGTAGACCCAGAGAATGAGTTTGCT
TCCATGTGGATTGAGAGAACCTCCTTCGTGACTGCATACAAGCTGCCGGGGATCCTGCGC
TGGTTTGAGGTGGTGCACATGTCGCAGACCACAATTAGTCCTCTGGAGAATGCCATAGAA
ACCATGTCCACGGCCAATGAGAAGATCCTGATGATGATAAACCAGTACCAGAGTGATGAG
ACCCTCCCCATCAACCCACTCTCCATGCTCCTGAACGGGATTGTGGACCCTGCTGTCATG
GGAGGCTTCGCCAAGTATGAGAAGGCCTTCTTCACTGAAGAGTATGTCAGGGACCACCCT
GAGGACCAGGACAAGCTGACCCACCTCAAGGACCTGATTGCATGGCAGATCCCCTTCTTG
GGAGCTGGGATTAAGATCCATGAGAAAAGGGTGTCAGATAACTTGCGACCCTTCCATGAC
CGGATGGAGGAATGTTTCAAGAACCTGAAAATGAAGGTGGAGAAGGAGTACGGTGTCCGA
GAGATGCCTGACTTTGACGACAGGAGAGTGGGCCGTCCCAGGTCTATGCTGCGCTCATAC
AGACAGATGTCCATCATCTCTCTGGCTTCCATGAATTCTGACTGCAGCACCCCCAGCAAG
CCTACCTCAGAGAGCTTTGACCTGGAATTAGCATCACCCAAGACGCCGAGAGTGGAGCAG
GAGGAACCGATCTCCCCGGGGAGCACCCTGCCTGAGGTCAAGCTGCGGAGGTCCAAGAAG
AGGACAAAGAGAAGCAGCGTAGTTTTTGCGGATGAGAAAGCAGCTGCAGAGTCGGACCTG
AAGCGGCTTTCCAGGAAGCATGAGTTCATGAGTGACACCAACCTCTCGGAGCATGCGGCC
ATCCCCCTCAAGGCGTCTGTCCTCTCTCAAATGAGCTTTGCCAGCCAGTCCATGCCTACC
ATCCCAGCCCTGGCGCTCTCAGTGGCAGGCATCCCTGGGTTGGATGAGGCCAACACATCT
CCCCGCCTCAGCCAGACCTTCCTCCAACTCTCAGATGGTGACAAGAAGACACTCACACGG
AAGAAGGTCAATCAGTTCTTCAAGACAATGCTGGCCAGCAAATCGGCTGAAGAAGGCAAA
CAGATCCCAGACTCGCTGTCCACGGACCTGTGA
Enzyme 83 GenBank Gene ID NM_004946.2 Link Image
Enzyme 83 GeneCard ID DOCK2 Link Image
Enzyme 83 GenAtlas ID DOCK2 Link Image
Enzyme 83 HGNC ID HGNC:2988 Link Image
Enzyme 83 Chromosome Location 5
Enzyme 83 Locus 5q35.1
Enzyme 83 SNPs SNPJam Report Link Image
Enzyme 83 General References
  1. Nagase T, Seki N, Ishikawa K, Ohira M, Kawarabayasi Y, Ohara O, Tanaka A, Kotani H, Miyajima N, Nomura N: Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. DNA Res. 1996 Oct 31;3(5):321-9, 341-54. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Nishihara H, Kobayashi S, Hashimoto Y, Ohba F, Mochizuki N, Kurata T, Nagashima K, Matsuda M: Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins. Biochim Biophys Acta. 1999 Nov 11;1452(2):179-87. [PubMed Link Image]
  4. Nishihara H, Maeda M, Oda A, Tsuda M, Sawa H, Nagashima K, Tanaka S: DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell lines. Blood. 2002 Dec 1;100(12):3968-74. Epub 2002 Jun 28. [PubMed Link Image]
  5. Nishihara H, Maeda M, Tsuda M, Makino Y, Sawa H, Nagashima K, Tanaka S: DOCK2 mediates T cell receptor-induced activation of Rac2 and IL-2 transcription. Biochem Biophys Res Commun. 2002 Aug 23;296(3):716-20. [PubMed Link Image]
  6. Cote JF, Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J Cell Sci. 2002 Dec 15;115(Pt 24):4901-13. [PubMed Link Image]
  7. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  8. Carrascal M, Ovelleiro D, Casas V, Gay M, Abian J: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. J Proteome Res. 2008 Dec;7(12):5167-76. [PubMed Link Image]
  9. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  10. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 83 Metabolite References Not Available
Enzyme 84 [top]
Enzyme 84 ID 14066
Enzyme 84 Name Dedicator of cytokinesis protein 3
Enzyme 84 Synonyms
  1. Modifier of cell adhesion
  2. Presenilin-binding protein
  3. PBP
Enzyme 84 Gene Name DOCK3
Enzyme 84 Protein Sequence >Dedicator of cytokinesis protein 3
MWTPTEEEKYGVVICSFRGSVPQGLVLEIGETVQILEKCEGWYRGVSTKKPNVKGIFPAN
YIHLKKAIVSNRGQYETVVPLEDSIVTEVTATLQEWASLWKQLYVKHKVDLFYKLRHVMN
ELIDLRRQLLSGHLTQDQVREVKRHITVRLDWGNEHLGLDLVPRKDFEVVDSDQISVSDL
YKMHLSSRQSVQQSTSQVDTMRPRHGETCRMPVPHHFFLSLKSFTYNTIGEDTDVFFSLY
DMREGKQISERFLVRLNKNGGPRNPEKIERMCALFTDLSSKDMKRDLYIVAHVIRIGRML
LNDSKKGPPHLHYRRPYGCAVLSILDVLQSLTEVKEEKDFVLKVYTCNNESEWSQIHENI
IRKSSAKYSAPSASHGLIISLQLLRGDMEQIRRENPMIFNRGLAITRKLGFPDVIMPGDI
RNDLYLTLEKGDFERGGKSVQKNIEVTMYVLYADGEILKDCISLGSGEPNRSSYHSFVLY
HSNSPRWGEIIKLPIPIDRFRGSHLRFEFRHCSTKDKGEKKLFGFAFSTLMRDDGTTLSD
DIHELYVYKCDENSTFNNHALYLGLPCCKEDYNGCPNIPSSLIFQRSTKESFFISTQLSS
TKLTQNVDLLALLKWKAFPDRIMDVLGRLRHVSGEEIVKFLQDILDTLFVILDDNTEKYG
LLVFQSLVFIINLLRDIKYFHFRPVMDTYIQKHFAGALAYKELIRCLKWYMDCSAELIRQ
DHIQEAMRALEYLFKFIVQSRILYSRATCGMEEEQFRSSIQELFQSIRFVLSLDSRNSET
LLFTQAALLNSFPTIFDELLQMFTVQEVAEFVRGTLGSMPSTVHIGQSMDVVKLQSIART
VDSRLFSFSESRRILLPVVLHHIHLHLRQQKELLICSGILGSIFSIVKTSSLEADVMEEV
EMMVESLLDVLLQTLLTIMSKSHAQEAVRGQRCPQCTAEITGEYVSCLLSLLRQMCDTHF
QHLLDNFQSKDELKEFLLKIFCVFRNLMKMSVFPRDWMVMRLLTSNIIVTTVQYLSSALH
KNFTETDFDFKVWNSYFSLAVLFINQPSLQLEIITSAKRKKILDKYGDMRVMMAYELFSM
WQNLGEHKIHFIPGMIGPFLGVTLVPQPEVRNIMIPIFHDMMDWEQRKNGNFKQVEAELI
DKLDSMVSEGKGDESYRELFSLLTQLFGPYPSLLEKVEQETWRETGISFVTSVTRLMERL
LDYRDCMKGEETENKKIGCTVNLMNFYKSEINKEEMYIRYIHKLCDMHLQAENYTEAAFT
LLLYCELLQWEDRPLREFLHYPSQTEWQRKEGLCRKIIHYFNKGKSWEFGIPLCRELACQ
YESLYDYQSLSWIRKMEASYYDNIMEQQRLEPEFFRVGFYGRKFPFFLRNKEYVCRGHDY
ERLEAFQQRMLSEFPQAVAMQHPNHPDDAILQCDAQYLQIYAVTPIPDYVDVLQMDRVPD
RVKSFYRVNNVRKFRYDRPFHKGPKDKENEFKSLWIERTTLTLTHSLPGISRWFEVERRE
LVEVSPLENAIQVVENKNQELRSLISQYQHKQVHGNINLLSMCLNGVIDAAVNGGIARYQ
EAFFDKDYINKHPGDAEKITQLKELMQEQVHVLGVGLAVHEKFVHPEMRPLHKKLIDQFQ
MMRASLYHEFPGLDKLSPACSGTSTPRGNVLASHSPMSPESIKMTHRHSPMNLMGTGRHS
SSSLSSHASSEAGNMVMLGDGSMGDAPEDLYHHMQLAYPNPRYQGSVTNVSVLSSSQASP
SSSSLSSTHSAPSQMITSAPSSARGSPSLPDKYRHAREMMLLLPTYRDRPSSAMYPAAIL
ENGQPPNFQRALFQQVVGACKPCSDPNLSVAEKGHYSLHFDAFHHPLGDTPPALPARTLR
KSPLHPIPASPTSPQSGLDGSNSTLSGSASSGVSSLSESNFGHSSEAPPRTDTMDSMPSQ
AWNADEDLEPPYLPVHYSLSESAVLDSIKAQPCRSHSAPGCVIPQDPMDPPALPPKPYHP
RLPALEHDEGVLLREETERPRGLHRKAPLPPGSAKEEQARMAWEHGRGEQ
Enzyme 84 Number of Residues 2030
Enzyme 84 Molecular Weight 233101.1
Enzyme 84 Theoretical pI 6.97
Enzyme 84 GO Classification
Function
  • GTP binding
  • GTPase binding
  • GTPase regulator activity
  • binding
  • enzyme binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
Process
Component
Enzyme 84 General Function Involved in guanyl-nucleotide exchange factor activity
Enzyme 84 Specific Function Potential guanine nucleotide exchange factor (GEF). GEF proteins activate some small GTPases by exchanging bound GDP for free GTP. Its interaction with presenilin proteins as well as its ability to stimulate Tau/MAPT phosphorylation suggest that it may be involved in Alzheimer disease. Ectopic expression in nerve cells decreases the secretion of beta-amyloid APBA1 protein and lowers the rate of cell-substratum adhesion, suggesting that it may affect the function of some small GTPase involved in the regulation of actin cytoskeleton or cell adhesion receptors
Enzyme 84 Pathways Not Available
Enzyme 84 Reactions Not Available
Enzyme 84 Pfam Domain Function
Enzyme 84 Signals
  • None
Enzyme 84 Transmembrane Regions
  • None
Enzyme 84 Essentiality Not Available
Enzyme 84 GenBank ID Protein 31415870 Link Image
Enzyme 84 UniProtKB/Swiss-Prot ID Q8IZD9 Link Image
Enzyme 84 UniProtKB/Swiss-Prot Entry Name DOCK3_HUMAN Link Image
Enzyme 84 PDB ID Not Available
Enzyme 84 Cellular Location Not Available
Enzyme 84 Gene Sequence >6093 bp
ATGTGGACCCCCACGGAGGAGGAGAAATACGGCGTAGTGATATGCAGCTTTCGAGGATCT
GTCCCTCAAGGGTTGGTCTTAGAAATAGGAGAAACAGTCCAGATTCTTGAAAAATGTGAA
GGTTGGTACAGAGGAGTTTCAACAAAGAAGCCAAATGTGAAGGGGATCTTTCCTGCAAAT
TACATTCACTTGAAAAAGGCAATTGTCAGTAATAGGGGGCAGTATGAAACTGTGGTTCCA
CTTGAAGATTCTATTGTGACTGAGGTTACAGCAACTCTACAAGAATGGGCAAGTTTGTGG
AAACAGTTGTATGTGAAACACAAAGTAGATCTTTTCTACAAACTACGCCATGTGATGAAT
GAACTTATTGACCTGCGAAGGCAGCTACTGTCTGGTCACCTGACTCAGGATCAGGTGCGG
GAGGTTAAGCGGCACATCACCGTGCGCCTGGACTGGGGTAATGAACATTTGGGCCTGGAC
CTGGTGCCTCGGAAGGACTTTGAAGTAGTGGACTCGGACCAGATTAGTGTCTCAGATCTC
TATAAGATGCATTTATCTAGCCGGCAGAGTGTACAGCAAAGCACATCCCAGGTAGATACA
ATGCGCCCACGTCATGGGGAAACATGTCGGATGCCAGTGCCACATCACTTCTTCCTCAGC
CTGAAGAGTTTCACTTACAATACTATTGGGGAAGATACCGATGTCTTCTTTTCCTTATAT
GACATGAGGGAAGGCAAGCAGATCAGTGAGCGGTTTCTGGTAAGACTGAACAAGAATGGT
GGGCCGAGGAACCCAGAGAAGATAGAACGAATGTGTGCCCTTTTTACAGATCTGAGCAGC
AAAGATATGAAGAGAGATTTGTATATCGTTGCCCATGTGATCCGAATAGGCCGGATGCTC
CTGAACGACTCAAAGAAAGGTCCTCCTCACCTGCACTACAGGCGACCATATGGCTGTGCG
GTCCTAAGCATCTTGGATGTCCTACAGTCACTCACAGAAGTAAAGGAAGAAAAGGATTTT
GTTCTTAAGGTTTACACGTGCAACAACGAGAGTGAGTGGTCCCAGATCCACGAGAACATC
ATCCGAAAGTCCAGTGCCAAGTACTCTGCCCCCAGCGCCAGCCATGGTCTTATCATTTCT
CTGCAGCTTCTTCGTGGAGACATGGAACAGATTCGGAGAGAAAATCCCATGATATTTAAT
AGGGGATTGGCAATTACAAGAAAATTGGGATTTCCTGATGTCATTATGCCAGGTGATATC
CGCAATGACCTGTACCTAACCCTGGAGAAGGGGGATTTCGAGAGAGGAGGAAAGAGTGTA
CAAAAGAATATTGAAGTGACCATGTATGTGCTTTATGCAGATGGAGAAATCTTGAAGGAT
TGCATCAGCTTGGGTTCAGGAGAGCCAAATAGGAGTTCCTACCACTCCTTTGTCCTCTAC
CACAGTAATAGTCCTCGCTGGGGAGAAATTATCAAATTGCCTATCCCCATTGACCGGTTC
CGGGGCTCCCACCTGCGCTTTGAGTTCAGACATTGTTCCACAAAGGACAAAGGGGAAAAG
AAACTCTTTGGCTTTGCATTCTCAACCCTGATGCGTGATGATGGCACCACCCTCTCAGAT
GATATTCACGAGCTTTATGTGTACAAGTGTGATGAGAATAGCACGTTTAATAACCATGCT
CTGTACCTGGGCCTGCCCTGCTGCAAAGAGGACTACAATGGCTGCCCTAATATTCCTTCT
AGCCTCATCTTCCAGCGCAGCACCAAAGAGTCTTTCTTCATCTCCACTCAGCTCTCCTCT
ACCAAACTCACCCAGAATGTGGACCTCCTAGCTCTGCTGAAGTGGAAAGCCTTCCCCGAC
CGGATCATGGATGTACTAGGGCGGCTGCGGCATGTCAGTGGGGAGGAAATTGTTAAGTTT
CTGCAGGACATCTTAGATACACTCTTTGTGATTTTGGATGATAATACAGAGAAGTACGGC
CTGTTGGTTTTTCAGTCTCTGGTGTTCATCATCAACCTGCTCCGAGACATCAAGTATTTT
CACTTTCGACCTGTGATGGACACGTATATCCAGAAGCACTTTGCTGGAGCTCTGGCATAC
AAGGAGCTCATCCGCTGTTTGAAGTGGTATATGGACTGCTCAGCAGAACTGATTCGACAG
GACCACATTCAAGAAGCTATGCGGGCCTTGGAGTACCTTTTCAAGTTCATTGTACAGTCA
CGGATCCTGTACTCACGAGCCACTTGTGGAATGGAAGAGGAACAATTCAGATCCAGTATC
CAAGAACTTTTCCAGTCCATCCGGTTTGTGCTCAGTCTGGACAGCCGAAACTCAGAAACA
CTCCTTTTTACTCAGGCTGCACTCCTCAATTCTTTCCCAACCATCTTTGATGAGCTTCTG
CAAATGTTCACCGTGCAAGAGGTGGCAGAGTTTGTGAGAGGGACACTGGGGAGCATGCCC
AGCACTGTGCACATTGGGCAGTCAATGGACGTGGTCAAGCTGCAGTCCATTGCCAGGACA
GTGGATAGCCGCCTGTTTTCTTTCTCAGAATCCCGCCGCATCCTGCTTCCTGTGGTTCTC
CATCACATTCACCTTCACCTGAGGCAGCAGAAAGAGCTGCTAATTTGCTCAGGGATTCTT
GGCAGCATCTTCTCCATCGTCAAGACCAGCTCTCTGGAGGCAGATGTCATGGAGGAAGTA
GAGATGATGGTGGAGAGCCTCCTGGACGTGCTCTTGCAGACTCTGCTCACCATCATGAGC
AAATCGCACGCTCAGGAGGCGGTAAGAGGGCAGCGGTGCCCGCAGTGCACAGCCGAGATC
ACTGGCGAGTATGTGTCCTGCCTTCTCTCACTGCTCCGCCAGATGTGTGACACCCATTTC
CAGCACCTCCTGGACAACTTCCAGAGCAAAGATGAACTCAAGGAATTTCTGCTGAAGATT
TTTTGCGTGTTCCGGAACCTGATGAAGATGAGTGTCTTCCCTCGGGACTGGATGGTAATG
AGACTGCTCACAAGCAATATTATAGTCACTACTGTCCAGTACCTGTCCTCTGCACTGCAC
AAGAATTTCACAGAGACTGACTTTGACTTTAAGGTGTGGAATTCTTACTTTAGCCTGGCA
GTTCTATTCATAAATCAGCCAAGCCTTCAGCTAGAAATTATCACCTCAGCCAAAAGGAAG
AAGATTCTAGATAAGTATGGGGACATGCGTGTAATGATGGCCTATGAACTGTTCAGCATG
TGGCAGAATTTGGGTGAACATAAGATCCACTTTATTCCGGGAATGATTGGTCCTTTTCTG
GGTGTGACACTGGTCCCACAGCCAGAAGTACGGAATATCATGATTCCCATCTTTCATGAC
ATGATGGACTGGGAGCAGAGAAAAAATGGCAACTTCAAACAGGTGGAGGCCGAGTTGATT
GACAAGCTGGACAGCATGGTGTCAGAAGGGAAAGGTGACGAGAGCTACAGGGAGCTCTTC
AGCCTACTAACCCAGCTGTTTGGGCCCTACCCCAGCCTGCTGGAGAAGGTTGAACAAGAA
ACATGGCGCGAGACCGGCATTTCCTTTGTGACCTCAGTCACCCGCCTCATGGAACGTCTT
CTTGACTACAGGGACTGCATGAAAGGAGAGGAAACAGAGAATAAGAAGATAGGCTGCACT
GTTAACCTGATGAATTTTTACAAATCTGAGATTAACAAGGAAGAAATGTATATCCGCTAC
ATCCATAAGCTTTGTGACATGCACTTGCAGGCCGAAAACTACACAGAGGCCGCATTTACC
CTGCTCCTTTACTGTGAGCTGCTGCAGTGGGAGGACCGGCCACTACGGGAATTCCTCCAC
TACCCATCGCAGACAGAGTGGCAGCGGAAGGAGGGACTGTGCCGGAAGATCATTCACTAC
TTCAACAAAGGCAAGAGCTGGGAGTTTGGGATCCCACTGTGCAGGGAGCTGGCGTGTCAG
TACGAGAGCCTCTATGATTACCAGAGCCTCAGCTGGATTCGGAAAATGGAGGCCAGCTAC
TATGACAACATTATGGAGCAGCAACGCCTGGAGCCTGAGTTCTTTCGGGTCGGCTTCTAT
GGCAGGAAGTTTCCTTTCTTTCTTCGGAACAAAGAATACGTGTGCCGTGGCCATGACTAC
GAGAGGCTGGAGGCCTTCCAGCAGAGGATGCTCAGTGAGTTTCCGCAGGCTGTCGCCATG
CAGCACCCCAACCATCCTGATGACGCCATCCTACAGTGCGATGCCCAGTACTTGCAGATC
TATGCAGTGACGCCCATTCCAGATTATGTGGATGTTCTGCAGATGGATAGGGTACCAGAT
CGAGTCAAGAGCTTCTATCGCGTCAACAATGTGAGGAAGTTCCGGTATGACAGGCCTTTT
CACAAAGGCCCCAAGGACAAGGAGAATGAATTCAAGAGCCTGTGGATTGAACGTACCACA
CTGACCCTGACCCACAGCTTGCCTGGCATCTCTCGGTGGTTTGAAGTGGAGAGGAGGGAA
CTGGTGGAGGTGAGCCCTCTGGAGAATGCCATCCAAGTGGTTGAGAATAAGAACCAGGAG
CTACGCTCCCTGATCAGCCAGTATCAACACAAGCAGGTGCATGGCAACATTAACCTGCTA
AGCATGTGCCTGAATGGTGTCATTGATGCAGCTGTCAATGGAGGCATTGCACGCTATCAG
GAGGCCTTCTTTGATAAAGATTACATCAACAAGCACCCAGGAGATGCTGAGAAGATCACC
CAGCTCAAGGAGCTTATGCAGGAGCAGGTTCATGTCCTTGGAGTTGGGCTAGCAGTTCAT
GAGAAGTTTGTGCACCCAGAAATGCGGCCTCTGCATAAGAAGCTAATTGATCAGTTCCAG
ATGATGCGGGCCAGTCTCTACCATGAGTTTCCAGGTTTGGATAAGCTAAGTCCTGCATGT
TCAGGCACCAGCACCCCACGGGGAAATGTTCTGGCATCCCATAGCCCCATGAGTCCGGAG
AGCATCAAGATGACCCACCGGCACAGCCCCATGAACTTGATGGGCACAGGCCGCCATTCA
TCATCCTCTCTCTCCTCACATGCGTCTAGTGAAGCAGGAAACATGGTGATGCTGGGTGAC
GGCTCCATGGGTGATGCTCCTGAGGACCTGTACCACCACATGCAGCTCGCGTATCCCAAC
CCCAGGTACCAAGGCTCAGTCACCAACGTCTCTGTTCTGTCCTCGTCCCAGGCAAGCCCT
TCTTCCTCCAGCCTGAGTTCCACTCACTCAGCACCATCCCAGATGATTACCTCTGCCCCT
TCCAGTGCCCGAGGCTCTCCCTCTCTGCCAGATAAGTACCGCCATGCCCGTGAAATGATG
TTGTTGCTGCCCACATACCGGGACCGCCCAAGCAGTGCCATGTATCCAGCAGCCATCCTG
GAGAACGGACAGCCGCCGAATTTCCAGCGAGCCCTGTTCCAGCAAGTGGTCGGAGCCTGC
AAACCCTGCAGTGATCCCAATCTGTCTGTGGCTGAAAAAGGTCATTACTCCCTACACTTT
GACGCCTTCCACCACCCTCTGGGTGATACCCCCCCAGCCCTCCCTGCCCGGACCCTGCGC
AAGTCTCCTCTCCACCCTATCCCAGCCTCCCCCACAAGCCCCCAGTCAGGTCTGGACGGC
AGCAACTCTACGCTGTCCGGCAGTGCCAGCAGCGGCGTGTCCTCCTTGAGTGAGAGTAAC
TTTGGGCACTCCTCGGAGGCCCCACCTCGCACTGACACCATGGACTCCATGCCAAGTCAG
GCCTGGAATGCTGACGAAGATCTTGAGCCACCCTACCTCCCTGTCCACTACAGCCTCTCT
GAGTCTGCCGTCCTGGACTCCATCAAGGCCCAGCCATGCCGAAGCCACTCAGCCCCAGGG
TGCGTCATCCCTCAGGACCCCATGGACCCGCCTGCGCTGCCGCCCAAGCCCTACCACCCC
CGCCTGCCGGCCCTGGAGCACGATGAGGGGGTGCTGCTGCGTGAAGAGACTGAGAGGCCT
CGAGGCCTGCACCGCAAGGCTCCATTGCCTCCTGGGAGCGCTAAGGAGGAGCAGGCCCGC
ATGGCCTGGGAGCACGGCCGAGGGGAGCAGTGA
Enzyme 84 GenBank Gene ID NM_004947.4 Link Image
Enzyme 84 GeneCard ID DOCK3 Link Image
Enzyme 84 GenAtlas ID DOCK3 Link Image
Enzyme 84 HGNC ID HGNC:2989 Link Image
Enzyme 84 Chromosome Location 3
Enzyme 84 Locus 3p21.2
Enzyme 84 SNPs SNPJam Report Link Image
Enzyme 84 General References
  1. Kashiwa A, Yoshida H, Lee S, Paladino T, Liu Y, Chen Q, Dargusch R, Schubert D, Kimura H: Isolation and characterization of novel presenilin binding protein. J Neurochem. 2000 Jul;75(1):109-16. [PubMed Link Image]
  2. de Silva MG, Elliott K, Dahl HH, Fitzpatrick E, Wilcox S, Delatycki M, Williamson R, Efron D, Lynch M, Forrest S: Disruption of a novel member of a sodium/hydrogen exchanger family and DOCK3 is associated with an attention deficit hyperactivity disorder-like phenotype. J Med Genet. 2003 Oct;40(10):733-40. [PubMed Link Image]
  3. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
  4. Chen Q, Yoshida H, Schubert D, Maher P, Mallory M, Masliah E: Presenilin binding protein is associated with neurofibrillary alterations in Alzheimer's disease and stimulates tau phosphorylation. Am J Pathol. 2001 Nov;159(5):1597-602. [PubMed Link Image]
  5. Cote JF, Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J Cell Sci. 2002 Dec 15;115(Pt 24):4901-13. [PubMed Link Image]
Enzyme 84 Metabolite References Not Available
Enzyme 85 [top]
Enzyme 85 ID 14067
Enzyme 85 Name Dedicator of cytokinesis protein 4
Enzyme 85 Synonyms Not Available
Enzyme 85 Gene Name DOCK4
Enzyme 85 Protein Sequence >Dedicator of cytokinesis protein 4
MWIPTEHEKYGVVIASFRGTVPYGLSLEIGDTVQILEKCDGWYRGFALKNPNIKGIFPSS
YVHLKNACVKNKGQFEMVIPTEDSVITEMTSTLRDWGTMWKQLYVRNEGDLFHRLWHIMN
EILDLRRQVLVGHLTHDRMKDVKRHITARLDWGNEQLGLDLVPRKEYAMVDPEDISITEL
YRLMEHRHRKKDTPVQASSHHLFVQMKSLMCSNLGEELEVIFSLFDSKENRPISERFFLR
LNRNGLPKAPDKPERHCSLFVDLGSSELRKDIYITVHIIRIGRMGAGEKKNACSVQYRRP
FGCAVLSIADLLTGETKDDLILKVYMCNTESEWYQIHENIIKKLNARYNLTGSNAGLAVS
LQLLHGDIEQIRREYSSVFSHGVSITRKLGFSNIIMPGEMRNDLYITIERGEFEKGGKSV
ARNVEVTMFIVDSSGQTLKDFISFGSGEPPASEYHSFVLYHNNSPRWSELLKLPIPVDKF
RGAHIRFEFRHCSTKEKGEKKLFGFSFVPLMQEDGRTLPDGTHELIVHKCEENTNLQDTT
RYLKLPFSKGIFLGNNNQAMKATKESFCITSFLCSTKLTQNGDMLDLLKWRTHPDKITGC
LSKLKEIDGSEIVKFLQDTLDTLFGILDENSQKYGSKVFDSLVHIINLLQDSKFHHFKPV
MDTYIESHFAGALAYRDLIKVLKWYVDRITEAERQEHIQEVLKAQEYIFKYIVQSRRLFS
LATGGQNEEEFRCCIQELLMSVRFFLSQESKGSGALSQSQAVFLSSFPAVYSELLKLFDV
REVANLVQDTLGSLPTILHVDDSLQAIKLQCIGKTVESQLYTNPDSRYILLPVVLHHLHI
HLQEQKDLIMCARILSNVFCLIKKNSSEKSVLEEIDVIVASLLDILLRTILEITSRPQPS
SSAMRFQFQDVTGEFVACLLSLLRQMTDRHYQQLLDSFNTKEELRDFLLQIFTVFRILIR
PEMFPKDWTVMRLVANNVIITTVLYLSDALRKNFLNENFDYKIWDSYFYLAVIFINQLCL
QLEMFTPSKKKKVLEKYGDMRVTMGCEIFSMWQNLGEHKLHFIPALIGPFLEVTLIPQPD
LRNVMIPIFHDMMDWEQRRSGNFKQVEAKLIDKLDSLMSEGKGDETYRELFNSILLKKIE
RETWRESGVSLIATVTRLMERLLDYRDCMKMGEVDGKKIGCTVSLLNFYKTELNKEEMYI
RYIHKLYDLHLKAQNFTEAAYTLLLYDELLEWSDRPLREFLTYPMQTEWQRKEHLHLTII
QNFDRGKCWENGIILCRKIAEQYESYYDYRNLSKMRMMEASLYDKIMDQQRLEPEFFRVG
FYGKKFPFFLRNKEFVCRGHDYERLEAFQQRMLNEFPHAIAMQHANQPDETIFQAEAQYL
QIYAVTPIPESQEVLQREGVPDNIKSFYKVNHIWKFRYDRPFHKGTKDKENEFKSLWVER
TSLYLVQSLPGISRWFEVEKREVVEMSPLENAIEVLENKNQQLKTLISQCQTRQMQNINP
LTMCLNGVIDAAVNGGVSRYQEAFFVKEYILSHPEDGEKIARLRELMLEQAQILEFGLAV
HEKFVPQDMRPLHKKLVDQFFVMKSSLGIQEFSACMQASPVHFPNGSPRVCRNSAPASVS
PDGTRVIPRRSPLSYPAVNRYSSSSLSSQASAEVSNITGQSESSDEVFNMQPSPSTSSLS
STHSASPNVTSSAPSSARASPLLSDKHKHSRENSCLSPRERPCSAIYPTPVEPSQRMLFN
HIGDGALPRSDPNLSAPEKAVNPTPSSWSLDSGKEAKNMSDSGKLISPPVPPRPTQTASP
ARHTTSVSPSPAGRSPLKGSVQSFTPSPVEYHSPGLISNSPVLSGSYSSGISSLSRCSTS
ETSGFENQVNEQSAPLPVPVPVPVPSYGGEEPVRKESKTPPPYSVYERTLRRPVPLPHSL
SIPVTSEPPALPPKPLAARSSHLENGARRTDPGPRPRPLPRKVSQL
Enzyme 85 Number of Residues 1966
Enzyme 85 Molecular Weight 225204.3
Enzyme 85 Theoretical pI 7.68
Enzyme 85 GO Classification
Function
  • GTP binding
  • GTPase binding
  • GTPase regulator activity
  • binding
  • enzyme binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
Process
Component
Enzyme 85 General Function Involved in guanyl-nucleotide exchange factor activity
Enzyme 85 Specific Function Involved in regulation of adherens junction between cells. Functions as a guanine nucleotide exchange factor (GEF), which activates Rap1 small GTPase by exchanging bound GDP for free GTP
Enzyme 85 Pathways Not Available
Enzyme 85 Reactions Not Available
Enzyme 85 Pfam Domain Function
Enzyme 85 Signals
  • None
Enzyme 85 Transmembrane Regions
  • None
Enzyme 85 Essentiality Not Available
Enzyme 85 GenBank ID Protein 92091572 Link Image
Enzyme 85 UniProtKB/Swiss-Prot ID Q8N1I0 Link Image
Enzyme 85 UniProtKB/Swiss-Prot Entry Name DOCK4_HUMAN Link Image
Enzyme 85 PDB ID Not Available
Enzyme 85 Cellular Location Not Available
Enzyme 85 Gene Sequence >5901 bp
ATGTGGATACCTACGGAGCACGAGAAATACGGCGTGGTTATTGCCAGTTTCCGAGGAACC
GTTCCATATGGCCTGTCATTGGAAATTGGAGATACAGTTCAGATCCTGGAGAAGTGTGAT
GGCTGGTACAGAGGATTTGCCTTAAAAAACCCAAATATCAAGGGTATATTTCCTTCCAGC
TACGTTCACTTGAAAAATGCCTGTGTAAAGAACAAAGGACAATTTGAAATGGTTATTCCC
ACTGAAGACTCTGTTATCACAGAAATGACATCAACATTAAGAGACTGGGGAACCATGTGG
AAACAACTCTATGTGCGTAATGAAGGCGATCTCTTCCACCGGCTGTGGCACATCATGAAT
GAAATCCTGGACCTGAGGCGGCAGGTGCTGGTGGGCCACCTCACCCACGACCGGATGAAG
GACGTGAAGCGCCACATTACTGCCCGGCTTGACTGGGGCAATGAACAACTGGGACTGGAC
CTGGTGCCTAGGAAAGAGTACGCAATGGTGGATCCGGAAGACATCAGCATTACTGAGCTC
TACCGATTGATGGAACATCGACATCGGAAGAAAGACACCCCGGTGCAGGCCAGCAGTCAC
CACCTCTTTGTCCAGATGAAGAGCCTCATGTGTTCCAACCTGGGAGAGGAGCTGGAGGTC
ATCTTCTCACTCTTTGACAGTAAAGAGAACCGGCCAATCAGTGAGAGATTTTTCTTGAGG
CTGAATAGAAACGGGCTTCCCAAAGCCCCTGATAAACCGGAACGACATTGCTCCCTCTTT
GTGGATTTGGGCAGCAGTGAGCTAAGAAAGGACATTTATATCACCGTGCACATTATCCGA
ATCGGTCGAATGGGAGCAGGAGAAAAAAAGAATGCCTGTAGTGTCCAGTACCGACGACCC
TTTGGCTGTGCAGTTCTTAGCATCGCTGACCTGCTAACAGGAGAGACAAAGGATGACCTC
ATTCTGAAAGTATACATGTGTAACACAGAGAGTGAGTGGTACCAAATCCATGAGAACATC
ATCAAAAAGCTGAATGCACGTTATAACTTGACTGGCTCCAATGCAGGTTTAGCAGTTTCC
TTACAGCTATTGCACGGAGACATTGAACAAATCAGAAGGGAATATTCATCAGTATTTTCT
CATGGAGTATCCATAACAAGGAAGCTGGGATTTTCAAATATTATTATGCCTGGTGAAATG
AGGAATGATTTATATATCACTATTGAAAGGGGAGAATTTGAGAAAGGAGGGAAGAGCGTG
GCCAGAAATGTGGAAGTTACGATGTTCATTGTAGACAGTAGTGGCCAAACCCTGAAGGAT
TTTATCTCCTTCGGCTCTGGGGAGCCACCAGCCAGTGAGTACCACTCCTTTGTGCTTTAC
CATAACAACAGTCCCAGGTGGTCTGAACTGCTGAAACTTCCCATTCCTGTGGATAAATTC
CGGGGTGCACACATCCGCTTCGAGTTTCGGCATTGTTCCACAAAGGAGAAAGGAGAGAAG
AAGTTGTTTGGGTTTTCTTTTGTCCCTCTGATGCAAGAAGATGGTAGGACTCTTCCAGAT
GGCACTCATGAGCTCATCGTGCATAAGTGTGAAGAAAACACAAATCTTCAGGATACTACC
CGCTACCTCAAACTTCCCTTTTCCAAGGGCATTTTCCTTGGGAATAATAATCAAGCCATG
AAGGCCACAAAGGAGTCCTTTTGTATTACATCTTTTCTCTGTTCCACAAAACTCACACAA
AATGGTGATATGCTTGATCTTTTGAAATGGAGAACCCACCCAGACAAGATCACTGGCTGT
CTCTCTAAATTAAAAGAAATTGATGGCTCAGAGATAGTAAAGTTTCTGCAGGATACACTG
GATACCTTATTTGGAATTTTAGATGAAAATTCCCAAAAATATGGGTCTAAAGTGTTTGAT
TCTTTGGTTCACATAATAAATTTGCTGCAAGATAGCAAATTTCATCATTTTAAACCTGTA
ATGGACACTTACATTGAGAGTCATTTTGCTGGGGCACTTGCATACAGAGATCTCATCAAA
GTGCTCAAATGGTACGTGGACCGGATCACAGAAGCAGAGCGGCAAGAGCATATCCAGGAG
GTGCTGAAGGCACAAGAATACATTTTTAAGTATATAGTTCAATCTCGAAGGCTGTTTTCC
CTTGCCACTGGTGGGCAAAACGAAGAGGAGTTCCGCTGCTGCATTCAGGAGCTTCTCATG
TCAGTCCGTTTCTTTCTTTCGCAAGAGAGCAAAGGGTCTGGAGCATTATCTCAGTCACAG
GCTGTGTTTCTGAGCTCTTTCCCTGCCGTGTACTCAGAACTGTTGAAGCTCTTTGATGTC
CGGGAAGTAGCCAACTTGGTCCAGGACACCCTGGGCAGTCTGCCGACCATCCTGCATGTG
GATGATTCCCTGCAGGCCATCAAACTGCAGTGCATTGGCAAAACCGTGGAAAGCCAGCTT
TATACCAACCCAGATTCCCGATACATTCTTCTGCCTGTCGTGTTACATCACCTCCACATT
CACTTGCAAGAACAGAAGGACCTGATCATGTGTGCACGTATCCTTAGCAACGTATTTTGT
CTTATCAAGAAAAATAGCTCAGAAAAATCTGTGCTGGAGGAAATAGATGTGATAGTGGCC
AGCTTGCTGGATATTCTGCTGAGGACCATATTGGAGATCACCAGCCGACCTCAGCCATCC
AGCTCAGCAATGCGGTTCCAGTTCCAGGATGTCACTGGGGAGTTTGTTGCTTGTCTCCTG
TCCCTATTACGACAAATGACAGATAGACATTATCAACAGCTTCTTGATAGTTTTAATACA
AAGGAAGAACTAAGGGATTTCCTGCTGCAGATATTTACTGTGTTCCGAATATTGATACGC
CCGGAGATGTTTCCAAAGGACTGGACTGTTATGCGCTTGGTTGCTAACAATGTTATTATT
ACAACAGTTCTATACCTCTCAGATGCACTTCGTAAGAACTTCTTAAATGAAAACTTTGAT
TATAAGATCTGGGATTCCTACTTTTACCTCGCAGTCATTTTTATAAACCAGTTGTGTCTG
CAGTTGGAGATGTTCACACCTTCCAAGAAGAAAAAGGTGTTAGAAAAGTATGGTGACATG
CGGGTAACAATGGGTTGTGAAATTTTCAGCATGTGGCAAAACCTAGGAGAGCACAAGCTT
CATTTTATCCCTGCCCTGATTGGCCCCTTCCTAGAAGTGACCTTGATACCCCAGCCAGAT
CTTCGGAATGTCATGATTCCAATTTTTCATGATATGATGGACTGGGAGCAGAGGCGGAGT
GGCAACTTTAAACAGGTGGAAGCCAAGCTAATTGACAAACTGGATAGCCTGATGTCAGAA
GGCAAAGGTGACGAAACATACCGCGAGCTCTTCAACAGTATTCTACTAAAGAAAATTGAG
CGGGAAACATGGCGGGAAAGTGGCGTTTCATTAATTGCTACTGTAACTCGTCTAATGGAG
AGGTTGTTAGATTACAGGGACTGCATGAAAATGGGAGAGGTAGATGGCAAAAAGATTGGC
TGCACAGTTAGCCTTCTGAACTTCTATAAGACTGAACTGAACAAGGAGGAGATGTATATA
CGCTACATTCACAAACTCTATGATCTGCATCTCAAAGCACAGAACTTTACAGAAGCTGCA
TATACCCTCCTCTTATATGACGAGCTACTGGAATGGTCTGATCGGCCCCTCAGGGAGTTC
CTGACCTACCCCATGCAAACAGAATGGCAGCGCAAAGAGCACCTGCACCTCACCATCATC
CAGAACTTTGACAGAGGCAAATGTTGGGAGAATGGCATTATCTTGTGCCGGAAGATTGCA
GAGCAGTATGAGAGTTATTATGACTACAGAAACCTGAGCAAGATGCGGATGATGGAAGCC
TCTTTGTATGACAAAATTATGGACCAGCAACGTCTTGAACCAGAGTTCTTCAGAGTTGGA
TTTTATGGAAAAAAATTTCCATTTTTCTTAAGAAATAAGGAGTTTGTGTGTCGAGGGCAT
GACTACGAGAGGCTGGAAGCCTTCCAACAGAGAATGCTGAACGAGTTCCCCCATGCCATC
GCCATGCAGCACGCCAACCAGCCCGATGAGACCATCTTCCAGGCAGAAGCTCAGTATTTG
CAGATATATGCTGTGACTCCCATTCCAGAGAGCCAGGAGGTCCTGCAGAGAGAGGGTGTT
CCGGACAACATCAAAAGCTTCTATAAAGTGAATCACATCTGGAAATTCCGCTATGACCGA
CCATTTCACAAAGGCACAAAAGATAAAGAGAATGAATTCAAGAGTCTCTGGGTGGAGAGA
ACGTCATTATACTTGGTGCAGAGTTTGCCTGGCATCTCTCGCTGGTTTGAAGTGGAAAAG
CGTGAAGTGGTAGAAATGAGTCCTCTGGAAAATGCAATTGAAGTGCTAGAAAATAAGAAT
CAGCAGCTGAAGACTCTGATTAGTCAGTGTCAGACAAGACAGATGCAGAATATTAATCCC
CTGACTATGTGCCTGAATGGAGTTATAGATGCTGCAGTTAATGGTGGCGTTTCCAGGTAT
CAAGAGGCATTCTTTGTCAAAGAATATATCTTAAGTCACCCTGAAGATGGGGAGAAAATT
GCACGATTAAGAGAGCTGATGCTTGAGCAGGCACAGATTCTGGAATTTGGTTTGGCCGTG
CATGAGAAGTTTGTACCTCAAGATATGAGACCCCTTCACAAAAAGCTGGTTGACCAATTC
TTTGTGATGAAGTCGAGCTTAGGGATACAGGAGTTCTCTGCTTGTATGCAAGCCAGTCCT
GTCCATTTTCCTAATGGAAGCCCTCGTGTGTGTAGAAACTCAGCACCTGCTTCTGTGAGC
CCAGATGGTACCAGGGTAATTCCTAGACGCAGCCCGTTAAGTTACCCAGCTGTCAACCGA
TATTCTTCCTCCTCACTGTCCTCACAAGCTTCTGCTGAAGTAAGCAATATTACAGGGCAA
TCAGAAAGCTCTGATGAAGTCTTTAACATGCAGCCAAGTCCATCTACCTCAAGCTTGAGT
TCTACTCACTCGGCTTCACCTAATGTGACAAGTTCTGCTCCATCGAGTGCCAGAGCTTCT
CCTTTGTTGTCTGACAAACACAAACATTCCCGAGAAAACTCTTGCCTGTCACCAAGAGAG
AGACCATGCAGTGCCATCTATCCAACACCTGTGGAGCCTTCGCAGAGGATGCTGTTTAAT
CATATTGGAGACGGGGCCTTGCCACGCAGTGACCCAAATCTCTCTGCACCTGAAAAAGCT
GTGAACCCCACCCCTAGCAGCTGGAGCCTGGACAGTGGGAAGGAAGCCAAGAACATGTCG
GATAGTGGGAAACTTATCTCTCCCCCTGTCCCTCCAAGACCCACACAGACTGCTTCACCA
GCAAGACACACGACATCAGTATCCCCCTCGCCTGCCGGGCGATCTCCATTGAAGGGCTCT
GTGCAGTCTTTCACCCCCTCTCCAGTGGAGTACCACTCGCCAGGACTCATCTCCAACTCC
CCTGTCTTGTCGGGCAGCTACAGCAGTGGGATTTCTTCTCTCAGCCGGTGCAGCACGTCG
GAAACCTCAGGCTTTGAAAATCAGGTGAATGAACAGTCGGCCCCCCTGCCGGTGCCAGTG
CCGGTGCCCGTGCCGAGCTACGGCGGGGAGGAGCCAGTGCGCAAGGAGAGCAAGACTCCG
CCCCCGTACAGCGTCTACGAGCGGACTCTGCGGCGCCCCGTCCCGCTACCTCACAGCCTC
TCCATCCCCGTCACGTCGGAGCCGCCCGCGCTGCCCCCCAAGCCTCTGGCAGCGCGATCC
AGCCACCTGGAGAATGGGGCCCGGAGGACTGACCCCGGCCCGCGGCCCAGGCCCCTGCCC
CGCAAGGTCTCTCAGTTATAA
Enzyme 85 GenBank Gene ID NM_014705.3 Link Image
Enzyme 85 GeneCard ID DOCK4 Link Image
Enzyme 85 GenAtlas ID DOCK4 Link Image
Enzyme 85 HGNC ID HGNC:19192 Link Image
Enzyme 85 Chromosome Location 7
Enzyme 85 Locus 7q31.1
Enzyme 85 SNPs SNPJam Report Link Image
Enzyme 85 General References
  1. Yajnik V, Paulding C, Sordella R, McClatchey AI, Saito M, Wahrer DC, Reynolds P, Bell DW, Lake R, van den Heuvel S, Settleman J, Haber DA: DOCK4, a GTPase activator, is disrupted during tumorigenesis. Cell. 2003 Mar 7;112(5):673-84. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  4. Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Oct 30;5(5):277-86. [PubMed Link Image]
  5. Cote JF, Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J Cell Sci. 2002 Dec 15;115(Pt 24):4901-13. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  7. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  8. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 85 Metabolite References Not Available
Enzyme 86 [top]
Enzyme 86 ID 14068
Enzyme 86 Name Dedicator of cytokinesis protein 5
Enzyme 86 Synonyms Not Available
Enzyme 86 Gene Name DOCK5
Enzyme 86 Protein Sequence >Dedicator of cytokinesis protein 5
MARWIPTKRQKYGVAIYNYNASQDVELSLQIGDTVHILEMYEGWYRGYTLQNKSKKGIFP
ETYIHLKEATVEDLGQHETVIPGELPLVQELTSTLREWAVIWRKLYVNNKLTLFRQLQQM
TYSLIEWRSQILSGTLPKDELAELKKKVTAKIDHGNRMLGLDLVVRDDNGNILDPDETST
IALFKAHEVASKRIEEKIQEEKSILQNLDLRGQSIFSTIHTYGLYVNFKNFVCNIGEDAE
LFMALYDPDQSTFISENYLIRWGSNGMPKEIEKLNNLQAVFTDLSSMDLIRPRVSLVCQI
VRVGHMELKEGKKHTCGLRRPFGVAVMDITDIIHGKVDDEEKQHFIPFQQIAMETYIRQR
QLIMSPLITSHVIGENEPLTSVLNKVIAAKEVNHKGQGLWVSLKLLPGDLTQVQKNFSHL
VDRSTAIARKMGFPEIILPGDVRNDIYVTLIHGEFDKGKKKTPKNVEVTMSVHDEEGKLL
EKAIHPGAGYEGISEYKSVVYYQVKQPCWYETVKVSIAIEEVTRCHIRFTFRHRSSQETR
DKSERAFGVAFVKLMNPDGTTLQDGRHDLVVYKGDNKKMEDAKFYLTLPGTKMEMEEKEL
QASKNLVTFTPSKDSTKDSFQIATLICSTKLTQNVDLLGLLNWRSNSQNIKHNLKKLMEV
DGGEIVKFLQDTLDALFNIMMEMSDSETYDFLVFDALVFIISLIGDIKFQHFNPVLETYI
YKHFSATLAYVKLSKVLNFYVANADDSSKTELLFAALKALKYLFRFIIQSRVLYLRFYGQ
SKDGDEFNNSIRQLFLAFNMLMDRPLEEAVKIKGAALKYLPSIINDVKLVFDPVELSVLF
CKFIQSIPDNQLVRQKLNCMTKIVESTLFRQSECREVLLPLLTDQLSGQLDDNSNKPDHE
ASSQLLSNILEVLDRKDVGATAVHIQLIMERLLRRINRTVIGMNRQSPHIGSFVACMIAL
LQQMDDSHYSHYISTFKTRQDIIDFLMETFIMFKDLIGKNVYAKDWMVMNMTQNRVFLRA
INQFAEVLTRFFMDQASFELQLWNNYFHLAVAFLTHESLQLETFSQAKRNKIVKKYGDMR
KEIGFRIRDMWYNLGPHKIKFIPSMVGPILEVTLTPEVELRKATIPIFFDMMQCEFNFSG
NGNFHMFENELITKLDQEVEGGRGDEQYKVLLEKLLLEHCRKHKYLSSSGEVFALLVSSL
LENLLDYRTIIMQDESKENRMSCTVNVLNFYKEKKREDIYIRYLYKLRDLHRDCENYTEA
AYTLLLHAELLQWSDKPCVPHLLQKDSYYVYTQQELKEKLYQEIISYFDKGKMWEKAIKL
SKELAETYESKVFDYEGLGNLLKKRASFYENIIKAMRPQPEYFAVGYYGQGFPSFLRNKI
FIYRGKEYERREDFSLRLLTQFPNAEKMTSTTPPGEDIKSSPKQYMQCFTVKPVMSLPPS
YKDKPVPEQILNYYRANEVQQFRYSRPFRKGEKDPDNEFATMWIERTTYTTAYTFPGILK
WFEVKQISTEEISPLENAIETMELTNERISNCVQQHAWDRSLSVHPLSMLLSGIVDPAVM
GGFSNYEKAFFTEKYLQEHPEDQEKVELLKRLIALQMPLLTEGIRIHGEKLTEQLKPLHE
RLSSCFRELKEKVEKHYGVITLPPNLTERKQSRTGSIVLPYIMSSTLRRLSITSVTSSVV
STSSNSSDNAPSRPGSDGSILEPLLERRASSGARVEDLSLREENSENRISKFKRKDWSLS
KSQVIAEKAPEPDLMSPTRKAQRPKSLQLMDNRLSPFHGSSPPQSTPLSPPPLTPKATRT
LSSPSLQTDGIAATPVPPPPPPKSKPYEGSQRNSTELAPPLPVRREAKAPPPPPPKARKS
GIPTSEPGSQ
Enzyme 86 Number of Residues 1870
Enzyme 86 Molecular Weight 215306.9
Enzyme 86 Theoretical pI 8.08
Enzyme 86 GO Classification
Function
  • GTP binding
  • GTPase binding
  • GTPase regulator activity
  • binding
  • enzyme binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
Process
Component
Enzyme 86 General Function Involved in binding
Enzyme 86 Specific Function Guanine nucleotide exchange factor (GEF) for Rho and Rac. GEF proteins activate small GTPases by exchanging bound GDP for free GTP
Enzyme 86 Pathways Not Available
Enzyme 86 Reactions Not Available
Enzyme 86 Pfam Domain Function
Enzyme 86 Signals
  • None
Enzyme 86 Transmembrane Regions
  • None
Enzyme 86 Essentiality Not Available
Enzyme 86 GenBank ID Protein 117553586 Link Image
Enzyme 86 UniProtKB/Swiss-Prot ID Q9H7D0 Link Image
Enzyme 86 UniProtKB/Swiss-Prot Entry Name DOCK5_HUMAN Link Image
Enzyme 86 PDB ID Not Available
Enzyme 86 Cellular Location Not Available
Enzyme 86 Gene Sequence >5613 bp
ATGGCCCGCTGGATCCCGACCAAGAGGCAGAAGTACGGGGTTGCGATCTATAACTACAAT
GCTTCTCAAGATGTGGAGCTCTCCTTGCAGATCGGTGACACAGTTCACATCCTGGAGATG
TACGAGGGTTGGTACAGAGGATATACCCTCCAAAATAAATCTAAAAAGGGCATTTTCCCT
GAAACATATATCCATTTGAAAGAGGCAACTGTGGAAGACCTGGGGCAGCATGAAACCGTG
ATTCCTGGCGAGCTCCCCCTGGTGCAGGAGCTCACGTCCACTCTGCGAGAATGGGCTGTC
ATCTGGCGAAAGCTCTACGTGAACAACAAGCTCACCCTCTTCCGCCAGCTGCAGCAGATG
ACGTACAGCCTGATCGAGTGGCGGTCCCAGATCCTGTCTGGGACGCTCCCCAAGGATGAA
CTGGCAGAGCTCAAGAAGAAAGTCACAGCCAAAATTGATCATGGGAACAGAATGCTGGGG
TTAGATCTGGTGGTGCGAGATGACAATGGGAACATCCTAGACCCTGACGAAACCAGCACC
ATTGCCCTCTTCAAGGCCCATGAGGTGGCCTCCAAAAGGATTGAGGAAAAGATCCAAGAA
GAGAAGTCAATCCTGCAGAACCTCGATTTGCGGGGCCAGTCCATCTTCAGTACCATCCAC
ACCTATGGCCTCTATGTGAACTTCAAGAACTTTGTCTGCAACATCGGGGAAGATGCAGAG
TTGTTTATGGCCCTCTACGACCCAGACCAGTCCACTTTTATCAGTGAGAACTATCTAATT
CGTTGGGGCAGTAACGGGATGCCCAAGGAAATAGAGAAGCTCAATAACCTCCAAGCAGTG
TTTACAGACCTTAGCAGCATGGACCTCATCCGGCCCCGCGTCAGCCTTGTGTGCCAGATT
GTCCGCGTGGGCCATATGGAGCTGAAGGAAGGCAAGAAGCACACCTGTGGACTCCGAAGA
CCTTTTGGAGTGGCAGTGATGGATATTACTGATATCATACATGGGAAGGTGGATGATGAA
GAAAAGCAGCATTTTATTCCCTTTCAGCAAATTGCGATGGAAACCTACATCCGCCAGAGG
CAGCTCATCATGTCGCCTTTGATAACATCACACGTGATTGGGGAGAATGAGCCACTCACT
TCAGTCTTGAATAAAGTGATTGCAGCAAAGGAAGTGAATCACAAAGGGCAAGGCCTTTGG
GTATCCTTGAAGCTCTTGCCCGGTGACCTCACCCAGGTTCAGAAGAATTTTTCACACTTG
GTTGATAGATCAACAGCAATAGCCCGGAAGATGGGCTTTCCTGAAATCATACTGCCAGGA
GATGTTCGGAATGACATTTATGTCACCCTGATCCACGGTGAGTTTGACAAAGGGAAGAAG
AAGACGCCAAAGAATGTGGAGGTGACGATGTCTGTGCACGATGAGGAGGGCAAGCTCTTG
GAGAAAGCAATTCACCCTGGTGCTGGATATGAAGGCATTTCAGAATACAAATCAGTAGTC
TATTACCAAGTCAAGCAGCCCTGTTGGTATGAGACTGTCAAGGTATCCATTGCTATAGAA
GAAGTCACACGCTGTCATATAAGATTTACCTTCCGACACAGGTCATCTCAGGAAACCAGA
GATAAATCGGAGCGAGCATTTGGGGTGGCCTTCGTGAAGCTGATGAACCCGGATGGCACC
ACTCTGCAGGATGGGAGGCACGATCTGGTGGTTTATAAGGGTGACAACAAAAAAATGGAA
GATGCTAAATTCTACCTGACCCTGCCTGGAACCAAGATGGAGATGGAAGAAAAAGAGCTT
CAAGCATCCAAAAACCTGGTCACCTTCACCCCAAGCAAGGATAGCACTAAAGACAGCTTT
CAGATTGCCACCCTCATCTGCTCCACAAAGCTCACCCAGAATGTTGACCTGTTAGGCTTG
TTAAATTGGCGTTCCAACTCCCAGAACATTAAACACAACCTAAAGAAGTTAATGGAAGTG
GATGGAGGAGAGATTGTTAAGTTTTTGCAAGATACACTAGATGCACTCTTTAACATAATG
ATGGAAATGTCAGACAGTGAAACCTATGACTTCCTTGTGTTTGACGCACTGGTATTTATT
ATTTCACTGATAGGAGACATCAAGTTCCAGCATTTTAATCCTGTACTTGAAACCTACATT
TACAAGCACTTCAGCGCCACTTTGGCATATGTGAAACTCTCCAAGGTACTGAACTTCTAT
GTGGCTAATGCAGATGACTCCAGCAAGACTGAACTGCTTTTTGCTGCGTTGAAAGCCTTG
AAGTACTTGTTTAGATTCATCATCCAATCCCGAGTGCTCTACTTGAGATTTTATGGGCAG
AGCAAAGATGGAGATGAGTTTAATAATTCAATTCGCCAGTTATTTCTTGCTTTCAATATG
CTGATGGACAGGCCTCTGGAGGAAGCCGTCAAGATCAAGGGGGCAGCTTTGAAGTACCTT
CCTAGCATAATTAATGATGTCAAACTTGTATTTGATCCTGTTGAGCTCAGCGTGCTCTTC
TGCAAATTCATTCAAAGCATTCCTGACAACCAGCTGGTTCGGCAGAAACTTAACTGCATG
ACCAAGATAGTAGAGAGCACTCTTTTTCGACAGTCAGAGTGCAGAGAAGTGCTGCTGCCA
CTGCTGACAGACCAGCTCAGCGGCCAGTTAGATGACAACTCCAACAAGCCTGACCACGAG
GCAAGCTCGCAGCTTCTGAGCAACATCCTGGAGGTGCTGGACAGGAAGGATGTGGGTGCC
ACTGCGGTGCACATTCAGCTTATAATGGAACGGCTGCTGAGAAGGATCAACCGGACAGTG
ATTGGGATGAACCGGCAGTCTCCCCACATCGGGAGTTTTGTGGCTTGCATGATTGCCCTG
CTGCAGCAAATGGACGACAGCCACTATAGCCACTACATCAGCACTTTCAAAACCAGACAA
GACATCATCGACTTCCTCATGGAAACTTTTATCATGTTCAAGGACCTGATTGGAAAGAAT
GTCTATGCCAAAGATTGGATGGTGATGAATATGACTCAAAACAGGGTTTTTCTCCGTGCT
ATAAATCAGTTTGCTGAAGTTCTCACAAGATTCTTCATGGATCAGGCAAGCTTTGAACTT
CAGCTCTGGAACAATTACTTCCATTTGGCAGTTGCATTTCTCACCCATGAGTCCCTTCAG
CTTGAAACCTTCTCACAAGCCAAGCGCAACAAAATTGTTAAAAAATATGGGGACATGAGA
AAGGAAATCGGCTTTAGAATCCGGGACATGTGGTATAACCTGGGTCCCCACAAAATCAAA
TTCATCCCATCCATGGTGGGTCCCATTCTGGAGGTCACTCTGACCCCTGAAGTAGAGCTC
CGGAAAGCCACAATCCCCATTTTCTTTGATATGATGCAGTGTGAGTTCAATTTCAGTGGA
AATGGCAATTTCCATATGTTTGAGAATGAGCTGATCACAAAGCTGGACCAGGAGGTAGAA
GGGGGCAGAGGAGACGAACAATACAAGGTTCTTCTGGAAAAACTGCTCCTAGAACATTGC
CGGAAACACAAATACCTCTCCAGCTCTGGGGAGGTCTTCGCCCTCCTGGTCAGCAGCCTC
TTAGAGAACCTGCTGGACTATAGAACCATCATCATGCAAGATGAGAGCAAGGAGAACCGT
ATGAGCTGCACTGTGAACGTGCTGAACTTTTATAAAGAAAAGAAGAGAGAGGACATATAC
ATAAGATATCTGTACAAGCTTCGAGATTTGCACCGAGACTGTGAGAACTACACAGAAGCT
GCCTACACGCTTCTCTTGCACGCTGAGCTTCTGCAGTGGTCTGACAAGCCCTGTGTGCCT
CATTTGCTTCAGAAGGACAGTTACTATGTTTATACCCAGCAAGAGCTTAAAGAGAAGCTG
TATCAAGAAATCATATCATATTTCGACAAAGGCAAAATGTGGGAGAAGGCCATCAAGCTG
AGCAAAGAGTTGGCTGAGACTTACGAAAGCAAAGTATTTGACTACGAGGGCCTTGGCAAC
CTCCTGAAAAAAAGGGCCTCATTTTATGAGAACATCATTAAGGCAATGAGGCCTCAGCCT
GAATACTTTGCTGTTGGATACTATGGACAGGGCTTTCCTTCTTTCCTACGGAATAAAATC
TTCATCTATCGGGGAAAGGAGTATGAGAGGCGAGAGGACTTCAGCCTGAGGTTGTTAACC
CAGTTCCCCAATGCGGAGAAGATGACCAGTACCACGCCTCCTGGGGAAGACATCAAGTCG
TCCCCCAAGCAGTACATGCAGTGCTTCACTGTAAAGCCAGTGATGAGCTTGCCGCCCAGC
TACAAGGATAAACCTGTTCCAGAGCAGATCTTAAACTACTACAGAGCCAATGAAGTGCAG
CAGTTCAGATACTCCCGGCCGTTCCGGAAAGGAGAAAAGGATCCAGACAATGAATTTGCT
ACGATGTGGATTGAACGGACCACGTATACGACTGCATATACCTTTCCTGGGATTCTCAAG
TGGTTTGAAGTCAAACAGATTTCAACAGAAGAGATCAGTCCTCTGGAGAATGCCATCGAA
ACCATGGAGCTGACCAACGAGAGGATCAGCAACTGTGTTCAGCAGCATGCCTGGGACCGG
TCCCTCTCTGTGCACCCTCTCTCCATGCTGCTCAGTGGCATCGTGGACCCGGCCGTCATG
GGGGGCTTCTCCAACTATGAAAAGGCTTTTTTTACAGAAAAGTACTTGCAGGAGCATCCT
GAAGACCAGGAGAAGGTTGAGCTGCTAAAGCGACTAATAGCATTACAGATGCCCCTGCTA
ACAGAAGGGATCCGCATCCATGGGGAGAAACTCACAGAGCAGCTGAAGCCGCTGCATGAG
CGGTTGTCTTCTTGCTTCCGGGAACTCAAGGAGAAAGTAGAAAAGCACTATGGGGTTATA
ACACTGCCACCCAACTTGACGGAGAGGAAGCAAAGCCGCACGGGGTCTATTGTGCTCCCC
TACATCATGTCTTCCACTCTGCGGAGGTTGTCCATCACCTCAGTCACTTCCTCTGTGGTT
TCCACCTCTTCAAACTCGTCTGACAATGCTCCTTCCAGACCGGGATCTGATGGCTCAATC
TTGGAGCCACTTTTGGAGCGCAGGGCCTCGTCAGGTGCCAGAGTTGAAGATCTGTCCCTT
AGAGAGGAGAACAGCGAGAACCGGATCAGCAAGTTTAAGAGAAAAGACTGGAGTCTGAGC
AAGTCCCAGGTCATTGCAGAGAAAGCACCAGAACCCGATTTGATGAGCCCAACCAGAAAA
GCACAAAGGCCAAAGAGTCTCCAGTTGATGGATAATCGGCTATCACCATTTCACGGTTCT
TCACCTCCTCAGTCAACACCCTTGAGCCCACCTCCACTCACTCCCAAAGCCACCAGGACC
CTAAGCTCCCCATCGTTGCAGACAGATGGAATCGCGGCCACTCCTGTCCCACCTCCACCT
CCCCCCAAAAGCAAGCCCTATGAAGGCAGCCAGAGGAACTCCACTGAGCTCGCTCCCCCA
CTGCCTGTCCGAAGAGAAGCCAAAGCACCACCCCCTCCACCTCCAAAGGCTCGGAAGTCT
GGCATCCCTACTTCCGAGCCTGGATCCCAGTAA
Enzyme 86 GenBank Gene ID NM_024940.6 Link Image
Enzyme 86 GeneCard ID DOCK5 Link Image
Enzyme 86 GenAtlas ID DOCK5 Link Image
Enzyme 86 HGNC ID HGNC:23476 Link Image
Enzyme 86 Chromosome Location 8
Enzyme 86 Locus 8p21.2
Enzyme 86 SNPs SNPJam Report Link Image
Enzyme 86 General References
  1. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Cote JF, Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J Cell Sci. 2002 Dec 15;115(Pt 24):4901-13. [PubMed Link Image]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  9. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  10. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 86 Metabolite References Not Available
Enzyme 87 [top]
Enzyme 87 ID 14069
Enzyme 87 Name Dedicator of cytokinesis protein 6
Enzyme 87 Synonyms Not Available
Enzyme 87 Gene Name DOCK6
Enzyme 87 Protein Sequence >Dedicator of cytokinesis protein 6
MAASERRAFAHKINRTVAAEVRKQVSRERSGSPHSSRRCSSSLGVPLTEVVEPLDFEDVL
LSRPPDAEPGPLRDLVEFPADDLELLLQPRECRTTEPGIPKDEKLDAQVRAAVEMYIEDW
VIVHRRYQYLSAAYSPVTTDTQRERQKGLPRQVFEQDASGDERSGPEDSNDSRRGSGSPE
DTPRSSGASSIFDLRNLAADSLLPSLLERAAPEDVDRRNETLRRQHRPPALLTLYPAPDE
DEAVERCSRPEPPREHFGQRILVKCLSLKFEIEIEPIFGILALYDVREKKKISENFYFDL
NSDSMKGLLRAHGTHPAISTLARSAIFSVTYPSPDIFLVIKLEKVLQQGDISECCEPYMV
LKEVDTAKNKEKLEKLRLAAEQFCTRLGRYRMPFAWTAVHLANIVSSAGQLDRDSDSEGE
RRPAWTDRRRRGPQDRASSGDDACSFSGFRPATLTVTNFFKQEAERLSDEDLFKFLADMR
RPSSLLRRLRPVTAQLKIDISPAPENPHFCLSPELLHIKPYPDPRGRPTKEILEFPAREV
YAPHTSYRNLLYVYPHSLNFSSRQGSVRNLAVRVQYMTGEDPSQALPVIFGKSSCSEFTR
EAFTPVVYHNKSPEFYEEFKLHLPACVTENHHLLFTFYHVSCQPRPGTALETPVGFTWIP
