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Human Metabolome Database Version 2.5

 

Showing metabocard for Guanosine triphosphate (HMDB01273)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2012-01-19 15:56:53
Accession Number HMDB01273
Secondary Accession Numbers Not Available
Common Name Guanosine triphosphate
Description Guanosine triphosphate (GTP) is a guanine nucleotide containing three phosphate groups esterified to the sugar moiety. GTP functions as a carrier of phosphates and pyrophosphates involved in channeling chemical energy into specific biosynthetic pathways. GTP activates the signal transducing G proteins which are involved in various cellular processes including proliferation, differentiation, and activation of several intracellular kinase cascades. Proliferation and apoptosis are regulated in part by the hydrolysis of GTP by small GTPases Ras and Rho. Another type of small GTPase, Rab, plays a role in the docking and fusion of vesicles and may also be involved in vesicle formation. In addition to its role in signal transduction, GTP also serves as an energy-rich precursor of mononucleotide units in the enzymatic biosynthesis of DNA and RNA.
Synonyms
  1. 5'-GTP
  2. GTG
  3. GTP
  4. Guanosine 5'-(tetrahydrogen triphosphate)
  5. Guanosine 5'-triphosphate
  6. Guanosine 5'-triphosphorate
  7. Guanosine 5'-triphosphoric acid
  8. Guanosine Triphosphate
  9. Guanosine mono(tetrahydrogen triphosphate) (ester)
  10. H4gtp
Chemical IUPAC Name [(2R,3S,4R,5R)-5-(2-amino-6-oxo-3H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl (hydroxy-phosphonooxyphosphoryl) hydrogen phosphate
Chemical Formula C10H16N5O14P3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide triphosphates
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 Folate biosynthesis
  • Component of Pyruvate metabolism
Application
Source
  • Endogenous
Average Molecular Weight 523.180
Monoisotopic Molecular Weight 522.990662
Isomeric SMILES NC1=NC2=C(N=CN2[C@@H]2O[C@H](COP(O)(=O)OP(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)OP(O)(O)=O)C(O)C2O)C(=O)N1
KEGG Compound ID C00044 Link Image
BioCyc ID GTP Link Image
BiGG ID 33641 Link Image
Wikipedia Link Guanosine triphosphate Link Image
NuGOwiki Link HMDB01273 Link Image
Metagene Link HMDB01273 Link Image
METLIN ID 6128 Link Image
PubChem Compound 6830 Link Image
PubChem Substance 819066 Link Image
ChEBI ID 15996 Link Image
CAS Registry Number 86-01-1
InChI Identifier InChI=1/C10H16N5O14P3/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(27-9)1-26-31(22,23)29-32(24,25)28-30(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H,24,25)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1
Synthesis Reference Stiller, Regine; Thiem, Joachim. Preparative enzymatic conversion of guanosine-5'-monophosphate to guanosine-5'-triphosphate. Synlett (1990), (11), 709-10.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 10.4 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.63 [Predicted by ALOGPS]; -5.8 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
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 Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • Extracellular
  • mitochondria
  • nucleus
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
Tissue Location
Tissue References
Neuron
Placenta
Platelet
Testes
Concentrations (Normal)
Biofluid Blood
Value 56.0 +/- 7.0 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 Blood
Value 108.0 +/- 35.0 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 CSF
Value 1.83 +/- 0.032 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 1.59 +/- 1.42 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 2.80 +/- 1.80 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 2.08 +/- 1.91 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 1.30 +/- 1.23 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 1.92 +/- 1.53 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
DNA Replication Fork SMP00477 Link Image
Gluconeogenesis SMP00128 Link Image map00010 Link Image
Pterine Biosynthesis SMP00005 Link Image map00790 Link Image
Purine Metabolism SMP00050 Link Image map00230 Link Image
Transcription/Translation SMP00019 Link Image
General References
  1. Lester HA, Steer ML, Levitzki A: Prostaglandin-stimulated GTP hydrolysis associated with activation of adenylate cyclase in human platelet membranes. Proc Natl Acad Sci U S A. 1982 Feb;79(3):719-23. [PubMed Link Image]
  2. Naylor EW, Ennis D, Davidson AG, Wong LT, Applegarth DA, Niederwieser A: Guanosine triphosphate cyclohydrolase I deficiency: early diagnosis by routine urine pteridine screening. Pediatrics. 1987 Mar;79(3):374-8. [PubMed Link Image]
  3. Iwanaga N, Yamamasu S, Tachibana D, Nishio J, Nakai Y, Shintaku H, Ishiko O: Activity of synthetic enzymes of tetrahydrobiopterin in the human placenta. Int J Mol Med. 2004 Jan;13(1):117-20. [PubMed Link Image]
  4. 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]
  5. Reichert LE Jr, Dattatreyamurty B: The follicle-stimulating hormone (FSH) receptor in testis: interaction with FSH, mechanism of signal transduction, and properties of the purified receptor. Biol Reprod. 1989 Jan;40(1):13-26. [PubMed Link Image]
  6. Schmidt VA, Scudder L, Devoe CE, Bernards A, Cupit LD, Bahou WF: IQGAP2 functions as a GTP-dependent effector protein in thrombin-induced platelet cytoskeletal reorganization. Blood. 2003 Apr 15;101(8):3021-8. Epub 2002 Dec 19. [PubMed Link Image]
  7. Chen Q, He Y, Yang K: Gene therapy for Parkinson's disease: progress and challenges. Curr Gene Ther. 2005 Feb;5(1):71-80. [PubMed Link Image]
  8. Wikipedia Link Image
Metabolic Enzymes
  1. Phospholipase D1
  2. Ectonucleoside triphosphate diphosphohydrolase 1
  3. Soluble calcium-activated nucleotidase 1
  4. Ectonucleoside triphosphate diphosphohydrolase 3
  5. Uridine-cytidine kinase 1
  6. Nucleoside diphosphate kinase, mitochondrial
  7. Nucleoside diphosphate kinase A
  8. Nucleoside diphosphate kinase 7
  9. Nucleoside diphosphate kinase B
  10. Nucleoside diphosphate kinase 3
  11. Nucleoside diphosphate kinase 6
  12. Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
  13. Fucose-1-phosphate guanylyltransferase
  14. Inosine triphosphate pyrophosphatase
  15. GMP synthase [glutamine-hydrolyzing]
  16. Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
  17. Adenylate kinase isoenzyme 5
  18. CTP synthase 1
  19. Glutamate dehydrogenase 1, mitochondrial
  20. Adenylate cyclase type 7
  21. Adenylate cyclase type 4
  22. Adenylate cyclase type 6
  23. Adenylate cyclase type 5
  24. Adenylate cyclase type 8
  25. Adenylate cyclase type 3
  26. Adenylate cyclase type 1
  27. DNA-directed RNA polymerase III subunit RPC4
  28. DNA-directed RNA polymerase II subunit RPB2
  29. DNA-directed RNA polymerase II subunit RPB1
  30. DNA-directed RNA polymerase, mitochondrial
  31. DNA-directed RNA polymerase I subunit RPA2
  32. DNA-directed RNA polymerase III subunit RPC7
  33. DNA-directed RNA polymerase III subunit RPC2
  34. DNA-directed RNA polymerase I subunit RPA49
  35. DNA-directed RNA polymerase III subunit RPC8
  36. DNA-directed RNA polymerase III subunit RPC10
  37. Pyruvate kinase isozymes M1/M2
  38. Pyruvate kinase isozymes R/L
  39. Ectonucleoside triphosphate diphosphohydrolase 4
  40. Adenylosuccinate synthetase isozyme 2
  41. Adenylosuccinate synthetase isozyme 1
  42. Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial
  43. Phosphoenolpyruvate carboxykinase [GTP], mitochondrial
  44. Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial
  45. Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
  46. Adenylate cyclase type 2
  47. GTP cyclohydrolase 1
  48. Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial
  49. Atrial natriuretic peptide receptor 2
  50. Guanylate cyclase soluble subunit beta-1
  51. Retinal guanylyl cyclase 1
  52. Guanylate cyclase soluble subunit alpha-3
  53. Atrial natriuretic peptide receptor 1
  54. Heat-stable enterotoxin receptor
  55. Guanylate cyclase soluble subunit alpha-2
  56. Retinal guanylyl cyclase 2
  57. Guanylate cyclase soluble subunit beta-2
  58. mRNA-capping enzyme
  59. Rap guanine nucleotide exchange factor 2
  60. Serine/threonine-protein kinase PAK 7
  61. Serine/threonine-protein kinase PAK 6
  62. Serine/threonine-protein kinase PAK 4
  63. Serine/threonine-protein kinase Nek9
  64. Citron Rho-interacting kinase
  65. Serine/threonine-protein kinase PAK 3
  66. Rho-associated protein kinase 1
  67. Serine/threonine-protein kinase PAK 2
