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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
SDF File Show
PDB File Show
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. Nucleoside diphosphate kinase, mitochondrial precursor
  4. Ribonucleoside-diphosphate reductase large subunit
  5. Nucleoside diphosphate kinase A
  6. Nucleoside diphosphate kinase 7
  7. Ribonucleoside-diphosphate reductase M2 subunit
  8. Nucleoside diphosphate kinase B
  9. Nucleoside diphosphate kinase 3
  10. Nucleoside diphosphate kinase 6
  11. Fucose-1-phosphate guanylyltransferase
  12. Alpha-1,3-mannosyltransferase ALG2
  13. Dolichol-phosphate mannosyltransferase
  14. GDP-mannose 4,6 dehydratase
  15. Galactoside 2-alpha-L-fucosyltransferase 2
  16. Galactoside 2-alpha-L-fucosyltransferase 1
  17. 6-phosphofructokinase type C
  18. 6-phosphofructokinase, liver type
  19. 6-phosphofructokinase, muscle type
  20. Pyruvate kinase isozymes R/L
  21. Ectonucleoside triphosphate diphosphohydrolase 4
  22. Ectonucleoside triphosphate diphosphohydrolase 6
  23. Ectonucleoside triphosphate diphosphohydrolase 5 precursor
  24. Adenylosuccinate synthetase isozyme 1
  25. Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial precursor
  26. Succinyl-CoA ligase [GDP-forming] beta-chain, mitochondrial precursor
  27. Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
  28. GDP-L-fucose synthetase
  29. Guanylate kinase
  30. Alpha-(1,3)-fucosyltransferase
  31. Rap guanine nucleotide exchange factor 2
  32. Polyribonucleotide nucleotidyltransferase 1, mitochondrial precursor
  33. Rho guanine nucleotide exchange factor 1
  34. Guanine nucleotide-binding protein G(I)/G(S)/G(O) gamma-2 subunit precursor
  35. Ras-related C3 botulinum toxin substrate 1 precursor
  36. Rho GDP-dissociation inhibitor 3
  37. Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
  38. Rab GDP dissociation inhibitor alpha
  39. Proto-oncogene DBL
  40. Cell division control protein 42 homolog precursor
  41. Rab GDP dissociation inhibitor beta
  42. Rho GDP-dissociation inhibitor 1
  43. Rho GDP-dissociation inhibitor 2
  44. Ras-related C3 botulinum toxin substrate 2 precursor
  45. Elongation factor 1-alpha 1
  46. Vinexin
  47. GTPase HRas precursor
  48. Rho-related GTP-binding protein RhoQ precursor
  49. Guanine nucleotide-binding protein G(q) subunit alpha
  50. Guanine nucleotide-binding protein subunit alpha-11
  51. Guanine nucleotide-binding protein G(I)/G(S)/G(O) gamma-11 subunit precursor
  52. Chitobiosyldiphosphodolichol beta-mannosyltransferase
  53. Guanine nucleotide-binding protein G(t), alpha-1 subunit
  54. Uridine-cytidine kinase 2
  55. Protein ALEX
  56. Rap guanine nucleotide exchange factor 3
  57. Lysophosphatidic acid receptor Edg-4
  58. Rap guanine nucleotide exchange factor 4
  59. Succinate-CoA ligase, ADP-forming, beta subunit
  60. ENTPD4 protein
  61. Mannose-1-phosphate guanyltransferase subunit beta
  62. GDP-mannose pyrophosphorylase A
  63. Alpha-(1,3)-fucosyltransferase
  64. Alpha-(1,6)-fucosyltransferase
  65. Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
  66. Ribonucleoside-diphosphate reductase subunit M2 B
  67. Uridine/cytidine kinase-like 1
  68. Ectonucleoside triphosphate diphosphohydrolase 8
  69. Synembryn-B
  70. Rap guanine nucleotide exchange factor 6
  71. Neuroepithelial cell-transforming gene 1 protein
  72. Cell cycle progression protein 1
  73. DEP domain-containing protein 2
  74. Dedicator of cytokinesis protein 10
  75. Dedicator of cytokinesis protein 1
  76. Dedicator of cytokinesis protein 2
  77. Dedicator of cytokinesis protein 3
  78. Dedicator of cytokinesis protein 4
  79. Dedicator of cytokinesis protein 5
  80. Dedicator of cytokinesis protein 6
  81. Dedicator of cytokinesis protein 7
  82. Dedicator of cytokinesis protein 8
  83. Dynamin-1
  84. Dynamin-2
  85. Elongation factor G 1, mitochondrial precursor
  86. Elongation factor G 2, mitochondrial precursor
  87. Elongation factor Tu, mitochondrial precursor
  88. Elongation factor Tu GTP-binding domain-containing protein 1
  89. GTPase activating protein and VPS9 domain-containing protein 1
  90. Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
  91. Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2
  92. Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3
  93. Guanine nucleotide-binding protein subunit beta-4
  94. Guanine nucleotide-binding protein subunit beta-5
  95. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10 precursor
  96. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12 precursor
  97. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13 precursor
  98. Guanine nucleotide-binding protein G(T) subunit gamma-T1 precursor
  99. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3 precursor
  100. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-4 precursor
  101. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5 precursor
  102. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7 precursor
  103. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-8 precursor
  104. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-T2 precursor
  105. HECT domain and RCC1-like domain-containing protein 1
  106. Eukaryotic translation initiation factor 5
  107. IQ motif and Sec7 domain-containing protein 1
  108. MAP kinase-activating death domain protein
  109. Guanine nucleotide exchange factor DBS
  110. Ras-related protein Rab-5A
  111. Ras-related protein Rab-5B
  112. Ran-binding protein 3
  113. Ral guanine nucleotide dissociation stimulator-like 2
  114. Ral guanine nucleotide dissociation stimulator-like 3
  115. Synembryn-A
  116. Ras and Rab interactor 1
  117. Ras and Rab interactor 2
  118. Ras and Rab interactor 3
  119. GTP-binding protein Rit1
  120. GTP-binding protein Rit2
  121. Rap guanine nucleotide exchange factor 5
  122. Ras-related GTP-binding protein A
  123. Ras-related GTP-binding protein B
  124. Ras-related GTP-binding protein C
  125. Ras-related GTP-binding protein D
  126. Secretion-regulating guanine nucleotide exchange factor
  127. KIAA2016 protein
  128. Protein XRP2
  129. Putative nucleoside diphosphate kinase
  130. Probable 7,8-dihydro-8-oxoguanine triphosphatase NUDT15
  131. Putative nucleoside diphosphate-linked moiety X motif 17, mitochondrial precursor
  132. Nucleoside diphosphate-linked moiety X motif 18
  133. Nucleoside diphosphate-linked moiety X motif 8, mitochondrial precursor
  134. GDP-fucose protein O-fucosyltransferase 1 precursor
  135. Not Available
  136. 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)
  137. Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
  138. Putative uncharacterized protein DKFZp761J1915 (Ectonucleoside triphosphate diphosphohydrolase 6 (Putative function), isoform CRA_a)
  139. Ectonucleoside triphosphate diphosphohydrolase 5 (Ectonucleoside triphosphate diphosphohydrolase 5, isoform CRA_d)
  140. cDNA FLJ78078, highly similar to Human alpha (1,3/1,4) fucosyltransferase (FUT3) (Fucosyltransferase 3) (Galactoside 3(4)-L- fucosyltransferase, Lewis blood group)
  141. Alpha-(1,3)-fucosyltransferase
  142. cDNA FLJ75308, highly similar to Human alpha(1,2)fucosyltransferase (FUT2) gene (HCG1998026, isoform CRA_a)
  143. cDNA FLJ76814, highly similar to Homo sapiens dynamin 1-like (DNM1L), transcript variant 3, mRNA
  144. cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
  145. cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
  146. Adenylosuccinate synthetase
  147. Eukaryotic translation elongation factor 1 alpha 2
  148. EEF2 protein (Eukaryotic translation elongation factor 2, isoform CRA_a)
  149. GDP-fucose protein O-fucosyltransferase 2
  150. Guanine nucleotide-binding protein G(i), alpha-1 subunit
  151. Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas
  152. Guanine nucleotide exchange factor VAV2
  153. Rho-guanine nucleotide exchange factor
  154. Ras guanyl-releasing protein 3
  155. Protein RCC2
  156. Protein very KIND
  157. Nucleoside diphosphate kinase
  158. Guanine nucleotide binding protein (G protein), gamma transducing activity polypeptide 1
  159. Abl interactor 1
  160. GTP-binding protein SAR1b
  161. Ras-GEF domain-containing family member 1A
  162. G-protein-signaling modulator 1
  163. GTP-binding protein GEM
  164. Rap guanine nucleotide exchange factor-like 1
  165. Guanine nucleotide binding protein-like 1
  166. Rho guanine nucleotide exchange factor 6
  167. Guanine nucleotide binding protein (G protein), alpha 13, isoform CRA_a
  168. cDNA, FLJ92996, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta polypeptide 1 (GNB1), mRNA
  169. Guanine nucleotide-binding protein subunit alpha-14
  170. PH and SEC7 domain-containing protein 4
  171. Rho guanine nucleotide exchange factor 9
  172. Guanine nucleotide-binding protein G(k) subunit alpha
  173. Epithelial cell transforming sequence 2 oncogene-like
  174. cDNA, FLJ95645, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta 5(GNB5), transcript variant 1, mRNA
  175. Pleckstrin homology domain-containing family G member 6
  176. Guanine nucleotide-binding protein G(i), alpha-2 subunit
  177. cDNA FLJ78228, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta 5(GNB5), transcript variant 1, mRNA
  178. Guanine nucleotide binding protein (G protein), beta polypeptide 1
  179. Guanine nucleotide-binding protein G(t) subunit alpha-2
  180. Probable guanine nucleotide exchange factor FLJ41603
  181. PH and SEC7 domain-containing protein 3
  182. PH and SEC7 domain-containing protein 1
  183. Guanine nucleotide-binding protein G(o) subunit alpha
  184. Ras-GEF domain-containing family member 1B
  185. Rho guanine nucleotide exchange factor 18
  186. ALS2 C-terminal-like protein
  187. Switch-associated protein 70
  188. Ras-specific guanine nucleotide-releasing factor RalGPS2
  189. FERM, RhoGEF and pleckstrin domain-containing protein 2
  190. Ral guanine nucleotide dissociation stimulator-like 1
  191. Guanine nucleotide-binding protein subunit alpha-13
  192. Vav-like protein C9orf100
  193. Probable guanine nucleotide exchange factor MCF2L2
  194. Rho guanine nucleotide exchange factor 7
  195. Guanine nucleotide binding protein (G protein), alpha 14
  196. Guanine nucleotide binding protein-like 1
  197. cDNA FLJ78702, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), alpha activating activity polypeptide, olfactory type (GNAL), transcript variant 2, mRNA
  198. Guanine nucleotide-binding protein subunit alpha-12
  199. Ras-specific guanine nucleotide-releasing factor RalGPS1
  200. Rho guanine nucleotide exchange factor 11
  201. cDNA FLJ76843, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), alpha 15 (Gq class) (GNA15), mRNA
  202. Growth factor receptor-bound protein 2
  203. Guanine nucleotide binding protein (G protein), beta polypeptide 1
  204. Rho guanine nucleotide exchange factor 10-like protein
  205. Guanine nucleotide binding protein (G protein), q polypeptide
  206. Protein SOLO
  207. Prolactin regulatory element-binding protein
  208. Rho guanine nucleotide exchange factor 4
  209. cDNA FLJ11028 fis, clone PLACE1004128, highly similar to Guanine nucleotide-binding protein subunit beta 4
  210. Guanine nucleotide exchange factor for Rab3A
  211. cDNA FLJ77654, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta polypeptide 4 (GNB4), mRNA
  212. Guanine nucleotide binding protein-like 1
  213. Engulfment and cell motility protein 1
  214. GRB2-related adapter protein
  215. Guanine nucleotide-binding protein G(z) subunit alpha
  216. Engulfment and cell motility protein 3
  217. Guanine nucleotide exchange factor GEFT
  218. Differentially expressed in FDCP 6 homolog
  219. Alpha-catulin
  220. Guanine nucleotide binding protein (G protein), beta polypeptide 1
  221. IQ motif and SEC7 domain-containing protein 3
  222. Engulfment and cell motility protein 2
  223. Rho guanine nucleotide exchange factor 17
  224. Ras-GEF domain-containing family member 1C
  225. Rho guanine nucleotide exchange factor 12
  226. Ephexin-1
  227. Guanine nucleotide binding protein-like 1
  228. Guanine nucleotide-binding protein G(olf) subunit alpha
  229. Guanine nucleotide-binding protein subunit alpha-15
  230. 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
  3. ATPDase
  4. Lymphoid cell activation antigen
  5. Ecto-apyrase
  6. 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 57965
Enzyme 1 Theoretical pI 6.29
Enzyme 1 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 1 General Function Not Available
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
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 765256 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 S73813 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 10
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. 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]
  5. 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]
  6. 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]
  7. Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed Link Image]
  8. 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]
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 NF-kappa-B-activating protein 107
  4. Putative MAPK-activating protein PM09
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 44840
Enzyme 2 Theoretical pI 5.98
Enzyme 2 GO Classification Not Available
Enzyme 2 General Function Not Available
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
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 22218108 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 >1116 bp
ATGACCAAGGCCGCGGACCCCCGCTTCCGCCCCCGCTGGAAGGTGATCCTGACGTTCTTT
GTGGGTGCTGCCATCCTCTGGCTGCTCTGCTCCCACCGCCCGGCCCCCGGCAGGCCCCCC
ACCCACAATGCACACAACTGGAGGCTCGGCCAGGCGCCCGCCAACTGGTACAATGACACC
TACCCCCTGTCTCCCCCACAAAGGACACCGGCTGGGATTCGGTATCGAATCGCAGTTATC
GCAGACCTGGACACAGAGTCAAGGGCCCAAGAGGAAAACACCTGGTTCAGTTACCTGAAA
AAGGGCTACCTGACCCTGTCAGACAGTGGGGACAAGGTGGCCGTGGAATGGGACAAAGAC
CATGGGGTCCTGGAGTCCCACCTGGCGGAGAAGGGGAGAGGCATGGAGCTATCCGACCTG
ATTGTTTTCAATGGGAAACTCTACTCCGTGGATGACCGGACGGGGGTCGTCTACCAGATC
GAAGGCAGCAAAGCCGTGCCCTGGGTGATTCTGTCCGACGGCGACGGCACCGTGGAGAAA
GGCTTCAAGGCCGAATGGCTGGCAGTGAAGGACGAGCGTCTGTACGTGGGCGGCCTGGGC
AAGGAGTGGACGACCACTACGGGTGATGTGGTGAACGAGAACCCGGAGTGGGTGAAGGTG
GTGGGCTACAAGGGCAGCGTGGACCACGAGAACTGGGTGTCCAACTACAACGCCCTGCGG
GCTGCTGCCGGCATCCAGCCGCCAGGCTACCTCATCCATGAGTCTGCCTGCTGGAGTGAC
ACGCTGCAGCGCTGGTTCTTCCTGCCGCGCCGCGCCAGCCAGGAGCGCTACAGCGAGAAG
GACGACGAGCGCAAGGGCGCCAACCTGCTGCTGAGCGCCTCCCCTGACTTCGGCGACATC
GCTGTGAGCCACGTCGGGGCGGTGGTCCCCACTCACGGCTTCTCGTCCTTCAAGTTCATC
CCCAACACCGACGACCAGATCATTGTGGCCCTCAAATCCGAGGAGGACAGCGGCAGAGTC
GCCTCCTACATCATGGCCTTCACGCTGGACGGGCGCTTCCTGTTGCCGGAGACCAAGATC
GGAAGCGTGAAATACGAAGGCATCGAGTTCATTTAA
Enzyme 2 GenBank Gene ID AF328554 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 17
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. 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]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5338
Enzyme 3 Name Nucleoside diphosphate kinase, mitochondrial precursor
Enzyme 3 Synonyms
  1. NDP kinase, mitochondrial
  2. NDK
  3. nm23-H4
  4. Nucleoside diphosphate kinase D
  5. NDPKD
Enzyme 3 Gene Name NME4
Enzyme 3 Protein Sequence >Nucleoside diphosphate kinase, mitochondrial precursor
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
Enzyme 3 Number of Residues 187
Enzyme 3 Molecular Weight 20659
Enzyme 3 Theoretical pI 10.75
Enzyme 3 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 3 General Function Nucleotide transport and metabolism
Enzyme 3 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-15
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 1945762 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O00746 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name NDKM_HUMAN Link Image
Enzyme 3 PDB ID 1EHW Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >564 bp
ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCA
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
Enzyme 3 GenBank Gene ID Y07604 Link Image