LLQHGRLRTGPFCLPVSVDQPPPSYSVLTPDVALPGMRWVDGHKGVFSVELTAVSSVHPQ
DPYLDKFFTLVHVLEEGAFPFRLKDTVLSEGNVEQELRASLAALRLASPEPLVAFSHHVL
DKLVRLVIRPPIISGQIVNLGRGAFEAMAHVVSLVHRSLEAAQDARGHCPQLAAYVHYAF
RLPGTEPSLPDGAPPVTVQAATLARGSGRPASLYLARSKSISSSNPDLAVAPGSVDDEVS
RILASKLLHEELALQWVVSSSAVREAILQHAWFFFQLMVKSMALHLLLGQRLDTPRKLRF
PGRFLDDITALVGSVGLEVITRVHKDVELAEHLNASLAFFLSDLLSLVDRGFVFSLVRAH
YKQVATRLQSSPNPAALLTLRMEFTRILCSHEHYVTLNLPCCPLSPPASPSPSVSSTTSQ
SSTFSSQAPDPKVTSMFELSGPFRQQHFLAGLLLTELALALEPEAEGAFLLHKKAISAVH
SLLCGHDTDPRYAEATVKARVAELYLPLLSIARDTLPRLHDFAEGPGQRSRLASMLDSDT
EGEGDIAGTINPSVAMAIAGGPLAPGSRASISQGPPTASRAGCALSAESSRTLLACVLWV
LKNTEPALLQRWATDLTLPQLGRLLDLLYLCLAAFEYKGKKAFERINSLTFKKSLDMKAR
LEEAILGTIGARQEMVRRSRERSPFGNPENVRWRKSVTHWKQTSDRVDKTKDEMEHEALV
EGNLATEASLVVLDTLEIIVQTVMLSEARESVLGAVLKVVLYSLGSAQSALFLQHGLATQ
RALVSKFPELLFEEDTELCADLCLRLLRHCGSRISTIRTHASASLYLLMRQNFEIGHNFA
RVKMQVTMSLSSLVGTTQNFSEEHLRRSLKTILTYAEEDMGLRDSTFAEQVQDLMFNLHM
ILTDTVKMKEHQEDPEMLIDLMYRIARGYQGSPDLRLTWLQNMAGKHAELGNHAEAAQCM
VHAAALVAEYLALLEDHRHLPVGCVSFQNISSNVLEESAISDDILSPDEEGFCSGKHFTE
LGLVGLLEQAAGYFTMGGLYEAVNEVYKNLIPILEAHRDYKKLAAVHGKLQEAFTKIMHQ
SSGWERVFGTYFRVGFYGAHFGDLDEQEFVYKEPSITKLAEISHRLEEFYTERFGDDVVE
IIKDSNPVDKSKLDSQKAYIQITYVEPYFDTYELKDRVTYFDRNYGLRTFLFCTPFTPDG
RAHGELPEQHKRKTLLSTDHAFPYIKTRIRVCHREETVLTPVEVAIEDMQKKTRELAFAT
EQDPPDAKMLQMVLQGSVGPTVNQGPLEVAQVFLAEIPEDPKLFRHHNKLRLCFKDFCKK
CEDALRKNKALIGPDQKEYHRELERNYCRLREALQPLLTQRLPQLMAPTPPGLRNSLNRA
SFRKADL
Enzyme 87 Number of Residues 2047
Enzyme 87 Molecular Weight 229555.6
Enzyme 87 Theoretical pI 6.72
Enzyme 87 GO Classification
Function
  • GTP binding
  • GTPase binding
  • GTPase regulator activity
  • binding
  • enzyme binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
Process
Component
Enzyme 87 General Function Involved in guanyl-nucleotide exchange factor activity
Enzyme 87 Specific Function Potential guanine nucleotide exchange factor (GEF). GEF proteins activate some small GTPases by exchanging bound GDP for free GTP
Enzyme 87 Pathways Not Available
Enzyme 87 Reactions Not Available
Enzyme 87 Pfam Domain Function
Enzyme 87 Signals
  • None
Enzyme 87 Transmembrane Regions
  • None
Enzyme 87 Essentiality Not Available
Enzyme 87 GenBank ID Protein 157426887 Link Image
Enzyme 87 UniProtKB/Swiss-Prot ID Q96HP0 Link Image
Enzyme 87 UniProtKB/Swiss-Prot Entry Name DOCK6_HUMAN Link Image
Enzyme 87 PDB ID Not Available
Enzyme 87 Cellular Location Not Available
Enzyme 87 Gene Sequence >6144 bp
ATGGCTGCCTCCGAGCGCCGCGCCTTCGCGCACAAGATCAACAGGACGGTGGCCGCAGAG
GTGCGGAAGCAGGTGTCCCGGGAACGCAGTGGCTCCCCCCACTCCAGCAGGCGCTGCAGC
AGCTCCCTGGGGGTCCCACTGACTGAAGTTGTCGAGCCCCTGGACTTTGAGGATGTACTT
CTGAGCCGGCCACCAGATGCTGAGCCCGGGCCCCTCAGGGACCTGGTAGAATTCCCAGCT
GATGACTTGGAGCTGCTGCTGCAGCCCCGGGAATGCCGGACCACGGAGCCCGGGATCCCC
AAGGATGAAAAACTGGATGCCCAGGTGAGGGCCGCGGTGGAGATGTATATTGAGGACTGG
GTCATTGTCCACAGAAGGTATCAGTACCTGAGTGCAGCATACAGCCCCGTCACCACAGAC
ACACAGCGGGAGCGACAGAAGGGCCTCCCCCGCCAGGTCTTTGAGCAGGATGCTTCTGGA
GACGAGAGGTCCGGCCCTGAGGACTCGAATGACTCCCGGCGTGGCTCGGGCTCCCCGGAA
GACACCCCTCGAAGCAGTGGTGCCTCTAGCATCTTCGACCTGAGGAACCTGGCAGCTGAC
TCATTGCTGCCCTCTCTGCTAGAGCGGGCGGCCCCAGAAGATGTGGACCGGCGCAATGAA
ACCCTTCGACGGCAGCACCGGCCCCCGGCCCTGCTCACCCTCTACCCGGCACCTGACGAG
GATGAAGCCGTGGAACGCTGTAGCCGCCCAGAGCCACCCCGCGAGCACTTTGGACAAAGG
ATCTTGGTCAAGTGTCTGTCGCTCAAGTTCGAGATTGAAATTGAGCCCATCTTTGGGATC
TTGGCTCTGTATGATGTGCGGGAGAAAAAGAAGATCTCGGAGAACTTCTACTTCGACCTG
AACTCGGACTCCATGAAGGGGCTGCTTCGGGCTCATGGCACCCACCCTGCCATCTCCACC
CTGGCCCGCTCTGCCATCTTCTCTGTGACCTACCCCTCACCTGACATCTTCCTGGTCATC
AAGTTGGAGAAGGTGCTTCAGCAAGGGGACATCAGTGAGTGCTGTGAGCCTTACATGGTG
TTGAAAGAAGTGGACACAGCCAAGAACAAAGAGAAGCTAGAGAAGCTGCGCCTGGCGGCC
GAGCAGTTCTGCACCCGCCTGGGCCGCTACCGCATGCCCTTCGCCTGGACGGCCGTGCAC
TTGGCCAACATCGTGAGCAGCGCTGGGCAGCTGGACCGGGACTCTGACTCGGAGGGCGAG
CGCCGGCCAGCCTGGACAGACCGCCGCCGTCGGGGGCCCCAGGACCGGGCGAGTAGTGGG
GACGACGCCTGCAGCTTCTCTGGCTTCCGTCCAGCCACGCTAACTGTCACAAACTTCTTT
AAGCAGGAGGCTGAGCGACTCAGTGACGAGGACCTCTTCAAGTTCCTGGCTGACATGAGG
CGCCCGTCGTCCCTGCTGCGGCGACTACGTCCTGTGACTGCCCAGCTCAAGATCGACATT
TCTCCGGCTCCTGAAAATCCCCACTTCTGCCTCTCCCCTGAGCTGCTTCATATCAAGCCC
TACCCGGACCCCAGGGGCCGGCCCACCAAGGAGATTCTGGAGTTCCCCGCCCGCGAAGTC
TATGCCCCCCATACCAGCTACAGGAACCTGCTGTACGTGTACCCGCACAGCCTCAACTTC
AGCAGCCGCCAGGGCTCCGTGCGCAACCTTGCTGTGCGAGTGCAGTACATGACAGGCGAG
GACCCCAGCCAGGCTCTGCCGGTCATCTTTGGCAAGTCCAGCTGCAGTGAATTTACCCGC
GAGGCCTTCACACCGGTGGTCTACCATAACAAGTCCCCCGAGTTCTACGAGGAGTTCAAG
CTGCATCTTCCAGCCTGCGTGACAGAGAACCATCACCTGCTGTTCACCTTCTACCATGTC
AGCTGCCAGCCCCGGCCGGGCACTGCCCTGGAGACACCCGTGGGCTTTACTTGGATCCCA
CTGCTGCAGCACGGGCGCCTGAGGACCGGCCCCTTCTGTCTCCCAGTGTCTGTGGACCAG
CCGCCGCCCAGCTATTCCGTGCTCACACCCGATGTGGCGCTTCCGGGCATGCGCTGGGTG
GACGGTCACAAGGGCGTGTTCAGTGTGGAGCTCACAGCCGTGTCCTCTGTGCACCCCCAG
GACCCCTACCTGGACAAATTCTTCACCCTGGTGCACGTCCTGGAGGAGGGAGCCTTCCCA
TTCCGGCTCAAGGACACTGTGCTGAGCGAGGGCAACGTGGAGCAGGAGCTGCGGGCCAGT
CTTGCAGCACTGCGCCTGGCCAGCCCCGAACCCCTTGTGGCCTTCTCCCACCACGTGCTG
GACAAGCTCGTGCGTCTGGTCATCAGGCCCCCGATCATCAGTGGCCAGATTGTGAACCTG
GGCCGTGGAGCCTTTGAAGCAATGGCCCATGTAGTCAGCCTTGTTCACCGGAGCCTGGAG
GCAGCCCAGGATGCCCGCGGTCACTGCCCACAGCTGGCTGCCTACGTCCACTACGCCTTT
CGCCTTCCTGGCACTGAGCCCAGCCTCCCGGATGGGGCCCCTCCAGTGACAGTGCAGGCT
GCCACACTGGCCCGTGGCTCTGGTCGCCCCGCAAGCCTCTACCTGGCGCGTTCCAAGAGC
ATCAGCAGCAGCAACCCTGACCTCGCCGTGGCCCCTGGCTCTGTGGATGACGAGGTTTCC
CGCATCCTGGCCAGCAAGCTGCTTCACGAGGAGCTGGCTCTGCAGTGGGTGGTCAGCAGC
AGTGCCGTACGCGAGGCCATCCTCCAGCACGCCTGGTTCTTCTTCCAGCTCATGGTGAAG
AGTATGGCGCTGCACCTGCTGCTTGGCCAGCGACTAGACACACCCCGCAAGCTGCGCTTC
CCCGGACGCTTCCTGGACGACATCACTGCCTTGGTGGGCTCTGTGGGCCTGGAGGTCATC
ACCCGTGTCCACAAGGATGTGGAGCTGGCCGAGCACCTCAACGCCAGCCTGGCTTTCTTC
CTCAGTGACCTTCTGTCCCTGGTGGACCGGGGCTTTGTCTTCAGCCTGGTCCGGGCCCAC
TACAAGCAGGTGGCCACGCGGCTCCAGTCGTCCCCTAATCCAGCAGCCCTGCTGACCCTG
CGCATGGAATTCACCCGCATCCTGTGCAGCCACGAGCACTACGTGACCCTCAACCTCCCC
TGCTGCCCCCTGTCACCTCCAGCCTCGCCCTCCCCCTCTGTGTCCTCCACCACCTCCCAG
AGCTCCACCTTCTCCAGCCAAGCCCCGGACCCCAAGGTGACCAGCATGTTCGAACTGAGT
GGACCATTCCGGCAGCAGCACTTCCTAGCTGGGCTCCTGCTGACGGAGCTGGCACTGGCC
CTCGAACCTGAGGCTGAAGGGGCATTCCTGTTGCACAAGAAGGCCATCAGTGCTGTGCAC
AGCCTGCTATGTGGCCATGACACTGACCCCCGCTACGCCGAGGCCACTGTGAAGGCTCGT
GTGGCCGAGCTGTACCTGCCACTGCTATCGATTGCACGGGATACCTTGCCACGGCTGCAT
GACTTTGCTGAGGGCCCAGGTCAGCGGTCAAGACTGGCCTCAATGCTTGACTCAGACACA
GAAGGCGAAGGGGACATTGCGGGTACCATCAACCCCTCTGTGGCCATGGCCATTGCTGGT
GGCCCCCTAGCCCCTGGCTCCCGGGCCAGCATCTCCCAGGGGCCACCAACGGCTTCTCGC
GCAGGCTGTGCCCTCTCTGCTGAGTCAAGCCGGACCTTGCTGGCGTGTGTGCTGTGGGTG
CTGAAAAACACCGAGCCGGCGCTCCTGCAGCGCTGGGCCACTGACCTGACACTCCCCCAG
CTGGGACGTCTGTTGGATTTGCTGTACCTTTGCCTAGCTGCCTTTGAGTACAAGGGGAAA
AAGGCCTTTGAACGCATCAACAGCCTCACATTCAAAAAATCTCTGGATATGAAGGCGCGG
CTAGAGGAAGCCATTCTGGGTACCATCGGAGCTCGACAAGAAATGGTTCGGCGAAGTCGT
GAGAGGAGCCCGTTTGGGAATCCGGAGAATGTGCGCTGGCGGAAGAGCGTCACACACTGG
AAGCAAACCTCAGACCGCGTGGACAAGACCAAGGATGAAATGGAACACGAGGCCTTGGTG
GAAGGGAACCTGGCAACCGAGGCAAGCCTAGTGGTTCTGGACACACTGGAGATCATCGTG
CAGACGGTGATGCTTTCAGAAGCCCGGGAGAGCGTCTTGGGGGCAGTGCTGAAGGTTGTG
CTGTACAGCCTGGGCAGTGCCCAGAGTGCCCTCTTCTTGCAGCATGGCCTGGCCACCCAG
AGGGCCCTTGTGTCCAAGTTCCCGGAGCTGCTGTTCGAGGAGGACACGGAGCTGTGTGCC
GACCTGTGCCTGAGGCTCCTACGACACTGTGGCAGCCGCATCAGCACCATCCGCACGCAC
GCCAGCGCCTCGCTGTACCTGCTCATGCGACAGAACTTCGAGATCGGCCACAACTTTGCC
CGTGTGAAGATGCAGGTCACCATGTCTCTCTCGTCCCTGGTGGGGACGACGCAGAACTTC
AGTGAAGAGCACCTGCGACGTTCACTCAAAACCATCCTCACCTATGCTGAGGAGGACATG
GGGCTGCGGGACAGCACCTTCGCAGAGCAGGTCCAGGACCTGATGTTCAACCTGCACATG
ATCCTGACGGACACGGTGAAGATGAAGGAACACCAGGAGGACCCTGAGATGCTCATCGAC
CTCATGTACAGAATTGCCCGGGGCTACCAGGGCTCACCGGACCTTCGGCTGACCTGGTTG
CAGAACATGGCCGGGAAGCACGCGGAGCTGGGCAACCACGCCGAGGCCGCCCAGTGCATG
GTGCACGCGGCCGCCCTCGTGGCTGAGTACCTCGCCCTGCTCGAGGACCACCGCCACCTG
CCCGTGGGCTGCGTTTCCTTCCAGAACATCTCATCCAACGTGCTAGAGGAGTCCGCCATC
TCCGACGACATCCTGTCGCCCGACGAGGAGGGCTTCTGCTCCGGGAAGCACTTCACTGAG
CTGGGGCTGGTAGGGTTGCTGGAACAGGCAGCCGGCTACTTCACCATGGGCGGGCTCTAC
GAGGCGGTGAATGAGGTCTACAAGAACCTCATCCCCATCCTGGAAGCCCACCGTGACTAC
AAGAAGCTGGCCGCGGTGCACGGCAAACTGCAGGAGGCCTTCACCAAGATCATGCACCAG
AGTTCCGGCTGGGAGCGCGTGTTCGGGACGTATTTCCGCGTGGGCTTCTACGGCGCCCAC
TTCGGTGACCTGGATGAGCAGGAGTTTGTGTACAAGGAGCCATCGATCACGAAGCTGGCA
GAGATCTCACACCGGCTGGAGGAGTTCTACACGGAGAGATTTGGCGACGACGTCGTTGAG
ATTATCAAAGACTCTAACCCTGTGGACAAGTCCAAGCTTGACTCACAAAAGGCCTACATC
CAGATCACGTATGTGGAACCGTACTTTGATACCTACGAGCTCAAGGACCGGGTGACCTAC
TTTGACCGCAACTATGGGCTTCGCACATTCCTGTTCTGCACGCCGTTCACGCCGGATGGG
CGCGCACACGGGGAGCTGCCCGAGCAACACAAGCGTAAGACGCTGCTCAGCACCGACCAC
GCCTTCCCCTACATCAAGACTCGCATCCGTGTGTGCCACCGGGAGGAGACGGTGCTGACG
CCAGTGGAGGTGGCCATCGAGGACATGCAGAAGAAGACACGGGAGCTGGCCTTTGCCACC
GAGCAGGACCCACCAGATGCTAAGATGCTACAGATGGTGCTTCAGGGCTCTGTAGGGCCC
ACCGTGAACCAGGGTCCCCTGGAGGTGGCCCAGGTGTTTTTAGCAGAGATCCCGGAAGAC
CCCAAGCTCTTCCGGCATCACAACAAATTGCGGCTCTGCTTCAAGGACTTCTGCAAGAAA
TGTGAGGATGCGCTGCGGAAAAATAAGGCCCTGATTGGGCCGGACCAGAAGGAGTACCAC
CGTGAGCTGGAGCGCAACTACTGCCGCCTGCGGGAGGCTCTGCAGCCCCTGCTTACCCAG
CGCCTGCCCCAGCTGATGGCACCCACCCCACCCGGCCTCAGGAACTCCTTGAACAGAGCA
AGTTTCCGAAAGGCAGACCTCTGA
Enzyme 87 GenBank Gene ID NM_020812.2 Link Image
Enzyme 87 GeneCard ID DOCK6 Link Image
Enzyme 87 GenAtlas ID DOCK6 Link Image
Enzyme 87 HGNC ID HGNC:19189 Link Image
Enzyme 87 Chromosome Location 1
Enzyme 87 Locus 19p13.2
Enzyme 87 SNPs SNPJam Report Link Image
Enzyme 87 General References
  1. Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Feb 28;7(1):65-73. [PubMed Link Image]
  2. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Cote JF, Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J Cell Sci. 2002 Dec 15;115(Pt 24):4901-13. [PubMed Link Image]
  5. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  6. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
Enzyme 87 Metabolite References Not Available
Enzyme 88 [top]
Enzyme 88 ID 14070
Enzyme 88 Name Dedicator of cytokinesis protein 7
Enzyme 88 Synonyms Not Available
Enzyme 88 Gene Name DOCK7
Enzyme 88 Protein Sequence >Dedicator of cytokinesis protein 7
MAERRAFAQKISRTVAAEVRKQISGQYSGSPQLLKNLNIVGNISHHTTVPLTEAVDPVDL
EDYLITHPLAVDSGPLRDLIEFPPDDIEVVYSPRDCRTLVSAVPEESEMDPHVRDCIRSY
TEDWAIVIRKYHKLGTGFNPNTLDKQKERQKGLPKQVFESDEAPDGNSYQDDQDDLKRRS
MSIDDTPRGSWACSIFDLKNSLPDALLPNLLDRTPNEEIDRQNDDQRKSNRHKELFALHP
SPDEEEPIERLSVPDIPKEHFGQRLLVKCLSLKFEIEIEPIFASLALYDVKEKKKISENF
YFDLNSEQMKGLLRPHVPPAAITTLARSAIFSITYPSQDVFLVIKLEKVLQQGDIGECAE
PYMIFKEADATKNKEKLEKLKSQADQFCQRLGKYRMPFAWTAIHLMNIVSSAGSLERDST
EVEISTGERKGSWSERRNSSIVGRRSLERTTSGDDACNLTSFRPATLTVTNFFKQEGDRL
SDEDLYKFLADMRRPSSVLRRLRPITAQLKIDISPAPENPHYCLTPELLQVKLYPDSRVR
PTREILEFPARDVYVPNTTYRNLLYIYPQSLNFANRQGSARNITVKVQFMYGEDPSNAMP
VIFGKSSCSEFSKEAYTAVVYHNRSPDFHEEIKVKLPATLTDHHHLLFTFYHVSCQQKQN
TPLETPVGYTWIPMLQNGRLKTGQFCLPVSLEKPPQAYSVLSPEVPLPGMKWVDNHKGVF
NVEVVAVSSIHTQDPYLDKFFALVNALDEHLFPVRIGDMRIMENNLENELKSSISALNSS
QLEPVVRFLHLLLDKLILLVIRPPVIAGQIVNLGQASFEAMASIINRLHKNLEGNHDQHG
RNSLLASYIHYVFRLPNTYPNSSSPGPGGLGGSVHYATMARSAVRPASLNLNRSRSLSNS
NPDISGTPTSPDDEVRSIIGSKGLDRSNSWVNTGGPKAAPWGSNPSPSAESTQAMDRSCN
RMSSHTETSSFLQTLTGRLPTKKLFHEELALQWVVCSGSVRESALQQAWFFFELMVKSMV
HHLYFNDKLEAPRKSRFPERFMDDIAALVSTIASDIVSRFQKDTEMVERLNTSLAFFLND
LLSVMDRGFVFSLIKSCYKQVSSKLYSLPNPSVLVSLRLDFLRIICSHEHYVTLNLPCSL
LTPPASPSPSVSSATSQSSGFSTNVQDQKIANMFELSVPFRQQHYLAGLVLTELAVILDP
DAEGLFGLHKKVINMVHNLLSSHDSDPRYSDPQIKARVAMLYLPLIGIIMETVPQLYDFT
ETHNQRGRPICIATDDYESESGSMISQTVAMAIAGTSVPQLTRPGSFLLTSTSGRQHTTF
SAESSRSLLICLLWVLKNADETVLQKWFTDLSVLQLNRLLDLLYLCVSCFEYKGKKVFER
MNSLTFKKSKDMRAKLEEAILGSIGARQEMVRRSRGQLGTYTIASPPERSPSGSAFGSQE
NLRWRKDMTHWRQNTEKLDKSRAEIEHEALIDGNLATEANLIILDTLEIVVQTVSVTESK
ESILGGVLKVLLHSMACNQSAVYLQHCFATQRALVSKFPELLFEEETEQCADLCLRLLRH
CSSSIGTIRSHASASLYLLMRQNFEIGNNFARVKMQVTMSLSSLVGTSQNFNEEFLRRSL
KTILTYAEEDLELRETTFPDQVQDLVFNLHMILSDTVKMKEHQEDPEMLIDLMYRIAKGY
QTSPDLRLTWLQNMAGKHSERSNHAEAAQCLVHSAALVAEYLSMLEDRKYLPVGCVTFQN
ISSNVLEESAVSDDVVSPDEEGICSGKYFTESGLVGLLEQAAASFSMAGMYEAVNEVYKV
LIPIHEANRDAKKLSTIHGKLQEAFSKIVHQSTGWERMFGTYFRVGFYGTKFGDLDEQEF
VYKEPAITKLAEISHRLEGFYGERFGEDVVEVIKDSNPVDKCKLDPNKAYIQITYVEPYF
DTYEMKDRITYFDKNYNLRRFMYCTPFTLDGRAHGELHEQFKRKTILTTSHAFPYIKTRV
NVTHKEEIILTPIEVAIEDMQKKTQELAFATHQDPADPKMLQMVLQGSVGTTVNQGPLEV
AQVFLSEIPSDPKLFRHHNKLRLCFKDFTKRCEDALRKNKSLIGPDQKEYQRELERNYHR
LKEALQPLINRKIPQLYKAVLPVTCHRDSFSRMSLRKMDL
Enzyme 88 Number of Residues 2140
Enzyme 88 Molecular Weight 242558.3
Enzyme 88 Theoretical pI 6.78
Enzyme 88 GO Classification
Function
  • GTP binding
  • GTPase binding
  • GTPase regulator activity
  • binding
  • enzyme binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
Process
Component
Enzyme 88 General Function Involved in guanyl-nucleotide exchange factor activity
Enzyme 88 Specific Function Functions as a guanine nucleotide exchange factor (GEF), which activates Rac1 and Rac3 Rho small GTPases by exchanging bound GDP for free GTP. Does not have a GEF activity for CDC42. Required for STMN1 'Ser-15' phosphorylation during axon formation and consequently for neuronal polarization
Enzyme 88 Pathways Not Available
Enzyme 88 Reactions Not Available
Enzyme 88 Pfam Domain Function
Enzyme 88 Signals
  • None
Enzyme 88 Transmembrane Regions
  • None
Enzyme 88 Essentiality Not Available
Enzyme 88 GenBank ID Protein 54112429 Link Image
Enzyme 88 UniProtKB/Swiss-Prot ID Q96N67 Link Image
Enzyme 88 UniProtKB/Swiss-Prot Entry Name DOCK7_HUMAN Link Image
Enzyme 88 PDB ID Not Available
Enzyme 88 Cellular Location Not Available
Enzyme 88 Gene Sequence >6330 bp
ATGGCCGAGCGCCGCGCCTTCGCCCAGAAGATCAGCAGAACGGTGGCAGCCGAAGTTAGG
AAGCAGATCTCCGGACAATATAGTGGTTCTCCCCAACTGCTCAAAAACCTTAATATTGTT
GGCAATATATCCCATCACACCACAGTGCCCCTTACCGAAGCAGTAGATCCAGTGGATTTG
GAAGATTACCTCATTACTCATCCTTTGGCTGTGGATTCTGGGCCTTTACGGGATTTGATT
GAATTTCCTCCAGATGATATTGAAGTTGTTTATAGTCCTCGGGACTGCAGAACTCTTGTT
TCAGCTGTACCTGAAGAAAGTGAAATGGATCCACATGTTAGAGACTGTATAAGAAGTTAT
ACAGAAGACTGGGCAATTGTCATCAGAAAATATCATAAATTGGGAACAGGATTTAATCCC
AATACATTAGATAAACAGAAAGAAAGGCAAAAAGGTTTGCCAAAACAAGTTTTTGAATCT
GATGAAGCTCCAGATGGCAACAGCTACCAGGATGATCAAGATGACCTTAAAAGACGTTCA
ATGTCAATAGATGATACCCCAAGGGGTAGCTGGGCCTGTAGTATCTTTGACTTGAAAAAT
TCACTTCCTGATGCTTTGCTTCCCAATTTACTTGATCGAACTCCAAATGAAGAAATAGAC
CGTCAGAATGATGACCAAAGGAAATCAAACCGTCACAAAGAACTTTTTGCTTTGCATCCA
TCACCAGATGAGGAAGAACCAATAGAACGGCTTAGTGTTCCTGATATACCCAAAGAACAT
TTTGGTCAAAGACTTCTTGTAAAATGCTTATCACTCAAGTTTGAAATTGAAATTGAACCC
ATTTTTGCAAGTTTGGCTTTATATGATGTCAAGGAAAAGAAAAAGATTTCAGAAAACTTT
TATTTTGACCTTAATTCTGAGCAGATGAAAGGGTTGTTACGTCCACATGTACCACCTGCT
GCCATTACTACCCTGGCAAGATCAGCAATTTTTTCTATCACTTATCCTTCCCAAGATGTT
TTTCTTGTAATAAAGCTAGAAAAAGTCCTACAGCAAGGAGACATTGGAGAGTGTGCAGAA
CCATATATGATTTTCAAAGAAGCAGATGCCACCAAGAATAAAGAAAAACTGGAGAAACTG
AAGAGTCAAGCAGATCAGTTTTGCCAAAGACTTGGGAAATATCGCATGCCTTTTGCTTGG
ACTGCAATCCATTTAATGAATATTGTTAGCAGTGCTGGGAGTTTGGAAAGAGATTCTACA
GAAGTAGAAATCAGTACTGGAGAACGAAAAGGGTCTTGGTCAGAGAGGAGGAATTCTAGT
ATTGTTGGCAGACGATCACTTGAAAGGACAACAAGTGGAGATGATGCTTGTAACTTGACG
AGCTTTCGACCAGCTACTCTCACAGTGACAAATTTTTTTAAGCAGGAAGGAGACCGCTTA
AGTGATGAAGATCTCTACAAATTCCTTGCTGATATGAGAAGGCCATCTTCTGTCTTACGG
CGACTAAGACCTATTACAGCTCAGCTCAAGATAGACATTTCTCCCGCACCTGAAAATCCC
CATTATTGCCTAACTCCGGAGCTGCTTCAAGTGAAGCTTTACCCTGACAGTAGAGTTAGA
CCTACCAGAGAAATCTTAGAGTTTCCCGCAAGGGATGTTTATGTTCCAAACACTACTTAC
AGAAATCTTCTCTACATATACCCTCAGAGTCTTAATTTTGCCAATCGTCAAGGTTCTGCT
AGAAATATAACAGTGAAAGTCCAGTTTATGTATGGAGAGGATCCAAGCAATGCCATGCCG
GTAATCTTTGGTAAATCTAGCTGTTCAGAATTTTCAAAGGAAGCCTATACAGCCGTAGTA
TATCATAACAGGTCTCCTGATTTTCATGAAGAAATCAAGGTTAAGCTTCCTGCTACTTTA
ACTGACCATCATCACTTGCTTTTTACTTTTTATCATGTTAGTTGTCAACAAAAACAAAAT
ACTCCTCTTGAAACACCAGTTGGATATACATGGATACCAATGCTTCAGAATGGACGGTTG
AAGACTGGCCAGTTTTGCTTGCCAGTCTCATTGGAAAAACCACCACAGGCTTATTCTGTA
CTGTCTCCTGAGGTTCCTCTACCTGGCATGAAATGGGTAGATAATCACAAAGGTGTTTTT
AATGTTGAAGTTGTTGCTGTTTCGTCTATCCATACACAAGATCCTTATCTTGACAAATTT
TTTGCTCTGGTCAATGCTCTGGATGAACACCTGTTCCCAGTCCGAATTGGGGACATGCGA
ATCATGGAAAATAACTTAGAAAATGAATTGAAGAGCAGTATTTCAGCACTGAATTCATCC
CAGCTGGAACCAGTGGTCCGATTTCTTCATCTTCTGCTAGATAAACTGATACTTTTAGTT
ATTAGACCTCCTGTCATTGCTGGCCAAATAGTTAACCTAGGTCAAGCATCTTTTGAAGCC
ATGGCATCAATTATAAATCGACTTCACAAAAACTTGGAAGGAAATCATGACCAGCATGGC
AGAAACAGCCTTCTTGCATCATATATTCATTATGTTTTCCGCCTACCAAATACTTACCCT
AATTCATCATCACCAGGTCCTGGGGGTTTGGGAGGATCAGTGCATTATGCCACAATGGCT
AGATCTGCGGTGAGACCTGCAAGCCTTAATTTAAATCGTTCTCGAAGCCTTAGTAATAGC
AATCCAGATATATCTGGGACTCCCACGTCACCAGATGATGAAGTTCGATCAATCATCGGG
AGTAAGGCTATGGATCGAAGTTGTAATCGTATGTCTTCGCACACAGAGACGTCAAGTTTC
TTACAAACATTAACGGGACGCTTACCAACTAAAAAGCTTTTTCACGAGGAGCTGGCTTTG
CAGTGGGTTGTTTGCAGTGGCAGCGTTCGGGAATCAGCTTTGCAACAAGCCTGGTTCTTT
TTTGAATTAATGGTAAAGAGCATGGTGCACCATTTATACTTTAATGATAAACTTGAGGCT
CCAAGGAAAAGTCGTTTTCCAGAACGTTTCATGGATGACATTGCAGCTCTTGTCAGCACG
ATTGCTAGTGATATAGTTTCACGATTTCAGAAGGACACAGAAATGGTTGAGAGACTCAAT
ACAAGCCTTGCATTCTTTCTCAATGATCTGTTGTCTGTTATGGACAGAGGATTTGTTTTT
AGCCTTATAAAGTCCTGCTATAAACAGGTGTCTTCAAAGCTTTACTCATTACCGAATCCC
AGTGTTCTGGTGTCCTTGAGGCTGGATTTTCTACGAATCATCTGCAGTCATGAGCACTAT
GTTACATTAAACTTACCCTGCAGCTTACTTACTCCACCTGCATCTCCATCACCTTCTGTT
TCTTCTGCAACATCTCAGAGTTCTGGATTTTCTACGAATGTACAAGACCAAAAGATTGCA
AATATGTTTGAATTATCCGTGCCTTTCCGCCAACAGCATTATTTGGCAGGACTTGTGTTA
ACAGAGCTGGCTGTCATTTTAGACCCTGATGCTGAAGGACTGTTTGGATTGCATAAGAAA
GTCATCAATATGGTACACAATTTACTCTCCAGTCACGACTCAGACCCGCGGTACTCTGAC
CCTCAGATAAAGGCTCGAGTGGCCATGTTGTATCTACCTCTGATTGGTATTATCATGGAA
ACTGTACCTCAGCTGTATGATTTTACAGAAACTCACAATCAACGAGGAAGACCAATTTGT
ATAGCCACTGATGATTATGAAAGTGAGAGCGGAAGTATGATAAGCCAGACCGTTGCCATG
GCAATCGCAGGGACATCGGTCCCTCAACTAACAAGGCCTGGCAGTTTCCTCCTCACGTCA
ACGAGTGGCAGGCAACACACTACCTTTTCAGCAGAATCAAGTCGAAGCCTTTTGATCTGT
CTACTTTGGGTTCTCAAAAATGCAGATGAAACAGTTCTACAGAAGTGGTTTACAGATCTC
TCAGTCTTGCAGCTAAACCGGCTATTAGATCTGCTTTATCTCTGTGTGTCTTGCTTTGAG
TATAAAGGGAAAAAAGTGTTTGAACGAATGAATAGCTTGACCTTTAAGAAATCAAAAGAC
ATGAGAGCAAAGCTTGAAGAAGCTATTCTTGGGAGCATAGGTGCCAGGCAAGAAATGGTA
CGGCGAAGCCGAGGACAGCTCGGTACGTACACAATAGCTTCTCCTCCTGAGAGAAGCCCA
TCTGGAAGTGCCTTTGGAAGTCAAGAAAATTTGAGGTGGAGGAAAGATATGACTCACTGG
CGTCAAAACACAGAGAAGCTTGACAAATCAAGAGCAGAGATTGAACACGAAGCACTGATT
GATGGAAACCTGGCTACAGAAGCAAACCTAATCATTTTAGATACATTAGAGATTGTTGTT
CAGACCGTTTCTGTAACGGAATCCAAAGAGAGCATTCTTGGTGGAGTGCTAAAAGTGCTA
CTACACAGCATGGCCTGTAACCAAAGTGCAGTTTATCTACAACACTGTTTTGCTACACAG
AGAGCCTTGGTTTCAAAGTTTCCTGAACTCTTATTTGAAGAAGAGACAGAGCAGTGTGCT
GATTTATGCCTCAGGCTTCTCCGACACTGTAGCAGTAGCATCGGTACAATACGGTCACAC
GCCAGTGCCTCCCTTTACCTACTAATGAGGCAAAACTTTGAGATTGGGAATAACTTTGCC
AGGGTTAAAATGCAGGTAACAATGTCACTATCCTCCTTGGTGGGCACATCTCAGAATTTT
AATGAAGAATTCTTAAGACGTTCTCTAAAGACTATATTGACATATGCTGAAGAAGATCTG
GAATTGAGGGAAACAACATTTCCTGATCAGGTCCAGGATCTGGTTTTCAATCTCCATATG
ATTCTTTCTGATACTGTGAAAATGAAGGAACACCAGGAGGATCCTGAAATGTTGATTGAT
CTAATGTACAGAATTGCCAAGGGTTACCAGACCTCTCCAGATCTGCGATTGACCTGGTTG
CAGAACATGGCAGGCAAGCACTCAGAACGAAGCAATCATGCTGAAGCTGCACAGTGTCTA
GTCCACTCAGCAGCACTTGTTGCTGAATATTTGAGCATGCTGGAGGACCGGAAATATCTT
CCTGTGGGATGTGTAACATTTCAGAATATTTCATCTAATGTTTTAGAAGAATCTGCGGTC
TCAGATGATGTGGTATCTCCAGATGAAGAAGGTATCTGCTCTGGAAAATACTTTACTGAG
TCAGGACTTGTGGGATTACTGGAACAAGCAGCTGCTTCCTTCTCTATGGCTGGCATGTAT
GAAGCAGTTAATGAAGTTTACAAAGTACTTATTCCTATTCATGAAGCTAATCGGGATGCA
AAGAAACTATCCACAATTCATGGTAAACTTCAAGAAGCATTCAGCAAAATTGTTCATCAG
AGTACTGGCTGGGAGCGGATGTTTGGCACCTATTTTCGTGTTGGTTTTTATGGAACCAAG
TTCGGGGATTTGGATGAACAAGAATTTGTTTACAAGGAGCCTGCAATAACCAAACTTGCA
GAGATATCTCACAGATTGGAGGGATTTTACGGAGAAAGATTTGGAGAGGATGTGGTTGAA
GTAATCAAAGACTCTAATCCTGTAGACAAGTGTAAATTAGATCCTAACAAGGCATATATT
CAGATTACCTATGTGGAGCCATACTTTGACACATATGAGATGAAGGACAGAATCACCTAT
TTCGACAAAAATTACAATCTTCGTCGATTCATGTACTGTACACCCTTTACTTTAGATGGC
CGTGCCCATGGGGAACTTCATGAACAATTCAAAAGGAAGACCATTCTGACTACGTCTCAT
GCCTTTCCTTATATTAAAACAAGGGTCAATGTCACTCATAAAGAAGAGATCATCTTAACA
CCAATTGAAGTTGCTATTGAGGACATGCAGAAAAAGACACAGGAGTTGGCATTTGCAACA
CATCAGGATCCCGCAGACCCCAAAATGCTTCAGATGGTACTCCAGGGATCTGTAGGCACC
ACAGTGAATCAGGGGCCTTTGGAAGTTGCCCAGGTTTTTCTGTCTGAAATACCTAGTGAC
CCAAAGCTCTTCAGACATCATAATAAACTGCGACTCTGCTTTAAAGATTTTACTAAAAGG
TGTGAAGATGCCTTAAGAAAAAATAAGAGCTTAATTGGGCCGGATCAAAAGGAGTATCAA
AGGGAACTGGAGAGAAACTATCATCGCCTTAAAGAGGCCCTACAGCCACTGATCAACAGA
AAGATCCCTCAGTTATACAAGGCAGTATTGCCTGTCACCTGCCACAGAGATTCCTTCAGT
CGAATGAGCCTTCGCAAAATGGATCTCTAA
Enzyme 88 GenBank Gene ID Not Available
Enzyme 88 GeneCard ID DOCK7 Link Image
Enzyme 88 GenAtlas ID DOCK7 Link Image
Enzyme 88 HGNC ID HGNC:19190 Link Image
Enzyme 88 Chromosome Location 1
Enzyme 88 Locus 1p31.3
Enzyme 88 SNPs SNPJam Report Link Image
Enzyme 88 General References
  1. Watabe-Uchida M, John KA, Janas JA, Newey SE, Van Aelst L: The Rac activator DOCK7 regulates neuronal polarity through local phosphorylation of stathmin/Op18. Neuron. 2006 Sep 21;51(6):727-39. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Nagase T, Kikuno R, Hattori A, Kondo Y, Okumura K, Ohara O: Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Dec 31;7(6):347-55. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Cote JF, Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J Cell Sci. 2002 Dec 15;115(Pt 24):4901-13. [PubMed Link Image]
  7. Nellist M, Burgers PC, van den Ouweland AM, Halley DJ, Luider TM: Phosphorylation and binding partner analysis of the TSC1-TSC2 complex. Biochem Biophys Res Commun. 2005 Aug 5;333(3):818-26. [PubMed Link Image]
  8. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  9. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  10. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  11. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  12. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  13. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  14. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 88 Metabolite References Not Available
Enzyme 89 [top]
Enzyme 89 ID 14071
Enzyme 89 Name Dedicator of cytokinesis protein 8
Enzyme 89 Synonyms Not Available
Enzyme 89 Gene Name DOCK8
Enzyme 89 Protein Sequence >Dedicator of cytokinesis protein 8
MATLPSAERRAFALKINRYSSAEIRKQFTLPPNLGQYHRQSISTSGFPSLQLPQFYDPVE
PVDFEGLLMTHLNSLDVQLAQELGDFTDDDLDVVFTPKECRTLQPSLPEEGVELDPHVRD
CVQTYIREWLIVNRKNQGSPEICGFKKTGSRKDFHKTLPKQTFESETLECSEPAAQAGPR
HLNVLCDVSGKGPVTACDFDLRSLQPDKRLENLLQQVSAEDFEKQNEEARRTNRQAELFA
LYPSVDEEDAVEIRPVPECPKEHLGNRILVKLLTLKFEIEIEPLFASIALYDVKERKKIS
ENFHCDLNSDQFKGFLRAHTPSVAASSQARSAVFSVTYPSSDIYLVVKIEKVLQQGEIGD
CAEPYTVIKESDGGKSKEKIEKLKLQAESFCQRLGKYRMPFAWAPISLSSFFNVSTLERE
VTDVDSVVGRSSVGERRTLAQSRRLSERALSLEENGVGSNFKTSTLSVSSFFKQEGDRLS
DEDLFKFLADYKRSSSLQRRVKSIPGLLRLEISTAPEIINCCLTPEMLPVKPFPENRTRP
HKEILEFPTREVYVPHTVYRNLLYVYPQRLNFVNKLASARNITIKIQFMCGEDASNAMPV
IFGKSSGPEFLQEVYTAVTYHNKSPDFYEEVKIKLPAKLTVNHHLLFTFYHISCQQKQGA
SVETLLGYSWLPILLNERLQTGSYCLPVALEKLPPNYSMHSAEKVPLQNPPIKWAEGHKG
VFNIEVQAVSSVHTQDNHLEKFFTLCHSLESQVTFPIRVLDQKISEMALEHELKLSIICL
NSSRLEPLVLFLHLVLDKLFQLSVQPMVIAGQTANFSQFAFESVVAIANSLHNSKDLSKD
QHGRNCLLASYVHYVFRLPEVQRDVPKSGAPTALLDPRSYHTYGRTSAAAVSSKLLQARV
MSSSNPDLAGTHSAADEEVKNIMSSKIADRNCSRMSYYCSGSSDAPSSPAAPRPASKKHF
HEELALQMVVSTGMVRETVFKYAWFFFELLVKSMAQHVHNMDKRDSFRRTRFSDRFMDDI
TTIVNVVTSEIAALLVKPQKENEQAEKMNISLAFFLYDLLSLMDRGFVFNLIRHYCSQLS
AKLSNLPTLISMRLEFLRILCSHEHYLNLNLFFMNADTAPTSPCPSISSQNSSSCSSFQD
QKIASMFDLTSEYRQQHFLTGLLFTELAAALDAEGEGISKVQRKAVSAIHSLLSSHDLDP
RCVKPEVKVKIAALYLPLVGIILDALPQLCDFTVADTRRYRTSGSDEEQEGAGAINQNVA
LAIAGNNFNLKTSGIVLSSLPYKQYNMLNADTTRNLMICFLWIMKNADQSLIRKWIADLP
STQLNRILDLLFICVLCFEYKGKQSSDKVSTQVLQKSRDVKARLEEALLRGEGARGEMMR
RRAPGNDRFPGLNENLRWKKEQTHWRQANEKLDKTKAELDQEALISGNLATEAHLIILDM
QENIIQASSALDCKDSLLGGVLRVLVNSLNCDQSTTYLTHCFATLRALIAKFGDLLFEEE
VEQCFDLCHQVLHHCSSSMDVTRSQACATLYLLMRFSFGATSNFARVKMQVTMSLASLVG
RAPDFNEEHLRRSLRTILAYSEEDTAMQMTPFPTQVEELLCNLNSILYDTVKMREFQEDP
EMLMDLMYRIAKSYQASPDLRLTWLQNMAEKHTKKKCYTEAAMCLVHAAALVAEYLSMLE
DHSYLPVGSVSFQNISSNVLEESVVSEDTLSPDEDGVCAGQYFTESGLVGLLEQAAELFS
TGGLYETVNEVYKLVIPILEAHREFRKLTLTHSKLQRAFDSIVNKDHKRMFGTYFRVGFF
GSKFGDLDEQEFVYKEPAITKLPEISHRLEAFYGQCFGAEFVEVIKDSTPVDKTKLDPNK
AYIQITFVEPYFDEYEMKDRVTYFEKNFNLRRFMYTTPFTLEGRPRGELHEQYRRNTVLT
TMHAFPYIKTRISVIQKEEFVLTPIEVAIEDMKKKTLQLAVAINQEPPDAKMLQMVLQGS
VGATVNQGPLEVAQVFLAEIPADPKLYRHHNKLRLCFKEFIMRCGEAVEKNKRLITADQR
EYQQELKKNYNKLKENLRPMIERKIPELYKPIFRVESQKRDSFHRSSFRKCETQLSQGS
Enzyme 89 Number of Residues 2099
Enzyme 89 Molecular Weight 238526.7
Enzyme 89 Theoretical pI 6.86
Enzyme 89 GO Classification
Function
  • GTP binding
  • GTPase binding
  • GTPase regulator activity
  • binding
  • enzyme binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
Process
Component
Enzyme 89 General Function Involved in binding
Enzyme 89 Specific Function Potential guanine nucleotide exchange factor (GEF). GEF proteins activate some small GTPases by exchanging bound GDP for free GTP
Enzyme 89 Pathways Not Available
Enzyme 89 Reactions Not Available
Enzyme 89 Pfam Domain Function
Enzyme 89 Signals
  • None
Enzyme 89 Transmembrane Regions
  • None
Enzyme 89 Essentiality Not Available
Enzyme 89 GenBank ID Protein 76150613 Link Image
Enzyme 89 UniProtKB/Swiss-Prot ID Q8NF50 Link Image
Enzyme 89 UniProtKB/Swiss-Prot Entry Name DOCK8_HUMAN Link Image
Enzyme 89 PDB ID Not Available
Enzyme 89 Cellular Location Not Available
Enzyme 89 Gene Sequence >6300 bp
ATGGCCACTCTGCCGAGCGCAGAGCGCCGCGCGTTCGCGCTCAAGATCAACAGGTATTCT
TCAGTGGAAATAAGGAAACAGTTTACTCTCCCACCAAACCTTGGCCAGTACCATCGACAG
AGCATAAGTACCTCTGGCTTCCCCTCTCTTCAACTACCTCAGTTTTATGACCCTGTGGAG
CCAGTGGACTTTGAAGGACTTCTGATGACACACCTGAACAGCCTGGATGTGCAGCTTGCC
CAGGAGCTCGGGGACTTCACTGATGACGACTTGGACGTGGTGTTCACGACAAAGGAATGT
AGGACTTTGCAGCCCTCTTTGCCGGAGGAAGGGGTTGAACTGGACCCTCATGTCAGGGAC
TGTGTTCAGACCTACATCCGTGAGTGGCTAATCGTGAACCGGAAAAACCAAGGAAGTCCA
GAAATCTGTGGCTTTAAAAAGACTGGATCTCGAAAAGATTTTCACAAGACGCTTCCGAAA
CAGACGTTTGAGTCGGAAACCTTGGAGTGCAGTGAACCCGCTGCTCAGGCAGGCCCCCGC
CACTTAAACGTGCTGTGCGACGTGTCTGGGAAAGGCCCCGTCACTGCCTGTGACTTTGAC
CTCCGCAGCCTGCAGCCTGACAAGCGGCTAGAAAACCTCCTGCAGCAAGTGAGTGCCGAG
GACTTTGAGAAGCAGAACGAGGAGGCCCGGAGGACCAATAGGCAGGCCGAGCTCTTTGCC
CTTTACCCATCAGTGGACGAGGAGGATGCTGTGGAAATACGTCCAGTACCAGAATGTCCC
AAGGAACACCTGGGCAACAGAATATTGGTCAAGTTGCTGACCTTGAAGTTCGAGATTGAA
ATTGAGCCCCTGTTTGCCAGCATTGCCCTCTACGATGTTAAAGAAAGGAAAAAGATCTCA
GAAAATTTTCACTGTGACCTGAACTCTGACCAGTTCAAAGGATTTCTGCGAGCTCACACG
CCTTCAGTGGCCGCATCAAGTCAGGCGAGATCTGCAGTCTTCTCAGTCACCTACCCGTCC
TCAGACATCTACCTGGTAGTCAAGATTGAAAAAGTCCTGCAGCAGGGAGAGATTGGAGAC
TGTGCAGAGCCCTACACGGTTATCAAAGAAAGTGATGGTGGAAAGAGTAAAGAAAAGATT
GAAAAACTAAAACTCCAAGCTGAATCCTTCTGCCAGCGTTTGGGGAAATACCGGATGCCC
TTTGCCTGGGCACCCATAAGCTTATCAAGCTTCTTCAATGTCTCCACCCTTGAGAGGGAG
GTAACTGATGTGGACTCTGTGGTTGGGAGAAGCTCAGTGGGTGAACGGAGGACATTGGCC
CAATCTAGAAGGCTTTCTGAAAGAGCCCTCTCCTTGGAGGAAAATGGGGTTGGATCCAAC
TTCAAAACCTCCACTCTGAGCGTTAGCAGCTTTTTCAAGCAGGAAGGAGATCGCCTTAGC
GATGAAGACTTATTCAAGTTTTTAGCTGACTACAAAAGATCATCATCCTTACAGAGACGA
GTCAAGTCAATTCCAGGCTTGCTAAGACTGGAGATTTCTACAGCTCCAGAGATCATCAAT
TGCTGTCTGACTCCTGAAATGCTGCCCGTGAAACCCTTTCCTGAAAACCGGACACGCCCG
CACAAAGAGATTTTGGAATTTCCAACACGAGAAGTATATGTCCCTCACACTGTGTACAGA
AACCTTCTCTATGTCTACCCACAGAGGCTGAACTTTGTAAACAAACTAGCATCAGCCCGG
AACATTACAATAAAGATCCAGTTTATGTGTGGAGAAGATGCTAGCAATGCGATGCCGGTC
ATCTTTGGAAAGTCCAGCGGGCCTGAATTTCTGCAGGAAGTGTACACAGCTGTTACATAC
CATAATAAGTCTCCTGACTTTTATGAAGAAGTGAAAATTAAGCTCCCCGCTAAGCTCACA
GTAAATCACCACCTCCTGTTCACCTTCTACCATATCAGCTGTCAGCAGAAGCAAGGAGCC
TCCGTGGAAACTCTCCTGGGATATTCATGGCTGCCAATTCTCTTAAATGAACGTCTTCAA
ACTGGATCCTACTGTCTCCCAGTTGCCTTGGAAAAATTGCCACCCAACTACTCCATGCAT
TCTGCTGAGAAAGTCCCATTACAGAATCCTCCCATTAAGTGGGCTGAAGGACATAAGGGA
GTATTTAATATTGAAGTGCAAGCTGTTTCTTCTGTACACACCCAGGACAACCACCTGGAG
AAGTTCTTCACCCTCTGCCACTCCCTGGAGAGCCAGGTGACCTTCCCCATCCGCGTGCTG
GATCAGAAAATCAGCGAGATGGCGCTGGAGCATGAGCTGAAGCTCAGCATCATCTGCCTC
AACTCCTCCCGCCTGGAGCCGCTCGTGCTCTTCCTGCACCTGGTGCTGGACAAGCTCTTC
CAGCTGTCCGTGCAGCCCATGGTCATCGCTGGCCAGACAGCCAACTTCTCCCAGTTTGCC
TTCGAGTCCGTGGTGGCCATCGCCAACAGTCTGCACAACAGCAAGGACCTGAGCAAGGAC
CAGCATGGGAGGAACTGCCTGCTGGCTTCCTACGTGCACTACGTCTTCCGCCTGCCAGAG
GTGCAAAGGGATGTGCCCAAGTCAGGCGCTCCCACTGCCCTCCTAGACCCTCGGAGCTAC
CACACGTATGGCCGCACATCAGCTGCTGCTGTGAGTTCAAAGCTGCTGCAGGCCCGGGTG
ATGAGCAGCAGTAACCCAGACCTCGCGGGGACACACTCCGCAGCAGACGAGGAAGTGAAG
AACATCATGTCTTCAAAGATCGCCGATCGCAACTGCAGCCGAATGTCTTACTATTGCTCT
GGCAGTAGTGATGCTCCAAGTTCACCTGCAGCCCCAAGGCCAGCCAGCAAAAAGCATTTC
CATGAGGAGCTTGCCCTTCAGATGGTGGTCAGCACCGGAATGGTGAGAGAAACAGTCTTC
AAGTATGCCTGGTTCTTCTTTGAGCTTCTGGTGAAAAGCATGGCCCAGCACGTACATAAC
ATGGACAAACGGGACAGTTTTCGGAGGACTCGTTTTTCTGACCGTTTCATGGATGACATA
ACTACTATTGTTAATGTGGTCACCTCGGAAATTGCAGCCCTTTTAGTAAAACCACAGAAG
GAAAATGAACAGGCGGAAAAGATGAACATCAGCCTGGCTTTCTTCTTGTATGACCTTCTC
TCCCTCATGGATCGGGGCTTTGTGTTTAACCTCATCAGACATTATTGCAGCCAGCTGTCA
GCCAAGCTCAGTAACCTTCCAACGCTCATTTCCATGAGGCTAGAGTTCCTGAGAATCCTC
TGTAGCCATGAGCATTACCTCAATCTGAACCTTTTTTTTATGAATGCTGATACTGCTCCA
ACATCTCCTTGTCCTTCCATATCTTCCCAGAACTCAAGCTCCTGCTCCAGCTTCCAGGAC
CAGAAGATCGCCAGCATGTTCGATCTGACTTCCGAGTACCGCCAGCAGCACTTCCTCACC
GGGCTCCTCTTCACAGAACTGGCTGCTGCCCTGGATGCCGAAGGGGAAGGAATCAGCAAA
GTACAAAGGAAAGCTGTCAGTGCAATTCACAGCCTGCTAAGTTCTCACGACCTGGACCCA
CGCTGTGTCAAACCAGAGGTGAAGGTCAAAATCGCCGCCCTTTACCTACCTTTAGTTGGC
ATCATTTTGGATGCTTTGCCACAGCTCTGTGACTTTACAGTTGCAGATACTCGCAGATAC
CGCACCAGTGGCTCGGATGAAGAACAAGAAGGAGCCGGTGCCATTAACCAGAATGTGGCT
CTGGCCATAGCAGGGAATAATTTCAATTTGAAAACAAGTGGAATAGTGCTGTCTTCCTTG
CCCTATAAGCAGTACAACATGCTGAACGCGGACACTACTCGCAACCTCATGATCTGCTTC
CTCTGGATCATGAAAAATGCTGATCAGAGCCTCATTAGGAAGTGGATTGCTGACCTGCCA
TCAACGCAGCTCAACAGGATTTTAGATCTACTTTTCATCTGTGTGTTATGTTTTGAGTAT
AAGGGAAAACAGAGTTCTGACAAAGTCAGTACCCAAGTCCTGCAGAAGTCAAGGGATGTC
AAGGCCCGGCTGGAAGAGGCTTTGCTCCGTGGGGAAGGGGCCAGAGGGGAGATGATGCGC
CGCCGGGCTCCAGGGAACGACCGATTTCCAGGCCTAAATGAAAATTTGAGATGGAAGAAA
GAGCAGACACATTGGCGGCAAGCTAATGAGAAGCTAGATAAAACAAAGGCCGAGTTAGAT
CAAGAAGCCTTGATCAGTGGCAATCTGGCTACAGAAGCACATTTAATCATCCTGGATATG
CAGGAAAACATTATCCAGGCGAGCTCGGCTCTGGACTGTAAAGACAGCCTGCTGGGAGGT
GTTCTGAGGGTGCTGGTGAATTCTCTGAACTGTGATCAGAGTACCACCTACCTGACTCAC
TGCTTTGCAACACTCCGTGCTCTCATCGCCAAGTTTGGAGACTTACTCTTCGAAGAGGAG
GTGGAACAGTGTTTCGACCTATGTCACCAAGTCCTGCACCACTGCAGCAGCAGCATGGAT
GTCACCCGGAGCCAAGCCTGTGCCACCCTTTACCTCCTCATGAGGTTCAGTTTTGGAGCC
ACCAGTAATTTTGCAAGAGTAAAGATGCAAGTAACCATGTCCCTGGCATCTTTGGTGGGA
AGAGCACCAGACTTTAATGAAGAGCACCTGAGAAGATCCTTGAGGACAATTTTGGCCTAT
TCAGAAGAGGACACAGCCATGCAGATGACTCCTTTTCCCACCCAGGTGGAGGAACTTCTC
TGTAATCTGAATAGCATCTTATATGACACAGTGAAAATGAGGGAATTTCAGGAAGATCCT
GAGATGCTTATGGATCTCATGTACAGAATTGCCAAGAGTTACCAGGCATCTCCTGATCTG
CGGCTGACCTGGCTCCAGAACATGGCAGAGAAACACACCAAGAAGAAGTGCTACACGGAG
GCTGCCATGTGCCTGGTGCACGCCGCTGCGTTAGTGGCTGAGTATCTGAGCATGCTGGAG
GACCACAGCTACCTGCCCGTGGGCAGTGTCAGCTTCCAGAATATTTCTTCCAATGTGCTG
GAGGAGTCTGTGGTCTCTGAGGACACCCTGTCACCTGACGAGGATGGGGTGTGCGCAGGC
CAGTACTTCACCGAGAGTGGCCTGGTAGGCCTCCTGGAGCAGGCCGCGGAGCTCTTCAGC
ACGGGAGGCTTATATGAGACAGTTAATGAGGTCTACAAGCTGGTCATCCCCATCCTAGAA
GCGCATCGAGAATTCCGGAAGCTGACACTCACTCACAGCAAGCTGCAGAGAGCCTTCGAC
AGCATCGTTAACAAGGATCATAAGAGAATGTTTGGAACCTACTTCCGAGTTGGTTTCTTT
GGATCCAAATTTGGGGATTTGGATGAACAGGAGTTTGTCTACAAAGAGCCTGCAATTACC
AAGCTTCCTGAGATCTCACATAGACTAGAGGCATTTTATGGTCAATGTTTTGGTGCAGAA
TTTGTGGAAGTGATTAAAGACTCCACTCCTGTGGACAAAACCAAGTTGGATCCTAACAAG
GCCTACATACAGATCACTTTTGTGGAGCCCTACTTTGATGAGTATGAGATGAAAGACAGG
GTCACATACTTTGAGAAGAATTTCAACCTCCGGAGGTTCATGTACACCACCCCGTTCACC
CTGGAGGGGCGGCCTCGGGGAGAGCTGCATGAGCAGTACAGAAGGAACACAGTCCTGACC
ACTATGCACGCCTTCCCCTACATCAAGACCAGGATCAGCGTCATCCAGAAGGAGGAGTTT
GTTTTGACACCGATTGAAGTTGCCATTGAAGACATGAAGAAGAAGACCCTGCAGTTAGCA
GTTGCCATTAACCAGGAGCCGCCTGATGCAAAGATGCTTCAGATGGTGCTGCAAGGCTCT
GTGGGAGCTACTGTAAATCAGGGACCACTGGAAGTAGCCCAAGTGTTTTTGGCTGAAATT
CCTGCTGATCCAAAACTCTATCGACATCACAACAAGTTGAGGTTATGCTTTAAGGAATTC
ATCATGAGATGTGGTGAAGCTGTAGAGAAAAACAAGCGTCTCATCACGGCAGACCAGAGG
GAATATCAGCAGGAACTCAAAAAGAACTATAACAAGCTAAAAGAGAACCTCAGGCCAATG
ATCGAGCGGAAAATTCCAGAACTGTACAAGCCAATATTCAGAGTTGAGAGTCAAAAGAGG
GACTCCTTCCACAGATCTAGTTTCAGGAAATGTGAAACCCAGTTGTCACAGGGCAGCTAA
Enzyme 89 GenBank Gene ID AB191037 Link Image
Enzyme 89 GeneCard ID DOCK8 Link Image
Enzyme 89 GenAtlas ID DOCK8 Link Image
Enzyme 89 HGNC ID HGNC:19191 Link Image
Enzyme 89 Chromosome Location 9
Enzyme 89 Locus 9p24.3
Enzyme 89 SNPs SNPJam Report Link Image
Enzyme 89 General References
  1. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Jikuya H, Takano J, Kikuno R, Hirosawa M, Nagase T, Nomura N, Ohara O: Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones. DNA Res. 2003 Feb 28;10(1):49-57. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Ottolenghi C, Veitia R, Quintana-Murci L, Torchard D, Scapoli L, Souleyreau-Therville N, Beckmann J, Fellous M, McElreavey K: The region on 9p associated with 46,XY sex reversal contains several transcripts expressed in the urogenital system and a novel doublesex-related domain. Genomics. 2000 Mar 1;64(2):170-8. [PubMed Link Image]
  7. Cote JF, Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J Cell Sci. 2002 Dec 15;115(Pt 24):4901-13. [PubMed Link Image]
  8. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
Enzyme 89 Metabolite References Not Available
Enzyme 90 [top]
Enzyme 90 ID 14075
Enzyme 90 Name Dynamin-1
Enzyme 90 Synonyms Not Available
Enzyme 90 Gene Name DNM1
Enzyme 90 Protein Sequence >Dynamin-1
MGNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRG
SGIVTRRPLVLQLVNATTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPI
NLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSD
LANSDALKVAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQK
DIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLPGLRNKL
QSQLLSIEKEVEEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSGDQIDTYELSGGA
RINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKI
REPCLKCVDMVISELISTVRQCTKKLQQYPRLREEMERIVTTHIREREGRTKEQVMLLID
IELAYMNTNHEDFIGFANAQQRSNQMNKKKTSGNQDEILVIRKGWLTINNIGIMKGGSKE
YWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDY
RQLELACETQEEVDSWKASFLRAGVYPERVGDKEKASETEENGSDSFMHSMDPQLERQVE
TIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAE
QAQRRDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPT
PQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAP
PGVPSRSGQASPSRPESPRPPFDL
Enzyme 90 Number of Residues 864
Enzyme 90 Molecular Weight 97407.5
Enzyme 90 Theoretical pI 7.17
Enzyme 90 GO Classification
Function
  • GTP binding
  • GTPase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
Process
Component
Enzyme 90 General Function Involved in GTP binding
Enzyme 90 Specific Function Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis
Enzyme 90 Pathways Not Available
Enzyme 90 Reactions
  • GTP + H2O = GDP + phosphate [RN:R00335]
Enzyme 90 Pfam Domain Function
Enzyme 90 Signals
  • None
Enzyme 90 Transmembrane Regions
  • None
Enzyme 90 Essentiality Not Available
Enzyme 90 GenBank ID Protein 55961114 Link Image
Enzyme 90 UniProtKB/Swiss-Prot ID Q05193 Link Image
Enzyme 90 UniProtKB/Swiss-Prot Entry Name DYN1_HUMAN Link Image
Enzyme 90 PDB ID Not Available
Enzyme 90 Cellular Location Not Available
Enzyme 90 Gene Sequence >2595 bp
ATGGGCAACCGCGGCATGGAAGATCTCATCCCGCTGGTCAACCGGCTGCAAGACGCCTTC
TCTGCCATCGGCCAGAACGCGGACCTCGACCTGCCGCAGATCGCTGTGGTGGGCGGCCAG
AGCGCCGGCAAGAGCTCGGTGCTCGAGAATTTCGTAGGCAGGGACTTCTTGCCTCGAGGA
TCTGGCATTGTCACCCGACGTCCCCTGGTCTTGCAGCTGGTCAATGCAACCACAGAATAT
GCCGAGTTCCTGCACTGCAAGGGAAAGAAATTCACCGACTTCGAGGAGGTGCGCCTTGAG
ATCGAGGCCGAGACCGACAGGGTCACCGGCACCAACAAGGGCATCTCGCCGGTGCCTATC
AACCTCCGCGTCTACTCGCCGCACGTGCTGAACCTGACCCTGGTGGACCTGCCCGGAATG
ACCAAGGTCCCGGTGGGGGACCAACCTCCCGACATCGAGTTCCAGATCCGAGACATGCTT
ATGCAGTTTGTCACCAAGGAGAACTGCCTCATCCTGGCCGTGTCCCCCGCCAACTCTGAC
CTGGCCAATTCTGACGCCCTCAAGGTCGCCAAGGAGGTGGACCCCCAGGGCCAGCGCACC
ATCGGGGTCATCACCAAGCTGGACCTGATGGACGAGGGCACAGATGCCCGTGATGTGCTG
GAGAACAAGCTGCTCCCCCTGCGCAGAGGCTACATTGGAGTGGTGAACCGGAGCCAGAAG
GACATTGATGGCAAGAAGGACATTACCGCCGCCTTGGCTGCTGAACGAAAGTTCTTCCTC
TCCCATCCATCTTATCGCCACTTGGCTGACCGTATGGGCACGCCCTACCTGCAGAAGGTC
CTCAATCAGCAACTGACGAACCACATCCGGGACACACTGCCGGGGCTGCGGAACAAGCTG
CAGAGCCAGCTACTGTCCATTGAGAAGGAGGTGGAGGAATACAAGAACTTCCGCCCTGAT
GACCCAGCTCGCAAGACCAAGGCCCTGCTGCAGATGGTCCAGCAGTTCGCCGTAGACTTT
GAGAAGCGCATTGAGGGCTCAGGAGATCAGATCGACACCTACGAACTGTCAGGGGGAGCC
CGCATTAACCGAATCTTCCACGAGCGCTTCCCTTTCGAGCTGGTCAAGATGGAGTTTGAT