  68. Ectonucleoside triphosphate diphosphohydrolase 2
  69. Rho-associated protein kinase 2
  70. Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2
  71. Rho guanine nucleotide exchange factor 1
  72. Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
  73. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
  74. GTP-binding nuclear protein Ran
  75. Ras-related C3 botulinum toxin substrate 1
  76. Rap1 GTPase-GDP dissociation stimulator 1
  77. Rho GDP-dissociation inhibitor 3
  78. Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
  79. Rab GDP dissociation inhibitor alpha
  80. Proto-oncogene DBL
  81. Cell division control protein 42 homolog
  82. Rab GDP dissociation inhibitor beta
  83. Rho GDP-dissociation inhibitor 1
  84. Rho GDP-dissociation inhibitor 2
  85. Ras-related C3 botulinum toxin substrate 2
  86. Elongation factor 1-alpha 1
  87. Elongation factor 1-alpha 2
  88. Vinexin
  89. Ras-related protein Rab-1A
  90. GTPase HRas
  91. Transforming protein RhoA
  92. GTP cyclohydrolase 1 feedback regulatory protein
  93. ADP-ribosylation factor 1
  94. Ras-related protein Rap-1A
  95. Rho-related GTP-binding protein RhoQ
  96. Breakpoint cluster region protein
  97. Molybdenum cofactor biosynthesis protein 1 A
  98. Guanine nucleotide-binding protein G(q) subunit alpha
  99. Guanine nucleotide-binding protein subunit alpha-11
  100. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-11
  101. Tubulin beta-3 chain
  102. Eukaryotic translation initiation factor 2 subunit 1
  103. RalA-binding protein 1
  104. Guanine nucleotide-binding protein G(t) subunit alpha-1
  105. Early endosome antigen 1
  106. Target of rapamycin complex 2 subunit MAPKAP1
  107. Uridine-cytidine kinase 2
  108. Protein ALEX
  109. Rap guanine nucleotide exchange factor 3
  110. Lysophosphatidic acid receptor 2
  111. Rho-related GTP-binding protein Rho6
  112. Selenocysteine-specific elongation factor
  113. Rap guanine nucleotide exchange factor 4
  114. Elongation factor 2
  115. Succinate-CoA ligase, ADP-forming, beta subunit
  116. Mannose-1-phosphate guanyltransferase beta
  117. Mannose-1-phosphate guanyltransferase alpha
  118. Acyl-coenzyme A synthetase ACSM1, mitochondrial
  119. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1
  120. Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
  121. Adenylate cyclase 1
  122. Guanylate cyclase 1, soluble, alpha 2
  123. Uncharacterized protein POLR3G
  124. Uridine-cytidine kinase-like 1
  125. Ectonucleoside triphosphate diphosphohydrolase 7
  126. Ectonucleoside triphosphate diphosphohydrolase 8
  127. RAS guanyl-releasing protein 1
  128. RAS guanyl-releasing protein 2
  129. Ras-specific guanine nucleotide-releasing factor 2
  130. Rho GTPase-activating protein 32
  131. Regulating synaptic membrane exocytosis protein 1
  132. Protein transport protein Sec31A
  133. Synaptotagmin-like protein 3
  134. Tubulin beta-2C chain
  135. Tubulin beta-4 chain
  136. Tubulin beta chain
  137. Tubulin beta-6 chain
  138. Phosducin
  139. Ras-related protein Rap-2a
  140. Rhophilin-2
  141. Synembryn-B
  142. Rap guanine nucleotide exchange factor 6
  143. Active breakpoint cluster region-related protein
  144. Acyl-coenzyme A synthetase ACSM6, mitochondrial
  145. ADP-ribosylation factor-like protein 2-binding protein
  146. ADP-ribosylation factor 3
  147. ADP-ribosylation factor 4
  148. ADP-ribosylation factor 5
  149. ADP-ribosylation factor 6
  150. ADP-ribosylation factor GTPase-activating protein 1
  151. ADP-ribosylation factor GTPase-activating protein 2
  152. ADP-ribosylation factor GTPase-activating protein 3
  153. Arfaptin-1
  154. Arfaptin-2
  155. Rho guanine nucleotide exchange factor 2
  156. Neuroepithelial cell-transforming gene 1 protein
  157. ADP-ribosylation factor-like protein 17
  158. ADP-ribosylation factor-like protein 4C
  159. ADP-ribosylation factor-like protein 5B
  160. Putative ADP-ribosylation factor-like protein 5C
  161. Brain-specific angiogenesis inhibitor 1-associated protein 2
  162. Brefeldin A-inhibited guanine nucleotide-exchange protein 1
  163. Brefeldin A-inhibited guanine nucleotide-exchange protein 2
  164. Cdc42 effector protein 2
  165. Cdc42 effector protein 3
  166. Cdc42 effector protein 5
  167. Cdc42 effector protein 4
  168. Cdc42 effector protein 1
  169. CDC42 small effector protein 1
  170. CDC42 small effector protein 2
  171. Cell cycle progression protein 1
  172. Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1
  173. Cdc42-interacting protein 4
  174. Coatomer subunit alpha
  175. Coatomer subunit beta'
  176. Coatomer subunit beta
  177. Coatomer subunit delta
  178. Coatomer subunit epsilon
  179. Coatomer subunit gamma-2
  180. Coatomer subunit gamma
  181. Coatomer subunit zeta-1
  182. Cytoplasmic FMR1-interacting protein 1
  183. Cytohesin-1
  184. Cytohesin-2
  185. Cytohesin-3
  186. Cytohesin-4
  187. Disheveled-associated activator of morphogenesis 1
  188. Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein
  189. Protein diaphanous homolog 1
  190. Protein diaphanous homolog 2
  191. Protein diaphanous homolog 3
  192. GTP-binding protein Di-Ras1
  193. GTP-binding protein Di-Ras2
  194. Dynamin-1-like protein
  195. Dedicator of cytokinesis protein 10
  196. Dedicator of cytokinesis protein 11
  197. Dedicator of cytokinesis protein 1
  198. Dedicator of cytokinesis protein 2
  199. Dedicator of cytokinesis protein 3
  200. Dedicator of cytokinesis protein 4
  201. Dedicator of cytokinesis protein 5
  202. Dedicator of cytokinesis protein 6
  203. Dedicator of cytokinesis protein 7
  204. Dedicator of cytokinesis protein 8
  205. Dedicator of cytokinesis protein 9
  206. Developmentally-regulated GTP-binding protein 1
  207. Developmentally-regulated GTP-binding protein 2
  208. Dynamin-1
  209. Dynamin-2
  210. Dynamin-3
  211. Putative elongation factor 1-alpha-like 3
  212. Elongation factor 1-beta
  213. Elongation factor 1-delta
  214. Elongation factor G, mitochondrial
  215. Ribosome-releasing factor 2, mitochondrial
  216. Elongation factor Ts, mitochondrial
  217. Elongation factor Tu, mitochondrial
  218. EH domain-containing protein 2
  219. Translation initiation factor eIF-2B subunit alpha
  220. Translation initiation factor eIF-2B subunit beta
  221. Translation initiation factor eIF-2B subunit delta
  222. Translation initiation factor eIF-2B subunit epsilon
  223. Translation initiation factor eIF-2B subunit gamma
  224. Eukaryotic translation initiation factor 2A
  225. GTP-binding protein era homolog
  226. Eukaryotic peptide chain release factor subunit 1
  227. Eukaryotic peptide chain release factor GTP-binding subunit ERF3A
  228. Eukaryotic peptide chain release factor GTP-binding subunit ERF3B
  229. Elongation factor Tu GTP-binding domain-containing protein 1
  230. Exocyst complex component 2
  231. Exocyst complex component 7
  232. Exocyst complex component 8
  233. Formin-binding protein 1-like
  234. F-box only protein 8
  235. FYVE, RhoGEF and PH domain-containing protein 1
  236. FYVE, RhoGEF and PH domain-containing protein 2
  237. FYVE, RhoGEF and PH domain-containing protein 3
  238. FYVE, RhoGEF and PH domain-containing protein 4
  239. FYVE, RhoGEF and PH domain-containing protein 5
  240. FYVE, RhoGEF and PH domain-containing protein 6
  241. Formin-binding protein 1
  242. GTPase-activating protein and VPS9 domain-containing protein 1
  243. Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
  244. Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2
  245. Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3
  246. Guanine nucleotide-binding protein subunit beta-4
  247. Guanine nucleotide-binding protein subunit beta-5
  248. Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
  249. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10
  250. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12
  251. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13
  252. Guanine nucleotide-binding protein G(T) subunit gamma-T1
  253. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3
  254. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-4
  255. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5
  256. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7
  257. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-8
  258. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-T2
  259. Interferon-induced guanylate-binding protein 1
  260. Interferon-induced guanylate-binding protein 2
  261. Guanylate-binding protein 3