Enzyme 3 GeneCard ID NME4 Link Image
Enzyme 3 GenAtlas ID NME4 Link Image
Enzyme 3 HGNC ID HGNC:7852 Link Image
Enzyme 3 Chromosome Location 16
Enzyme 3 Locus 16p13.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 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. 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]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5340
Enzyme 4 Name Ribonucleoside-diphosphate reductase large subunit
Enzyme 4 Synonyms
  1. Ribonucleoside-diphosphate reductase M1 subunit
  2. Ribonucleotide reductase large chain
Enzyme 4 Gene Name RRM1
Enzyme 4 Protein Sequence >Ribonucleoside-diphosphate reductase large subunit
MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLA
AETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKST
LDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHK
EDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCAL
ISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIY
LEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLD
EVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNL
GTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKI
IDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGAL
EASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIA
PMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQII
ACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKL
TSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCS
LENRDECLMCGS
Enzyme 4 Number of Residues 792
Enzyme 4 Molecular Weight 90071
Enzyme 4 Theoretical pI 7.16
Enzyme 4 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH2 groups
  • oxidoreductase activity, acting on CH2 groups, disulfide as acceptor
  • ribonucleoside-diphosphate reductase activity
Process
  • DNA metabolism
  • DNA replication
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • protein complex
  • ribonucleoside-diphosphate reductase complex
Enzyme 4 General Function Nucleotide transport and metabolism
Enzyme 4 Specific Function Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides
Enzyme 4 Pathways
Enzyme 4 Reactions
  • 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 36065 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P23921 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name RIR1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 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 4 GenBank Gene ID X59543 Link Image
Enzyme 4 GeneCard ID RRM1 Link Image
Enzyme 4 GenAtlas ID RRM1 Link Image
Enzyme 4 HGNC ID HGNC:10451 Link Image
Enzyme 4 Chromosome Location 11
Enzyme 4 Locus 11p15.5
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 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. 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]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5341
Enzyme 5 Name Nucleoside diphosphate kinase A
Enzyme 5 Synonyms
  1. NDK A
  2. NDP kinase A
  3. Tumor metastatic process-associated protein
  4. Metastasis inhibition factor nm23
  5. nm23-H1
  6. Granzyme A-activated DNase
  7. GAAD
Enzyme 5 Gene Name NME1
Enzyme 5 Protein Sequence >Nucleoside diphosphate kinase A
MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
Enzyme 5 Number of Residues 152
Enzyme 5 Molecular Weight 17149
Enzyme 5 Theoretical pI 6.11
Enzyme 5 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 5 General Function Nucleotide transport and metabolism
Enzyme 5 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 35068 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P15531 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name NDKA_HUMAN Link Image
Enzyme 5 PDB ID 1JXV Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >543 bp
TGCTGCGAACCACGTGGGTCCCGGGCGCGTTTCGGGTGCTGGCGGCTGCAGCCGGAGTTC
AAACCTAAGCAGCTGGAAGGAACCATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAA
CCAGATGGGGTCCAGCGGGGTCTTGTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGA
TTCCGCCTTGTTGGTCTGAAATTCATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTAC
GTTGACCTGAAGGACCGTCCATTCTTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCG
GTAGTTGCCATGGTCTGGGAGGGGCTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGG
GAGACCAACCCTGCAGACTCCAAGCCTGGGACCATCCGTGGAGACTTCTGCATACAAGTT
GGCAGGAACATTATACATGGCAGTGATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTG
TGGTTTCACCCTGAGGAACTGGTAGATTACACGAGCTGTGCTCAGAACTGGATCTATGAA
TGA
Enzyme 5 GenBank Gene ID X17620 Link Image
Enzyme 5 GeneCard ID NME1 Link Image
Enzyme 5 GenAtlas ID NME1 Link Image
Enzyme 5 HGNC ID HGNC:7849 Link Image
Enzyme 5 Chromosome Location 17
Enzyme 5 Locus 17q21.3
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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. 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]
  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. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5342
Enzyme 6 Name Nucleoside diphosphate kinase 7
Enzyme 6 Synonyms
  1. NDK 7
  2. NDP kinase 7
  3. nm23-H7
Enzyme 6 Gene Name NME7
Enzyme 6 Protein Sequence >Nucleoside diphosphate kinase 7
MNHSERFVFIAEWYDPNASLLRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYDNLHLEDL
FIGNKVNVFSRQLVLIDYGDQYTARQLGSRKEKTLALIKPDAISKAGEIIEIINKAGFTI
TKLKMMMLSRKEALDFHVDHQSRPFFNELIQFITTGPIIAMEILRDDAICEWKRLLGPAN
SGVARTDASESIRALFGTDGIRNAAHGPDSFASAAREMELFFPSSGGCGPANTAKFTNCT
CCIVKPHAVSEGLLGKILMAIRDAGFEISAMQMFNMDRVNVEEFYEVYKGVVTEYHDMVT
EMYSGPCVAMEIQQNNATKTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLP
EDGLLEVQYFFKILDN
Enzyme 6 Number of Residues 376
Enzyme 6 Molecular Weight 42492
Enzyme 6 Theoretical pI 6.44
Enzyme 6 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 6 General Function Nucleotide transport and metabolism
Enzyme 6 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 6 Pathways
Enzyme 6 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 4960169 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q9Y5B8 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name NDK7_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1131 bp
ATGAATCATAGTGAAAGATTCGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
Enzyme 6 GenBank Gene ID AF153191 Link Image
Enzyme 6 GeneCard ID NME7 Link Image
Enzyme 6 GenAtlas ID NME7 Link Image
Enzyme 6 HGNC ID HGNC:20461 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 1q24
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5343
Enzyme 7 Name Ribonucleoside-diphosphate reductase M2 subunit
Enzyme 7 Synonyms
  1. Ribonucleotide reductase small subunit
  2. Ribonucleotide reductase small chain
Enzyme 7 Gene Name RRM2
Enzyme 7 Protein Sequence >Ribonucleoside-diphosphate reductase M2 subunit
MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKT
KAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLK
PEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLI
DTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSF
ASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIE
QEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTN
FFEKRVGEYQRMGVMSSPTENSFTLDADF
Enzyme 7 Number of Residues 389
Enzyme 7 Molecular Weight 44878
Enzyme 7 Theoretical pI 5.05
Enzyme 7 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH2 groups
  • oxidoreductase activity, acting on CH2 groups, disulfide as acceptor
  • ribonucleoside-diphosphate reductase activity
Process
  • cellular metabolism
  • deoxyribonucleoside diphosphate metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside diphosphate metabolism
  • nucleotide metabolism
  • physiological process
Component
Enzyme 7 General Function Nucleotide transport and metabolism
Enzyme 7 Specific Function Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides
Enzyme 7 Pathways
Enzyme 7 Reactions
  • 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 36155 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P31350 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name RIR2_HUMAN Link Image
Enzyme 7 PDB ID 1H0N Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 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 7 GenBank Gene ID X59618 Link Image
Enzyme 7 GeneCard ID RRM2 Link Image
Enzyme 7 GenAtlas ID RRM2 Link Image
Enzyme 7 HGNC ID HGNC:10452 Link Image
Enzyme 7 Chromosome Location 2
Enzyme 7 Locus 2p25-p24
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5344
Enzyme 8 Name Nucleoside diphosphate kinase B
Enzyme 8 Synonyms
  1. NDK B
  2. NDP kinase B
  3. nm23-H2
  4. C-myc purine-binding transcription factor PUF
Enzyme 8 Gene Name NME2
Enzyme 8 Protein Sequence >Nucleoside diphosphate kinase B
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
Enzyme 8 Number of Residues 152
Enzyme 8 Molecular Weight 17298
Enzyme 8 Theoretical pI 8.69
Enzyme 8 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 8 General Function Nucleotide transport and metabolism
Enzyme 8 Specific Function Acts as a transcriptional activator of the c-Myc gene; binds DNA nonspecifically (Ref.3)
Enzyme 8 Pathways
Enzyme 8 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 4467843 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P22392 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name NDKB_HUMAN Link Image
Enzyme 8 PDB ID 1NSK Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >459 bp
ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
Enzyme 8 GenBank Gene ID X58965 Link Image
Enzyme 8 GeneCard ID NME2 Link Image
Enzyme 8 GenAtlas ID NME2 Link Image
Enzyme 8 HGNC ID HGNC:7850 Link Image
Enzyme 8 Chromosome Location 17
Enzyme 8 Locus 17q21.3
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. 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]
  2. 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]
  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. 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]
  5. 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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5345
Enzyme 9 Name Nucleoside diphosphate kinase 3
Enzyme 9 Synonyms
  1. NDK 3
  2. NDP kinase 3
  3. Nucleoside diphosphate kinase C
  4. NDPKC
  5. nm23-H3
  6. DR-nm23
Enzyme 9 Gene Name NME3
Enzyme 9 Protein Sequence >Nucleoside diphosphate kinase 3
MICLVLTIFANLFPAACTGAHERTFLAVKPDGVQRRLVGEIVRRFERKGFKLVALKLVQA
SEELLREHYAELRERPFYGRLVKYMASGPVVAMVWQGLDVVRTSRALIGATNPADAPPGT
IRGDFCIEVGKNLIHGSDSVESARREIALWFRADELLCWEDSAGHWLYE
Enzyme 9 Number of Residues 169
Enzyme 9 Molecular Weight 19015
Enzyme 9 Theoretical pI 7.97
Enzyme 9 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 9 General Function Nucleotide transport and metabolism
Enzyme 9 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 9 Pathways
Enzyme 9 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-19
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 1051256 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q13232 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name NDK3_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >507 bp
ATGATCTGCCTGGTGCTGACCATCTTCGCTAACCTCTTCCCCGCGGCCTGCACCGGCGCA
CACGAACGCACCTTCCTGGCCGTGAAGCCGGACGGCGTGCAGCGGCGGCTGGTGGGCGAG
ATTGTGCGGCGCTTCGAGAGGAAGGGCTTCAAGTTGGTGGCGCTGAAGCTGGTGCAGTCC
TCCGAGGAGCTGCTGCGTGAGCACTACGCCGAGCTGCGTGAACGCCCGTTCTACGGCCGC
CTTGTCAAGTATATGGCCTCCGGGCCGGTGGTGGCCATGGTTTGGCAGGGGCTGGACGTG
GTGCGCACCTCGCGGGCGCTCATCGGAGCCACGAACCCGGCCGACGCCCCGCCCGGCACC
ATCCGCGGGGATTTCTGCATCGAGGTTGGCAACCTGATTCACGGCAGCGACTCGGTGGAG
AGTGCCCGCCGCGAGATCGCTCTCTGGTTCCGCGCAGACGAGCTCCTCTGCTGGGAGGAC
AGCGCTGGGCACTGGCTGTATGAGTAG
Enzyme 9 GenBank Gene ID U29656 Link Image
Enzyme 9 GeneCard ID NME3 Link Image
Enzyme 9 GenAtlas ID NME3 Link Image
Enzyme 9 HGNC ID HGNC:7851 Link Image
Enzyme 9 Chromosome Location 16
Enzyme 9 Locus 16q13
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 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]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5346
Enzyme 10 Name Nucleoside diphosphate kinase 6
Enzyme 10 Synonyms
  1. NDK 6
  2. NDP kinase 6
  3. nm23-H6
  4. Inhibitor of p53-induced apoptosis-alpha
  5. IPIA-alpha
Enzyme 10 Gene Name NME6
Enzyme 10 Protein Sequence >Nucleoside diphosphate kinase 6
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA
Enzyme 10 Number of Residues 186
Enzyme 10 Molecular Weight 21142
Enzyme 10 Theoretical pI 8.49
Enzyme 10 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 10 General Function Nucleotide transport and metabolism
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. Inhibitor of p53-induced apoptosis
Enzyme 10 Pathways
Enzyme 10 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-24
Enzyme 10 Transmembrane Regions Not Available
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 3228530 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID O75414 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name NDK6_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >561 bp
ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA
Enzyme 10 GenBank Gene ID AF051941 Link Image
Enzyme 10 GeneCard ID NME6 Link Image
Enzyme 10 GenAtlas ID NME6 Link Image
Enzyme 10 HGNC ID HGNC:20567 Link Image
Enzyme 10 Chromosome Location 3
Enzyme 10 Locus 3p21
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 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]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5486
Enzyme 11 Name Fucose-1-phosphate guanylyltransferase
Enzyme 11 Synonyms
  1. GDP-L-fucose pyrophosphorylase
  2. GDP-L-fucose diphosphorylase
Enzyme 11 Gene Name FPGT
Enzyme 11 Protein Sequence >Fucose-1-phosphate guanylyltransferase
MAAARDPPEVSLREATQRKLRRFSELRGKLVARGEFWDIVAITAADEKQELAYNQQLSEK
LKRKELPLGVQYHVFVDPAGAKIGNGGSTLCALQCLEKLYGDKWNSFTILLIHSGGYSQR
LPNASALGKIFTALPLGNPIYQMLELKLAMYIDFPLNMNPGILVTCADDIELYSIGEFEF
IRFDKPGFTALAHPSSLTIGTTHGVFVLDPFDDLKHRDLEYRSCHRFLHKPSIEKMYQFN
AVCRPGNFCQQDFAGGDIADLKLDSDYVYTDSLFYMDHKSAKMLLAFYEKIGTLSCEIDA
YGDFLQALGPGATVEYTRNTSNVIKEESELVEMRQRIFHLLKGTSLNVVVLNNSKFYHIG
TTEEYLFYFTSDNSLKSELGLQSITFSIFPDIPECSGKTSCIIQSILDSRCSVAPGSVVE
YSRLGPDVSVGENCIISGSYILTKAALPAHSFVCSLSLKMNRCLKYATMAFGVQDNLKKS
VKTLSDIKLLQFFGVCFLSCLDVWNLKVTEELFSGNKTCLSLWTARIFPVCSSLSDSVIT
SLKMLNAVKNKSAFSLNSYKLLSIEEMLIYKDVEDMITYREQIFLEISLKSSLM
Enzyme 11 Number of Residues 594
Enzyme 11 Molecular Weight 66600
Enzyme 11 Theoretical pI 6.44
Enzyme 11 GO Classification Not Available
Enzyme 11 General Function Not Available
Enzyme 11 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 11 Pathways
Enzyme 11 Reactions
  • GTP + beta-L-fucose 1-phosphate = diphosphate + GDP-L-fucose
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 2582185 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID O14772 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name FPGT_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 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 11 GenBank Gene ID AF017445 Link Image
Enzyme 11 GeneCard ID FPGT Link Image
Enzyme 11 GenAtlas ID FPGT Link Image
Enzyme 11 HGNC ID HGNC:3825 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 1p31.1
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 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]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5620
Enzyme 12 Name Alpha-1,3-mannosyltransferase ALG2
Enzyme 12 Synonyms
  1. GDP- Man:Man(1GlcNAc(2-PP-dolichol mannosyltransferase
Enzyme 12 Gene Name ALG2
Enzyme 12 Protein Sequence >Alpha-1,3-mannosyltransferase ALG2
MAEEQGRERDSVPKPSVLFLHPDLGVGGAERLVLDAALALQARGCSVKIWTAHYDPGHCF
AESRELPVRCAGDWLPRGLGWGGRGAAVCAYVRMVFLALYVLFLADEEFDVVVCDQVSAC
IPVFRLARRRKKILFYCHFPDLLLTKRDSFLKRLYRAPIDWIEEYTTGMADCILVNSQFT
AAVFKETFKSLSHIDPDVLYPSLNVTSFDSVVPEKLDDLVPKGKKFLLLSINRYERKKNL
TLALEALVQLRGRLTSQDWERVHLIVAGGYDERVLENVEHYQELKKMVQQSDLGQYVTFL
RSFSDKQKISLLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGF
LCEPDPVHFSEAIEKFIREPSLKATMGLAGRARVKEKFSPEAFTEQLYRYVTKLLV
Enzyme 12 Number of Residues 416
Enzyme 12 Molecular Weight 47092
Enzyme 12 Theoretical pI 7.05
Enzyme 12 GO Classification
Function
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 12 General Function Cell wall/membrane/envelope biogenesis
Enzyme 12 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 12 Pathways Not Available
Enzyme 12 Reactions Not Available
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • 85-105