GAGAAGGAACTCCGAAGGGAGATCAGCTATGCTATCAAGAATATCCATGGCATTAGAACG
GGGCTGTTTACCCCAGACATGGCCTTTGAGACCATTGTGAAAAAGCAGGTGAAGAAGATC
CGAGAACCGTGTCTCAAGTGTGTGGACATGGTTATCTCGGAGCTAATCAGCACCGTTAGA
CAGTGCACCAAGAAGCTCCAGCAGTACCCGCGGCTACGGGAGGAGATGGAGCGCATCGTG
ACCACCCACATCCGGGAGCGCGAGGGCCGCACTAAGGAGCAGGTCATGCTTCTCATCGAT
ATCGAGCTGGCTTACATGAACACCAACCATGAGGACTTCATAGGCTTTGCCAATGCTCAG
CAGAGGAGCAACCAGATGAACAAGAAGAAGACTTCAGGGAACCAGGATGAGATTCTGGTC
ATCCGCAAGGGCTGGCTGACTATCAATAATATTGGCATCATGAAAGGGGGCTCCAAGGAG
TACTGGTTTGTGCTGACTGCTGAGAATCTGTCCTGGTACAAGGATGATGAGGAGAAAGAG
AAGAAATACATGCTGTCTGTGGACAACCTCAAGCTGCGGGACGTGGAGAAGGGCTTTATG
TCGAGCAAGCATATCTTTGCCCTCTTTAACACGGAGCAGAGGAATGTCTACAAGGATTAT
CGGCAGCTGGAGCTAGCCTGTGAGACACAGGAGGAGGTGGACAGCTGGAAGGCCTCCTTC
CTGAGGGCTGGCGTGTACCCTGAGCGTGTTGGGGACAAAGAGAAAGCCAGCGAGACCGAG
GAGAATGGCTCCGACAGCTTCATGCATTCCATGGACCCACAGCTGGAACGGCAAGTGGAG
ACCATCCGGAATCTTGTGGACTCATACATGGCCATTGTCAACAAGACCGTGAGGGACCTC
ATGCCCAAGACCATCATGCACCTCATGATTAACAATACCAAGGAGTTCATCTTCTCGGAG
CTGCTGGCCAACCTGTACTCGTGTGGGGACCAGAACACGCTGATGGAGGAGTCGGCGGAG
CAGGCACAGCGGCGCGACGAGATGCTGCGCATGTACCACGCACTGAAGGAGGCGCTCAGC
ATCATCGGCGACATCAACACGACCACCGTCAGCACGCCCATGCCCCCGCCCGTGGACGAC
TCCTGGCTGCAGGTGCAGAGCGTACCGGCCGGACGCAGGTCGCCCACGTCCAGCCCCACG
CCGCAGCGCCGAGCCCCCGCCGTGCCCCCAGCCCGGCCCGGGTCGCGGGGCCCTGCTCCT
GGGCCTCCGCCTGCTGGGTCCGCCCTGGGGGGGGCGCCCCCCGTGCCCTCCAGGCCGGGG
GCTTCCCCTGACCCTTTCGGCCCTCCCCCTCAGGTGCCCTCGCGCCCCAACCGCGCCCCG
CCCGGGGTCCCCAGCCGATCGGGTCAGGCAAGTCCATCCCGTCCTGAGAGCCCCAGGCCC
CCCTTCGACCTCTAA
Enzyme 90 GenBank Gene ID AL590708 Link Image
Enzyme 90 GeneCard ID DNM1 Link Image
Enzyme 90 GenAtlas ID DNM1 Link Image
Enzyme 90 HGNC ID HGNC:2972 Link Image
Enzyme 90 Chromosome Location 9
Enzyme 90 Locus 9q34
Enzyme 90 SNPs SNPJam Report Link Image
Enzyme 90 General References
  1. van der Bliek AM, Redelmeier TE, Damke H, Tisdale EJ, Meyerowitz EM, Schmid SL: Mutations in human dynamin block an intermediate stage in coated vesicle formation. J Cell Biol. 1993 Aug;122(3):553-63. [PubMed Link Image]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  5. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  6. Downing AK, Driscoll PC, Gout I, Salim K, Zvelebil MJ, Waterfield MD: Three-dimensional solution structure of the pleckstrin homology domain from dynamin. Curr Biol. 1994 Oct 1;4(10):884-91. [PubMed Link Image]
  7. Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB: Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin. Cell. 1994 Oct 21;79(2):199-209. [PubMed Link Image]
  8. Timm D, Salim K, Gout I, Guruprasad L, Waterfield M, Blundell T: Crystal structure of the pleckstrin homology domain from dynamin. Nat Struct Biol. 1994 Nov;1(11):782-8. [PubMed Link Image]
Enzyme 90 Metabolite References Not Available
Enzyme 91 [top]
Enzyme 91 ID 14076
Enzyme 91 Name Dynamin-2
Enzyme 91 Synonyms Not Available
Enzyme 91 Gene Name DNM2
Enzyme 91 Protein Sequence >Dynamin-2
MGNRGMEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRG
SGIVTRRPLILQLIFSKTEHAEFLHCKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPI
NLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFISRESSLILAVTPANMD
LANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQK
DIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLPALRSKL
QSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSGDQVDTLELSGGA
RINRIFHERFPFELVKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKL
KEPCLKCVDLVIQELINTVRQCTSKLSSYPRLREETERIVTTYIREREGRTKDQILLLID
IEQSYINTNHEDFIGFANAQQRSTQLNKKRAIPNQGEILVIRRGWLTINNISLMKGGSKE
YWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDL
RQIELACDSQEDVDSWKASFLRAGVYPEKDQAENEDGAQENTFSMDPQLERQVETIRNLV
DSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESADQAQRRD
DMLRMYHALKEALNIIGDISTSTVSTPVPPPVDDTWLQSASSHSPTPQRRPVSSIHPPGR
PPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPQSVFANSDLFPAPPQIPSRPVRIPP
GIPPGVPSRRPPAAPSRPTIIRPAEPSLLD
Enzyme 91 Number of Residues 870
Enzyme 91 Molecular Weight 98063.3
Enzyme 91 Theoretical pI 7.50
Enzyme 91 GO Classification
Function
  • GTP binding
  • GTPase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
Process
Component
Enzyme 91 General Function Involved in GTP binding
Enzyme 91 Specific Function Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes, in particular endocytosis
Enzyme 91 Pathways Not Available
Enzyme 91 Reactions
  • GTP + H2O = GDP + phosphate [RN:R00335]
Enzyme 91 Pfam Domain Function
Enzyme 91 Signals
  • None
Enzyme 91 Transmembrane Regions
  • None
Enzyme 91 Essentiality Not Available
Enzyme 91 GenBank ID Protein 56549121 Link Image
Enzyme 91 UniProtKB/Swiss-Prot ID P50570 Link Image
Enzyme 91 UniProtKB/Swiss-Prot Entry Name DYN2_HUMAN Link Image
Enzyme 91 PDB ID Not Available
Enzyme 91 Cellular Location Not Available
Enzyme 91 Gene Sequence >2613 bp
ATGGGCAACCGCGGGATGGAAGAGCTGATCCCGCTGGTCAACAAACTGCAGGACGCCTTC
AGCTCCATCGGCCAGAGCTGCCACCTGGACCTGCCGCAGATCGCTGTAGTGGGCGGCCAG
AGCGCCGGCAAGAGCTCGGTGCTGGAGAACTTCGTGGGCCGGGACTTCCTTCCCCGCGGT
TCAGGAATCGTCACCCGGCGGCCTCTCATTCTGCAGCTCATCTTCTCAAAAACAGAACAT
GCCGAGTTTTTGCACTGCAAGTCCAAAAAGTTTACAGACTTTGATGAAGTCCGGCAGGAG
ATTGAAGCAGAGACCGACAGGGTCACGGGGACCAACAAAGGCATCTCCCCAGTGCCCATC
AACCTTCGAGTCTACTCGCCACACGTGTTGAACTTGACCCTCATCGACCTCCCGGGTATC
ACCAAGGTGCCTGTGGGCGACCAGCCTCCAGACATCGAGTACCAGATCAAGGACATGATC
CTGCAGTTCATCAGCCGGGAGAGCAGCCTCATTCTGGCTGTCACGCCCGCCAACATGGAC
CTGGCCAACTCCGACGCCCTCAAGCTGGCCAAGGAAGTCGATCCCCAAGGCCTACGGACC
ATCGGTGTCATCACCAAGCTTGACCTGATGGACGAGGGCACCGACGCCAGGGACGTCTTG
GAGAACAAGTTGCTCCCGTTGAGAAGAGGCTACATTGGCGTGGTGAACCGCAGCCAGAAG
GATATTGAGGGCAAGAAGGACATCCGTGCAGCACTGGCAGCTGAGAGGAAGTTCTTCCTC
TCCCACCCGGCCTACCGGCACATGGCCGACCGCATGGGCACGCCACATCTGCAGAAGACG
CTGAATCAGCAACTGACCAACCACATCCGGGAGTCGCTGCCGGCCCTACGTAGCAAACTA
CAGAGCCAGCTGCTGTCCCTGGAGAAGGAGGTGGAGGAGTACAAGAACTTTCGGCCCGAC
GACCCCACCCGCAAAACCAAAGCCCTGCTGCAGATGGTCCAGCAGTTTGGGGTGGATTTT
GAGAAGAGGATCGAGGGCTCAGGAGATCAGGTGGACACTCTGGAGCTCTCCGGGGGCGCC
CGAATCAATCGCATCTTCCACGAGCGGTTCCCATTTGAGCTGGTGAAGATGGAGTTTGAC
GAGAAGGACTTACGACGGGAGATCAGCTATGCCATTAAGAACATCCATGGAGTCAGGACC
GGGCTTTTCACCCCGGACTTGGCATTCGAGGCCATTGTGAAAAAGCAGGTCGTCAAGCTG
AAAGAGCCCTGTCTGAAATGTGTCGACCTGGTTATCCAGGAGCTAATCAATACAGTTAGG
CAGTGTACCAGTAAGCTCAGTTCCTACCCCCGGTTGCGAGAGGAGACAGAGCGAATCGTC
ACCACTTACATCCGGGAACGGGAGGGGAGAACGAAGGACCAGATTCTTCTGCTGATCGAC
ATTGAGCAGTCCTACATCAACACGAACCATGAGGACTTCATCGGGTTTGCCAATGCCCAG
CAGAGGAGCACGCAGCTGAACAAGAAGAGAGCCATCCCCAATCAGGGGGAGATCCTGGTG
ATCCGCAGGGGCTGGCTGACCATCAACAACATCAGCCTGATGAAAGGCGGCTCCAAGGAG
TACTGGTTTGTGCTGACTGCCGAGTCACTGTCCTGGTACAAGGATGAGGAGGAGAAAGAG
AAGAAGTACATGCTGCCTCTGGACAACCTCAAGATCCGTGATGTGGAGAAGGGCTTCATG
TCCAACAAGCACGTCTTCGCCATCTTCAACACGGAGCAGAGAAACGTCTACAAGGACCTG
CGGCAGATCGAGCTGGCCTGTGACTCCCAGGAAGACGTGGACAGCTGGAAGGCCTCGTTC
CTCCGAGCTGGCGTCTACCCCGAGAAGGACCAGGCAGAAAACGAGGATGGGGCCCAGGAG
AACACCTTCTCCATGGACCCCCAACTGGAGCGGCAGGTGGAGACCATTCGCAACCTGGTG
GACTCATACGTGGCCATCATCAACAAGTCCATCCGCGACCTCATGCCAAAGACCATCATG
CACCTCATGATCAACAATACGAAGGCCTTCATCCACCACGAGCTGCTGGCCTACCTATAC
TCCTCGGCAGACCAGAGCAGCCTCATGGAGGAGTCGGCTGACCAGGCACAGCGGCGGGAC
GACATGCTGCGCATGTACCATGCCCTCAAGGAGGCGCTCAACATCATCGGTGACATCAGC
ACCAGCACTGTGTCCACGCCTGTACCCCCGCCTGTCGATGACACCTGGCTCCAGAGCGCC
AGCAGCCACAGCCCCACTCCACAGCGCCGACCGGTGTCCAGCATACACCCCCCTGGCCGG
CCCCCAGCAGTGAGGGGCCCCACTCCAGGGCCCCCCCTGATTCCTGTTCCCGTGGGGGCA
GCAGCCTCCTTCTCGGCGCCCCCAATCCCATCCCGGCCTGGACCCCAGAGCGTGTTTGCC
AACAGTGACCTCTTCCCAGCCCCGCCTCAGATCCCATCTCGGCCAGTTCGGATCCCCCCA
GGGATTCCCCCAGGAGTGCCCAGCAGAAGACCCCCTGCTGCGCCCAGCCGGCCCACCATT
ATCCGCCCAGCCGAGCCATCCCTGCTCGACTAG
Enzyme 91 GenBank Gene ID NM_001005360.2 Link Image
Enzyme 91 GeneCard ID DNM2 Link Image
Enzyme 91 GenAtlas ID DNM2 Link Image
Enzyme 91 HGNC ID HGNC:2974 Link Image
Enzyme 91 Chromosome Location 1
Enzyme 91 Locus 19p13.2
Enzyme 91 SNPs SNPJam Report Link Image
Enzyme 91 General References
  1. Diatloff-Zito C, Gordon AJ, Duchaud E, Merlin G: Isolation of an ubiquitously expressed cDNA encoding human dynamin II, a member of the large GTP-binding protein family. Gene. 1995 Oct 3;163(2):301-6. [PubMed Link Image]
  2. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Okamoto PM, Gamby C, Wells D, Fallon J, Vallee RB: Dynamin isoform-specific interaction with the shank/ProSAP scaffolding proteins of the postsynaptic density and actin cytoskeleton. J Biol Chem. 2001 Dec 21;276(51):48458-65. Epub 2001 Oct 2. [PubMed Link Image]
  5. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  6. Tosoni D, Puri C, Confalonieri S, Salcini AE, De Camilli P, Tacchetti C, Di Fiore PP: TTP specifically regulates the internalization of the transferrin receptor. Cell. 2005 Dec 2;123(5):875-88. [PubMed Link Image]
  7. Icking A, Matt S, Opitz N, Wiesenthal A, Muller-Esterl W, Schilling K: NOSTRIN functions as a homotrimeric adaptor protein facilitating internalization of eNOS. J Cell Sci. 2005 Nov 1;118(Pt 21):5059-69. Epub 2005 Oct 18. [PubMed Link Image]
  8. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  10. Zuchner S, Noureddine M, Kennerson M, Verhoeven K, Claeys K, De Jonghe P, Merory J, Oliveira SA, Speer MC, Stenger JE, Walizada G, Zhu D, Pericak-Vance MA, Nicholson G, Timmerman V, Vance JM: Mutations in the pleckstrin homology domain of dynamin 2 cause dominant intermediate Charcot-Marie-Tooth disease. Nat Genet. 2005 Mar;37(3):289-94. Epub 2005 Jan 30. [PubMed Link Image]
  11. Bitoun M, Maugenre S, Jeannet PY, Lacene E, Ferrer X, Laforet P, Martin JJ, Laporte J, Lochmuller H, Beggs AH, Fardeau M, Eymard B, Romero NB, Guicheney P: Mutations in dynamin 2 cause dominant centronuclear myopathy. Nat Genet. 2005 Nov;37(11):1207-9. Epub 2005 Oct 16. [PubMed Link Image]
  12. Bitoun M, Bevilacqua JA, Prudhon B, Maugenre S, Taratuto AL, Monges S, Lubieniecki F, Cances C, Uro-Coste E, Mayer M, Fardeau M, Romero NB, Guicheney P: Dynamin 2 mutations cause sporadic centronuclear myopathy with neonatal onset. Ann Neurol. 2007 Dec;62(6):666-70. [PubMed Link Image]
  13. Fabrizi GM, Ferrarini M, Cavallaro T, Cabrini I, Cerini R, Bertolasi L, Rizzuto N: Two novel mutations in dynamin-2 cause axonal Charcot-Marie-Tooth disease. Neurology. 2007 Jul 17;69(3):291-5. [PubMed Link Image]
  14. Bitoun M, Durieux AC, Prudhon B, Bevilacqua JA, Herledan A, Sakanyan V, Urtizberea A, Cartier L, Romero NB, Guicheney P: Dynamin 2 mutations associated with human diseases impair clathrin-mediated receptor endocytosis. Hum Mutat. 2009 Oct;30(10):1419-27. [PubMed Link Image]
Enzyme 91 Metabolite References Not Available
Enzyme 92 [top]
Enzyme 92 ID 14081
Enzyme 92 Name Elongation factor G, mitochondrial
Enzyme 92 Synonyms
  1. EF-Gmt
  2. Elongation factor G 1, mitochondrial
  3. mEF-G 1
  4. Elongation factor G1
  5. hEFG1
Enzyme 92 Gene Name GFM1
Enzyme 92 Protein Sequence >Elongation factor G, mitochondrial
MRLLGAAAVAALGRGRAPASLGWQRKQVNWKACRWSSSGVIPNEKIRNIGISAHIDSGKT
TLTERVLYYTGRIAKMHEVKGKDGVGAVMDSMELERQRGITIQSAATYTMWKDVNINIID
TPGHVDFTIEVERALRVLDGAVLVLCAVGGVQCQTMTVNRQMKRYNVPFLTFINKLDRMG
SNPARALQQMRSKLNHNAAFMQIPMGLEGNFKGIVDLIEERAIYFDGDFGQIVRYGEIPA
ELRAAATDHRQELIECVANSDEQLGEMFLEEKIPSISDLKLAIRRATLKRSFTPVFLGSA
LKNKGVQPLLDAVLEYLPNPSEVQNYAILNKEDDSKEKTKILMNSSRDNSHPFVGLAFKL
EVGRFGQLTYVRSYQGELKKGDTIYNTRTRKKVRLQRLARMHADMMEDVEEVYAGDICAL
FGIDCASGDTFTDKANSGLSMESIHVPDPVISIAMKPSNKNDLEKFSKGIGRFTREDPTF
KVYFDTENKETVISGMGELHLEIYAQRLEREYGCPCITGKPKVAFRETITAPVPFDFTHK
KQSGGAGQYGKVIGVLEPLDPEDYTKLEFSDETFGSNIPKQFVPAVEKGFLDACEKGPLS
GHKLSGLRFVLQDGAHHMVDSNEISFIRAGEGALKQALANATLCILEPIMAVEVVAPNEF
QGQVIAGINRRHGVITGQDGVEDYFTLYADVPLNDMFGYSTELRSCTEGKGEYTMEYSRY
QPCLPSTQEDVINKYLEATGQLPVKKGKAKN
Enzyme 92 Number of Residues 751
Enzyme 92 Molecular Weight 83470.9
Enzyme 92 Theoretical pI 7.01
Enzyme 92 GO Classification
Function
  • GTP binding
  • GTPase activity
  • RNA binding
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleic acid binding
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • translation elongation factor activity
  • translation factor activity, nucleic acid binding
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • translational elongation
Component
  • cell part
  • intracellular
Enzyme 92 General Function Involved in GTPase activity
Enzyme 92 Specific Function Mitochondrial GTPase that plays a central role in protein elongation by promoting the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site of the ribosome. Does not mediate the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis
Enzyme 92 Pathways Not Available
Enzyme 92 Reactions Not Available
Enzyme 92 Pfam Domain Function
Enzyme 92 Signals
  • None
Enzyme 92 Transmembrane Regions
  • None
Enzyme 92 Essentiality Not Available
Enzyme 92 GenBank ID Protein 18390331 Link Image
Enzyme 92 UniProtKB/Swiss-Prot ID Q96RP9 Link Image
Enzyme 92 UniProtKB/Swiss-Prot Entry Name EFGM_HUMAN Link Image
Enzyme 92 PDB ID Not Available
Enzyme 92 Cellular Location Not Available
Enzyme 92 Gene Sequence >2256 bp
ATGAGACTCCTGGGAGCTGCAGCCGTCGCGGCTCTGGGGCGCGGAAGGGCCCCCGCCTCC
CTAGGCTGGCAGAGGAAGCAGGTTAATTGGAAGGCCTGCCGATGGTCTTCATCAGGGGTG
ATTCCTAATGAAAAAATACGAAATATTGGAATCTCAGCTCACATTGATTCTGGGAAAACT
ACATTAACAGAACGAGTCCTTTACTACACTGGCAGAATTGCAAAGATGCATGAGGTGAAA
GGTAAAGATGGAGTTGGTGCTGTCATGGATTCCATGGAACTAGAGAGACAAAGAGGAATC
ACTATTCAGTCAGCAGCCACTTACACCATGTGGAAAGATGTCAATATTAACATTATAGAT
ACTCCTGGGCATGTGGACTTCACAATAGAAGTGGAAAGGGCCCTGAGAGTGTTGGATGGT
GCAGTCCTTGTTCTCTGTGCTGTTGGAGGGGTACAGTGCCAGACCATGACTGTCAATCGT
CAGATGAAGCGCTACAACGTTCCGTTTCTAACTTTTATTAACAAATTGGACCGAATGGGC
TCCAACCCAGCCAGGGCCCTGCAGCAAATGAGGTCTAAACTAAATCATAATGCAGCGTTT
ATGCAGATACCCATGGGTTTGGAGGGTAATTTTAAAGGTATTGTAGATCTTATTGAGGAA
CGAGCCATCTATTTTGATGGAGACTTTGGTCAGATTGTTCGATATGGTGAGATTCCAGCT
GAATTAAGGGCGGCGGCCACTGACCACCGGCAGGAGCTAATTGAATGTGTTGCCAATTCA
GATGAACAGCTTGGTGAGATGTTTCTGGAAGAAAAAATCCCCTCGATTTCTGATTTAAAG
CTAGCAATTCGAAGAGCTACTCTGAAAAGATCATTTACTCCTGTATTTTTGGGAAGCGCC
TTGAAGAACAAAGGAGTTCAGCCTCTTTTAGATGCTGTTTTAGAATACCTCCCAAATCCA
TCTGAAGTCCAGAACTATGCTATTCTCAATAAAGAGGATGACTCAAAAGAGAAAACCAAA
ATCCTAATGAACTCCAGTAGAGACAATTCCCACCCATTTGTAGGCCTGGCTTTTAAACTG
GAGGTAGGTCGATTTGGACAATTAACTTATGTTCGCAGTTATCAGGGAGAGCTAAAGAAG
GGTGACACCATCTATAACACAAGGACAAGAAAGAAAGTACGGTTGCAACGGCTGGCTCGC
ATGCATGCCGACATGATGGAGGATGTTGAGGAAGTATATGCCGGAGACATCTGTGCATTG
TTTGGCATTGACTGTGCTAGTGGAGACACATTCACAGACAAAGCCAACAGCGGCCTTTCT
ATGGAGTCAATTCATGTTCCTGATCCTGTCATTTCAATAGCAATGAAGCCTTCTAACAAG
AACGATCTGGAAAAATTTTCAAAAGGTATTGGCAGGTTTACAAGAGAAGATCCCACATTT
AAAGTATACTTTGACACTGAGAACAAAGAGACAGTTATATCTGGAATGGGAGAATTACAC
CTGGAAATCTATGCTCAGAGGCTGGAAAGAGAGTATGGCTGTCCTTGTATCACAGGAAAG
CCAAAAGTTGCCTTTCGAGAGACCATTACTGCCCCTGTCCCGTTTGACTTTACACATAAA
AAACAATCAGGTGGTGCAGGCCAGTATGGAAAAGTAATAGGTGTCCTGGAGCCTCTGGAC
CCAGAGGACTACACTAAATTGGAATTTTCAGATGAAACATTCGGATCAAATATTCCAAAG
CAGTTTGTGCCTGCTGTAGAAAAGGGGTTTTTAGATGCCTGCGAGAAGGGCCCTCTTTCT
GGTCACAAGCTCTCTGGGCTCCGGTTTGTCCTGCAAGATGGAGCACACCACATGGTTGAT
TCTAATGAAATCTCTTTCATCCGAGCAGGAGAAGGTGCTCTTAAACAAGCCTTGGCAAAT
GCAACATTATGTATTCTTGAACCTATTATGGCTGTGGAAGTTGTAGCTCCAAATGAATTT
CAGGGACAAGTAATTGCAGGAATTAACCGACGCCATGGGGTAATCACTGGGCAAGATGGA
GTTGAGGACTATTTTACACTGTATGCAGATGTCCCTCTAAATGATATGTTTGGTTATTCC
ACTGAACTTAGGTCATGCACAGAGGGAAAGGGAGAATACACAATGGAGTATAGCAGGTAT
CAGCCATGTTTACCATCCACACAAGAAGACGTCATTAATAAGTATTTGGAAGCTACAGGT
CAACTTCCTGTTAAAAAAGGAAAAGCCAAGAACTAA
Enzyme 92 GenBank Gene ID NM_024996.5 Link Image
Enzyme 92 GeneCard ID GFM1 Link Image
Enzyme 92 GenAtlas ID GFM1 Link Image
Enzyme 92 HGNC ID HGNC:13780 Link Image
Enzyme 92 Chromosome Location 3
Enzyme 92 Locus 3q25
Enzyme 92 SNPs SNPJam Report Link Image
Enzyme 92 General References
  1. Gao J, Yu L, Zhang P, Jiang J, Chen J, Peng J, Wei Y, Zhao S: Cloning and characterization of human and mouse mitochondrial elongation factor G, GFM and Gfm, and mapping of GFM to human chromosome 3q25.1-q26.2. Genomics. 2001 May 15;74(1):109-14. [PubMed Link Image]
  2. Hammarsund M, Wilson W, Corcoran M, Merup M, Einhorn S, Grander D, Sangfelt O: Identification and characterization of two novel human mitochondrial elongation factor genes, hEFG2 and hEFG1, phylogenetically conserved through evolution. Hum Genet. 2001 Nov;109(5):542-50. Epub 2001 Oct 13. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Tsuboi M, Morita H, Nozaki Y, Akama K, Ueda T, Ito K, Nierhaus KH, Takeuchi N: EF-G2mt is an exclusive recycling factor in mammalian mitochondrial protein synthesis. Mol Cell. 2009 Aug 28;35(4):502-10. [PubMed Link Image]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  8. Coenen MJ, Antonicka H, Ugalde C, Sasarman F, Rossi R, Heister JG, Newbold RF, Trijbels FJ, van den Heuvel LP, Shoubridge EA, Smeitink JA: Mutant mitochondrial elongation factor G1 and combined oxidative phosphorylation deficiency. N Engl J Med. 2004 Nov 11;351(20):2080-6. [PubMed Link Image]
  9. Valente L, Tiranti V, Marsano RM, Malfatti E, Fernandez-Vizarra E, Donnini C, Mereghetti P, De Gioia L, Burlina A, Castellan C, Comi GP, Savasta S, Ferrero I, Zeviani M: Infantile encephalopathy and defective mitochondrial DNA translation in patients with mutations of mitochondrial elongation factors EFG1 and EFTu. Am J Hum Genet. 2007 Jan;80(1):44-58. Epub 2006 Nov 15. [PubMed Link Image]
Enzyme 92 Metabolite References Not Available
Enzyme 93 [top]
Enzyme 93 ID 14082
Enzyme 93 Name Ribosome-releasing factor 2, mitochondrial
Enzyme 93 Synonyms
  1. RRF2mt
  2. Elongation factor G 2, mitochondrial
  3. EF-G2mt
  4. mEF-G 2
  5. Elongation factor G2
  6. hEFG2
Enzyme 93 Gene Name GFM2
Enzyme 93 Protein Sequence >Ribosome-releasing factor 2, mitochondrial
MLTNLRIFAMSHQTIPSVYINNICCYKIRASLKRLKPHVPLGRNCSSLPGLIGNDIKSLH
SIINPPIAKIRNIGIMAHIDAGKTTTTERILYYSGYTRSLGDVDDGDTVTDFMAQERERG
ITIQSAAVTFDWKGYRVNLIDTPGHVDFTLEVERCLRVLDGAVAVFDASAGVEAQTLTVW
RQADKHNIPRICFLNKMDKTGASFKYAVESIREKLKAKPLLLQLPIGEAKTFKGVVDVVM
KEKLLWNCNSNDGKDFERKPLLEMNDPELLKETTEARNALIEQVADLDDEFADLVLEEFS
ENFDLLPAEKLQTAIHRVTLAQTAVPVLCGSALKNKGIQPLLDAVTMYLPSPEERNYEFL
QWYKDDLCALAFKVLHDKQRGPLVFMRIYSGTIKPQLAIHNINGNCTERISRLLLPFADQ
HVEIPSLTAGNIALTVGLKHTATGDTIVSSKSSALAAARRAEREGEKKHRQNNEAERLLL
AGVEIPEPVFFCTIEPPSLSKQPDLEHALKCLQREDPSLKVRLDPDSGQTVLCGMGELHI
EIIHDRIKREYGLETYLGPLQVAYRETILNSVRATDTLDRTLGDKRHLVTVEVEARPIET
SSVMPVIEFEYAESINEGLLKVSQEAIENGIHSACLQGPLLGSPIQDVAITLHSLTIHPG
TSTTMISACVSRCVQKALKKADKQVLEPLMNLEVTVARDYLSPVLADLAQRRGNIQEIQT
RQDNKVVIGFVPLAEIMGYSTVLRTLTSGSATFALELSTYQAMNPQDQNTLLNRRSGLT
Enzyme 93 Number of Residues 779
Enzyme 93 Molecular Weight 86599.7
Enzyme 93 Theoretical pI 6.47
Enzyme 93 GO Classification
Function
  • GTP binding
  • GTPase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
Process
Component
Enzyme 93 General Function Involved in GTPase activity
Enzyme 93 Specific Function Mitochondrial GTPase that mediates the disassembly of ribosomes from messenger RNA at the termination of mitochondrial protein biosynthesis. Acts in collaboration with MRRF. GTP hydrolysis follows the ribosome disassembly and probably occurs on the ribosome large subunit. Not involved in protein elongation and does not promote the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site of the ribosome
Enzyme 93 Pathways Not Available
Enzyme 93 Reactions Not Available
Enzyme 93 Pfam Domain Function
Enzyme 93 Signals
  • None
Enzyme 93 Transmembrane Regions
  • None
Enzyme 93 Essentiality Not Available
Enzyme 93 GenBank ID Protein 19923640 Link Image
Enzyme 93 UniProtKB/Swiss-Prot ID Q969S9 Link Image
Enzyme 93 UniProtKB/Swiss-Prot Entry Name RRF2M_HUMAN Link Image
Enzyme 93 PDB ID Not Available
Enzyme 93 Cellular Location Not Available
Enzyme 93 Gene Sequence >2340 bp
ATGTTGACCAACTTGAGGATATTTGCAATGAGTCATCAGACAATACCCAGTGTGTATATT
AATAATATATGCTGCTATAAAATAAGAGCAAGTTTAAAAAGATTAAAGCCACATGTGCCG
CTTGGAAGAAATTGCAGTTCTCTACCAGGCTTAATAGGAAATGATATCAAATCCCTTCAT
TCCATCATCAATCCTCCCATAGCTAAAATCCGTAATATTGGAATTATGGCTCATATTGAT
GCAGGCAAAACTACCACCACAGAAAGAATATTGTACTATTCCGGATATACAAGATCACTG
GGAGATGTTGATGATGGAGACACAGTGACAGATTTCATGGCCCAAGAGCGAGAAAGAGGC
ATTACTATTCAATCAGCTGCTGTTACATTTGATTGGAAAGGTTATAGAGTCAATCTAATT
GATACACCAGGTCATGTGGACTTTACCTTGGAGGTTGAGCGGTGCCTAAGAGTGTTGGAT
GGTGCAGTGGCTGTATTTGATGCCTCTGCTGGTGTAGAGGCCCAGACTCTCACAGTATGG
AGGCAAGCTGATAAACACAATATACCTCGAATCTGTTTTTTAAACAAGATGGACAAAACT
GGAGCAAGCTTTAAGTATGCAGTTGAAAGCATCAGAGAGAAGTTAAAGGCAAAGCCTTTG
CTTTTACAGTTACCAATTGGTGAAGCCAAAACTTTCAAAGGAGTGGTGGATGTAGTAATG
AAAGAAAAACTTCTTTGGAATTGCAATTCAAATGATGGAAAAGACTTTGAGAGAAAGCCC
CTCTTGGAAATGAATGATCCTGAATTGCTGAAGGAAACAACTGAAGCAAGGAATGCCTTA
ATTGAACAAGTTGCAGATTTGGATGATGAATTTGCTGACTTGGTTTTAGAAGAATTTAGT
GAGAATTTTGATTTGTTACCAGCTGAAAAGCTACAGACTGCAATACATAGAGTGACACTA
GCTCAGACAGCAGTGCCTGTGCTTTGTGGAAGTGCCCTGAAAAACAAAGGGATACAGCCC
TTGTTAGATGCTGTTACTATGTACTTACCTTCACCTGAAGAGCGTAACTATGAATTTCTG
CAGTGGTATAAGGATGACTTATGTGCATTGGCATTTAAAGTTCTCCATGACAAGCAGCGA
GGACCACTGGTTTTTATGCGCATTTACTCAGGCACTATAAAACCCCAGTTGGCCATTCAT
AATATTAATGGAAACTGCACGGAGAGAATAAGTCGTCTGCTTTTGCCGTTTGCTGACCAA
CATGTAGAAATCCCTTCATTGACTGCTGGTAACATTGCTTTGACTGTTGGGCTTAAACAT
ACTGCCACTGGAGACACCATTGTCTCATCCAAGTCCAGTGCATTAGCTGCAGCTCGTAGA
GCCGAACGGGAGGGAGAAAAGAAGCACAGACAAAACAATGAAGCAGAGAGACTTTTATTG
GCTGGAGTGGAGATTCCAGAACCTGTTTTCTTCTGTACCATAGAACCCCCATCACTGTCT
AAGCAGCCAGATTTGGAACATGCGTTGAAATGTCTTCAGCGTGAAGATCCCAGTTTGAAA
GTGAGGCTAGATCCTGACTCTGGACAAACTGTTCTGTGTGGTATGGGGGAGTTACATATA
GAGATTATTCATGATCGAATCAAGAGGGAATATGGACTGGAGACCTATCTCGGGCCTCTC
CAGGTGGCATATCGAGAGACCATCCTAAACTCAGTTCGTGCCACAGATACCTTAGATAGA
ACTTTAGGAGACAAAAGGCATCTTGTGACTGTAGAAGTGGAAGCAAGGCCAATTGAAACA
TCATCTGTTATGCCTGTGATTGAGTTTGAGTATGCTGAAAGTATCAATGAAGGCCTTTTG
AAGGTCTCCCAAGAGGCCATTGAAAATGGAATTCACAGCGCATGTCTCCAAGGACCATTG
CTTGGATCCCCAATTCAGGATGTAGCAATTACTTTACATTCCCTGACAATTCATCCTGGC
ACCTCCACAACTATGATTTCTGCCTGTGTCTCAAGATGCGTGCAAAAGGCTCTGAAGAAA
GCTGATAAGCAAGTTTTGGAGCCTCTGATGAATCTTGAGGTTACAGTAGCTAGAGATTAT
CTCAGCCCTGTCCTGGCAGATCTGGCACAAAGAAGAGGAAACATTCAGGAAATTCAGACT
CGCCAGGACAACAAAGTTGTTATTGGATTTGTTCCCTTAGCAGAAATTATGGGTTATTCA
ACTGTGCTTCGAACGCTAACATCAGGCTCAGCTACTTTTGCCTTAGAACTATCTACTTAT
CAAGCCATGAATCCTCAAGATCAAAATACACTGCTCAACCGGAGAAGTGGTTTGACCTAA
Enzyme 93 GenBank Gene ID NM_032380.3 Link Image
Enzyme 93 GeneCard ID GFM2 Link Image
Enzyme 93 GenAtlas ID GFM2 Link Image
Enzyme 93 HGNC ID HGNC:29682 Link Image
Enzyme 93 Chromosome Location 5
Enzyme 93 Locus 5q13
Enzyme 93 SNPs SNPJam Report Link Image
Enzyme 93 General References
  1. Hammarsund M, Wilson W, Corcoran M, Merup M, Einhorn S, Grander D, Sangfelt O: Identification and characterization of two novel human mitochondrial elongation factor genes, hEFG2 and hEFG1, phylogenetically conserved through evolution. Hum Genet. 2001 Nov;109(5):542-50. Epub 2001 Oct 13. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Tsuboi M, Morita H, Nozaki Y, Akama K, Ueda T, Ito K, Nierhaus KH, Takeuchi N: EF-G2mt is an exclusive recycling factor in mammalian mitochondrial protein synthesis. Mol Cell. 2009 Aug 28;35(4):502-10. [PubMed Link Image]
Enzyme 93 Metabolite References Not Available
Enzyme 94 [top]
Enzyme 94 ID 14084
Enzyme 94 Name Elongation factor Tu, mitochondrial
Enzyme 94 Synonyms
  1. EF-Tu
  2. P43
Enzyme 94 Gene Name TUFM
Enzyme 94 Protein Sequence >Elongation factor Tu, mitochondrial
MAAATLLRATPHFSGLAAGRTFLLQGLLRLLKAPALPLLCRGLAVEAKKTYVRDKPHVNV
GTIGHVDHGKTTLTAAITKILAEGGGAKFKKYEEIDNAPEERARGITINAAHVEYSTAAR
HYAHTDCPGHADYVKNMITGTAPLDGCILVVAANDGPMPQTREHLLLARQIGVEHVVVYV
NKADAVQDSEMVELVELEIRELLTEFGYKGEETPVIVGSALCALEGRDPELGLKSVQKLL
DAVDTYIPVPARDLEKPFLLPVEAVYSVPGRGTVVTGTLERGILKKGDECELLGHSKNIR
TVVTGIEMFHKSLERAEAGDNLGALVRGLKREDLRRGLVMVKPGSIKPHQKVEAQVYILS
KEEGGRHKPFVSHFMPVMFSLTWDMACRIILPPEKELAMPGEDLKFNLILRQPMILEKGQ
RFTLRDGNRTIGTGLVTNTLAMTEEEKNIKWG
Enzyme 94 Number of Residues 452
Enzyme 94 Molecular Weight 49541.1
Enzyme 94 Theoretical pI 7.68
Enzyme 94 GO Classification
Function
  • GTP binding
  • GTPase activity
  • RNA binding
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleic acid binding
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • translation elongation factor activity
  • translation factor activity, nucleic acid binding
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • translational elongation
Component
  • cell part
  • intracellular
Enzyme 94 General Function Involved in GTPase activity
Enzyme 94 Specific Function This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis
Enzyme 94 Pathways Not Available
Enzyme 94 Reactions Not Available
Enzyme 94 Pfam Domain Function
Enzyme 94 Signals
  • None
Enzyme 94 Transmembrane Regions
  • None
Enzyme 94 Essentiality Not Available
Enzyme 94 GenBank ID Protein 704416 Link Image
Enzyme 94 UniProtKB/Swiss-Prot ID P49411 Link Image
Enzyme 94 UniProtKB/Swiss-Prot Entry Name EFTU_HUMAN Link Image
Enzyme 94 PDB ID 1D2E Link Image
Enzyme 94 PDB File Show
Enzyme 94 3D Structure
Enzyme 94 Cellular Location Not Available
Enzyme 94 Gene Sequence >1359 bp
ATGGCGGCCGCCACCCTGCTGCGCGCGACGCCCCACTTCAGCGGTCTCGCCGCCGGCCGG
ACCTTCCTGCTGCAGGGTCTGTTGCGGCTGCTGAAAGCCCCGGCATTGCCTCTCTTGTGC
CGCGGCCTGGCCGTGGAGGCCAAGAAGACTTACGTGCGCGACAAGCCACATGTGAATGTG
GGTACCATCGGCCATGTGGACCACGGGAAGACCACGCTGACTGCAGCCATCACGAAGATT
CTAGCTGAGGGAGGTGGGGCTAAGTTCAAGAAGTACGAGGAGATTGACAATGCCCCGGAG
GAGCGAGCTCGGGGTATCACCATCAATGCGGCTCATGTGGAGTATAGCACTGCCGCCCGC
CACTACGCCCACACAGACTGCCCGGGTCATGCAGATTATGTTAAGAATATGATCACAGGC
ACTGCACCCCTCGACGGCTGCATCCTGGTGGTAGCAGCCAATGACGGCCCCATGCCCCAG
ACCCGAGAGCACTTATTACTGGCCAGACAGATTGGGGTGGAGCATGTGGTGGTGTATGTG
AACAAGGCTGACGCTGTCCAGGACTCTGAGATGGTGGAACTGGTGGAACTGGAGATCCGG
GAGCTGCTCACCGAGTTTGGCTATAAAGGGGAGGAGACCCCAGTCATCGTAGGCTCTGCT
CTCTGTGCCCTTGAGGGTCGGGACCCTGAGTTAGGCCTGAAGTCTGTGCAGAAGCTACTG
GATGCTGTGGACACTTACATCCCAGTGCCCGCCCGGGACCTGGAGAAGCCTTTCCTGCTG
CCTGTGGAGGCGGTGTACTCCGTCCCTGGCCGTGGCACCGTGGTGACAGGTACACTAGAG
CGTGGCATTTTAAAGAAGGGAGACGAGTGTGAGCTCCTAGGACATAGCAAGAACATCCGC
ACTGTGGTGACAGGCATTGAGATGTTCCACAAGAGCCTGGAGAGGGCCGAGGCCGGAGAT
AACCTCGGGGCCCTGGTCCGAGGCTTGAAGCGGGAGGACTTGCGGCGGGGCCTGGTCATG
GTCAAGCCAGGTTCCATCAAGCCCCACCAGAAGGTGGAGGCCCAGGTTTACATCCTCAGC
AAGGAGGAAGGTGGCCGCCACAAGCCCTTTGTGTCCCACTTCATGCCTGTCATGTTCTCC
CTGACTTGGAACATGGCCTGTCGGATTATCCTGCCCCCAGAGAAGGAGCTTGCCATGCCC
GGGGAGGACCTGAAGTTCAACCTAATCTTGCGGCAGCCAATGATCTTAGAGAAAGGCCAG
CGTTTCACCCTGCGAGATGGCAACCGGACTATTGGCACCGGTCTAGTCACCAACACGCTG
GCCATGACTGAGGAGGAGAAGAATATCAAATGGGGTTGA
Enzyme 94 GenBank Gene ID L38995 Link Image
Enzyme 94 GeneCard ID TUFM Link Image
Enzyme 94 GenAtlas ID TUFM Link Image
Enzyme 94 HGNC ID HGNC:12420 Link Image
Enzyme 94 Chromosome Location 1
Enzyme 94 Locus 16p11.2
Enzyme 94 SNPs SNPJam Report Link Image
Enzyme 94 General References
  1. Woriax VL, Burkhart W, Spremulli LL: Cloning, sequence analysis and expression of mammalian mitochondrial protein synthesis elongation factor Tu. Biochim Biophys Acta. 1995 Dec 27;1264(3):347-56. [PubMed Link Image]
  2. Wells J, Henkler F, Leversha M, Koshy R: A mitochondrial elongation factor-like protein is over-expressed in tumours and differentially expressed in normal tissues. FEBS Lett. 1995 Jan 23;358(2):119-25. [PubMed Link Image]
  3. Ling M, Merante F, Chen HS, Duff C, Duncan AM, Robinson BH: The human mitochondrial elongation factor tu (EF-Tu) gene: cDNA sequence, genomic localization, genomic structure, and identification of a pseudogene. Gene. 1997 Sep 15;197(1-2):325-36. [PubMed Link Image]
  4. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  8. Valente L, Tiranti V, Marsano RM, Malfatti E, Fernandez-Vizarra E, Donnini C, Mereghetti P, De Gioia L, Burlina A, Castellan C, Comi GP, Savasta S, Ferrero I, Zeviani M: Infantile encephalopathy and defective mitochondrial DNA translation in patients with mutations of mitochondrial elongation factors EFG1 and EFTu. Am J Hum Genet. 2007 Jan;80(1):44-58. Epub 2006 Nov 15. [PubMed Link Image]
Enzyme 94 Metabolite References Not Available
Enzyme 95 [top]
Enzyme 95 ID 14096
Enzyme 95 Name Elongation factor Tu GTP-binding domain-containing protein 1
Enzyme 95 Synonyms
  1. Protein FAM42A
Enzyme 95 Gene Name EFTUD1
Enzyme 95 Protein Sequence >Elongation factor Tu GTP-binding domain-containing protein 1
MVLNSLDKMIQLQKNTANIRNICVLAHVDHGKTTLADCLISSNGIISSRLAGKLRYMDSR
EDEQIRGITMKSSAISLHYATGNEEYLINLIDSPGHVDFSSEVSTAVRICDGCIIVVDAV
EGVCPQTQAVLRQAWLENIRPVLVINKIDRLIVELKFTPQEAYSHLKNILEQINALTGTL
FTSKVLEERAERETESQVNPNSEQGEQVYDWSTGLEDTDDSHLYFSPEQGNVVFTSAIDG
WGFGIEHFARIYSQKIGIKKEVLMKTLWGDYYINMKAKKIMKGDQAKGKKPLFVQLILEN
IWSLYDAVLKKDKDKIDKIVTSLGLKIGAREARHSDPKVQINAICSQWLPISHAVLAMVC
QKLPSPLDITAERVERLMCTGSQTFDSFPPETQALKAAFMKCGSEDTAPVIIFVSKMFAV
DAKALPQNKPRPLTQEEIAQRRERARQRHAEKLAAAQGQAPLEPTQDGSAIETCPKGEEP
RGDEQQVESMTPKPVLQEENNQESFIAFARVFSGVARRGKKIFVLGPKYSPLEFLRRVPL
GFSAPPDGLPQVPHMAYCALENLYLLMGRELEYLEEVPPGNVLGIGGLQDFVLKSATLCS
LPSCPPFIPLNFEATPIVRVAVEPKHPSEMPQLVKGMKLLNQADPCVQILIQETGEHVLV
TAGEVHLQRCLDDLKERFAKIHISVSEPIIPFRETITKPPKVDMVNEEIGKQQKVAVIHQ
MKEDQSKIPEGIQVDSDGLITITTPNKLATLSVRAMPLPEEVTQILEENSDLIRSMEQLT
SSLNEGENTHMIHQKTQEKIWEFKGKLEQHLTGRRWRNIVDQIWSFGPRKCGPNILVNKS
EDFQNSVWTGPADKASKEASRYRDLGNSIVSGFQLATLSGPMCEEPLMGVCFVLEKWDLS
KFEEQGASDLAKEGQEENETCSGGNENQELQDGCSEAFEKRTSQKGESPLTDCYGPFSGQ
LIATMKEACRYALQVKPQRLMAAMYTCDIMATGDVLGRVYAVLSKREGRVLQEEMKEGTD
MFIIKAVLPVAESFGFADEIRKRTSGLASPQLVFSHWEIIPSDPFWVPTTEEEYLHFGEK
ADSENQARKYMNAVRKRKGLYVEEKIVEHAEKQRTLSKNK
Enzyme 95 Number of Residues 1120
Enzyme 95 Molecular Weight 125428.7
Enzyme 95 Theoretical pI 5.72
Enzyme 95 GO Classification
Function
  • GTP binding
  • GTPase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
Process
Component
Enzyme 95 General Function Involved in GTPase activity
Enzyme 95 Specific Function Not Available
Enzyme 95 Pathways Not Available
Enzyme 95 Reactions Not Available
Enzyme 95 Pfam Domain Function
Enzyme 95 Signals
  • None
Enzyme 95 Transmembrane Regions
  • None
Enzyme 95 Essentiality Not Available
Enzyme 95 GenBank ID Protein 94966754 Link Image
Enzyme 95 UniProtKB/Swiss-Prot ID Q7Z2Z2 Link Image
Enzyme 95 UniProtKB/Swiss-Prot Entry Name ETUD1_HUMAN Link Image
Enzyme 95 PDB ID Not Available
Enzyme 95 Cellular Location Not Available
Enzyme 95 Gene Sequence >3363 bp
ATGGTGCTCAACAGTTTGGATAAGATGATTCAACTCCAGAAAAACACTGCCAACATCAGG
AATATTTGTGTTTTGGCTCATGTTGACCATGGAAAAACTACTCTGGCTGACTGTCTTATA
TCTAGCAATGGAATCATCTCCAGCCGCCTAGCAGGCAAGTTAAGGTACATGGACAGCAGA
GAAGATGAACAGATCCGAGGGATCACTATGAAATCCAGTGCCATTTCCCTACATTATGCA
ACAGGTAATGAGGAGTACCTGATCAATCTGATAGACTCTCCAGGACACGTGGACTTTTCC
TCAGAAGTATCAACCGCTGTTCGCATTTGTGATGGATGCATCATTGTGGTAGATGCTGTG
GAAGGAGTCTGTCCACAGACACAGGCAGTTCTGCGACAAGCTTGGCTTGAAAACATCCGT
CCGGTTTTAGTGATTAATAAGATTGATCGCTTGATAGTGGAACTGAAATTCACCCCACAA
GAGGCCTATTCTCACCTCAAGAATATTTTAGAACAGATTAATGCGCTCACAGGGACTCTT
TTTACTTCTAAAGTCCTAGAAGAAAGAGCAGAGAGGGAGACTGAATCCCAAGTGAATCCA
AATTCTGAACAAGGAGAGCAAGTATATGACTGGAGCACTGGCTTGGAGGACACAGATGAT
TCTCACCTTTACTTCTCTCCAGAACAGGGAAATGTGGTGTTTACCAGTGCAATAGATGGG
TGGGGCTTTGGAATTGAGCACTTCGCCAGAATCTACAGTCAAAAAATTGGCATCAAAAAG
GAAGTTCTTATGAAAACCTTGTGGGGAGATTACTATATAAATATGAAGGCTAAAAAGATC
ATGAAGGGTGATCAGGCCAAAGGAAAGAAACCTTTATTTGTACAGTTGATCCTGGAAAAT
ATATGGAGTTTGTATGATGCTGTTTTGAAAAAGGACAAAGACAAAATTGATAAAATAGTG
ACTTCTTTAGGATTAAAAATTGGAGCCCGGGAGGCACGACATTCAGACCCTAAAGTTCAG
ATCAACGCCATTTGCAGTCAGTGGCTACCCATATCCCATGCTGTTCTTGCTATGGTGTGT
CAGAAACTTCCTAGTCCCCTTGATATTACAGCTGAGAGAGTGGAGAGACTGATGTGCACA
GGATCACAAACTTTTGACTCTTTTCCACCAGAAACTCAAGCACTGAAAGCAGCTTTTATG
AAATGTGGAAGTGAGGACACTGCTCCAGTTATTATATTTGTTTCCAAAATGTTTGCAGTT
GATGCTAAGGCCTTGCCTCAGAATAAGCCAAGGCCTCTCACTCAAGAAGAAATTGCTCAG
AGACGTGAGCGTGCAAGACAAAGGCATGCAGAGAAGCTTGCAGCAGCACAGGGACAGGCA
CCCTTGGAGCCCACCCAAGATGGGAGTGCCATTGAAACATGTCCAAAAGGAGAGGAGCCA
AGAGGTGACGAGCAACAGGTGGAAAGTATGACCCCTAAACCTGTGCTCCAGGAAGAAAAC
AACCAAGAGTCTTTTATTGCATTTGCTCGGGTGTTCAGTGGTGTGGCTCGAAGAGGAAAG
AAAATTTTTGTCTTGGGGCCCAAATACAGTCCTCTTGAGTTTTTACGAAGGGTACCATTA
GGCTTCTCAGCTCCACCAGATGGCCTCCCCCAAGTCCCCCACATGGCATACTGTGCTCTG
GAAAACCTGTATCTTCTGATGGGAAGGGAACTGGAATATCTAGAGGAGGTACCTCCAGGA
AATGTGCTAGGAATAGGAGGCCTTCAAGATTTTGTGCTGAAATCTGCAACACTGTGTAGC
CTGCCATCCTGCCCACCATTTATACCACTCAACTTCGAAGCCACTCCTATTGTGAGAGTT
GCTGTTGAACCAAAACATCCAAGTGAAATGCCTCAGCTCGTAAAAGGAATGAAACTGTTA
AACCAGGCTGATCCCTGTGTCCAGATTTTAATTCAGGAAACGGGAGAGCACGTTTTAGTC
ACAGCAGGAGAAGTCCACCTTCAGCGATGCCTGGATGACTTAAAAGAAAGGTTTGCAAAG
ATTCATATCAGTGTATCTGAACCTATTATTCCATTCAGAGAAACAATCACAAAACCCCCA
AAAGTTGACATGGTCAATGAAGAAATAGGCAAACAGCAAAAAGTTGCAGTCATACACCAA
ATGAAAGAAGATCAAAGCAAAATCCCTGAAGGAATCCAAGTTGACTCTGACGGGCTAATC
ACCATAACAACTCCCAATAAACTTGCCACGCTCAGTGTTCGAGCCATGCCCCTTCCAGAA
GAAGTCACCCAGATTCTGGAAGAAAATAGTGATTTGATTCGTTCTATGGAGCAGTTGACA
TCCTCTTTGAATGAGGGTGAAAATACTCACATGATTCATCAGAAGACCCAAGAGAAAATT
TGGGAATTCAAAGGAAAACTGGAGCAACACCTAACAGGGAGAAGATGGAGGAACATTGTT
GACCAAATCTGGTCATTTGGCCCAAGAAAATGTGGGCCCAACATACTAGTCAATAAAAGT
GAAGATTTTCAGAACTCAGTATGGACAGGTCCAGCTGACAAAGCTTCAAAAGAAGCCAGT
AGATACCGAGATTTGGGCAATAGCATTGTGAGTGGCTTCCAACTAGCAACCCTCTCTGGC
CCCATGTGTGAGGAGCCTCTCATGGGTGTCTGTTTTGTTCTGGAAAAATGGGACCTAAGT
AAATTTGAGGAACAAGGAGCAAGTGATCTGGCAAAAGAGGGACAGGAGGAAAATGAAACC
TGTTCTGGTGGAAATGAAAACCAAGAGCTACAAGATGGCTGCTCTGAGGCCTTTGAGAAG
AGGACATCACAGAAAGGAGAATCTCCACTCACTGACTGCTATGGACCTTTCTCAGGACAG
CTAATTGCCACCATGAAAGAAGCATGTCGCTATGCACTGCAAGTGAAACCTCAGCGCCTG
ATGGCAGCTATGTACACATGTGACATCATGGCCACTGGTGATGTTCTCGGTCGAGTCTAT
GCTGTCTTGTCAAAGAGAGAAGGTCGGGTACTTCAAGAAGAAATGAAAGAAGGGACAGAC
ATGTTCATCATCAAGGCTGTGCTGCCTGTTGCTGAAAGCTTTGGTTTTGCTGATGAAATC
AGGAAGAGGACAAGTGGCCTGGCCAGCCCACAACTAGTATTCAGCCATTGGGAGATCATT
CCCAGTGACCCCTTCTGGGTGCCAACTACTGAGGAGGAATACTTGCACTTTGGGGAGAAG
GCTGACTCTGAGAACCAAGCCCGGAAGTACATGAACGCAGTACGAAAGCGGAAGGGGCTT
TATGTGGAAGAAAAGATTGTGGAGCATGCAGAAAAGCAGAGGACACTCAGCAAAAATAAG
TAG
Enzyme 95 GenBank Gene ID NM_024580.5 Link Image
Enzyme 95 GeneCard ID EFTUD1 Link Image
Enzyme 95 GenAtlas ID EFTUD1 Link Image
Enzyme 95 HGNC ID HGNC:25789 Link Image
Enzyme 95 Chromosome Location 1
Enzyme 95 Locus 15q25.2
Enzyme 95 SNPs SNPJam Report Link Image
Enzyme 95 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  3. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed Link Image]
  4. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 95 Metabolite References Not Available
Enzyme 96 [top]
Enzyme 96 ID 14109
Enzyme 96 Name GTPase-activating protein and VPS9 domain-containing protein 1
Enzyme 96 Synonyms
  1. GAPex-5
  2. Rab5-activating protein 6
Enzyme 96 Gene Name GAPVD1
Enzyme 96 Protein Sequence >GTPase-activating protein and VPS9 domain-containing protein 1
MVKLDIHTLAHHLKQERLYVNSEKQLIQRLNADVLKTAEKLYRTAWIAKQQRINLDRLII
TSAEASPAECCQHAKILEDTQFVDGYKQLGFQETAYGEFLSRLRENPRLIASSLVAGEKL
NQENTQSVIYTVFTSLYGNCIMQEDESYLLQVLRYLIEFELKESDNPRRLLRRGTCAFSI
LFKLFSEGLFSAKLFLTATLHEPIMQLLVEDEDHLETDPNKLIERFSPSQQEKLFGEKGS
DRFRQKVQEMVESNEAKLVALVNKFIGYLKQNTYCFPHSLRWIVSQMYKTLSCVDRLEVG
EVRAMCTDLLLACFICPAVVNPEQYGIISDAPINEVARFNLMQVGRLLQQLAMTGSEEGD
PRTKSSLGKFDKSCVAAFLDVVIGGRAVETPPLSSVNLLEGLSRTVVYITYSQLITLVNF
MKSVMSGDQLREDRMALDNLLANLPPAKPGKSSSLEMTPYNTPQLSPATTPANKKNRLPI
ATRSRSRTNMLMDLHMDHEGSSQETIQEVQPEEVLVISLGTGPQLTPGMMSENEVLNMQL
SDGGQGDVPVDENKLHGKPDKTLRFSLCSDNLEGISEGPSNRSNSVSSLDLEGESVSELG
AGPSGSNGVEALQLLEHEQATTQDNLDDKLRKFEIRDMMGLTDDRDISETVSETWSTDVL
GSDFDPNIDEDRLQEIAGAAAENMLGSLLCLPGSGSVLLDPCTGSTISETTSEAWSVEVL
PSDSEAPDLKQEERLQELESCSGLGSTSDDTDVREVSSRPSTPGLSVVSGISATSEDIPN
KIEDLRSECSSDFGGKDSVTSPDMDEITHGAHQLTSPPSQSESLLAMFDPLSSHEGASAV
VRPKVHYARPSHPPPDPPILEGAVGGNEARLPNFGSHVLTPAEMEAFKQRHSYPERLVRS
RSSDIVSSVRRPMSDPSWNRRPGNEERELPPAAAIGATSLVAAPHSSSSSPSKDSSRGET
EERKDSDDEKSDRNRPWWRKRFVSAMPKAPIPFRKKEKQEKDKDDLGPDRFSTLTDDPSP
RLSAQAQVAEDILDKYRNAIKRTSPSDGAMANYESTGDNHDRDLSSKLLYHSDKEVMGDG