  262. Guanylate-binding protein 4
  263. Guanylate-binding protein 6
  264. Guanylate-binding protein 7
  265. ADP-ribosylation factor-binding protein GGA1
  266. ADP-ribosylation factor-binding protein GGA2
  267. ADP-ribosylation factor-binding protein GGA3
  268. GTPase IMAP family member 1
  269. GTPase IMAP family member 2
  270. GTPase IMAP family member 4
  271. GTPase IMAP family member 5
  272. GTPase IMAP family member 6
  273. GTPase IMAP family member 7
  274. GTPase IMAP family member 8
  275. Ral guanine nucleotide dissociation stimulator
  276. Guanine nucleotide-binding protein-like 1
  277. Guanine nucleotide-binding protein-like 3
  278. Guanine nucleotide-binding protein-like 3-like protein
  279. Golgin-45
  280. Golgin subfamily A member 2
  281. Golgin subfamily A member 5
  282. RAS guanyl-releasing protein 4
  283. GTP-binding protein 1
  284. GTP-binding protein 2
  285. tRNA modification GTPase GTPBP3, mitochondrial
  286. GTP-binding protein 5
  287. Putative GTP-binding protein 6
  288. GTP-binding protein 10
  289. GTP-binding protein GUF1 homolog
  290. PTB domain-containing engulfment adapter protein 1
  291. HBS1-like protein
  292. Probable E3 ubiquitin-protein ligase HERC1
  293. Protein-cysteine N-palmitoyltransferase HHAT
  294. Eukaryotic translation initiation factor 2 subunit 2
  295. Eukaryotic translation initiation factor 2 subunit 2-like protein
  296. Eukaryotic translation initiation factor 2 subunit 3
  297. Eukaryotic translation initiation factor 2 subunit 3-like protein
  298. Translation initiation factor IF-2, mitochondrial
  299. Eukaryotic translation initiation factor 5
  300. Interferon-inducible GTPase 5
  301. Importin subunit alpha-1
  302. Importin subunit alpha-2
  303. Importin subunit alpha-3
  304. Importin subunit alpha-4
  305. Importin subunit alpha-6
  306. Importin subunit alpha-7
  307. Importin subunit beta-1
  308. Importin-11
  309. Importin-13
  310. Importin-4
  311. Importin-5
  312. Importin-7
  313. Importin-8
  314. Importin-9
  315. IQ motif and SEC7 domain-containing protein 1
  316. Ras GTPase-activating-like protein IQGAP1
  317. Kalirin
  318. NF-kappa-B inhibitor-interacting Ras-like protein 1
  319. NF-kappa-B inhibitor-interacting Ras-like protein 2
  320. Kinesin-like protein KIF20A
  321. Leucine-rich repeat serine/threonine-protein kinase 1
  322. Large subunit GTPase 1 homolog
  323. MAP kinase-activating death domain protein
  324. Guanine nucleotide exchange factor DBS
  325. Melanophilin
  326. Mitofusin-1
  327. Mitofusin-2
  328. Ran guanine nucleotide release factor
  329. Molybdenum cofactor biosynthesis protein 1
  330. Serine/threonine-protein kinase MRCK alpha
  331. Serine/threonine-protein kinase MRCK beta
  332. Serine/threonine-protein kinase MRCK gamma
  333. Mitochondrial GTPase 1
  334. Rab effector MyRIP
  335. Nucleolar GTP-binding protein 1
  336. Nucleolar GTP-binding protein 2
  337. Nucleolar protein 8
  338. NTF2-related export protein 1
  339. 2'-5'-oligoadenylate synthase 3
  340. Obg-like ATPase 1
  341. Oligophrenin-1
  342. Phosphatidylinositol 4-kinase type 2-beta
  343. Polyadenylate-binding protein 2
  344. Serine/threonine-protein kinase PAK 1
  345. Partitioning defective 6 homolog alpha
  346. Partitioning defective 6 homolog beta
  347. Partitioning defective 6 homolog gamma
  348. Partitioning defective 3 homolog
  349. Phosducin-like protein
  350. PRKCA-binding protein
  351. Plexin-B1
  352. DENN domain-containing protein 5A
  353. Ras-related protein Rab-15
  354. Ras-related protein Rab-1B
  355. Ras-related protein Rab-5A
  356. Ras-related protein Rab-5B
  357. Rab GTPase-binding effector protein 1
  358. Rab GTPase-binding effector protein 2
  359. Rab9 effector protein with kelch motifs
  360. Rab5 GDP/GTP exchange factor
  361. Ras-related C3 botulinum toxin substrate 3
  362. Ras-interacting protein 1
  363. Ran-binding protein 3
  364. Ran-binding protein 9
  365. Ran-specific GTPase-activating protein
  366. Ras-related protein Rap-2b
  367. GTPase ERas
  368. Ras and EF-hand domain-containing protein
  369. Ras association domain-containing protein 2
  370. Ras association domain-containing protein 4
  371. GTPase KRas
  372. GTPase NRas
  373. Rab3 GTPase-activating protein catalytic subunit
  374. ELKS/Rab6-interacting/CAST family member 1
  375. Rab3 GTPase-activating protein non-catalytic subunit
  376. RNA-binding protein 4
  377. Rabenosyn-5
  378. Ran-binding protein 17
  379. E3 SUMO-protein ligase RanBP2
  380. Regulator of chromosome condensation
  381. GTPase RhebL1
  382. GTP-binding protein REM 2
  383. Rab15 effector protein
  384. Ras-related and estrogen-regulated growth inhibitor
  385. Ras-related and estrogen-regulated growth inhibitor-like protein
  386. Rab11 family-interacting protein 2
  387. Rab11 family-interacting protein 4
  388. Rab11 family-interacting protein 5
  389. Ral guanine nucleotide dissociation stimulator-like 2
  390. Ral guanine nucleotide dissociation stimulator-like 3
  391. RANBP2-like and GRIP domain-containing protein 8
  392. Ras-specific guanine nucleotide-releasing factor 1
  393. GTP-binding protein Rheb
  394. GTP-binding protein Rhes
  395. Rho GTPase-activating protein 21
  396. Rho-related GTP-binding protein RhoD
  397. Rho-related GTP-binding protein RhoF
  398. Rho-related GTP-binding protein RhoJ
  399. Rhophilin-1
  400. Synembryn-A
  401. Regulating synaptic membrane exocytosis protein 2
  402. Ras and Rab interactor 1
  403. Ras and Rab interactor 2
  404. Ras and Rab interactor 3
  405. GTP-binding protein Rit1
  406. GTP-binding protein Rit2
  407. Rho-related GTP-binding protein RhoE
  408. Phosphorylated adapter RNA export protein
  409. Rap guanine nucleotide exchange factor 5
  410. Rab effector Noc2
  411. Ras-related GTP-binding protein A
  412. Ras-related GTP-binding protein B
  413. Ras-related GTP-binding protein C
  414. Ras-related GTP-binding protein D
  415. Ras-related protein R-Ras2
  416. Rhotekin
  417. RUN and FYVE domain-containing protein 1
  418. RUN domain-containing protein 3A
  419. GTP-binding protein SAR1a
  420. Ribosome maturation protein SBDS
  421. Protein transport protein Sec16A
  422. Sterol regulatory element-binding protein cleavage-activating protein
  423. Septin-10
  424. Uncharacterized protein ENSP00000381893
  425. SH3 domain-containing guanine exchange factor
  426. Putative E3 ubiquitin-protein ligase SH3RF1
  427. Son of sevenless homolog 1
  428. Son of sevenless homolog 2
  429. Sperm-associated antigen 1
  430. Protein sprouty homolog 4
  431. Secretion-regulating guanine nucleotide exchange factor
  432. Signal recognition particle 54 kDa protein
  433. Signal recognition particle receptor subunit alpha
  434. Sex-determining region Y protein
  435. Double-stranded RNA-binding protein Staufen homolog 2
  436. Syntaxin-binding protein 1
  437. Synaptotagmin-like protein 1
  438. Synaptotagmin-like protein 2
  439. Synaptotagmin-like protein 5
  440. Tubulin alpha-1A chain
  441. Tubulin alpha-1B chain
  442. Tubulin alpha-1C chain
  443. Tubulin alpha-3C/D chain
  444. Tubulin alpha-3E chain
  445. Tubulin alpha-4A chain
  446. Tubulin alpha-8 chain
  447. Tubulin alpha chain-like 3
  448. Tubulin beta-1 chain
  449. Tubulin beta-2A chain
  450. Tubulin beta-2B chain
  451. Putative tubulin beta-4q chain
  452. Tubulin beta-8 chain
  453. Tubulin beta-8 chain B
  454. Tubulin-specific chaperone D
  455. T-lymphoma invasion and metastasis-inducing protein 1
  456. T-lymphoma invasion and metastasis-inducing protein 2
  457. Transportin-1
  458. Transportin-2
  459. Tubulin polymerization-promoting protein
  460. Triple functional domain protein
  461. 116 kDa U5 small nuclear ribonucleoprotein component
  462. Guanine nucleotide exchange factor VAV3
  463. WD repeat-containing protein 44
  464. Exportin-1
  465. Exportin-2
  466. Exportin-4
  467. Exportin-5
  468. Exportin-7
  469. Exportin-T
  470. Protein XRP2
  471. Putative GTP-binding protein FLJ12595
  472. Putative tubulin beta chain-like protein ENSP00000290377
  473. Putative nucleoside diphosphate kinase
  474. Rho-related GTP-binding protein RhoU
  475. Adenylate cyclase 9 (Adenylate cyclase 9, isoform CRA_a)
  476. 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)
  477. DNA-directed RNA polymerase III subunit RPC1
  478. DNA-directed RNA polymerase I subunit RPA1
  479. Zinc ribbon domain containing 1
  480. DNA-directed RNA polymerases I and III subunit RPAC2