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 44885912 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q9H553 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name ALG2_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 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 12 GenBank Gene ID AB161356 Link Image
Enzyme 12 GeneCard ID ALG2 Link Image
Enzyme 12 GenAtlas ID ALG2 Link Image
Enzyme 12 HGNC ID HGNC:23159 Link Image
Enzyme 12 Chromosome Location 9
Enzyme 12 Locus 9q22.33
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 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]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5621
Enzyme 13 Name Dolichol-phosphate mannosyltransferase
Enzyme 13 Synonyms
  1. Dolichol- phosphate mannose synthase
  2. Dolichyl-phosphate beta-D- mannosyltransferase
  3. Mannose-P-dolichol synthase
  4. MPD synthase
  5. DPM synthase
Enzyme 13 Gene Name DPM1
Enzyme 13 Protein Sequence >Dolichol-phosphate mannosyltransferase
MASLEVSRSPRRSRRELEVRSPRQNKYSVLLPTYNERENLPLIVWLLVKSFSESGINYEI
IIIDDGSPDGTRDVAEQLEKIYGSDRILLRPREKKLGLGTAYIHGMKHATGNYIIIMDAD
LSHHPKFIPEFIRKQKEGNFDIVSGTRYKGNGGVYGWDLKRKIISRGANFLTQILLRPGA
SDLTGSFRLYRKEVLEKLIEKCVSKGYVFQMEMIVRARQLNYTIGEVPISFVDRVYGESK
LGGNEIVSFLKGLLTLFATT
Enzyme 13 Number of Residues 260
Enzyme 13 Molecular Weight 29635
Enzyme 13 Theoretical pI 10.02
Enzyme 13 GO Classification Not Available
Enzyme 13 General Function Cell wall/membrane/envelope biogenesis
Enzyme 13 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 13 Pathways
Enzyme 13 Reactions
  • GDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl phosphate
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 3062806 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID O60762 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name DPM1_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >783 bp
ATGGCCTCCTTGGAAGTCAGTCGTAGTCCTCGCAGGTCTCGGCGGGAGCTGGAAGTGCGC
AGTCCACGACAGAACAAATATTCGGTGCTTTTACCTACCTACAACGAGCGCGAGAACCTG
CCGCTCATCGTGTGGCTGCTGGTGAAAAGCTTCTCCGAGAGTGGAATCAACTATGAAATT
ATAATCATAGATGATGGAAGCCCAGATGGAACAAGGGATGTTGCTGAACAGTTGGAGAAG
ATCTATGGGTCAGACAGAATTCTTCTAAGACCACGAGAGAAAAAGTTGGGACTAGGAACT
GCATATATTCATGGAATGAAACATGCCACAGGAAACTACATCATTATTATGGATGCTGAT
CTCTCACACCATCCAAAATTTATTCCTGAATTTATTAGGAAGCAAAAGGAGGGTAATTTT
GATATTGTCTCTGGAACTCGCTACAAAGGAAATGGAGGTGTATATGGCTGGGATTTGAAA
AGAAAAATAATCAGCCGTGGGGCCAATTTTTTAACTCAGATCTTGCTGAGACCAGGAGCA
TCTGATTTAACAGGAAGTTTCAGATTATACCGAAAAGAAGTTCTAGAGAAATTAATAGAA
AAATGTGTTTCTAAAGGCTACGTCTTCCAGATGGAGATGATTGTTCGGGCAAGACAGTTG
AATTATACTATTGGCGAGGTTCCAATATCATTTGTGGATCGTGTTTATGGTGAATCCAAG
TTGGGAGGAAATGAAATAGTATCTTTCTTGAAAGGATTATTGACTCTTTTTGCTACTACA
TAA
Enzyme 13 GenBank Gene ID D86198 Link Image
Enzyme 13 GeneCard ID DPM1 Link Image
Enzyme 13 GenAtlas ID DPM1 Link Image
Enzyme 13 HGNC ID HGNC:3005 Link Image
Enzyme 13 Chromosome Location 20
Enzyme 13 Locus 20q13.13
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 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. 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. 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]
  4. 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]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5622
Enzyme 14 Name GDP-mannose 4,6 dehydratase
Enzyme 14 Synonyms
  1. GDP-D-mannose dehydratase
  2. GMD
Enzyme 14 Gene Name GMDS
Enzyme 14 Protein Sequence >GDP-mannose 4,6 dehydratase
MAHAPARCPSARGSGDGEMGKPRNVALITGITGQDGSYLAEFLLEKGYEVHGIVRRSSSF
NTGRIEHLYKNPQAHIEGNMKLHYGDLTDSTCLVKIINEVKPTEIYNLGAQSHVKISFDL
AEYTADVDGVGTLRLLDAVKTCGLINSVKFYQASTSELYGKVQEIPQKETTPFYPRSPYG
AAKLYAYWIVVNFREAYNLFAVNGILFNHESPRRGANFVTRKISRSVAKIYLGQLECFSL
GNLDAKRDWGHAKDYVEAMWLMLQNDEPEDFVIATGEVHSVREFVEKSFLHIGKTIVWEG
KNENEVGRCKETGKVHVTVDLKYYRPTEVDFLQGDCTKAKQKLNWKPRVAFDELVREMVH
ADVELMRTNPNA
Enzyme 14 Number of Residues 372
Enzyme 14 Molecular Weight 41950
Enzyme 14 Theoretical pI 7.35
Enzyme 14 GO Classification
Function
  • GDP-mannose 4,6-dehydratase activity
  • NAD binding
  • binding
  • carbon-oxygen lyase activity
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • hydro-lyase activity
  • lyase activity
Process
  • biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide-sugar metabolism
  • physiological process
Component
Enzyme 14 General Function Cell wall/membrane/envelope biogenesis
Enzyme 14 Specific Function Conversion of GDP-D-mannose to GDP-4-keto-6-D- deoxymannose
Enzyme 14 Pathways
Enzyme 14 Reactions
  • GDP-mannose = GDP-4-dehydro-6-deoxy-D-mannose + H2O
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 3005057 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID O60547 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name GMDS_HUMAN Link Image
Enzyme 14 PDB ID 1T2A Link Image
Enzyme 14 PDB File Show
Enzyme 14 3D Structure
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1119 bp
ATGGCACACGCACCGGCACGCTGCCCCAGCGCCCGGGGCTCCGGGGACGGCGAGATGGGC
AAGCCCAGGAACGTGGCGCTCATCACCGGTATCACAGGCCAGGATGGTTCCTACCTGGCT
GAGTTCCTGCTGGAGAAAGGCTATGAGGTCCATGGAATTGTACGGCGGTCCAGTTCATTT
AATACGGGTCGAATTGAGCATCTGTATAAGAATCCCCAGGCTCACATTGAAGGAAACATG
AAGTTGCACTATGGCGATCTCACTGACAGTACCTGCCTTGTGAAGATCATTAATGAAGTA
AAGCCCACAGAGATCTACAACCTTGGAGCCCAGAGCCACGTCAAAATTTCCTTTGACCTC
GCTGAGTACACTGCGGACGTTGACGGAGTTGGCACTCTACGACTTCTAGATGCAGTTAAG
ACTTGTGGCCTTATCAACTCTGTGAAGTTCTACCAAGCCTCAACAAGTGAACTTTATGGG
AAAGTGCAGGAAATACCCCAGAAGGAGACCACCCCTTTCTATCCCCGGTCACCCTATGGG
GCAGCAAAACTCTATGCCTATTGGATTGTGGTGAACTTCCGTGAGGCGTATAATCTCTTT
GCAGTGAACGGCATTCTCTTCAATCATGAGAGTCCCAGAAGAGGAGCTAATTTCGTTACT
CGAAAAATTAGCCGGTCAGTAGCTAAGATTTACCTTGGACAACTGGAATGTTTCAGTTTG
GGAAATCTGGATGCCAAACGAGATTGGGGCCATGCCAAGGACTATGTGGAGGCTATGTGG
TTGATGTTGCAGAATGATGAGCCGGAGGACTTCGTTATAGCTACTGGGGAGGTCCATAGT
GTCCGGGAATTTGTCGAGAAATCATTCTTGCACATTGGAAAAACCATTGTGTGGGAAGGA
AAGAATGAAAATGAAGTGGGCAGATGTAAAGAGACCGGCAAAGTTCACGTGACTGTGGAT
CTCAAGTACTACCGGCCAACTGAAGTGGACTTTCTGCAGGGCGACTGCACCAAAGCGAAA
CAGAAGCTGAACTGGAAGCCCCGGGTCGCTTTCGATGAGCTGGTGAGGGAGATGGTGCAC
GCCGACGTGGAGCTCATGAGGACAAACCCCAATGCCTGA
Enzyme 14 GenBank Gene ID AF042377 Link Image
Enzyme 14 GeneCard ID GMDS Link Image
Enzyme 14 GenAtlas ID GMDS Link Image
Enzyme 14 HGNC ID HGNC:4369 Link Image
Enzyme 14 Chromosome Location 6
Enzyme 14 Locus 6p25
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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. 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]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5706
Enzyme 15 Name Galactoside 2-alpha-L-fucosyltransferase 2
Enzyme 15 Synonyms
  1. GDP-L- fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 2
  2. Alpha(1,2FT 2
  3. Fucosyltransferase 2
  4. Secretor blood group alpha-2- fucosyltransferase
  5. Secretor factor
  6. Se
  7. SE2
Enzyme 15 Gene Name FUT2
Enzyme 15 Protein Sequence >Galactoside 2-alpha-L-fucosyltransferase 2
MLVVQMPFSFPMAHFILFVFTVSTIFHVQQRLAKIQAMWELPVQIPVLASTSKALGPSQL
RGMWTINAIGRLGNQMGEYATLYALAKMNGRPAFIPAQMHSTLAPIFRITLPVLHSATAS
RIPWQNYHLNDWMEEEYRHIPGEYVRFTGYPCSWTFYHHLRQEILQEFTLHDHVREEAQK
FLRGLQVNGSRPGTFVGVHVRRGDYVHVMPKVWKGVVADRRYLQQALDWFRARYSSLIFV
VTSNGMAWCRENIDTSHGDVVFAGDGIEGSPAKDFALLTQCNHTIMTIGTFGIWAAYLTG
GDTIYLANYTLPDSPFLKIFKPEAAFLPEWTGIAADLSPLLKH
Enzyme 15 Number of Residues 343
Enzyme 15 Molecular Weight 39018
Enzyme 15 Theoretical pI 8.73
Enzyme 15 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 metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
  • Golgi apparatus
  • cell
  • intracellular membrane-bound organelle
  • membrane
  • membrane-bound organelle
  • organelle
Enzyme 15 General Function Not Available
Enzyme 15 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 15 Pathways
  • Blood group glycolipid biosynthesis-neolactoseries (map00602 Link Image)
  • Globoside metabolism (map00603 Link Image)
  • Glycosphingolipid biosynthesis - lactoseries (map00601 Link Image)
Enzyme 15 Reactions
  • GDP-beta-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-24
Enzyme 15 Transmembrane Regions Not Available
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 687619 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q10981 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name FUT2_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1032 bp
ATGCTGGTCGTTCAGATGCCTTTCTCCTTTCCCATGGCCCACTTCATCCTCTTTGTCTTT
ACGGTTTCCACTATATTTCACGTTCAGCAGCGGCTAGCGAAGATTCAAGCCATGTGGGAG
TTACCGGTGCAGATACCAGTGCTAGCCTCAACATCAAAGGCACTGGGACCCAGCCAGCTC
AGGGGGATGTGGACGATCAATGCAATAGGCCGCCTGGGGAACCAGATGGGCGAGTACGCC
ACACTGTACGCCCTGGCCAAGATGAACGGGCGGCCCGCCTTCATCCCGGCCCAGATGCAC
AGCACCCTGGCCCCCATCTTCAGAATCACCCTGCCGGTGCTGCACAGCGCCACGGCCAGC
AGGATCCCCTGGCAGAACTACCACCTGAACGACTGGATGGAGGAGGAATACCGCCACATC
CCGGGGGAGTACGTCCGCTTCACCGGCTACCCCTGCTCCTGGACCTTCTACCACCACCTC
CGCCAGGAGATCCTCCAGGAGTTCACCCTGCACGACCACGTGCGGGAGGAGGCCCAGAAG
TTCCTGCGGGGCCTGCAGGTGAACGGGAGCCGGCCGGGCACCTTTGTAGGGGTCCATGTT
CGCCGAGGGGACTATGTCCATGTCATGCCAAAAGTGTGGAAGGGGGTGGTGGCCGACCGG
CGATACCTACAGCAGGCCCTGGACTGGTTCCGAGCTCGCTACAGCTCCCTCATCTTCGTG
GTCACCAGTAATGGCATGGCCTGGTGTCGGGAGAACATTGACACCTCCCACGGTGATGTG
GTGTTTGCTGGCGATGGCATTGAGGGCTCACCTGCCAAAGATTTTGCTCTACTCACACAG
TGTAACCACACCATCATGACCATTGGGACGTTCGGGATCTGGGCCGCATACCTCACGGGC
GGAGACACCATCTACCTGGCCAATTACACCCTCCCCGACTCCCCTTTCCTCAAAATCTTT
AAGCCAGAGGCAGCCTTCCTGCCGGAGTGGACAGGGATTGCCGCAGACCTGTCCCCCTTA
CTCAAGCACTAA
Enzyme 15 GenBank Gene ID U17894 Link Image
Enzyme 15 GeneCard ID FUT2 Link Image
Enzyme 15 GenAtlas ID FUT2 Link Image
Enzyme 15 HGNC ID HGNC:4013 Link Image
Enzyme 15 Chromosome Location 19
Enzyme 15 Locus 19q13.3
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 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. 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]
  5. 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]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5707
Enzyme 16 Name Galactoside 2-alpha-L-fucosyltransferase 1
Enzyme 16 Synonyms
  1. GDP-L- fucose:beta-D-galactoside 2-alpha-L-fucosyltransferase 1
  2. Alpha(1,2FT 1
  3. Fucosyltransferase 1
  4. Blood group H alpha 2- fucosyltransferase
Enzyme 16 Gene Name FUT1
Enzyme 16 Protein Sequence >Galactoside 2-alpha-L-fucosyltransferase 1
MWLRSHRQLCLAFLLVCVLSVIFFLHIHQDSFPHGLGLSILCPDRRLVTPPVAIFCLPGT
AMGPNASSSCPQHPASLSGTWTVYPNGRFGNQMGQYATLLALAQLNGRRAFILPAMHAAL
APVFRITLPVLAPEVDSRTPWRELQLHDWMSEEYADLRDPFLKLSGFPCSWTFFHHLREQ
IRREFTLHDHLREEAQSVLGQLRLGRTGDRPRTFVGVHVRRGDYLQVMPQRWKGVVGDSA
YLRQAMDWFRARHEAPVFVVTSNGMEWCKENIDTSQGDVTFAGDGQEATPWKDFALLTQC
NHTIMTIGTFGFWAAYLAGGDTVYLANFTLPDSEFLKIFKPEAAFLPEWVGINADLSPLW
TLAKP
Enzyme 16 Number of Residues 365
Enzyme 16 Molecular Weight 41252
Enzyme 16 Theoretical pI 7.38
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 metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
  • Golgi apparatus
  • cell
  • intracellular membrane-bound organelle
  • membrane
  • membrane-bound organelle
  • organelle
Enzyme 16 General Function Not Available
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-R = GDP + alpha-L-fucosyl-1,2-beta-D-galactosyl-R
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-24
Enzyme 16 Transmembrane Regions Not Available
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 306830 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID P19526 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name FUT1_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1098 bp
ATGTGGCTCCGGAGCCATCGTCAGCTCTGCCTGGCCTTCCTGCTAGTCTGTGTCCTCTCT
GTAATCTTCTTCCTCCATATCCATCAAGACAGCTTTCCACATGGCCTAGGCCTGTCGATC
CTGTGTCCAGACCGCCGCCTGGTGACACCCCCAGTGGCCATCTTCTGCCTGCCGGGTACT
GCGATGGGCCCCAACGCCTCCTCTTCCTGTCCCCAGCACCCTGCTTCCCTCTCCGGCACC
TGGACTGTCTACCCCAATGGCCGGTTTGGTAATCAGATGGGACAGTATGCCACGCTGCTG
GCTCTGGCCCAGCTCAACGGCCGCCGGGCCTTTATCCTGCCTGCCATGCATGCCGCCCTG
GCCCCGGTATTCCGCATCACCCTGCCCGTGCTGGCCCCAGAAGTGGACAGCCGCACGCCG
TGGCGGGAGCTGCAGCTTCACGACTGGATGTCGGAGGAGTACGCGGACTTGAGAGATCCT
TTCCTGAAGCTCTCTGGCTTCCCCTGCTCTTGGACTTTCTTCCACCATCTCCGGGAACAG
ATCCGCAGAGAGTTCACCCTGCACGACCACCTTCGGGAAGAGGCGCAGAGTGTGCTGGGT
CAGCTCCGCCTGGGCCGCACAGGGGACCGCCCGCGCACCTTTGTCGGCGTCCACGTGCGC
CGTGGGGACTATCTGCAGGTTATGCCTCAGCGCTGGAAGGGTGTGGTGGGCGACAGCGCC
TACCTCCGGCAGGCCATGGACTGGTTCCGGGCACGGCACGAAGCCCCCGTTTTCGTGGTC
ACCAGCAACGGCATGGAGTGGTGTAAAGAAAACATCGACACCTCCCAGGGCGATGTGACG
TTTGCTGGCGATGGACAGGAGGCTACACCGTGGAAAGACTTTGCCCTGCTCACACAGTGC
AACCACACCATTATGACCATTGGCACCTTCGGCTTCTGGGCTGCCTACCTGGCTGGCGGA
GACACTGTCTACCTGGCCAACTTCACCCTGCCAGACTCTGAGTTCCTGAAGATCTTTAAG
CCGGAGGCGGCCTTCCTGCCCGAGTGGGTGGGCATTAATGCAGACTTGTCTCCACTCTGG
ACATTGGCTAAGCCTTGA
Enzyme 16 GenBank Gene ID M35531 Link Image
Enzyme 16 GeneCard ID FUT1 Link Image
Enzyme 16 GenAtlas ID FUT1 Link Image
Enzyme 16 HGNC ID HGNC:4012 Link Image
Enzyme 16 Chromosome Location 19
Enzyme 16 Locus 19q13.3
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 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. 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]
  5. 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 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 6009
Enzyme 17 Name 6-phosphofructokinase type C
Enzyme 17 Synonyms
  1. Phosphofructokinase 1
  2. Phosphohexokinase
  3. Phosphofructo-1-kinase isozyme C
  4. PFK-C
  5. 6- phosphofructokinase, platelet type
Enzyme 17 Gene Name PFKP
Enzyme 17 Protein Sequence >6-phosphofructokinase type C
MDADDSRAPKGSLRKFLEHLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFI
YEGYQGMVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTREGRLKAACNLLQRGIT
NLCVIGGDGSLTGANLFRKEWSGLLEELARNGQIDKEAVQKYAYLNVVGMVGSIDNDFCG
TDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLP
ESPPEEGWEEQMCVKLSENRARKKRLNIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDT
RVTILGHVQRGGTPSAFDRILASRMGVEAVIALLEATPDTPACVVSLNGNHAVRLPLMEC
VQMTQDVQKAMDERRFQDAVRLRGRSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVINVGA
PAAGMNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWTDVGGWTGQGGSILGTK
RVLPGKYLEEIATQMRTHSINALLIIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVS
NNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGA
DAAYIFEEPFDIRDLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKG
VFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKEARGRGKKFTTDDSICVL
GISKRNVIFQPVAELKKQTDFEHRIPKEQWWLKLRPLMKILAKYKASYDVSDSGQLEHVQ
PWSV
Enzyme 17 Number of Residues 784
Enzyme 17 Molecular Weight 85597
Enzyme 17 Theoretical pI 7.60
Enzyme 17 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 metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
  • 6-phosphofructokinase complex
  • cell
  • cytoplasm
  • intracellular
  • protein complex
Enzyme 17 General Function Carbohydrate transport and metabolism
Enzyme 17 Specific Function ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate
Enzyme 17 Pathways
Enzyme 17 Reactions
  • ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 560105 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q01813 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name K6PP_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 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 17 GenBank Gene ID D25328 Link Image
Enzyme 17 GeneCard ID PFKP Link Image
Enzyme 17 GenAtlas ID PFKP Link Image
Enzyme 17 HGNC ID HGNC:8878 Link Image
Enzyme 17 Chromosome Location 10
Enzyme 17 Locus 10p15.3-p15.2
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 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. 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]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 6033
Enzyme 18 Name 6-phosphofructokinase, liver type
Enzyme 18 Synonyms
  1. Phosphofructokinase 1
  2. Phosphohexokinase
  3. Phosphofructo-1-kinase isozyme B
  4. PFK-B
Enzyme 18 Gene Name PFKL
Enzyme 18 Protein Sequence >6-phosphofructokinase, liver type
MAAVDLEKLRASGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVE
GGENIKQANWLSVSNIIQLGGTIIGSARCKAFTTREGRRAAAYNLVQHGITNLCVIGGDG
SLTGANIFRSEWGSLLEELVAEGKISETTARTYSHLNIAGLVGSIDNDFCGTDMTIGTDS
ALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWE
NFMCERLGETRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQ
RGGTPSAFDRILSSKMGMEAVMALLEATPDTPACVVTLSGNQSVRLPLMECVQMTKEVQK
AMDDKRFDEATQLRGGSFENNWNIYKLLAHQKPPKEKSNFSLAILNVGAPAAGMNAAVRS
AVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPKGQLESI
VENIRIYGIHALLVVGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLG
SDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFN
IHDLKVNVEHMTEKMKTDIQRGLVLRNEKCHDYYTTEFLYNLYSSEGKGVFDCRTNVLGH
LQQGGAPTPFDRNYGTKLGVKAMLWLSEKLREVYRKGRVFANAPDSACVIGLKKKAVAFS
PVTELKKDTDFEHRMPREQWWLSLRLMLKMLAQYRISMAAYVSGELEHVTRRTLSMDKGF
Enzyme 18 Number of Residues 780
Enzyme 18 Molecular Weight 85020
Enzyme 18 Theoretical pI 7.54
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 metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
  • 6-phosphofructokinase complex
  • cell
  • cytoplasm
  • intracellular
  • protein complex
Enzyme 18 General Function Carbohydrate transport and metabolism
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
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 35431 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID P17858 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name K6PL_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 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 18 GenBank Gene ID X15573 Link Image
Enzyme 18 GeneCard ID PFKL Link Image
Enzyme 18 GenAtlas ID PFKL Link Image
Enzyme 18 HGNC ID HGNC:8876 Link Image
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 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. 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 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 6037
Enzyme 19 Name 6-phosphofructokinase, muscle type
Enzyme 19 Synonyms
  1. Phosphofructokinase 1
  2. Phosphohexokinase
  3. Phosphofructo-1-kinase isozyme A
  4. PFK-A
  5. Phosphofructokinase-M
Enzyme 19 Gene Name PFKM
Enzyme 19 Protein Sequence >6-phosphofructokinase, muscle type
MTHEEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVD
GGDHIKEATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAYNLVKRGITNLCVIGGDG
SLTGADTFRSEWSDLLSDLQKAGKITDEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDS
ALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWE
EHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQ
RGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTK
AMDEKKFDEALKLRGRSFMNNWEVYKLLAHVRPPVSKSGSHTVAVMNVGAPAAGMNAAVR
STVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQ
ISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSV
GADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPF
TIRDLQANVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLG
HMQQGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVF
QPVAELKDQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSDHAHLEHITRKRSGEAAV
Enzyme 19 Number of Residues 780
Enzyme 19 Molecular Weight 85184
Enzyme 19 Theoretical pI 8.07
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 metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
  • 6-phosphofructokinase complex
  • cell
  • cytoplasm
  • intracellular
  • protein complex
Enzyme 19 General Function Carbohydrate transport and metabolism
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
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 1101758 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID P08237 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name K6PF_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >2343 bp
ATGACCCATGAAGAGCACCATGCAGCCAAAACCCTGGGGATTGGCAAAGCCATTGCTGTC
TTAACCTCTGGTGGAGATGCCCAAGGTATGAATGCTGCTGTCAGGGCTGTGGTTCGAGTT
GGTATCTTCACCGGTGCCCGTGTCTTCTTTGTCCATGAGGGTTATCAAGGCCTGGTGGAT
GGTGGAGATCACATCAAGGAAGCCACCTGGGAGAGCGTTTCGATGATGCTTCAGCTGGGA
GGCACGGTGATTGGAAGTGCCCGGTGCAAGGACTTTCGGGAACGAGAAGGACGACTCCGA
GCTGCCTACAACCTGGTGAAGCGTGGGATCACCAATCTCTGTGTCATTGGGGGTGATGGC
AGCCTCACTGGGGCTGACACCTTCCGTTCTGAGTGGAGTGACTTGTTGAGTGACCTCCAG
AAAGCAGGTAAGATCACAGATGAGGAGGCTACGAAGTCCAGCTACCTGAACATTGTGGGC
CTGGTTGGGTCAATTGACAATGACTTCTGTGGCACTGATATGACCATTGGCACTGACTCT
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 19 GenBank Gene ID M59741 Link Image
Enzyme 19 GeneCard ID PFKM Link Image
Enzyme 19 GenAtlas ID PFKM Link Image
Enzyme 19 HGNC ID HGNC:8877 Link Image
Enzyme 19 Chromosome Location 12
Enzyme 19 Locus 12q13.3
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 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. 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]
  5. 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]
  6. Raben N, Sherman JB: Mutations in muscle phosphofructokinase gene. Hum Mutat. 1995;6(1):1-6. [PubMed Link Image]
  7. 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]
  8. 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]
  9. 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 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 6041
Enzyme 20 Name Pyruvate kinase isozymes R/L
Enzyme 20 Synonyms
  1. R-type/L-type pyruvate kinase
  2. Red cell/liver pyruvate kinase
  3. Pyruvate kinase 1
Enzyme 20 Gene Name PKLR
Enzyme 20 Protein Sequence >Pyruvate kinase isozymes R/L
MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQ
LPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFS
HGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKG
SQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQV
ENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAA
LGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRC
NLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKM
QHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRS
AQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESG
KLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
Enzyme 20 Number of Residues 574
Enzyme 20 Molecular Weight 61831
Enzyme 20 Theoretical pI 7.83
Enzyme 20 GO Classification
Function
  • catalytic activity
  • kinase activity
  • pyruvate kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 20 General Function Carbohydrate transport and metabolism
Enzyme 20 Specific Function ATP + pyruvate = ADP + phosphoenolpyruvate
Enzyme 20 Pathways
Enzyme 20 Reactions
  • ATP + pyruvate = ADP + phosphoenolpyruvate
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 3327365 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P30613 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name KPYR_HUMAN Link Image
Enzyme 20 PDB ID 1LIU Link Image
Enzyme 20 PDB File Show
Enzyme 20 3D Structure
Enzyme 20 Cellular Location Not Available
Enzyme 20 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 20 GenBank Gene ID AB015983 Link Image
Enzyme 20 GeneCard ID PKLR Link Image
Enzyme 20 GenAtlas ID PKLR Link Image
Enzyme 20 HGNC ID HGNC:9020 Link Image
Enzyme 20 Chromosome Location 1
Enzyme 20 Locus 1q21
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 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. 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]
  4. 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]
  5. Beutler E, Baronciani L: Mutations in pyruvate kinase. Hum Mutat. 1996;7(1):1-6. [PubMed Link Image]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. 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]
  17. 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]
  18. 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]
  19. 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]
  20. 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]
  21. 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]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 6159
Enzyme 21 Name Ectonucleoside triphosphate diphosphohydrolase 4
Enzyme 21 Synonyms
  1. NTPDase 4
  2. Uridine-diphosphatase
  3. UDPase
  4. Lysosomal apyrase-like protein of 70 kDa
Enzyme 21 Gene Name ENTPD4
Enzyme 21 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 4
MGRIGISCLFPASWHFSISPVGCPRILNTNLRQIMVISVLAAAVSLLYFSVVIIRNKYGR
LTRDKKFQRYLARVTDIEATDTNNPNVNYGIVVDCGSSGSRVFVYCWPRHNGNPHDLLDI
RQMRDKNRKPVVMKIKPGISEFATSPEKVSDYISPLLNFAAEHVPRAKHKETPLYILCTA
GMRILPESQQKAILEDLLTDIPVHFDFLFSDSHAEVISGKQEGVYAWIGINFVLGRFEHI
EDDDEAVVEVNIPGSESSEAIVRKRTAGILDMGGVSTQIAYEVPKTVSFASSQQEEVAKN
LLAEFNLGCDVHQTEHVYRVYVATFLGFGGNAARQRYEDRIFANTIQKNRLLGKQTGLTP
DMPYLDPCLPLDIKDEIQQNGQTIYLRGTGDFDLCRETIQPFMNKTNETQTSLNGVYQPP
IHFQNSEFYGFSEFYYCTEDVLRMGGDYNAAKFTKAAKDYCATKWSILRERFDRGLYASH
ADLHRLKYQCFKSAWMFEVFHRGFSFPVNYKSLKTALQVYDKEVQWTLGAILYRTRFLPL
RDIQQEAFRASHTHWRGVSFVYNHYLFSGCFLVVLLAILLYLLRLRRIHRRTPRSSSAAA
LWMEEGLPAQNAPGTL
Enzyme 21 Number of Residues 616
Enzyme 21 Molecular Weight 70256
Enzyme 21 Theoretical pI 8.39
Enzyme 21 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 21 General Function Not Available
Enzyme 21 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 21 Pathways
Enzyme 21 Reactions
  • A nucleoside diphosphate + H2O = a nucleotide + phosphate
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • 34-54 560-580
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 3153211 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q9Y227 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name ENTP4_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1830 bp
ATGGGGAGGATTGGCATCTCCTGTCTTTTTCCTGCTTCTTGGCATTTTAGCATATCTCCA
GTAGGGTGTCCTCGAATTCTGAATACCAATTTACGCCAAATTATGGTCATTAGTGTCCTG
GCTGCTGCTGCTGTTTCACTTTTATATTTTTCTGTTGTCATAATCCGAAATAAGTATGGG
CGACTAACCAGAGACAAGAAATTTCAAAGGTACCTGGCACGAGTTACCGACATTGAAGCT
ACAGACACCAATAACCCCAATGTGAACTATGGGATCGTGGTGGACTGTGGTAGCAGTGGG
TCTCGAGTATTTGTTTACTGCTGGCCAAGGCATAATGGCAATCCACATGATCTGTTGGAT
ATCAGGCAAATGAGGGATAAAAACCGAAAGCCAGTGGTCATGAAGATAAAACCGGGCATT
TCAGAATTTGCTACCTCTCCAGAGAAAGTCAGTGATTACATTTCTCCACTTTTGAACTTT
GCTGCAGAGCATGTGCCACGGGCAAAACACAAAGAGACACCTCTCTACATTCTCTGCACG
GCTGGAATGAGAATCCTCCCCGAAAGCCAGCAGAAAGCTATTCTGGAAGACCTTCTGACC
GATATCCCCGTGCACTTTGACTTTCTGTTTTCTGACTCTCATGCAGAAGTAATTTCTGGG
AAACAAGAAGGTGTGTATGCTTGGATTGGCATTAATTTTGTCCTTGGACGATTTGAGCAT
ATTGAAGATGATGATGAGGCCGTTGTGGAAGTTAACATTCCTGGAAGTGAAAGCAGCGAA
GCCATTGTCCGTAAAAGGACAGCGGGCATTCTCGACATGGGCGGCGTGTCGACTCAGATA
GCGTACGAAGTCCCCAAAACTGAAGAAGTAGCTAAAAACTTGTTAGCTGAATTTAACTTG
GGATGTGATGTTCACCAAACTGAGCATGTGTATCGAGTCTATGTGGCCACGTTTCTTGGG
TTTGGTGGCAATGCTGCTCGACAGAGATACGAAGACAGAATATTTGCCAACACCATTCAA
AAGAACAGGCTCCTGGGTAAACAGACTGGTCTGACTCCTGATATGCCGTACTTGGACCCC
TGCCTACCCCTAGACATTAAAGATGAAATCCAGCAAAATGGACAAACCATATACCTACGA
GGGACTGGAGACTTTGACCTGTGTCGAGAGACTATCCAGCCTTTCATGAATAAAACAAAC
GAGACCCAGACTTCCCTCAATGGGGTCTACCAGCCCCCAATTCACTTCCAGAACAGTGAA
TTCTATGGCTTCTCCGAATTCTACTACTGCACCGAGGATGTGTTACGAATGGGGGGAGAC
TACAATGCTGCTAAATTTACTAAAGCTGCAAAGGATTACTGTGCAACAAAGTGGTCCATT
TTGCGGGAACGCTTTGACCGAGGACTGTACGCCTCTCATGCTGACCTCCACAGGCTTAAG
TATCAGTGCTTCAAATCGGCCTGGATGTTTGAGGTGTTTCATAGGGGCTTTTCGTTTCCT
GTCAACTATAAAAGCTTAAAGACTGCCTTGCAAGTTTACGACAAGGAGGTTCAGTGGACC
CTTGGAGCCATCCTCTACAGGACCCGCTTTCTACCATTAAGAGACATCCAGCAGGAGGCC
TTCCGAGCCAGTCACACCCACTGGCGGGGCGTTTCCTTTGTCTACAACCACTACCTGTTC
TCTGGCTGCTTCCTGGTGGTGCTGCTGGCCATCCTGCTGTACCTGCTGCGGCTGCGGCGC
ATCCACAGGCGCACTCCCCGGAGCAGCTCGGCCGCCGCCCTCTGGATGGAGGAGGGCCTT
CCCGCCCAGAATGCCCCAGGGACCTTGTGA
Enzyme 21 GenBank Gene ID AF016032 Link Image
Enzyme 21 GeneCard ID ENTPD4 Link Image
Enzyme 21 GenAtlas ID ENTPD4 Link Image
Enzyme 21 HGNC ID HGNC:14573 Link Image
Enzyme 21 Chromosome Location 8
Enzyme 21 Locus 8p21.3
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 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]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 6160
Enzyme 22 Name Ectonucleoside triphosphate diphosphohydrolase 6
Enzyme 22 Synonyms
  1. NTPDase 6
  2. CD39 antigen-like 2
Enzyme 22 Gene Name ENTPD6
Enzyme 22 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 6
MKKGIRYETSRKTSYIFQQPQHGPWQTRMRKISNHGSLRVAKVAYPLGLCVGVFIYVAYI
KWHRATATQAFFSITRAAPGARWGQQAHSPLGTAADGHEVFYGIMFDAGSTGTRVHVFQF
TRPPRETPTLTHETFKALKPGLSAYADDVEKSAQGIRELLDVAKQDIPFDFWKATPLVLK
ATAGLRLLPGEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITINFLTGSLK
TPGGSSVGMLDLGGGSTQIAFLPRVEGTLQASPPGYLTALRMFNRTYKLYSYSYLGLGLM
SARLAILGGVEGQPAKDGKELVSPCLSPSFKGEWEHAEVTYRVSGQKAAASLHELCAARV
SEVLQNRVHRTEEVKHVDFYAFSYYYDLAAGVGLIDAEKGGSLVVGDFEIAAKYVCRTLE
TQPQSSPFSCMDLTYVSLLLQEFGFPRSKVLKLTRKIDNVETSWALGAIFHYIDSLNRQK
SPAS
Enzyme 22 Number of Residues 484
Enzyme 22 Molecular Weight 53248
Enzyme 22 Theoretical pI 9.52
Enzyme 22 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 22 General Function Not Available
Enzyme 22 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 22 Pathways
Enzyme 22 Reactions
  • A nucleoside diphosphate + H2O = a nucleotide + phosphate
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • 40-60
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 3335098 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID O75354 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name ENTP6_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 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 22 GenBank Gene ID AF039916 Link Image
Enzyme 22 GeneCard ID ENTPD6 Link Image
Enzyme 22 GenAtlas ID ENTPD6 Link Image
Enzyme 22 HGNC ID HGNC:3368 Link Image
Enzyme 22 Chromosome Location 20
Enzyme 22 Locus 20p11.2-p11.22
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 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. 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. 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]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 6161
Enzyme 23 Name Ectonucleoside triphosphate diphosphohydrolase 5 precursor
Enzyme 23 Synonyms
  1. NTPDase 5
  2. Nucleoside diphosphatase
  3. CD39 antigen-like 4
  4. ER-UDPase
Enzyme 23 Gene Name ENTPD5
Enzyme 23 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 5 precursor
MATSWGTVFFMLVVSCVCSAVSHRNQQTWFEGIFLSSMCPINVSASTLYGIMFDAGSTGT
RIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHW
KKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTV
NFLTGQLHGHRQETVGTLDLGGASTQITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTH
SYLGFGLKAARLATLGALETEGTDGHTFRSACLPRWLEAEWIFGGVKYQYGGNQEGEVGF
EPCYAEVLRVVRGKLHQPEEVQRGSFYAFSYYYDRAVDTDMIDYEKGGILKVEDFERKAR
EVCDNLENFTSGSPFLCMDLSYITALLKDGFGFADSTVLQLTKKVNNIETGWALGATFHL
LQSLGISH
Enzyme 23 Number of Residues 428
Enzyme 23 Molecular Weight 47518
Enzyme 23 Theoretical pI 6.29
Enzyme 23 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 23 General Function Not Available
Enzyme 23 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 23 Pathways
Enzyme 23 Reactions
  • A nucleoside diphosphate + H2O = a nucleotide + phosphate
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • 1-20
Enzyme 23 Transmembrane Regions
  • 29-51
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 3335102 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID O75356 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name ENTP5_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 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 23 GenBank Gene ID AF039918 Link Image
Enzyme 23 GeneCard ID ENTPD5 Link Image
Enzyme 23 GenAtlas ID ENTPD5 Link Image
Enzyme 23 HGNC ID HGNC:3367 Link Image
Enzyme 23 Chromosome Location 14
Enzyme 23 Locus 14q24
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 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]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 6166
Enzyme 24 Name Adenylosuccinate synthetase isozyme 1
Enzyme 24 Synonyms
  1. IMP--aspartate ligase 1
  2. AdSS 1
  3. AMPSase 1
Enzyme 24 Gene Name ADSSL1
Enzyme 24 Protein Sequence >Adenylosuccinate synthetase isozyme 1
MSGTRASNDRPPGAGGVKRGRLQQEAAATGSRVTVVLGAQWGDEGKGKVVDLLATDADII
SRCQGGNNAGHTVVVDGKEYDFHLLPSGIINTKAVSFIGNGVVIHLPGLFEEAEKNEKKG
LKDWEKRLIISDRAHLVFDFHQAVDGLQEVQRQAQEGKNIGTTKKGIGPTYSSKAARTGL
RICDLLSDFDEFSSRFKNLAHQHQSMFPTLEIDIEGQLKRLKGFAERIRPMVRDGVYFMY
EALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDVYGVVKA
YTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALA
LTKLDILDVLGEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWE
DLPPQAQNYIRFVENHVGVAVKWVGVGKSRESMIQLF
Enzyme 24 Number of Residues 457
Enzyme 24 Molecular Weight 50209
Enzyme 24 Theoretical pI 8.85
Enzyme 24 GO Classification
Function
  • GTP binding
  • adenylosuccinate synthase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleotide binding
  • purine nucleotide binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
Component
Enzyme 24 General Function Nucleotide transport and metabolism
Enzyme 24 Specific Function Plays an important role in the de novo pathway of purine nucleotide biosynthesis
Enzyme 24 Pathways
Enzyme 24 Reactions
  • GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 21303413 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q8N142 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name PURA1_HUMAN Link Image
Enzyme 24 PDB ID 1MF1 Link Image
Enzyme 24 PDB File Show
Enzyme 24 3D Structure
Enzyme 24 Cellular Location Not Available
Enzyme 24 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 24 GenBank Gene ID AY037159 Link Image
Enzyme 24 GeneCard ID ADSSL1 Link Image
Enzyme 24 GenAtlas ID ADSSL1 Link Image
Enzyme 24 HGNC ID HGNC:20093 Link Image
Enzyme 24 Chromosome Location 14
Enzyme 24 Locus 14q32.33
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References Not Available
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 6171
Enzyme 25 Name Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial precursor
Enzyme 25 Synonyms
  1. Succinyl-CoA synthetase subunit alpha
  2. SCS- alpha
Enzyme 25 Gene Name SUCLG1
Enzyme 25 Protein Sequence >Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial precursor
MVSGSSGLAAARLLSRSFLLPQNGIRHCSYTASRQHLYVDKNTKIICQGFTGKQGTFHSQ
QALEYGTKLVGGTTPGKGGQTHLGLPVFNTVKEAKEQTGATASVIYVPPPFAAAAINEAI
EAEIPLVVCITEGIPQQDMVRVKHKLLRQEKTRLIGPNCPGVINPGECKIGIMPGHIHKK
GRIGIVSRSGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFIDCLEIFLNDSATEGII
LIGEIGGNAEENAAEFLKQHNSGPNSKPVVSFIAGLTAPPGRRMGHAGAIIAGGKGGAKE
KISALQSAGVVVSMSPAQLGTTIYKEFEKRKML
Enzyme 25 Number of Residues 333
Enzyme 25 Molecular Weight 35048
Enzyme 25 Theoretical pI 9.24
Enzyme 25 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 25 General Function Energy production and conversion
Enzyme 25 Specific Function GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
Enzyme 25 Pathways
Enzyme 25 Reactions
  • GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • 1-19
Enzyme 25 Transmembrane Regions Not Available
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 9409794 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID P53597 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name SUCA_HUMAN Link Image
Enzyme 25 PDB ID 1EUC Link Image
Enzyme 25 PDB File Show
Enzyme 25 3D Structure
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >1002 bp
ATGGTCTCCGGCAGCAGCGGCCTCGCCGCCGCCCGTCTCCTGTCGCGCAGCTTCCTCCTG
CCGCAGAATGGAATTCGGCATTGTTCCTACACAGCTTCTCGGCAACATCTCTATGTTGAT
AAAAATACAAAGATTATTTGCCAGGGTTTCACTGGCAAACAGGGCACCTTTCACAGCCAG
CAGGCATTGGAATATGGCACCAAACTCGTTGGAGGAACACTCCCAGGGAAAGGAGGCCAG
ACACATCTGGGCTTACCTGTCTTTAATACTGTGAAGGAGGCCAAAGAACAGACAGGAGCA
ACGGCTTCTGTCATTTATGTTCCTCCGCCTTTTGCTGCTGCTGCCATTAATGAAGCTATT
GAGGCAGAAATTCCCTTGGTTGTGTGTATCACTGAAGGAATTCCCCAGCAGGACATGGTA
CGAGTCAAGCACAAACTGCTGCGCCAGGAAAAGACAAGGCTAATTGGGCCCAACTGCCCT
GGAGTCATCAATCCTGGAGAATGTAAAATTGGGATCATGCCTGGCCATATTCACAAAAAA
GGAAGGATTGGCATTGTGTCCAGATCTGGCACCCTGACTTATGAAGCAGTTCACCAAACA
ACGCAAGTTGGATTGGGGCAGTCTTTGTGCGTTGGCATTGGAGGTGATCCTTTTAATGGA
ACAGATTTTATTGACTGCCTCGAAATCTTTTTGAACGATTCTGCCACAGAAGGCATCATA
TTGATTGGTGAAATTGGTGGTAATGCAGAAGAGAATGCTGCAGAATTTTTGAAGCAACAT
AATTCAGGTCCAAATTCCAAGCCTGTAGTGTCCTTCATTGCTGGTTTAACTGCTCCTCCT
GGGAGAAGAATGGGTCATGCCGGGGCAATTATTGCTGGAGGAAAAGGTGGAGCTAAAGAG
AAGATCTCTGCCCTTCAGAGTGCAGGAGTTGTGGTCAGTATGTCTCCTGCACAGCTGGGA
ACCACGATCTACAAGGAATTTGAAAAGAGGAAGATGCTATGA
Enzyme 25 GenBank Gene ID AF104921 Link Image
Enzyme 25 GeneCard ID SUCLG1 Link Image
Enzyme 25 GenAtlas ID SUCLG1 Link Image
Enzyme 25 HGNC ID HGNC:11449 Link Image
Enzyme 25 Chromosome Location 2
Enzyme 25 Locus 2p11.2
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. 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]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 6173
Enzyme 26 Name Succinyl-CoA ligase [GDP-forming] beta-chain, mitochondrial precursor
Enzyme 26 Synonyms
  1. Succinyl-CoA synthetase, betaG chain
  2. SCS-betaG
  3. GTP- specific succinyl-CoA synthetase subunit beta
Enzyme 26 Gene Name SUCLG2
Enzyme 26 Protein Sequence >Succinyl-CoA ligase [GDP-forming] beta-chain, mitochondrial precursor
MASPVAAQAGKLLRALALRPRFLAAGSQAVQLTSRRWLNLQEYQSKKLMSDNGVRVQRFF
VADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPNVVGQLAKQM
IGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEV
AASNPELIFKEQIDIFEGIKDSQAQRMAENLGFVGPLKSQAADQITKLYNLFLKIDATQV
EVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAAKYDLKYIGLD
GNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKEAQVYQAFKLLTADPKVEAILV
NIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVQEAQKILNNSGLPITSAIDLED
AAKKAVASVAKK
Enzyme 26 Number of Residues 432
Enzyme 26 Molecular Weight 46511
Enzyme 26 Theoretical pI 6.18
Enzyme 26 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 26 General Function Energy production and conversion
Enzyme 26 Specific Function GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
Enzyme 26 Pathways
Enzyme 26 Reactions
  • GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • 1-29
Enzyme 26 Transmembrane Regions Not Available
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 133777003 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q96I99 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name SUCB2_HUMAN Link Image
Enzyme 26 PDB ID 1EUC Link Image
Enzyme 26 PDB File Show
Enzyme 26 3D Structure
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >1155 bp
ATGTCTGACAACGGAGTGAGAGTTCAAAGATTCTTTGTAGCAGACACTGCAAATGAAGCT
CTCGAGGCTGCTAAGAGACTAAATGCAAAAGAAATTGTTTTAAAAGCCCAGATCTTAGCT
GGAGGAAGAGGAAAAGGTGTCTTCAATAGTGGTTTGAAAGGAGGTGTTCATTTAACAAAA
GACCCTAATGTTGTGGGACAGCTGGCTAAACAGATGATTGGGTACAATCTAGCGACAAAA
CAAACTCCAAAAGAAGGTGTGAAAGTTAACAAGGTGATGGTTGCTGAAGCCTTGGATATT
TCCAGAGAAACCTACCTGGCAATTCTGATGGACCGGTCCTGCAATGGCCCCGTGCTGGTG
GGCAGCCCCCAGGGGGGCGTCGACATTGAAGAGGTGGCTGCTTCAAACCCGGAGCTCATT
TTTAAGGAGCAAATTGACATTTTTGAAGGAATAAAGGACAGCCAAGCTCAGCGGATGGCC
GAAAATCTAGGCTTCGTTGGGCCTTTGAAAAGCCAGGCTGCAGATCAAATTACGAAGCTG
TATAATCTCTTCCTGAAAATTGATGCTACTCAGGTGGAAGTGAATCCCTTTGGTGAAACT
CCAGAAGGACAAGTTGTCTGTTTTGATGCCAAGATAAACTTTGATGACAACGCAGAATTC
CGACAAAAAGACATATTTGCTATGGACGACAAATCAGAGAATGAGCCCATTGAAAATGAA
GCTGCCAAATATGATCTAAAATACATAGGACTAGATGGGAACATTGCCTGCTTTGTGAAT
GGTGCTGGGCTCGCCATGGCTACTTGTGATATCATTTTCCTTAATGGTGGGAAGCCAGCC
AACTTCTTGGATCTTGGAGGTGGTGTAAAGGAAGCTCAAGTATATCAAGCATTCAAATTG
CTCACAGCTGATCCTAAGGTTGAAGCCATCCTTGTCAATATATTTGGTGGTATCGTCAAC
TGTGCCATCATTGCCAATGGGATCACCAAAGCCTGCCGGGAGCTAGAACTCAAGGTGCCC
CTGGTGGTCCGGCTTGAAGGAACCAACGTCCAAGAGGCCCAGAAGATACTCAACAACAGC
GGACTCCCCATTACTTCAGCCATTGACCTGGAGGATGCAGCCAAGAAGGCTGTGGCCAGT
GTGGCCAAGAAGTGA
Enzyme 26 GenBank Gene ID BC007716 Link Image
Enzyme 26 GeneCard ID SUCLG2 Link Image
Enzyme 26 GenAtlas ID SUCLG2 Link Image
Enzyme 26 HGNC ID HGNC:11450 Link Image
Enzyme 26 Chromosome Location 3
Enzyme 26 Locus 3p14.1
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. 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]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 6174
Enzyme 27 Name Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
Enzyme 27 Synonyms
  1. Phosphoenolpyruvate carboxylase
  2. PEPCK-C
Enzyme 27 Gene Name PCK1
Enzyme 27 Protein Sequence >Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
MPPQLQNGLNLSAKVVQGSLDSLPQAVREFLENNAELCQPDHIHICDGSEEENGRLLGQM
EEEGILRRLKKYDNCWLALTDPRDVARIESKTVIVTQEQRDTVPIPKTGLSQLGRWMSEE
DFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLSKIGIELTDSPYVVASMRIMTRMGTPV
LEAVGDGEFVKCLHSVGCPLPLQKPLVNNWPCNPELTLIAHLPDRREIISFGSGYGGNSL
LGKKCFALRMASRLAKEEGWLAEHMLILGITNPEGEKKYLAAAFPSACGKTNLAMMNPSL
PGWKVECVGDDIAWMKFDAQGHLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNV
AETSDGGVYWEGIDEPLASGVTITSWKNKEWSSEDGEPCAHPNSRFCTPASQCPIIDAAW
ESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKIIMHDPF
AMRPFFGYNFGKYLAHWLSMAQHPAAKLPKIFHVNWFRKDKEGKFLWPGFGENSRVLEWM
FNRIDGKASTKLTPIGYIPKEDALNLKGLGHINMMELFSISKEFWEKEVEDIEKYLEDQV
NADLPCEIEREILALKQRISQM
Enzyme 27 Number of Residues 622
Enzyme 27 Molecular Weight 69195
Enzyme 27 Theoretical pI 6.05
Enzyme 27 GO Classification
Function
  • GTP binding
  • binding
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • guanyl nucleotide binding
  • lyase activity
  • nucleotide binding
  • phosphoenolpyruvate carboxykinase activity
  • purine nucleotide binding
Process
  • alcohol metabolism
  • cellular metabolism
  • gluconeogenesis
  • glucose metabolism
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 27 General Function Energy production and conversion
Enzyme 27 Specific Function GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO(2)
Enzyme 27 Pathways
Enzyme 27 Reactions
  • GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 189945 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID P35558 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name PPCKC_HUMAN Link Image
Enzyme 27 PDB ID 1NHX Link Image
Enzyme 27 PDB File Show
Enzyme 27 3D Structure
Enzyme 27 Cellular Location Not Available
Enzyme 27 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 27 GenBank Gene ID L05144 Link Image
Enzyme 27 GeneCard ID PCK1 Link Image
Enzyme 27 GenAtlas ID PCK1 Link Image
Enzyme 27 HGNC ID HGNC:8724 Link Image
Enzyme 27 Chromosome Location 20
Enzyme 27 Locus 20q13.31
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 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. 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. 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]
  5. 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 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 6213
Enzyme 28 Name GDP-L-fucose synthetase
Enzyme 28 Synonyms
  1. Protein FX
  2. Red cell NADP(H- binding protein
  3. GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4- reductase
Enzyme 28 Gene Name TSTA3
Enzyme 28 Protein Sequence >GDP-L-fucose synthetase
MGEPQGSMRILVTGGSGLVGKAIQKVVADGAGLPGEDWVFVSSKDADLTDTAQTRALFEK
VQPTHVIHLAAMVGGLFRNIKYNLDFWRKNVHMNDNVLHSAFEVGARKVVSCLSTCIFPD
KTTYPIDETMIHNGPPHNSNFGYSYAKRMIDVQNRAYFQQYGCTFTAVIPTNVFGPHDNF
NIEDGHVLPGLIHKVHLAKSSGSALTVWGTGNPRRQFIYSLDLAQLFIWVLREYNEVEPI
ILSVGEEDEVSIKEAAEAVVEAMDFHGEVTFDTTKSDGQFKKTASNSKLRTYLPDFRFTP
FKQAVKETCAWFTDNYEQARK
Enzyme 28 Number of Residues 321
Enzyme 28 Molecular Weight 35893
Enzyme 28 Theoretical pI 6.59
Enzyme 28 GO Classification
Function
  • NAD binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide-sugar metabolism
  • physiological process
Component
Enzyme 28 General Function Cell wall/membrane/envelope biogenesis
Enzyme 28 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 28 Pathways
Enzyme 28 Reactions
  • GDP-L-fucose + NADP+ = GDP-4-dehydro-6-deoxy-D-mannose + NADPH + H+
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 1381179 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID Q13630 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name FCL_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >966 bp
ATGGGTGAACCCCAGGGATCCATGCGGATTCTAGTGACAGGGGGCTCTGGGCTGGTAGGC
AAAGCCATCCAGAAGGTGGTAGCAGATGGAGCTGGACTTCCTGGAGAGGACTGGGTGTTT
GTCTCCTCTAAAGACGCCGATCTCACGGATACAGCACAGACCCGCGCCCTGTTTGAGAAG
GTCCAACCCACACACGTCATCCATCTTGCTGCAATGGTGGGGGGCCTGTTCCGGAATATC
AAATACAATTTGGACTTCTGGAGGAAAAACGTGCACATGAACGACAACGTCCTGCACTCG
GCCTTTGAGGTGGGGGCCCGCAAGGTGGTGTCCTGCCTGTCCACCTGTATCTTCCCTGAC
AAGACGACCTACCCGATAGATGAGACCATGATCCACAATGGGCCTCCCCACAACAGCAAT
TTTGGGTACTCGTATGCCAAGAGGATGATCGACGTGCAGAACAGGGCCTACTTCCAGCAG
TACGGCTGCACCTTCACCGCTGTCATCCCCACCAACGTTTTCGGGCCCCACGACAACTTC
AACATCGAGGATGGCCACGTGCTGCCTGGCCTCATCCACAAGGTGCACCTGGCCAAGAGC
AGCGGCTCGGCCCTGACGGTGTGGGGTACAGGGAATCCGCGGAGGCAGTTCATATACTCG
CTGGACCTGGCCCAGCTCTTTATCTGGGTCCTGCGGGAGTACAATGAAGTGGAGCCCATC
ATCCTCTCCGTGGGCGAGGAAGATGAGGTCTCCATCAAGGAGGCAGCCGAGGCGGTGGTG
GAGGCCATGGACTTCCATGGGGAAGTCACCTTTGATACAACCAAGTCGGATGGGCAGTTT
AAGAAGACAGCCAGTAACAGCAAGCTGAGGACCTACCTGCCCGACTTCCGGTTCACACCC
TTCAAGCAGGCGGTGAAGGAGACCTGTGCTTGGTTCACTGACAACTACGAGCAGGCCCGG
AAGTGA
Enzyme 28 GenBank Gene ID U58766 Link Image
Enzyme 28 GeneCard ID TSTA3 Link Image
Enzyme 28 GenAtlas ID TSTA3 Link Image
Enzyme 28 HGNC ID HGNC:12390 Link Image
Enzyme 28 Chromosome Location 8
Enzyme 28 Locus 8q24.3
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 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. 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]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 6218
Enzyme 29 Name Guanylate kinase
Enzyme 29 Synonyms
  1. GMP kinase
Enzyme 29 Gene Name GUK1
Enzyme 29 Protein Sequence >Guanylate kinase
MSGPRPVVLSGPSGAGKSTLLKRLLQEHSGIFGFSVSHTTRNPRPGEENGKDYYFVTREV
MQRDIAAGDFIEHAEFSGNLYGTSKVAVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYI
SVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMESSKEPGLFDVVIINDSLDQAYAE
LKEALSEEIKKAQRTGA
Enzyme 29 Number of Residues 197
Enzyme 29 Molecular Weight 21726
Enzyme 29 Theoretical pI 6.53
Enzyme 29 GO Classification Not Available
Enzyme 29 General Function Nucleotide transport and metabolism
Enzyme 29 Specific Function Essential for recycling GMP and indirectly, cGMP
Enzyme 29 Pathways
Enzyme 29 Reactions
  • ATP + GMP = ADP + GDP
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 1196436 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q16774 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name KGUA_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >594 bp
ATGTCGGGCCCCAGGCCTGTGGTGCTGAGCGGGCCTTCGGGAGCTGGGAAGAGCACCCTG
CTGAAGAGGCTGCTCCAGGAGCACAGCGGCATCTTTGGCTTCAGCGTGTCCCATACCACG
AGGAACCCGAGGCCCGGCGAGGAGAACGGCAAAGATTACTACTTTGTAACCAGGGAGGTG
ATGCAGCGTGACATAGCAGCCGGCGACTTCATCGAGCATGCCGAGTTCTCGGGGAACCTG
TATGGCACGAGCAAGGTGGCGGTGCAGGCCGTGCAGGCCATGAACCGCATCTGTGTGCTG
GACGTGGACCTGCAGGGTGTGCGGAACATCAAGGCCACCGATCTGCGGCCCATCTACATC
TCTGTGCAGCCGCCTTCACTGCACGTGCTGGAGCAGCGGCTGCGGCAGCGCAACACTGAA
ACCGAGGAGAGCCTGGTGAAGCGGCTGGCTGCTGCCCAGGCCGACATGGAGAGCAGCAAG
GAGCCCGGCCTGTTTGATGTGGTCATCATTAACGACAGCCTGGACCAGGCCTACGCAGAG
CTGAAGGAGGCGCTCTCTGAGGAAATCAAGAAAGCTCAAAGGACCGGCGCCTGA
Enzyme 29 GenBank Gene ID L76200 Link Image
Enzyme 29 GeneCard ID GUK1 Link Image
Enzyme 29 GenAtlas ID GUK1 Link Image
Enzyme 29 HGNC ID HGNC:4693 Link Image
Enzyme 29 Chromosome Location 1
Enzyme 29 Locus 1q32-q41
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 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]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 6308
Enzyme 30 Name Alpha-(1,3)-fucosyltransferase
Enzyme 30 Synonyms
  1. Galactoside 3-L- fucosyltransferase
  2. Fucosyltransferase 5
  3. FucT-V
  4. Fuc-TV
Enzyme 30 Gene Name FUT5
Enzyme 30 Protein Sequence >Alpha-(1,3)-fucosyltransferase
MDPLGPAKPQWLWRRCLAGLLFQLLVAVCFFSYLRVSRDDATGSPRPGLMAVEPVTGAPN
GSRCQDSMATPAHPTLLILLWTWPFNTPVALPRCSEMVPGAADCNITADSSVYPQADAVI
VHHWDIMYNPSANLPPPTRPQGQRWIWFSMESPSNCRHLEALDGYFNLTMSYRSDSDIFT
PYGWLEPWSGQPAHPPLNLSAKTELVAWAVSNWKPDSARVRYYQSLQAHLKVDVYGRSHK
PLPKGTMMETLSRYKFYLAFENSLHPDYITEKLWRNALEAWAVPVVLGPSRSNYERFLPP
DAFIHVDDFQSPKDLARYLQELDKDHARYLSYFRWRETLRPRSFSWALAFCKACWKLQQE
SRYQTVRSIAAWFT
Enzyme 30 Number of Residues 374
Enzyme 30 Molecular Weight 43008
Enzyme 30 Theoretical pI 8.37
Enzyme 30 GO Classification
Function
  • catalytic activity
  • fucosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • membrane
Enzyme 30 General Function Not Available
Enzyme 30 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 30 Pathways
  • Glycosphingolipid biosynthesis - lactoseries (map00601 Link Image)
Enzyme 30 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
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • 1-27
Enzyme 30 Transmembrane Regions Not Available
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 1280209 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID Q11128 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name FUT5_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >1125 bp
ATGGATCCCCTGGGCCCAGCCAAGCCACAGTGGCTGTGGCGCCGCTGTCTGGCCGGGCTG
CTGTTTCAGCTGCTGGTGGCTGTGTGTTTCTTCTCCTACCTGCGTGTGTCCCGAGACGAT
GCCACTGGATCCCCTAGGCCAGGGCTTATGGCAGTGGAACCTGTCACCGGGGCTCCCAAT
GGGTCCCGCTGCCAGGACAGCATGGCGACCCCTGCCCACCCCACCCTACTGATCCTGCTG
TGGACGTGGCCTTTTAACACACCCGTGGCTCTGCCCCGCTGCTCAGAGATGGTGCCCGGC
GCGGCCGACTGCAACATCACTGCCGACTCCAGTGTGTACCCACAGGCAGACGCGGTCATC
GTGCACCACTGGGATATCATGTACAACCCCAGTGCCAACCTCCCGCCCCCCACCAGGCCG
CAGGGGCAGCGCTGGATCTGGTTCAGCATGGAGTCCCCCAGCAACTGCCGGCACCTGGAA
GCCCTGGACGGATACTTCAATCTCACCATGTCCTACCGCAGCGACTCCGACATCTTCACG
CCCTACGGCTGGCTGGAGCCGTGGTCCGGCCAGCCTGCCCACCCACCGCTCAACCTCTCG
GCCAAGACCGAGCTGGTGGCCTGGGCGGTGTCCAACTGGAAGCCGGACTCGGCCAGGGTG
CGCTACTACCAGAGCCTGCAGGCTCATCTCAAGGTGGACGTGTACGGACGCTCCCACAAG