ESAHDSPRDEALQNISADDLPDSASQAAHPQDSAFSYRDAKKKLRLALCSADSVAFPVLT
HSTRNGLPDHTDPEDNEIVCFLKVQIAEAINLQDKNLMAQLQETMRCVCRFDNRTCRKLL
ASIAEDYRKRAPYIAYLTRCRQGLQTTQAHLERLLQRVLRDKEVANRYFTTVCVRLLLES
KEKKIREFIQDFQKLTAADDKTAQVEDFLQFLYGAMAQDVIWQNASEEQLQDAQLAIERS
VMNRIFKLAFYPNQDGDILRDQVLHEHIQRLSKVVTANHRALQIPEVYLREAPWPSAQSE
IRTISAYKTPRDKVQCILRMCSTIMNLLSLANEDSVPGADDFVPVLVFVLIKANPPCLLS
TVQYISSFYASCLSGEESYWWMQFTAAVEFIKTIDDRK
Enzyme 96 Number of Residues 1478
Enzyme 96 Molecular Weight 164978.1
Enzyme 96 Theoretical pI 4.86
Enzyme 96 GO Classification
Function
  • GTPase activator activity
  • enzyme activator activity
  • enzyme regulator activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
Component
  • cell part
  • intracellular
Enzyme 96 General Function Involved in GTPase activator activity
Enzyme 96 Specific Function Acts both as a GTPase-activating protein (GAP) and a guanine nucleotide exchange factor (GEF), and participates in various processes such as endocytosis, insulin receptor internalization or LC2A4/GLUT4 trafficking. Acts as a GEF for the Ras-related protein RAB31 by exchanging bound GDP for free GTP, leading to regulate LC2A4/GLUT4 trafficking. In the absence of insulin, it maintains RAB31 in an active state and promotes a futile cycle between LC2A4/GLUT4 storage vesicles and early endosomes, retaining LC2A4/GLUT4 inside the cells. Upon insulin stimulation, it is translocated to the plasma membrane, releasing LC2A4/GLUT4 from intracellular storage vesicles. Also involved in EGFR trafficking and degradation, possibly by promoting EGFR ubiquitination and subsequent degradation by the proteasome. Has GEF activity for Rab5 and GAP activity for Ras
Enzyme 96 Pathways Not Available
Enzyme 96 Reactions Not Available
Enzyme 96 Pfam Domain Function
Enzyme 96 Signals
  • None
Enzyme 96 Transmembrane Regions
  • None
Enzyme 96 Essentiality Not Available
Enzyme 96 GenBank ID Protein 51093832 Link Image
Enzyme 96 UniProtKB/Swiss-Prot ID Q14C86 Link Image
Enzyme 96 UniProtKB/Swiss-Prot Entry Name GAPD1_HUMAN Link Image
Enzyme 96 PDB ID Not Available
Enzyme 96 Cellular Location Not Available
Enzyme 96 Gene Sequence >4464 bp
ATGGTGAAACTAGATATTCATACTCTGGCTCATCACCTCAAGCAGGAACGCTTATATGTA
AACTCTGAGAAACAGCTCATTCAGAGGCTCAATGCAGATGTACTTAAGACAGCTGAAAAG
TTGTATCGTACAGCATGGATTGCGAAGCAACAGAGAATCAATTTGGATCGGCTTATCATA
ACCAGTGCTGAAGCTTCCCCTGCTGAATGTTGCCAACATGCCAAAATTTTGGAAGATACA
CAATTTGTTGATGGGTATAAGCAATTGGGATTTCAGGAGACTGCTTATGGAGAATTCTTG
AGTCGATTGAGGGAAAATCCTCGTCTTATTGCCTCCTCTTTGGTTGCTGGAGAGAAACTT
AATCAGGAGAACACACAAAGTGTTATTTACACAGTTTTTACCTCCCTGTATGGCAATTGC
ATCATGCAAGAAGATGAAAGCTACCTCCTTCAGGTTTTGCGATACTTGATTGAATTTGAA
CTTAAAGAAAGTGACAACCCTAGGCGACTTTTGAGGAGAGGAACTTGTGCCTTCAGCATC
TTATTTAAACTTTTTTCTGAAGGACTGTTTTCTGCCAAACTTTTCCTCACAGCCACTTTA
CATGAGCCAATTATGCAACTGCTTGTTGAAGATGAAGATCACCTGGAAACAGATCCAAAC
AAGCTAATTGAGAGGTTCTCTCCATCTCAGCAGGAAAAACTCTTTGGAGAGAAGGGCTCA
GATAGATTCAGGCAAAAAGTTCAAGAAATGGTGGAGTCCAATGAAGCAAAGCTAGTGGCT
TTGGTGAACAAATTTATTGGTTATCTCAAACAGAACACATATTGTTTTCCACATAGTTTA
AGGTGGATCGTGTCTCAGATGTACAAAACCCTCTCCTGTGTAGATAGGCTGGAAGTTGGG
GAGGTCAGGGCAATGTGTACTGATCTCCTGTTGGCCTGCTTCATTTGTCCTGCAGTTGTC
AATCCAGAACAATATGGAATAATTTCCGATGCTCCTATTAATGAAGTAGCACGATTTAAT
CTGATGCAGGTAGGCCGCCTTTTGCAGCAGTTAGCAATGACTGGCTCTGAAGAGGGAGAT
CCCCGAACAAAGAGCAGCCTTGGAAAGTTTGACAAAAGCTGTGTTGCCGCTTTCCTTGAT
GTTGTGATTGGGGGCCGTGCAGTGGAGACCCCTCCATTGTCTTCCGTCAATCTTCTGGAA
GGATTGAGCAGAACTGTGGTTTATATAACCTACAGTCAGCTTATTACTCTGGTGAATTTT
ATGAAGAGTGTGATGTCTGGAGATCAACTGAGAGAAGATAGAATGGCTCTTGACAATTTA
TTGGCAAACCTACCCCCGGCCAAGCCAGGAAAAAGTAGCAGTTTAGAAATGACTCCCTAC
AATACACCTCAGCTATCTCCAGCAACCACTCCAGCAAATAAAAAGAATCGATTACCTATA
GCAACTCGGAGCAGAAGCCGCACCAATATGCTAATGGACCTACATATGGACCATGAAGGA
TCATCTCAAGAAACCATCCAGGAGGTGCAACCAGAAGAGGTGTTGGTCATTTCCTTAGGT
ACAGGTCCCCAGCTTACTCCAGGGATGATGTCAGAAAATGAGGTCCTAAACATGCAGCTT
TCGGATGGAGGACAAGGAGATGTCCCTGTTGATGAAAACAAACTCCATGGTAAACCTGAT
AAAACCTTGCGCTTTTCCCTCTGCAGTGATAATCTGGAAGGAATATCTGAAGGTCCTTCA
AATCGCTCCAATTCAGTGTCCTCCCTAGACCTAGAAGGAGAGTCTGTGTCAGAACTTGGA
GCAGGACCTTCTGGCAGTAATGGAGTTGAAGCTCTACAGCTGTTAGAACATGAGCAAGCT
ACAACACAGGATAACCTTGATGATAAGCTAAGGAAGTTTGAAATTCGTGACATGATGGGA
TTAACAGATGATAGGGACATATCAGAAACAGTGAGTGAGACCTGGAGTACAGACGTCTTG
GGAAGTGACTTTGACCCTAATATTGATGAAGATCGCTTGCAAGAAATTGCAGGTGCTGCA
GCAGAGAACATGTTAGGCAGTTTGCTGTGCCTCCCAGGTTCAGGGTCAGTGCTTCTTGAC
CCCTGCACTGGTTCTACCATATCAGAGACAACAAGTGAAGCTTGGAGTGTAGAGGTATTG
CCAAGTGACTCAGAGGCCCCAGACCTAAAGCAGGAGGAGCGTCTGCAAGAACTGGAGAGC
TGTTCTGGACTGGGTAGCACATCTGATGATACGGATGTCAGGGAGGTCAGTTCCCGCCCC
AGCACACCAGGCCTCAGTGTTGTGTCCGGCATAAGTGCAACCTCTGAGGATATTCCCAAT
AAGATTGAAGACCTGAGATCTGAGTGCAGCTCTGATTTTGGGGGTAAAGATTCTGTCACT
AGTCCAGACATGGATGAAATAACTCACGATTTTCTTTATATACTTCAGCCAAAACAACAT
TTTCAACACATTGAAGCAGAAGCAGACATGAGAATCCAGCTGTCTTCTAGTGCCCACCAG
CTGACCTCTCCTCCTTCTCAGTCAGAGTCTCTGCTGGCCATGTTTGATCCACTGTCTTCA
CATGAAGGGGCTTCTGCTGTGGTAAGGCCAAAGGTTCACTATGCTAGGCCATCGCATCCA
CCACCAGATCCCCCAATCCTGGAAGGAGCTGTGGGAGGAAATGAGGCCAGGTTGCCAAAC
TTTGGTTCCCATGTTTTAACTCCAGCTGAAATGGAGGCATTCAAGCAAAGGCATTCTTAC
CCTGAGAGACTAGTTCGAAGCAGGAGCTCTGATATAGTATCTTCTGTCCGGAGACCCATG
AGTGACCCCAGCTGGAACCGGCGTCCAGGAAATGAAGAGCGAGAACTCCCTCCAGCTGCA
GCCATTGGTGCTACTTCTTTGGTGGCTGCACCTCATTCATCATCTTCATCCCCGAGTAAG
GACTCCTCAAGAGGAGAGACTGAAGAACGCAAAGATAGCGATGATGAGAAATCAGACAGG
AACAGACCTTGGTGGAGAAAACGTTTTGTTTCAGCCATGCCTAAAGCTCCTATACCATTT
AGAAAGAAAGAAAAACAAGAAAAAGACAAAGATGATCTGGGGCCTGACAGATTCTCAACA
CTCACAGATGATCCCAGCCCTAGACTCAGTGCACAAGCTCAGGTGGCTGAGGATATTCTG
GACAAATACAGGAATGCCATTAAACGGACCAGCCCCAGTGATGGAGCAATGGCAAACTAT
GAAAGTACAGAGGTTATGGGTGATGGTGAAAGTGCACATGATTCTCCCCGTGACGAAGCA
CTGCAGAACATCTCGGCTGATGATCTCCCAGACTCTGCAAGCCAAGCAGCCCACCCGCAG
GATTCAGCTTTCTCTTACAGAGATGCAAAAAAGAAACTGAGGCTTGCTCTTTGCTCTGCG
GACTCTGTTGCCTTCCCAGTGCTGACCCATTCAACAAGGAATGGTTTACCAGACCACACA
GACCCAGAAGACAATGAAATTGTATGCTTCTTAAAAGTTCAAATAGCTGAAGCAATTAAT
TTACAAGATAAGAATCTAATGGCTCAACTTCAAGAAACAATGCGCTGTGTGTGCCGTTTT
GATAATAGGACTTGTAGGAAACTGCTGGCTTCGATTGCTGAGGACTACAGAAAAAGAGCC
CCATATATTGCTTATCTCACTCGTTGTCGACAAGGACTACAGACCACACAGGCTCACCTG
GAAAGGCTATTGCAAAGAGTTTTGCGGGACAAAGAAGTGGCCAATCGATACTTTACCACT
GTCTGTGTGAGATTACTGCTTGAGAGCAAAGAAAAGAAGATCAGGGAATTCATTCAAGAC
TTTCAGAAACTCACCGCAGCTGACGATAAAACTGCTCAGGTAGAAGATTTTCTGCAGTTT
CTTTATGGTGCAATGGCCCAGGATGTCATATGGCAAAACGCGAGTGAAGAACAGCTTCAA
GATGCACAGCTGGCCATTGAGCGAAGCGTGATGAACCGGATTTTCAAGCTCGCCTTCTAC
CCTAATCAAGATGGGGACATACTTCGCGACCAGGTTCTTCATGAACATATCCAGAGATTG
TCTAAAGTAGTGACTGCAAATCACAGAGCTCTTCAGATACCAGAGGTTTATCTTCGAGAA
GCACCATGGCCATCTGCACAATCAGAAATCAGGACAATAAGTGCTTATAAAACCCCCCGG
GACAAAGTGCAGTGCATCCTGAGAATGTGCTCTACGATTATGAACCTCCTGAGCCTGGCC
AATGAGGACTCTGTCCCTGGAGCGGATGACTTTGTTCCTGTGTTGGTGTTTGTGTTGATA
AAGGCAAATCCACCCTGTTTGCTGTCTACTGTGCAGTATATCAGTAGCTTTTATGCTAGC
TGTCTGTCTGGAGAGGAGTCCTATTGGTGGATGCAGTTCACAGCAGCAGTAGAATTCATT
AAAACCATCGATGACCGAAAGTGA
Enzyme 96 GenBank Gene ID Not Available
Enzyme 96 GeneCard ID GAPVD1 Link Image
Enzyme 96 GenAtlas ID GAPVD1 Link Image
Enzyme 96 HGNC ID HGNC:23375 Link Image
Enzyme 96 Chromosome Location 9
Enzyme 96 Locus 9q33.3
Enzyme 96 SNPs SNPJam Report Link Image
Enzyme 96 General References
  1. Hunker CM, Galvis A, Kruk I, Giambini H, Veisaga ML, Barbieri MA: Rab5-activating protein 6, a novel endosomal protein with a role in endocytosis. Biochem Biophys Res Commun. 2006 Feb 17;340(3):967-75. Epub 2006 Jan 4. [PubMed Link Image]
  2. Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Apr 28;7(2):143-50. [PubMed Link Image]
  3. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  4. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  7. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  9. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  10. Nousiainen M, Sillje HH, Sauer G, Nigg EA, Korner R: Phosphoproteome analysis of the human mitotic spindle. Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5391-6. Epub 2006 Mar 24. [PubMed Link Image]
  11. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  12. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  13. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  14. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  15. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  16. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  17. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 96 Metabolite References Not Available
Enzyme 97 [top]
Enzyme 97 ID 14110
Enzyme 97 Name Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Enzyme 97 Synonyms
  1. Transducin beta chain 1
Enzyme 97 Gene Name GNB1
Enzyme 97 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
MSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYA
MHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNI
CSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTF
TGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNA
FATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDAL
KADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
Enzyme 97 Number of Residues 340
Enzyme 97 Molecular Weight 37376.6
Enzyme 97 Theoretical pI 5.85
Enzyme 97 GO Classification Not Available
Enzyme 97 General Function Involved in GTPase activity
Enzyme 97 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Enzyme 97 Pathways Not Available
Enzyme 97 Reactions Not Available
Enzyme 97 Pfam Domain Function
Enzyme 97 Signals
  • None
Enzyme 97 Transmembrane Regions
  • None
Enzyme 97 Essentiality Not Available
Enzyme 97 GenBank ID Protein 31669 Link Image
Enzyme 97 UniProtKB/Swiss-Prot ID P62873 Link Image
Enzyme 97 UniProtKB/Swiss-Prot Entry Name GBB1_HUMAN Link Image
Enzyme 97 PDB ID 1OMW Link Image
Enzyme 97 PDB File Show
Enzyme 97 3D Structure
Enzyme 97 Cellular Location Not Available
Enzyme 97 Gene Sequence >1023 bp
ATGAGTGAGCTTGACCAGTTACGGCAGGAGGCCGAGCAACTTAAGAACCAGATTCGAGAC
GCCAGGAAAGCATGTGCAGATGCAACTCTCTCTCAGATCACAAACAACATCGACCCAGTG
GGAAGAATCCAAATGCGCACGAGGAGGACACTGCGGGGGCACCTGGCCAAGATCTACGCC
ATGCACTGGGGCACAGACTCCAGGCTTCTCGTCAGTGCCTCGCAGGATGGTAAACTTATC
ATCTGGGACAGCTACACCACCAACAAGGTCCACGCCATCCCTCTGCGCTCCTCCTGGGTC
ATGACCTGTGCATATGCCCCTTCTGGGAACTATGTGGCCTGCGGTGGCCTGGATAACATT
TGCTCCATTTACAATCTGAAAACTCGTGAGGGGAACGTGCGCGTGAGTCGTGAGCTGGCA
GGACACACAGGTTACCTGTCCTGCTGCCGATTCCTGGATGACAATCAGATCGTCACCAGC
TCTGGAGACACCACGTGTGCCCTGTGGGACATCGAGACCGGCCAGCAGACGACCACGTTT
ACCGGACACACTGGAGATGTCATGAGCCTTTCTCTTGCTCCTGACACCAGACTGTTCGTC
TCTGGTGCTTGTGATGCTTCAGCCAAACTCTGGGATGTGCGAGAAGGCATGTGCCGGCAG
ACCTTCACTGGCCACGAGTCTGACATCAATGCCATATGCTTCTTTCCAAATGGCAATGCA
TTTGCCACTGGCTCAGACGACGCCACCTGCAGGCTGTTTGACCTTCGTGCTGACCAGGAG
CTCATGACTTACTCCCATGACAACATCATCTGCGGGATCACCTCTGTCTCCTTCTCCAAG
AGCGGGCGCCTCCTCCTTGCTGGGTACGACGACTTCAACTGCAACGTCTGGGATGCACTC
AAAGCCGACCGGGCAGGTGTCTTGGCTGGGCATGACAACCGCGTCAGCTGCCTGGGCGTG
ACTGACGATGGCATGGCTGTGGCGACAGGGTCCTGGGATAGCTTCCTCAAGATCTGGAAC
TAA
Enzyme 97 GenBank Gene ID X04526 Link Image
Enzyme 97 GeneCard ID GNB1 Link Image
Enzyme 97 GenAtlas ID GNB1 Link Image
Enzyme 97 HGNC ID HGNC:4396 Link Image
Enzyme 97 Chromosome Location 1
Enzyme 97 Locus 1p36.33
Enzyme 97 SNPs SNPJam Report Link Image
Enzyme 97 General References
  1. Codina J, Stengel D, Woo SL, Birnbaumer L: Beta-subunits of the human liver Gs/Gi signal-transducing proteins and those of bovine retinal rod cell transducin are identical. FEBS Lett. 1986 Oct 27;207(2):187-92. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Niu J, Profirovic J, Pan H, Vaiskunaite R, Voyno-Yasenetskaya T: G Protein betagamma subunits stimulate p114RhoGEF, a guanine nucleotide exchange factor for RhoA and Rac1: regulation of cell shape and reactive oxygen species production. Circ Res. 2003 Oct 31;93(9):848-56. Epub 2003 Sep 25. [PubMed Link Image]
  5. Hill C, Goddard A, Ladds G, Davey J: The cationic region of Rhes mediates its interactions with specific Gbeta subunits. Cell Physiol Biochem. 2009;23(1-3):1-8. Epub 2009 Feb 18. [PubMed Link Image]
Enzyme 97 Metabolite References Not Available
Enzyme 98 [top]
Enzyme 98 ID 14111
Enzyme 98 Name Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2
Enzyme 98 Synonyms
  1. G protein subunit beta-2
  2. Transducin beta chain 2
Enzyme 98 Gene Name GNB2
Enzyme 98 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2
MSELEQLRQEAEQLRNQIRDARKACGDSTLTQITAGLDPVGRIQMRTRRTLRGHLAKIYA
MHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNI
CSIYSLKTREGNVRVSRELPGHTGYLSCCRFLDDNQIITSSGDTTCALWDIETGQQTVGF
AGHSGDVMSLSLAPDGRTFVSGACDASIKLWDVRDSMCRQTFIGHESDINAVAFFPNGYA
FTTGSDDATCRLFDLRADQELLMYSHDNIICGITSVAFSRSGRLLLAGYDDFNCNIWDAM
KGDRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
Enzyme 98 Number of Residues 340
Enzyme 98 Molecular Weight 37330.6
Enzyme 98 Theoretical pI 5.85
Enzyme 98 GO Classification Not Available
Enzyme 98 General Function Involved in GTPase activity
Enzyme 98 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Enzyme 98 Pathways Not Available
Enzyme 98 Reactions Not Available
Enzyme 98 Pfam Domain Function
Enzyme 98 Signals
  • None
Enzyme 98 Transmembrane Regions
  • None
Enzyme 98 Essentiality Not Available
Enzyme 98 GenBank ID Protein 3135310 Link Image
Enzyme 98 UniProtKB/Swiss-Prot ID P62879 Link Image
Enzyme 98 UniProtKB/Swiss-Prot Entry Name GBB2_HUMAN Link Image
Enzyme 98 PDB ID Not Available
Enzyme 98 Cellular Location Not Available
Enzyme 98 Gene Sequence >1023 bp
ATGAGTGAGCTGGAGCAACTGAGACAGGAGGCCGAGCAGCTCCGGAACCAGATCCGGGAT
GCCCGAAAAGCATGTGGGGACTCAACACTGACCCAGATCACAGCTGGGCTGGACCCAGTG
GGGAGAATCCAGATGAGGACCCGGAGGACCCTCCGTGGGCACCTGGCAAAGATCTATGCC
ATGCACTGGGGGACCGACTCAAGGCTGCTGGTCAGCGCCTCCCAGGATGGGAAGCTCATC
ATCTGGGACAGCTACACCACCAACAAGGTCCACGCCATCCCGCTGCGCTCCTCCTGGGTA
ATGACCTGTGCCTACGCGCCCTCAGGGAACTTTGTGGCCTGTGGGGGGTTGGACAACATC
TGCTCCATCTACAGCCTCAAGACCCGCGAGGGCAACGTCAGGGTCAGCCGGGAGCTGCCT
GGCCACACTGGGTACCTGTCGTGTTGCCGCTTCCTGGATGACAACCAAATCATCACCAGC
TCTGGGGATACCACCTGTGCCCTGTGGGACATTGAGACAGGCCAGCAGACAGTGGGTTTT
GCTGGACACAGTGGGGATGTGATGTCCCTGTCCCTGGCCCCCGATGGCCGCACGTTTGTG
TCAGGCGCCTGTGATGCCTCTATCAAGCTGTGGGACGTGCGGGATTCCATGTGCCGACAG
ACCTTCATCGGCCATGAATCCGACATCAATGCAGTGGCTTTCTTCCCCAACGGCTACGCC
TTCACCACCGGCTCTGACGACGCCACGTGCCGCCTCTTCGACCTGCGGGCCGATCAGGAG
CTCCTCATGTACTCCCATGACAACATCATCTGTGGCATCACCTCTGTTGCCTTCTCGCGC
AGCGGACGGCTGCTGCTCGCTGGCTACGACGACTTCAACTGCAACATCTGGGATGCCATG
AAGGGCGACCGTGCAGGAGTCCTCGCTGGCCACGACAACCGCGTGAGCTGCCTCGGGGTC
ACCGACGATGGCATGGCTGTGGCCACGGGCTCCTGGGACTCCTTCCTCAAGATCTGGAAC
TAA
Enzyme 98 GenBank Gene ID AF053356 Link Image
Enzyme 98 GeneCard ID GNB2 Link Image
Enzyme 98 GenAtlas ID GNB2 Link Image
Enzyme 98 HGNC ID HGNC:4398 Link Image
Enzyme 98 Chromosome Location 7
Enzyme 98 Locus 7q21.3-q22.1|7q22
Enzyme 98 SNPs SNPJam Report Link Image
Enzyme 98 General References
  1. Fong HK, Amatruda TT 3rd, Birren BW, Simon MI: Distinct forms of the beta subunit of GTP-binding regulatory proteins identified by molecular cloning. Proc Natl Acad Sci U S A. 1987 Jun;84(11):3792-6. [PubMed Link Image]
  2. Gao B, Gilman AG, Robishaw JD: A second form of the beta subunit of signal-transducing G proteins. Proc Natl Acad Sci U S A. 1987 Sep;84(17):6122-5. [PubMed Link Image]
  3. Glockner G, Scherer S, Schattevoy R, Boright A, Weber J, Tsui LC, Rosenthal A: Large-scale sequencing of two regions in human chromosome 7q22: analysis of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17 genes. Genome Res. 1998 Oct;8(10):1060-73. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Niu J, Profirovic J, Pan H, Vaiskunaite R, Voyno-Yasenetskaya T: G Protein betagamma subunits stimulate p114RhoGEF, a guanine nucleotide exchange factor for RhoA and Rac1: regulation of cell shape and reactive oxygen species production. Circ Res. 2003 Oct 31;93(9):848-56. Epub 2003 Sep 25. [PubMed Link Image]
  6. Waragai M, Nagamitsu S, Xu W, Li YJ, Lin X, Ashizawa T: Ataxin 10 induces neuritogenesis via interaction with G-protein beta2 subunit. J Neurosci Res. 2006 May 15;83(7):1170-8. [PubMed Link Image]
  7. Hill C, Goddard A, Ladds G, Davey J: The cationic region of Rhes mediates its interactions with specific Gbeta subunits. Cell Physiol Biochem. 2009;23(1-3):1-8. Epub 2009 Feb 18. [PubMed Link Image]
Enzyme 98 Metabolite References Not Available
Enzyme 99 [top]
Enzyme 99 ID 14112
Enzyme 99 Name Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3
Enzyme 99 Synonyms
  1. Transducin beta chain 3
Enzyme 99 Gene Name GNB3
Enzyme 99 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3
MGEMEQLRQEAEQLKKQIADARKACADVTLAELVSGLEVVGRVQMRTRRTLRGHLAKIYA
MHWATDSKLLVSASQDGKLIVWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNM
CSIYNLKSREGNVKVSRELSAHTGYLSCCRFLDDNNIVTSSGDTTCALWDIETGQQKTVF
VGHTGDCMSLAVSPDFNLFISGACDASAKLWDVREGTCRQTFTGHESDINAICFFPNGEA
ICTGSDDASCRLFDLRADQELICFSHESIICGITSVAFSLSGRLLFAGYDDFNCNVWDSM
KSERVGILSGHDNRVSCLGVTADGMAVATGSWDSFLKIWN
Enzyme 99 Number of Residues 340
Enzyme 99 Molecular Weight 37220.8
Enzyme 99 Theoretical pI 5.38
Enzyme 99 GO Classification Not Available
Enzyme 99 General Function Involved in GTPase activity
Enzyme 99 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Enzyme 99 Pathways Not Available
Enzyme 99 Reactions Not Available
Enzyme 99 Pfam Domain Function
Enzyme 99 Signals
  • None
Enzyme 99 Transmembrane Regions
  • None
Enzyme 99 Essentiality Not Available
Enzyme 99 GenBank ID Protein 20257502 Link Image
Enzyme 99 UniProtKB/Swiss-Prot ID P16520 Link Image
Enzyme 99 UniProtKB/Swiss-Prot Entry Name GBB3_HUMAN Link Image
Enzyme 99 PDB ID Not Available
Enzyme 99 Cellular Location Not Available
Enzyme 99 Gene Sequence >1023 bp
ATGGGGGAGATGGAGCAACTGCGTCAGGAAGCGGAGCAGCTCAAGAAGCAGATTGCAGAT
GCCAGGAAAGCCTGTGCTGACGTTACTCTGGCAGAGCTGGTGTCTGGCCTAGAGGTGGTG
GGACGAGTCCAGATGCGGACGCGGCGGACGTTAAGGGGACACCTGGCCAAGATTTACGCC
ATGCACTGGGCCACTGATTCTAAGCTGCTGGTAAGTGCCTCGCAAGATGGGAAGCTGATC
GTGTGGGACAGCTACACCACCAACAAGGTGCACGCCATCCCACTGCGCTCCTCCTGGGTC
ATGACCTGTGCCTATGCCCCATCAGGGAACTTTGTGGCGTGTGGGGGGCTGGACAACATG
TGTTCCATCTACAACCTCAAATCCCGTGAGGGCAATGTCAAGGTCAGCCGGGAGCTTTCT
GCTCACACAGGTTATCTCTCCTGCTGCCGCTTCCTGGATGACAACAATATTGTGACCAGC
TCGGGGGACACCACGTGTGCCTTGTGGGACATTGAGACTGGGCAGCAGAAGACTGTATTT
GTGGGACACACGGGTGACTGCATGAGCCTGGCTGTGTCTCCTGACTTCAATCTCTTCATT
TCGGGGGCCTGTGATGCCAGTGCCAAGCTCTGGGATGTGCGAGAGGGGACCTGCCGACAG
ACTTTCACTGGCCACGAGTCGGACATCAACGCCATCTGTTTCTTCCCCAATGGAGAGGCC
ATCTGCACGGGCTCGGATGACGCTTCCTGCCGCTTGTTTGACCTGCGGGCAGACCAGGAG
CTGATCTGCTTCTCCCACGAGAGCATCATCTGCGGCATCACGTCTGTGGCCTTCTCCCTC
AGTGGCCGCCTACTATTCGCTGGCTACGACGACTTCAACTGCAATGTCTGGGACTCCATG
AAGTCTGAGCGTGTGGGCATCCTCTCTGGCCACGATAACAGGGTGAGCTGCCTGGGAGTC
ACAGCTGACGGGATGGCTGTGGCCACAGGTTCCTGGGACAGCTTCCTCAAAATCTGGAAC
TGA
Enzyme 99 GenBank Gene ID AF501884 Link Image
Enzyme 99 GeneCard ID GNB3 Link Image
Enzyme 99 GenAtlas ID GNB3 Link Image
Enzyme 99 HGNC ID HGNC:4400 Link Image
Enzyme 99 Chromosome Location 1
Enzyme 99 Locus 12p13
Enzyme 99 SNPs SNPJam Report Link Image
Enzyme 99 General References
  1. Levine MA, Smallwood PM, Moen PT Jr, Helman LJ, Ahn TG: Molecular cloning of beta 3 subunit, a third form of the G protein beta-subunit polypeptide. Proc Natl Acad Sci U S A. 1990 Mar;87(6):2329-33. [PubMed Link Image]
  2. Ansari-Lari MA, Muzny DM, Lu J, Lu F, Lilley CE, Spanos S, Malley T, Gibbs RA: A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13. Genome Res. 1996 Apr;6(4):314-26. [PubMed Link Image]
  3. Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA: Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. Genome Res. 1997 Mar;7(3):268-80. [PubMed Link Image]
  4. Rosskopf D, Busch S, Manthey I, Siffert W: G protein beta 3 gene: structure, promoter, and additional polymorphisms. Hypertension. 2000 Jul;36(1):33-41. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Hill C, Goddard A, Ladds G, Davey J: The cationic region of Rhes mediates its interactions with specific Gbeta subunits. Cell Physiol Biochem. 2009;23(1-3):1-8. Epub 2009 Feb 18. [PubMed Link Image]
Enzyme 99 Metabolite References Not Available
Enzyme 100 [top]
Enzyme 100 ID 14113
Enzyme 100 Name Guanine nucleotide-binding protein subunit beta-4
Enzyme 100 Synonyms
  1. Transducin beta chain 4
Enzyme 100 Gene Name GNB4
Enzyme 100 Protein Sequence >Guanine nucleotide-binding protein subunit beta-4
MSELEQLRQEAEQLRNQIQDARKACNDATLVQITSNMDSVGRIQMRTRRTLRGHLAKIYA
MHWGYDSRLLVSASQDGKLIIWDSYTTNKMHAIPLRSSWVMTCAYAPSGNYVACGGLDNI
CSIYNLKTREGNVRVSRELPGHTGYLSCCRFLDDSQIVTSSGDTTCALWDIETAQQTTTF
TGHSGDVMSLSLSPDMRTFVSGACDASSKLWDIRDGMCRQSFTGHVSDINAVSFFPNGYA
FATGSDDATCRLFDLRADQELLLYSHDNIICGITSVAFSKSGRLLLAGYDDFNCNVWDTL
KGDRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLRIWN
Enzyme 100 Number of Residues 340
Enzyme 100 Molecular Weight 37566.8
Enzyme 100 Theoretical pI 5.85
Enzyme 100 GO Classification Not Available
Enzyme 100 General Function Involved in signal transducer activity
Enzyme 100 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Enzyme 100 Pathways Not Available
Enzyme 100 Reactions Not Available
Enzyme 100 Pfam Domain Function
Enzyme 100 Signals
  • None
Enzyme 100 Transmembrane Regions
  • None
Enzyme 100 Essentiality Not Available
Enzyme 100 GenBank ID Protein 20257506 Link Image
Enzyme 100 UniProtKB/Swiss-Prot ID Q9HAV0 Link Image
Enzyme 100 UniProtKB/Swiss-Prot Entry Name GBB4_HUMAN Link Image
Enzyme 100 PDB ID 1OMW Link Image
Enzyme 100 PDB File Show
Enzyme 100 3D Structure
Enzyme 100 Cellular Location Not Available
Enzyme 100 Gene Sequence >1023 bp
ATGAGCGAGCTGGAGCAGCTGAGGCAGGAGGCTGAACAGCTTCGGAATCAGATCCAGGAT
GCTCGGAAGGCCTGCAATGATGCCACGCTGGTTCAGATCACGTCTAATATGGACTCCGTG
GGCCGAATACAAATGCGAACAAGGCGCACGCTGCGCGGCCACCTCGCTAAGATCTACGCC
ATGCACTGGGGATATGATTCCAGGCTACTAGTCAGTGCTTCGCAAGATGGAAAATTAATT
ATTTGGGATAGCTATACGACAAATAAGATGCACGCCATCCCTCTGAGGTCCTCCTGGGTG
ATGACCTGTGCCTACGCCCCGTCCGGGAACTACGTTGCCTGTGGAGGCTTGGATAACATC
TGCTCCATATACAACCTAAAGACCCGAGAGGGGAATGTGCGGGTGAGCCGAGAATTGCCA
GGACACACGGGCTACTTGTCCTGCTGCCGATTCTTAGATGATGGACAAATCATTACAAGT
TCGGGAGACACGACTTGTGCTTTGTGGGACATTGAGACCGGACAGCAGACTACGACCTTC
ACGGGACACTCGGGTGACGTGATGAGCCTCTCACTGAGTCCTGACTTGAAGACCTTTGTG
TCTGGTGCTTGTGATGCATCCTCAAAGCTGTGGGATATCCGAGATGGGATGTGTAGACAG
TCTTTCACCGGACACATCTCAGACATCAACGCTGTCAGTTTCTTCCCGAGTGTATATGCC
TTTGCCACTGGTTCTGATGATGCCACATGCCGACTCTTTGACCTCCGTGCAGACCAGGAG
CTCCTGCTATACTCTCATGACAATATCATCTGTGGCATTACTTCTGTGGCCTTCTCAAAG
AGTGGGCGCCTCCTGTTAGCCGGCTATGACGACTTCAACTGCAGTGTGTGGGACGCTCTG
AAAGGAGGCCGGTCAGGTGTCCTTGCTGGTCATGACAACCGTGTTAGCTGCTTAGGTGTG
ACTGATGACGGCATGGCTGTGGCCACTGGCTCCTGGGACAGTTTTCTTAGAATCTGGAAT
TGA
Enzyme 100 GenBank Gene ID AF501886 Link Image
Enzyme 100 GeneCard ID GNB4 Link Image
Enzyme 100 GenAtlas ID GNB4 Link Image
Enzyme 100 HGNC ID HGNC:20731 Link Image
Enzyme 100 Chromosome Location 3
Enzyme 100 Locus 3q26.33
Enzyme 100 SNPs SNPJam Report Link Image
Enzyme 100 General References
  1. Ruiz-Velasco V, Ikeda SR, Puhl HL: Cloning, tissue distribution, and functional expression of the human G protein beta 4-subunit. Physiol Genomics. 2002 Feb 11;8(1):41-50. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 100 Metabolite References Not Available
Enzyme 101 [top]
Enzyme 101 ID 14114
Enzyme 101 Name Guanine nucleotide-binding protein subunit beta-5
Enzyme 101 Synonyms
  1. Gbeta5
  2. Transducin beta chain 5
Enzyme 101 Gene Name GNB5
Enzyme 101 Protein Sequence >Guanine nucleotide-binding protein subunit beta-5
MCDQTFLVNVFGSCDKCFKQRALRPVFKKSQQLSYCSTCAEIMATEGLHENETLASLKSE
AESLKGKLEEERAKLHDVELHQVAERVEALGQFVMKTRRTLKGHGNKVLCMDWCKDKRRI
VSSSQDGKVIVWDSFTTNKEHAVTMPCTWVMACAYAPSGCAIACGGLDNKCSVYPLTFDK
NENMAAKKKSVAMHTNYLSACSFTNSDMQILTASGDGTCALWDVESGQLLQSFHGHGADV
LCLDLAPSETGNTFVSGGCDKKAMVWDMRSGQCVQAFETHESDINSVRYYPSGDAFASGS
DDATCRLYDLRADREVAIYSKESIIFGASSVDFSLSGRLLFAGYNDYTINVWDVLKGSRV
SILFGHENRVSTLRVSPDGTAFCSGSWDHTLRVWA
Enzyme 101 Number of Residues 395
Enzyme 101 Molecular Weight 43565.9
Enzyme 101 Theoretical pI 6.42
Enzyme 101 GO Classification Not Available
Enzyme 101 General Function Involved in GTPase activity
Enzyme 101 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Enzyme 101 Pathways Not Available
Enzyme 101 Reactions Not Available
Enzyme 101 Pfam Domain Function
Enzyme 101 Signals
  • None
Enzyme 101 Transmembrane Regions
  • None
Enzyme 101 Essentiality Not Available
Enzyme 101 GenBank ID Protein 20336270 Link Image
Enzyme 101 UniProtKB/Swiss-Prot ID O14775 Link Image
Enzyme 101 UniProtKB/Swiss-Prot Entry Name GBB5_HUMAN Link Image
Enzyme 101 PDB ID Not Available
Enzyme 101 Cellular Location Not Available
Enzyme 101 Gene Sequence >1188 bp
ATGTGTGATCAGACCTTTCTCGTTAATGTATTTGGCTCATGTGACAAATGTTTCAAACAA
CGAGCTCTGAGACCAGTTTTCAAGAAGTCTCAACAACTCAGCTACTGTTCAACATGTGCA
GAAATTATGGCAACCGAGGGGCTGCACGAGAACGAGACGCTGGCGTCGCTGAAGAGCGAG
GCCGAGAGCCTCAAGGGCAAGCTGGAGGAGGAGCGAGCCAAGCTGCACGATGTGGAGCTG
CACCAGGTGGCGGAGCGGGTGGAGGCCCTGGGGCAGTTTGTCATGAAGACCAGAAGGACC
CTCAAAGGCCACGGGAACAAAGTCCTGTGCATGGACTGGTGCAAAGATAAGAGGAGGATC
GTGAGCTCGTCACAGGATGGGAAGGTGATCGTGTGGGATTCCTTCACCACAAACAAGGAG
CACGCGGTCACCATGCCCTGCACGTGGGTGATGGCATGTGCTTATGCCCCATCGGGATGT
GCCATTGCTTGTGGTGGTTTGGATAATAAGTGTTCTGTGTACCCCTTGACGTTTGACAAA
AATGAAAACATGGCTGCCAAAAAGAAGTCTGTTGCTATGCACACCAACTACCTGTCGGCC
TGCAGCTTCACCAACTCTGACATGCAGATCCTGACAGCGAGCGGCGATGGCACATGTGCC
CTGTGGGACGTGGAGAGCGGGCAGCTGCTGCAGAGCTTCCACGGACATGGGGCTGACGTC
CTCTGCTTGGACCTGGCCCCCTCAGAAACTGGAAACACCTTCGTGTCTGGGGGATGTGAC
AAGAAAGCCATGGTGTGGGACATGCGCTCCGGCCAGTGCGTGCAGGCCTTTGAAACACAT
GAATCTGACATCAACAGTGTCCGGTACTACCCCAGTGGAGATGCCTTTGCTTCAGGGTCA
GATGACGCTACGTGTCGCCTCTATGACCTGCGGGCAGATAGGGAGGTTGCCATCTATTCC
AAAGAAAGCATCATATTTGGAGCATCCAGCGTGGACTTCTCCCTCAGTGGTCGCCTGCTG
TTTGCTGGATACAATGATTACACTATCAACGTCTGGGATGTTCTCAAAGGGTCCCGGGTC
TCCATCCTGTTTGGACATGAAAACCGCGTTAGCACTCTACGAGTTTCCCCCGATGGGACT
GCTTTCTGCTCTGGATCATGGGATCATACCCTCAGAGTCTGGGCCTAA
Enzyme 101 GenBank Gene ID NM_016194.3 Link Image
Enzyme 101 GeneCard ID GNB5 Link Image
Enzyme 101 GenAtlas ID GNB5 Link Image
Enzyme 101 HGNC ID HGNC:4401 Link Image
Enzyme 101 Chromosome Location 1
Enzyme 101 Locus 15q21.2
Enzyme 101 SNPs SNPJam Report Link Image
Enzyme 101 General References
  1. Jones PG, Lombardi SJ, Cockett MI: Cloning and tissue distribution of the human G protein beta 5 cDNA. Biochim Biophys Acta. 1998 Apr 24;1402(3):288-91. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 101 Metabolite References Not Available
Enzyme 102 [top]
Enzyme 102 ID 14116
Enzyme 102 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10
Enzyme 102 Synonyms Not Available
Enzyme 102 Gene Name GNG10
Enzyme 102 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10
MSSGASASALQRLVEQLKLEAGVERIKVSQAAAELQQYCMQNACKDALLVGVPAGSNPFR
EPRSCALL
Enzyme 102 Number of Residues 68
Enzyme 102 Molecular Weight 7205.2
Enzyme 102 Theoretical pI 8.04
Enzyme 102 GO Classification
Function
  • molecular transducer activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • extrinsic to membrane
  • extrinsic to plasma membrane
  • heterotrimeric G-protein complex
  • membrane part
Enzyme 102 General Function Involved in signal transducer activity
Enzyme 102 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. Interacts with beta-1 and beta-2, but not with beta-3
Enzyme 102 Pathways Not Available
Enzyme 102 Reactions Not Available
Enzyme 102 Pfam Domain Function
Enzyme 102 Signals
  • None
Enzyme 102 Transmembrane Regions
  • None
Enzyme 102 Essentiality Not Available
Enzyme 102 GenBank ID Protein 20147647 Link Image
Enzyme 102 UniProtKB/Swiss-Prot ID P50151 Link Image
Enzyme 102 UniProtKB/Swiss-Prot Entry Name GBG10_HUMAN Link Image
Enzyme 102 PDB ID Not Available
Enzyme 102 Cellular Location Not Available
Enzyme 102 Gene Sequence >207 bp
ATGTCCTCCGGGGCTAGCGCGAGCGCCCTGCAGCGCTTGGTAGAGCAGCTCAAGTTGGAG
GCTGGCGTGGAGAGGATCAAGGTCTCTCAGGCAGCTGCAGAGCTTCAACAGTACTGTATG
CAGAATGCCTGCAAGGATGCCCTGCTGGTGGGTGTTCCAGCTGGAAGTAACCCCTTCCGG
GAGCCTAGATCCTGTGCTTTACTCTGA
Enzyme 102 GenBank Gene ID AF493877 Link Image
Enzyme 102 GeneCard ID GNG10 Link Image
Enzyme 102 GenAtlas ID GNG10 Link Image
Enzyme 102 HGNC ID HGNC:4402 Link Image
Enzyme 102 Chromosome Location 9
Enzyme 102 Locus 9q31.3
Enzyme 102 SNPs SNPJam Report Link Image
Enzyme 102 General References
  1. Ray K, Kunsch C, Bonner LM, Robishaw JD: Isolation of cDNA clones encoding eight different human G protein gamma subunits, including three novel forms designated the gamma 4, gamma 10, and gamma 11 subunits. J Biol Chem. 1995 Sep 15;270(37):21765-71. [PubMed Link Image]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 102 Metabolite References Not Available
Enzyme 103 [top]
Enzyme 103 ID 14117
Enzyme 103 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12
Enzyme 103 Synonyms Not Available
Enzyme 103 Gene Name GNG12
Enzyme 103 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12
MSSKTASTNNIAQARRTVQQLRLEASIERIKVSKASADLMSYCEEHARSDPLLIGIPTSE
NPFKDKKTCIIL
Enzyme 103 Number of Residues 72
Enzyme 103 Molecular Weight 8006.1
Enzyme 103 Theoretical pI 9.38
Enzyme 103 GO Classification
Function
  • molecular transducer activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • extrinsic to membrane
  • extrinsic to plasma membrane
  • heterotrimeric G-protein complex
  • membrane part
Enzyme 103 General Function Involved in signal transducer activity
Enzyme 103 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Enzyme 103 Pathways Not Available
Enzyme 103 Reactions Not Available
Enzyme 103 Pfam Domain Function
Enzyme 103 Signals
  • None
Enzyme 103 Transmembrane Regions
  • None
Enzyme 103 Essentiality Not Available
Enzyme 103 GenBank ID Protein 6563252 Link Image
Enzyme 103 UniProtKB/Swiss-Prot ID Q9UBI6 Link Image
Enzyme 103 UniProtKB/Swiss-Prot Entry Name GBG12_HUMAN Link Image
Enzyme 103 PDB ID Not Available
Enzyme 103 Cellular Location Not Available
Enzyme 103 Gene Sequence >219 bp
ATGTCCAGCAAAACAGCAAGCACCAACAATATAGCCCAGGCAAGGAGAACTGTGCAGCAG
TTAAGATTAGAAGCCTCCATTGAAAGAATAAAGGTTTCGAAGGCATCAGCGGACCTCATG
TCCTACTGTGAGGAACATGCCAGGAGTGACCCTTTGCTGATAGGAATACCAACTTCAGAA
AACCCTTTCAAGGATAAAAAAACTTGCATCATCTTATAG
Enzyme 103 GenBank Gene ID AF119663 Link Image
Enzyme 103 GeneCard ID GNG12 Link Image
Enzyme 103 GenAtlas ID GNG12 Link Image
Enzyme 103 HGNC ID HGNC:19663 Link Image
Enzyme 103 Chromosome Location 1
Enzyme 103 Locus 1p31.3
Enzyme 103 SNPs SNPJam Report Link Image
Enzyme 103 General References
  1. Hurowitz EH, Melnyk JM, Chen YJ, Kouros-Mehr H, Simon MI, Shizuya H: Genomic characterization of the human heterotrimeric G protein alpha, beta, and gamma subunit genes. DNA Res. 2000 Apr 28;7(2):111-20. [PubMed Link Image]
  2. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed Link Image]
  3. Cook LA, Schey KL, Cleator JH, Wilcox MD, Dingus J, Hildebrandt JD: Identification of a region in G protein gamma subunits conserved across species but hypervariable among subunit isoforms. Protein Sci. 2001 Dec;10(12):2548-55. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  6. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 103 Metabolite References Not Available
Enzyme 104 [top]
Enzyme 104 ID 14118
Enzyme 104 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13
Enzyme 104 Synonyms Not Available
Enzyme 104 Gene Name GNG13
Enzyme 104 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13
MEEWDVPQMKKEVESLKYQLAFQREMASKTIPELLKWIEDGIPKDPFLNPDLMKNNPWVE
KGKCTIL
Enzyme 104 Number of Residues 67
Enzyme 104 Molecular Weight 7949.3
Enzyme 104 Theoretical pI 4.76
Enzyme 104 GO Classification
Function
  • molecular transducer activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • extrinsic to membrane
  • extrinsic to plasma membrane
  • heterotrimeric G-protein complex
  • membrane part
Enzyme 104 General Function Involved in signal transducer activity
Enzyme 104 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Enzyme 104 Pathways Not Available
Enzyme 104 Reactions Not Available
Enzyme 104 Pfam Domain Function
Enzyme 104 Signals
  • None
Enzyme 104 Transmembrane Regions
  • None
Enzyme 104 Essentiality Not Available
Enzyme 104 GenBank ID Protein 7259306 Link Image
Enzyme 104 UniProtKB/Swiss-Prot ID Q9P2W3 Link Image
Enzyme 104 UniProtKB/Swiss-Prot Entry Name GBG13_HUMAN Link Image
Enzyme 104 PDB ID Not Available
Enzyme 104 Cellular Location Not Available
Enzyme 104 Gene Sequence >204 bp
ATGGAGGAGTGGGACGTGCCACAGATGAAGAAAGAGGTGGAGAGCCTTAAGTACCAGCTG
GCCTTCCAGCGGGAGATGGCGTCCAAGACCATCCCCGAGCTGCTGAAGTGGATCGAGGAC
GGGATCCCCAAGGACCCCTTCCTGAACCCCGACCTGATGAAGAACAACCCATGGGTGGAA
AAGGGCAAATGCACCATCCTGTGA
Enzyme 104 GenBank Gene ID AB030207 Link Image
Enzyme 104 GeneCard ID GNG13 Link Image
Enzyme 104 GenAtlas ID GNG13 Link Image
Enzyme 104 HGNC ID HGNC:14131 Link Image
Enzyme 104 Chromosome Location 1
Enzyme 104 Locus 16p13.3
Enzyme 104 SNPs SNPJam Report Link Image
Enzyme 104 General References
  1. Huang L, Shanker YG, Dubauskaite J, Zheng JZ, Yan W, Rosenzweig S, Spielman AI, Max M, Margolskee RF: Ggamma13 colocalizes with gustducin in taste receptor cells and mediates IP3 responses to bitter denatonium. Nat Neurosci. 1999 Dec;2(12):1055-62. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  4. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 104 Metabolite References Not Available
Enzyme 105 [top]
Enzyme 105 ID 14119
Enzyme 105 Name Guanine nucleotide-binding protein G(T) subunit gamma-T1
Enzyme 105 Synonyms
  1. Transducin gamma chain
Enzyme 105 Gene Name GNGT1
Enzyme 105 Protein Sequence >Guanine nucleotide-binding protein G(T) subunit gamma-T1
MPVINIEDLTEKDKLKMEVDQLKKEVTLERMLVSKCCEEVRDYVEERSGEDPLVKGIPED
KNPFKELKGGCVIS
Enzyme 105 Number of Residues 74
Enzyme 105 Molecular Weight 8495.8
Enzyme 105 Theoretical pI 4.47
Enzyme 105 GO Classification
Function
  • molecular transducer activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • extrinsic to membrane
  • extrinsic to plasma membrane
  • heterotrimeric G-protein complex
  • membrane part
Enzyme 105 General Function Involved in signal transducer activity
Enzyme 105 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Enzyme 105 Pathways Not Available
Enzyme 105 Reactions Not Available
Enzyme 105 Pfam Domain Function
Enzyme 105 Signals
  • None
Enzyme 105 Transmembrane Regions
  • None
Enzyme 105 Essentiality Not Available
Enzyme 105 GenBank ID Protein 41393496 Link Image
Enzyme 105 UniProtKB/Swiss-Prot ID P63211 Link Image
Enzyme 105 UniProtKB/Swiss-Prot Entry Name GBG1_HUMAN Link Image
Enzyme 105 PDB ID 1B9Y Link Image
Enzyme 105 PDB File Show
Enzyme 105 3D Structure
Enzyme 105 Cellular Location Not Available
Enzyme 105 Gene Sequence >225 bp
ATGCCAGTAATCAATATTGAGGACCTGACAGAAAAGGACAAATTGAAGATGGAAGTTGAC
CAGCTCAAGAAAGAAGTGACACTGGAAAGAATGCTAGTTTCCAAATGTTGTGAAGAAGTA
AGAGATTACGTTGAAGAACGATCTGGCGAGGATCCACTGGTAAAGGGCATCCCAGAGGAC
AAAAATCCCTTCAAGGAGCTCAAAGGAGGCTGTGTGATTTCATAA
Enzyme 105 GenBank Gene ID AC002076 Link Image
Enzyme 105 GeneCard ID GNGT1 Link Image
Enzyme 105 GenAtlas ID GNGT1 Link Image
Enzyme 105 HGNC ID HGNC:4411 Link Image
Enzyme 105 Chromosome Location 7
Enzyme 105 Locus 7q21.3
Enzyme 105 SNPs SNPJam Report Link Image
Enzyme 105 General References
  1. Tao L, Pandey S, Simon MI, Fong HK: Structure of the bovine transducin gamma subunit gene and analysis of promoter function in transgenic mice. Exp Eye Res. 1993 Apr;56(4):497-507. [PubMed Link Image]
  2. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Scherer SW, Feinstein DS, Oliveira L, Tsui LC, Pittler SJ: Gene structure and chromosome localization to 7q21.3 of the human rod photoreceptor transducin gamma-subunit gene (GNGT1). Genomics. 1996 Jul 1;35(1):241-3. [PubMed Link Image]