  481. cDNA FLJ75210, highly similar to H.sapiens RNA polymerase II 140 kDa subunit (Polymerase (RNA) II (DNA directed) polypeptide B, 140kDa)
  482. DNA-directed RNA polymerase
  483. DNA-directed RNA polymerase III subunit RPC7-like
  484. POLR1C protein
  485. Uridine kinase
  486. Leucine-rich repeat serine/threonine-protein kinase 2
  487. cDNA FLJ76814, highly similar to Homo sapiens dynamin 1-like (DNM1L), transcript variant 3, mRNA
  488. cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
  489. cDNA FLJ16206 fis, clone CTONG2019590, highly similar to Adenylate cyclase type 4 (EC 4.6.1.1)
  490. cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
  491. Adenylosuccinate synthetase
  492. Guanylate cyclase 2C (Heat stable enterotoxin receptor)
  493. Guanylate cyclase
  494. Guanylate cyclase
  495. Eukaryotic translation elongation factor 1 alpha 2
  496. EEF2 protein (Eukaryotic translation elongation factor 2, isoform CRA_a)
  497. Mitochondrial Rho GTPase 1
  498. Ninein
  499. Nucleolar and coiled-body phosphoprotein 1
  500. Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1
  501. Guanine nucleotide-binding protein G(i) subunit alpha-1
  502. Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas
  503. Eukaryotic translation initiation factor 5B
  504. Guanine nucleotide exchange factor VAV2
  505. Rho-guanine nucleotide exchange factor
  506. Ras guanyl-releasing protein 3
  507. Protein RCC2
  508. Protein very KIND
  509. RNA-directed RNA polymerase catalytic subunit
  510. Genome polyprotein
  511. DNA-directed RNA polymerase 132 kDa polypeptide
  512. Non-structural polyprotein pORF1
  513. Genome polyprotein
  514. RNA-directed RNA polymerase
  515. RNA-directed RNA polymerase L
  516. RNA-directed RNA polymerase catalytic subunit
  517. Genome polyprotein
  518. DNA-directed RNA polymerase 30 kDa polypeptide
  519. RNA-directed RNA polymerase catalytic subunit
  520. RNA-directed RNA polymerase catalytic subunit
  521. Genome polyprotein
  522. Genome polyprotein
  523. RNA-directed RNA polymerase L
  524. RNA-directed RNA polymerase
  525. Non-structural polyprotein p200
  526. Genome polyprotein
  527. Genome polyprotein
  528. RNA-directed RNA polymerase
  529. Genome polyprotein
  530. DNA-directed RNA polymerase 35 kDa subunit
  531. RNA-directed RNA polymerase
  532. RNA-directed RNA polymerase L
  533. Genome polyprotein
  534. RNA-directed RNA polymerase L
  535. Genome polyprotein
  536. RNA-directed RNA polymerase
  537. RNA-directed RNA polymerase catalytic subunit
  538. Genome polyprotein
  539. DNA-directed RNA polymerase 7 kDa subunit
  540. Genome polyprotein
  541. Large structural protein
  542. DNA-directed RNA polymerase 147 kDa polypeptide
  543. Genome polyprotein
  544. RNA-directed RNA polymerase L
  545. Non-structural polyprotein p200
  546. Genome polyprotein
  547. RNA-directed RNA polymerase catalytic subunit
  548. Non-structural polyprotein pORF1
  549. RNA-directed RNA polymerase L
  550. Non-structural polyprotein
  551. Genome polyprotein
  552. RNA-directed RNA polymerase catalytic subunit
  553. Genome polyprotein
  554. Genome polyprotein
  555. Genome polyprotein
  556. RNA-directed RNA polymerase L
  557. Genome polyprotein
  558. Genome polyprotein
  559. Genome polyprotein
  560. Genome polyprotein
  561. DNA-directed RNA polymerase 132 kDa polypeptide
  562. RNA-directed RNA polymerase catalytic subunit
  563. RNA-directed RNA polymerase L
  564. RNA-directed RNA polymerase catalytic subunit
  565. Genome polyprotein
  566. DNA-directed RNA polymerase 35 kDa subunit
  567. RNA-directed RNA polymerase catalytic subunit
  568. Genome polyprotein
  569. Non-structural polyprotein pORF1
  570. RNA-directed RNA polymerase L
  571. RNA-directed RNA polymerase
  572. RNA-directed RNA polymerase L
  573. RNA-directed RNA polymerase catalytic subunit
  574. RNA-directed RNA polymerase L
  575. DNA-directed RNA polymerase 132 kDa polypeptide
  576. RNA-directed RNA polymerase catalytic subunit
  577. RNA-directed RNA polymerase catalytic subunit
  578. RNA-directed RNA polymerase
  579. RNA-directed RNA polymerase L
  580. Non-structural polyprotein 1A
  581. RNA-directed RNA polymerase L
  582. Replicase polyprotein 1ab
  583. Genome polyprotein
  584. Non-structural polyprotein pORF1
  585. RNA-directed RNA polymerase catalytic subunit
  586. Non-structural polyprotein
  587. RNA-directed RNA polymerase
  588. RNA-directed RNA polymerase catalytic subunit
  589. Non-structural polyprotein 1A
  590. Genome polyprotein
  591. RNA-directed RNA polymerase catalytic subunit
  592. RNA-directed RNA polymerase catalytic subunit
  593. Genome polyprotein
  594. Genome polyprotein
  595. RNA-directed RNA polymerase catalytic subunit
  596. Non-structural polyprotein
  597. RNA-directed RNA polymerase catalytic subunit
  598. Genome polyprotein
  599. Genome polyprotein
  600. RNA-directed RNA polymerase catalytic subunit
  601. RNA-directed RNA polymerase catalytic subunit
  602. RNA-directed RNA polymerase L
  603. Genome polyprotein
  604. Genome polyprotein
  605. RNA-directed RNA polymerase catalytic subunit
  606. RNA-directed RNA polymerase catalytic subunit
  607. Non-structural polyprotein
  608. Genome polyprotein
  609. Genome polyprotein
  610. RNA-directed RNA polymerase catalytic subunit
  611. Genome polyprotein
  612. RNA-directed RNA polymerase L
  613. RNA-directed RNA polymerase catalytic subunit
  614. RNA-directed RNA polymerase catalytic subunit
  615. Genome polyprotein
  616. Genome polyprotein
  617. RNA-directed RNA polymerase L
  618. RNA-directed RNA polymerase catalytic subunit
  619. Genome polyprotein
  620. Non-structural polyprotein
  621. Replicase polyprotein 1ab
  622. Non-structural polyprotein p200
  623. Genome polyprotein
  624. DNA-directed RNA polymerase 18 kDa subunit
  625. Genome polyprotein
  626. DNA-directed RNA polymerase 19 kDa subunit
  627. RNA-directed RNA polymerase catalytic subunit
  628. Non-structural polyprotein
  629. Non-structural polyprotein
  630. Non-structural polyprotein p200
  631. RNA-directed RNA polymerase L
  632. Genome polyprotein
  633. RNA-directed RNA polymerase L
  634. RNA-directed RNA polymerase catalytic subunit
  635. DNA-directed RNA polymerase 19 kDa subunit
  636. RNA-directed RNA polymerase
  637. RNA-directed RNA polymerase
  638. RNA-directed RNA polymerase L
  639. RNA-directed RNA polymerase L
  640. Genome polyprotein
  641. DNA-directed RNA polymerase 132 kDa polypeptide
  642. Genome polyprotein
  643. Genome polyprotein
  644. Non-structural polyprotein
  645. RNA-directed RNA polymerase L
  646. Non-structural polyprotein
  647. Genome polyprotein
  648. Large structural protein
  649. DNA-directed RNA polymerase 22 kDa subunit
  650. Replicase polyprotein 1ab
  651. Non-structural polyprotein p200
  652. RNA-directed RNA polymerase catalytic subunit
  653. Genome polyprotein
  654. Genome polyprotein
  655. Genome polyprotein
  656. RNA-directed RNA polymerase catalytic subunit
  657. Replicase polyprotein 1ab
  658. RNA-directed RNA polymerase L
  659. Genome polyprotein
  660. RNA-directed RNA polymerase L
  661. DNA-directed RNA polymerase 35 kDa subunit
  662. Genome polyprotein
  663. Genome polyprotein
  664. RNA-directed RNA polymerase
  665. RNA-directed RNA polymerase catalytic subunit
  666. RNA-directed RNA polymerase L
  667. Non-structural polyprotein p200
  668. RNA-directed RNA polymerase catalytic subunit
  669. Genome polyprotein
  670. RNA-directed RNA polymerase L
  671. RNA-directed RNA polymerase catalytic subunit
  672. Genome polyprotein
  673. RNA-directed RNA polymerase L
  674. RNA-directed RNA polymerase
  675. Non-structural polyprotein 1AB
  676. RNA-directed RNA polymerase
  677. RNA-directed RNA polymerase catalytic subunit
  678. Non-structural polyprotein
  679. Genome polyprotein
  680. Non-structural polyprotein 1AB
  681. RNA-directed RNA polymerase catalytic subunit
  682. Non-structural polyprotein
  683. Genome polyprotein
  684. RNA-directed RNA polymerase catalytic subunit
  685. Genome polyprotein
  686. Genome polyprotein
  687. Genome polyprotein
  688. Genome polyprotein
  689. RNA-directed RNA polymerase catalytic subunit
  690. RNA-directed RNA polymerase L
  691. Genome polyprotein
  692. Replicase polyprotein 1ab
  693. Genome polyprotein
  694. RNA-directed RNA polymerase catalytic subunit
  695. Non-structural polyprotein
  696. DNA-directed RNA polymerase 18 kDa subunit
  697. Genome polyprotein
  698. RNA-directed RNA polymerase catalytic subunit