CCCCTGCCCAAGGGGACCATGATGGAGACGCTGTCCCGGTACAAGTTCTATCTGGCCTTC
GAGAACTCCTTGCACCCCGACTACATCACCGAGAAGCTGTGGAGGAACGCCCTGGAGGCC
TGGGCCGTGCCCGTGGTGCTGGGCCCCAGCAGAAGCAACTACGAGAGGTTCCTGCCGCCC
GACGCCTTCATCCACGTGGATGACTTCCAGAGCCCCAAGGACCTGGCCCGGTACCTGCAG
GAGCTGGACAAGGACCACGCCCGCTACCTGAGCTACTTTCGCTGGCGGGAGACGCTGCGG
CCTCGCTCCTTCAGCTGGGCACTGGCTTTCTGCAAGGCCTGCTGGAAGCTGCAGCAGGAA
TCCAGGTACCAGACGGTGCGCAGCATAGCGGCTTGGTTCACCTGA
Enzyme 30 GenBank Gene ID M81485 Link Image
Enzyme 30 GeneCard ID FUT5 Link Image
Enzyme 30 GenAtlas ID FUT5 Link Image
Enzyme 30 HGNC ID HGNC:4016 Link Image
Enzyme 30 Chromosome Location 19
Enzyme 30 Locus 19p13.3
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 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]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 6417
Enzyme 31 Name Rap guanine nucleotide exchange factor 2
Enzyme 31 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 31 Gene Name RAPGEF2
Enzyme 31 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 31 Number of Residues 1499
Enzyme 31 Molecular Weight 167419
Enzyme 31 Theoretical pI 6.64
Enzyme 31 GO Classification
Function
  • GTPase regulator activity
  • binding
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • protein binding
  • small GTPase regulator activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • signal transduction
  • small GTPase mediated signal transduction
Component
Enzyme 31 General Function Not Available
Enzyme 31 Specific Function Guanine nucleotide exchange factor (GEF) for Rap1A, Rap1B and Rap2B GTPases. Does not interact with cAMP or cGMP
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 40788210 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q9Y4G8 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name RPGF2_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >4527 bp
ATTCAGTTCAGCATATGTTTCTTCATTATGAAACCACTAGCAATCCCAGCTAACCATGGA
GTTATGGGCCAGCAGGAGAAACACTCACTTCCTGCAGATTTCACAAAACTGCATCTTACT
GACAGTCTCCACCCACAGGTGACCCACGTTTCTTCTAGCCATTCAGGATGTAGTATCACT
AGTGATTCTGGGAGCAGCAGTCTTTCTGATATCTACCAGGCCACAGAAAGCGAGGCTGGT
GATATGGACCTGAGTGGGTTGCCAGAAACAGCAGTGGATTCCGAAGACGACGACGATGAA
GAAGACATTGAGAGAGCATCAGATCCTCTGATGAGCAGGGACATTGTGAGAGACTGCCTA
GAGAAGGACCCAATTGACCGGACAGATGATGACATTGAACAACTCTTGGAATTTATGCAC
CAGTTGCCTGCTTTTGCCAATATGACAATGTCAGTGAGGCGAGAACTCTGTGCTGTGATG
GTGTTCGCAGTGGTGGAAAGAGCAGGGACCATAGTGTTAAATGATGGTGAAGAGCTGGAC
TCCTGGTCAGTGATTCTCAATGGATCTGTGGAAGTGACTTATCCAGATGGAAAAGCAGAA
ATACTGTGCATGGGAAATAGTTTTGGTGTCTCTCCTACCATGGACAAAGAATACATGAAA
GGAGTGATGAGAACAAAGGTGGATGACTGCCAGTTTGTCTGCATAGCCCAGCAAGATTAC
TGCCGTATTCTCAATCAAGTAGAAAAGAACATGCAAAAAGTTGAAGAGGAAGGAGAGATT
GTTATGGTGAAAGAACACCGAGAACTTGATCGAACTGGAACAAGAAAGGGACACATTGTC
ATCAAGGGTACCTCAGAAAGGTTAACAATGCATTTGGTGGAAGAGCATTCAGTAGTAGAT
CCAACATTCATAGAAGACTTTCTGTTGACCTATAGGACTTTTCTTTCTAGCCCAATGGAA
GTGGGCAAAAAGTTATTGGAGTGGTTTAATGACCCGAGCCTCAGGGATAAGGTTACACGG
GTAGTATTATTGTGGGTAAATAATCACTTCAATGACTTTGAAGGAGATCCTGCAATGACT
CGATTTTTAGAAGAATTTGAAAACAATCTGGAAAGAGAGAAAATGGGTGGACACCTAAGG
CTGTTGAATATCGCGTGTGCTGCTAAAGCAAAAAGAAGATTGATGACGTTAACAAAACCA
TCCCGAGAAGCTCCTTTGCCTTTTATCTTACTTGGAGGCTCTGAGAAGGGATTTGGAATC
TTTGTTGACAGTGTAGATTCAGGTAGCAAAGCAACTGAAGCAGGCTTGAAACGGGGGGAT
CAGATATTAGAAGTAAATGGCCAAAACTTTGAAAACATTCAGCTGTCAAAAGCTATGGAA
ATTCTTAGAAATAACACACATTTATCTATCACTGTGAAAACCAATTTATTTGTATTTAAA
GAACTTCTAACAAGATTGTCAGAAGAGAAAAGAAATGGTGCCCCCCACCTTCCTAAAATT
GGTGACATTAAAAAGGCCAGTCGCTACTCCATTCCAGATCTTGCTGTAGATGTAGAACAG
GTGATAGGACTTGAAAAAGTGAACAAAAAAAGTAAAGCCAACACTGTGGGAGGAAGGAAC
AAGCTGAAAAAGATACTCGACAAGACTCGGATCAGTATCTTGCCACAGAAACCATACAAT
GATATTGGGATTGGTCAGTCTCAAGATGACAGCATAGTAGGATTAAGGCAGACAAAGCAC
ATCCCAACTGCATTGCCTGTCAGTGGAACCTTATCATCCAGTAATCCTGATTTATTGCAG
TCACATCATCGCATTTTAGACTTCAGTGCTACTCCTGACTTGCCAGATCAAGTGCTAAGG
GTTTTTAAGGCTGATCAGCAAAGCCGCTACATCATGATCAGTAAGGACACTACAGCAAAG
GAAGTGGTCATTCAGGCTATCAGGGAGTTTGCTGTTACTGCCACCCCGGATCAATATTCA
CTATGTGAGGTCTCTGTCACACCTGAGGGAGTAATCAAACAAAGAAGACTTCCAGATCAG
CTTTCCAAACTTGCAGACAGAATACAACTGAGTGGAAGGTATTATCTGAAAAACAACATG
GAAACAGAAACTCTTTGTTCAGATGAAGATGCTCAGGAGTTGTTGAGAGAGAGTCAAATT
TCCCTCCTTCAGCTCAGCACTGTGGAAGTTGCAACACAGCTCTCTATGCGAAATTTTGAA
CTCTTTCGCAACATTGAACCTACTGAATATATAGATGATTTATTTAAACTCAGATCAAAA
ACCAGCTGTGCCAACCTGAAGAGATTTGAAGAAGTCATTAACCAGGAAACATTTTGGGTA
GCATCTGAAATTCTCAGAGAAACAAACCAGCTGAAGAGGATGAAGATCATTAAGCATTTC
ATCAAGATAGCACTGCACTGTAGGGAATGCAAGAATTTTAACTCAATGTTTGCAATCATC
AGTGGCCTAAACCTGGCACCAGTGGCAAGACTGCGAACGACCTGGGAGAAACTTCCCAAT
AAATACGAAAAACTATTTCAAGATCTCCAAGACCTGTTTGATCCTTCCAGAAACATGGCA
AAATATCGTAATGTTCTCAATAGTCAAAATCTACAACCTCCCATAATCCCTCTATTCCCA
GTTATCAAAAAGGATCTCACCTTCCTTCACGAAGGAAATGACTCAAAAGTAGACGGGCTG
GTCAATTTTGAGAAGCTAAGGATGATTGCAAAAGAAATTCGTCACGTTGGCCGAATGGCT
TCAGTGAACATGGACCCTGCCCTCATGTTCAGGACTCGGAAGAAGAAATGGCGGAGTTTG
GGGTCTCTCAGCCAGGGTAGTACAAATGCAACAGTGCTAGATGTTGCTCAGACAGGTGGT
CATAAAAAGCGGGTACGTCGTAGTTCCTTTCTCAATGCCAAAAAGCTTTATGAAGATGCC
CAAATGGCTCGAAAAGTGAAGCAGTACCTTTCCAATTTGGAGCTAGAAATGGACGAGGAG
AGTCTTCAGACATTATCTCTGCAGTGTGAGCCAGCAACCAACACATTGCCTAAGAATCCT
GGTGACAAAAAGCCTGTCAAATCCGAGACCTCTCCAGTAGCTCCAAGGGCAGGGTCACAA
CAGAAAGCTCAGTCCCTGCCACAGCCCCAGCAGCAGCCACCACCAGCACATAAAATCAAC
CAGGGACTACAGGTTCCCGCCGTGTCCCTTTATCCTTCACGGAAGAAAGTGCCCGTAAAG
GATCTCCCACCTTTTGGCATAAACTCTCCACAAGCTTTAAAAAAAATTCTTTCTTTGTCT
GAAGAAGGAAGTTTGGAACGTCACAAGAAACAGGCTGAAGATACAATATCAAATGCATCT
TCGCAGCTTTCTTCTCCTCCTACTTCTCCACAGAGTTCTCCAAGGAAAGGCTATACTTTG
GCTCCCAGTGGTACTGTGGATAATTTTTCAGATTCTGGTCACAGTGAAATTTCTTCACGA
TCCAGTATTGTTAGCAATTCGTCTTTTGACTCAGTGCCAGTCTCACTGCACGATGAGAGG
CGCCAGAGGCATTCTGTCAGCATCGTGGAAACAAACCTAGGGATGGGCAGGATGGAGAGG
CGGACCATGATTGAACCTGATCAGTATAGCTTGGGGTCCTATGCACCAATGTCCGAGGGC
CGAGGCTTATATGCTACAGCTACAGTAATTTCTTCTCCAAGCACAGAGGAACTTTCCCAG
GATCAGGGGGATCGCGCGTCACTTGATGCTGCTGACAGTGGCCGTGGGAGCTGGACGTCA
TGCTCAAGTGGCTCCCATGATAATATACAGACGATCCAGCACCAGAGAAGCTGGGAGACT
CTTCCATTCGGGCATACTCACTTTGATTATTCAGGGGATCCTGCAGGTTTATGGGCATCA
AGCAGCCATATGGACCAAATTATGTTTTCTGATCATAGCACAAAGTATAACAGGCAAAAT
CAAAGTAGAGAGAGCCTTGAACAAGCCCAGTCCCGAGCAAGCTGGGCGTCTTCCACAGGT
TACTGGGGAGAAGACTCAGAAGGTGACACAGGCACAATAAAGCGGAGGGGTGGAAAGGAT
GTTTCCATTGAAGCCGAAAGCAGTAGCCTAACGTCTGTGACTACGGAAGAAACCAAGCCT
GTCCCCATGCCTGCCCACATAGCTGTGGCATCAAGTACTACAAAGGGGCTCATTGCACGA
AAGGAGGGCAGGTATCGAGAGCCCCCGCCCACCCCTCCCGGCTACATTGGAATTCCCATT
ACTGACTTTCCAGAAGGGCACTCCCATCCAGCCAGGAAACCGCCGGACTACAACGTGGCC
CTTCAGAGATCGCGGATGGTCGCACGATCCTCCGACACAGCTGGGCCTTCATCCGTACAG
CAGCCACATGGGCATCCCACCAGCAGCAGGCCTGTGAACAAACCTCAGTGGCATAAACCG
AACGAGTCTGACCCGCGCCTCGCCCCTTATCAGTCCCAAGGGTTTTCCACCGAGGAGGAT
GAAGATGAACAAGTTTCTGCTGTTTGA
Enzyme 31 GenBank Gene ID AB002311 Link Image
Enzyme 31 GeneCard ID RAPGEF2 Link Image
Enzyme 31 GenAtlas ID RAPGEF2 Link Image
Enzyme 31 HGNC ID HGNC:16854 Link Image
Enzyme 31 Chromosome Location 4
Enzyme 31 Locus 4q32.1
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 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. 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]
  3. 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 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 6586
Enzyme 32 Name Polyribonucleotide nucleotidyltransferase 1, mitochondrial precursor
Enzyme 32 Synonyms
  1. PNPase 1
  2. Polynucleotide phosphorylase-like protein
  3. PNPase old-35
  4. 3'-5' RNA exonuclease OLD35
Enzyme 32 Gene Name PNPT1
Enzyme 32 Protein Sequence >Polyribonucleotide nucleotidyltransferase 1, mitochondrial precursor
MAACRYCCSCLRLRPLSDGPFLLPRRDRALTQLQVRALWSSAGSRAVAVDLGNRKLEISS
GKLARFADGSAVVQSGDTAVMVTAVSKTKPSPSQFMPLVVDYRQKAAAAGRIPTNYLRRE
IGTSDKEILTSRIIDRSIRPLFPAGYFYDTQVLCNLLAVDGVNEPDVLAINGASVALSLS
DIPWNGPVGAVRIGIIDGEYVVNPTRKEMSSSTLNLVVAGAPKSQIVMLEASAENILQQD
FCHAIKVGVKYTQQIIQGIQQLVKETGVTKRTPQKLFTPSPEIVKYTHKLAMERLYAVFT
DYEHDKVSRDEAVNKIRLDTEEQLKEKFPEADPYEIIESFNVVAKEVFRSIVLNEYKRCD
GRDLTSLRNVSCEVDMFKTLHGSALFQRGQTQVLCTVTFDSLESGIKSDQVITAINGIKD
KNFMLHYEFPPYATNEIGKVTGLNRRELGHGALAEKALYPVIPRDFPFTIRVTSEVLESN
GSSSMASACGGSLALMDSGVPISSAVAGVAIGLVTKTDPEKGEIEDYRLLTDILGIEDYN
GDMDFKIAGTNKGITALQADIKLPGIPIKIVMEAIQQASVAKKEILQIMNKTISKPRASR
KENGPVVETVQVPLSKRAKFVGPGGYNLKKLQAETGVTISQVDEETFSVFAPTPSAMHEA
RDFITEICKDDQEQQLEFGAVYTATITEIRDTGVMVKLYPNMTAVLLHNTQLDQRKIKHP
TALGLEVGQEIQVKYFGRDPADGRMRLSRKVLQSPATTVVRTLNDRSSIVMGEPISQSSS
NSQ
Enzyme 32 Number of Residues 783
Enzyme 32 Molecular Weight 85952
Enzyme 32 Theoretical pI 7.86
Enzyme 32 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 catabolism
  • RNA metabolism
  • RNA processing
  • cellular metabolism
  • mRNA catabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
Enzyme 32 General Function Translation, ribosomal structure and biogenesis
Enzyme 32 Specific Function Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3' to 5' direction
Enzyme 32 Pathways
Enzyme 32 Reactions
  • RNA(n+1) + phosphate = RNA(n) + a nucleoside diphosphate
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 20372922 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID Q8TCS8 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name PNPT1_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >2352 bp
ATGGCGGCCTGCAGGTACTGCTGCTCGTGCCTCCGGCTCCGGCCCCTGAGCGATGGTCCT
TTCCTTCTGCCACGGCGGGATCGGGCACTCACCCAGTTGCAAGTGCGAGCACTATGGAGT
AGCGCAGGGTCTCGAGCTGTGGCCGTGGACTTAGGCAACAGGAAATTAGAAATATCTTCT
GGAAAGCTGGCCAGATTTGCAGATGGCTCTGCTGTAGTACAGTCAGGTGACACTGCAGTA
ATGGTCACAGCGGTCAGTAAAACAAAACCTTCCCCTTCCCAGTTTATGCCTTTGGTGGTT
GACTACAGACAAAAAGCTGCTGCAGCAGGTAGAATTCCCACAAACTATCTGAGAAGAGAG
GTTGGTACTTCTGATAAAGAAATTCTAACAAGTCGAATAATAGATCGTTCAATTAGACCG
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 32 GenBank Gene ID AJ458465 Link Image
Enzyme 32 GeneCard ID PNPT1 Link Image
Enzyme 32 GenAtlas ID PNPT1 Link Image
Enzyme 32 HGNC ID HGNC:23166 Link Image
Enzyme 32 Chromosome Location 2
Enzyme 32 Locus 2p15
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 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]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 7002
Enzyme 33 Name Rho guanine nucleotide exchange factor 1
Enzyme 33 Synonyms
  1. p115-RhoGEF
  2. p115RhoGEF
  3. 115 kDa guanine nucleotide exchange factor
  4. Sub1.5
Enzyme 33 Gene Name ARHGEF1
Enzyme 33 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 33 Number of Residues 912
Enzyme 33 Molecular Weight 102437
Enzyme 33 Theoretical pI 5.37
Enzyme 33 GO Classification
Function
  • GTPase regulator activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • small GTPase regulator activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • signal transduction
Component
Enzyme 33 General Function Not Available
Enzyme 33 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 33 Pathways Not Available
Enzyme 33 Reactions Not Available
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 1654344 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q92888 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name ARHG1_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >2739 bp
ATGGAAGACTTCGCCCGAGGGGCGGCCTCCCCAGGCCCCTCCCGGCCTGGCCTGGTTCCC
GTCAGCATCATCGGGGCTGAGGATGAGGATTTTGAGAACGAGCTGGAGACAAACTCAGAA
GAGCAAAACAGCCAGTTCCAGAGCCTGGAGCAGGTGAAGCGGCGCCCAGCCCACCTCATG
GCCCTCCTGCAGCACGTGGCCCTGCAGTTTGAGCCAGGACCCCTGCTTTGCTGTCTGCAT
GCCGACATGCTGGGCTCACTGGGCCCCAAGGAGGCCAAGAAGGCCTTCCTGGACTTCTAC
CACAGCTTCCTGGAGAAGACAGCGGTTCTCCGGGTGCCGGTCCCTCCCAACGTCGCCTTT
GAACTTGACCGCACTAGGGCTGACCTCATCTCCGAGGATGTCCAGCGGCGGTTCGTGCAG
GAGGTGGTGCAAAGCCAGCAGGTAGCCGTGGGCCGGCAGCTGGAGGACTTCCGTTCCAAG
CGGCTCATGGGCATGACGCCCTGGGAGCAGGAGCTGGCCCAGCTGGAGGCTTGGGTTGGG
CGGGACCGAGCCAGCTACGAGGCCCGGGAGCGGCACGTGGCGGAGCGGCTGCTCATGCAC
CTGGAGGAGATGCAACATACCATCTCTACCGACGAAGAAAAGAGTGCTGCCGTGGTCAAC
GCCATTGGGCTGTACATGCGCCACCTTGGGGTGCGGACCAAGAGTGGAGACAAGAAGTCG
GGGAGGAACTTCTTCCGGAAAAAGGTGATGGGGAACCGGCGGTCGGACGACCCTCCCAAG
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
TCCCTGAAAGTCCCTGCCCCTGCCTCTCGCCCTAAGCCCCGGCCCAGGCCGAGCAGCACC
CGAGAACCCCTCCTCAGCAGCTCTGAGAACGGGAATGGTGGCCGAGAGACGTCTCCAGCT
GATGCCCGGACCGAGAGAATCCTCAGTGACCTCCTGCCCTTCTGCAGACCAGGCCCCGAG
GGCCAGCTCGCTGCCACGGCCCTTCGGAAAGTGCTGTCCCTGAAGCAGCTTCTGTTTCCG
GCGGAGGAAGACAATGGGGCGGGGCCTCCTCGAGATGGGGATGGGGTCCCAGGGGGCGGG
CCCCTGAGCCCAGCACGGACCCAGGAAATCCAGGAGAACCTGCTCAGCTTGGAGGAGACC
ATGAAGCAGCTGGAGGAGTTGGAGGAGGAATTTTGCCGCCTGAGACCCCTCCTGTCTCAG
CTTGGGGGGAACTCTGTCCCCCAGCCTGGCTGCACTTGA
Enzyme 33 GenBank Gene ID U64105 Link Image
Enzyme 33 GeneCard ID ARHGEF1 Link Image
Enzyme 33 GenAtlas ID ARHGEF1 Link Image
Enzyme 33 HGNC ID HGNC:681 Link Image
Enzyme 33 Chromosome Location 19
Enzyme 33 Locus 19q13.13
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 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. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 7120
Enzyme 34 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) gamma-2 subunit precursor
Enzyme 34 Synonyms
  1. G gamma-I
Enzyme 34 Gene Name GNG2
Enzyme 34 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) gamma-2 subunit precursor
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL
Enzyme 34 Number of Residues 71
Enzyme 34 Molecular Weight 7850
Enzyme 34 Theoretical pI 8.22
Enzyme 34 GO Classification
Function
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
  • cell
  • extrinsic to membrane
  • extrinsic to plasma membrane
  • heterotrimeric G-protein complex
  • membrane
Enzyme 34 General Function Not Available
Enzyme 34 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 34 Pathways Not Available
Enzyme 34 Reactions Not Available
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 20147633 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID P59768 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name GBG2_HUMAN Link Image
Enzyme 34 PDB ID 1GP2 Link Image
Enzyme 34 PDB File Show
Enzyme 34 3D Structure
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >216 bp
ATGGCCAGCAACAACACCGCCAGCATAGCACAAGCCAGGAAGCTGGTAGAGCAGCTTAAG
ATGGAAGCCAATATCGACAGGATAAAGGTGTCCAAGGCAGCTGCAGATTTGATGGCCTAC
TGTGAAGCACATGCCAAGGAAGACCCCCTCCTGACCCCTGTTCCGGCTTCAGAAAACCCG
TTTAGGGAGAAGAAGTTTTTCTGTGCCATCCTTTAA
Enzyme 34 GenBank Gene ID AF493870 Link Image
Enzyme 34 GeneCard ID GNG2 Link Image
Enzyme 34 GenAtlas ID GNG2 Link Image
Enzyme 34 HGNC ID HGNC:4404 Link Image
Enzyme 34 Chromosome Location 14
Enzyme 34 Locus 14q21
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 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]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 7131
Enzyme 35 Name Ras-related C3 botulinum toxin substrate 1 precursor
Enzyme 35 Synonyms
  1. p21-Rac1
  2. Ras- like protein TC25
  3. Cell migration-inducing gene 5 protein
Enzyme 35 Gene Name RAC1
Enzyme 35 Protein Sequence >Ras-related C3 botulinum toxin substrate 1 precursor
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAG
QEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLR
DDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPP
PVKKRKRKCLLL
Enzyme 35 Number of Residues 192
Enzyme 35 Molecular Weight 21450
Enzyme 35 Theoretical pI 8.65
Enzyme 35 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • signal transduction
  • small GTPase mediated signal transduction
Component
Enzyme 35 General Function Not Available
Enzyme 35 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 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 190824 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID P63000 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name RAC1_HUMAN Link Image
Enzyme 35 PDB ID 1I4L Link Image
Enzyme 35 PDB File Show
Enzyme 35 3D Structure
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >579 bp
ATGCAGGCCATCAAGTGTGTGGTGGTGGGAGACGGAGCTGTAGGTAAAACTTGCCTACTG
ATCAGTTACACAACCAATGCATTTCCTGGAGAATATATCCCTACTGTCTTTGACAATTAT
TCTGCCAATGTTATGGTAGATGGAAAACCGGTGAATCTGGGCTTATGGGATACAGCTGGA
CAAGAAGATTATGACAGATTACGCCCCCTATCCTATCCGCAAACAGATGTGTTCTTAATT
TGCTTTTCCCTTGTGAGTCCTGCATCATTTGAAAATGTCCGTGCAAAGTGGTATCCTGAG
GTGCGGCACCACTGTCCCAACACTCCCATCATCCTAGTGGGAACTAAACTTGATCTTAGG
GATGATAAAGACACGATCGAGAAACTGAAGGAGAAGAAGCTGACTCCCATCACCTATCCG
CAGGGTCTAGCCATGGCTAAGGAGATTGGTGCTGTAAAATACCTGGAGTGCTCGGCGCTC
ACACAGCGAGGCCTCAAGACAGTGTTTGACGAAGCGATCCGAGCAGTCCTCTGCCCGCCT
CCCGTGAAGAAGAGGAAGAGAAAATGCCTGCTGTTGTAA
Enzyme 35 GenBank Gene ID M29870 Link Image
Enzyme 35 GeneCard ID RAC1 Link Image
Enzyme 35 GenAtlas ID RAC1 Link Image
Enzyme 35 HGNC ID HGNC:9801 Link Image
Enzyme 35 Chromosome Location 7