Enzyme 105 Metabolite References Not Available
Enzyme 106 [top]
Enzyme 106 ID 14120
Enzyme 106 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3
Enzyme 106 Synonyms Not Available
Enzyme 106 Gene Name GNG3
Enzyme 106 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3
MKGETPVNSTMSIGQARKMVEQLKIEASLCRIKVSKAAADLMTYCDAHACEDPLITPVPT
SENPFREKKFFCALL
Enzyme 106 Number of Residues 75
Enzyme 106 Molecular Weight 8304.7
Enzyme 106 Theoretical pI 7.93
Enzyme 106 GO Classification
Function
  • molecular transducer activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • extrinsic to membrane
  • extrinsic to plasma membrane
  • heterotrimeric G-protein complex
  • membrane part
Enzyme 106 General Function Involved in signal transducer activity
Enzyme 106 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Enzyme 106 Pathways Not Available
Enzyme 106 Reactions Not Available
Enzyme 106 Pfam Domain Function
Enzyme 106 Signals
  • None
Enzyme 106 Transmembrane Regions
  • None
Enzyme 106 Essentiality Not Available
Enzyme 106 GenBank ID Protein 33150642 Link Image
Enzyme 106 UniProtKB/Swiss-Prot ID P63215 Link Image
Enzyme 106 UniProtKB/Swiss-Prot Entry Name GBG3_HUMAN Link Image
Enzyme 106 PDB ID Not Available
Enzyme 106 Cellular Location Not Available
Enzyme 106 Gene Sequence >228 bp
ATGAAAGGTGAGACCCCGGTGAACAGCACTATGAGTATTGGGCAAGCACGCAAGATGGTG
GAACAGCTTAAGATTGAAGCCAGCTTGTGTCGGATAAAGGTGTCCAAGGCAGCAGCAGAC
CTGATGACTTACTGTGATGCCCACGCCTGTGAGGATCCCCTCATCACCCCTGTGCCCACT
TCGGAGAACCCCTTCCGGGAGAAGAAGTTCTTCTGTGCTCTCCTCTGA
Enzyme 106 GenBank Gene ID AF087900 Link Image
Enzyme 106 GeneCard ID GNG3 Link Image
Enzyme 106 GenAtlas ID GNG3 Link Image
Enzyme 106 HGNC ID HGNC:4405 Link Image
Enzyme 106 Chromosome Location 1
Enzyme 106 Locus 11p11
Enzyme 106 SNPs SNPJam Report Link Image
Enzyme 106 General References
  1. Hurowitz EH, Melnyk JM, Chen YJ, Kouros-Mehr H, Simon MI, Shizuya H: Genomic characterization of the human heterotrimeric G protein alpha, beta, and gamma subunit genes. DNA Res. 2000 Apr 28;7(2):111-20. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 106 Metabolite References Not Available
Enzyme 107 [top]
Enzyme 107 ID 14121
Enzyme 107 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-4
Enzyme 107 Synonyms Not Available
Enzyme 107 Gene Name GNG4
Enzyme 107 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-4
MKEGMSNNSTTSISQARKAVEQLKMEACMDRVKVSQAAADLLAYCEAHVREDPLIIPVPA
SENPFREKKFFCTIL
Enzyme 107 Number of Residues 75
Enzyme 107 Molecular Weight 8388.6
Enzyme 107 Theoretical pI 7.19
Enzyme 107 GO Classification
Function
  • molecular transducer activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • extrinsic to membrane
  • extrinsic to plasma membrane
  • heterotrimeric G-protein complex
  • membrane part
Enzyme 107 General Function Involved in signal transducer activity
Enzyme 107 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Enzyme 107 Pathways Not Available
Enzyme 107 Reactions Not Available
Enzyme 107 Pfam Domain Function
Enzyme 107 Signals
  • None
Enzyme 107 Transmembrane Regions
  • None
Enzyme 107 Essentiality Not Available
Enzyme 107 GenBank ID Protein 20147637 Link Image
Enzyme 107 UniProtKB/Swiss-Prot ID P50150 Link Image
Enzyme 107 UniProtKB/Swiss-Prot Entry Name GBG4_HUMAN Link Image
Enzyme 107 PDB ID Not Available
Enzyme 107 Cellular Location Not Available
Enzyme 107 Gene Sequence >228 bp
ATGAAAGAGGGCATGTCTAATAACAGCACCACTAGCATCTCCCAAGCCAGGAAAGCTGTG
GAGCAGCTAAAGATGGAAGCCTGTATGGACAGGGTCAAGGTCTCCCAGGCAGCCGCGGAC
CTCCTGGCCTACTGTGAAGCTCACGTGCGGGAAGATCCTCTCATCATTCCAGTGCCTGCA
TCAGAAAACCCCTTTCGCGAGAAGAAGTTCTTTTGTACCATTCTCTAA
Enzyme 107 GenBank Gene ID AF493872 Link Image
Enzyme 107 GeneCard ID GNG4 Link Image
Enzyme 107 GenAtlas ID GNG4 Link Image
Enzyme 107 HGNC ID HGNC:4407 Link Image
Enzyme 107 Chromosome Location 1
Enzyme 107 Locus 1q42.3
Enzyme 107 SNPs SNPJam Report Link Image
Enzyme 107 General References
  1. Ray K, Kunsch C, Bonner LM, Robishaw JD: Isolation of cDNA clones encoding eight different human G protein gamma subunits, including three novel forms designated the gamma 4, gamma 10, and gamma 11 subunits. J Biol Chem. 1995 Sep 15;270(37):21765-71. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 107 Metabolite References Not Available
Enzyme 108 [top]
Enzyme 108 ID 14122
Enzyme 108 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5
Enzyme 108 Synonyms Not Available
Enzyme 108 Gene Name GNG5
Enzyme 108 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5
MSGSSSVAAMKKVVQQLRLEAGLNRVKVSQAAADLKQFCLQNAQHDPLLTGVSSSTNPFR
PQKVCSFL
Enzyme 108 Number of Residues 68
Enzyme 108 Molecular Weight 7318.4
Enzyme 108 Theoretical pI 10.62
Enzyme 108 GO Classification
Function
  • molecular transducer activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • extrinsic to membrane
  • extrinsic to plasma membrane
  • heterotrimeric G-protein complex
  • membrane part
Enzyme 108 General Function Involved in signal transducer activity
Enzyme 108 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Enzyme 108 Pathways Not Available
Enzyme 108 Reactions Not Available
Enzyme 108 Pfam Domain Function
Enzyme 108 Signals
  • None
Enzyme 108 Transmembrane Regions
  • None
Enzyme 108 Essentiality Not Available
Enzyme 108 GenBank ID Protein 3329380 Link Image
Enzyme 108 UniProtKB/Swiss-Prot ID P63218 Link Image
Enzyme 108 UniProtKB/Swiss-Prot Entry Name GBG5_HUMAN Link Image
Enzyme 108 PDB ID Not Available
Enzyme 108 Cellular Location Not Available
Enzyme 108 Gene Sequence >207 bp
ATGTCTGGCTCCTCCAGCGTCGCCGCTATGAAGAAAGTGGTTCAACAGCTCCGGCTGGAG
GCCGGACTCAACCGCGTAAAAGTTTCCCAGGCAGCTGCAGACTTGAAACAGTTCTGTCTG
CAGAATGCTCAACATGACCCTCTGCTGACTGGAGTATCTTCAAGTACAAATCCCTTCAGA
CCCCAGAAAGTCTGTTCCTTTTTGTAG
Enzyme 108 GenBank Gene ID AF038955 Link Image
Enzyme 108 GeneCard ID GNG5 Link Image
Enzyme 108 GenAtlas ID GNG5 Link Image
Enzyme 108 HGNC ID HGNC:4408 Link Image
Enzyme 108 Chromosome Location 1
Enzyme 108 Locus 1p22
Enzyme 108 SNPs SNPJam Report Link Image
Enzyme 108 General References
  1. Liu B, Aronson NN Jr: Structure of human G protein G gamma 5 gene GNG5. Biochem Biophys Res Commun. 1998 Oct 9;251(1):88-94. [PubMed Link Image]
  2. Mao M, Fu G, Wu JS, Zhang QH, Zhou J, Kan LX, Huang QH, He KL, Gu BW, Han ZG, Shen Y, Gu J, Yu YP, Xu SH, Wang YX, Chen SJ, Chen Z: Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning. Proc Natl Acad Sci U S A. 1998 Jul 7;95(14):8175-80. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
Enzyme 108 Metabolite References Not Available
Enzyme 109 [top]
Enzyme 109 ID 14123
Enzyme 109 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7
Enzyme 109 Synonyms Not Available
Enzyme 109 Gene Name GNG7
Enzyme 109 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7
MSATNNIAQARKLVEQLRIEAGIERIKVSKAASDLMSYCEQHARNDPLLVGVPASENPFK
DKKPCIIL
Enzyme 109 Number of Residues 68
Enzyme 109 Molecular Weight 7521.7
Enzyme 109 Theoretical pI 8.77
Enzyme 109 GO Classification
Function
  • molecular transducer activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • extrinsic to membrane
  • extrinsic to plasma membrane
  • heterotrimeric G-protein complex
  • membrane part
Enzyme 109 General Function Involved in signal transducer activity
Enzyme 109 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. Plays a role in the regulation of adenylyl cyclase signaling in certain regions of the brain. Plays a role in the formation or stabilzation of a G protein heterotrimer (G(olf) subunit alpha-beta-gamma-7) that is required for adenylyl cyclase activity in the striatum
Enzyme 109 Pathways Not Available
Enzyme 109 Reactions Not Available
Enzyme 109 Pfam Domain Function
Enzyme 109 Signals
  • None
Enzyme 109 Transmembrane Regions
  • None
Enzyme 109 Essentiality Not Available
Enzyme 109 GenBank ID Protein 3149954 Link Image
Enzyme 109 UniProtKB/Swiss-Prot ID O60262 Link Image
Enzyme 109 UniProtKB/Swiss-Prot Entry Name GBG7_HUMAN Link Image
Enzyme 109 PDB ID Not Available
Enzyme 109 Cellular Location Not Available
Enzyme 109 Gene Sequence >207 bp
ATGTCAGCCACTAACAACATAGCCCAGGCCCGGAAGCTGGTGGAACAGCTACGCATAGAA
GCCGGGATTGAGCGCATCAAGGTCTCCAAAGCGGCGTCTGACCTCATGAGCTACTGTGAG
CAACATGCTCGGAACGACCCCCTGCTGGTCGGAGTCCCTGCCTCGGAGAACCCCTTTAAG
GACAAGAAACCTTGTATTATTTTATAA
Enzyme 109 GenBank Gene ID AB010414 Link Image
Enzyme 109 GeneCard ID GNG7 Link Image
Enzyme 109 GenAtlas ID GNG7 Link Image
Enzyme 109 HGNC ID HGNC:4410 Link Image
Enzyme 109 Chromosome Location 1
Enzyme 109 Locus 19p13.3
Enzyme 109 SNPs SNPJam Report Link Image
Enzyme 109 General References
  1. Shibata K, Mori M, Tanaka S, Kitano S, Akiyoshi T: Identification and cloning of human G-protein gamma 7, down-regulated in pancreatic cancer. Biochem Biophys Res Commun. 1998 May 8;246(1):205-9. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Ohta M, Mimori K, Fukuyoshi Y, Kita Y, Motoyama K, Yamashita K, Ishii H, Inoue H, Mori M: Clinical significance of the reduced expression of G protein gamma 7 (GNG7) in oesophageal cancer. Br J Cancer. 2008 Jan 29;98(2):410-7. Epub 2008 Jan 22. [PubMed Link Image]
Enzyme 109 Metabolite References Not Available
Enzyme 110 [top]
Enzyme 110 ID 14124
Enzyme 110 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-8
Enzyme 110 Synonyms
  1. Gamma-9
Enzyme 110 Gene Name GNG8
Enzyme 110 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-8
MSNNMAKIAEARKTVEQLKLEVNIDRMKVSQAAAELLAFCETHAKDDPLVTPVPAAENPF
RDKRLFCVLL
Enzyme 110 Number of Residues 70
Enzyme 110 Molecular Weight 7841.1
Enzyme 110 Theoretical pI 7.27
Enzyme 110 GO Classification
Function
  • molecular transducer activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • extrinsic to membrane
  • extrinsic to plasma membrane
  • heterotrimeric G-protein complex
  • membrane part
Enzyme 110 General Function Involved in signal transducer activity
Enzyme 110 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Enzyme 110 Pathways Not Available
Enzyme 110 Reactions Not Available
Enzyme 110 Pfam Domain Function
Enzyme 110 Signals
  • None
Enzyme 110 Transmembrane Regions
  • None
Enzyme 110 Essentiality Not Available
Enzyme 110 GenBank ID Protein 6164867 Link Image
Enzyme 110 UniProtKB/Swiss-Prot ID Q9UK08 Link Image
Enzyme 110 UniProtKB/Swiss-Prot Entry Name GBG8_HUMAN Link Image
Enzyme 110 PDB ID Not Available
Enzyme 110 Cellular Location Not Available
Enzyme 110 Gene Sequence >213 bp
ATGTCCAACAACATGGCCAAGATTGCCGAGGCCCGCAAGACGGTGGAACAGCTGAAGCTG
GAGGTGAACATCGACCGCATGAAGGTGTCGCAGGCAGCAGCGGAACTCCTGGCTTTCTGC
GAGACGCATGCCAAAGATGACCCGCTGGTGACGCCAGTACCCGCCGCGGAGAACCCCTTC
CGCGACAAGCGCCTCTTTTGTGTTCTGCTCTGA
Enzyme 110 GenBank Gene ID AF188179 Link Image
Enzyme 110 GeneCard ID GNG8 Link Image
Enzyme 110 GenAtlas ID GNG8 Link Image
Enzyme 110 HGNC ID HGNC:19664 Link Image
Enzyme 110 Chromosome Location 1
Enzyme 110 Locus 19q13.32
Enzyme 110 SNPs SNPJam Report Link Image
Enzyme 110 General References
  1. Hurowitz EH, Melnyk JM, Chen YJ, Kouros-Mehr H, Simon MI, Shizuya H: Genomic characterization of the human heterotrimeric G protein alpha, beta, and gamma subunit genes. DNA Res. 2000 Apr 28;7(2):111-20. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 110 Metabolite References Not Available
Enzyme 111 [top]
Enzyme 111 ID 14125
Enzyme 111 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-T2
Enzyme 111 Synonyms
  1. G gamma-C
  2. G-gamma-8
  3. G-gamma-9
Enzyme 111 Gene Name GNGT2
Enzyme 111 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-T2
MAQDLSEKDLLKMEVEQLKKEVKNTRIPISKAGKEIKEYVEAQAGNDPFLKGIPEDKNPF
KEKGGCLIS
Enzyme 111 Number of Residues 69
Enzyme 111 Molecular Weight 7746.9
Enzyme 111 Theoretical pI 6.73
Enzyme 111 GO Classification
Function
  • molecular transducer activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • extrinsic to membrane
  • extrinsic to plasma membrane
  • heterotrimeric G-protein complex
  • membrane part
Enzyme 111 General Function Involved in signal transducer activity
Enzyme 111 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Enzyme 111 Pathways Not Available
Enzyme 111 Reactions Not Available
Enzyme 111 Pfam Domain Function
Enzyme 111 Signals
  • None
Enzyme 111 Transmembrane Regions
  • None
Enzyme 111 Essentiality Not Available
Enzyme 111 GenBank ID Protein 2392823 Link Image
Enzyme 111 UniProtKB/Swiss-Prot ID O14610 Link Image
Enzyme 111 UniProtKB/Swiss-Prot Entry Name GBGT2_HUMAN Link Image
Enzyme 111 PDB ID Not Available
Enzyme 111 Cellular Location Not Available
Enzyme 111 Gene Sequence >210 bp
ATGGCCCAGGATCTCAGCGAGAAGGACCTGTTGAAGATGGAGGTGGAGCAGCTGAAGAAA
GAAGTGAAAAACACAAGAATTCCGATTTCCAAAGCGGGAAAGGAAATCAAGGAGTACGTG
GAGGCCCAAGCAGGAAACGATCCTTTTCTCAAAGGCATCCCTGAGGACAAGAATCCCTTC
AAGGAGAAAGGTGGCTGTCTGATAAGCTGA
Enzyme 111 GenBank Gene ID AF001160 Link Image
Enzyme 111 GeneCard ID GNGT2 Link Image
Enzyme 111 GenAtlas ID GNGT2 Link Image
Enzyme 111 HGNC ID HGNC:4412 Link Image
Enzyme 111 Chromosome Location 1
Enzyme 111 Locus 17q21
Enzyme 111 SNPs SNPJam Report Link Image
Enzyme 111 General References
  1. Ong OC, Hu K, Rong H, Lee RH, Fung BK: Gene structure and chromosome localization of the G gamma c subunit of human cone G-protein (GNGT2). Genomics. 1997 Aug 15;44(1):101-9. [PubMed Link Image]
  2. Cook LA, Schey KL, Cleator JH, Wilcox MD, Dingus J, Hildebrandt JD: Identification of a region in G protein gamma subunits conserved across species but hypervariable among subunit isoforms. Protein Sci. 2001 Dec;10(12):2548-55. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 111 Metabolite References Not Available
Enzyme 112 [top]
Enzyme 112 ID 14143
Enzyme 112 Name Guanine nucleotide-binding protein-like 1
Enzyme 112 Synonyms
  1. GTP-binding protein HSR1
Enzyme 112 Gene Name GNL1
Enzyme 112 Protein Sequence >Guanine nucleotide-binding protein-like 1
MPRKKPFSVKQKKKQLQDKRERKRGLQDGLRSSSNSRSGSRERREEQTDTSDGESVTHHI
RRLNQQPSQGLGPRGYDPNRYRLHFERDSREEVERRKRAAREQVLQPVSAELLELDIREV
YQPGSVLDFPRRPPWSYEMSKEQLMSQEERSFQDYLGKIHGAYSSEKLSYFEHNLETWRQ
LWRVLEMSDIVLLITDIRHPVVNFPPALYEYVTGELGLALVLVLNKVDLAPPALVVAWKH
YFHQHYPQLHVVLFTSFPRDPRTPQDPSSVLKKSRRRGRGWTRALGPEQLLRACEAITVG
KVDLSSWREKIARDVAGATWGNGSGEEEEEEDGPAVLVEQQTDSAMEPTGPTQERYKDGV
VTIGCVGFPNVGKSSLINGLVGRKVVSVSRTPGHTRYFQTYFLTPSVKLCDCPGLIFPSL
LPRQLQVLAGIYPIAQIQEPYTAVGYLASRIPVQALLHLRHPEAEDPSAEHPWCAWDICE
AWAEKRGYKTAKAARNDVYRAANSLLRLAVDGRLSLCFHPPGYSEQKGTWESHPETTELV
VLQGRVGPAGDEEEEEEEELSSSCEEEGEEDRDADEEGEGDEETPTSAPGSSLAGRNPYA
LLGEDEC
Enzyme 112 Number of Residues 607
Enzyme 112 Molecular Weight 68660.3
Enzyme 112 Theoretical pI 5.58
Enzyme 112 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
Component
  • cell part
  • intracellular
Enzyme 112 General Function Involved in GTP binding
Enzyme 112 Specific Function Possible regulatory or functional link with the histocompatibility cluster
Enzyme 112 Pathways Not Available
Enzyme 112 Reactions Not Available
Enzyme 112 Pfam Domain Function
Enzyme 112 Signals
  • None
Enzyme 112 Transmembrane Regions
  • None
Enzyme 112 Essentiality Not Available
Enzyme 112 GenBank ID Protein 55961299 Link Image
Enzyme 112 UniProtKB/Swiss-Prot ID P36915 Link Image
Enzyme 112 UniProtKB/Swiss-Prot Entry Name GNL1_HUMAN Link Image
Enzyme 112 PDB ID Not Available
Enzyme 112 Cellular Location Not Available
Enzyme 112 Gene Sequence >1824 bp
ATGCCGAGGAAGAAGCCATTCAGCGTGAAGCAGAAGAAGAAGCAGTTGCAGGACAAACGG
GAGCGGAAGAGAGGGCTTCAAGATGGGCTGCGCTCCAGTTCCAACAGCCGCAGCGGGAGC
CGGGAGCGGCGAGAGGAACAGACCGACACCTCGGACGGGGAGTCTGTGACCCATCATATC
CGCAGGCTTAACCAGCAGCCTTCTCAGGGGCTGGGTCCACGAGGCTACGACCCAAATCGA
TACCGACTGCATTTTGAGAGAGACAGCAGGGAGGAGGTAGAGAGGAGAAAGAGAGCAGCC
CGGGAGCAAGTTCTACAGCCGGTCAGTGCTGAGTTGTTGGAGCTGGACATCCGGGAGGTG
TATCAGCCTGGCTCAGTTCTGGACTTTCCTCGACGTCCTCCTTGGAGCTATGAGATGTCC
AAGGAGCAACTAATGAGCCAAGAGGAACGGAGCTTCCAAGACTATCTTGGGAAGATTCAT
GGGGCTTACTCCTCTGAGAAACTCAGCTACTTTGAGCACAATCTGGAGACATGGAGGCAG
CTGTGGCGGGTGTTAGAGATGTCTGACATCGTCCTGCTTATCACTGATATCCGACATCCA
GTTGTGAATTTCCCGCCAGCACTTTATGAGTATGTGACTGGAGAACTTGGACTGGCCCTG
GTGCTGGTTTTGAACAAGGTGGATCTGGCCCCGCCAGCTCTTGTGGTTGCCTGGAAGCAT
TATTTCCATCAACACTATCCCCAGCTCCACGTCGTCCTTTTCACCTCTTTTCCTCGGGAC
CCCCGCACCCCACAGGACCCTAGTAGTGTCTTGAAGAAGAGTCGGAGGCGGGGGAGAGGA
TGGACTCGGGCCCTGGGGCCAGAGCAGTTGCTGAGAGCCTGTGAAGCCATCACTGTGGGG
AAAGTGGACTTGAGCAGCTGGCGGGAGAAGATTGCTCGGGATGTGGCTGGGGCCACCTGG
GGTAATGGCTCTGGGGAGGAGGAGGAAGAGGAGGATGGCCCAGCAGTCCTGGTGGAGCAG
CAGACTGATTCAGCAATGGAGCCAACTGGCCCAACCCAAGAGCGCTACAAGGATGGGGTG
GTGACCATCGGCTGTGTGGGTTTCCCTAATGTGGGAAAGTCCTCGCTGATCAATGGGCTG
GTGGGGCGGAAAGTCGTGAGTGTCTCCAGAACCCCGGGCCATACCCGATACTTTCAGACC
TACTTTCTTACCCCCTCTGTGAAGCTCTGTGACTGCCCAGGCCTCATCTTCCCATCTCTT
CTGCCTAGGCAGTTGCAGGTTCTGGCAGGGATCTACCCTATCGCCCAGATCCAGGAGCCC
TACACTGCTGTGGGCTACCTGGCCTCCCGAATTCCCGTGCAGGCCCTGCTCCACCTGCGC
CACCCAGAGGCTGAGGACCCCTCAGCGGAACACCCCTGGTGTGCCTGGGACATCTGTGAA
GCCTGGGCAGAGAAACGTGGTTACAAGACAGCCAAGGCGGCTCGGAATGATGTGTACAGA
GCAGCCAACAGTCTCTTGCGGCTGGCAGTGGACGGCCGCCTCAGCCTGTGTTTTCATCCC
CCAGGCTACAGTGAACAGAAAGGCACCTGGGAGTCCCATCCAGAGACCACGGAGCTGGTG
GTTTTGCAGGGCAGGGTGGGGCCAGCAGGTGACGAGGAGGAGGAGGAAGAGGAAGAGCTG
AGCAGCTCCTGTGAGGAGGAGGGAGAGGAGGACCGGGATGCGGATGAGGAGGGAGAAGGG
GATGAGGAGACCCCAACCTCGGCTCCAGGGTCCAGCCTGGCTGGCCGAAACCCTTATGCC
CTGCTGGGTGAGGATGAGTGCTGA
Enzyme 112 GenBank Gene ID AL662800 Link Image
Enzyme 112 GeneCard ID GNL1 Link Image
Enzyme 112 GenAtlas ID GNL1 Link Image
Enzyme 112 HGNC ID HGNC:4413 Link Image
Enzyme 112 Chromosome Location 6
Enzyme 112 Locus 6p21.3
Enzyme 112 SNPs SNPJam Report Link Image
Enzyme 112 General References
  1. Vernet C, Ribouchon MT, Chimini G, Pontarotti P: Structure and evolution of a member of a new subfamily of GTP-binding proteins mapping to the human MHC class I region. Mamm Genome. 1994 Feb;5(2):100-5. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  5. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  7. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 112 Metabolite References Not Available
Enzyme 113 [top]
Enzyme 113 ID 14159
Enzyme 113 Name Probable E3 ubiquitin-protein ligase HERC1
Enzyme 113 Synonyms
  1. HECT domain and RCC1-like domain-containing protein 1
  2. p532
  3. p619
Enzyme 113 Gene Name HERC1
Enzyme 113 Protein Sequence >Probable E3 ubiquitin-protein ligase HERC1
MATMIPPVKLKWLEHLNSSWITEDSESIATREGVAVLYSKLVSNKEVVPLPQQVLCLKGP
QLPDFERESLSSDEQDHYLDALLSSQLALAKMVCSDSPFAGALRKRLLVLQRVFYALSNK
YHDKGKVKQQQHSPESSSGSADVHSVSERPRSSTDALIEMGVRTGLSLLFALLRQSWMMP
VSGPGLSLCNDVIHTAIEVVSSLPPLSLANESKIPPMGLDCLSQVTTFLKGVTIPNSGAD
TLGRRLASELLLGLAAQRGSLRYLLEWIEMALGASAVVHTMEKGKLLSSQEGMISFDCFM
TILMQMRRSLGSSADRSQWREPTRTSDGLCSLYEAALCLFEEVCRMASDYSRTCASPDSI
QTGDAPIVSETCEVYVWGSNSSHQLVEGTQEKILQPKLAPSFSDAQTIEAGQYCTFVIST
DGSVRACGKGSYGRLGLGDSNNQSTLKKLTFEPHRSIKKVSSSKGSDGHTLAFTTEGEVF
SWGDGDYGKLGHGNSSTQKYPKLIQGPLQGKVVVCVSAGYRHSAAVTEDGELYTWGEGDF
GRLGHGDSNSRNIPTLVKDISNVGEVSCGSSHTIALSKDGRTVWSFGGGDNGKLGHGDTN
RVYKPKVIEALQGMFIRKVCAGSQSSLALTSTGQVYAWGCGACLGCGSSEATALRPKLIE
ELAATRIVDVSIGDSHCLALSHDNEVYAWGNNSMGQCGQGNSTGPITKPKKVSGLDGIAI
QQISAGTSHSLAWTALPRDRQVVAWHRPYCVDLEESTFSHLRSFLERYCDKINSEIPPLP
FPSSREHHSFLKLCLKLLSNHLALALAGGVATSILGRQAGPLRNLLFRLMDSTVPDEIQE
VVIETLSVGATMLLPPLRERMELLHSLLPQGPDRWESLSKGQRMQLDIILTSLQDHTHVA
SLLGYSSPSDAADLSSVCTGYGNLSDQPYGTQSCHPDTHLAEILMKTLLRNLGFYTDQAF
GELEKNSDKFLLGTSSSENSQPAHLHELLCSLQKQLLAFCHINNISENSSSVALLHKHLQ
LLLPHATDIYSRSANLLKESPWNGSVGEKLRDVIYVSAAGSMLCQIVNSLLLLPVSVARP
LLSYLLDLLPPLDCLNRLLPAADLLEDQELQWPLHGGPELIDPAGLPLPQPAQSWVWLVD
LERTIALLIGRCLGGMLQGSPVSPEEQDTAYWMKTPLFSDGVEMDTPQLDKCMSCLLEVA
LSGNEEQKPFDYKLRPEIAVYVDLALGCSKEPARSLWISMQDYAVSKDWDSATLSNESLL
DTVSRFVLAALLKHTNLLSQACGESRYQPGKHLSEVYRCVYKVRSRLLACKNLELIQTRS
SSRDRWISENQDSADVDPQEHSFTRTIDEEAEMEEQAERDREEGHPEPEDEEEEREHEVM
TAGKIFQCFLSAREVARSRDRDRMNSGAGSGARADDPPPQSQQERRVSTDLPEGQDVYTA
ACNSVIHRCALLILGVSPVIDELQKRREEGQLQQPSTSASEGGGLMTRSESLTAESRLVH
TSPNYRLIKSRSESDLSQPESDEEGYALSGRRNVDLDLAASHRKRGPMHSQLESLSDSWA
RLKHSRDWLCNSSYSFESDFDLTKSLGVHTLIENVVSFVSGDVGNAPGFKEPEESMSTSP
QASIIAMEQQQLRAELRLEALHQILVLLSGMEEKGSISLAGSRLSSGFQSSTLLTSVRLQ
FLAGCFGLGTVGHTGGKGESGRLHHYQDGIRAAKRNIQIEIQVAVHKIYQQLSATLERAL
QANKHHIEAQQRLLLVTVFALSVHYQPVDVSLAISTGLLNVLSQLCGTDTMLGQPLQLLP
KTGVSQLSTALKVASTRLLQILAITTGTYADKLSPKVVQSLLDLLCSQLKNLLSQTGVLH
MASFGEGEQEDGEEEEKKVDSSGETEKKDFRAALRKQHAAELHLGDFLVFLRRVVSSKAI
QSKMASPKWTEVLLNIASQKCSSGIPLVGNLRTRLLALHVLEAVLPACESGVEDDQMAQI
VERLFSLLSDCMWETPIAQAKHAIQIKEKEQEIKLQKQGELEEEDENLPIQEVSFDPEKA
QCCLVENGQILTHGSGGKGYGLASTGVTSGCYQWKFYIVKENRGNEGTCVGVSRWPVHDF
NHRTTSDMWLYRAYSGNLYHNGEQTLTLSSFTQGDFITCVLDMEARTISFGKNGEEPKLA
FEDVDAAELYPCVMFYSSNPGEKVKICDMQMRGTPRDLLPGDPICSPVAAVLAEATIQLI
RILHRTDRWTYCINKKMMERLHKIKICIKESGQKLKKSRSVQSREENEMREEKESKEEEK
GKHTRHGLADLSELQLRTLCIEVWPVLAVIGGVDAGLRVGGRCVHKQTGRHATLLGVVKE
GSTSAKVQWDEAEITISFPTFWSPSDTPLYNLEPCEPLPFDVARFRGLTASVLLDLTYLT
GVHEDMGKQSTKRHEKKHRHESEEKGDVEQKPESESALDMRTGLTSDDVKSQSTTSSKSE
NEIASFSLDPTLPSVESQHQITEGKRKNHEHMSKNHDVAQSEIRAVQLSYLYLGAMKSLS
ALLGCSKYAELLLIPKVLAENGHNSDCASSPVVHEDVEMRAALQFLMRHMVKRAVMRSPI
KRALGLADLERAQAMIYKLVVHGLLEDQFGGKIKQEIDQQAEESDPAQQAQTPVTTSPSA
SSTTSFMSSSLEDTTTATTPVTDTETVPASESPGVMPLSLLRQMFSSYPTTTVLPTRRAQ
TPPISSLPTSPSDEVGRRQSLTSPDSQSARPANRTALSDPSSRLSTSPPPPAIAVPLLEM
GFSLRQIAKAMEATGARGEADAQNITVLAMWMIEHPGHEDEEEPQSGSTADSRPGAAVLG
SGGKSNDPCYLQSPGDIPSADAAEMEEGFSESPDNLDHTENAASGSGPSARGRSAVTRRH
KFDLAARTLLARAAGLYRSVQAHRNQSRREGISLQQDPGALYDFNLDEELEIDLDDEAME
AMFGQDLTSDNDILGMWIPEVLDWPTWHVCESEDREEVVVCELCECSVVSFNQHMKRNHP
GCGRSANRQGYRSNGSYVDGWFGGECGSGNPYYLLCGTCREKYLAMKTKSKSTSSERYKG
QAPDLIGKQDSVYEEDWDMLDVDEDEKLTGEEEFELLAGPLGLNDRRIVPEPVQFPDSDP
LGASVAMVTATNSMEETLMQIGCHGSVEKSSSGRITLGEQAAALANPHDRVVALRRVTAA
AQVLLARTMVMRALSLLSVSGSSCSLAAGLESLGLTDIRTLVRLMCLAAAGRAGLSTSPS
AMASTSERSRGGHSKANKPISCLAYLSTAVGCLASNAPSAAKLLVQLCTQNLISAATGVN
LTTVDDSIQRKFLPSFLRGIAEENKLVTSPNFVVTQALVALLADKGAKLRPNYDKSEVEK
KGPLELANALAACCLSSRLSSQHRQWAAQQLVRTLAAHDRDNQTTLQTLADMGGDLRKCS
FIKLEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTKKQYSLQQTCVFNRLEGDAEES
LGSPSDPSFSPVSWSISGKYLAGALEKMVNIWQVNGGKGLVDIQPHWVSALAWPEEGPAT
AWSGESPELLLVGRMDGSLGLIEVVDVSTMHRRELEHCYRKDVSVTCIAWFSEDRPFAVG
YFDGKLLLGTKEPLEKGGIVLIDAHKDTLISMKWDPTGHILMTCAKEDSVKLWGSISGCW
CCLHSLCHPSIVNGIAWCRLPGKGSKLQLLMATGCQSGLVCVWRIPQDTTQTNVTSAEGW
WEQESNCQDGYRKSSGAKCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWSLRDGS
VLQTVVIGSGAIQTTVWIPEVGVAACSNRSKDVLVVNCTAEWAAANHVLATCRTALKQQG
VLGLNMAPCMRAFLERLPMMLQEQYAYEKPHVVCGDQLVHSPYMQCLASLAVGLHLDQLL
CNPPVPPHHQNCLPDPASWNPNEWAWLECFSTTIKAAEALTNGAQFPESFTVPDLEPVPE
DELVFLMDNSKWINGMDEQIMSWATSRPEDWHLGGKCDVYLWGAGRHGQLAEAGRNVMVP
AAAPSFSQAQQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISALQGFV
VTQLVTSCGSDGHSMALTESGEVFSWGDGDYGKLGHGNSDRQRRPRQIEALQGEEVVQMS
CGFKHSAVVTSDGKLFTFGNGDYGRLGLGNTSNKKLPERVTALEGYQIGQVACGLNHTLA
VSADGSMVWAFGDGDYGKLGLGNSTAKSSPQKIDVLCGIGIKKVACGTQFSVALTKDGHV
YTFGQDRLIGLPEGRARNHNRPQQIPVLAGVIIEDVAVGAEHTLALASNGDVYAWGSNSE
GQLGLGHTNHVREPTLVTGLQGKNVRQISAGRCHSAAWTAPPVPPRAPGVSVPLQLGLPD
TVPPQYGALREVSIHTVRARLRLLYHFSDLMYSSWRLLNLSPNNQNSTSHYNAGTWGIVQ
GQLRPLLAPRVYTLPMVRSIGKTMVQGKNYGPQITVKRISTRGRKCKPIFVQIARQVVKL
NASDLRLPSRAWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPNATAEVGYN
RDRFLFNPSACLDEHLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEE
VDLLYVQTLNSILHIEDSGITEESFHEMIPLDSFVGQSADGKMVPIIPGGNSIPLTFSNR
KEYVERAIEYRLHEMDRQVAAVREGMSWIVPVPLLSLLTAKQLEQMVCGMPEISVEVLKK
VVRYREVDEQHQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPANTADISQRFQIMKVDR
PYDSLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNCRSIDMDNYMLSRNVDNAEGSDTD
Y
Enzyme 113 Number of Residues 4861
Enzyme 113 Molecular Weight 532223.1
Enzyme 113 Theoretical pI 5.93
Enzyme 113 GO Classification
Function
  • acid-amino acid ligase activity
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein modification process
Component
  • cell part
  • intracellular
Enzyme 113 General Function Involved in acid-amino acid ligase activity
Enzyme 113 Specific Function Involved in membrane trafficking via some guanine nucleotide exchange factor (GEF) activity and its ability to bind clathrin. Acts as a GEF for Arf and Rab, by exchanging bound GDP for free GTP. Binds phosphatidylinositol-4,5-bisphosphate, which is required for GEF activity. May also act as a E3 ubiquitin- protein ligase which accepts ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates
Enzyme 113 Pathways Not Available
Enzyme 113 Reactions Not Available
Enzyme 113 Pfam Domain Function
Enzyme 113 Signals
  • None
Enzyme 113 Transmembrane Regions
  • None
Enzyme 113 Essentiality Not Available
Enzyme 113 GenBank ID Protein 126131099 Link Image
Enzyme 113 UniProtKB/Swiss-Prot ID Q15751 Link Image
Enzyme 113 UniProtKB/Swiss-Prot Entry Name HERC1_HUMAN Link Image
Enzyme 113 PDB ID Not Available
Enzyme 113 Cellular Location Not Available
Enzyme 113 Gene Sequence >14586 bp
ATGGCAACTATGATTCCACCAGTGAAGCTGAAATGGCTTGAACACTTGAACAGCTCCTGG
ATTACAGAGGACAGTGAATCTATTGCTACAAGAGAGGGAGTTGCTGTTCTGTATTCTAAA
CTGGTTAGCAATAAGGAAGTAGTACCTTTGCCCCAACAAGTTTTATGCCTCAAAGGACCA
CAGTTGCCAGACTTTGAACGTGAGTCTCTTTCAAGTGATGAGCAGGACCACTATTTGGAT
GCCCTTCTTAGCAGCCAGCTAGCATTGGCAAAGATGGTATGTTCAGATTCCCCATTTGCC
GGGGCACTTAGAAAACGACTGCTTGTACTCCAGCGTGTCTTTTATGCACTTTCTAATAAA
TACCATGACAAAGGCAAGGTGAAGCAGCAGCAGCATTCTCCGGAGAGCAGTTCTGGTTCA
GCAGATGTCCATTCTGTTAGTGAACGCCCCCGGTCAAGCACTGATGCACTTATAGAAATG
GGTGTTCGAACTGGTCTAAGTTTATTATTTGCGCTTCTAAGACAAAGTTGGATGATGCCT
GTGTCAGGACCTGGTCTCAGTCTTTGCAACGATGTCATTCATACTGCAATTGAAGTTGTG
AGCTCTTTGCCACCATTATCATTAGCAAATGAAAGCAAGATTCCTCCTATGGGCTTGGAC
TGCTTATCGCAAGTAACAACATTTCTTAAAGGAGTCACTATTCCTAATTCTGGGGCAGAC
ACTTTAGGTCGTAGATTAGCTTCTGAGTTGCTGCTTGGTTTGGCAGCTCAACGAGGCTCA
TTGCGATATCTTCTTGAATGGATAGAAATGGCTTTGGGGGCTTCGGCAGTTGTACACACC
ATGGAGAAAGGCAAACTACTCTCAAGCCAGGAAGGAATGATCAGCTTTGACTGCTTTATG
ACCATATTAATGCAGATGAGGCGTTCTTTGGGTTCATCTGCTGATCGGAGTCAGTGGAGA
GAACCAACCAGAACATCGGATGGCTTGTGCTCCCTTTACGAGGCAGCATTATGTCTCTTT
GAAGAGGTTTGCAGAATGGCTTCTGATTATTCGAGAACATGTGCTAGCCCAGATAGCATT
CAGACTGGTGATGCTCCCATTGTCTCCGAAACCTGTGAGGTTTATGTTTGGGGGAGCAAT
AGCAGCCATCAGTTGGTAGAAGGTACACAGGAGAAAATACTGCAACCCAAACTGGCTCCT
AGTTTCTCTGATGCACAGACCATTGAAGCTGGACAGTACTGCACTTTTGTCATTTCTACG
GATGGCTCTGTTAGAGCTTGCGGGAAAGGCAGCTATGGGAGACTGGGCCTTGGAGACTCC
AATAATCAGTCAACTTTAAAAAAGTTAACATTCGAGCCTCACAGATCCATTAAAAAGGTT
TCATCTTCTAAAGGATCTGATGGTCACACTTTAGCCTTTACGACAGAAGGAGAAGTCTTC
AGTTGGGGAGATGGTGATTATGGGAAACTGGGGCATGGAAATAGTTCAACACAGAAATAT
CCCAAGCTTATTCAGGGACCTCTACAAGGAAAGGTAGTTGTTTGTGTGTCAGCTGGATAC
AGACATAGTGCTGCTGTCACAGAGGATGGGGAATTATACACATGGGGTGAAGGAGACTTT
GGAAGATTAGGTCATGGTGACAGCAATAGTCGTAACATTCCAACATTAGTAAAAGACATC
AGCAATGTAGGAGAGGTTTCTTGTGGCAGTTCACATACTATTGCTCTGTCTAAAGATGGG
AGAACTGTATGGTCTTTTGGAGGAGGAGACAATGGTAAACTTGGTCATGGTGATACCAAC
AGAGTGTATAAACCTAAAGTTATTGAAGCTTTACAAGGAATGTTCATTCGCAAAGTTTGT
GCTGGGAGCCAGTCTTCACTTGCTTTGACATCAACAGGGCAGGTCTATGCTTGGGGCTGT
GGAGCTTGTCTAGGTTGTGGTTCTTCAGAAGCTACTGCTTTGAGACCCAAGCTTATTGAA
GAACTGGCTGCCACAAGAATAGTTGATGTTTCTATTGGAGACAGTCATTGTTTGGCTCTT
TCTCATGATAATGAAGTTTATGCCTGGGGCAATAACTCAATGGGGCAATGTGGTCAGGGA
AATTCCACAGGTCCTATTACTAAACCAAAGAAAGTGAGTGGCTTAGATGGCATAGCTATT
CAGCAGATTTCGGCTGGAACATCACATAGTCTGGCATGGACTGCTCTTCCTAGGGACAGA
CAAGTTGTTGCATGGCACCGACCTTATTGTGTAGATCTTGAAGAGAGTACCTTCTCACAC
CTGCGTTCTTTTCTTGAGAGATACTGTGATAAAATAAACAGTGAGATTCCCCCACTCCCT
TTCCCTTCATCAAGAGAACACCACAGTTTTCTCAAGCTGTGCCTGAAGCTACTTTCAAAT
CACCTTGCTCTTGCACTTGCGGGAGGGGTAGCTACCAGCATTCTCGGGAGGCAGGCAGGT
CCACTTCGAAATTTGCTCTTCAGACTGATGGACTCAACTGTCCCAGATGAAATCCAAGAG
GTGGTAATTGAAACTTTATCAGTGGGAGCAACCATGCTGTTACCTCCATTACGAGAACGG
ATGGAATTACTTCATTCTCTTTTACCTCAAGGACCTGATAGATGGGAAAGCTTATCTAAA
GGACAGAGAATGCAACTGGATATCATCCTGACAAGTTTGCAAGATCATACCCACGTAGCC
TCCCTACTTGGCTATAGTTCACCCTCTGATGCTGCTGACCTATCTTCTGTGTGTACTGGC
TACGGAAATCTGTCAGATCAACCTTACGGCACTCAGAGCTGCCATCCAGATACCCACCTG
GCTGAAATTTTGATGAAGACCCTCTTAAGAAATTTAGGATTTTATACAGATCAAGCATTT
GGAGAGCTAGAAAAGAATAGTGATAAATTTCTACTTGGAACATCATCATCAGAAAACAGT
CAGCCTGCTCATCTTCATGAACTGCTATGTTCACTACAGAAACAGCTGCTGGCATTTTGC
CATATCAATAACATTAGTGAGAACTCAAGCAGTGTGGCATTGCTTCATAAACATCTTCAG
CTTTTGTTGCCTCATGCCACAGATATTTATTCACGTTCTGCAAATTTGCTCAAAGAAAGT
CCTTGGAATGGCAGTGTTGGAGAAAAATTAAGAGATGTGATATACGTCTCAGCTGCTGGC
AGTATGCTCTGCCAGATTGTTAACTCCCTGCTGTTACTCCCTGTGTCAGTGGCTCGGCCT
TTATTGAGTTACCTCCTCGACTTGTTGCCACCTCTTGATTGCCTTAATAGACTCCTGCCA
GCTGCTGATCTTTTAGAAGACCAGGAGTTACAGTGGCCTCTTCATGGAGGGCCAGAACTA
ATTGATCCTGCTGGTCTGCCATTACCTCAGCCAGCTCAGTCCTGGGTATGGCTTGTGGAT
CTAGAAAGAACAATTGCTCTCCTTATTGGGCGGTGTCTTGGTGGCATGCTTCAGGGCTCC
CCTGTGTCTCCAGAGGAACAGGACACTGCATATTGGATGAAAACGCCACTGTTCAGTGAC
GGTGTAGAAATGGACACTCCTCAATTGGATAAATGTATGAGTTGCCTGTTAGAAGTAGCA
CTTTCTGGAAATGAAGAACAGAAGCCTTTTGATTATAAATTGCGGCCTGAAATTGCTGTC
TATGTAGACTTGGCATTGGGTTGTTCTAAAGAGCCTGCCCGAAGCCTTTGGATCAGCATG
CAGGACTATGCTGTTAGTAAAGATTGGGACAGTGCAACTTTAAGTAATGAGTCACTCTTG
GACACTGTGTCTAGATTTGTTCTTGCAGCTCTTCTGAAACACACAAATTTACTTAGTCAA
GCATGTGGAGAAAGCCGATATCAACCTGGTAAACACTTATCAGAAGTGTACCGTTGTGTA
TACAAAGTTCGAAGTCGTTTACTTGCTTGCAAGAACCTTGAACTTATTCAAACAAGGTCA
TCATCACGGGACAGATGGATATCAGAAAACCAGGACTCTGCAGATGTTGATCCTCAGGAG
CATTCATTTACTCGAACTATTGATGAAGAAGCTGAAATGGAAGAACAGGCTGAGAGAGAC
CGGGAAGAGGGGCATCCGGAGCCAGAGGATGAAGAGGAGGAACGGGAACATGAAGTGATG
ACAGCTGGCAAAATCTTTCAGTGTTTCCTCTCAGCCCGTGAAGTAGCTCGTAGCCGAGAC
CGAGATAGAATGAACAGTGGGGCAGGGTCTGGGGCTCGAGCTGATGATCCACCTCCTCAG
TCTCAGCAAGAGCGAAGGGTCAGCACAGACCTTCCTGAGGGTCAGGATGTGTACACTGCT
GCATGCAACTCCGTGATCCATCGGTGTGCCCTGTTAATATTAGGAGTAAGTCCTGTGATA
GATGAGCTTCAGAAGCGAAGAGAAGAAGGACAGTTGCAGCAACCTTCAACAAGTGCCTCT
GAAGGGGGTGGACTTATGACCAGGAGTGAAAGTCTTACTGCAGAGAGCCGGCTAGTCCAC
ACAAGCCCAAATTATAGACTGATCAAATCGAGGAGTGAATCTGATTTGTCTCAGCCTGAA
TCAGATGAAGAGGGTTACGCACTGAGTGGCAGACGAAATGTTGATTTGGATTTGGCAGCA
TCTCACAGAAAGAGAGGTCCTATGCACAGTCAATTGGAATCCCTGAGTGACTCTTGGGCT
CGCCTGAAACATAGCAGAGACTGGTTATGCAACTCCTCCTATTCCTTTGAGTCAGATTTT
GATCTTACCAAGTCTTTGGGAGTTCACACTTTGATTGAAAATGTTGTAAGCTTTGTGAGT
GGAGATGTGGGGAATGCCCCAGGTTTTAAAGAGCCAGAGGAAAGTATGTCTACAAGTCCC
CAGGCCTCCATCATTGCAATGGAACAGCAGCAGTTAAGGGCAGAACTTCGTTTAGAGGCA
CTTCATCAGATCCTCGTTCTATTGTCTGGGATGGAAGAAAAAGGTAGCATCTCACTGGCA
GGAAGCAGATTGAGTTCAGGCTTCCAGTCCTCCACACTACTCACGTCTGTGAGGCTGCAG
TTCCTAGCAGGGTGTTTTGGTTTAGGCACTGTTGGACACACAGGAGGCAAGGGAGAGAGT
GGCCGATTGCATCACTATCAGGATGGGATCAGAGCAGCTAAGAGAAATATTCAGATTGAA
ATCCAGGTAGCTGTGCATAAAATTTATCAACAGTTGTCTGCTACCCTGGAAAGAGCCCTG
CAAGCAAACAAGCATCACATTGAAGCCCAGCAACGTCTGCTTCTGGTTACAGTTTTTGCC
CTAAGTGTTCATTATCAACCAGTAGATGTTTCTTTGGCAATTTCCACTGGTCTGCTAAAC
GTATTGTCACAGTTGTGTGGTACAGACACCATGCTAGGACAGCCCCTGCAGTTGTTGCCA
AAGACGGGTGTTTCCCAGCTTAGCACAGCTTTGAAAGTGGCCAGTACAAGGTTGCTCCAG
ATTCTAGCCATCACTACTGGGACCTATGCTGATAAACTGAGTCCCAAAGTAGTTCAATCC
TTGTTGGATCTACTCTGTAGTCAGTTGAAGAATTTATTGTCCCAAACTGGTGTACTACAT
ATGGCCTCTTTCGGAGAAGGGGAGCAAGAAGACGGTGAAGAAGAAGAAAAAAAAGTTGAC
TCCAGTGGAGAAACTGAGAAGAAAGATTTCAGAGCTGCTCTTAGGAAACAACATGCAGCC
GAACTCCATCTAGGGGATTTTTTAGTTTTTCTTCGCAGAGTTGTATCTTCAAAAGCAATT
CAATCAAAAATGGCTTCCCCAAAGTGGACCGAAGTGCTTCTAAATATAGCATCTCAGAAA
TGTTCTTCAGGTATCCCTCTGGTTGGTAACTTAAGAACAAGGCTCCTTGCACTTCATGTC
CTTGAAGCTGTGCTGCCAGCTTGTGAATCTGGTGTAGAAGATGATCAAATGGCCCAGATT
GTTGAGCGCTTATTTTCCCTTCTCTCTGATTGTATGTGGGAGACACCCATTGCTCAGGCC
AAACATGCTATTCAGATAAAGGAAAAAGAACAAGAAATAAAACTACAGAAGCAGGGCGAG
TTGGAAGAAGAAGATGAGAATCTTCCTATCCAAGAAGTATCCTTTGACCCGGAGAAAGCT
CAGTGTTGCCTAGTGGAGAATGGACAGATTTTAACTCACGGCAGTGGAGGGAAAGGATAT
GGATTGGCATCTACAGGAGTAACTTCTGGGTGCTATCAGTGGAAGTTTTATATTGTGAAG
GAAAACAGAGGTAATGAAGGCACGTGTGTTGGAGTTTCTCGCTGGCCAGTACATGACTTT
AATCACCGCACTACCTCGGATATGTGGCTCTATAGGGCCTACAGTGGTAACCTCTATCAC
AATGGAGAACAGACTCTCACATTGTCCAGCTTTACTCAAGGAGATTTCATTACCTGTGTG
TTAGACATGGAAGCCAGGACCATTTCTTTTGGGAAAAATGGAGAGGAACCCAAATTAGCT
TTTGAAGATGTGGATGCAGCAGAGTTGTACCCATGTGTGATGTTCTATAGTAGCAATCCA
GGGGAAAAGGTGAAAATTTGTGATATGCAGATGCGTGGCACACCCCGAGACTTACTTCCA
GGAGACCCTATTTGTAGTCCAGTAGCAGCAGTGCTGGCTGAGGCCACTATTCAGCTCATC
CGTATCCTTCACCGAACAGACCGTTGGACTTACTGCATTAACAAAAAAATGATGGAAAGG
CTTCACAAAATTAAGATATGTATTAAAGAGTCAGGTCAGAAGCTAAAGAAAAGCCGCTCG
GTTCAGAGCCGAGAGGAAAATGAAATGAGAGAGGAGAAGGAGAGCAAAGAGGAAGAGAAA
GGTAAACATACTAGGCATGGCCTCGCTGACCTCTCAGAGCTGCAGCTGAGGACTCTTTGC
ATAGAGGTGTGGCCCGTGCTGGCTGTGATAGGAGGAGTTGATGCTGGTCTTAGAGTTGGA
GGTCGGTGTGTTCACAAGCAAACTGGGCGCCATGCCACGCTGCTGGGAGTGGTCAAAGAG
GGCAGCACGTCTGCCAAGGTCCAATGGGATGAAGCAGAAATTACTATCAGCTTCCCAACT
TTTTGGTCGCCTAGTGATACTCCATTGTATAATCTGGAACCCTGTGAACCATTGCCGTTT
GATGTGGCGCGATTCCGAGGCCTGACGGCTTCTGTGCTGCTGGACCTAACATATCTCACT
GGCGTTCATGAAGACATGGGCAAACAGAGCACCAAACGACATGAAAAGAAACACCGACAT
GAATCCGAGGAGAAAGGGGATGTTGAGCAGAAACCTGAGAGTGAATCCGCTTTAGATATG
CGAACAGGCCTAACATCTGATGACGTCAAAAGTCAGAGTACCACAAGCTCCAAATCAGAA
AATGAAATCGCTTCATTTTCTTTAGATCCAACACTGCCAAGTGTGGAATCCCAACATCAA
ATAACAGAAGGGAAAAGAAAAAATCATGAACACATGTCCAAAAACCATGATGTAGCCCAG
TCAGAAATCAGAGCAGTCCAGCTGTCCTATCTTTACCTCGGTGCTATGAAGTCACTTAGT
GCCCTTCTTGGCTGTAGTAAATATGCTGAGCTGTTGCTGATACCAAAAGTTCTGGCTGAA
AATGGCCACAACTCAGACTGTGCAAGTTCTCCAGTTGTTCATGAAGACGTGGAGATGCGA
GCAGCCCTGCAGTTCTTGATGCGACACATGGTGAAGCGAGCAGTCATGCGGTCACCCATA
AAGAGAGCATTGGGATTAGCTGATCTGGAACGAGCGCAAGCCATGATCTATAAATTAGTG
GTTCATGGGCTTTTGGAAGACCAGTTTGGGGGCAAAATTAAGCAAGAGATTGATCAACAA
GCTGAAGAAAGTGACCCTGCCCAGCAGGCACAGACACCAGTTACTACTAGCCCATCAGCC
TCAAGCACGACCTCCTTTATGAGCAGCTCTCTGGAGGACACCACAACTGCCACCACTCCA
GTCACTGACACAGAAACAGTGCCTGCATCCGAGTCCCCGGGAGTGATGCCTCTTAGTCTT
CTCAGGCAAATGTTCTCTAGTTACCCAACTACCACTGTACTTCCCACACGTCGGGCACAG
ACTCCTCCAATATCTTCGTTACCAACCTCTCCTTCTGATGAAGTAGGAAGGAGGCAAAGT
TTAACTTCTCCTGATTCCCAGTCAGCAAGGCCAGCTAACCGCACAGCCTTGTCAGACCCA
AGCAGTAGACTTTCAACTTCTCCTCCTCCTCCAGCAATTGCAGTTCCCTTGCTGGAAATG
GGGTTCTCTCTTCGGCAGATTGCCAAAGCCATGGAAGCTACAGGTGCTAGGGGAGAGGCT
GATGCCCAGAATATCACTGTCCTTGCCATGTGGATGATAGAGCACCCTGGGCATGAGGAT
GAAGAGGAGCCCCAGTCGGGCAGCACAGCAGACTCTAGGCCTGGAGCAGCCGTTCTAGGC
AGTGGCGGGAAGTCAAATGATCCCTGTTATTTGCAGTCACCTGGAGACATACCATCAGCT
GATGCTGCTGAAATGGAGGAAGGTTTTAGTGAAAGCCCTGATAATTTGGATCATACAGAG
AATGCAGCTTCTGGAAGTGGACCATCAGCTAGAGGTCGCTCAGCGGTAACAAGAAGACAC
AAGTTTGACTTAGCTGCTCGCACACTGCTAGCAAGAGCAGCGGGATTATACCGCTCTGTG
CAGGCCCACAGGAATCAAAGTCGGAGAGAAGGAATATCTTTGCAGCAAGACCCAGGGGCG
TTGTATGACTTTAATTTAGATGAGGAATTGGAAATTGATCTTGATGATGAGGCGATGGAA
GCTATGTTTGGACAAGACCTGACCAGTGACAATGATATTCTGGGAATGTGGATCCCAGAG
GTACTGGATTGGCCTACCTGGCATGTTTGTGAGTCTGAAGACAGGGAAGAAGTGGTGGTG
TGTGAACTGTGTGAATGCAGCGTCGTCAGCTTCAATCAGCACATGAAGAGAAACCATCCA
GGCTGTGGGCGCAGTGCAAACCGCCAGGGCTATCGCAGCAATGGTTCCTATGTGGATGGC
TGGTTTGGCGGTGAATGTGGGAGTGGAAATCCGTACTACCTGTTATGTGGCACCTGCAGG
GAGAAGTACTTAGCCATGAAGACCAAATCTAAGTCAACAAGTTCTGAAAGGTACAAGGGA
CAAGCTCCAGATCTAATTGGCAAGCAAGACAGTGTGTATGAAGAAGACTGGGACATGTTG
GATGTTGATGAAGATGAAAAGCTAACTGGTGAAGAAGAATTTGAATTACTTGCTGGACCG
CTTGGTTTAAATGACCGGCGCATTGTACCAGAACCAGTTCAGTTCCCTGACAGCGATCCA
CTGGGAGCATCAGTAGCAATGGTCACAGCCACCAACAGTATGGAAGAGACTCTGATGCAA
ATAGGTTGCCATGGCTCCGTAGAAAAGAGCTCCTCTGGGAGAATAACGTTAGGAGAGCAG
GCAGCTGCCCTAGCAAACCCTCATGACCGTGTGGTGGCTTTAAGGAGAGTGACTGCTGCT
GCTCAGGTTCTTCTGGCCAGAACCATGGTCATGAGAGCGCTGTCTCTTCTCTCAGTCAGT
GGTTCCAGTTGTAGCCTGGCTGCTGGTCTTGAGTCTCTGGGGCTAACAGATATCCGAACG
CTAGTTCGATTAATGTGCTTGGCAGCAGCAGGGAGAGCTGGCCTCTCCACCAGCCCTTCT
GCCATGGCTAGCACCTCAGAACGATCACGAGGTGGGCATAGCAAGGCTAACAAGCCTATC
TCTTGCCTGGCCTATTTGAGCACAGCAGTGGGATGTCTGGCATCAAATGCTCCTAGTGCT
GCCAAACTGCTTGTACAGTTGTGTACACAGAACTTGATTTCTGCTGCAACAGGTGTAAAT
CTAACCACAGTTGATGACTCAATTCAGCGAAAGTTTCTACCCAGCTTTCTCCGAGGAATT
GCTGAAGAGAACAAGCTTGTGACCTCCCCAAACTTTGTTGTAACACAGGCCCTTGTGGCA
TTGCTAGCAGACAAAGGGGCCAAACTAAGACCTAACTATGATAAGTCAGAAGTTGAAAAG
AAAGGCCCTCTGGAGTTGGCTAATGCCCTGGCAGCCTGCTGCCTCTCCTCCAGGCTGTCC