  699. Genome polyprotein
  700. RNA-directed RNA polymerase catalytic subunit
  701. RNA-directed RNA polymerase L
  702. Genome polyprotein
  703. RNA-directed RNA polymerase catalytic subunit
  704. RNA-directed RNA polymerase catalytic subunit
  705. DNA-directed RNA polymerase 7 kDa subunit
  706. Genome polyprotein
  707. Genome polyprotein
  708. RNA-directed RNA polymerase L
  709. Genome polyprotein
  710. Non-structural polyprotein 1AB
  711. Genome polyprotein
  712. RNA-directed RNA polymerase catalytic subunit
  713. Genome polyprotein
  714. Non-structural polyprotein pORF1
  715. RNA-directed RNA polymerase L
  716. Genome polyprotein
  717. DNA-directed RNA polymerase 22 kDa subunit
  718. Genome polyprotein
  719. RNA-directed RNA polymerase catalytic subunit
  720. Genome polyprotein
  721. Non-structural polyprotein
  722. Non-structural polyprotein
  723. Genome polyprotein
  724. Genome polyprotein
  725. DNA-directed RNA polymerase 35 kDa subunit
  726. Genome polyprotein
  727. RNA-directed RNA polymerase catalytic subunit
  728. DNA-directed RNA polymerase 7 kDa subunit
  729. RNA-directed RNA polymerase catalytic subunit
  730. RNA-directed RNA polymerase catalytic subunit
  731. RNA-directed RNA polymerase catalytic subunit
  732. Non-structural polyprotein pORF1
  733. Genome polyprotein
  734. RNA-directed RNA polymerase catalytic subunit
  735. Non-structural polyprotein
  736. RNA-directed RNA polymerase catalytic subunit
  737. Genome polyprotein
  738. DNA-directed RNA polymerase 7 kDa subunit
  739. Genome polyprotein
  740. Genome polyprotein
  741. Genome polyprotein
  742. Non-structural polyprotein
  743. Genome polyprotein
  744. Genome polyprotein
  745. RNA-directed RNA polymerase L
  746. DNA-directed RNA polymerase 147 kDa polypeptide
  747. Genome polyprotein
  748. Genome polyprotein
  749. RNA-directed RNA polymerase catalytic subunit
  750. Non-structural polyprotein p200
  751. RNA-directed RNA polymerase L
  752. DNA-directed RNA polymerase 132 kDa polypeptide
  753. Genome polyprotein
  754. RNA-directed RNA polymerase L
  755. RNA-directed RNA polymerase
  756. RNA-directed RNA polymerase
  757. Genome polyprotein
  758. Non-structural polyprotein
  759. Genome polyprotein
  760. RNA-directed RNA polymerase catalytic subunit
  761. Genome polyprotein
  762. RNA-directed RNA polymerase catalytic subunit
  763. Genome polyprotein
  764. Non-structural polyprotein 1A
  765. RNA-directed RNA polymerase catalytic subunit
  766. Genome polyprotein
  767. RNA-directed RNA polymerase catalytic subunit
  768. RNA-directed RNA polymerase catalytic subunit
  769. Genome polyprotein
  770. RNA-directed RNA polymerase catalytic subunit
  771. RNA-directed RNA polymerase L
  772. Genome polyprotein
  773. RNA-directed RNA polymerase catalytic subunit
  774. RNA-directed RNA polymerase catalytic subunit
  775. RNA-directed RNA polymerase L
  776. DNA-directed RNA polymerase 18 kDa subunit
  777. Non-structural polyprotein pORF1
  778. Genome polyprotein
  779. DNA-directed RNA polymerase 7 kDa subunit
  780. Genome polyprotein
  781. Non-structural polyprotein
  782. RNA-directed RNA polymerase catalytic subunit
  783. RNA-directed RNA polymerase catalytic subunit
  784. Genome polyprotein
  785. DNA-directed RNA polymerase 132 kDa polypeptide
  786. RNA-directed RNA polymerase catalytic subunit
  787. RNA-directed RNA polymerase L
  788. Non-structural polyprotein p200
  789. Genome polyprotein
  790. Genome polyprotein
  791. RNA-directed RNA polymerase L
  792. RNA-directed RNA polymerase L
  793. Genome polyprotein
  794. Genome polyprotein
  795. Non-structural polyprotein
  796. Genome polyprotein
  797. Non-structural polyprotein pORF1
  798. Genome polyprotein
  799. Genome polyprotein
  800. RNA-directed RNA polymerase L
  801. Genome polyprotein
  802. RNA-directed RNA polymerase catalytic subunit
  803. Genome polyprotein
  804. Genome polyprotein
  805. DNA-directed RNA polymerase 7 kDa subunit
  806. Genome polyprotein
  807. DNA-directed RNA polymerase 147 kDa polypeptide
  808. RNA-directed RNA polymerase catalytic subunit
  809. RNA-directed RNA polymerase L
  810. RNA-directed RNA polymerase catalytic subunit
  811. RNA-directed RNA polymerase L
  812. RNA-directed RNA polymerase L
  813. Genome polyprotein
  814. Non-structural polyprotein
  815. DNA-directed RNA polymerase 30 kDa polypeptide
  816. Genome polyprotein
  817. RNA-directed RNA polymerase catalytic subunit
  818. RNA-directed RNA polymerase
  819. Genome polyprotein
  820. DNA-directed RNA polymerase 30 kDa polypeptide
  821. Genome polyprotein
  822. Genome polyprotein
  823. Genome polyprotein
  824. Genome polyprotein
  825. Genome polyprotein
  826. Genome polyprotein
  827. Genome polyprotein
  828. RNA-directed RNA polymerase catalytic subunit
  829. Genome polyprotein
  830. RNA-directed RNA polymerase L
  831. Genome polyprotein
  832. DNA-directed RNA polymerase 132 kDa polypeptide
  833. Replicase polyprotein 1ab
  834. RNA-directed RNA polymerase catalytic subunit
  835. RNA-directed RNA polymerase L
  836. Genome polyprotein
  837. Genome polyprotein
  838. Genome polyprotein
  839. Genome polyprotein
  840. RNA-directed RNA polymerase catalytic subunit
  841. RNA-directed RNA polymerase L
  842. Genome polyprotein
  843. RNA-directed RNA polymerase catalytic subunit
  844. RNA-directed RNA polymerase catalytic subunit
  845. Genome polyprotein
  846. Genome polyprotein
  847. RNA-directed RNA polymerase
  848. Non-structural polyprotein 1AB
  849. Replicase polyprotein 1ab
  850. Non-structural polyprotein p200
  851. RNA-directed RNA polymerase catalytic subunit
  852. RNA-directed RNA polymerase catalytic subunit
  853. Non-structural polyprotein
  854. Non-structural polyprotein
  855. RNA-directed RNA polymerase
  856. RNA-directed RNA polymerase catalytic subunit
  857. RNA-directed RNA polymerase catalytic subunit
  858. RNA-directed RNA polymerase catalytic subunit
  859. Non-structural polyprotein 1A
  860. Genome polyprotein
  861. DNA-directed RNA polymerase 19 kDa subunit
  862. Genome polyprotein
  863. RNA-directed RNA polymerase L
  864. Genome polyprotein
  865. Guanine nucleotide binding protein (G protein), gamma transducing activity polypeptide 1
  866. Abl interactor 1
  867. GTP-binding protein SAR1b
  868. Ras-GEF domain-containing family member 1A
  869. G-protein-signaling modulator 1
  870. GTP-binding protein GEM
  871. Rap guanine nucleotide exchange factor-like 1
  872. Guanine nucleotide binding protein-like 1
  873. Rho guanine nucleotide exchange factor 6
  874. Guanine nucleotide binding protein (G protein), alpha 13, isoform CRA_a
  875. cDNA, FLJ92996, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta polypeptide 1 (GNB1), mRNA
  876. Guanine nucleotide-binding protein subunit alpha-14
  877. PH and SEC7 domain-containing protein 4
  878. Rho guanine nucleotide exchange factor 9
  879. Guanine nucleotide-binding protein G(k) subunit alpha
  880. Epithelial cell-transforming sequence 2 oncogene-like
  881. cDNA, FLJ95645, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta 5(GNB5), transcript variant 1, mRNA
  882. Pleckstrin homology domain-containing family G member 6
  883. Guanine nucleotide-binding protein G(i) subunit alpha-2
  884. cDNA FLJ78228, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta 5(GNB5), transcript variant 1, mRNA
  885. Guanine nucleotide binding protein (G protein), beta polypeptide 1
  886. Guanine nucleotide-binding protein G(t) subunit alpha-2
  887. Rho guanine nucleotide exchange factor 37
  888. PH and SEC7 domain-containing protein 3
  889. PH and SEC7 domain-containing protein 1
  890. Guanine nucleotide-binding protein G(o) subunit alpha
  891. Ras-GEF domain-containing family member 1B
  892. Rho guanine nucleotide exchange factor 18
  893. ALS2 C-terminal-like protein
  894. Switch-associated protein 70
  895. Ras-specific guanine nucleotide-releasing factor RalGPS2
  896. FERM, RhoGEF and pleckstrin domain-containing protein 2
  897. Ral guanine nucleotide dissociation stimulator-like 1
  898. Guanine nucleotide-binding protein subunit alpha-13
  899. Vav-like protein C9orf100
  900. Probable guanine nucleotide exchange factor MCF2L2
  901. Rho guanine nucleotide exchange factor 7
  902. Guanine nucleotide binding protein (G protein), alpha 14
  903. Guanine nucleotide binding protein-like 1
  904. Guanine nucleotide binding protein (G protein), alpha activating activity polypeptide, olfactory type, isoform CRA_b