Enzyme 35 Locus 7p22
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 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. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. 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]
  17. 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]
  18. 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]
  19. 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]
  20. 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]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 7133
Enzyme 36 Name Rho GDP-dissociation inhibitor 3
Enzyme 36 Synonyms
  1. Rho GDI 3
  2. Rho-GDI gamma
Enzyme 36 Gene Name ARHGDIG
Enzyme 36 Protein Sequence >Rho GDP-dissociation inhibitor 3
MLGLDACELGAQLLELLRLALCARVLLADKEGGPPAVDEVLDEAVPEYRAPGRKSLLEIR
QLDPDDRSLAKYKRVLLGPLPPAVDPSLPNVQVTRLTLLSEQAPGPVVMDLTGDLAVLKD
QVFVLKEGVDYRVKISFKVHREIVSGLKCLHHTYRRGLRVDKTVYMVGSYGPSAQEYEFV
TPVEEAPRGALVRGPYLVVSLFTDDDRTHHLSWEWGLCICQDWKD
Enzyme 36 Number of Residues 225
Enzyme 36 Molecular Weight 25098
Enzyme 36 Theoretical pI 5.37
Enzyme 36 GO Classification
Function
  • GDP-dissociation inhibitor activity
  • GTPase regulator activity
  • Rho GDP-dissociation inhibitor activity
  • enzyme regulator activity
  • small GTPase regulator activity
Process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 36 General Function Not Available
Enzyme 36 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 36 Pathways Not Available
Enzyme 36 Reactions Not Available
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • 1-28
Enzyme 36 Transmembrane Regions Not Available
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 1772913 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q99819 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name GDIT_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >678 bp
ATGCTGGGCCTGGACGCGTGCGAGCTGGGGGCGCAGCTGCTGGAGCTGCTCCGGCTGGCG
CTGTGCGCCCGAGTCCTCCTGGCTGACAAGGAGGGTGGGCCGCCGGCAGTGGACGAGGTG
TTGGATGAGGCTGTGCCCGAGTACCGGGCGCCGGGGAGGAAGAGCCTCTTGGAGATCCGG
CAGCTGGACCCGGACGACAGGAGCCTGGCCAAGTACAAGCGGGTGCTGCTGGGGCCCCTG
CCACCGGCCGTGGACCCAAGCCTGCCCAATGTGCAGGTGACCAGGCTGACACTCCTGTCG
GAACAGGCTCCGGGGCCCGTCGTCATGGATCTCACAGGGAACCTGGCTGTTCTGAAGGAC
CAGGTGTTTGTCCTGAAGGAAGGTGTTGATTACAGAGTGAAGATCTCCTTCAAGGTCCAC
AGGGAGATTGTCAGCGGCCTCAAGTGTCTGCACCACACCTACCGCCGGGGCCTGCGCGTG
GACAAGACCGTCTACATGGTGGGCAGCTATGGCCCGAGCGCCCAGGAGTATGAGTTTGTG
ACTCCGGTGGAGGAAGCGCCGAGGGGTGCGCTGGTGCGGGGCCCCTATCTGGTGGTGTCC
CTCTTCACCGACGATGACAGGACGCACCACCTGTCCTGGGAGTGGGGTCTCTGCATCTGC
CAGGACTGGAAGGACTGA
Enzyme 36 GenBank Gene ID U82532 Link Image
Enzyme 36 GeneCard ID ARHGDIG Link Image
Enzyme 36 GenAtlas ID ARHGDIG Link Image
Enzyme 36 HGNC ID HGNC:680 Link Image
Enzyme 36 Chromosome Location 16
Enzyme 36 Locus 16p13.3
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 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]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 7134
Enzyme 37 Name Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Enzyme 37 Synonyms
  1. Adenylate cyclase-stimulating G alpha protein
Enzyme 37 Gene Name GNAS
Enzyme 37 Protein Sequence >Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQM
RILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELA
NPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLD
KIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFND
VTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEK
VLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCY
PHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL
Enzyme 37 Number of Residues 394
Enzyme 37 Molecular Weight 45665
Enzyme 37 Theoretical pI 5.56
Enzyme 37 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • nucleotide binding
  • purine nucleotide binding
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • signal transduction
Component
Enzyme 37 General Function Not Available
Enzyme 37 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 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 31915 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID P63092 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name GNAS2_HUMAN Link Image
Enzyme 37 PDB ID 1U0H Link Image
Enzyme 37 PDB File Show
Enzyme 37 3D Structure
Enzyme 37 Cellular Location Not Available
Enzyme 37 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 37 GenBank Gene ID X04408 Link Image
Enzyme 37 GeneCard ID GNAS Link Image
Enzyme 37 GenAtlas ID GNAS Link Image
Enzyme 37 HGNC ID HGNC:4392 Link Image
Enzyme 37 Chromosome Location 20
Enzyme 37 Locus 20q13.3
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 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. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 7135
Enzyme 38 Name Rab GDP dissociation inhibitor alpha
Enzyme 38 Synonyms
  1. Rab GDI alpha
  2. Guanosine diphosphate dissociation inhibitor 1
  3. GDI-1
  4. XAP-4
  5. Oligophrenin- 2
Enzyme 38 Gene Name GDI1
Enzyme 38 Protein Sequence >Rab GDP dissociation inhibitor alpha
MDEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDRNPYYGGESSSITPLEELYKRFQLLE
GPPESMGRGRDWNVDLIPKFLMANGQLVKMLLYTEVTRYLDFKVVEGSFVYKGGKIYKVP
STETEALASNLMGMFEKRRFRKFLVFVANFDENDPKTFEGVDPQTTSMRDVYRKFDLGQD
VIDFTGHALALYRTDDYLDQPCLETVNRIKLYSESLARYGKSPYLYPLYGLGELPQGFAR
LSAIYGGTYMLNKPVDDIIMENGKVVGVKSEGEVARCKQLICDPSYIPDRVRKAGQVIRI
ICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISYAHNVAAQGKYIAIASTTVETT
DPEKEVEPALELLEPIDQKFVAISDLYEPIDDGCESQVFCSCSYDATTHFETTCNDIKDI
YKRMAGTAFDFENMKRKQNDVFGEAEQ
Enzyme 38 Number of Residues 447
Enzyme 38 Molecular Weight 50583
Enzyme 38 Theoretical pI 4.75
Enzyme 38 GO Classification
Function
  • GDP-dissociation inhibitor activity
  • GTPase regulator activity
  • Rab GDP-dissociation inhibitor activity
  • enzyme regulator activity
  • small GTPase regulator activity
Process
  • cellular physiological process
  • physiological process
  • protein transport
  • regulation of GTPase activity
  • regulation of biological process
  • regulation of enzyme activity
  • regulation of hydrolase activity
  • transport
Component
Enzyme 38 General Function Not Available
Enzyme 38 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 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 695523 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID P31150 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name GDIA_HUMAN Link Image
Enzyme 38 PDB ID 1GND Link Image
Enzyme 38 PDB File Show
Enzyme 38 3D Structure
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >45 bp
ATGGACGAGGAATACGATGTGATCGTGCTGGGGACCGGTCTCACC
Enzyme 38 GenBank Gene ID X79354 Link Image
Enzyme 38 GeneCard ID GDI1 Link Image
Enzyme 38 GenAtlas ID GDI1 Link Image
Enzyme 38 HGNC ID HGNC:4226 Link Image
Enzyme 38 Chromosome Location X
Enzyme 38 Locus Xq28
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 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. 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]
  6. 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]
  7. 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]
  8. 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 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 7136
Enzyme 39 Name Proto-oncogene DBL
Enzyme 39 Synonyms
  1. Proto-oncogene MCF-2[Contains: MCF2-transforming protein
  2. DBL-transforming protein]
Enzyme 39 Gene Name MCF2
Enzyme 39 Protein Sequence >Proto-oncogene DBL
MAEANPRRGKMRFRRNAASFPGNLHLVLVLRPTSFLQRTFTDIGFWFSQEDFMLKLPVVM
LSSVSDLLTYIDDKQLTPELGGTLQYCHSEWIIFRNAIENFALTVKEMAQMLQSFGTELA
ETELPDDIPSIEEILAIRAERYHLLKNDITAVTKEGKILLTNLEVPDTEGAVSSRLECHR
QISGDWQTINKLLTQVHDMETAFDGFWEKHQLKMEQYLQLWKFEQDFQQLVTEVEFLLNQ
QAELADVTGTIAQVKQKIKKLENLDENSQELLSKAQFVILHGHKLAANHHYALDLICQRC
NELRYLSDILVNEIKAKRIQLSRTFKMHKLLQQARQCCDEGECLLANQEIDKFQSKEDAQ
KALQDIENFLEMALPFINYEPETLQYEFDVILSPELKVQMKTIQLKLENIRSIFENQQAG
FRNLADKHVRPIQFVVPTPENLVTSGTPFFSSKQGKKTWRQNQSNLKIEVVPDCQEKRSS
GPSSSLDNGNSLDVLKNHVLNELIQTERVYVRELYTVLLGYRAEMDNPEMFDLMPPLLRN
KKDILFGNMAEIYEFHNDIFLSSLENCAHAPERVGPCFLERKDDFQMYAKYCQNKPRSET
IWRKYSECAFFQECQRKLKHRLRLDSYLLKPVQRITKYQLLLKELLKYSKDCEGSALLKK
ALDAMLDLLKSVNDSMHQIAINGYIGNLNELGKMIMQGGFSVWIGHKKGATKMKDLARFK
PMQRHLFLYEKAIVFCKRRVESGEGSDRYPSYSFKHCWKMDEVGITEYVKGDNRKFEIWY
GEKEEVYIVQASNVDVKMTWLKEIRNILLKQQELLTVKKRKQQDQLTERDKFQISLQQND
EKQQGAFISTEETELEHTSTVVEVCEAIASVQAEANTVWTEASQSAEISEEPAEWSSNYF
YPTYDENEEENRPLMRPVSEMALLY
Enzyme 39 Number of Residues 925
Enzyme 39 Molecular Weight 107675
Enzyme 39 Theoretical pI 5.87
Enzyme 39 GO Classification
Function
  • GTPase regulator activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • small GTPase regulator activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • signal transduction
Component
Enzyme 39 General Function Not Available
Enzyme 39 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 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 30482 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID P10911 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name MCF2_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >2778 bp
ATGGCAGAAGCAAATCCCCGGAGAGGCAAGATGAGGTTCAGAAGGAATGCGGCTTCCTTC
CCTGGGAACTTGCACTTGGTTTTGGTTTTACGTCCTACCAGCTTTCTTCAACGAACGTTC
ACAGACATTGGATTTTGGTTTAGTCAGGAGGATTTTATGCCTAAATTACCAGTTGTTATG
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
TTGTTGAAGGAGCTATTAAAATATAGCAAAGACTGTGAAGGTTCTGCTCTGTTGAAGAAG
GCACTCGATGCAATGCTGGATTTACTGAAGTCAGTTAATGATTCTATGCATCAGATTGCA
ATAAATGGCTATATTGGAAACTTAAATGAACTGGGCAAGATGATAATGCAAGGTGGATTC
AGCGTTTGGATAGGGCACAAGAAAGGTGCTACAAAAATGAAGGATTTGGCTAGATTCAAA
CCAATGCAGCGACACCTTTTCTTGTATGAAAAAGCCATTGTTTTTTGCAAAAGGCGTGTT
GAAAGTGGAGAAGGCTCTGACAGATACCCGTCATACAGTTTTAAACACTGTTGGAAAATG
GATGAAGTTGGAATCACTGAATATGTAAAAGGTGATAACCGCAAGTTTGAAATCTGGTAT
GGTGAAAAGGAAGAAGTTTATATTGTCCAGGCTTCTAATGTAGATGTGAAGATGACGTGG
CTAAAAGAAATAAGAAATATTTTGTTGAAGCAGCAGGAACTTTTGACAGTTAAAAAAAGA
AAGCAACAGGATCAATTAACAGAACGGGATAAGTTTCAGATTTCTCTTCAGCAGAATGAT
GAAAAGCAACAGGGAGCTTTTATAAGTACTGAGGAAACTGAATTGGAACACACCAGCACT
GTGGTGGAGGTCTGTGAGGCAATTGCGTCAGTTCAGGCAGAAGCAAATACAGTTTGGACT
GAGGCATCACAATCTGCAGAAATCTCTGAAGAACCTGCGGAATGGTCAAGCAACTATTTC
TACCCTACTTATGATGAAAATGAAGAAGAAAATAGGCCCCTCATGAGACCTGTGTCGGAG
ATGGCTCTCCTATATTGA
Enzyme 39 GenBank Gene ID X12556 Link Image
Enzyme 39 GeneCard ID MCF2 Link Image
Enzyme 39 GenAtlas ID MCF2 Link Image
Enzyme 39 HGNC ID HGNC:6940 Link Image
Enzyme 39 Chromosome Location X
Enzyme 39 Locus Xq27
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 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. 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]
  4. 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]
  5. 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]
  6. 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]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 7137
Enzyme 40 Name Cell division control protein 42 homolog precursor
Enzyme 40 Synonyms
  1. G25K GTP-binding protein
Enzyme 40 Gene Name CDC42
Enzyme 40 Protein Sequence >Cell division control protein 42 homolog precursor
MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAG
QEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLR
DDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQRGLKNVFDEAILAALEPP
ETQPKRKCCIF
Enzyme 40 Number of Residues 191
Enzyme 40 Molecular Weight 21311
Enzyme 40 Theoretical pI 5.83
Enzyme 40 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • signal transduction
  • small GTPase mediated signal transduction
Component
Enzyme 40 General Function Not Available
Enzyme 40 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 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 182857 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID P60953 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name CDC42_HUMAN Link Image
Enzyme 40 PDB ID 1GRN Link Image
Enzyme 40 PDB File Show
Enzyme 40 3D Structure
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >576 bp
ATGCAGACAATTAAGTGTGTTGTTGTGGGCGATGGTGCTGTTGGTAAAACATGTCTCCTG
ATATCCTACACAACAAACAAATTTCCATCGGAATATGTACCGACTGTTTTTGACAACTAT
GCAGTCACAGTTATGATTGGTGGAGAACCATATACTCTTGGACTTTTTGATACTGCAGGG
CAAGAGGATTATGACAGATTACGACCGCTGAGTTATCCACAAACAGATGTATTTCTAGTC
TGTTTTTCAGTGGTCTCTCCATCTTCATTTGAAAACGTGAAAGAAAAGTGGGTGCCTGAG
ATAACTCACCACTGTCCAAAGACTCCTTTCTTGCTTGTTGGGACTCAAATTGATCTCAGA
GATGACCCCTCTACTATTGAGAAACTTGCCAAGAACAAACAGAAGCCTATCACTCCAGAG
ACTGCTGAAAAGCTGGCCCGTGACCTGAAGGCTGTCAAGTATGTGGAGTGTTCTGCACTT
ACACAGAGAGGTCTGAAGAATGTGTTTGATGAGGCTATCCTAGCTGCCCTCGAGCCTCCG
GAAACTCAACCCAAAAGGAAGTGCTGTATATTCTAA
Enzyme 40 GenBank Gene ID M35543 Link Image
Enzyme 40 GeneCard ID CDC42 Link Image
Enzyme 40 GenAtlas ID CDC42 Link Image
Enzyme 40 HGNC ID HGNC:1736 Link Image
Enzyme 40 Chromosome Location 1
Enzyme 40 Locus 1p36.1
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 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. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 7138
Enzyme 41 Name Rab GDP dissociation inhibitor beta
Enzyme 41 Synonyms
  1. Rab GDI beta
  2. Guanosine diphosphate dissociation inhibitor 2
  3. GDI-2
Enzyme 41 Gene Name GDI2
Enzyme 41 Protein Sequence >Rab GDP dissociation inhibitor beta
MNEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDRNPYYGGESASITPLEDLYKRFKIPG
SPPESMGRGRDWNVDLIPKFLMANGQLVKMLLYTEVTRYLDFKVTEGSFVYKGGKIYKVP
STEAEALASSLMGLFEKRRFRKFLVYVANFDEKDPRTFEGIDPKKTTMRDVYKKFDLGQD
VIDFTGHALALYRTDDYLDQPCYETINRIKLYSESLARYGKSPYLYPLYGLGELPQGFAR
LSAIYGGTYMLNKPIEEIIVQNGKVIGVKSEGEIARCKQLICDPSYVKDRVEKVGQVIRV
ICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISFAHNVAAQGKYIAIVSTTVETK
EPEKEIRPALELLEPIEQKFVSISDLLVPKDLGTESQIFISRTYDATTHFETTCDDIKNI
YKRMTGSEFDFEEMKRKKNDIYGED
Enzyme 41 Number of Residues 445
Enzyme 41 Molecular Weight 50664
Enzyme 41 Theoretical pI 6.39
Enzyme 41 GO Classification
Function
  • GDP-dissociation inhibitor activity
  • GTPase regulator activity
  • Rab GDP-dissociation inhibitor activity
  • enzyme regulator activity
  • small GTPase regulator activity
Process
  • cellular physiological process
  • physiological process
  • protein transport
  • regulation of GTPase activity
  • regulation of biological process
  • regulation of enzyme activity
  • regulation of hydrolase activity
  • transport
Component
Enzyme 41 General Function Not Available
Enzyme 41 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 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 285975 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID P50395 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name GDIB_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >1338 bp
ATGGACGAGGAATACGATGTGATCGTGCTGGGCACCGGCCTGACGGAATGTATCCTGTCA
GGTATAATGTCAGTGAATGGCAAGAAAGTTCTTCATATGGATCGAAACCCTTACTACGGA
GGAGAAAGTGCATCTATAACACCATTGGAAGATTTATACAAAAGATTTAAAATACCAGGA
TCACCACCCGAGTCAATGGGGAGAGGAAGAGACTGGAATGTTGACTTGATTCCCAAGTTC
CTTATGGCTAATGGTCAGCTGGTTAAGATGCTGCTTTATACAGAGGTAACTCGCTATCTG
GATTTTAAAGTGACTGAAGGGAGCTTTGTCTATAAGGGTGGAAAAATCTACAAGGTTCCT
TCCACTGAAGCAGAAGCCCTGGCATCTAGCCTAATGGGATTGTTTGAAAAACGTCGCTTC
AGGAAATTCCTAGTGTATGTTGCCAACTTCGATGAAAAAGATCCAAGAACTTTTGAAGGC
ATTGATCCTAAGAAGACCACAATGCGAGATGTGTATAAGAAATTTGATTTGGGTCAAGAC
GTTATAGATTTTACTGGTCATGCTCTTGCACTTTACAGAACTGATGATTACTTAGATCAA
CCGTGTTATGAAACCATTAATAGAATTAAACTTTACAGTGAATCTTTGGCAAGATATGGC
AAAAGCCCATACCTTTATCCACTCTATGGCCTTGGAGAACTGCCCCAAGGATTTGCAAGG
CTAAGTGCTATTTATGGAGGTACCTATATGCTGAATAAACCCATTGAAGAAATCATTGTA
CAGAATGGAAAAGTAATTGGTGTAAAATCTGAAGGAGAAATTGCTCGCTGTAAGCAGCTC
ATCTGTGACCCCAGCTACGTAAAAGATCGGGTAGAAAAAGTGGGCCAGGTGATCAGAGTT
ATTTGCATCCTCAGCCACCCCATCAAGAACACCAATGATGCCAACTCCTGCCAGATCATT
ATTCCACAGAACCAAGTCAATCGAAAGTCAGATATCTACGTCTGCATGATCTCCTTTGCG
CACAATGTAGCAGCACAAGGGAAGTACATTGCTATAGTTAGTACAACTGTGGAAACCAAG
GAGCCTGAGAAGGAAATCAGACCAGCTTTGGAGCTCTTGGAACCAATTGAACAGAAATTT
GTTAGCATCAGTGACCTCCTGGTACCAAAAGACTTGGGAACAGAAAGCCAGATCTTTATT
TCCCGCACATATGATGCCACCACTCATTTTGAGACAACGTGTGATGACATTAAAAACATC
TATAAGAGGATGACAGGATCAGAGTTTGACTTTGAGGAAATGAAGCGCAAGAAGAATGAC
ATCTATGGGGAAGACTAA
Enzyme 41 GenBank Gene ID D13988 Link Image
Enzyme 41 GeneCard ID GDI2 Link Image
Enzyme 41 GenAtlas ID GDI2 Link Image
Enzyme 41 HGNC ID HGNC:4227 Link Image
Enzyme 41 Chromosome Location 10
Enzyme 41 Locus 10p15
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 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. 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]