TCACAGCATCGGCAATGGGCAGCTCAGCAACTCGTGCGCACTCTTGCTGCACACGACCGT
GACAACCAAACTACTCTGCAGACACTTGCTGATATGGGAGGAGATCTTAGAAAATGCTCC
TTTATCAAATTGGAGGCTCATCAGAACAGAGTAATGACATGTGTTTGGTGTAATAAAAAA
GGTCTTTTGGCTACAAGTGGCAATGATGGCACCATCCGCGTATGGAATGTTACCAAGAAG
CAATATTCACTGCAACAGACCTGTGTGTTCAACAGATTGGAAGGGGATGCTGAGGAAAGC
CTGGGATCACCCAGTGATCCAAGTTTCTCACCAGTTTCCTGGAGTATCAGTGGCAAATAT
CTAGCAGGCGCTTTGGAAAAGATGGTGAATATCTGGCAAGTTAATGGAGGAAAAGGATTA
GTAGATATTCAGCCTCATTGGGTATCTGCCCTGGCTTGGCCAGAAGAGGGTCCGGCTACA
GCCTGGTCAGGAGAGTCTCCAGAATTGTTGTTGGTGGGACGGATGGATGGATCTCTGGGA
CTGATTGAAGTTGTTGATGTGTCCACCATGCACCGTCGAGAATTGGAGCATTGCTATCGA
AAGGATGTGTCTGTTACTTGCATTGCATGGTTCAGTGAAGACAGACCATTTGCAGTGGGA
TATTTTGATGGAAAACTGTTACTGGGAACAAAGGAACCACTTGAGAAAGGAGGCATTGTT
CTAATTGATGCACATAAGGATACTCTTATTAGCATGAAGTGGGACCCTACAGGTCATATT
CTTATGACATGTGCCAAAGAAGACAGTGTGAAACTCTGGGGCTCTATTTCGGGATGCTGG
TGCTGTCTACATTCACTCTGCCATCCATCTATTGTAAATGGCATTGCTTGGTGCCGCCTT
CCAGGGAAAGGATCCAAGTTGCAGTTACTGATGGCTACTGGCTGTCAGAGTGGCTTAGTA
TGTGTTTGGCGCATTCCTCAAGATACTACACAGACCAATGTGACTAGTGCAGAAGGATGG
TGGGAGCAGGAATCAAATTGCCAGGATGGATATAGGAAATCATCAGGAGCCAAGTGTGTT
TATCAGCTGCGGGGACACATCACTCCTGTTCGGACTGTTGCCTTTAGTTCTGATGGGTTG
GCCCTGGTGTCTGGTGGACTAGGTGGGCTCATGAACATTTGGTCTTTAAGGGATGGCTCT
GTCTTGCAAACTGTTGTGATAGGCTCTGGAGCTATTCAGACCACAGTATGGATTCCAGAA
GTTGGAGTAGCTGCTTGCTCAAATAGATCAAAGGATGTTTTGGTCGTGAATTGTACAGCA
GAATGGGCAGCTGCCAATCATGTTTTGGCAACCTGTAGGACAGCATTGAAACAGCAGGGT
GTTCTGGGATTGAACATGGCTCCCTGCATGAGAGCATTTTTGGAGCGGCTCCCCATGATG
CTTCAGGAGCAGTATGCCTATGAAAAGCCTCATGTGGTTTGTGGTGACCAACTTGTTCAT
AGCCCCTATATGCAATGCTTGGCTTCCCTTGCTGTGGGACTTCATCTGGATCAGCTGTTG
TGTAACCCTCCAGTGCCACCACACCACCAGAACTGTCTCCCTGACCCTGCATCCTGGAAT
CCAAATGAATGGGCCTGGTTAGAATGTTTCTCAACCACTATAAAAGCTGCCGAAGCCCTG
ACCAATGGAGCCCAGTTTCCAGAATCTTTTACCGTTCCAGATCTAGAACCTGTTCCAGAG
GATGAACTTGTATTTCTAATGGATAACAGTAAATGGATTAACGGCATGGATGAACAAATT
ATGTCTTGGGCAACTTCCAGACCTGAGGACTGGCACCTGGGAGGTAAATGTGATGTCTAC
TTATGGGGTGCTGGTAGGCATGGACAGCTGGCAGAAGCTGGAAGAAATGTAATGGTACCT
GCAGCAGCTCCCTCATTCTCACAGGCCCAACAGGTCATTTGTGGTCAGAATTGTACCTTT
GTCATCCAGGCCAATGGCACAGTGTTGGCTTGTGGGGAAGGAAGTTATGGCAGATTAGGA
CAAGGAAATTCAGATGACCTTCATGTGCTGACAGTTATTTCAGCCTTACAAGGCTTTGTG
GTGACCCAGCTGGTGACTTCCTGTGGTTCTGATGGGCACTCTATGGCCCTAACTGAAAGT
GGTGAGGTCTTTAGCTGGGGAGATGGTGACTATGGTAAACTTGGCCATGGGAACAGCGAC
AGGCAGCGGCGGCCCAGGCAGATCGAGGCCTTACAAGGAGAAGAAGTGGTGCAGATGTCT
TGTGGCTTCAAGCACTCAGCAGTGGTCACTTCAGATGGCAAACTGTTCACCTTTGGGAAT
GGTGACTATGGTCGTCTGGGTCTTGGAAATACCTCTAACAAAAAACTTCCAGAGAGAGTG
ACTGCACTGGAGGGATATCAGATTGGACAGGTGGCCTGTGGATTAAACCACACTTTGGCA
GTGTCAGCAGATGGTTCCATGGTGTGGGCTTTTGGAGATGGAGACTATGGAAAACTAGGC
TTAGGAAATTCCACTGCAAAATCTTCACCTCAGAAAATTGACGTCCTTTGTGGAATTGGA
ATAAAAAAGGTTGCTTGTGGAACTCAGTTTTCTGTTGCTTTGACCAAAGATGGTCATGTG
TATACCTTTGGTCAAGATCGCCTGATAGGCTTGCCAGAGGGGCGTGCTCGCAATCACAAT
CGACCGCAACAAATCCCTGTCCTGGCTGGAGTAATCATAGAAGATGTGGCAGTTGGAGCT
GAACACACACTTGCTTTGGCATCAAATGGAGATGTGTATGCCTGGGGGAGCAATTCAGAA
GGGCAGCTCGGCTTAGGCCATACCAACCATGTTCGAGAACCAACCCTGGTAACAGGTCTG
CAAGGGAAAAATGTTCGGCAGATCTCGGCTGGCCGCTGCCACAGTGCTGCATGGACAGCA
CCACCTGTCCCACCAAGAGCACCAGGTGTGTCAGTACCTCTGCAGCTGGGCCTGCCTGAC
ACAGTGCCCCCCCAGTATGGGGCGCTGAGAGAAGTCAGCATTCACACGGTGCGGGCCAGG
CTCCGGCTGCTCTACCACTTCTCTGACCTCATGTACTCATCCTGGAGACTGCTGAACCTT
AGCCCCAACAACCAGAACAGCACATCCCATTATAATGCTGGAACTTGGGGCATTGTACAG
GGACAACTTCGGCCTTTGTTAGCCCCAAGAGTCTACACTCTGCCAATGGTGCGCTCCATA
GGAAAAACCATGGTTCAAGGCAAAAACTATGGACCTCAGATAACTGTAAAGAGGATATCA
ACCAGAGGACGGAAGTGTAAGCCTATTTTTGTCCAAATAGCGAGACAAGTAGTTAAGCTG
AATGCTTCAGACCTCCGCCTGCCTTCCCGAGCGTGGAAGGTTAAGCTGGTTGGAGAAGGG
GCTGATGATGCTGGAGGAGTGTTTGATGACACCATCACAGAGATGTGCCAGGAACTTGAA
ACTGGTATTGTTGACCTTCTTATACCCTCTCCCAATGCCACCGCAGAAGTGGGTTACAAT
AGGGACAGGTTCCTTTTTAACCCTTCTGCCTGCCTCGATGAACACTTAATGCAGTTTAAG
TTTTTAGGAATTTTAATGGGGGTTGCCATTCGCACAAAGAAGCCTCTGGACCTCCACTTG
GCCCCTCTGGTGTGGAAGCAGCTGTGCTGTGTCCCACTCACCCTAGAGGACCTGGAGGAG
GTGGATCTGCTCTACGTGCAGACTCTCAACAGCATTCTTCACATTGAAGACAGTGGGATT
ACCGAGGAGAGTTTCCATGAGATGATTCCTCTTGATTCTTTTGTTGGCCAGAGTGCTGAT
GGCAAAATGGTTCCTATAATCCCTGGTGGAAATAGTATCCCACTCACATTTTCCAACAGG
AAGGAATATGTGGAGAGGGCCATTGAATATCGACTTCATGAGATGGACAGACAGGTGGCT
GCAGTCCGAGAAGGGATGTCCTGGATTGTTCCTGTGCCGCTGCTGTCCCTCCTCACAGCA
AAACAACTGGAGCAGATGGTGTGTGGGATGCCCGAGATCTCTGTGGAAGTCTTGAAGAAA
GTGGTGCGGTACCGTGAGGTGGATGAGCAGCATCAGCTGGTGCAGTGGTTCTGGCACACG
CTGGAAGAGTTCTCCAATGAGGAGCGGGTGCTTTTCATGAGGTTTGTGTCAGGAAGATCT
CGACTACCAGCCAACACTGCTGACATTTCTCAGAGATTTCAAATCATGAAGGTTGATAGG
CCTTACGACAGTCTGCCTACCTCACAGACCTGCTTCTTCCAGCTGAGGCTGCCCCCGTAC
TCCAGCCAGCTGGTCATGGCCGAGCGCCTGCGCTATGCCATCAACAACTGCCGCTCAATC
GACATGGACAACTACATGCTCTCGAGAAACGTGGACAACGCCGAGGGCTCCGACACTGAC
TACTGA
Enzyme 113 GenBank Gene ID NM_003922.3 Link Image
Enzyme 113 GeneCard ID HERC1 Link Image
Enzyme 113 GenAtlas ID HERC1 Link Image
Enzyme 113 HGNC ID HGNC:4867 Link Image
Enzyme 113 Chromosome Location 1
Enzyme 113 Locus 15q22
Enzyme 113 SNPs SNPJam Report Link Image
Enzyme 113 General References
  1. Rosa JL, Casaroli-Marano RP, Buckler AJ, Vilaro S, Barbacid M: p619, a giant protein related to the chromosome condensation regulator RCC1, stimulates guanine nucleotide exchange on ARF1 and Rab proteins. EMBO J. 1996 Aug 15;15(16):4262-73. [PubMed Link Image]
  2. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Rosa JL, Barbacid M: A giant protein that stimulates guanine nucleotide exchange on ARF1 and Rab proteins forms a cytosolic ternary complex with clathrin and Hsp70. Oncogene. 1997 Jul 3;15(1):1-6. [PubMed Link Image]
  5. Garcia-Gonzalo FR, Cruz C, Munoz P, Mazurek S, Eigenbrodt E, Ventura F, Bartrons R, Rosa JL: Interaction between HERC1 and M2-type pyruvate kinase. FEBS Lett. 2003 Mar 27;539(1-3):78-84. [PubMed Link Image]
  6. Garcia-Gonzalo FR, Munoz P, Gonzalez E, Casaroli-Marano RP, Vilaro S, Bartrons R, Ventura F, Rosa JL: The giant protein HERC1 is recruited to aluminum fluoride-induced actin-rich surface protrusions in HeLa cells. FEBS Lett. 2004 Feb 13;559(1-3):77-83. [PubMed Link Image]
  7. Garcia-Gonzalo FR, Bartrons R, Ventura F, Rosa JL: Requirement of phosphatidylinositol-4,5-bisphosphate for HERC1-mediated guanine nucleotide release from ARF proteins. FEBS Lett. 2005 Jan 17;579(2):343-8. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  9. Chong-Kopera H, Inoki K, Li Y, Zhu T, Garcia-Gonzalo FR, Rosa JL, Guan KL: TSC1 stabilizes TSC2 by inhibiting the interaction between TSC2 and the HERC1 ubiquitin ligase. J Biol Chem. 2006 Mar 31;281(13):8313-6. Epub 2006 Feb 7. [PubMed Link Image]
  10. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  11. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  12. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  13. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  14. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  15. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 113 Metabolite References Not Available
Enzyme 114 [top]
Enzyme 114 ID 14166
Enzyme 114 Name Eukaryotic translation initiation factor 5
Enzyme 114 Synonyms
  1. eIF-5
Enzyme 114 Gene Name EIF5
Enzyme 114 Protein Sequence >Eukaryotic translation initiation factor 5
MSVNVNRSVSDQFYRYKMPRLIAKVEGKGNGIKTVIVNMVDVAKALNRPPTYPTKYFGCE
LGAQTQFDVKNDRYIVNGSHEANKLQDMLDGFIKKFVLCPECENPETDLHVNPKKQTIGN
SCKACGYRGMLDTHHKLCTFILKNPPENSDSGTGKKEKEKKNRKGKDKENGSVSSSETPP
PPPPPNEINPPPHTMEEEEDDDWGEDTTEEAQRRRMDEISDHAKVLTLSDDLERTIEERV
NILFDFVKKKKEEGVIDSSDKEIVAEAERLDVKAMGPLVLTEVLFNEKIREQIKKYRRHF
LRFCHNNKKAQRYLLHGLECVVAMHQAQLISKIPHILKEMYDADLLEEEVIISWSEKASK
KYVSKELAKEIRVKAEPFIKWLKEAEEESSGGEEEDEDENIEVVYSKAASVPKVETVKSD
NKDDDIDIDAI
Enzyme 114 Number of Residues 431
Enzyme 114 Molecular Weight 49222.4
Enzyme 114 Theoretical pI 5.26
Enzyme 114 GO Classification
Function
  • RNA binding
  • binding
  • nucleic acid binding
  • translation factor activity, nucleic acid binding
  • translation initiation factor activity
Process
  • cellular process
  • translational initiation
Component
Enzyme 114 General Function Involved in binding
Enzyme 114 Specific Function Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F])
Enzyme 114 Pathways Not Available
Enzyme 114 Reactions Not Available
Enzyme 114 Pfam Domain Function
Enzyme 114 Signals
  • None
Enzyme 114 Transmembrane Regions
  • None
Enzyme 114 Essentiality Not Available
Enzyme 114 GenBank ID Protein 10439908 Link Image
Enzyme 114 UniProtKB/Swiss-Prot ID P55010 Link Image
Enzyme 114 UniProtKB/Swiss-Prot Entry Name IF5_HUMAN Link Image
Enzyme 114 PDB ID Not Available
Enzyme 114 Cellular Location Not Available
Enzyme 114 Gene Sequence >1296 bp
ATGTCTGTCAATGTCAACCGCAGCGTGTCAGACCAGTTCTATCGCTACAAGATGCCCCGT
CTGATTGCCAAGGTTGAGGGCAAAGGCAATGGAATCAAGACAGTTATAGTCAACATGGTT
GACGTTGCAAAGGCGCTTAATCGGCCTCCAACGTATCCCACCAAATATTTTGGTTGTGAG
CTGGGAGCACAGACCCAGTTTGATGTTAAGAATGACCGTTACATTGTCAATGGATCTCAT
GAGGCGAATAAGCTGCAAGACATGTTGGATGGATTCATTAAAAAATTTGTTCTCTGTCCT
GAATGTGAGAATCCTGAAACAGATTTGCATGTCAATCCAAAGAAGCAAACAATAGGTAAT
TCTTGTAAAGCCTGTGGCTATCGAGGCATGCTTGACACACATCATAAACTCTGCACATTC
ATTCTCAAAAACCCACCTGAGAATAGTGACAGTGGTACAGGAAAGAAAGAAAAAGAAAAG
AAAAACAGAAAGGGCAAAGACAAGGAAAATGGCTCCGTATCCAGCAGTGAGACACCACCA
CCACCACCACCACCAAATGAAATTAATCCTCCTCCACATACAATGGAAGAAGAGGAGGAT
GATGACTGGGGAGAAGATACAACTGAGGAAGCTCAAAGGCGTCGAATGGATGAAATCAGT
GACCATGCAAAAGTTCTGACACTCAGTGATGATTTGGAAAGAACAATTGAGGAGAGGGTC
AATATCCTCTTTGATTTTGTTAAGAAAAAGAAAGAAGAGGGTGTTATTGATTCATCTGAC
AAAGAAATCGTTGCTGAAGCAGAAAGACTGGATGTAAAAGCCATGGGCCCTCTTGTTCTA
ACTGAAGTTCTTTTTAATGAGAAGATTAGAGAACAGATTAAGAAATACAGGCGCCATTTC
CTACGATTTTGTCACAACAACAAAAAAGCCCAACGGTACCTTCTTCATGGTTTGGAGTGT
GTGGTAGCAATGCATCAAGCTCAGCTTATCTCCAAGATTCCACATATCTTGAAGGAGATG
TACGATGCAGACCTTTTAGAAGAAGAGGTCATCATCAGCTGGTCGGAAAAGGCCTCTAAG
AAATATGTCTCCAAAGAACTTGCCAAAGAGATTCGTGTCAAAGCAGAACCATTTATAAAA
TGGTTGAAGGAGGCAGAGGAAGAATCTTCTGGTGGCGAAGAAGAAGATGAAGATGAGAAC
ATTGAGGTGGTGTATTCGAAGGCTGCCAGTGTACCGAAAGTTGAGACTGTAAAGTCAGAC
AACAAGGATGACGACATCGATATTGATGCCATTTAA
Enzyme 114 GenBank Gene ID AK026933 Link Image
Enzyme 114 GeneCard ID EIF5 Link Image
Enzyme 114 GenAtlas ID EIF5 Link Image
Enzyme 114 HGNC ID HGNC:3299 Link Image
Enzyme 114 Chromosome Location 1
Enzyme 114 Locus 14q32.32
Enzyme 114 SNPs SNPJam Report Link Image
Enzyme 114 General References
  1. Si K, Das K, Maitra U: Characterization of multiple mRNAs that encode mammalian translation initiation factor 5 (eIF-5). J Biol Chem. 1996 Jul 12;271(28):16934-8. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  8. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  9. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  10. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  11. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  12. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 114 Metabolite References Not Available
Enzyme 115 [top]
Enzyme 115 ID 14182
Enzyme 115 Name IQ motif and SEC7 domain-containing protein 1
Enzyme 115 Synonyms
  1. ADP-ribosylation factors guanine nucleotide-exchange protein 100
  2. ADP-ribosylation factors guanine nucleotide-exchange protein 2
  3. Brefeldin-resistant Arf-GEF 2 protein
Enzyme 115 Gene Name IQSEC1
Enzyme 115 Protein Sequence >IQ motif and SEC7 domain-containing protein 1
MWCLHCNSERTQSLLELELDSGVEGEAPSSETGTSLDSPSAYPQGPLVPGSSLSPDHYEH
TSVGAYGLYSGPPGQQQRTRRPKLQHSTSILRKQAEEEAIKRSRSLSESYELSSDLQDKQ
VEMLERKYGGRLVTRHAARTIQTAFRQYQMNKNFERLRSSMSENRMSRRIVLSNMRMQFS
FEGPEKVHSSYFEGKQVSVTNDGSQLGALVSPECGDLSEPTTLKSPAPSSDFADAITELE
DAFSRQVKSLAESIDDALNCRSLHTEEAPALDAARARDTEPQTALHGMDHRKLDEMTASY
SDVTLYIDEEELSPPLPLSQAGDRPSSTESDLRLRAGGAAPDYWALAHKEDKADTDTSCR
STPSLERQEQRLRVEHLPLLTIEPPSDSSVDLSDRSERGSLKRQSAYERSLGGQQGSPKH
GPHSGAPKSLPREEPELRPRPPRPLDSHLAINGSANRQSKSESDYSDGDNDSINSTSNSN
DTINCSSESSSRDSLREQTLSKQTYHKEARNSWDSPAFSNDVIRKRHYRIGLNLFNKKPE
KGVQYLIERGFVPDTPVGVAHFLLQRKGLSRQMIGEFLGNRQKQFNRDVLDCVVDEMDFS
TMELDEALRKFQAHIRVQGEAQKVERLIEAFSQRYCICNPGVVRQFRNPDTIFILAFAII
LLNTDMYSPNVKPERKMKLEDFIKNLRGVDDGEDIPREMLMGIYERIRKRELKTNEDHVS
QVQKVEKLIVGKKPIGSLHPGLGCVLSLPHRRLVCYCRLFEVPDPNKPQKLGLHQREIFL
FNDLLVVTKIFQKKKNSVTYSFRQSFSLYGMQVLLFENQYYPNGIRLTSSVPGADIKVLI
NFNAPNPQDRKKFTDDLRESIAEVQEMEKHRIESELEKQKGVVRPSMSQCSSLKKESGNG
TLSRACLDDSYASGEGLKRSALSSSLRDLSEAGKRGRRSSAGSLESNVEFQPFEPLQPSV
LCS
Enzyme 115 Number of Residues 963
Enzyme 115 Molecular Weight 108313.3
Enzyme 115 Theoretical pI 6.93
Enzyme 115 GO Classification
Function
  • ARF guanyl-nucleotide exchange factor activity
  • GTPase regulator activity
  • enzyme regulator activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
  • biological regulation
  • regulation of ARF protein signal transduction
  • regulation of Ras protein signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 115 General Function Involved in ARF guanyl-nucleotide exchange factor activity
Enzyme 115 Specific Function In addition to accelerate GTP gamma S binding by ARFs of all three classes, it appears to function preferentially as a guanine nucleotide exchange protein for ARF6, mediating internalisation of beta-1 integrin
Enzyme 115 Pathways Not Available
Enzyme 115 Reactions Not Available
Enzyme 115 Pfam Domain Function
Enzyme 115 Signals
  • None
Enzyme 115 Transmembrane Regions
  • None
Enzyme 115 Essentiality Not Available
Enzyme 115 GenBank ID Protein 50582989 Link Image
Enzyme 115 UniProtKB/Swiss-Prot ID Q6DN90 Link Image
Enzyme 115 UniProtKB/Swiss-Prot Entry Name IQEC1_HUMAN Link Image
Enzyme 115 PDB ID Not Available
Enzyme 115 Cellular Location Not Available
Enzyme 115 Gene Sequence >2892 bp
ATGTGGTGCCTGCACTGCAACTCGGAGAGGACCCAGTCCCTTCTGGAGCTAGAGCTTGAC
AGCGGCGTCGAGGGCGAGGCCCCCAGCAGTGAGACTGGCACATCCCTGGACAGCCCCTCA
GCCTACCCCCAGGGCCCCTTGGTGCCCGGTTCCAGCCTGAGCCCGGATCACTACGAGCAC
ACGTCAGTGGGAGCCTATGGGCTGTACTCGGGGCCGCCGGGGCAACAGCAGCGCACGCGG
AGGCCCAAGCTGCAGCACTCGACCTCCATCCTGCGCAAGCAGGCTGAGGAGGAGGCCATC
AAGCGCTCACGCTCACTCTCCGAGAGCTATGAGCTCTCCTCGGACCTGCAGGACAAGCAG
GTGGAGATGCTAGAACGAAAGTATGGGGGGCGCCTGGTAACCCGCCATGCGGCCCGCACC
ATCCAGACGGCGTTTCGCCAGTACCAGATGAACAAGAACTTCGAGCGCTTGCGCAGCTCC
ATGTCAGAGAACCGCATGTCACGCCGGATTGTGCTGTCCAACATGAGGATGCAGTTCTCC
TTTGAGGGGCCTGAGAAAGTGCACAGCTCCTACTTCGAGGGGAAGCAGGTCTCAGTGACT
AACGACGGCTCCCAGCTGGGAGCCCTGGTGTCCCCTGAGTGTGGTGACCTCAGCGAGCCC
ACCACCCTCAAGTCTCCGGCCCCCTCCAGTGACTTTGCGGACGCCATCACCGAGCTGGAG
GACGCCTTCTCTAGGCAAGTGAAATCACTGGCCGAGTCCATCGACGATGCCCTCAACTGC
CGCAGCCTGCACACTGAGGAGGCACCGGCCCTGGATGCGGCGCGGGCCCGGGACACCGAA
CCCCAGACAGCCCTGCACGGCATGGACCACCGCAAACTGGACGAGATGACGGCCTCGTAC
AGTGATGTCACCCTGTACATCGATGAGGAGGAGCTGTCGCCCCCTCTGCCCCTCTCGCAG
GCAGGGGACCGGCCGTCCAGCACCGAGTCGGACCTGCGGCTACGGGCTGGGGGCGCAGCC
CCAGACTACTGGGCCCTGGCCCACAAAGAGGACAAGGCTGACACGGACACGAGCTGCCGG
AGCACGCCGTCGCTGGAGCGGCAGGAGCAGCGGCTGCGGGTGGAGCATCTGCCGCTGCTC
ACCATCGAGCCACCCAGCGACAGCTCTGTGGACCTTAGTGACCGCTCGGAGCGGGGGTCA
CTCAAGAGGCAGAGTGCTTACGAGCGCAGCCTTGGCGGGCAGCAGGGCAGTCCCAAGCAT
GGTCCCCACAGCGGCGCCCCCAAGAGCCTCCCCCGGGAGGAGCCTGAGTTGCGGCCCCGG
CCCCCCAGGCCCCTGGACAGCCACTTGGCCATCAATGGCTCAGCCAACCGGCAGAGCAAG
TCTGAGTCGGACTACTCAGACGGTGACAATGACAGCATCAACAGCACGTCCAACTCCAAC
GATACCATCAACTGCAGCTCCGAGTCATCGTCCCGTGACAGCCTGCGGGAGCAGACGCTC
AGCAAGCAGACCTACCACAAGGAGGCCCGCAACAGCTGGGACTCGCCTGCCTTTAGCAAC
GATGTCATCCGCAAGAGGCACTACCGCATCGGCCTGAACCTCTTCAACAAGAAGCCTGAG
AAGGGAGTCCAGTACCTCATCGAGCGTGGCTTTGTGCCCGACACGCCCGTCGGGGTGGCC
CACTTCCTGCTGCAGCGCAAGGGCCTCAGCCGGCAGATGATCGGCGAGTTCCTGGGCAAC
CGGCAGAAGCAGTTCAACCGTGACGTGCTCGACTGCGTCGTGGACGAGATGGACTTCTCT
ACCATGGAGCTGGATGAGGCCCTCAGGAAATTCCAGGCGCACATCCGTGTCCAAGGGGAG
GCTCAGAAAGTGGAGCGGCTCATAGAGGCGTTCAGCCAGCGCTACTGCATCTGCAACCCT
GGGGTGGTGCGGCAATTCCGGAACCCAGACACCATTTTCATCCTGGCCTTCGCCATCATC
CTGCTGAACACCGACATGTACAGCCCCAATGTCAAGCCCGAGCGGAAAATGAAGCTAGAG
GACTTCATCAAGAACCTCCGAGGTGTGGACGATGGTGAGGACATTCCCCGTGAGATGCTG
ATGGGGATCTATGAACGGATCCGTAAGCGAGAGCTAAAGACCAATGAGGACCATGTGTCC
CAGGTGCAGAAGGTGGAGAAGCTCATTGTGGGGAAAAAGCCGATCGGATCCCTGCATCCC
GGGCTCGGCTGTGTGCTCTCTCTGCCCCACCGTCGGTTGGTCTGCTACTGCCGGCTCTTT
GAGGTTCCAGACCCAAACAAGCCCCAGAAACTCGGACTACACCAGCGAGAAATCTTCCTG
TTCAACGACCTCCTGGTGGTCACCAAGATCTTCCAGAAGAAGAAGAACTCGGTGACGTAC
AGCTTCCGACAGTCCTTCTCCTTGTACGGCATGCAGGTCCTGCTCTTCGAGAACCAGTAC
TACCCCAATGGCATCCGGCTCACCTCGTCTGTCCCCGGAGCAGATATCAAAGTGTTAATA
AACTTCAACGCCCCCAACCCTCAAGACCGGAAGAAATTCACCGATGACCTGCGGGAGTCC
ATTGCGGAAGTCCAAGAGATGGAGAAGCACAGGATAGAGTCGGAGCTCGAGAAGCAGAAA
GGCGTCGTGCGGCCCAGCATGTCCCAGTGCTCTAGCCTCAAAAAGGAGTCGGGCAACGGA
ACACTGAGCCGGGCCTGCCTGGACGACAGCTATGCCAGCGGTGAGGGCCTCAAGCGCAGC
GCCCTCAGCAGCTCCCTGCGGGACCTCTCGGAAGCCGGGAAGCGAGGGCGTCGCAGCAGT
GCGGGATCGCTAGAGAGCAATGTGGAATTTCAGCCTTTCGAGCCACTGCAGCCGTCAGTG
CTGTGCTCCTAA
Enzyme 115 GenBank Gene ID NM_014869.4 Link Image
Enzyme 115 GeneCard ID IQSEC1 Link Image
Enzyme 115 GenAtlas ID IQSEC1 Link Image
Enzyme 115 HGNC ID HGNC:29112 Link Image
Enzyme 115 Chromosome Location 3
Enzyme 115 Locus 3p25.2
Enzyme 115 SNPs SNPJam Report Link Image
Enzyme 115 General References
  1. Dunphy JL, Moravec R, Ly K, Lasell TK, Melancon P, Casanova JE: The Arf6 GEF GEP100/BRAG2 regulates cell adhesion by controlling endocytosis of beta1 integrins. Curr Biol. 2006 Feb 7;16(3):315-20. [PubMed Link Image]
  2. Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Oct 30;5(5):277-86. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Someya A, Sata M, Takeda K, Pacheco-Rodriguez G, Ferrans VJ, Moss J, Vaughan M: ARF-GEP(100), a guanine nucleotide-exchange protein for ADP-ribosylation factor 6. Proc Natl Acad Sci U S A. 2001 Feb 27;98(5):2413-8. [PubMed Link Image]
  5. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  8. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 115 Metabolite References Not Available
Enzyme 116 [top]
Enzyme 116 ID 14190
Enzyme 116 Name MAP kinase-activating death domain protein
Enzyme 116 Synonyms
  1. Differentially expressed in normal and neoplastic cells
  2. Insulinoma glucagonoma clone 20
  3. Rab3 GDP/GTP exchange factor
Enzyme 116 Gene Name MADD
Enzyme 116 Protein Sequence >MAP kinase-activating death domain protein
MVQKKKFCPRLLDYLVIVGARHPSSDSVAQTPELLRRYPLEDHTEFPLPPDVVFFCQPEG
CLSVRQRRMSLRDDTSFVFTLTDKDTGVTRYGICVNFYRSFQKRISKEKGEGGAGSRGKE
GTHATCASEEGGTESSESGSSLQPLSADSTPDVNQSPRGKRRAKAGSRSRNSTLTSLCVL
SHYPFFSTFRECLYTLKRLVDCCSERLLGKKLGIPRGVQRDTMWRIFTGSLLVEEKSSAL
LHDLREIEAWIYRLLRSPVPVSGQKRVDIEVLPQELQPALTFALPDPSRFTLVDFPLHLP
LELLGVDACLQVLTCILLEHKVVLQSRDYNALSMSVMAFVAMIYPLEYMFPVIPLLPTCM
ASAEQLLLAPTPYIIGVPASFFLYKLDFKMPDDVWLVDLDSNRVIAPTNAEVLPILPEPE
SLELKKHLKQALASMSLNTQPILNLEKFHEGQEIPLLLGRPSNDLQSTPSTEFNPLIYGN
DVDSVDVATRVAMVRFFNSANVLQGFQMHTRTLRLFPRPVVAFQAGSFLASRPRQTPFAE
KLARTQAVEYFGEWILNPTNYAFQRIHNNMFDPALIGDKPKWYAHQLQPIHYRVYDSNSQ
LAEALSVPPERDSDSEPTDDSGSDSMDYDDSSSSYSSLGDFVSEMMKCDINGDTPNVDPL
THAALGDASEVEIDELQNQKEAEEPGPDSENSQENPPLRSSSSTTASSSPSTVIHGANSE
PADSTEMDDKAAVGVSKPLPSVPPSIGKSNVDRRQAEIGEGSVRRRIYDNPYFEPQYGFP
PEEDEDEQGESYTPRFSQHVSGNRAQKLLRPNSLRLASDSDAESDSRASSPNSTVSNTST
EGFGGIMSFASSLYRNHSTSFSLSNLTLPTKGAREKATPFPSLKVFGLNTLMEIVTEAGP
GSGEGNRRALVDQKSSVIKHSPTVKREPPSPQGRSSNSSENQQFLKEVVHSVLDGQGVGW
LNMKKVRRLLESEQLRVFVLSKLNRMVQSEDDARQDIIPDVEISRKVYKGMLDLLKCTVL
SLEQSYAHAGLGGMASIFGLLEIAQTHYYSKEPDKRKRSPTESVNTPVGKDPGLAGRGDP
KAMAQLRVPQLGPRAPSATGKGPKELDTRSLKEENFIASIELWNKHQEVKKQKALEKQRP
EVIKPVFDLGETEEKKSQISADSGVSLTSSSQRTDQDSVIGVSPAVMIRSSSQDSEVSTV
VSNSSGETLGADSDLSSNAGDGPGGEGSVHLASSRGTLSDSEIETNSATSTIFGKAHSLK
PSIKEKLAGSPIRTSEDVSQRVYLYEGLLGRDKGSMWDQLEDAAMETFSISKERSTLWDQ
MQFWEDAFLDAVMLEREGMGMDQGPQEMIDRYLSLGEHDRKRLEDDEDRLLATLLHNLIS
YMLLMKVNKNDIRKKVRRLMGKSHIGLVYSQQINEVLDQLANLNGRDLSIWSSGSRHMKK
QTFVVHAGTDTNGDIFFMEVCDDCVVLRSNIGTVYERWWYEKLINMTYCPKTKVLCLWRR
NGSETQLNKFYTKKCRELYYCVKDSMERAAARQQSIKPGPELGGEFPVQDLKTGEGGLLQ
VTLEGINLKFMHNQVFIELNHIKKCNTVRGVFVLEEFVPEIKEVVSHKYKTPMAHEICYS
VLCLFSYVAAVHSSEEDLRTPPRPVSS
Enzyme 116 Number of Residues 1647
Enzyme 116 Molecular Weight 183301.5
Enzyme 116 Theoretical pI 5.90
Enzyme 116 GO Classification Not Available
Enzyme 116 General Function Involved in death receptor binding
Enzyme 116 Specific Function Plays a significant role in regulating cell proliferation, survival and death through alternative mRNA splicing. Isoform 5 shows increased cell proliferation and isoform 2 shows decreased. Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms. Component of the TNFRSF1A signaling complex:MADD links TNFRSF1A with MAP kinase activation. Plays an important regulatory role in physiological cell death (TNF-alpha-induced, caspase-mediated apoptosis); isoform 1 is susceptible to inducing apoptosis, isoform 5 is resistant and isoform 3 and isoform 4 have no effect
Enzyme 116 Pathways Not Available
Enzyme 116 Reactions Not Available
Enzyme 116 Pfam Domain Function
Enzyme 116 Signals
  • None
Enzyme 116 Transmembrane Regions
  • 336-356 366-386
Enzyme 116 Essentiality Not Available
Enzyme 116 GenBank ID Protein 209862994 Link Image
Enzyme 116 UniProtKB/Swiss-Prot ID Q8WXG6 Link Image
Enzyme 116 UniProtKB/Swiss-Prot Entry Name MADD_HUMAN Link Image
Enzyme 116 PDB ID Not Available
Enzyme 116 Cellular Location Not Available
Enzyme 116 Gene Sequence >4944 bp
ATGGTGCAAAAGAAGAAGTTCTGTCCTCGGTTACTTGACTATCTAGTGATCGTAGGGGCC
AGGCACCCGAGCAGTGATAGCGTGGCCCAGACTCCTGAATTGCTACGGCGATACCCCTTG
GAGGATCACACTGAGTTTCCCCTGCCCCCAGATGTAGTGTTCTTCTGCCAGCCCGAGGGC
TGCCTGAGCGTGCGGCAGCGGCGCATGAGCCTTCGGGATGATACCTCTTTTGTCTTCACC
CTCACTGACAAGGACACTGGAGTCACGCGATATGGCATCTGTGTTAACTTCTACCGCTCC
TTCCAAAAGCGAATCTCTAAGGAGAAGGGGGAAGGTGGGGCAGGGTCCCGTGGGAAGGAA
GGAACCCATGCCACCTGTGCCTCAGAAGAGGGTGGCACTGAGAGCTCAGAGAGTGGCTCA
TCCCTGCAGCCTCTCAGTGCTGACTCTACCCCTGATGTGAACCAGTCTCCTCGGGGCAAA
CGCCGGGCCAAGGCGGGGAGCCGCTCCCGCAACAGTACTCTCACGTCCCTGTGCGTGCTC
AGCCACTACCCTTTCTTCTCCACCTTCCGAGAGTGTTTGTATACTCTCAAGCGCCTGGTG
GACTGCTGTAGTGAGCGCCTTCTGGGCAAGAAACTGGGCATCCCTCGAGGCGTACAAAGG
GACACCATGTGGCGGATCTTTACTGGATCGCTGCTGGTAGAGGAGAAGTCAAGTGCCCTT
CTGCATGACCTTCGAGAGATTGAGGCCTGGATCTATCGATTGCTGCGCTCCCCAGTACCC
GTCTCTGGGCAGAAGCGAGTAGACATCGAGGTCCTACCCCAAGAGCTCCAGCCAGCTCTG
ACCTTTGCTCTTCCAGACCCATCTCGATTCACCCTAGTGGATTTCCCACTGCACCTTCCC
TTGGAACTTCTAGGTGTGGACGCCTGTCTCCAGGTGCTAACCTGCATTCTGTTAGAGCAC
AAGGTGGTGCTACAGTCCCGAGACTACAATGCACTCTCCATGTCTGTGATGGCATTCGTG
GCAATGATCTACCCACTGGAGTATATGTTTCCTGTCATCCCGCTGCTACCCACCTGCATG
GCATCAGCAGAGCAGCTGCTGTTGGCTCCAACCCCGTACATCATTGGGGTTCCTGCCAGC
TTCTTCCTCTACAAACTGGACTTCAAAATGCCTGATGATGTATGGCTAGTGGATCTGGAC
AGCAATAGGGTGATTGCCCCCACCAATGCAGAAGTGCTGCCTATCCTGCCAGAACCAGAA
TCACTAGAGCTGAAAAAGCATTTAAAGCAGGCCTTGGCCAGCATGAGTCTCAACACCCAG
CCCATCCTCAATCTGGAGAAATTTCATGAGGGCCAGGAGATCCCCCTTCTCTTGGGAAGG
CCTTCTAATGACCTGCAGTCCACACCGTCCACTGAATTCAACCCACTCATCTATGGCAAT
GATGTGGATTCTGTGGATGTTGCAACCAGGGTTGCCATGGTACGGTTCTTCAATTCCGCC
AACGTGCTGCAGGGATTTCAGATGCACACGCGTACCCTGCGCCTCTTTCCTCGGCCTGTG
GTAGCTTTTCAAGCTGGCTCCTTTCTAGCCTCACGTCCCCGGCAGACTCCTTTTGCCGAG
AAATTGGCCAGGACTCAGGCTGTGGAGTACTTTGGGGAATGGATCCTTAACCCCACCAAC
TATGCCTTTCAGCGAATTCACAACAATATGTTTGATCCAGCCCTGATTGGTGACAAGCCA
AAGTGGTATGCTCATCAGCTGCAGCCTATCCACTATCGCGTCTATGACAGCAATTCCCAG
CTGGCTGAGGCCCTGAGTGTACCACCAGAGCGGGACTCTGACTCCGAACCTACTGATGAT
AGTGGCAGTGATAGTATGGATTATGACGATTCAAGCTCTTCTTACTCCTCCCTTGGTGAC
TTTGTCAGTGAAATGATGAAATGTGACATTAATGGTGATACTCCCAATGTGGACCCTCTG
ACACATGCAGCACTGGGGGATGCCAGCGAGGTGGAGATTGACGAGCTGCAGAATCAGAAG
GAAGCAGAAGAGCCTGGCCCAGACAGTGAGAACTCTCAGGAAAACCCCCCACTGCGCTCC
AGCTCTAGCACCACAGCCAGCAGCAGCCCCAGCACTGTCATCCACGGAGCCAACTCTGAA
CCTGCTGACTCTACGGAGATGGATGATAAGGCAGCAGTAGGCGTCTCCAAGCCCCTCCCT
TCCGTGCCTCCCAGCATTGGCAAATCGAACGTGGACAGACGTCAGGCAGAAATTGGAGAG
GGGTCAGTGCGCCGGCGAATCTATGACAATCCATACTTCGAGCCCCAATATGGCTTTCCC
CCTGAGGAAGATGAGGATGAGCAGGGGGAAAGTTACACTCCCCGATTCAGCCAACATGTC
AGTGGCAATCGGGCTCAAAAGCTGCTGCGGCCCAACAGCTTGAGACTGGCAAGTGACTCA
GATGCAGAGTCAGACTCTCGGGCAAGCTCTCCCAACTCCACCGTCTCCAACACCAGCACC
GAGGGCTTCGGGGGCATCATGTCTTTTGCCAGCAGCCTCTATCGGAACCACAGTACCAGC
TTCAGTCTTTCAAACCTCACACTGCCCACCAAAGGTGCCCGAGAGAAGGCCACGCCCTTC
CCCAGTCTGAAAGTATTTGGGCTAAATACTCTAATGGAGATTGTTACTGAAGCCGGCCCC
GGGAGTGGTGAAGGAAACAGGAGGGCGTTAGTGGATCAGAAGTCATCTGTCATTAAACAC
AGCCCAACAGTGAAAAGAGAACCTCCATCACCCCAGGGTCGATCCAGCAATTCTAGTGAG
AACCAGCAGTTCCTGAAGGAGGTGGTGCACAGCGTGCTGGACGGCCAGGGAGTTGGCTGG
CTCAACATGAAAAAGGTGCGCCGGCTGCTGGAGAGCGAGCAGCTGCGAGTCTTTGTCCTG
AGCAAGCTGAACCGCATGGTGCAGTCAGAGGACGATGCCCGGCAGGACATCATCCCGGAT
GTGGAGATCAGTCGGAAGGTGTACAAGGGAATGTTAGACCTCCTCAAGTGTACAGTCCTC
AGCTTGGAGCAGTCCTATGCCCACGCGGGTCTGGGTGGCATGGCCAGCATCTTTGGGCTT
TTGGAGATTGCCCAGACCCACTACTATAGTAAAGAACCAGACAAGCGGAAGAGAAGTCCA
ACAGAAAGTGTAAATACCCCAGTTGGCAAGGATCCTGGCCTAGCTGGGCGGGGGGACCCA
AAGGCTATGGCACAACTGAGAGTTCCACAACTGGGACCTCGGGCACCAAGTGCCACAGGA
AAGGGTCCTAAGGAACTGGACACCAGAAGTTTAAAGGAAGAAAATTTTATAGCATCTATT
GAATTGTGGAACAAGCACCAGGAAGTGAAAAAGCAAAAAGCTTTGGAAAAACAGAGGCCT
GAAGTAATCAAACCTGTCTTTGACCTTGGTGAGACAGAGGAGAAAAAGTCCCAGATCAGC
GCAGACAGTGGTGTGAGCCTGACGTCTAGTTCCCAGAGGACTGATCAAGACTCTGTCATC
GGCGTGAGTCCAGCTGTTATGATCCGCAGCTCAAGTCAGGATTCTGAAGTTAGCACCGTG
GTGAGTAATAGCTCTGGAGAGACCCTTGGAGCTGACAGTGACTTGAGCAGCAATGCAGGT
GATGGACCAGGTGGCGAGGGCAGTGTTCACCTGGCAAGCTCTCGGGGCACTTTGTCTGAT
AGTGAAATTGAGACCAACTCTGCCACAAGCACCATCTTTGGTAAAGCCCACAGCTTGAAG
CCAAGCATAAAGGAGAAGCTGGCAGGCAGCCCCATTCGTACTTCTGAAGATGTGAGCCAG
CGAGTCTATCTCTATGAGGGACTCCTAGGAAGGGACAAAGGATCCATGTGGGACCAGTTA
GAGGATGCAGCTATGGAGACCTTTTCTATAAGCAAAGAGCGTTCTACTTTATGGGACCAA
ATGCAATTCTGGGAAGATGCCTTCTTAGATGCTGTGATGTTGGAGAGAGAAGGGATGGGT
ATGGACCAGGGTCCCCAGGAAATGATCGACAGGTACCTGTCCCTTGGAGAACATGACCGG
AAGCGCCTGGAAGATGATGAAGATCGCTTGCTGGCCACACTTCTGCACAACCTCATCTCC
TACATGCTGCTGATGAAGGTAAATAAGAATGACATCCGCAAGAAGGTGAGGCGCCTAATG
GGAAAGTCGCACATTGGGCTTGTGTACAGCCAGCAAATCAATGAGGTGCTTGATCAGCTG
GCGAACCTGAATGGACGCGATCTCTCTATCTGGTCCAGTGGCAGCCGGCACATGAAGAAG
CAGACATTTGTGGTACATGCAGGGACAGATACAAACGGAGATATCTTTTTCATGGAGGTG
TGCGATGACTGTGTGGTGTTGCGTAGTAACATCGGAACAGTGTATGAGCGCTGGTGGTAC
GAGAAGCTCATCAACATGACCTACTGTCCCAAGACGAAGGTGTTGTGCTTGTGGCGTAGA
AATGGCTCTGAGACCCAGCTCAACAAGTTCTATACTAAAAAGTGTCGGGAGCTGTACTAC
TGTGTGAAGGACAGCATGGAGCGCGCTGCCGCCCGACAGCAAAGCATCAAACCCGGACCT
GAATTGGGTGGCGAGTTCCCTGTGCAGGACCTGAAGACTGGTGAGGGTGGCCTGCTGCAG
GTGACCCTGGAAGGGATCAACCTCAAATTCATGCACAATCAGGTTTTCATAGAGCTGAAT
CACATTAAAAAGTGCAATACAGTTCGAGGCGTCTTTGTCCTGGAGGAATTTGTTCCTGAA
ATTAAAGAAGTGGTGAGCCACAAGTACAAGACACCAATGGCCCACGAAATCTGCTACTCC
GTATTATGTCTCTTCTCGTACGTGGCTGCAGTTCATAGCAGTGAGGAAGATCTCAGAACC
CCGCCCCGGCCTGTCTCTAGCTGA
Enzyme 116 GenBank Gene ID NM_003682.3 Link Image
Enzyme 116 GeneCard ID MADD Link Image
Enzyme 116 GenAtlas ID MADD Link Image
Enzyme 116 HGNC ID HGNC:6766 Link Image
Enzyme 116 Chromosome Location 1
Enzyme 116 Locus 11p11.2
Enzyme 116 SNPs SNPJam Report Link Image
Enzyme 116 General References
  1. Chow VT, Lee SS: DENN, a novel human gene differentially expressed in normal and neoplastic cells. DNA Seq. 1996;6(5):263-73. [PubMed Link Image]
  2. Schievella AR, Chen JH, Graham JR, Lin LL: MADD, a novel death domain protein that interacts with the type 1 tumor necrosis factor receptor and activates mitogen-activated protein kinase. J Biol Chem. 1997 May 2;272(18):12069-75. [PubMed Link Image]
  3. Chow VT, Lim KM, Lim D: The human DENN gene: genomic organization, alternative splicing, and localization to chromosome 11p11.21-p11.22. Genome. 1998 Aug;41(4):543-52. [PubMed Link Image]
  4. Al-Zoubi AM, Efimova EV, Kaithamana S, Martinez O, El-Idrissi Mel-A, Dogan RE, Prabhakar BS: Contrasting effects of IG20 and its splice isoforms, MADD and DENN-SV, on tumor necrosis factor alpha-induced apoptosis and activation of caspase-8 and -3. J Biol Chem. 2001 Dec 14;276(50):47202-11. Epub 2001 Sep 27. [PubMed Link Image]
  5. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Lim KM, Yeo WS, Chow VT: Antisense abrogation of DENN expression induces apoptosis of leukemia cells in vitro, causes tumor regression in vivo and alters the transcription of genes involved in apoptosis and the cell cycle. Int J Cancer. 2004 Mar;109(1):24-37. [PubMed Link Image]
  8. Efimova EV, Al-Zoubi AM, Martinez O, Kaithamana S, Lu S, Arima T, Prabhakar BS: IG20, in contrast to DENN-SV, (MADD splice variants) suppresses tumor cell survival, and enhances their susceptibility to apoptosis and cancer drugs. Oncogene. 2004 Feb 5;23(5):1076-87. [PubMed Link Image]
  9. Del Villar K, Miller CA: Down-regulation of DENN/MADD, a TNF receptor binding protein, correlates with neuronal cell death in Alzheimer's disease brain and hippocampal neurons. Proc Natl Acad Sci U S A. 2004 Mar 23;101(12):4210-5. Epub 2004 Mar 8. [PubMed Link Image]
  10. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  11. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  12. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 116 Metabolite References Not Available
Enzyme 117 [top]
Enzyme 117 ID 14191
Enzyme 117 Name Guanine nucleotide exchange factor DBS
Enzyme 117 Synonyms
  1. DBL's big sister
  2. MCF2-transforming sequence-like protein
Enzyme 117 Gene Name MCF2L
Enzyme 117 Protein Sequence >Guanine nucleotide exchange factor DBS
MFDCWRFILCKRPGSNSYSSPQRPNEAKKEETDHQIDVSDVIRLVQDTPEATAMATDEIM
HQDIVPLCAADIQDQLKKRFAYLSGGRGQDGSPVITFPDYPAFSEIPDKEFQNVMTYLTS
IPSLQDAGIGFILVIDRRRDKWTSVKASVLRIAASFPANLQLVLVLRPTGFFQRTLSDIA
FKFNRDDFKMKVPVIMLSSVPDLHGYIDKSQLTEDLGGTLDYCHSRWLCQRTAIESFALM
VKQTAQMLQSFGTELAETELPNDVQSTSSVLCAHTEKKDKAKEDLRLALKEGHSVLESLR
ELQAEGSEPSVNQDQLDNQATVQRLLAQLNETEAAFDEFWAKHQQKLEQCLQLRHFEQGF
REVKAILDAASQKIATFTDIGNSLAHVEHLLRDLASFEEKSGVAVERARALSLDGEQLIG
NKHYAVDSIRPKCQELRHLCDQFSAEIARRRGLLSKSLELHRRLETSMKWCDEGIYLLAS
QPVDKCQSQDGAEAALQEIEKFLETGAENKIQELNAIYKEYESILNQDLMEHVRKVFQKQ
ASMEEVFHRRQASLKKLAARQTRPVQPVAPRPEALAKSPCPSPGIRRGSENSSSEGGALR
RGPYRRAKSEMSESRQGRGSAGEEEESLAILRRHVMSELLDTERAYVEELLCVLEGYAAE
MDNPLMAHLLSTGLHNKKDVLFGNMEEIYHFHNRIFLRELENYTDCPELVGRCFLERMED
FQIYEKYCQNKPRSESLWRQCSDCPFFQECQRKLDHKLSLDSYLLKPVQRITKYQLLLKE
MLKYSRNCEGAEDLQEALSSILGILKAVNDSMHLIAITGYDGNLGDLGKLLMQGSFSVWT
DHKRGHTKVKELARFKPMQRHLFLHEKAVLFCKKREENGEGYEKAPSYSYKQSLNMAAVG
ITENVKGDAKKFEIWYNAREEVYIVQAPTPEIKAAWVNEIRKVLTSQLQACREASQHRAL
EQSQSLPLPAPTSTSPSRGNSRNIKKLEERKTDPLSLEGYVSSAPLTKPPEKGKGWSKTS
HSLEAPEDDGGWSSAEEQINSSDAEEDGGLGPKKLVPGKYTVVADHEKGGPDALRVRSGD
VVELVQEGDEGLWYVRDPTTGKEGWVPASSLSVRLGPSGSAQCLSSSGKAHVPRAHP
Enzyme 117 Number of Residues 1137
Enzyme 117 Molecular Weight 128107.9
Enzyme 117 Theoretical pI 6.39
Enzyme 117 GO Classification
Function
  • GTPase regulator activity
  • Ras guanyl-nucleotide exchange factor activity
  • Rho guanyl-nucleotide exchange factor activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
  • biological regulation
  • intracellular signaling pathway
  • regulation of Ras protein signal transduction
  • regulation of Rho protein signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signaling
  • signaling pathway
Component
  • cell part
  • intracellular
Enzyme 117 General Function Involved in Rho guanyl-nucleotide exchange factor activity
Enzyme 117 Specific Function Guanine nucleotide exchange factor that potentially links pathways that signal through RAC1, RHOA and CDC42. Catalyzes guanine nucleotide exchange on RHOA and CDC42 and interacts specifically with the GTP-bound form of RAC1, suggesting that it functions as an effector of RAC1. May also participate in axonal transport in the brain. Becomes activated and highly tumorigenic by truncation of the N-terminus. Isoform 5 activates CDC42
Enzyme 117 Pathways Not Available
Enzyme 117 Reactions Not Available
Enzyme 117 Pfam Domain Function
Enzyme 117 Signals
  • None
Enzyme 117 Transmembrane Regions
  • None
Enzyme 117 Essentiality Not Available
Enzyme 117 GenBank ID Protein 163644323 Link Image
Enzyme 117 UniProtKB/Swiss-Prot ID O15068 Link Image
Enzyme 117 UniProtKB/Swiss-Prot Entry Name MCF2L_HUMAN Link Image
Enzyme 117 PDB ID 1RJ2 Link Image
Enzyme 117 PDB File Show
Enzyme 117 3D Structure
Enzyme 117 Cellular Location Not Available
Enzyme 117 Gene Sequence >3390 bp
ATGGCCGAGAAGGGAGCATCCCGGGGAACCCTGCGGCGGCTGTGGTCACTGCCCAGGAGG
CGCCGGGGAACTGCAGGGCGCTCGAGGCCAGATGAAATCATGCACCAGGACATCGTCCCG
CTCTGTGCTGCCGACATCCAGGACCAGCTAAAGAAGCGCTTTGCTTACCTGTCCGGTGGG
CGGGGGCAGGACGGAAGCCCGGTTATCACCTTCCCTGACTACCCGGCCTTCAGCGAGATT
CCGGACAAGGAGTTCCAGAATGTCATGACCTACCTCACCAGCATCCCCAGCCTGCAGGAC
GCTGGCATCGGATTCATCCTGGTGATAGACCGGCGACGGGACAAATGGACCTCCGTGAAG
GCGTCCGTCCTGCGCATCGCAGCATCTTTCCCGGCAAACCTGCAGCTCGTCCTCGTGCTT
CGCCCGACGGGTTTTTTCCAAAGGACTCTCTCCGACATCGCTTTCAAATTCAATAGAGAT
GACTTTAAGATGAAGGTGCCGGTCATAATGCTGAGCTCCGTACCAGACTTACACGGTTAC
ATCGATAAGTCGCAGCTGACCGAGGACCTGGGTGGGACCCTGGACTACTGCCACTCCCGG
TGGCTGTGCCAGCGCACGGCCATCGAAAGTTTCGCCCTCATGGTGAAGCAGACGGCTCAG
ATGCTGCAGTCCTTCGGGACCGAGCTGGCTGAAACAGAGCTGCCCAATGACGTCCAGTCG
ACAAGCTCAGTGCTGTGTGCGCACACAGAGAAGAAGGACAAGGCGAAGGAGGATTTGAGG
CTGGCACTGAAAGAGGGGCACAGTGTCCTGGAGAGCCTCAGGGAGCTGCAGGCTGAGGGC
TCAGAGCCCAGTGTGAACCAGGACCAGCTTGACAACCAGGCCACCGTGCAGAGGCTCCTG
GCCCAGCTGAACGAAACCGAGGCTGCCTTCGATGAGTTCTGGGCAAAGCATCAGCAGAAA
CTGGAGCAGTGTCTGCAGCTCCGGCACTTTGAGCAGGGCTTCCGGGAGGTCAAAGCCATC
TTGGACGCAGCGTCCCAGAAGATAGCAACCTTCACAGACATCGGCAACAGCCTGGCGCAT
GTGGAGCACCTGCTGAGGGACCTGGCCAGCTTCGAGGAGAAATCAGGCGTGGCCGTGGAG
AGGGCCCGGGCCCTGTCTCTGGACGGCGAGCAGCTCATTGGGAACAAGCACTACGCGGTA
GACTCCATCCGCCCAAAGTGCCAGGAGCTCCGGCACCTCTGTGACCAGTTCTCTGCGGAG
ATCGCAAGGAGGAGGGGGCTGCTCAGCAAGTCCCTGGAGCTGCACCGCCGCCTGGAGACG
TCCATGAAGTGGTGTGATGAAGGGATTTACCTGCTGGCCTCACAACCTGTGGACAAGTGC
CAGTCCCAGGACGGCGCGGAGGCTGCCCTCCAGGAAATCGAGAAGTTTTTGGAGACCGGT
GCGGAAAATAAGATCCAGGAGCTCAACGCGATTTACAAGGAATACGAATCCATCCTCAAC
CAAGATCTCATGGAGCACGTGCGAAAGGTCTTCCAGAAGCAGGCAAGCATGGAGGAGGTG
TTCCACCGCAGGCAGGCCAGCCTGAAGAAGCTGGCGGCCAGGCAGACGCGGCCCGTGCAG
CCGGTGGCCCCCAGACCCGAGGCACTGGCAAAGTCGCCCTGCCCCTCCCCAGGCATTCGG
CGAGGCTCTGAGAACTCCAGCTCCGAGGGCGGTGCGCTCCGGAGAGGGCCCTACCGGAGG
GCCAAGAGTGAGATGAGTGAGAGCCGGCAGGGCCGCGGCTCAGCGGGGGAGGAGGAGGAA
AGCCTGGCCATCCTGCGCAGGCACGTGATGAGCGAGCTCCTGGACACAGAACGGGCCTAC
GTGGAGGAGCTGCTGTGCGTCCTGGAGGGCTACGCCGCGGAGATGGATAACCCACTGATG
GCTCACCTCCTGTCAACAGGCCTTCACAACAAGAAGGATGTTTTGTTTGGAAACATGGAG
GAAATCTATCACTTCCACAACAGGATATTCCTCAGGGAGCTGGAAAACTACACTGACTGC
CCAGAACTGGTTGGAAGATGCTTTCTGGAGAGGATGGAAGATTTCCAGATCTATGAGAAG
TACTGTCAGAACAAGCCCCGCTCTGAGAGCCTGTGGAGACAGTGCTCCGACTGCCCGTTT
TTCCAGGAATGCCAGAGAAAGCTGGACCACAAGCTGAGCCTGGACTCCTACCTGCTGAAG
CCAGTGCAGAGGATCACCAAGTACCAGCTGCTGCTCAAGGAAATGCTGAAATACAGCAGG
AACTGCGAGGGGGCTGAGGACCTGCAGGAGGCGCTGAGCTCCATCCTGGGCATCCTGAAG
GCCGTGAACGACTCCATGCACCTCATCGCTATCACCGGCTATGACGGGAATCTCGGCGAC
CTGGGCAAGCTGCTGATGCAGGGCTCGTTCAGCGTCTGGACCGACCACAAGAGGGGCCAC
ACCAAGGTGAAGGAGCTGGCCAGGTTCAAGCCCATGCAGCGGCACCTGTTCCTGCACGAG
AAGGCAGTGCTCTTCTGCAAGAAGAGGGAGGAGAATGGGGAGGGGTATGAGAAAGCTCCC
TCCTACAGCTACAAGCAGTCCTTAAACATGGCTGCCGTTGGCATTACGGAGAACGTGAAG
GGAGATGCTAAGAAGTTCGAGATCTGGTACAACGCGCGCGAGGAGGTCTACATCGTCCAG
GCGCCAACTCCTGAGATTAAAGCCGCGTGGGTGAATGAAATTCGGAAAGTGCTGACCAGC
CAGCTGCAGGCTTGTAGAGAAGCCAGCCAGCACCGGGCGCTGGAGCAGTCACAGAGCCTG
CCCCTGCCGGCCCCGACCAGCACCAGTCCCTCAAGAGGAAACTCAAGGAACATCAAGAAG
CTGGAAGAAAGGAAAACAGACCCCCTAAGCCTGGAGGGATACGTCAGCTCAGCGCCACTG
ACAAAGCCCCCCGAAAAGGGCAAAGGTTGGAGCAAAACGTCCCACTCACTGGAGGCACCT
GAGGACGACGGGGGCTGGTCAAGTGCAGAGGAGCAGATTAACTCGTCCGACGCAGAGGAG
GACGGCGGGTTGGGCCCCAAGAAGCTGGTTCCAGGTAAATACACGGTCGTGGCGGACCAC
GAGAAGGGAGGCCCCGATGCGCTGCGCGTGAGGAGCGGGGACGTGGTGGAGCTGGTGCAG
GAGGGCGACGAGGGCCTCTGGTACGTCAGGGACCCGACCACTGGCAAGGAGGGCTGGGTG
CCGGCCAGCAGCCTGTCCGTCCGGCTCGGCCCGTCCGGCTCGGCCCAGTGCCTGAGCAGC
TCAGAGTCGAGCCCGGGGTCGGCCGTGCTGAGCAACTCGTCCAGCTGCAGCGAGGGCGGC
CAGGCCCCCTTCTCCGACCTGCAGGGGTAG
Enzyme 117 GenBank Gene ID NM_024979 Link Image
Enzyme 117 GeneCard ID MCF2L Link Image
Enzyme 117 GenAtlas ID MCF2L Link Image
Enzyme 117 HGNC ID HGNC:14576 Link Image
Enzyme 117 Chromosome Location 1
Enzyme 117 Locus 13q34
Enzyme 117 SNPs SNPJam Report Link Image
Enzyme 117 General References
  1. Ueda S, Kataoka T, Satoh T: Role of the Sec14-like domain of Dbl family exchange factors in the regulation of Rho family GTPases in different subcellular sites. Cell Signal. 2004 Aug;16(8):899-906. [PubMed Link Image]