  905. Guanine nucleotide-binding protein subunit alpha-12
  906. Ras-specific guanine nucleotide-releasing factor RalGPS1
  907. Rho guanine nucleotide exchange factor 11
  908. cDNA FLJ76843, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), alpha 15 (Gq class) (GNA15), mRNA
  909. Growth factor receptor-bound protein 2
  910. Guanine nucleotide binding protein (G protein), beta polypeptide 1
  911. Rho guanine nucleotide exchange factor 10-like protein
  912. Guanine nucleotide binding protein (G protein), q polypeptide
  913. Protein SOLO
  914. Prolactin regulatory element-binding protein
  915. Rho guanine nucleotide exchange factor 4
  916. Not Available
  917. Guanine nucleotide exchange factor for Rab-3A
  918. cDNA FLJ77654, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta polypeptide 4 (GNB4), mRNA
  919. Guanine nucleotide binding protein-like 1
  920. Engulfment and cell motility protein 1
  921. GRB2-related adapter protein
  922. Guanine nucleotide-binding protein G(z) subunit alpha
  923. Engulfment and cell motility protein 3
  924. Guanine nucleotide exchange factor GEFT
  925. Differentially expressed in FDCP 6 homolog
  926. Alpha-catulin
  927. Guanine nucleotide binding protein (G protein), beta polypeptide 1
  928. IQ motif and SEC7 domain-containing protein 3
  929. Engulfment and cell motility protein 2
  930. Rho guanine nucleotide exchange factor 17
  931. Ras-GEF domain-containing family member 1C
  932. Rho guanine nucleotide exchange factor 12
  933. Ephexin-1
  934. Guanine nucleotide binding protein-like 1
  935. Guanine nucleotide-binding protein G(olf) subunit alpha
  936. Guanine nucleotide-binding protein subunit alpha-15
  937. Rho guanine nucleotide exchange factor 3
Enzyme 1 [top]
Enzyme 1 ID 5311
Enzyme 1 Name Phospholipase D1
Enzyme 1 Synonyms
  1. PLD 1
  2. hPLD1
  3. Choline phosphatase 1
  4. Phosphatidylcholine-hydrolyzing phospholipase D1
Enzyme 1 Gene Name PLD1
Enzyme 1 Protein Sequence >Phospholipase D1
MSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEGEEVDYDVSPSDPKIQEVYIPFSA
IYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRVPSINLYTIELTHGEFKWQVKRKF
KHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEPREMPSLPRSSENMIREEQFLGRR
KQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDLGPKGIEGMIMKRSGGHRIPGLNC
CGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFKIKVGKKETETKYGIRID
NLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKDHRFGSYAAIQENALAKWYVNAKG
YFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFIMLY
KEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSTVYLWAHHEKLVIIDQSVAFVGGI
DLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAMESMESLRLKDKNEPVQNLPIQKS
IDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSISSIDSTSSYFNHYRSHHNLIHGL
KPHFKLFHPSSESEQGLTRPHADTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQL
DKPFADFIDRYSTPRMPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLL
PKSQTTAHELRYQVPGSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIE
NQFFISCADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQ
AIMHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLL
IADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCF
RVVLGYLDDPSEDIQDPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFI
NKPVLAKEDPIRAEEELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT
Enzyme 1 Number of Residues 1074
Enzyme 1 Molecular Weight 124183.1
Enzyme 1 Theoretical pI 9.07
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • lipid binding
  • phosphoinositide binding
  • phospholipid binding
  • protein binding
Process
  • cell communication
  • cellular process
  • metabolic process
Component
Enzyme 1 General Function Involved in protein binding
Enzyme 1 Specific Function Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic
Enzyme 1 Pathways
Enzyme 1 Reactions
  • a phosphatidylcholine + H2O = choline + a phosphatidate [RN:R01310]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID Q13393 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PLD1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >3225 bp
ATGTCACTGAAAAACGAGCCACGGGTAAATACCTCTGCACTGCAGAAAATTGCTGCTGAC
ATGAGTAATATCATAGAAAATCTGGACACGCGGGAACTCCACTTTGAGGGAGAGGAGGTA
GACTACGACGTGTCTCCCAGCGATCCCAAGATACAAGAAGTGTATATCCCTTTCTCTGCT
ATTTATAACACTCAAGGATTTAAGGAGCCTAATATACAGACGTATCTCTCCGGCTGTCCA
ATAAAAGCACAAGTTCTGGAAGTGGAACGCTTCACATCTACAACAAGGGTACCAAGTATT
AATCTTTACACTATTGAATTAACACATGGGGAATTTAAATGGCAAGTTAAGAGGAAATTC
AAGCATTTTCAAGAATTTCACAGAGAGCTGCTCAAGTACAAAGCCTTTATCCGCATCCCC
ATTCCCACTAGAAGACACACGTTTAGGAGGCAAAACGTCAGAGAGGAGCCTCGAGAGATG
CCCAGTTTGCCCCGTTCATCTGAAAACATGATAAGAGAAGAACAATTCCTTGGTAGAAGA
AAACAACTGGAAGATTACTTGACAAAGATACTAAAAATGCCCATGTATAGAAACTATCAT
GCCACAACAGAGTTTCTTGATATAAGCCAGCTGTCTTTCATCCATGATTTGGGACCAAAG
GGCATAGAAGGTATGATAATGAAAAGATCTGGAGGACACAGAATACCAGGCTTGAATTGC
TGTGGTCAGGGAAGAGCCTGCTACAGATGGTCAAAAAGATGGTTAATAGTGAAAGATTCC
TTTTTATTGTATATGAAACCAGACAGCGGTGCCATTGCCTTCGTCCTGCTGGTAGACAAA
GAATTCAAAATTAAGGTGGGGAAGAAGGAGACAGAAACGAAATATGGAATCCGAATTGAT
AATCTTTCAAGGACACTTATTTTAAAATGCAACAGCTATAGACATGCTCGGTGGTGGGGA
GGGGCTATAGAAGAATTCATCCAGAAACATGGCACCAACTTTCTCAAAGATCATCGATTT
GGGTCATATGCTGCTATCCAAGAGAATGCTTTAGCTAAATGGTATGTTAATGCCAAAGGA
TATTTTGAAGATGTGGCAAATGCAATGGAAGAGGCAAATGAAGAGATTTTTATCACAGAC
TGGTGGCTGAGTCCAGAAATCTTCCTGAAACGCCCAGTGGTTGAGGGAAATCGTTGGAGG
TTGGACTGCATTCTTAAACGAAAAGCACAACAAGGAGTGAGGATCTTCATAATGCTCTAC
AAAGAGGTGGAACTCGCTCTTGGCATCAATAGTGAATACACCAAGAGGACTTTGATGCGT
CTACATCCCAACATAAAGGTGATGAGACACCCGGATCATGTGTCATCCACCGTCTATTTG
TGGGCTCACCATGAGAAGCTTGTCATCATTGACCAATCGGTGGCCTTTGTGGGAGGGATT
GACCTGGCCTATGGAAGGTGGGACGACAATGAGCACAGACTCACAGACGTGGGCAGTGTG
AAGCGGGTCACTTCAGGACCGTCTCTGGGTTCCCTCCCACCTGCCGCAATGGAGTCTATG
GAATCCTTAAGACTCAAAGATAAAAATGAGCCTGTTCAAAACCTACCCATCCAGAAGAGT
ATTGATGATGTGGATTCAAAACTGAAAGGAATAGGAAAGCCAAGAAAGTTCTCCAAATTT
AGTCTCTACAAGCAGCTCCACAGGCACCACCTGCACGACGCAGATAGCATCAGCAGCATT
GACAGCACCTCCAGTTATTTTAATCACTATAGAAGTCATCACAATTTAATCCATGGTTTA
AAACCCCACTTCAAACTCTTTCACCCGTCCAGTGAGTCTGAGCAAGGACTCACTAGACCT
CATGCTGATACCGGGTCCATCCGTAGTTTACAGACAGGTGTGGGAGAGCTGCATGGGGAA
ACCAGATTCTGGCATGGAAAGGACTACTGCAATTTCGTCTTCAAAGACTGGGTTCAACTT
GATAAACCTTTTGCTGATTTCATTGACAGGTACTCCACGCCCCGGATGCCCTGGCATGAC
ATTGCCTCTGCAGTCCACGGGAAGGCGGCTCGTGATGTGGCACGTCACTTCATCCAGCGC
TGGAACTTCACAAAAATTATGAAATCAAAATATCGGTCCCTTTCTTATCCTTTTCTGCTT
CCAAAGTCTCAAACAACAGCCCATGAGTTGAGATATCAAGTGCCTGGGTCTGTCCATGCT
AACGTACAGTTGCTCCGCTCTGCTGCTGATTGGTCTGCTGGTATAAAGTACCATGAAGAG
TCCATCCACGCCGCTTACGTCCATGTGATAGAGAACAGCAGGCACTATATCTATATCGAA
AACCAGTTTTTCATAAGCTGTGCTGATGACAAAGTTGTGTTCAACAAGATAGGCGATGCC
ATTGCCCAGAGGATCCTGAAAGCTCACAGGGAAAACCAGAAATACCGGGTATATGTCGTG
ATACCACTTCTGCCAGGGTTCGAAGGAGACATTTCAACCGGCGGAGGAAATGCTCTACAG
GCAATCATGCACTTCAACTACAGAACCATGTGCAGAGGAGAAAATTCCATCCTTGGACAG
TTAAAAGCAGAGCTTGGTAATCAGTGGATAAATTACATATCATTCTGTGGTCTTAGAACA
CATGCAGAGCTCGAAGGAAACCTAGTAACTGAGCTTATCTATGTCCACAGCAAGTTGTTA
ATTGCTGATGATAACACTGTTATTATTGGCTCTGCCAACATAAATGACCGCAGCATGCTG
GGAAAGCGTGACAGTGAAATGGCTGTCATTGTGCAAGATACAGAGACTGTTCCTTCAGTA
ATGGATGGAAAAGAGTACCAAGCTGGCCGGTTTGCCCGAGGACTTCGGCTACAGTGCTTT
AGGGTTGTCCTTGGCTATCTTGATGACCCAAGTGAGGACATTCAGGATCCAGTGAGTGAC
AAATTCTTCAAGGAGGTGTGGGTTTCAACAGCAGCTCGAAATGCTACAATTTATGACAAG
GTTTTCCGGTGCCTTCCCAATGATGAAGTACACAATTTAATTCAGCTGAGAGACTTTATA
AACAAGCCCGTATTAGCTAAGGAAGATCCCATTCGAGCTGAGGAGGAACTGAAGAAGATC
CGTGGATTTTTGGTGCAATTCCCCTTTTATTTCTTGTCTGAAGAAAGCCTACTGCCTTCT
GTTGGGACCAAAGAGGCCATAGTGCCCATGGAGGTTTGGACTTAA
Enzyme 1 GenBank Gene ID U38545 Link Image
Enzyme 1 GeneCard ID PLD1 Link Image
Enzyme 1 GenAtlas ID PLD1 Link Image
Enzyme 1 HGNC ID HGNC:9067 Link Image
Enzyme 1 Chromosome Location 3
Enzyme 1 Locus 3q26
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Hammond SM, Altshuller YM, Sung TC, Rudge SA, Rose K, Engebrecht J, Morris AJ, Frohman MA: Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family. J Biol Chem. 1995 Dec 15;270(50):29640-3. [PubMed Link Image]
  2. Hammond SM, Jenco JM, Nakashima S, Cadwallader K, Gu Q, Cook S, Nozawa Y, Prestwich GD, Frohman MA, Morris AJ: Characterization of two alternately spliced forms of phospholipase D1. Activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding proteins and protein kinase C-alpha. J Biol Chem. 1997 Feb 7;272(6):3860-8. [PubMed Link Image]
  3. Steed PM, Clark KL, Boyar WC, Lasala DJ: Characterization of human PLD2 and the analysis of PLD isoform splice variants. FASEB J. 1998 Oct;12(13):1309-17. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Lopez I, Arnold RS, Lambeth JD: Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2. J Biol Chem. 1998 May 22;273(21):12846-52. [PubMed Link Image]