  3. 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]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 7139
Enzyme 42 Name Rho GDP-dissociation inhibitor 1
Enzyme 42 Synonyms
  1. Rho GDI 1
  2. Rho-GDI alpha
Enzyme 42 Gene Name ARHGDIA
Enzyme 42 Protein Sequence >Rho GDP-dissociation inhibitor 1
MAEQEPTAEQLAQIAAENEEDEHSVNYKPPAQKSIQEIQELDKDDESLRKYKEALLGRVA
VSADPNVPNVVVTGLTLVCSSAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNR
EIVSGMKYIQHTYRKGVKIDKTDYMVGSYGPRAEEYEFLTPVEEAPKGMLARGSYSIKSR
FTDDDKTDHLSWEWNLTIKKDWKD
Enzyme 42 Number of Residues 204
Enzyme 42 Molecular Weight 23207
Enzyme 42 Theoretical pI 4.74
Enzyme 42 GO Classification
Function
  • GDP-dissociation inhibitor activity
  • GTPase regulator activity
  • Rho GDP-dissociation inhibitor activity
  • enzyme regulator activity
  • small GTPase regulator activity
Process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 42 General Function Not Available
Enzyme 42 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 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 456191 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID P52565 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name GDIR_HUMAN Link Image
Enzyme 42 PDB ID 1HH4 Link Image
Enzyme 42 PDB File Show
Enzyme 42 3D Structure
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >615 bp
ATGGCTGAGCAGGAGCCCACAGCCGAGCAGCTGGCCCAGATTGCAGCGGAGAACGAGGAG
GATGAGCACTCGGTCAACTACAAGCCCCCGGCCCAGAAGAGCATCCAGGAGATCCAGGAG
CTGGACAAGGACGACGAGAGCCTGCGAAAGTACAAGGAGGCCCTGCTGGGCCGCGTGGCC
GTTTCCGCAGACCCCAACGTCCCCAACGTCGTGGTGACTGGCCTGACCCTGGTGTGCAGC
TCGGCCCCGGGCCCCCTGGAGCTGGACCTGACGGGCGACCTGGAGAGCTTCAAGAAGCAG
TCGTTTGTGCTGAAGGAGGGTGTGGAGTACCGGATAAAAATCTCTTTCCGGGTTAACCGA
GAGATAGTGTCCGGCATGAAGTACATCCAGCATACGTACAGGAAAGGCGTCAAGATTGAC
AAGACTGACTACATGGTAGGCAGCTATGGGCCCCGGGCCGAGGAGTACGAGTTCCTGACC
CCCGTGGAGGAGGCACCCAAGGGTATGCTGGCCCGGGGCAGCTACAGCATCAAGTCCCGC
TTCACAGACGACGACAAGACCGACCACCTGTCCTGGGAGTGGAATCTCACCATCAAGAAG
GACTGGAAGGACTGA
Enzyme 42 GenBank Gene ID X69550 Link Image
Enzyme 42 GeneCard ID ARHGDIA Link Image
Enzyme 42 GenAtlas ID ARHGDIA Link Image
Enzyme 42 HGNC ID HGNC:678 Link Image
Enzyme 42 Chromosome Location 17
Enzyme 42 Locus 17q25.3
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 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. 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 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 7140
Enzyme 43 Name Rho GDP-dissociation inhibitor 2
Enzyme 43 Synonyms
  1. Rho GDI 2
  2. Rho-GDI beta
  3. Ly-GDI
Enzyme 43 Gene Name ARHGDIB
Enzyme 43 Protein Sequence >Rho GDP-dissociation inhibitor 2
MTEKAPEPHVEEDDDDELDSKLNYKPPPQKSLKELQEMDKDDESLIKYKKTLLGDGPVVT
DPKAPNVVVTRLTLVCESAPGPITMDLTGDLEALKKETIVLKEGSEYRVKIHFKVNRDIV
SGLKYVQHTYRTGVKVDKATFMVGSYGPRPEEYEFLTPVEEAPKGMLARGTYHNKSFFTD
DDKQDHLSWEWNLSIKKEWTE
Enzyme 43 Number of Residues 201
Enzyme 43 Molecular Weight 22988
Enzyme 43 Theoretical pI 4.84
Enzyme 43 GO Classification
Function
  • GDP-dissociation inhibitor activity
  • GTPase regulator activity
  • Rho GDP-dissociation inhibitor activity
  • enzyme regulator activity
  • small GTPase regulator activity
Process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 43 General Function Not Available
Enzyme 43 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 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 404045 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID P52566 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name GDIS_HUMAN Link Image
Enzyme 43 PDB ID 1DS6 Link Image
Enzyme 43 PDB File Show
Enzyme 43 3D Structure
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >606 bp
ATGACTGAAAAAGCCCCAGAGCCACATGTGGAGGAGGATGACGATGATGAGCTGGACAGC
AAGCTCAATTATAAGCCTCCACCACAGAAGTCCCTGAAAGAGCTGCAGGAAATGGACAAA
GATGATGAGAGTCTAATTAAGTACAAGAAAACGCTGCTGGGAGATGGTCCTGTGGTGACA
GATCCGAAAGCCCCCAATGTCGTTGTCACCCGGCTCACCCTGGTTTGTGAGAGTGCCCCG
GGACCAATCACCATGGACCTTACTGGAGATCTGGAAGCCCTCAAAAAGGAAACCATTGTG
TTAAAGGAAGGTTCTGAATATAGAGTCAAAATTCACTTCAAAGTGAACAGGGATATTGTG
TCAGGCCTGAAATACGTTCAGCACACCTACAGGACTGGGGTGAAAGTGGATAAAGCAACA
TTTATGGTTGGCAGCTATGGACCTCGGCCTGAGGAGTATGAGTTCCTCACTCCAGTTGAG
GAGGCTCCCAAGGGCATGCTGGCCCGAGGCACGTACCACAACAAGTCCTTCTTCACCGAC
GATGACAAGCAAGACCACCTCAGCTGGGAGTGGAACCTGTCGATTAAGAAGGAGTGGACA
GAATGA
Enzyme 43 GenBank Gene ID L20688 Link Image
Enzyme 43 GeneCard ID ARHGDIB Link Image
Enzyme 43 GenAtlas ID ARHGDIB Link Image
Enzyme 43 HGNC ID HGNC:679 Link Image
Enzyme 43 Chromosome Location 12
Enzyme 43 Locus 12p12.3
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 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. 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 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 7141
Enzyme 44 Name Ras-related C3 botulinum toxin substrate 2 precursor
Enzyme 44 Synonyms
  1. p21-Rac2
  2. Small G protein
  3. GX
Enzyme 44 Gene Name RAC2
Enzyme 44 Protein Sequence >Ras-related C3 botulinum toxin substrate 2 precursor
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDSKPVNLGLWDTAG
QEDYDRLRPLSYPQTDVFLICFSLVSPASYENVRAKWFPEVRHHCPSTPIILVGTKLDLR
DDKDTIEKLKEKKLAPITYPQGLALAKEIDSVKYLECSALTQRGLKTVFDEAIRAVLCPQ
PTRQQKRACSLL
Enzyme 44 Number of Residues 192
Enzyme 44 Molecular Weight 21429
Enzyme 44 Theoretical pI 7.70
Enzyme 44 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • signal transduction
  • small GTPase mediated signal transduction
Component
Enzyme 44 General Function Not Available
Enzyme 44 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. Seems to be involved in the regulation of the NADPH oxidase
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 190826 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID P15153 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name RAC2_HUMAN Link Image
Enzyme 44 PDB ID 1DS6 Link Image
Enzyme 44 PDB File Show
Enzyme 44 3D Structure
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence >579 bp
ATGCAGGCCATCAAGTGTGTGGTGGTGGGAGATGGGGCCGTGGGCAAGACCTGCCTTCTC
ATCAGCTACACCACCAACGCCTTTCCCGGAGAGTACATCCCCACCGTGTTTGACAACTAT
TCAGCCAATGTGATGGTGGACAGCAAGCCAGTGAACCTGGGGCTGTGGGACACTGCTGGG
CAGGAGGACTACGACCGTCTCCGGCCGCTCTCCTATCCACAGACGGACGTCTTCCTCATC
TGCTTCTCCCTCGTCAGCCCAGCCTCTTATGAGAACGTCCGCGCCAAGTGGTTCCCAGAA
GTGCGGCACCACTGCCCCAGCACACCCATCATCCTGGTGGGCACCAAGCTGGACCTGCGG
GACGACAAGGACACCATCGAGAAACTGAAGGAGAAGAAGCTGGCTCCCATCACCTACCCG
CAGGGCCTGGCACTGGCCAAGGAGATTGACTCGGTGAAATACCTGGAGTGCTCAGCCCTC
ACCCAGAGAGGCCTGAAAACCGTGTTCGACGAGGCCATCCGGGCCGTGCTGTGCCCTCAG
CCCACGCGGCAGCAGAAGCGCGCCTGCAGCCTCCTCTAG
Enzyme 44 GenBank Gene ID M29871 Link Image
Enzyme 44 GeneCard ID RAC2 Link Image
Enzyme 44 GenAtlas ID RAC2 Link Image
Enzyme 44 HGNC ID HGNC:9802 Link Image
Enzyme 44 Chromosome Location 22
Enzyme 44 Locus 22q13.1
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 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. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 7272
Enzyme 45 Name Elongation factor 1-alpha 1
Enzyme 45 Synonyms
  1. EF-1-alpha-1
  2. Elongation factor 1 A-1
  3. eEF1A-1
  4. Elongation factor Tu
  5. EF-Tu
  6. Leukocyte receptor cluster member 7
Enzyme 45 Gene Name EEF1A1
Enzyme 45 Protein Sequence >Elongation factor 1-alpha 1
MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVL
DKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGV
GEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKK
IGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTR
PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALS
EALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPV
LDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPP
LGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK
Enzyme 45 Number of Residues 462
Enzyme 45 Molecular Weight 50141
Enzyme 45 Theoretical pI 9.50
Enzyme 45 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • nucleic acid binding
  • nucleotide binding
  • purine nucleotide binding
  • translation elongation factor activity
  • translation factor activity, nucleic acid binding
Process
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein biosynthesis
  • translation
  • translational elongation
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 45 General Function Translation, ribosomal structure and biogenesis
Enzyme 45 Specific Function This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis
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 31098 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID P68104 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name EF1A1_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 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 45 GenBank Gene ID X03558 Link Image
Enzyme 45 GeneCard ID EEF1A1 Link Image
Enzyme 45 GenAtlas ID EEF1A1 Link Image
Enzyme 45 HGNC ID HGNC:3189 Link Image
Enzyme 45 Chromosome Location 6
Enzyme 45 Locus 6q14.1
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 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. 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]
  5. 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]
  6. 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]
  7. 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]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 7342
Enzyme 46 Name Vinexin
Enzyme 46 Synonyms
  1. Sorbin and SH3 domain-containing protein 3
  2. SH3-containing adapter molecule 1
  3. SCAM-1
Enzyme 46 Gene Name SORBS3
Enzyme 46 Protein Sequence >Vinexin
MQGPPRSLRAGLSLDDFIPGHLQSHIGSSSRGTRVPVIRNGGSNTLNFQFHDPAPRTVCN
GGYTPRRDASQHPDPAWYQTWPGPGSKPSASTKIPASQHTQNWSATWTKDSKRRDKRWVK
YEGIGPVDESGMPIAPRSSVDRPRDWYRRMFQQIHRKMPDLQLDWTFEEPPRDPRHLGAQ
QRPAHRPGPATSSSGRSWDHSEELPRSTFNYRPGAFSTVLQPSNQVLRRREKVDNVWTEE
SWNQFLQELETGQRPKKPLVDDPGEKPSQPIEVLLERELAELSAELDKDLRAIETRLPSP
KSSPAPRRAPEQRPPAGPASAWSSSYPHAPYLGSARSLSPHKMADGGSPFLGRRDFVYPS
STRDPSASNGGGSPARREEKKRKAARLKFDFQAQSPKELTLQKGDIVYIHKEVDKNWLEG
EHHGRLGIFPANYVEVLPADEIPKPIKPPTYQVLEYGEAVAQYTFKGDLEVELSFRKGEH
ICLIRKVNENWYEGRITGTGRQGIFPASYVQVSREPRLRLCDDGPQLPTSPRLTAAARSA
RHPSSPSALRSPADPTDLGGQTSPRRTGFSFPTQEPRPQTQNLGTPGPALSHSRGPSHPL
DLGTSSPNTSQIHWTPYRAMYQYRPQNEDELELREGDRVDVMQQCDDGWFVGVSRRTQKF
GTFPGNYVAPV
Enzyme 46 Number of Residues 671
Enzyme 46 Molecular Weight 75330
Enzyme 46 Theoretical pI 9.87
Enzyme 46 GO Classification Not Available
Enzyme 46 General Function Not Available
Enzyme 46 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 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • 1-2
Enzyme 46 Transmembrane Regions Not Available
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 4894215 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID O60504 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name VINEX_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >990 bp
ATGGCTGATGGAGGAAGCCCCTTCCTAGGTCGGAGGGACTTTGTCTACCCTTCCTCAACC
CGAGACCCTAGTGCCTCTAACGGAGGGGGCAGCCCAGCCAGGAGGGAAGAGAAGAAGAGA
AAGGCCGCCAGGCTCAAGTTTGACTTCCAGGCGCAGTCCCCCAAGGAGCTGACTCTGCAG
AAGGGTGACATTGTCTACATCCACAAGGAGGTGGACAAGAACTGGCTGGAGGGAGAGCAC
CACGGCCGCCTGGGCATCTTCCCTGCTAATTATGTGGAGGTGCTGCCCGCAGATGAGATC
CCTAAGCCCATCAAGCCCCCGACCTACCAGGTGCTGGAGTATGGAGAGGCTGTGGCCCAG
TACACCTTCAAGGGGGACCTGGAGGTGGAGCTGTCCTTCCGCAAGGGAGAGCACATCTGC
CTGATCCGCAAGGTGAACGAGAACTGGTACGAGGGACGCATCACGGGCACGGGGCGCCAA
GGCATATTCCCTGCCAGCTACGTGCAGGTGTCTCGTGAACCCCGGCTCCGGCTCTGTGAC
GACGGCCCCCAGCTCCCCACGTCTCCCCGCCTGACCGCTGCCGCCCGCTCAGCCCGTCAC
CCCAGCTCCCCCTCAGCCCTGCGCAGCCCAGCTGACCCCACCGACTTGGGGGGACAGACC
TCCCCCCGTCGCACTGGCTTCTCCTTCCCCACCCAGGAGCCTAGACCCCAGACCCAGAAT
TTTGGCACCCCTGGTCCAGCTTTGTCCCACTCTCGAGGTCCCAGCCATCCCCTGGACCTG
GGGACCTCCTCTCCTAACACCTCTCAGATACACTGGACCCCGTACCGGGCGATGTACCAG
TACAGGCCCCAGAACGAAGACGAGCTGGAGCTGCGCGAGGGGGACAGGGTGGATGTCATG
CAGCAGTGTGACGATGGCTGGTTTGTGGGTGTCTCCCGGAGGACCCAGAAATTCGGAACG
TTCCCTGGAAATTACGTTGCCCCGGTGTGA
Enzyme 46 GenBank Gene ID AF064807 Link Image
Enzyme 46 GeneCard ID SORBS3 Link Image
Enzyme 46 GenAtlas ID SORBS3 Link Image
Enzyme 46 HGNC ID HGNC:30907 Link Image
Enzyme 46 Chromosome Location 8
Enzyme 46 Locus 8p21.3
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 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. 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]
  3. 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]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 7383
Enzyme 47 Name GTPase HRas precursor
Enzyme 47 Synonyms
  1. Transforming protein p21
  2. p21ras
  3. H-Ras-1
  4. c-H-ras
  5. Ha-Ras
Enzyme 47 Gene Name HRAS
Enzyme 47 Protein Sequence >GTPase HRas precursor
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG
QEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL
AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPG
CMSCKCVLS
Enzyme 47 Number of Residues 189
Enzyme 47 Molecular Weight 21298
Enzyme 47 Theoretical pI 4.94
Enzyme 47 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • signal transduction
  • small GTPase mediated signal transduction
Component
Enzyme 47 General Function Not Available
Enzyme 47 Specific Function Ras proteins bind GDP/GTP and possess intrinsic GTPase activity
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 190891 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID P01112 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name RASH_HUMAN Link Image
Enzyme 47 PDB ID 4Q21 Link Image
Enzyme 47 PDB File Show
Enzyme 47 3D Structure
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence >570 bp
ATGACGGAATATAAGCTGGTGGTGGTGGGCGCCGGCGGTGTGGGCAAGAGTGCGCTGACC
ATCCAGCTGATCCAGAACCATTTTGTGGACGAATACGACCCCACTATAGAGGATTCCTAC
CGGAAGCAGGTGGTCATTGATGGGGAGACGTGCCTGTTGGACATCCTGGATACCGCCGGC
CAGGAGGAGTACAGCGCCATGCGGGACCAGTACATGCGCACCGGGGAGGGCTTCCTGTGT
GTGTTTGCCATCAACAACACCAAGTCTTTTGAGGACATCCACCAGTACAGGGAGCAGATC
AAACGGGTGAAGGACTCGGATGACGTGCCCATGGTGCTGGTGGGGAACAAGTGTGACCTG
GCTGCACGCACTGTGGAATCTCGGCAGGCTCAGGACCTCGCCCGAAGCTACGGCATCCCC
TACATCGAGACCTCGGCCAAGACCCGGCAGGGAGTGGAGGATGCCTTCTACACGTTGGTG
CGTGAGATCCGGCAGCACAAGCTGCGGAAGCTGAACCCTCCTGATGAGAGTGGCCCCGGC
TGCATGAGCTGCAAGTGTGTGCTCTCCTGA
Enzyme 47 GenBank Gene ID J00277 Link Image
Enzyme 47 GeneCard ID HRAS Link Image
Enzyme 47 GenAtlas ID HRAS Link Image
Enzyme 47 HGNC ID HGNC:5173 Link Image
Enzyme 47 Chromosome Location 11
Enzyme 47 Locus 11p15.5
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 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. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
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  10. 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]
  11. 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]
  12. 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]
  13. 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]
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Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 7391
Enzyme 48 Name Rho-related GTP-binding protein RhoQ precursor
Enzyme 48 Synonyms
  1. Ras-related GTP- binding protein TC10
Enzyme 48 Gene Name RHOQ
Enzyme 48 Protein Sequence >Rho-related GTP-binding protein RhoQ precursor
MAHGPGALMLKCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVSVTVGGKQYLLG
LYDTAGQEDYDRLRPLSYPMTDVFLICFSVVNPASFQNVKEEWVPELKEYAPNVPFLLIG
TQIDLRDDPKTLARLNDMKEKPICVEQGQKLAKEIGACCYVECSALTQKGLKTVFDEAII
AILTPKKHTVKKRIGSRCINCCLIT
Enzyme 48 Number of Residues 205
Enzyme 48 Molecular Weight 22660
Enzyme 48 Theoretical pI 6.25
Enzyme 48 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • signal transduction
  • small GTPase mediated signal transduction
Component
Enzyme 48 General Function Not Available
Enzyme 48 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 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 190881 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID P17081 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name RHOQ_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence >642 bp
ATGCCCGGAGCCGGCCGCAGCAGCATGGCTCACGGGCCCGGCGCGCTGATGCTCAAGTGC
GTGGTGGTCGGCGACGGGGCGGTGGGCAAGACGTGCCTACTCATGAGCTATGCCAACGAC
GCCTTCCCGGAGGAGTACGTGCCCACCGTCTTCGACCACTACGCAGTCAGCGTCACCGTG
GGGGGCAAGCAGTACCTCCTAGGACTCTATGACACGGCCGGACAGGAAGACTATGACCGT
CTGAGGCCTTTATCTTACCCAATGACCGATGTCTTCCTTATATGCTTCTCGGTGGTAAAT
CCAGCCTCATTTCAAAATGTGAAAGAGGAGTGGGTACCGGAACTTAAGGAATACGCACCA
AATGTACCCTT