  2. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
Enzyme 117 Metabolite References Not Available
Enzyme 118 [top]
Enzyme 118 ID 14222
Enzyme 118 Name Ras-related protein Rab-5A
Enzyme 118 Synonyms Not Available
Enzyme 118 Gene Name RAB5A
Enzyme 118 Protein Sequence >Ras-related protein Rab-5A
MASRGATRPNGPNTGNKICQFKLVLLGESAVGKSSLVLRFVKGQFHEFQESTIGAAFLTQ
TVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNEESFARAKNWVKELQR
QASPNIVIALSGNKADLANKRAVDFQEAQSYADDNSLLFMETSAKTSMNVNEIFMAIAKK
LPKNEPQNPGANSARGRGVDLTEPTQPTRNQCCSN
Enzyme 118 Number of Residues 215
Enzyme 118 Molecular Weight 23658.5
Enzyme 118 Theoretical pI 8.31
Enzyme 118 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • biological regulation
  • establishment of localization
  • intracellular signal transduction
  • protein transport
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
  • transport
Component
Enzyme 118 General Function Involved in GTP binding
Enzyme 118 Specific Function Required for the fusion of plasma membranes and early endosomes
Enzyme 118 Pathways Not Available
Enzyme 118 Reactions Not Available
Enzyme 118 Pfam Domain Function
Enzyme 118 Signals
  • None
Enzyme 118 Transmembrane Regions
  • None
Enzyme 118 Essentiality Not Available
Enzyme 118 GenBank ID Protein 20379048 Link Image
Enzyme 118 UniProtKB/Swiss-Prot ID P20339 Link Image
Enzyme 118 UniProtKB/Swiss-Prot Entry Name RAB5A_HUMAN Link Image
Enzyme 118 PDB ID 1R2Q Link Image
Enzyme 118 PDB File Show
Enzyme 118 3D Structure
Enzyme 118 Cellular Location Not Available
Enzyme 118 Gene Sequence >648 bp
ATGGCTAGTCGAGGCGCAACAAGACCCAACGGGCCAAATACGGGAAATAAAATATGCCAG
TTCAAACTAGTACTTCTGGGAGAGTCCGCTGTTGGCAAATCAAGCCTAGTGCTTCGTTTT
GTGAAAGGCCAATTTCATGAATTTCAAGAGAGTACCATTGGGGCTGCTTTTCTAACCCAA
ACTGTATGTCTTGATGACACTACAGTAAAGTTTGAAATATGGGATACAGCTGGTCAAGAA
CGATACCATAGCCTAGCACCAATGTACTACAGAGGAGCACAAGCAGCCATAGTTGTATAT
GATATCACAAATGAGGAGTCCTTTGCAAGAGCAAAAAATTGGGTTAAAGAACTTCAGAGG
CAAGCAAGTCCTAACATTGTAATAGCTTTATCGGGAAACAAGGCCGACCTAGCAAATAAA
AGAGCAGTAGATTTCCAGGAAGCACAGTCCTATGCAGATGACAATAGTTTATTATTCATG
GAGACATCCGCTAAAACATCAATGAATGTAAATGAAATATTCATGGCAATAGCTAAAAAA
TTGCCAAAGAATGAACCACAAAATCCAGGAGCAAATTCTGCCAGAGGAAGAGGAGTAGAC
CTTACCGAACCCACACAACCAACCAGGAATCAGTGTTGTAGTAACTAA
Enzyme 118 GenBank Gene ID AF498936 Link Image
Enzyme 118 GeneCard ID RAB5A Link Image
Enzyme 118 GenAtlas ID RAB5A Link Image
Enzyme 118 HGNC ID HGNC:9783 Link Image
Enzyme 118 Chromosome Location 3
Enzyme 118 Locus 3p24-p22
Enzyme 118 SNPs SNPJam Report Link Image
Enzyme 118 General References
  1. Zahraoui A, Touchot N, Chardin P, Tavitian A: The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion. J Biol Chem. 1989 Jul 25;264(21):12394-401. [PubMed Link Image]
  2. Farnsworth CC, Seabra MC, Ericsson LH, Gelb MH, Glomset JA: Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A. Proc Natl Acad Sci U S A. 1994 Dec 6;91(25):11963-7. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Callaghan J, Nixon S, Bucci C, Toh BH, Stenmark H: Direct interaction of EEA1 with Rab5b. Eur J Biochem. 1999 Oct 1;265(1):361-6. [PubMed Link Image]
  5. Hoffenberg S, Liu X, Nikolova L, Hall HS, Dai W, Baughn RE, Dickey BF, Barbieri MA, Aballay A, Stahl PD, Knoll BJ: A novel membrane-anchored Rab5 interacting protein required for homotypic endosome fusion. J Biol Chem. 2000 Aug 11;275(32):24661-9. [PubMed Link Image]
  6. Nielsen E, Christoforidis S, Uttenweiler-Joseph S, Miaczynska M, Dewitte F, Wilm M, Hoflack B, Zerial M: Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain. J Cell Biol. 2000 Oct 30;151(3):601-12. [PubMed Link Image]
  7. Tall GG, Barbieri MA, Stahl PD, Horazdovsky BF: Ras-activated endocytosis is mediated by the Rab5 guanine nucleotide exchange activity of RIN1. Dev Cell. 2001 Jul;1(1):73-82. [PubMed Link Image]
  8. Hadano S, Otomo A, Suzuki-Utsunomiya K, Kunita R, Yanagisawa Y, Showguchi-Miyata J, Mizumura H, Ikeda JE: ALS2CL, the novel protein highly homologous to the carboxy-terminal half of ALS2, binds to Rab5 and modulates endosome dynamics. FEBS Lett. 2004 Sep 24;575(1-3):64-70. [PubMed Link Image]
  9. Fouraux MA, Deneka M, Ivan V, van der Heijden A, Raymackers J, van Suylekom D, van Venrooij WJ, van der Sluijs P, Pruijn GJ: Rabip4' is an effector of rab5 and rab4 and regulates transport through early endosomes. Mol Biol Cell. 2004 Feb;15(2):611-24. Epub 2003 Nov 14. [PubMed Link Image]
  10. Eathiraj S, Pan X, Ritacco C, Lambright DG: Structural basis of family-wide Rab GTPase recognition by rabenosyn-5. Nature. 2005 Jul 21;436(7049):415-9. [PubMed Link Image]
  11. Hunker CM, Galvis A, Kruk I, Giambini H, Veisaga ML, Barbieri MA: Rab5-activating protein 6, a novel endosomal protein with a role in endocytosis. Biochem Biophys Res Commun. 2006 Feb 17;340(3):967-75. Epub 2006 Jan 4. [PubMed Link Image]
  12. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed Link Image]
  13. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  14. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  15. Zhu G, Liu J, Terzyan S, Zhai P, Li G, Zhang XC: High resolution crystal structures of human Rab5a and five mutants with substitutions in the catalytically important phosphate-binding loop. J Biol Chem. 2003 Jan 24;278(4):2452-60. Epub 2002 Nov 13. [PubMed Link Image]
  16. Zhu G, Zhai P, Liu J, Terzyan S, Li G, Zhang XC: Structural basis of Rab5-Rabaptin5 interaction in endocytosis. Nat Struct Mol Biol. 2004 Oct;11(10):975-83. Epub 2004 Sep 19. [PubMed Link Image]
Enzyme 118 Metabolite References Not Available
Enzyme 119 [top]
Enzyme 119 ID 14223
Enzyme 119 Name Ras-related protein Rab-5B
Enzyme 119 Synonyms Not Available
Enzyme 119 Gene Name RAB5B
Enzyme 119 Protein Sequence >Ras-related protein Rab-5B
MTSRSTARPNGQPQASKICQFKLVLLGESAVGKSSLVLRFVKGQFHEYQESTIGAAFLTQ
SVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNQETFARAKTWVKELQR
QASPSIVIALAGNKADLANKRMVEYEEAQAYADDNSLLFMETSAKTAMNVNDLFLAIAKK
LPKSEPQNLGGAAGRSRGVDLHEQSQQNKSQCCSN
Enzyme 119 Number of Residues 215
Enzyme 119 Molecular Weight 23706.6
Enzyme 119 Theoretical pI 8.30
Enzyme 119 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • biological regulation
  • establishment of localization
  • intracellular signal transduction
  • protein transport
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
  • transport
Component
Enzyme 119 General Function Involved in GTP binding
Enzyme 119 Specific Function Protein transport. Probably involved in vesicular traffic
Enzyme 119 Pathways Not Available
Enzyme 119 Reactions Not Available
Enzyme 119 Pfam Domain Function
Enzyme 119 Signals
  • None
Enzyme 119 Transmembrane Regions
  • None
Enzyme 119 Essentiality Not Available
Enzyme 119 GenBank ID Protein 20379050 Link Image
Enzyme 119 UniProtKB/Swiss-Prot ID P61020 Link Image
Enzyme 119 UniProtKB/Swiss-Prot Entry Name RAB5B_HUMAN Link Image
Enzyme 119 PDB ID 1R2Q Link Image
Enzyme 119 PDB File Show
Enzyme 119 3D Structure
Enzyme 119 Cellular Location Not Available
Enzyme 119 Gene Sequence >648 bp
ATGACTAGCAGAAGCACAGCTAGGCCCAATGGGCAACCCCAGGCCAGCAAAATTTGCCAG
TTCAAATTGGTCCTGCTGGGAGAATCTGCAGTGGGAAAGTCAAGCCTGGTATTACGTTTT
GTCAAAGGGCAGTTCCATGAGTACCAGGAGAGCACCATTGGAGCGGCCTTCCTCACCCAG
TCCGTTTGTCTAGATGACACAACAGTGAAGTTTGAGATCTGGGACACAGCTGGGCAGGAG
CGATATCACAGCTTAGCCCCCATGTACTACAGGGGTGCCCAAGCTGCAATCGTGGTTTAC
GACATTACTAATCAGGAAACCTTTGCCCGAGCAAAGACATGGGTGAAGGAACTACAGCGA
CAGGCCAGTCCTAGCATCGTTATTGCCCTGGCAGGGAACAAAGCTGACCTGGCCAACAAA
CGTATGGTGGAGTATGAAGAGGCCCAGGCATATGCAGATGACAACAGCTTATTGTTCATG
GAGACTTCAGCCAAGACAGCTATGAACGTGAATGATCTCTTCCTGGCAATAGCTAAGAAG
TTGCCAAAGAGTGAACCCCAGAATCTGGGAGGTGCAGCAGGCCGAAGCCGGGGTGTGGAT
CTCCATGAACAGTCCCAGCAGAACAAGAGCCAGTGTTGTAGCAACTGA
Enzyme 119 GenBank Gene ID AF498937 Link Image
Enzyme 119 GeneCard ID RAB5B Link Image
Enzyme 119 GenAtlas ID RAB5B Link Image
Enzyme 119 HGNC ID HGNC:9784 Link Image
Enzyme 119 Chromosome Location 1
Enzyme 119 Locus 12q13
Enzyme 119 SNPs SNPJam Report Link Image
Enzyme 119 General References
  1. Wilson DB, Wilson MP: Identification and subcellular localization of human rab5b, a new member of the ras-related superfamily of GTPases. J Clin Invest. 1992 Mar;89(3):996-1005. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Callaghan J, Nixon S, Bucci C, Toh BH, Stenmark H: Direct interaction of EEA1 with Rab5b. Eur J Biochem. 1999 Oct 1;265(1):361-6. [PubMed Link Image]
  6. Saito K, Murai J, Kajiho H, Kontani K, Kurosu H, Katada T: A novel binding protein composed of homophilic tetramer exhibits unique properties for the small GTPase Rab5. J Biol Chem. 2002 Feb 1;277(5):3412-8. Epub 2001 Dec 3. [PubMed Link Image]
  7. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed Link Image]
Enzyme 119 Metabolite References Not Available
Enzyme 120 [top]
Enzyme 120 ID 14230
Enzyme 120 Name Ran-binding protein 3
Enzyme 120 Synonyms
  1. RanBP3
Enzyme 120 Gene Name RANBP3
Enzyme 120 Protein Sequence >Ran-binding protein 3
MADLANEEKPAIAPPVFVFQKDKGQKSPAEQKNLSDSGEEPRGEAEAPHHGTGHPESAGE
HALEPPAPAGASASTPPPPAPEAQLPPFPRELAGRSAGGSSPEGGEDSDREDGNYCPPVK
RERTSSLTQFPPSQSEERSSGFRLKPPTLIHGQAPSAGLPSQKPKEQQRSVLRPAVLQAP
QPKALSQTVPSSGTNGVSLPADCTGAVPAASPDTAAWRSPSEAADEVCALEEKEPQKNES
SNASEEEACEKKDPATQQAFVFGQNLRDRVKLINESVDEADMENAGHPSADTPTATNYFL
QYISSSLENSTNSADASSNKFVFGQNMSERVLSPPKLNEVSSDANRENAAAESGSESSSQ
EATPEKESLAESAAAYTKATARKCLLEKVEVITGEEAESNVLQMQCKLFVFDKTSQSWVE
RGRGLLRLNDMASTDDGTLQSRLVMRTQGSLRLILNTKLWAQMQIDKASEKSIRITAMDT
EDQGVKVFLISASSKDTGQLYAALHHRILALRSRVEQEQEAKMPAPEPGAAPSNEEDDSD
DDDVLAPSGATAAGAGDEGDGQTTGST
Enzyme 120 Number of Residues 567
Enzyme 120 Molecular Weight 60209.3
Enzyme 120 Theoretical pI 4.42
Enzyme 120 GO Classification
Function
Process
  • establishment of localization
  • intracellular transport
  • transport
Component
Enzyme 120 General Function Involved in intracellular transport
Enzyme 120 Specific Function Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner
Enzyme 120 Pathways Not Available
Enzyme 120 Reactions Not Available
Enzyme 120 Pfam Domain Function
Enzyme 120 Signals
  • None
Enzyme 120 Transmembrane Regions
  • None
Enzyme 120 Essentiality Not Available
Enzyme 120 GenBank ID Protein 6466466 Link Image
Enzyme 120 UniProtKB/Swiss-Prot ID Q9H6Z4 Link Image
Enzyme 120 UniProtKB/Swiss-Prot Entry Name RANB3_HUMAN Link Image
Enzyme 120 PDB ID Not Available
Enzyme 120 Cellular Location Not Available
Enzyme 120 Gene Sequence >1704 bp
ATGGCGGACCTGGCGAACGAAGAAAAGCCTGCCATTGCTCCGCCCGTCTTTGTGTTTCAG
AAGGATAAAGGACAAAAGTCCCCTGCAGAGCAAAAAAACTTGTCGGATTCGGGAGAGGAG
CCTCGGGGGGAGGCTGAGGCCCCCCACCATGGCACGGGTCACCCCGAGTCAGCTGGCGAG
CATGCCCTAGAACCTCCTGCCCCTGCTGGCGCCTCAGCCAGCACTCCTCCGCCTCCCGCT
CCTGAAGCCCAGCTTCCTCCTTTTCCGCGAGAACTGGCAGGGAGGTCAGCTGGCGGCTCC
AGTCCTGAAGGCGGAGAAGATTCTGACAGAGAAGATGGAAATTACTGCCCTCCTGTCAAG
CGAGAAAGAACATCCTCTTTAACCCAGTTCCCACCCTCACAGTCAGAGGAAAGGAGCAGT
GGCTTCCGGTTGAAGCCACCAACGCTGATCCACGGCCAAGCCCCCAGCGCAGGTCTGCCA
AGCCAGAAGCCCAAGGAGCAGCAGCGGAGCGTGCTTCGCCCGGCAGTGTTACAAGCTCCG
CAGCCAAAGGCGCTGTCCCAGACTGTCCCCAGCAGTGGCACCAACGGGGTCAGCCTCCCA
GCAGACTGCACGGGGGCAGTGCCCGCAGCATCCCCTGACACTGCTGCATGGAGAAGTCCT
TCCGAAGCTGCCGATGAGGTGTGTGCACTTGAGGAGAAAGAGCCCCAGAAAAATGAGTCC
AGCAATGCCTCTGAAGAGGAAGCCTGTGAGAAAAAAGACCCCGCCACACAGCAAGCCTTT
GTATTTGGGCAGAACTTGAGGGACAGAGTTAAGCTGATAAATGAGAGCGTGGACGAAGCC
GACATGGAGAATGCTGGACACCCCAGCGCAGACACGCCAACCGCAACGAACTATTTCCTC
CAGTATATCAGTTCCAGTTTAGAGAACTCAACCAATAGTGCCGACGCCTCCAGCAACAAA
TTTGTATTTGGCCAGAACATGAGCGAGCGAGTTTTGAGCCCCCCAAAATTAAACGAGGTC
AGTTCAGATGCCAACAGGGAAAATGCAGCTGCCGAGTCAGGGTCTGAGTCCTCGTCCCAG
GAGGCCACCCCTGAGAAAGAGTCCCTGGCTGAGTCGGCAGCCGCCTACACCAAGGCAACA
GCGCGGAAGTGTTTGTTGGAAAAAGTGGAAGTCATCACCGGGGAGGAGGCGGAGAGCAAT
GTGTTACAGATGCAGTGCAAGCTGTTTGTCTTTGACAAGACCTCACAGTCCTGGGTGGAG
AGAGGCCGGGGGCTGCTCAGACTCAATGACATGGCGTCCACCGATGACGGCACACTACAG
TCCCGACTAGTGATGCGGACCCAGGGGAGCCTGCGACTGATCCTCAACACCAAGCTGTGG
GCCCAGATGCAGATCGACAAGGCCAGCGAGAAGAGCATTCGCATCACAGCCATGGACACC
GAGGACCAGGGCGTGAAGGTCTTCCTGATCTCGGCCAGCTCCAAGGACACAGGTCAGTTG
TATGCAGCCCTGCACCACCGCATCCTGGCCCTGCGCAGCCGCGTGGAGCAGGAGCAGGAG
GCCAAGATGCCCGCGCCTGAGCCTGGGGCAGCCCCATCCAACGAGGAGGACGACAGCGAC
GATGACGATGTCCTGGCTCCTTCAGGGGCCACCGCAGCTGGTGCTGGTGACGAAGGGGAC
GGGCAGACGACCGGGAGCACATAG
Enzyme 120 GenBank Gene ID NM_007322.2 Link Image
Enzyme 120 GeneCard ID RANBP3 Link Image
Enzyme 120 GenAtlas ID RANBP3 Link Image
Enzyme 120 HGNC ID HGNC:9850 Link Image
Enzyme 120 Chromosome Location 1
Enzyme 120 Locus 19p13.3
Enzyme 120 SNPs SNPJam Report Link Image
Enzyme 120 General References
  1. Mueller L, Cordes VC, Bischoff FR, Ponstingl H: Human RanBP3, a group of nuclear RanGTP binding proteins. FEBS Lett. 1998 May 15;427(3):330-6. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Englmeier L, Fornerod M, Bischoff FR, Petosa C, Mattaj IW, Kutay U: RanBP3 influences interactions between CRM1 and its nuclear protein export substrates. EMBO Rep. 2001 Oct;2(10):926-32. Epub 2001 Sep 24. [PubMed Link Image]
  7. Lindsay ME, Holaska JM, Welch K, Paschal BM, Macara IG: Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export. J Cell Biol. 2001 Jun 25;153(7):1391-402. [PubMed Link Image]
  8. Nemergut ME, Lindsay ME, Brownawell AM, Macara IG: Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor. J Biol Chem. 2002 May 17;277(20):17385-8. Epub 2002 Apr 3. [PubMed Link Image]
  9. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  10. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  11. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  12. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  13. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  14. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  15. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 120 Metabolite References Not Available
Enzyme 121 [top]
Enzyme 121 ID 14256
Enzyme 121 Name Ral guanine nucleotide dissociation stimulator-like 2
Enzyme 121 Synonyms
  1. RalGDS-like 2
  2. RalGDS-like factor
  3. Ras-associated protein RAB2L
Enzyme 121 Gene Name RGL2
Enzyme 121 Protein Sequence >Ral guanine nucleotide dissociation stimulator-like 2
MLPRPLRLLLDTSPPGGVVLSSFRSRDPEEGGGPGGLVVGGGQEEEEEEEEEAPVSVWDE
EEDGAVFTVTSRQYRPLDPLVPMPPPRSSRRLRAGTLEALVRHLLDTRTSGTDVSFMSAF
LATHRAFTSTPALLGLMADRLEALESHPTDELERTTEVAISVLSTWLASHPEDFGSEAKG
QLDRLESFLLQTGYAAGKGVGGGSADLIRNLRSRVDPQAPDLPKPLALPGDPPADPTDVL
VFLADHLAEQLTLLDAELFLNLIPSQCLGGLWGHRDRPGHSHLCPSVRATVTQFNKVAGA
VVSSVLGATSTGEGPGEVTIRPLRPPQRARLLEKWIRVAEECRLLRNFSSVYAVVSALQS
SPIHRLRAAWGEATRDSLRVFSSLCQIFSEEDNYSQSRELLVQEVKLQSPLEPHSKKAPR
SGSRGGGVVPYLGTFLKDLVMLDAASKDELENGYINFDKRRKEFAVLSELRRLQNECRGY
NLQPDHDIQRWLQGLRPLTEAQSHRVSCEVEPPGSSDPPAPRVLRPTLVISQWTEVLGSV
GVPTPLVSCDRPSTGGDEAPTTPAPLLTRLAQHMKWPSVSSLDSALESSPSLHSPADPSH
LSPPASSPRPSRGHRRSASCGSPLSGGAEEASGGTGYGGEGSGPGASDCRIIRVQMELGE
DGSVYKSILVTSQDKAPSVISRVLKKNNRDSAVASEYELVQLLPGERELTIPASANVFYA
MDGASHDFLLRQRRRSSTATPGVTSGPSASGTPPSEGGGGSFPRIKATGRKIARALF
Enzyme 121 Number of Residues 777
Enzyme 121 Molecular Weight 83548.1
Enzyme 121 Theoretical pI 6.09
Enzyme 121 GO Classification
Function
  • GTPase regulator activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 121 General Function Involved in signal transduction
Enzyme 121 Specific Function Probable guanine nucleotide exchange factor. Putative effector of Ras and/or Rap. Associates with the GTP-bound form of Rap 1A and H-Ras in vitro
Enzyme 121 Pathways Not Available
Enzyme 121 Reactions Not Available
Enzyme 121 Pfam Domain Function
Enzyme 121 Signals
  • None
Enzyme 121 Transmembrane Regions
  • None
Enzyme 121 Essentiality Not Available
Enzyme 121 GenBank ID Protein 4886477 Link Image
Enzyme 121 UniProtKB/Swiss-Prot ID O15211 Link Image
Enzyme 121 UniProtKB/Swiss-Prot Entry Name RGL2_HUMAN Link Image
Enzyme 121 PDB ID 1RLF Link Image
Enzyme 121 PDB File Show
Enzyme 121 3D Structure
Enzyme 121 Cellular Location Not Available
Enzyme 121 Gene Sequence >2334 bp
ATGCTCCCGCGGCCCCTGCGGCTGCTTTTGGACACGAGCCCCCCCGGGGGAGTCGTACTG
AGCAGCTTCCGAAGCCGGGACCCCGAAGAGGGTGGGGGCCCAGGTGGCCTGGTCGTGGGC
GGGGGGCAGGAGGAAGAGGAGGAGGAAGAAGAAGAGGCCCCTGTGTCCGTCTGGGATGAG
GAGGAGGATGGTGCCGTGTTTACCGTCACAAGCCGCCAATATCGACCTCTTGATCCCTTG
GTCCCTATGCCTCCCCCACGTTCCTCCCGACGGCTCCGAGCTGGCACTCTGGAGGCCCTG
GTCAGACACCTACTGGATACCCGGACATCAGGGACTGATGTGAGCTTCATGTCAGCCTTC
CTGGCTACCCACCGGGCCTTCACCTCCACGCCTGCCTTGCTAGGGCTTATGGCTGACAGG
CTGGAAGCCCTTGAATCTCATCCTACCGACGAACTAGAGAGGACAACAGAGGTAGCCATC
TCTGTACTGTCAACCTGGCTGGCCTCTCACCCTGAGGATTTTGGCTCTGAGGCCAAGGGT
CAGCTTGACCGGCTTGAGAGCTTCTTACTTCAGACAGGGTATGCAGCAGGGAAGGGTGTT
GGGGGGGGCAGCGCTGACCTCATCCGCAATCTCCGGTCCCGGGTGGACCCCCAGGCCCCC
GACCTTCCTAAGCCCCTGGCCCTCCCCGGCGATCCCCCTGCTGACCCCACGGATGTCCTG
GTGTTCCTCGCTGACCACTTGGCCGAACAGCTGACCCTGCTAGATGCGGAACTTTTTCTC
AATTTGATCCCCTCTCAGTGCCTGGGAGGCCTGTGGGGTCACAGAGACCGGCCAGGACAT
TCTCACCTCTGCCCATCTGTCCGAGCTACTGTCACACAGTTTAACAAGGTGGCAGGGGCA
GTGGTTAGTTCTGTCCTGGGGGCTACTTCCACTGGAGAGGGACCTGGGGAGGTGACCATA
CGGCCACTCCGTCCCCCACAGAGGGCCCGGCTCCTGGAGAAGTGGATCCGCGTGGCAGAG
GAGTGCCGGCTGCTCCGAAACTTCTCTTCAGTTTATGCCGTGGTGTCAGCCCTGCAGTCC
AGCCCCATCCACAGGCTTCGGGCAGCCTGGGGGGAAGCAACCAGGGACAGCCTCAGAGTC
TTTTCCAGCCTCTGCCAGATTTTCTCCGAGGAGGATAATTATTCCCAGAGTCGGGAGCTG
CTCGTGCAGGAGGTGAAGCTGCAGTCTCCTCTGGAGCCACACTCCAAGAAGGCCCCGAGG
TCTGGCTCCCGGGGTGGGGGTGTGGTCCCATACCTTGGCACCTTCCTGAAGGACCTTGTG
ATGCTGGATGCAGCCTCCAAGGATGAGTTGGAGAATGGATACATCAATTTTGACAAGCGG
AGGAAGGAGTTTGCAGTCCTTTCTGAGTTGCGACGGCTCCAGAATGAATGTCGTGGCTAT
AACCTCCAACCTGACCATGATATCCAGAGGTGGCTACAGGGGCTCCGGCCACTGACAGAG
GCTCAGAGCCATCGTGTATCCTGTGAGGTGGAGCCACCTGGTTCCAGTGACCCTCCTGCC
CCACGGGTGCTTCGGCCAACATTGGTCATCTCGCAGTGGACAGAGGTTTTGGGCTCTGTT
GGGGTCCCTACCCCGCTTGTGTCCTGTGACCGGCCCAGTACTGGGGGAGATGAGGCGCCT
ACAACTCCTGCTCCTCTGCTGACTCGGCTGGCCCAGCACATGAAGTGGCCATCTGTCTCG
TCACTAGACTCTGCCTTGGAAAGCAGTCCATCCCTGCACAGTCCAGCTGACCCCAGCCAC
CTCTCCCCACCAGCCTCCTCCCCTAGGCCTTCTCGAGGTCACCGCCGCTCAGCCTCCTGT
GGCTCCCCGCTGAGTGGGGGTGCAGAAGAGGCCTCCGGGGGGACTGGATATGGGGGAGAG
GGATCTGGGCCAGGGGCCTCTGATTGCCGTATCATCCGAGTCCAGATGGAGTTGGGGGAA
GATGGCAGTGTCTATAAGAGCATTTTGGTGACAAGCCAGGACAAGGCTCCAAGTGTCATC
AGTCGTGTCCTTAAGAAAAACAATCGTGACTCTGCAGTGGCTTCAGAGTATGAGCTGGTA
CAGCTGCTACCAGGGGAGCGAGAGCTGACTATCCCAGCCTCGGCTAATGTATTCTACGCC
ATGGATGGAGCTTCACACGATTTCCTCCTGCGGCAGCGGCGAAGGTCCTCTACTGCTACA
CCTGGCGTCACCAGTGGCCCGTCTGCCTCAGGAACTCCTCCGAGTGAGGGAGGAGGGGGC
TCCTTTCCCAGGATCAAGGCCACAGGGAGGAAGATTGCACGGGCACTGTTCTGA
Enzyme 121 GenBank Gene ID AL050259 Link Image
Enzyme 121 GeneCard ID RGL2 Link Image
Enzyme 121 GenAtlas ID RGL2 Link Image
Enzyme 121 HGNC ID HGNC:9769 Link Image
Enzyme 121 Chromosome Location 6
Enzyme 121 Locus 6p21.3
Enzyme 121 SNPs SNPJam Report Link Image
Enzyme 121 General References
  1. Herberg JA, Beck S, Trowsdale J: TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form a dense cluster at the centromeric end of the MHC. J Mol Biol. 1998 Apr 10;277(4):839-57. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Isomura M, Okui K, Fujiwara T, Shin S, Nakamura Y: Isolation and mapping of RAB2L, a human cDNA that encodes a protein homologous to RalGDS. Cytogenet Cell Genet. 1996;74(4):263-5. [PubMed Link Image]
  6. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
Enzyme 121 Metabolite References Not Available
Enzyme 122 [top]
Enzyme 122 ID 14257
Enzyme 122 Name Ral guanine nucleotide dissociation stimulator-like 3
Enzyme 122 Synonyms
  1. RalGDS-like 3
Enzyme 122 Gene Name RGL3
Enzyme 122 Protein Sequence >Ral guanine nucleotide dissociation stimulator-like 3
MERTAGKELALAPLQDWGEETEDGAVYSVSLRRQRSQRRSPAEGPGGSQAPSPIANTFLH
YRTSKVRVLRAARLERLVGELVFGDREQDPSFMPAFLATYRTFVPTACLLGFLLPPMPPP
PPPGVEIKKTAVQDLSFNKNLRAVVSVLGSWLQDHPQDFRDPPAHSDLGSVRTFLGWAAP
GSAEAQKAEKLLEDFLEEAEREQEEEPPQVWTGPPRVAQTSDPDSSEACAEEEEGLMPQG
PQLLDFSVDEVAEQLTLIDLELFSKVRLYECLGSVWSQRDRPGAAGASPTVRATVAQFNT
VTGCVLGSVLGAPGLAAPQRAQRLEKWIRIAQRCRELRNFSSLRAILSALQSNPIYRLKR
SWGAVSREPLSTFRKLSQIFSDENNHLSSREILFQEEATEGSQEEDNTPGSLPSKPPPGP
VPYLGTFLTDLVMLDTALPDMLEGDLINFEKRRKEWEILARIQQLQRRCQSYTLSPHPPI
LAALHAQNQLTEEQSYRLSRVIEPPAASCPSSPRIRRRISLTKRLSAKLAREKSSSPSGS
PGDPSSPTSSVSPGSPPSSPRSRDAPAGSPPASPGPQGPSTKLPLSLDLPSPRPFALPLG
SPRIPLPAQQSSEARVIRVSIDNDHGNLYRSILLTSQDKAPSVVRRALQKHNVPQPWACD
YQLFQVLPGDRVLLIPDNANVFYAMSPVAPRDFMLRRKEGTRNTLSVSPS
Enzyme 122 Number of Residues 710
Enzyme 122 Molecular Weight 78078.5
Enzyme 122 Theoretical pI 7.76
Enzyme 122 GO Classification
Function
  • GTPase regulator activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 122 General Function Involved in signal transduction
Enzyme 122 Specific Function Guanine nucleotide exchange factor (GEF) for Ral-A. Potential effector of GTPase HRas and Ras-related protein M-Ras. Negatively regulates Elk-1-dependent gene induction downstream of HRas and MEKK1
Enzyme 122 Pathways Not Available
Enzyme 122 Reactions Not Available
Enzyme 122 Pfam Domain Function
Enzyme 122 Signals
  • None
Enzyme 122 Transmembrane Regions
  • None
Enzyme 122 Essentiality Not Available
Enzyme 122 GenBank ID Protein 239582763 Link Image
Enzyme 122 UniProtKB/Swiss-Prot ID Q3MIN7 Link Image
Enzyme 122 UniProtKB/Swiss-Prot Entry Name RGL3_HUMAN Link Image
Enzyme 122 PDB ID Not Available
Enzyme 122 Cellular Location Not Available
Enzyme 122 Gene Sequence >2133 bp
ATGGAGCGCACAGCAGGCAAAGAGCTGGCCCTGGCACCGCTGCAGGACTGGGGTGAAGAG
ACCGAGGACGGCGCGGTGTACAGTGTCTCCCTGCGGCGGCAGCGCAGTCAGCGCAGGAGC
CCGGCGGAGGGCCCCGGGGGCAGCCAGGCTCCCAGCCCCATTGCCAATACCTTCCTCCAC
TATCGAACCAGCAAGGTGAGGGTGCTGAGGGCAGCGCGCCTGGAGCGGCTGGTGGGAGAG
TTGGTGTTTGGAGACCGTGAGCAGGACCCCAGCTTCATGCCCGCCTTCCTGGCCACCTAC
CGGACCTTTGTACCCACTGCCTGCCTGCTGGGCTTTCTGCTGCCACCAATGCCACCGCCC
CCACCTCCCGGGGTAGAGATCAAGAAGACAGCGGTACAAGATCTGAGCTTCAACAAGAAC
CTGAGGGCTGTGGTGTCAGTGCTGGGCTCCTGGCTGCAGGACCACCCTCAGGATTTCCGA
GACCCCCCTGCCCATTCGGACCTGGGCAGTGTCCGAACCTTTCTGGGCTGGGCGGCCCCA
GGGAGTGCTGAGGCTCAAAAAGCAGAGAAGCTTCTGGAAGATTTTTTGGAGGAGGCTGAG
CGAGAGCAGGAAGAGGAGCCGCCTCAGGTGTGGACAGGACCTCCCAGAGTTGCCCAAACT
TCTGACCCAGACTCTTCAGAGGCCTGCGCGGAGGAAGAGGAAGGGCTCATGCCTCAAGGT
CCCCAGCTCCTGGACTTCAGCGTGGACGAGGTGGCCGAGCAGCTGACCCTCATAGACTTG
GAGCTCTTCTCCAAGGTGAGGCTCTACGAGTGCTTGGGCTCCGTGTGGTCGCAGAGGGAC
CGGCCGGGGGCTGCAGGCGCCTCCCCCACTGTGCGCGCCACCGTGGCCCAGTTCAACACC
GTGACCGGCTGTGTGCTGGGTTCCGTGCTCGGAGCACCGGGCTTGGCCGCCCCGCAGAGG
GCGCAGCGGCTGGAGAAGTGGATCCGCATCGCCCAGCGCTGCCGAGAACTGCGGAACTTC
TCCTCCTTGCGCGCCATCCTGTCCGCCCTGCAATCTAACCCCATCTACCGGCTCAAGCGC
AGCTGGGGGGCAGTGAGCCGGGAACCGCTATCTACTTTCAGGAAACTTTCGCAGATTTTC
TCCGATGAGAACAACCACCTCAGCAGCAGAGAGATTCTTTTCCAGGAGGAGGCCACTGAG
GGATCCCAAGAAGAGGACAACACCCCAGGCAGCCTGCCCTCAAAACCACCCCCAGGCCCT
GTCCCCTACCTTGGCACCTTCCTTACGGACCTGGTTATGCTGGACACAGCCCTGCCGGAT
ATGTTGGAGGGGGATCTCATTAACTTTGAGAAGAGGAGGAAGGAGTGGGAGATCCTGGCC
CGCATCCAGCAGCTGCAGAGGCGCTGTCAGAGCTACACCCTGAGCCCCCACCCGCCCATC
CTGGCTGCCCTGCATGCCCAGAACCAGCTCACCGAGGAGCAGAGCTACCGGCTCTCCCGG
GTCATTGAGCCACCAGCTGCCTCCTGCCCCAGCTCCCCACGCATCCGACGGCGGATCAGC
CTCACCAAGCGTCTCAGTGCGAAGCTTGCCCGAGAGAAAAGCTCATCACCTAGTGGGAGT
CCCGGGGACCCCTCATCCCCCACCTCCAGTGTGTCCCCAGGGTCACCCCCCTCAAGTCCT
AGAAGCAGAGATGCTCCTGCTGGCAGTCCCCCGGCCTCTCCAGGGCCCCAGGGCCCCAGC
ACCAAGCTGCCCCTGAGCCTGGACCTGCCCAGCCCCCGGCCCTTCGCTTTGCCTCTGGGC
AGCCCTCGAATCCCCCTCCCGGCGCAGCAGAGCTCGGAGGCCCGTGTCATCCGCGTCAGC
ATCGACAATGACCACGGGAACCTGTATCGAAGCATCTTGCTGACCAGTCAGGACAAAGCC
CCCAGCGTGGTCCGGCGAGCCTTGCAGAAGCACAATGTGCCCCAGCCCTGGGCCTGTGAC
TATCAGCTCTTTCAAGTCCTTCCTGGGGACCGGGTGCTCCTGATTCCTGACAATGCCAAC
GTCTTCTATGCCATGAGTCCAGTCGCCCCCAGAGACTTCATGCTGCGGCGGAAAGAGGGG
ACCCGGAACACTCTGTCTGTCTCCCCAAGCTGA
Enzyme 122 GenBank Gene ID NM_001035223.2 Link Image
Enzyme 122 GeneCard ID RGL3 Link Image
Enzyme 122 GenAtlas ID RGL3 Link Image
Enzyme 122 HGNC ID HGNC:30282 Link Image
Enzyme 122 Chromosome Location 1
Enzyme 122 Locus 19p13.2
Enzyme 122 SNPs SNPJam Report Link Image
Enzyme 122 General References
  1. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 122 Metabolite References Not Available
Enzyme 123 [top]
Enzyme 123 ID 14268
Enzyme 123 Name Synembryn-A
Enzyme 123 Synonyms
  1. Protein Ric-8A
Enzyme 123 Gene Name RIC8A
Enzyme 123 Protein Sequence >Synembryn-A
MEPRAVAEAVETGEEDVIMEALRSYNQEHSQSFTFDDAQQEDRKRLAELLVSVLEQGLPP
SHRVIWLQSVRILSRDRNCLDPFTSRQSLQALACYADISVSEGSVPESADMDVVLESLKC
LCNLVLSSPVAQMLAAEARLVVKLTERVGLYRERSFPHDVQFFDLRLLFLLTALRTDVRQ
QLFQELKGVRLLTDTLELTLGVTPEGNPPPTLLPSQETERAMEILKVLFNITLDSIKGEV
DEEDAALYRHLGTLLRHCVMIATAGDRTEEFHGHAVNLLGNLPLKCLDVLLTLEPHGDST
EFMGVNMDVIRALLIFLEKRLHKTHRLKESVAPVLSVLTECARMHRPARKFLKAQVLPPL
RDVRTRPEVGEMLRNKLVRLMTHLDTDVKRVAAEFLFVLCSESVPRFIKYTGYGNAAGLL
AARGLMAGGRPEGQYSEDEDTDTDEYKEAKASINPVTGRVEEKPPNPMEGMTEEQKEHEA
MKLVTMFDKLSRNRVIQPMGMSPRGHLTSLQDAMCETMEQQLSSDPDSDPD
Enzyme 123 Number of Residues 531
Enzyme 123 Molecular Weight 59708.9
Enzyme 123 Theoretical pI 4.98
Enzyme 123 GO Classification Not Available
Enzyme 123 General Function Involved in binding
Enzyme 123 Specific Function Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein, possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex. Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation
Enzyme 123 Pathways Not Available
Enzyme 123 Reactions Not Available
Enzyme 123 Pfam Domain Function
Enzyme 123 Signals
  • None
Enzyme 123 Transmembrane Regions
  • None
Enzyme 123 Essentiality Not Available
Enzyme 123 GenBank ID Protein 9368538 Link Image
Enzyme 123 UniProtKB/Swiss-Prot ID Q9NPQ8 Link Image
Enzyme 123 UniProtKB/Swiss-Prot Entry Name RIC8A_HUMAN Link Image
Enzyme 123 PDB ID Not Available
Enzyme 123 Cellular Location Not Available
Enzyme 123 Gene Sequence >1596 bp
ATGGAGCCCCGGGCGGTTGCAGAAGCCGTGGAGACGGGTGAGGAGGATGTGATTATGGAA
GCTCTGCGGTCATACAACCAGGAGCACTCCCAGAGCTTCACGTTTGATGATGCCCAACAG
GAGGACCGGAAGAGACTGGCGGAGCTGCTGGTCTCCGTCCTGGAACAGGGCTTGCCACCC
TCCCACCGTGTCATCTGGCTGCAGAGTGTCCGAATCCTGTCCCGGGACCGCAACTGCCTG
GACCCGTTCACCAGCCGCCAGAGCCTGCAGGCACTAGCCTGCTATGCTGACATCTCTGTC
TCTGAGGGGTCCGTCCCAGAGTCCGCAGACATGGATGTTGTACTGGAGTCCCTCAAGTGC
CTGTGCAACCTCGTGCTCAGCAGCCCTGTGGCACAGATGCTGGCAGCAGAGGCCCGCCTA
GTGGTGAAGCTCACAGAGCGTGTGGGGCTGTACCGTGAGAGGAGCTTCCCCCACGATGTC
CAGTTCTTTGACTTGCGGCTCCTCTTCCTGCTAACGGCACTCCGCACCGATGTGCGCCAG
CAGCTGTTTCAGGAGCTGAAAGGAGTGCGCCTGCTAACTGACACACTGGAGCTGACGCTG
GGGGTGACTCCTGAAGGGAACCCCCCACCCACGCTCCTTCCTTCCCAAGAGACTGAGCGG
GCCATGGAGATCCTCAAAGTGCTCTTCAACATCACCCTGGACTCCATCAAGGGGGAGGTG
GACGAGGAAGACGCTGCCCTTTACCGACACCTGGGGACCCTTCTCCGGCACTGTGTGATG
ATCGCTACTGCTGGAGACCGCACAGAGGAGTTCCACGGCCACGCAGTGAACCTCCTGGGG
AACTTGCCCCTCAAGTGTCTGGATGTTCTCCTCACCCTGGAGCCACATGGAGACTCCACG
GAGTTCATGGGAGTGAATATGGATGTGATTCGTGCCCTCCTCATCTTCCTAGAGAAGCGT
TTGCACAAGACACACAGGCTGAAGGAGAGTGTAGCTCCCGTGCTGAGCGTGCTGACTGAA
TGTGCCCGGATGCACCGCCCAGCCAGGAAGTTCCTGAAGGCCCAGGTGCTGCCCCCTCTG
CGGGATGTGAGGACACGGCCTGAGGTTGGGGAGATGCTGCGGAACAAGCTTGTCCGCCTC
ATGACACACCTGGACACAGATGTGAAGAGGGTGGCTGCCGAGTTCTTGTTTGTCCTGTGC
TCTGAGAGTGTGCCCCGATTCATCAAGTACACAGGCTATGGGAATGCTGCTGGCCTTCTG
GCTGCCAGGGGCCTCATGGCAGGAGGCCGGCCCGAGGGCCAGTACTCAGAGGATGAGGAC
ACAGACACAGATGAGTACAAGGAAGCCAAAGCCAGCATAAACCCTGTGACCGGGAGGGTG
GAGGAGAAGCCGCCTAACCCTATGGAGGGCATGACAGAGGAGCAGAAGGAGCACGAGGCC
ATGAAGCTGGTGACCATGTTTGACAAGCTCTCCAGGAACAGAGTCATCCAGCCAATGGGG
ATGAGTCCCCGGGGTCATCTTACGTCCCTGCAGGATGCCATGTGCGAGACTATGGAGCAG
CAGCTCTCCTCGGACCCTGACTCGGACCCTGACTGA
Enzyme 123 GenBank Gene ID AL390088 Link Image
Enzyme 123 GeneCard ID RIC8A Link Image
Enzyme 123 GenAtlas ID RIC8A Link Image
Enzyme 123 HGNC ID HGNC:29550 Link Image
Enzyme 123 Chromosome Location 1
Enzyme 123 Locus 11p15.5
Enzyme 123 SNPs SNPJam Report Link Image
Enzyme 123 General References
  1. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Nishimura A, Okamoto M, Sugawara Y, Mizuno N, Yamauchi J, Itoh H: Ric-8A potentiates Gq-mediated signal transduction by acting downstream of G protein-coupled receptor in intact cells. Genes Cells. 2006 May;11(5):487-98. [PubMed Link Image]
  7. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  8. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  9. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  10. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed Link Image]
  11. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  12. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 123 Metabolite References Not Available
Enzyme 124 [top]
Enzyme 124 ID 14270
Enzyme 124 Name Ras and Rab interactor 1
Enzyme 124 Synonyms
  1. Ras inhibitor JC99
  2. Ras interaction/interference protein 1
Enzyme 124 Gene Name RIN1
Enzyme 124 Protein Sequence >Ras and Rab interactor 1
MESPGESGAGSPGAPSPSSFTTGHLAREKPAQDPLYDVPNASGGQAGGPQRPGRVVSLRE
RLLLTRPVWLQLQANAAAALHMLRTEPPGTFLVRKSNTRQCQALCMRLPEASGPSFVSSH
YILESPGGVSLEGSELMFPDLVQLICAYCHTRDILLLPLQLPRAIHHAATHKELEAISHL
GIEFWSSSLNIKAQRGPAGGPVLPQLKARSPQELDQGTGAALCFFNPLFPGDLGPTKREK
FKRSFKVRVSTETSSPLSPPAVPPPPVPVLPGAVPSQTERLPPCQLLRRESSVGYRVPAG
SGPSLPPMPSLQEVDCGSPSSSEEEGVPGSRGSPATSPHLGRRRPLLRSMSAAFCSLLAP
ERQVGRAAAALMQDRHTAAGQLVQDLLTQVRAGPEPQELQGIRQALSRARAMLSAELGPE
KLLSPKRLEHVLEKSLHCSVLKPLRPILAARLRRRLAADGSLGRLAEGLRLARAQGPGAF
GSHLSLPSPVELEQVRQKLLQLLRTYSPSAQVKRLLQACKLLYMALRTQEGEGAGADEFL
PLLSLVLAHCDLPELLLEAEYMSELLEPSLLTGEGGYYLTSLSASLALLSGLGQAHTLPL
SPVQELRRSLSLWEQRRLPATHCFQHLLRVAYQDPSSGCTSKTLAVPPEASIATLNQLCA
TKFRVTQPNTFGLFLYKEQGYHRLPPGALAHRLPTTGYLVYRRAEWPETQGAVTEEEGSG
QSEARSRGEEQGCQGDGDAGVKASPRDIREQSETTAEGGQGQAQEGPAQPGEPEAEGSRA
AEE
Enzyme 124 Number of Residues 783
Enzyme 124 Molecular Weight 84098.0
Enzyme 124 Theoretical pI 8.08
Enzyme 124 GO Classification
Function
  • binding
  • protein binding
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 124 General Function Involved in signal transduction
Enzyme 124 Specific Function Ras effector protein, which may serve as an inhibitory modulator of neuronal plasticity in aversive memory formation. Can affect Ras signaling at different levels. First, by competing with RAF1 protein for binding to activated Ras. Second, by enhancing signaling from ABL1 and ABL2, which regulate cytoskeletal remodeling. Third, by activating RAB5A, possibly by functioning as a guanine nucleotide exchange factor (GEF) for RAB5A, by exchanging bound GDP for free GTP, and facilitating Ras-activated receptor endocytosis
Enzyme 124 Pathways Not Available
Enzyme 124 Reactions Not Available
Enzyme 124 Pfam Domain Function
Enzyme 124 Signals
  • None
Enzyme 124 Transmembrane Regions
  • None
Enzyme 124 Essentiality Not Available
Enzyme 124 GenBank ID Protein 15680148 Link Image
Enzyme 124 UniProtKB/Swiss-Prot ID Q13671 Link Image
Enzyme 124 UniProtKB/Swiss-Prot Entry Name RIN1_HUMAN Link Image
Enzyme 124 PDB ID Not Available
Enzyme 124 Cellular Location Not Available
Enzyme 124 Gene Sequence >2352 bp
ATGGAAAGCCCTGGAGAGTCAGGCGCGGGCTCTCCTGGAGCCCCCAGCCCGTCCAGCTTC
ACTACTGGGCACCTGGCGAGAGAAAAGCCAGCCCAGGACCCACTGTATGACGTGCCCAAT
GCCAGCGGCGGGCAGGCAGGCGGGCCGCAGCGGCCGGGGCGCGTTGTGAGCCTGCGGGAG
CGCCTGCTGCTCACCCGGCCCGTGTGGCTGCAGCTGCAAGCCAACGCAGCGGCCGCACTG
CACATGCTGAGGACCGAGCCCCCGGGGACGTTCCTCGTGCGGAAATCTAACACCCGCCAG
TGCCAGGCCCTGTGCATGCGGTTGCCTGAAGCCAGTGGCCCCTCCTTCGTCTCCAGCCAC
TACATCCTGGAGAGCCCTGGCGGCGTCTCCTTGGAGGGCTCGGAGCTCATGTTCCCAGAC
CTAGTCCAGCTCATCTGTGCCTACTGCCACACCCGGGACATCCTTCTCCTCCCGCTGCAG
CTCCCCAGAGCCATCCACCACGCAGCCACTCACAAAGAGCTGGAGGCCATCTCCCATCTG
GGCATTGAGTTCTGGAGCTCCTCCCTCAACATCAAGGCTCAGCGGGGCCCGGCTGGAGGC
CCAGTGTTGCCCCAGCTGAAGGCCCGGTCCCCTCAAGAGCTGGACCAGGGCACCGGAGCC
GCCTTGTGCTTCTTCAACCCCCTGTTCCCGGGGGACCTAGGGCCCACCAAGCGGGAGAAA
TTCAAGAGAAGCTTCAAAGTGCGCGTGTCCACAGAGACCTCCAGCCCCCTGTCTCCACCT
GCCGTGCCACCTCCCCCCGTCCCCGTGCTGCCAGGGGCAGTCCCCAGCCAGACAGAGCGG
CTGCCCCCTTGCCAGCTGCTACGGAGGGAGAGCTCAGTGGGGTACCGCGTGCCAGCAGGC
AGTGGCCCTAGCCTTCCGCCTATGCCCTCCCTCCAAGAGGTGGACTGCGGCTCCCCCAGC
AGCTCCGAGGAGGAGGGGGTGCCAGGGTCCCGGGGGAGCCCAGCGACCTCACCCCACCTG
GGCCGCCGACGACCTCTGCTTCGGTCCATGAGCGCCGCCTTCTGCTCCCTACTGGCACCG
GAGCGGCAGGTGGGCCGGGCTGCGGCAGCACTGATGCAGGACCGACACACAGCCGCGGGC
CAGCTGGTGCAGGACCTACTGACCCAGGTGCGGGCTGGGCCCGAGCCCCAGGAGCTGCAG
GGCATCCGTCAGGCGCTGAGCCGGGCCCGGGCCATGCTGAGTGCGGAGCTGGGCCCTGAG
AAGCTGCTGTCGCCTAAGAGGCTGGAACATGTCCTGGAGAAGTCATTGCATTGCTCTGTG
CTCAAGCCTCTCCGGCCCATCCTGGCAGCCCGCCTGCGGCGCCGGCTTGCCGCAGACGGC
TCCCTGGGCCGCCTAGCTGAGGGCCTCCGCCTGGCCCGGGCCCAGGGCCCCGGAGCCTTC
GGGTCCCACCTGAGCCTGCCCTCCCCAGTAGAGTTGGAGCAAGTGCGCCAGAAGCTGCTG
CAGCTGCTCCGCACCTACTCACCCAGCGCCCAGGTCAAGCGGCTCCTGCAGGCCTGCAAG
CTGCTCTACATGGCCCTGAGGACCCAGGAAGGGGAGGGCGCGGGTGCCGACGAGTTCCTG
CCTCTGCTGAGCCTCGTCTTGGCCCACTGTGACCTTCCTGAGCTGCTGCTGGAGGCCGAG
TACATGTCGGAGCTGCTGGAGCCCAGCCTGCTTACTGGAGAGGGTGGCTACTACCTGACC
AGCCTCTCTGCCAGCCTGGCCCTGCTGAGTGGCCTGGGTCAGGCCCACACCCTCCCACTG
AGCCCCGTGCAGGAGCTACGGCGCTCCCTCAGCCTCTGGGAGCAGCGCCGCCTGCCTGCC
ACCCACTGCTTCCAGCACCTCCTCCGAGTAGCCTATCAGGATCCCAGCAGTGGCTGCACC
TCCAAGACCCTGGCCGTGCCCCCAGAGGCCTCGATTGCCACCCTGAACCAGCTCTGTGCC
ACCAAGTTCCGAGTGACCCAGCCCAACACTTTTGGCCTCTTCCTGTACAAGGAGCAGGGC
TACCACCGCCTGCCCCCTGGGGCCCTGGCCCACAGGCTGCCCACCACTGGCTACCTCGTC
TACCGCCGGGCAGAGTGGCCTGAGACCCAGGGGGCTGTGACAGAGGAGGAGGGCAGTGGG
CAGTCAGAGGCAAGAAGCAGAGGGGAGGAGCAAGGGTGCCAGGGAGATGGGGATGCTGGG
GTCAAAGCCAGCCCCAGGGACATTCGGGAACAGTCTGAGACAACTGCTGAAGGGGGCCAG
GGTCAAGCCCAGGAAGGCCCTGCTCAGCCAGGGGAACCAGAGGCAGAGGGAAGCCGGGCA
GCAGAGGAGTAG
Enzyme 124 GenBank Gene ID BC014417 Link Image
Enzyme 124 GeneCard ID RIN1 Link Image
Enzyme 124 GenAtlas ID RIN1 Link Image
Enzyme 124 HGNC ID HGNC:18749 Link Image
Enzyme 124 Chromosome Location 1
Enzyme 124 Locus 11q13.2
Enzyme 124 SNPs SNPJam Report Link Image
Enzyme 124 General References
  1. Colicelli J, Nicolette C, Birchmeier C, Rodgers L, Riggs M, Wigler M: Expression of three mammalian cDNAs that interfere with RAS function in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2913-7. [PubMed Link Image]
  2. Han L, Colicelli J: A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1. Mol Cell Biol. 1995 Mar;15(3):1318-23. [PubMed Link Image]
  3. Han L, Wong D, Dhaka A, Afar D, White M, Xie W, Herschman H, Witte O, Colicelli J: Protein binding and signaling properties of RIN1 suggest a unique effector function. Proc Natl Acad Sci U S A. 1997 May 13;94(10):4954-9. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Afar DE, Han L, McLaughlin J, Wong S, Dhaka A, Parmar K, Rosenberg N, Witte ON, Colicelli J: Regulation of the oncogenic activity of BCR-ABL by a tightly bound substrate protein RIN1. Immunity. 1997 Jun;6(6):773-82. [PubMed Link Image]
  6. Tall GG, Barbieri MA, Stahl PD, Horazdovsky BF: Ras-activated endocytosis is mediated by the Rab5 guanine nucleotide exchange activity of RIN1. Dev Cell. 2001 Jul;1(1):73-82. [PubMed Link Image]
  7. Wang Y, Waldron RT, Dhaka A, Patel A, Riley MM, Rozengurt E, Colicelli J: The RAS effector RIN1 directly competes with RAF and is regulated by 14-3-3 proteins. Mol Cell Biol. 2002 Feb;22(3):916-26. [PubMed Link Image]
  8. Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM: Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics. 2005 Sep;4(9):1240-50. Epub 2005 Jun 11. [PubMed Link Image]
  9. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed Link Image]
  10. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  11. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  12. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  13. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
Enzyme 124 Metabolite References Not Available
Enzyme 125 [top]
Enzyme 125 ID 14271
Enzyme 125 Name Ras and Rab interactor 2
Enzyme 125 Synonyms
  1. Ras association domain family 4
  2. Ras inhibitor JC265
  3. Ras interaction/interference protein 2