  6. Divecha N, Roefs M, Halstead JR, D'Andrea S, Fernandez-Borga M, Oomen L, Saqib KM, Wakelam MJ, D'Santos C: Interaction of the type Ialpha PIPkinase with phospholipase D: a role for the local generation of phosphatidylinositol 4, 5-bisphosphate in the regulation of PLD2 activity. EMBO J. 2000 Oct 16;19(20):5440-9. [PubMed Link Image]
  7. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5313
Enzyme 2 Name Ectonucleoside triphosphate diphosphohydrolase 1
Enzyme 2 Synonyms
  1. NTPDase 1
  2. Ecto-ATP diphosphohydrolase 1
  3. Ecto-ATPDase 1
  4. Ecto-ATPase 1
  5. Ecto-apyrase
  6. Lymphoid cell activation antigen
  7. CD39 antigen
Enzyme 2 Gene Name ENTPD1
Enzyme 2 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 1
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
Enzyme 2 Number of Residues 510
Enzyme 2 Molecular Weight 57964.1
Enzyme 2 Theoretical pI 6.29
Enzyme 2 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 2 General Function Involved in hydrolase activity
Enzyme 2 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 2 Pathways
Enzyme 2 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 17-37 479-499
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 45580700 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P49961 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ENTP1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID NM_001776.5 Link Image
Enzyme 2 GeneCard ID ENTPD1 Link Image
Enzyme 2 GenAtlas ID ENTPD1 Link Image
Enzyme 2 HGNC ID HGNC:3363 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 10q24
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Maliszewski CR, Delespesse GJ, Schoenborn MA, Armitage RJ, Fanslow WC, Nakajima T, Baker E, Sutherland GR, Poindexter K, Birks C, et al.: The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. J Immunol. 1994 Oct 15;153(8):3574-83. [PubMed Link Image]
  2. Robson SC, Kaczmarek E, Siegel JB, Candinas D, Koziak K, Millan M, Hancock WW, Bach FH: Loss of ATP diphosphohydrolase activity with endothelial cell activation. J Exp Med. 1997 Jan 6;185(1):153-63. [PubMed Link Image]
  3. Matsumoto M, Sakurai Y, Kokubo T, Yagi H, Makita K, Matsui T, Titani K, Fujimura Y, Narita N: The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II. FEBS Lett. 1999 Jun 25;453(3):335-40. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  6. Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O: Purification and properties of human placental ATP diphosphohydrolase. Eur J Biochem. 1995 Nov 15;234(1):66-74. [PubMed Link Image]
  7. Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y: Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. Int J Hematol. 1998 Oct;68(3):297-310. [PubMed Link Image]
  8. Kaczmarek E, Koziak K, Sevigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC: Identification and characterization of CD39/vascular ATP diphosphohydrolase. J Biol Chem. 1996 Dec 20;271(51):33116-22. [PubMed Link Image]
  9. Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed Link Image]
  10. Koziak K, Kaczmarek E, Kittel A, Sevigny J, Blusztajn JK, Schulte Am Esch J 2nd, Imai M, Guckelberger O, Goepfert C, Qawi I, Robson SC: Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae. J Biol Chem. 2000 Jan 21;275(3):2057-62. [PubMed Link Image]
  11. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed Link Image]
  12. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5314
Enzyme 3 Name Soluble calcium-activated nucleotidase 1
Enzyme 3 Synonyms
  1. SCAN-1
  2. Apyrase homolog
  3. Putative MAPK-activating protein PM09
  4. Putative NF-kappa-B-activating protein 107
Enzyme 3 Gene Name CANT1
Enzyme 3 Protein Sequence >Soluble calcium-activated nucleotidase 1
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
Enzyme 3 Number of Residues 401
Enzyme 3 Molecular Weight 44839.2
Enzyme 3 Theoretical pI 5.98
Enzyme 3 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • ion binding
  • metal ion binding
  • pyrophosphatase activity
Process
Component
Enzyme 3 General Function Involved in calcium ion binding
Enzyme 3 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 3 Pathways
Enzyme 3 Reactions
  • a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 45-62
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 229577440 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q8WVQ1 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name CANT1_HUMAN Link Image
Enzyme 3 PDB ID 1S1D Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1206 bp
ATGCCCGTGCAGCTGTCTGAGCACCCGGAATGGAATGAGTCTATGCACTCCCTCCGGATC
AGTGTGGGGGGCCTTCCTGTGCTGGCGTCCATGACCAAGGCCGCGGACCCCCGCTTCCGC
CCCCGCTGGAAGGTGATCCTGACGTTCTTTGTGGGTGCTGCCATCCTCTGGCTGCTCTGC
TCCCACCGCCCGGCCCCCGGCAGGCCCCCCACCCACAATGCACACAACTGGAGGCTCGGC
CAGGCGCCCGCCAACTGGTACAATGACACCTACCCCCTGTCTCCCCCACAAAGGACACCG
GCTGGGATTCGGTATCGAATCGCAGTTATCGCAGACCTGGACACAGAGTCAAGGGCCCAA
GAGGAAAACACCTGGTTCAGTTACCTGAAAAAGGGCTACCTGACCCTGTCAGACAGTGGG
GACAAGGTGGCCGTGGAATGGGACAAAGACCATGGGGTCCTGGAGTCCCACCTGGCGGAG
AAGGGGAGAGGCATGGAGCTATCCGACCTGATTGTTTTCAATGGGAAACTCTACTCCGTG
GATGACCGGACGGGGGTCGTCTACCAGATCGAAGGCAGCAAAGCCGTGCCCTGGGTGATT
CTGTCCGACGGCGACGGCACCGTGGAGAAAGGCTTCAAGGCCGAATGGCTGGCAGTGAAG
GACGAGCGTCTGTACGTGGGCGGCCTGGGCAAGGAGTGGACGACCACTACGGGTGATGTG
GTGAACGAGAACCCGGAGTGGGTGAAGGTGGTGGGCTACAAGGGCAGCGTGGACCACGAG
AACTGGGTGTCCAACTACAACGCCCTGCGGGCTGCTGCCGGCATCCAGCCGCCAGGCTAC
CTCATCCATGAGTCTGCCTGCTGGAGTGACACGCTGCAGCGCTGGTTCTTCCTGCCGCGC
CGCGCCAGCCAGGAGCGCTACAGCGAGAAGGACGACGAGCGCAAGGGCGCCAACCTGCTG
CTGAGCGCCTCCCCTGACTTCGGCGACATCGCTGTGAGCCACGTCGGGGCGGTGGTCCCC
ACTCACGGCTTCTCGTCCTTCAAGTTCATCCCCAACACCGACGACCAGATCATTGTGGCC
CTCAAATCCGAGGAGGACAGCGGCAGAGTCGCCTCCTACATCATGGCCTTCACGCTGGAC
GGGCGCTTCCTGTTGCCGGAGACCAAGATCGGAAGCGTGAAATACGAAGGCATCGAGTTC
ATTTAA
Enzyme 3 GenBank Gene ID NM_001159772.1 Link Image
Enzyme 3 GeneCard ID CANT1 Link Image
Enzyme 3 GenAtlas ID CANT1 Link Image
Enzyme 3 HGNC ID HGNC:19721 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 17q25.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Smith TM, Hicks-Berger CA, Kim S, Kirley TL: Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases. Arch Biochem Biophys. 2002 Oct 1;406(1):105-15. [PubMed Link Image]
  2. Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S: Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003 May 22;22(21):3307-18. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Failer BU, Braun N, Zimmermann H: Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J Biol Chem. 2002 Oct 4;277(40):36978-86. Epub 2002 Aug 6. [PubMed Link Image]
  6. Yang M, Kirley TL: Site-directed mutagenesis of human soluble calcium-activated nucleotidase 1 (hSCAN-1): identification of residues essential for enzyme activity and the Ca(2+)-induced conformational change. Biochemistry. 2004 Jul 20;43(28):9185-94. [PubMed Link Image]
  7. Dai J, Liu J, Deng Y, Smith TM, Lu M: Structure and protein design of a human platelet function inhibitor. Cell. 2004 Mar 5;116(5):649-59. [PubMed Link Image]
  8. Huber C, Oules B, Bertoli M, Chami M, Fradin M, Alanay Y, Al-Gazali LI, Ausems MG, Bitoun P, Cavalcanti DP, Krebs A, Le Merrer M, Mortier G, Shafeghati Y, Superti-Furga A, Robertson SP, Le Goff C, Muda AO, Paterlini-Brechot P, Munnich A, Cormier-Daire V: Identification of CANT1 mutations in Desbuquois dysplasia. Am J Hum Genet. 2009 Nov;85(5):706-10. Epub 2009 Oct 22. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5318
Enzyme 4 Name Ectonucleoside triphosphate diphosphohydrolase 3
Enzyme 4 Synonyms
  1. NTPDase 3
  2. CD39 antigen-like 3
  3. Ecto-ATP diphosphohydrolase 3
  4. Ecto-ATPDase 3
  5. Ecto-ATPase 3
  6. Ecto-apyrase 3
  7. HB6
Enzyme 4 Gene Name ENTPD3
Enzyme 4 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 3
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
Enzyme 4 Number of Residues 529
Enzyme 4 Molecular Weight 59104.8
Enzyme 4 Theoretical pI 6.40
Enzyme 4 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 4 General Function Involved in hydrolase activity
Enzyme 4 Specific Function Has a threefold preference for the hydrolysis of ATP over ADP
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 23-43 486-506
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 13817037 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O75355 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name ENTP3_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1590 bp
ATGTTCACTGTGCTGACCCGCCAACCATGTGAGCAAGCAGGCCTCAAGGCCCTCTACCGA
ACTCCAACCATCATTGCCTTGGTGGTCTTGCTTGTGAGTATTGTGGTACTTGTGAGTATC
ACTGTCATCCAGATCCACAAGCAAGAGGTCCTCCCTCCAGGACTGAAGTATGGTATTGTG