Enzyme 125 Gene Name RIN2
Enzyme 125 Protein Sequence >Ras and Rab interactor 2
MTAWTMGARGLDKRGSFFKLIDTIASEIGELKQEMVRTDVNLENGLEPAETHSMVRHKDG
GYSEEEDVKTCARDSGYDSLSNRLSILDRLLHTHPIWLQLSLSEEEAAEVLQAQPPGIFL
VHKSTKMQKKVLSLRLPCEFGAPLKEFAIKESTYTFSLEGSGISFADLFRLIAFYCISRD
VLPFTLKLPYAISTAKSEAQLEELAQMGLNFWSSPADSKPPNLPPPHRPLSSDGVCPASL
RQLCLINGVHSIKTRTPSELECSQTNGALCFINPLFLKVHSQDLSGGLKRPSTRTPNANG
TERTRSPPPRPPPPAINSLHTSPRLARTETQTSMPETVNHNKHGNVALPGTKPTPIPPPR
LKKQASFLEAEGGAKTLSGGRPGAGPELELGTAGSPGGAPPEAAPGDCTRAPPPSSESRP
PCHGGRQRLSDMSISTSSSDSLEFDRSMPLFGYEADTNSSLEDYEGESDQETMAPPIKSK
KKRSSSFVLPKLVKSQLQKVSGVFSSFMTPEKRMVRRIAELSRDKCTYFGCLVQDYVSFL
QENKECHVSSTDMLQTIRQFMTQVKNYLSQSSELDPPIESLIPEDQIDVVLEKAMHKCIL
KPLKGHVEAMLKDFHMADGSWKQLKENLQLVRQRNPQELGVFAPTPDFVDVEKIKVKFMT
MQKMYSPEKKVMLLLRVCKLIYTVMENNSGRMYGADDFLPVLTYVIAQCDMLELDTEIEY
MMELLDPSLLHGEGGYYLTSAYGALSLIKNFQEEQAARLLSSETRDTLRQWHKRRTTNRT
IPSVDDFQNYLRVAFQEVNSGCTGKTLLVRPYITTEDVCQICAEKFKVGDPEEYSLFLFV
DETWQQLAEDTYPQKIKAELHSRPQPHIFHFVYKRIKNDPYGIIFQNGEEDLTTS
Enzyme 125 Number of Residues 895
Enzyme 125 Molecular Weight 100162.3
Enzyme 125 Theoretical pI 6.55
Enzyme 125 GO Classification
Function
  • binding
  • protein binding
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 125 General Function Involved in signal transduction
Enzyme 125 Specific Function Ras effector protein. May function as an upstream activator and/or downstream effector for RAB5B in endocytic pathway. May function as a guanine nucleotide exchange (GEF) of RAB5B, required for activating the RAB5 proteins by exchanging bound GDP for free GTP
Enzyme 125 Pathways Not Available
Enzyme 125 Reactions Not Available
Enzyme 125 Pfam Domain Function
Enzyme 125 Signals
  • None
Enzyme 125 Transmembrane Regions
  • None
Enzyme 125 Essentiality Not Available
Enzyme 125 GenBank ID Protein 18413654 Link Image
Enzyme 125 UniProtKB/Swiss-Prot ID Q8WYP3 Link Image
Enzyme 125 UniProtKB/Swiss-Prot Entry Name RIN2_HUMAN Link Image
Enzyme 125 PDB ID Not Available
Enzyme 125 Cellular Location Not Available
Enzyme 125 Gene Sequence >2688 bp
ATGACAGCTTGGACCATGGGCGCCCGCGGTCTGGACAAGCGAGGAAGTTTCTTTAAGCTC
ATTGACACAATTGCCTCGGAGATCGGAGAACTGAAACAGGAGATGGTGCGGACAGATGTC
AACCTGGAAAATGGCCTGGAACCCGCTGAAACCCACAGCATGGTAAGACACAAGGATGGT
GGCTATTCCGAGGAAGAGGACGTGAAGACCTGTGCCCGGGACTCAGGCTATGACAGCCTC
TCCAACAGGCTCAGCATCTTGGACCGGCTCCTCCACACCCACCCCATATGGCTGCAGCTG
AGTCTGAGTGAGGAGGAGGCAGCAGAGGTCCTGCAGGCCCAGCCTCCGGGGATCTTCCTG
GTTCATAAATCTACCAAGATGCAGAAGAAAGTCCTCTCCCTCCGCCTGCCCTGTGAATTT
GGGGCCCCACTCAAGGAATTTGCCATAAAGGAAAGCACATACACCTTTTCCCTGGAAGGA
TCCGGAATCAGTTTCGCAGATTTATTCCGGCTCATTGCTTTCTACTGCATCAGCAGGGAT
GTTCTACCATTTACCTTGAAGTTGCCTTATGCCATTTCAACAGCCAAGTCGGAGGCTCAG
CTTGAAGAACTGGCCCAGATGGGACTAAATTTCTGGAGCTCCCCAGCTGACAGCAAACCC
CCGAACCTTCCACCTCCCCATAGGCCTCTTTCCTCCGACGGTGTCTGTCCTGCCTCCCTG
CGTCAGCTCTGCCTTATAAATGGAGTGCATTCTATCAAAACCAGGACGCCTTCAGAGCTG
GAGTGCAGCCAGACCAACGGGGCTCTGTGCTTTATTAATCCCCTTTTCTTGAAAGTGCAC
AGCCAGGACCTCAGTGGAGGCCTGAAACGGCCGAGCACAAGGACTCCCAACGCGAATGGC
ACGGAGCGGACTCGGTCCCCCCCACCCAGGCCCCCGCCACCCGCTATTAATAGTCTCCAC
ACAAGCCCTCGGCTGGCCAGGACTGAAACCCAGACGAGCATGCCAGAAACAGTCAACCAT
AACAAACATGGGAACGTAGCTCTGCCTGGAACGAAACCAACTCCCATCCCTCCACCCCGG
CTGAAGAAGCAGGCTTCTTTTCTGGAAGCAGAGGGCGGTGCAAAGACCTTGAGCGGCGGC
CGGCCGGGCGCAGGCCCGGAGCTGGAGCTGGGCACAGCTGGCAGCCCAGGTGGGGCCCCG
CCTGAGGCCGCCCCGGGGGATTGCACAAGGGCCCCGCCGCCCAGCTCTGAATCACGGCCC
CCGTGCCATGGAGGCCGGCAGCGGCTGAGCGACATGAGCATTTCTACTTCCTCCTCCGAC
TCGCTGGAGTTCGACCGGAGCATGCCTCTGTTTGGCTACGAGGCGGACACCAACAGCAGC
CTGGAGGACTACGAGGGGGAAAGTGACCAAGAGACCATGGCGCCCCCCATCAAGTCCAAA
AAGAAAAGGAGCAGCTCCTTCGTGCTGCCCAAGCTCGTCAAGTCCCAGCTGCAGAAGGTG
AGCGGGGTGTTCAGCTCCTTCATGACCCCGGAGAAGCGGATGGTCCGCAGGATCGCCGAG
CTTTCCCGGGACAAATGCACCTACTTCGGGTGCTTAGTGCAGGACTACGTGAGCTTCCTG
CAGGAGAACAAGGAGTGCCACGTGTCCAGCACCGACATGCTGCAGACCATCCGGCAGTTC
ATGACCCAGGTCAAGAACTATTTGTCTCAGAGCTCGGAGCTGGACCCCCCCATCGAGTCG
CTGATCCCTGAAGACCAAATAGATGTGGTGCTGGAAAAAGCCATGCACAAGTGCATCTTG
AAGCCCCTCAAGGGGCACGTGGAGGCCATGCTGAAGGACTTTCACATGGCCGATGGCTCA
TGGAAGCAACTCAAGGAGAACCTGCAGCTTGTGCGGCAGAGGAATCCGCAGGAGCTGGGG
GTCTTCGCCCCGACCCCTGATTTTGTGGATGTGGAGAAAATCAAAGTCAAGTTCATGACC
ATGCAGAAGATGTATTCGCCGGAAAAGAAGGTCATGCTGCTGCTGCGGGTCTGCAAGCTC
ATTTACACGGTCATGGAGAACAACTCAGGGAGGATGTATGGCGCTGATGACTTCTTGCCA
GTCCTGACCTATGTCATAGCCCAGTGTGACATGCTTGAATTGGACACTGAAATCGAGTAC
ATGATGGAGCTCCTAGACCCATCGCTGTTACATGGAGAAGGAGGCTATTACTTGACAAGC
GCATATGGAGCACTTTCTCTGATAAAGAATTTCCAAGAAGAACAAGCAGCGCGACTGCTC
AGCTCAGAAACCAGAGACACCCTGAGGCAGTGGCACAAACGGAGAACCACCAACCGGACC
ATCCCCTCTGTGGACGACTTCCAGAATTACCTCCGAGTTGCATTTCAGGAGGTCAACAGT
GGTTGCACAGGAAAGACCCTCCTTGTGAGACCTTACATCACCACTGAGGATGTGTGTCAG
ATCTGCGCTGAGAAGTTCAAGGTGGGGGACCCTGAGGAGTACAGCCTCTTTCTCTTCGTT
GACGAGACATGGCAGCAGCTGGCAGAGGACACTTACCCTCAAAAAATCAAGGCGGAGCTG
CACAGCCGACCACAGCCCCACATCTTCCACTTTGTCTACAAACGCATCAAGAACGATCCT
TATGGCATCATTTTCCAGAACGGGGAAGAAGACCTCACCACCTCCTAG
Enzyme 125 GenBank Gene ID AB060339 Link Image
Enzyme 125 GeneCard ID RIN2 Link Image
Enzyme 125 GenAtlas ID RIN2 Link Image
Enzyme 125 HGNC ID HGNC:18750 Link Image
Enzyme 125 Chromosome Location 2
Enzyme 125 Locus 20p11.22
Enzyme 125 SNPs SNPJam Report Link Image
Enzyme 125 General References
  1. Saito K, Murai J, Kajiho H, Kontani K, Kurosu H, Katada T: A novel binding protein composed of homophilic tetramer exhibits unique properties for the small GTPase Rab5. J Biol Chem. 2002 Feb 1;277(5):3412-8. Epub 2001 Dec 3. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  5. Colicelli J, Nicolette C, Birchmeier C, Rodgers L, Riggs M, Wigler M: Expression of three mammalian cDNAs that interfere with RAS function in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2913-7. [PubMed Link Image]
  6. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed Link Image]
  7. Basel-Vanagaite L, Sarig O, Hershkovitz D, Fuchs-Telem D, Rapaport D, Gat A, Isman G, Shirazi I, Shohat M, Enk CD, Birk E, Kohlhase J, Matysiak-Scholze U, Maya I, Knopf C, Peffekoven A, Hennies HC, Bergman R, Horowitz M, Ishida-Yamamoto A, Sprecher E: RIN2 deficiency results in macrocephaly, alopecia, cutis laxa, and scoliosis: MACS syndrome. Am J Hum Genet. 2009 Aug;85(2):254-63. Epub 2009 Jul 23. [PubMed Link Image]
Enzyme 125 Metabolite References Not Available
Enzyme 126 [top]
Enzyme 126 ID 14272
Enzyme 126 Name Ras and Rab interactor 3
Enzyme 126 Synonyms
  1. Ras interaction/interference protein 3
Enzyme 126 Gene Name RIN3
Enzyme 126 Protein Sequence >Ras and Rab interactor 3
MIRHAGAPARGDPTGPVPVVGKGEEEEEEDGMRLCLPANPKNCLPHRRGISILEKLIKTC
PVWLQLSLGQAEVARILHRVVAGMFLVRRDSSSKQLVLCVHFPSLNESSAEVLEYTIKEE
KSILYLEGSALVFEDIFRLIAFYCVSRDLLPFTLRLPQAILEASSFTDLETIANLGLGFW
DSSLNPPQERGKPAEPPRDRAPGFPLVSSLRPTAHDANCACEIELSVGNDRLWFVNPIFI
EDCSSALPTDQPPLGNCPARPLPPTSDATSPTSRWAPRRPPPPPPVLPLQPCSPAQPPVL
PALAPAPACPLPTSPPVPAPHVTPHAPGPPDHPNQPPMMTCERLPCPTAGLGPLREEAMK
PGAASSPLQQVPAPPLPAKKNLPTAPPRRRVSERVSLEDQSPGMAAEGDQLSLPPQGTSD
GPEDTPRESTEQGQDTEVKASDPHSMPELPRTAKQPPVPPPRKKRISRQLASTLPAPLEN
AELCTQAMALETPTPGPPREGQSPASQAGTQHPPAQATAHSQSSPEFKGSLASLSDSLGV
SVMATDQDSYSTSSTEEELEQFSSPSVKKKPSMILGKARHRLSFASFSSMFHAFLSNNRK
LYKKVVELAQDKGSYFGSLVQDYKVYSLEMMARQTSSTEMLQEIRTMMTQLKSYLLQSTE
LKALVDPALHSEEELEAIVESALYKCVLKPLKEAINSCLHQIHSKDGSLQQLKENQLVIL
ATTTTDLGVTTSVPEVPMMEKILQKFTSMHKAYSPEKKISILLKTCKLIYDSMALGNPGK
PYGADDFLPVLMYVLARSNLTEMLLNVEYMMELMDPALQLGEGSYYLTTTYGALEHIKSY
DKITVTRQLSVEVQDSIHRWERRRTLNKARASRSSVQDFICVSYLEPEQQARTLASRADT
QAQALCAQCAEKFAVERPQAHRLFVLVDGRCFQLADDALPHCIKGYLLRSEPKRDFHFVY
RPLDGGGGGGGGSPPCLVVREPNFL
Enzyme 126 Number of Residues 985
Enzyme 126 Molecular Weight 107852.4
Enzyme 126 Theoretical pI 6.58
Enzyme 126 GO Classification
Function
  • binding
  • protein binding
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 126 General Function Involved in signal transduction
Enzyme 126 Specific Function Potential Ras effector protein. May function as a guanine nucleotide exchange (GEF), by exchanging bound GDP for free GTP
Enzyme 126 Pathways Not Available
Enzyme 126 Reactions Not Available
Enzyme 126 Pfam Domain Function
Enzyme 126 Signals
  • None
Enzyme 126 Transmembrane Regions
  • None
Enzyme 126 Essentiality Not Available
Enzyme 126 GenBank ID Protein 40353729 Link Image
Enzyme 126 UniProtKB/Swiss-Prot ID Q8TB24 Link Image
Enzyme 126 UniProtKB/Swiss-Prot Entry Name RIN3_HUMAN Link Image
Enzyme 126 PDB ID Not Available
Enzyme 126 Cellular Location Not Available
Enzyme 126 Gene Sequence >2958 bp
ATGATCCGACACGCCGGGGCGCCCGCGCGCGGGGACCCCACGGGTCCGGTTCCAGTTGTT
GGCAAAGGAGAGGAAGAGGAAGAGGAAGATGGCATGCGGCTTTGTCTGCCAGCCAACCCG
AAAAACTGCCTTCCTCACCGCCGGGGCATCAGCATCCTGGAGAAGCTCATCAAAACATGC
CCGGTGTGGCTGCAGCTGAGTCTGGGCCAGGCAGAGGTGGCCAGGATCCTGCACCGGGTG
GTGGCTGGGATGTTCCTGGTTCGCCGGGACAGCAGCTCGAAGCAGCTGGTGCTCTGTGTC
CACTTTCCTTCTCTGAACGAAAGCTCGGCCGAGGTGCTCGAATACACCATTAAGGAAGAA
AAGTCGATATTGTACCTGGAAGGCTCGGCTCTTGTGTTTGAGGACATCTTCAGATTGATT
GCGTTCTACTGTGTCAGTAGAGACTTACTGCCCTTCACACTGCGGCTACCCCAGGCCATC
CTTGAGGCCAGCAGCTTCACGGACCTTGAGACCATCGCCAACCTGGGTCTGGGTTTCTGG
GACTCCTCGCTGAATCCTCCACAAGAAAGAGGGAAGCCAGCAGAGCCCCCAAGAGACCGG
GCCCCCGGATTCCCCCTAGTCTCCAGCCTCAGGCCCACAGCCCATGACGCAAACTGTGCC
TGTGAAATCGAGCTGTCGGTAGGAAATGACCGCCTGTGGTTTGTGAATCCTATTTTCATC
GAGGACTGCAGCAGCGCCCTGCCCACCGACCAGCCACCTCTTGGAAATTGCCCTGCACGC
CCTTTGCCGCCCACCTCTGATGCCACCTCACCCACCTCCAGGTGGGCCCCACGCCGCCCA
CCACCCCCTCCCCCAGTGCTGCCCCTGCAGCCCTGCAGCCCAGCCCAGCCCCCTGTGCTC
CCTGCTCTTGCCCCCGCCCCTGCCTGTCCTTTGCCCACCTCTCCCCCAGTGCCTGCCCCC
CACGTCACACCCCATGCCCCAGGTCCCCCAGACCATCCGAACCAGCCGCCCATGATGACC
TGCGAGAGACTCCCATGCCCCACTGCAGGCCTGGGCCCCCTCAGGGAGGAAGCGATGAAG
CCAGGGGCAGCCTCCAGTCCCTTGCAGCAGGTCCCCGCCCCGCCACTGCCTGCGAAGAAG
AACCTTCCCACTGCCCCTCCCAGACGCCGCGTTTCCGAGAGGGTGTCCTTAGAAGACCAA
AGTCCGGGGATGGCGGCAGAGGGGGACCAGCTCAGCCTGCCTCCCCAAGGGACCTCAGAC
GGCCCTGAGGACACGCCCCGGGAGAGCACGGAGCAAGGCCAGGACACAGAGGTGAAAGCC
AGCGATCCTCACAGCATGCCAGAGCTGCCCAGGACAGCCAAACAACCCCCAGTCCCGCCC
CCCAGGAAAAAACGGATCTCTCGACAACTGGCCTCGACCCTCCCAGCTCCCTTAGAGAAC
GCTGAGCTCTGCACACAGGCGATGGCCTTGGAGACACCCACGCCGGGTCCACCCAGAGAG
GGCCAAAGCCCTGCTTCTCAGGCTGGGACTCAGCACCCTCCTGCCCAGGCCACTGCCCAT
TCCCAGAGCTCTCCAGAGTTCAAGGGCTCCCTGGCCTCCCTCTCAGACAGCTTGGGGGTG
TCTGTCATGGCCACCGACCAGGACTCCTACTCCACCAGCAGCACGGAGGAGGAGCTGGAG
CAGTTCAGCAGCCCCAGCGTGAAGAAGAAGCCCTCCATGATCCTGGGCAAGGCTCGGCAC
CGGCTGAGCTTTGCCAGTTTCAGCAGCATGTTCCACGCTTTCCTCTCCAACAACCGCAAG
CTGTACAAGAAGGTGGTGGAGCTGGCGCAGGACAAGGGCTCGTACTTTGGCAGCCTGGTG
CAGGACTACAAGGTGTACAGCCTGGAGATGATGGCGCGCCAGACCTCCAGCACGGAGATG
CTGCAGGAGATTCGCACCATGATGACCCAGCTCAAGAGCTACCTGCTGCAGAGCACCGAG
CTCAAGGCCCTGGTGGACCCCGCCCTGCACTCCGAGGAGGAGCTCGAAGCAATTGTAGAG
TCTGCCTTGTACAAATGTGTCCTGAAGCCCCTGAAGGAAGCCATCAACTCATGCCTGCAT
CAGATCCACAGCAAGGATGGTTCGCTGCAGCAGCTCAAGGAGAACCAGTTAGTGATCCTG
GCCACCACCACCACTGACCTAGGTGTGACCACCAGCGTGCCGGAGGTGCCCATGATGGAG
AAGATCCTGCAGAAGTTCACCAGCATGCACAAGGCCTACTCACCTGAGAAGAAGATCTCC
ATCCTGCTCAAGACCTGCAAACTCATCTACGACTCCATGGCCCTCGGCAACCCAGGGAAG
CCCTATGGGGCGGATGACTTCCTGCCTGTGCTCATGTATGTGCTGGCCCGCAGCAACCTC
ACGGAGATGCTTCTCAATGTGGAGTACATGATGGAGCTCATGGACCCCGCCCTGCAGCTG
GGGGAGGGTTCCTACTATCTGACCACCACCTACGGGGCCCTGGAGCACATCAAGAGCTAC
GACAAGATCACGGTGACCCGGCAGCTGAGTGTGGAGGTGCAGGACTCCATCCACCGCTGG
GAGCGCCGGCGTACTCTCAACAAGGCCCGGGCCTCCCGCTCCTCCGTACAGGACTTCATC
TGCGTGTCGTACCTGGAGCCCGAGCAGCAGGCGCGGACGCTGGCGTCGCGGGCGGACACC
CAGGCCCAGGCGCTGTGCGCGCAGTGCGCGGAGAAGTTCGCGGTGGAGCGGCCGCAGGCG
CACCGGCTGTTCGTGCTGGTGGACGGGCGCTGCTTCCAGCTGGCGGACGACGCGCTGCCG
CACTGCATCAAGGGCTACCTGCTGCGCAGCGAGCCCAAGCGCGACTTCCACTTTGTCTAC
CGGCCCCTGGACGGTGGTGGCGGCGGCGGCGGCGGGAGCCCGCCCTGCCTGGTGGTGCGG
GAGCCCAACTTCCTGTGA
Enzyme 126 GenBank Gene ID NM_024832.3 Link Image
Enzyme 126 GeneCard ID RIN3 Link Image
Enzyme 126 GenAtlas ID RIN3 Link Image
Enzyme 126 HGNC ID HGNC:18751 Link Image
Enzyme 126 Chromosome Location 1
Enzyme 126 Locus 14q32.12
Enzyme 126 SNPs SNPJam Report Link Image
Enzyme 126 General References
  1. Kajiho H, Saito K, Tsujita K, Kontani K, Araki Y, Kurosu H, Katada T: RIN3: a novel Rab5 GEF interacting with amphiphysin II involved in the early endocytic pathway. J Cell Sci. 2003 Oct 15;116(Pt 20):4159-68. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Saito K, Murai J, Kajiho H, Kontani K, Kurosu H, Katada T: A novel binding protein composed of homophilic tetramer exhibits unique properties for the small GTPase Rab5. J Biol Chem. 2002 Feb 1;277(5):3412-8. Epub 2001 Dec 3. [PubMed Link Image]
  6. Yoshikawa M, Kajiho H, Sakurai K, Minoda T, Nakagawa S, Kontani K, Katada T: Tyr-phosphorylation signals translocate RIN3, the small GTPase Rab5-GEF, to early endocytic vesicles. Biochem Biophys Res Commun. 2008 Jul 18;372(1):168-72. Epub 2008 May 16. [PubMed Link Image]
Enzyme 126 Metabolite References Not Available
Enzyme 127 [top]
Enzyme 127 ID 14273
Enzyme 127 Name GTP-binding protein Rit1
Enzyme 127 Synonyms
  1. Ras-like protein expressed in many tissues
  2. Ras-like without CAAX protein 1
Enzyme 127 Gene Name RIT1
Enzyme 127 Protein Sequence >GTP-binding protein Rit1
MDSGTRPVGSCCSSPAGLSREYKLVMLGAGGVGKSAMTMQFISHRFPEDHDPTIEDAYKI
RIRIDDEPANLDILDTAGQAEFTAMRDQYMRAGEGFIICYSITDRRSFHEVREFKQLIYR
VRRTDDTPVVLVGNKSDLKQLRQVTKEEGLALAREFSCPFFETSAAYRYYIDDVFHALVR
EIRRKEKEAVLAMEKKSKPKNSVWKRLKSPFRKKKDSVT
Enzyme 127 Number of Residues 219
Enzyme 127 Molecular Weight 25144.6
Enzyme 127 Theoretical pI 9.50
Enzyme 127 GO Classification
Function
  • GTP binding
  • GTPase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
  • membrane
Enzyme 127 General Function Involved in GTP binding
Enzyme 127 Specific Function Plays a crucial role in coupling NGF stimulation to the activation of both EPHB2 and MAPK14 signaling pathways and in NGF- dependent neuronal differentiation
Enzyme 127 Pathways Not Available
Enzyme 127 Reactions Not Available
Enzyme 127 Pfam Domain Function
Enzyme 127 Signals
  • None
Enzyme 127 Transmembrane Regions
  • None
Enzyme 127 Essentiality Not Available
Enzyme 127 GenBank ID Protein 4234918 Link Image
Enzyme 127 UniProtKB/Swiss-Prot ID Q92963 Link Image
Enzyme 127 UniProtKB/Swiss-Prot Entry Name RIT1_HUMAN Link Image
Enzyme 127 PDB ID Not Available
Enzyme 127 Cellular Location Not Available
Enzyme 127 Gene Sequence >660 bp
ATGGATTCTGGAACTCGCCCAGTTGGTAGCTGCTGTAGCAGCCCCGCTGGGCTCTCACGG
GAGTACAAACTAGTGATGCTGGGTGCTGGTGGTGTAGGGAAGAGTGCCATGACCATGCAG
TTCATCAGCCACCGATTCCCAGAAGATCATGATCCCACCATTGAAGATGCTTATAAGATC
AGGATCCGTATTGATGATGAGCCTGCCAATCTGGACATTTTGGATACAGCTGGACAGGCA
GAGTTTACAGCCATGCGGGACCAGTATATGAGGGCAGGAGAAGGGTTTATCATCTGTTAC
TCTATCACGGATCGTCGAAGTTTCCATGAAGTTCGAGAGTTTAAACAGCTTATTTATCGA
GTCCGACGTACTGACGATACACCTGTGGTTCTTGTGGGAAACAAGTCAGACCTCAAACAG
CTAAGACAGGTCACCAAGGAAGAAGGATTGGCCTTGGCCCGAGAATTCAGCTGTCCCTTT
TTTGAGACATCTGCTGCATACCGCTACTATATTGATGATGTTTTCCATGCCCTTGTACGG
GAGATACGTAGGAAAGAAAAGGAGGCAGTACTGGCCATGGAGAAAAAATCTAAGCCCAAA
AACAGTGTATGGAAGAGGCTAAAATCACCATTCCGGAAGAAGAAAGATTCAGTAACTTGA
Enzyme 127 GenBank Gene ID AF084462 Link Image
Enzyme 127 GeneCard ID RIT1 Link Image
Enzyme 127 GenAtlas ID RIT1 Link Image
Enzyme 127 HGNC ID HGNC:10023 Link Image
Enzyme 127 Chromosome Location 1
Enzyme 127 Locus 1q22
Enzyme 127 SNPs SNPJam Report Link Image
Enzyme 127 General References
  1. Lee CH, Della NG, Chew CE, Zack DJ: Rin, a neuron-specific and calmodulin-binding small G-protein, and Rit define a novel subfamily of ras proteins. J Neurosci. 1996 Nov 1;16(21):6784-94. [PubMed Link Image]
  2. Wes PD, Yu M, Montell C: RIC, a calmodulin-binding Ras-like GTPase. EMBO J. 1996 Nov 1;15(21):5839-48. [PubMed Link Image]
  3. Shao H, Kadono-Okuda K, Finlin BS, Andres DA: Biochemical characterization of the Ras-related GTPases Rit and Rin. Arch Biochem Biophys. 1999 Nov 15;371(2):207-19. [PubMed Link Image]
  4. Shi GX, Andres DA: Rit contributes to nerve growth factor-induced neuronal differentiation via activation of B-Raf-extracellular signal-regulated kinase and p38 mitogen-activated protein kinase cascades. Mol Cell Biol. 2005 Jan;25(2):830-46. [PubMed Link Image]
Enzyme 127 Metabolite References Not Available
Enzyme 128 [top]
Enzyme 128 ID 14274
Enzyme 128 Name GTP-binding protein Rit2
Enzyme 128 Synonyms
  1. Ras-like protein expressed in neurons
  2. Ras-like without CAAX protein 2
Enzyme 128 Gene Name RIT2
Enzyme 128 Protein Sequence >GTP-binding protein Rit2
MEVENEASCSPGSASGGSREYKVVMLGAGGVGKSAMTMQFISHQFPDYHDPTIEDAYKTQ
VRIDNEPAYLDILDTAGQAEFTAMREQYMRGGEGFIICYSVTDRQSFQEAAKFKELIFQV
RHTYEIPLVLVGNKIDLEQFRQVSTEEGLSLAQEYNCGFFETSAALRFCIDDAFHGLVRE
IRKKESMPSLMEKKLKRKDSLWKKLKGSLKKKRENMT
Enzyme 128 Number of Residues 217
Enzyme 128 Molecular Weight 24667.9
Enzyme 128 Theoretical pI 6.52
Enzyme 128 GO Classification
Function
  • GTP binding
  • GTPase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
  • membrane
Enzyme 128 General Function Involved in GTP binding
Enzyme 128 Specific Function Binds and exchanges GTP and GDP
Enzyme 128 Pathways Not Available
Enzyme 128 Reactions Not Available
Enzyme 128 Pfam Domain Function
Enzyme 128 Signals
  • None
Enzyme 128 Transmembrane Regions
  • None
Enzyme 128 Essentiality Not Available
Enzyme 128 GenBank ID Protein 20147737 Link Image
Enzyme 128 UniProtKB/Swiss-Prot ID Q99578 Link Image
Enzyme 128 UniProtKB/Swiss-Prot Entry Name RIT2_HUMAN Link Image
Enzyme 128 PDB ID Not Available
Enzyme 128 Cellular Location Not Available
Enzyme 128 Gene Sequence >654 bp
ATGGAGGTAGAAAATGAAGCCAGCTGCTCCCCGGGCAGCGCATCAGGCGGGTCCAGAGAG
TACAAGGTGGTAATGCTGGGAGCAGGGGGAGTTGGTAAAAGCGCAATGACAATGCTGTTT
ATTAGTCATCAGTTCCCTGATTATCATGACCCTACTATAGAAGATGCTTATAAGACCCAG
GTCAGGATTGACAATGAGCCAGCTTACTTGGACATCTTGGACACTGCTGGCCAGGCAGAA
TTCACAGCCATGCGGGAGCAGTACATGCGAGGTGGGGAAGGCTTCATCATCTGCTACTCC
GTCACTGACCGTCAATCATTTCAGGAGGCTGCCAAGTTTAAAGAGCTCATTTTTCAGGTC
CGCCACACCTATGAAATTCCCCTGGTGCTGGTGGGTAACAAAATTGATCTGGAACAGTTC
CGCCAGGTTTCTACAGAAGAAGGCTTGAGTCTTGCCCAAGAATATAATTGTGGTTTTTTT
GAGACCTCTGCAGCCCTCAGATTCTGTATTGATGATGCTTTTCATGGCTTAGTGAGGGAA
ATTCGCAAGAAGGAGTCCATGCCATCCTTGATGGAAAAGAAACTGAAGAGAAAAGACAGC
CTGTGGAAGAAGCTCAAAGGTTCTTTGAAGAAGAAGAGAGAAAATATGACATGA
Enzyme 128 GenBank Gene ID AF493922 Link Image
Enzyme 128 GeneCard ID RIT2 Link Image
Enzyme 128 GenAtlas ID RIT2 Link Image
Enzyme 128 HGNC ID HGNC:10017 Link Image
Enzyme 128 Chromosome Location 1
Enzyme 128 Locus 18q12.3
Enzyme 128 SNPs SNPJam Report Link Image
Enzyme 128 General References
  1. Lee CH, Della NG, Chew CE, Zack DJ: Rin, a neuron-specific and calmodulin-binding small G-protein, and Rit define a novel subfamily of ras proteins. J Neurosci. 1996 Nov 1;16(21):6784-94. [PubMed Link Image]
  2. Wes PD, Yu M, Montell C: RIC, a calmodulin-binding Ras-like GTPase. EMBO J. 1996 Nov 1;15(21):5839-48. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 128 Metabolite References Not Available
Enzyme 129 [top]
Enzyme 129 ID 14277
Enzyme 129 Name Rap guanine nucleotide exchange factor 5
Enzyme 129 Synonyms
  1. Guanine nucleotide exchange factor for Rap1
  2. M-Ras-regulated Rap GEF
  3. MR-GEF
  4. Related to Epac
  5. Repac
Enzyme 129 Gene Name RAPGEF5
Enzyme 129 Protein Sequence >Rap guanine nucleotide exchange factor 5
MGSSRLRVFDPHLERKDSAAALSDRELPLPTFDVPYFKYIDEEDEDDEWSSRSQSSTEDD
SVDSLLSDRYVVVSGTPEKILEHLLNDLHLEEVQDKETETLLDDFLLTYTVFMTTDDLCQ
ALLRHYSAKKYQGKEENSDVPRRKRKVLHLVSQWIALYKDWLPEDEHSKMFLKTIYRNVL
DDVYEYPILEKELKEFQKILGMHRRHTVDEYSPQKKNKALFHQFSLKENWLQHRGTVTET
EEIFCHVYITEHSYVSVKAKVSSIAQEILKVVAEKIQYAEEDLALVAITFSGEKHELQPN
DLVISKSLEASGRIYVYRKDLADTLNPFAENEESQQRSMRILGMNTWDLALELMNFDWSL
FNSIHEQELIYFTFSRQGSGEHTANLSLLLQRCNEVQLWVATEILLCSQLGKRVQLVKKF
IKIAAHCKAQRNLNSFFAIVMGLNTASVSRLSQTWEKIPGKFKKLFSELESLTDPSLNHK
AYRDAFKKMKPPKIPFMPLLLKDVTFIHEGNKTFLDNLVNFEKLHMIADTVRTLRHCRTN
QFGDLSPKEHQELKSYVNHLYVIDSQQALFELSHRIEPRV
Enzyme 129 Number of Residues 580
Enzyme 129 Molecular Weight 67732.6
Enzyme 129 Theoretical pI 6.27
Enzyme 129 GO Classification
Function
  • GTPase regulator activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 129 General Function Involved in guanyl-nucleotide exchange factor activity
Enzyme 129 Specific Function Guanine nucleotide exchange factor (GEF) for RAP1A, RAP2A and MRAS/M-Ras-GTP. Its association with MRAS inhibits Rap1 activation
Enzyme 129 Pathways Not Available
Enzyme 129 Reactions Not Available
Enzyme 129 Pfam Domain Function
Enzyme 129 Signals
  • None
Enzyme 129 Transmembrane Regions
  • None
Enzyme 129 Essentiality Not Available
Enzyme 129 GenBank ID Protein 40788937 Link Image
Enzyme 129 UniProtKB/Swiss-Prot ID Q92565 Link Image
Enzyme 129 UniProtKB/Swiss-Prot Entry Name RPGF5_HUMAN Link Image
Enzyme 129 PDB ID 1WGY Link Image
Enzyme 129 PDB File Show
Enzyme 129 3D Structure
Enzyme 129 Cellular Location Not Available
Enzyme 129 Gene Sequence >1752 bp
CCGTTCACAATGGGCAGCTCCCGGCTGAGGGTCTTTGACCCTCATTTGGAGAGGAAAGAT
TCCGCCGCGGCGCTCTCAGACCGAGAGCTGCCCTTGCCTACCTTCGATGTGCCTTATTTC
AAATACATCGACGAGGAGGATGAGGACGATGAATGGAGCAGCCGTTCGCAGTCTTCCACC
GAGGATGACTCAGTGGACTCTCTGCTCTCTGACAGATATGTGGTGGTGTCCGGGACCCCG
GAGAAGATTTTGGAGCACCTTTTGAATGACTTGCACCTGGAAGAAGTCCAGGACAAAGAA
ACAGAGACCCTCCTGGATGACTTCCTTCTCACGTACACTGTCTTCATGACAACTGATGAC
TTGTGCCAGGCTCTGTTAAGGCACTATTCTGCTAAGAAGTATCAAGGCAAAGAGGAAAAC
TCAGATGTTCCGCGTAGGAAACGTAAAGTCTTGCATCTTGTTTCCCAGTGGATTGCTCTG
TACAAAGACTGGTTACCTGAAGATGAACATTCAAAAATGTTTTTAAAGACCATATATAGG
AATGTACTGGATGATGTTTATGAATATCCAATACTTGAAAAAGAATTGAAAGAATTTCAA
AAGATACTTGGAATGCACCGTCGTCACACTGTAGATGAATATTCACCACAAAAAAAGAAT
AAAGCCCTTTTCCACCAATTCAGTCTTAAGGAGAACTGGCTCCAGCATAGAGGAACTGTG
ACTGAAACGGAGGAAATTTTCTGCCACGTGTATATAACAGAGCACTCCTATGTCAGTGTG
AAGGCAAAAGTTTCCAGTATAGCCCAAGAGATCCTAAAAGTCGTGGCAGAAAAGATCCAG
TATGCAGAAGAGGATCTGGCTCTGGTGGCCATCACATTCTCTGGGGAAAAGCATGAACTT
CAGCCAAATGACTTAGTCATCTCCAAATCCCTCGAGGCATCTGGTCGAATATATGTCTAC
CGGAAAGACCTGGCGGACACTTTGAACCCATTTGCAGAAAATGAGGAATCACAGCAAAGG
TCGATGAGGATTTTGGGAATGAACACTTGGGATCTTGCTCTGGAATTAATGAATTTTGAT
TGGAGTCTATTCAATTCAATTCACGAGCAAGAGCTGATCTACTTCACGTTCAGCAGACAG
GGAAGTGGGGAACACACTGCAAATCTCAGCCTTCTGCTCCAGAGATGCAATGAGGTCCAG
CTTTGGGTGGCCACGGAGATTCTGCTCTGCAGCCAGCTGGGCAAGCGAGTGCAGCTGGTG
AAAAAATTCATCAAAATTGCGGCTCACTGCAAAGCCCAGAGAAACCTGAATTCTTTCTTT
GCCATTGTGATGGGTCTCAACACTGCTTCTGTCAGTCGACTGTCGCAGACCTGGGAGAAA
ATCCCTGGGAAGTTTAAGAAACTTTTCTCTGAACTTGAAAGTTTAACAGATCCTTCCCTA
AATCACAAAGCCTACAGAGATGCATTCAAAAAGATGAAGCCACCAAAAATCCCTTTCATG
CCCTTATTGCTTAAAGATGTAACATTTATTCATGAAGGAAATAAAACTTTTTTGGATAAT
CTTGTCAATTTTGAAAAGCTGCATATGATCGCAGACACTGTCCGAACCCTGAGACACTGC
AGGACTAACCAGTTTGGTGACCTGTCTCCAAAAGAGCATCAAGAGTTAAAGTCCTATGTT
AATCACCTGTATGTCATTGACAGCCAGCAGGCTCTGTTTGAGCTCTCACACAGGATCGAG
CCTCGGGTGTGA
Enzyme 129 GenBank Gene ID D87467 Link Image
Enzyme 129 GeneCard ID RAPGEF5 Link Image
Enzyme 129 GenAtlas ID RAPGEF5 Link Image
Enzyme 129 HGNC ID HGNC:16862 Link Image
Enzyme 129 Chromosome Location 7
Enzyme 129 Locus 7p15.3
Enzyme 129 SNPs SNPJam Report Link Image
Enzyme 129 General References
  1. Nagase T, Seki N, Ishikawa K, Ohira M, Kawarabayasi Y, Ohara O, Tanaka A, Kotani H, Miyajima N, Nomura N: Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. DNA Res. 1996 Oct 31;3(5):321-9, 341-54. [PubMed Link Image]
  2. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ichiba T, Hoshi Y, Eto Y, Tajima N, Kuraishi Y: Characterization of GFR, a novel guanine nucleotide exchange factor for Rap1. FEBS Lett. 1999 Aug 20;457(1):85-9. [PubMed Link Image]
  5. de Rooij J, Rehmann H, van Triest M, Cool RH, Wittinghofer A, Bos JL: Mechanism of regulation of the Epac family of cAMP-dependent RapGEFs. J Biol Chem. 2000 Jul 7;275(27):20829-36. [PubMed Link Image]
  6. Rebhun JF, Castro AF, Quilliam LA: Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction. J Biol Chem. 2000 Nov 10;275(45):34901-8. [PubMed Link Image]
Enzyme 129 Metabolite References Not Available
Enzyme 130 [top]
Enzyme 130 ID 14279
Enzyme 130 Name Ras-related GTP-binding protein A
Enzyme 130 Synonyms
  1. Rag A
  2. RagA
  3. Adenovirus E3 14.7 kDa-interacting protein 1
  4. FIP-1
Enzyme 130 Gene Name RRAGA
Enzyme 130 Protein Sequence >Ras-related GTP-binding protein A
MPNTAMKKKVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNL
WDCGGQDTFMENYFTSQRDNIFRNVEVLIYVFDVESRELEKDMHYYQSCLEAILQNSPDA
KIFCLVHKMDLVQEDQRDLIFKEREEDLRRLSRPLECACFRTSIWDETLYKAWSSIVYQL
IPNVQQLEMNLRNFAQIIEADEVLLFERATFLVISHYQCKEQRDVHRFEKISNIIKQFKL
SCSKLAASFQSMEVRNSNFAAFIDIFTSNTYVMVVMSDPSIPSAATLINIRNARKHFEKL
ERVDGPKHSLLMR
Enzyme 130 Number of Residues 313
Enzyme 130 Molecular Weight 36565.8
Enzyme 130 Theoretical pI 7.81
Enzyme 130 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
Component
  • cell part
  • cytoplasm
  • intracellular membrane-bounded organelle
  • intracellular part
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 130 General Function Involved in GTP binding
Enzyme 130 Specific Function Involved in the RCC1/Ran-GTPase pathway. May play a direct role in a TNF-alpha signaling pathway leading to induction of cell death. May alternatively act as a cellular target for adenovirus E3-14.7K, an inhibitor of TNF-alpha functions, thereby affecting cell death. Has guanine nucleotide-binding activity but undetectable intrinsic GTPase activity
Enzyme 130 Pathways Not Available
Enzyme 130 Reactions Not Available
Enzyme 130 Pfam Domain Function
Enzyme 130 Signals
  • None
Enzyme 130 Transmembrane Regions
  • None
Enzyme 130 Essentiality Not Available
Enzyme 130 GenBank ID Protein 189053606 Link Image
Enzyme 130 UniProtKB/Swiss-Prot ID Q7L523 Link Image
Enzyme 130 UniProtKB/Swiss-Prot Entry Name RRAGA_HUMAN Link Image
Enzyme 130 PDB ID Not Available
Enzyme 130 Cellular Location Not Available
Enzyme 130 Gene Sequence >942 bp
ATGCCAAATACAGCCATGAAGAAAAAGGTGCTGCTGATGGGGAAGAGCGGGTCGGGGAAG
ACCAGCATGAGGTCGATAATCTTCGCCAATTACATTGCTCGCGACACCCGGCGCCTGGGG
GCCACCATTGACGTGGAACACTCCCACGTCCGATTCCTAGGGAACCTGGTGCTGAACCTG
TGGGACTGTGGCGGTCAGGACACCTTCATGGAAAATTACTTCACCAGCCAGCGAGACAAT
ATCTTCCGTAACGTGGAAGTTTTGATTTACGTGTTTGACGTGGAGAGCCGCGAACTGGAA
AAGGACATGCATTATTACCAGTCGTGTCTGGAGGCCATCCTCCAGAACTCTCCTGACGCC
AAAATCTTCTGCCTGGTGCACAAAATGGATCTGGTTCAGGAGGATCAGCGTGACCTGATT
TTTAAAGAGCGAGAGGAAGACCTGAGGCGTCTGTCTCGCCCGCTGGAGTGTGCTTGTTTT
CGAACGTCCATCTGGGATGAGACGCTCTACAAAGCCTGGTCCAGCATCGTCTACCAGCTG
ATTCCCAACGTTCAGCAGCTGGAGATGAACCTCAGGAATTTTGCCCAAATCATTGAGGCC
GATGAAGTTCTGCTGTTCGAAAGAGCTACATTCTTGGTTATTTCCCACTACCAGTGCAAA
GAGCAGCGCGACGTCCACCGGTTTGAGAAGATCAGCAACATCATCAAACAGTTCAAGCTG
AGCTGCAGTAAATTGGCCGCTTCCTTCCAGAGCATGGAAGTTAGGAATTCCAACTTCGCT
GCTTTCATCGACATCTTCACCTCAAATACGTACGTGATGGTGGTCATGTCAGATCCGTCG
ATCCCTTCTGCGGCCACTCTGATCAACATTCGCAATGCCCGGAAACACTTTGAGAAGCTG
GAGAGAGTGGATGGCCCCAAGCACAGTCTCCTTATGCGTTGA
Enzyme 130 GenBank Gene ID AK313023 Link Image
Enzyme 130 GeneCard ID RRAGA Link Image
Enzyme 130 GenAtlas ID RRAGA Link Image
Enzyme 130 HGNC ID HGNC:16963 Link Image
Enzyme 130 Chromosome Location 9
Enzyme 130 Locus 9p22.1
Enzyme 130 SNPs SNPJam Report Link Image
Enzyme 130 General References
  1. Schurmann A, Brauers A, Massmann S, Becker W, Joost HG: Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs, RagB1) with remote similarity to the Ras-related GTPases. J Biol Chem. 1995 Dec 1;270(48):28982-8. [PubMed Link Image]
  2. Li Y, Kang J, Horwitz MS: Interaction of an adenovirus 14.7-kilodalton protein inhibitor of tumor necrosis factor alpha cytolysis with a new member of the GTPase superfamily of signal transducers. J Virol. 1997 Feb;71(2):1576-82. [PubMed Link Image]
  3. Hirose E, Nakashima N, Sekiguchi T, Nishimoto T: RagA is a functional homologue of S. cerevisiae Gtr1p involved in the Ran/Gsp1-GTPase pathway. J Cell Sci. 1998 Jan;111 ( Pt 1):11-21. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Sekiguchi T, Hirose E, Nakashima N, Ii M, Nishimoto T: Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B. J Biol Chem. 2001 Mar 9;276(10):7246-57. Epub 2000 Nov 9. [PubMed Link Image]
  8. Sekiguchi T, Todaka Y, Wang Y, Hirose E, Nakashima N, Nishimoto T: A novel human nucleolar protein, Nop132, binds to the G proteins, RRAG A/C/D. J Biol Chem. 2004 Feb 27;279(9):8343-50. Epub 2003 Dec 4. [PubMed Link Image]
Enzyme 130 Metabolite References Not Available
Enzyme 131 [top]
Enzyme 131 ID 14280
Enzyme 131 Name Ras-related GTP-binding protein B
Enzyme 131 Synonyms
  1. Rag B
  2. RagB
Enzyme 131 Gene Name RRAGB
Enzyme 131 Protein Sequence >Ras-related GTP-binding protein B
MEESDSEKTTEKENLGPRMDPPLGEPEGSLGWVLPNTAMKKKVLLMGKSGSGKTSMRSII
FANYIARDTRRLGATILDRIHSLQINSSLSTYSLVDSVGNTKTFDVEHSHVRFLGNLVLN
LWDCGGQDTFMENYFTSQRDNIFRNVEVLIYVFDVESRELEKDMHYYQSCLEAILQNSPD
AKIFCLVHKMDLVQEDQRDLIFKEREEDLRRLSRPLECSCFRTSIWDETLYKAWSSIVYQ
LIPNVQQLEMNLRNFAEIIEADEVLLFERATFLVISHYQCKEQRDAHRFEKISNIIKQFK
LSCSKLAASFQSMEVRNSNFAAFIDIFTSNTYVMVVMSDPSIPSAATLINIRNARKHFEK
LERVDGPKQCLLMR
Enzyme 131 Number of Residues 374
Enzyme 131 Molecular Weight 43250.0
Enzyme 131 Theoretical pI 6.13
Enzyme 131 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
Component
  • cell part
  • cytoplasm
  • intracellular membrane-bounded organelle
  • intracellular part
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 131 General Function Involved in GTP binding
Enzyme 131 Specific Function Involved in the RCC1/Ran-GTPase pathway. Has guanine nucleotide-binding activity but undetectable intrinsic GTPase activity
Enzyme 131 Pathways Not Available
Enzyme 131 Reactions Not Available
Enzyme 131 Pfam Domain Function
Enzyme 131 Signals
  • None
Enzyme 131 Transmembrane Regions
  • None
Enzyme 131 Essentiality Not Available
Enzyme 131 GenBank ID Protein 46249397 Link Image
Enzyme 131 UniProtKB/Swiss-Prot ID Q5VZM2 Link Image
Enzyme 131 UniProtKB/Swiss-Prot Entry Name RRAGB_HUMAN Link Image
Enzyme 131 PDB ID Not Available
Enzyme 131 Cellular Location Not Available
Enzyme 131 Gene Sequence >1125 bp
ATGGAAGAATCTGACTCTGAGAAAACGACGGAGAAAGAAAATCTGGGGCCGAGAATGGAT
CCACCACTAGGGGAACCGGAAGGATCGCTTGGGTGGGTGCTACCAAATACAGCCATGAAG
AAAAAGGTGCTGTTGATGGGTAAAAGTGGGTCTGGTAAGACCAGCATGAGGTCTATTATC
TTTGCAAATTATATTGCCAGAGACACACGTCGCCTTGGCGCAACAATACTAGACCGTATA
CATAGTCTTCAAATTAATAGCAGTTTGAGCACCTACTCTCTCGTAGACTCTGTTGGAAAT
ACAAAGACATTTGATGTAGAACATTCTCATGTTCGATTTCTGGGAAACCTGGTATTGAAC
CTGTGGGATTGTGGTGGGCAAGACACCTTCATGGAAAATTATTTCACTAGCCAACGGGAC
AACATCTTCCGAAATGTGGAGGTTCTGATTTATGTCTTTGATGTGGAGAGCCGCGAACTG
GAAAAGGACATGCACTATTACCAATCATGCCTGGAGGCCATTCTGCAGAATTCTCCAGAT
GCCAAAATATTTTGCTTGGTACACAAAATGGATCTGGTACAGGAGGATCAACGGGACCTG
ATTTTTAAAGAGCGAGAAGAAGATTTGAGGCGTTTGTCTCGCCCATTGGAATGTTCTTGT
TTCCGAACATCTATCTGGGATGAAACCCTCTATAAGGCTTGGTCCAGCATAGTTTATCAG
CTGATTCCCAATGTTCAGCAGCTGGAAATGAACCTAAGGAATTTTGCTGAAATTATCGAA
GCTGATGAAGTACTTCTTTTTGAGAGAGCTACTTTTCTGGTAATTTCTCACTATCAGTGT
AAAGAGCAGCGTGATGCCCATAGATTTGAGAAAATAAGCAACATTATTAAGCAGTTCAAG
CTGAGCTGCAGCAAGCTGGCTGCCTCTTTCCAGAGTATGGAAGTCAGGAACTCTAACTTC
GCTGCTTTCATTGACATCTTTACATCCAACACTTATGTGATGGTTGTGATGTCTGATCCG
TCCATTCCTTCTGCAGCTACTCTGATCAACATCCGCAATGCCAGGAAACACTTTGAAAAG
CTGGAAAGAGTGGATGGACCAAAGCAGTGTCTTCTCATGCGCTAA
Enzyme 131 GenBank Gene ID NM_016656.3 Link Image
Enzyme 131 GeneCard ID RRAGB Link Image
Enzyme 131 GenAtlas ID RRAGB Link Image
Enzyme 131 HGNC ID HGNC:19901 Link Image
Enzyme 131 Chromosome Location Not Available
Enzyme 131 Locus Not Available
Enzyme 131 SNPs SNPJam Report Link Image
Enzyme 131 General References
  1. Schurmann A, Brauers A, Massmann S, Becker W, Joost HG: Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs, RagB1) with remote similarity to the Ras-related GTPases. J Biol Chem. 1995 Dec 1;270(48):28982-8. [PubMed Link Image]
  2. Hirose E, Nakashima N, Sekiguchi T, Nishimoto T: RagA is a functional homologue of S. cerevisiae Gtr1p involved in the Ran/Gsp1-GTPase pathway. J Cell Sci. 1998 Jan;111 ( Pt 1):11-21. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Sekiguchi T, Hirose E, Nakashima N, Ii M, Nishimoto T: Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B. J Biol Chem. 2001 Mar 9;276(10):7246-57. Epub 2000 Nov 9. [PubMed Link Image]
Enzyme 131 Metabolite References Not Available
Enzyme 132 [top]
Enzyme 132 ID 14281
Enzyme 132 Name Ras-related GTP-binding protein C
Enzyme 132 Synonyms
  1. Rag C
  2. RagC
  3. GTPase-interacting protein 2
  4. TIB929
Enzyme 132 Gene Name RRAGC
Enzyme 132 Protein Sequence >Ras-related GTP-binding protein C
MSLQYGAEETPLAGSYGAADSFPKDFGYGVEEEEEEAAAAGGGVGAGAGGGCGPGGADSS
KPRILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKIYKDDISNSSFVNFQIWDFPGQ
MDFFDPTFDYEMIFRGTGALIYVIDAQDDYMEALTRLHITVSKAYKVNPDMNFEVFIHKV
DGLSDDHKIETQRDIHQRANDDLADAGLEKLHLSFYLTSIYDHSIFEAFSKVVQKLIPQL
PTLENLLNIFISNSGIEKAFLFDVVSKIYIATDSSPVDMQSYELCCDMIDVVIDVSCIYG
LKEDGSGSAYDKESMAIIKLNNTTVLYLKEVTKFLALVCILREESFERKGLIDYNFHCFR
KAIHEVFEVGVTSHRSCGHQTSASSLKALTHNGTPRNAI
Enzyme 132 Number of Residues 399
Enzyme 132 Molecular Weight 44223.5
Enzyme 132 Theoretical pI 4.72
Enzyme 132 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
Component
  • cell part
  • cytoplasm
  • intracellular membrane-bounded organelle
  • intracellular part
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 132 General Function Involved in GTP binding
Enzyme 132 Specific Function Has guanine nucleotide-binding activity but weak intrinsic GTPase activity
Enzyme 132 Pathways Not Available
Enzyme 132 Reactions Not Available
Enzyme 132 Pfam Domain Function
Enzyme 132 Signals
  • None
Enzyme 132 Transmembrane Regions
  • None
Enzyme 132 Essentiality Not Available
Enzyme 132 GenBank ID Protein 11181618 Link Image
Enzyme 132 UniProtKB/Swiss-Prot ID Q9HB90 Link Image
Enzyme 132 UniProtKB/Swiss-Prot Entry Name RRAGC_HUMAN Link Image
Enzyme 132 PDB ID Not Available
Enzyme 132 Cellular Location Not Available
Enzyme 132 Gene Sequence >1200 bp
ATGTCCCTGCAGTACGGGGCGGAGGAGACGCCCCTCGCCGGCAGTTACGGCGCGGCCGAT
TCGTTTCCAAAGGACTTCGGCTACGGCGTGGAGGAGGAGGAAGAGGAGGCGGCGGCGGCG
GGCGGAGGGGTTGGGGCAGGGGCAGGCGGTGGCTGTGGTCCGGGGGGCGCTGACAGCTCC
AAGCCGAGGATTCTGCTCATGGGACTCCGGCGCAGCGGCAAGTCCTCCATCCAGAAGGTG
GTGTTTCATAAGATGTCACCCAACGAGACCCTCTTTTTGGAAAGTACCAACAAGATTTAT
AAGGATGACATTTCCAATAGCTCCTTTGTGAATTTCCAGATATGGGATTTTCCTGGGCAA
ATGGACTTTTTTGACCCAACCTTTGACTATGAGATGATCTTCAGGGGAACAGGAGCATTG
ATATACGTCATTGACGCACAGGATGACTACATGGAGGCTTTAACAAGACTTCACATTACT
GTTTCTAAAGCCTACAAAGTTAACCCAGACATGAATTTTGAGGTTTTTATTCACAAAGTT
GATGGTCTGTCTGATGATCACAAAATAGAAACACAGAGGGACATTCATCAAAGGGCCAAT
GATGACCTTGCAGATGCTGGGCTAGAAAAACTCCATCTTAGCTTTTATCTGACTAGTATC
TATGACCATTCAATATTTGAAGCCTTTAGTAAGGTGGTGCAGAAACTCATTCCACAACTG
CCGACCTTGGAAAACCTATTAAATATCTTTATATCAAATTCAGGTATTGAAAAAGCTTTT
CTCTTTGATGTTGTCAGCAAAATCTACATTGCAACAGACAGTTCCCCTGTGGATATGCAA
TCTTATGAACTTTGCTGTGACATGATCGATGTTGTAATTGATGTGTCTTGTATATATGGG
TTAAAGGAAGATGGAAGTGGAAGTGCTTATGACAAAGAATCTATGGCAATTATCAAGCTG
AATAATACAACTGTCCTTTATTTAAAGGAGGTGACTAAATTTTTGGCACTGGTCTGCATT
CTAAGGGAAGAAAGCTTTGAAAGAAAAGGTTTAATAGACTACAACTTCCACTGTTTCCGA
AAAGCTATTCATGAGGTTTTTGAGGTGGGTGTGACTTCTCACAGGAGCTGTGGTCACCAG
ACTAGTGCCTCCAGTCTGAAAGCGCTGACACACAATGGCACGCCACGAAACGCCATCTAG
Enzyme 132 GenBank Gene ID AF272035 Link Image
Enzyme 132 GeneCard ID RRAGC Link Image
Enzyme 132 GenAtlas ID RRAGC Link Image
Enzyme 132 HGNC ID HGNC:19902 Link Image
Enzyme 132 Chromosome Location 1
Enzyme 132 Locus 1p34
Enzyme 132 SNPs SNPJam Report Link Image
Enzyme 132 General References
  1. Horwitz MS: Adenovirus immunoregulatory genes and their cellular targets. Virology. 2001 Jan 5;279(1):1-8. [PubMed Link Image]
  2. Sekiguchi T, Hirose E, Nakashima N, Ii M, Nishimoto T: Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B. J Biol Chem. 2001 Mar 9;276(10):7246-57. Epub 2000 Nov 9. [PubMed Link Image]
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