CTGGATGCCGGGTCTTCAAGAACCACAGTCTACGTGTATCAATGGCCAGCAGAAAAAGAG
AATAATACCGGAGTGGTCAGTCAAACCTTCAAATGTAGTGTGAAAGGCTCTGGAATCTCC
AGCTATGGAAATAACCCCCAAGATGTCCCCAGAGCCTTTGAGGAGTGTATGCAAAAAGTC
AAGGGGCAGGTTCCATCCCACCTCCACGGATCCACCCCCATTCACCTGGGAGCCACGGCT
GGGATGCGCTTGCTGAGGTTGCAAAATGAAACAGCAGCTAATGAAGTCCTTGAAAGCATC
CAAAGCTACTTCAAGTCCCAGCCCTTTGACTTTAGGGGTGCTCAAATCATTTCTGGGCAA
GAAGAAGGGGTATATGGATGGATTACAGCCAACTATTTAATGGGAAATTTCCTGGAGAAG
AACCTGTGGCACATGTGGGTGCACCCGCATGGAGTGGAAACCACGGGTGCCCTGGACTTA
GGTGGTGCCTCCACCCAAATATCCTTCGTGGCAGGAGAGAAGATGGATCTGAACACCAGC
GACATCATGCAGGTGTCCCTGTATGGCTACGTATACACGCTCTACACACACAGCTTCCAG
TGCTATGGCCGGAATGAGGCTGAGAAGAAGTTTCTGGCAATGCTCCTGCAGAATTCTCCT
ACCAAAAACCATCTCACCAATCCCTGTTACCCTCGGGATTATAGCATCAGCTTCACCATG
GGCCATGTATTTGATAGCCTGTGCACTGTGGACCAGAGGCCAGAAAGTTATAACCCCAAT
GATGTCATCACTTTTGAAGGAACTGGGGACCCATCTCTGTGTAAGGAGAAGGTGGCTTCC
ATATTTGACTTCAAAGCTTGCCATGATCAAGAAACCTGTTCTTTTGATGGGGTTTATCAG
CCAAAGATTAAAGGGCCATTTGTGGCTTTTGCAGGATTCTACTACACAGCCAGTGCTTTA
AATCTTTCAGGTAGCTTTTCCCTGGACACCTTCAACTCCAGCACCTGGAATTTCTGCTCA
CAGAATTGGAGTCAGCTCCCACTGCTGCTCCCCAAATTTGATGAGGTATATGCCCGCTCT
TACTGCTTCTCAGCCAACTACATCTACCACTTGTTTGTGAACGGTTACAAATTCACAGAG
GAGACTTGGCCCCAAATACACTTTGAAAAAGAAGTGGGGAATAGCAGCATAGCCTGGTCT
CTTGGCTACATGCTCAGCCTGACCAACCAGATCCCAGCTGAAAGCCCTCTGATCCGTCTG
CCCATAGAACCACCTGTCTTTGTGGGCACCCTCGCTTTCTTCACAGCGGCAGCCTTGCTG
TGTCTGGCATTTCTTGCATACCTGTGTTCAGCAACCAGAAGAAAGAGGCACTCCGAGCAT
GCCTTTGACCATGCAGTGGATTCTGACTGA
Enzyme 4 GenBank Gene ID AF034840 Link Image
Enzyme 4 GeneCard ID ENTPD3 Link Image
Enzyme 4 GenAtlas ID ENTPD3 Link Image
Enzyme 4 HGNC ID HGNC:3365 Link Image
Enzyme 4 Chromosome Location 3
Enzyme 4 Locus 3p21.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Chadwick BP, Frischauf AM: The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster. Genomics. 1998 Jun 15;50(3):357-67. [PubMed Link Image]
  2. Smith TM, Kirley TL: Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases1. Biochim Biophys Acta. 1998 Jul 28;1386(1):65-78. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Smith TM, Lewis Carl SA, Kirley TL: Mutagenesis of two conserved tryptophan residues of the E-type ATPases: inactivation and conversion of an ecto-apyrase to an ecto-NTPase. Biochemistry. 1999 May 4;38(18):5849-57. [PubMed Link Image]
  5. Yang F, Hicks-Berger CA, Smith TM, Kirley TL: Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: the importance of residues in the apyrase conserved regions. Biochemistry. 2001 Apr 3;40(13):3943-50. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5337
Enzyme 5 Name Uridine-cytidine kinase 1
Enzyme 5 Synonyms
  1. UCK 1
  2. Cytidine monophosphokinase 1
  3. Uridine monophosphokinase 1
Enzyme 5 Gene Name UCK1
Enzyme 5 Protein Sequence >Uridine-cytidine kinase 1
MASAGGEDCESPAPEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRKVV
ILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTH
SRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVRRGRDL
EQILTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNGDICKWHR
GGSNGRSYKRTFSEPGDHPGMLTSGKRSHLESSSRPH
Enzyme 5 Number of Residues 277
Enzyme 5 Molecular Weight 31434.5
Enzyme 5 Theoretical pI 7.33
Enzyme 5 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolic process
Component
Enzyme 5 General Function Involved in ATP binding
Enzyme 5 Specific Function Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and N(4)-anisoylcytidine
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + uridine = ADP + UMP [RN:R00964]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 13899253 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q9HA47 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name UCK1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >834 bp
ATGGCTTCGGCGGGAGGCGAAGACTGCGAGAGCCCCGCGCCGGAGGCCGACCGTCCGCAC
CAGCGGCCCTTCCTGATAGGGGTGAGCGGCGGCACTGCCAGCGGGAAGTCGACCGTGTGT
GAGAAGATCATGGAGTTGCTGGGACAGAACGAGGTGGAACAGCGGCAGCGGAAGGTGGTC
ATCCTGAGCCAGGACAGGTTCTACAAGGTCCTGACGGCAGAGCAGAAGGCCAAGGCCTTG
AAAGGACAGTACAATTTTGACCATCCAGATGCCTTTGATAATGATTTGATGCACAGGACT
CTGAAGAACATCGTGGAGGGCAAAACGGTGGAGGTGCCGACCTATGATTTTGTGACACAC
TCAAGGTTACCAGAGACCACGGTGGTCTACCCTGCGGACGTGGTTCTGTTTGAGGGCATC
TTGGTGTTCTACAGCCAGGAGATCCGGGACATGTTCCACCTGCGCCTCTTCGTGGACACC
GACTCCGACGTCAGGCTGTCTCGAAGAGTTCTCCGGGACGTGCGCCGAGGGAGGGACCTG
GAGCAGATTCTGACGCAGTACACCACCTTCGTGAAGCCGGCCTTCGAGGAGTTCTGCCTG
CCGACAAAGAAGTATGCCGATGTGATCATCCCGCGAGGAGTGGACAATATGGTTGCCATC
AACCTGATCGTGCAGCACATCCAGGACATTCTGAATGGTGACATCTGCAAATGGCACCGA
GGAGGGTCCAATGGGCGGAGCTACAAGCGGACCTTTTCTGAGCCAGGGGACCACCCTGGG
ATGCTGACCTCTGGCAAACGGTCACATTTGGAGTCCAGCAGCAGACCCCACTGA
Enzyme 5 GenBank Gene ID NM_031432.2 Link Image
Enzyme 5 GeneCard ID UCK1 Link Image
Enzyme 5 GenAtlas ID UCK1 Link Image
Enzyme 5 HGNC ID HGNC:14859 Link Image
Enzyme 5 Chromosome Location 9
Enzyme 5 Locus 9q34.13
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Van Rompay AR, Norda A, Linden K, Johansson M, Karlsson A: Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases. Mol Pharmacol. 2001 May;59(5):1181-6. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5338
Enzyme 6 Name Nucleoside diphosphate kinase, mitochondrial
Enzyme 6 Synonyms
  1. NDK
  2. NDP kinase, mitochondrial
  3. Nucleoside diphosphate kinase D
  4. NDPKD
  5. nm23-H4
Enzyme 6 Gene Name NME4
Enzyme 6 Protein Sequence >Nucleoside diphosphate kinase, mitochondrial
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
Enzyme 6 Number of Residues 187
Enzyme 6 Molecular Weight 20658.5
Enzyme 6 Theoretical pI 10.75
Enzyme 6 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 6 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 6 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP
Enzyme 6 Pathways
Enzyme 6 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 14336697 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID O00746 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name NDKM_HUMAN Link Image
Enzyme 6 PDB ID 1EHW Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >564 bp
ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCG
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
Enzyme 6 GenBank Gene ID AE006463 Link Image
Enzyme 6 GeneCard ID NME4 Link Image
Enzyme 6 GenAtlas ID NME4 Link Image
Enzyme 6 HGNC ID HGNC:7852 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 16p13.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Milon L, Rousseau-Merck MF, Munier A, Erent M, Lascu I, Capeau J, Lacombe ML: nm23-H4, a new member of the family of human nm23/nucleoside diphosphate kinase genes localised on chromosome 16p13. Hum Genet. 1997 Apr;99(4):550-7. [PubMed Link Image]
  2. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  3. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Milon L, Meyer P, Chiadmi M, Munier A, Johansson M, Karlsson A, Lascu I, Capeau J, Janin J, Lacombe ML: The human nm23-H4 gene product is a mitochondrial nucleoside diphosphate kinase. J Biol Chem. 2000 May 12;275(19):14264-72. [PubMed Link Image]
  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5341
Enzyme 7 Name Nucleoside diphosphate kinase A
Enzyme 7 Synonyms
  1. NDK A
  2. NDP kinase A
  3. Granzyme A-activated DNase
  4. GAAD
  5. Metastasis inhibition factor nm23
  6. Tumor metastatic process-associated protein
  7. nm23-H1
Enzyme 7 Gene Name NME1
Enzyme 7 Protein Sequence >Nucleoside diphosphate kinase A
MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
Enzyme 7 Number of Residues 152
Enzyme 7 Molecular Weight 17148.6
Enzyme 7 Theoretical pI 6.11
Enzyme 7 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 7 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 7 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein- coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination
Enzyme 7 Pathways
Enzyme 7 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 4557797 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P15531 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name NDKA_HUMAN Link Image
Enzyme 7 PDB ID 1JXV Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >459 bp
ATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAACCAGATGGGGTCCAGCGGGGTCTT
GTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGATTCCGCCTTGTTGGTCTGAAATTC
ATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTACGTTGACCTGAAGGACCGTCCATTC
TTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCGGTAGTTGCCATGGTCTGGGAGGGG
CTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGGGAGACCAACCCTGCAGACTCCAAG
CCTGGGACCATCCGTGGAGACTTCTGCATACAAGTTGGCAGGAACATTATACATGGCAGT
GATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTGTGGTTTCACCCTGAGGAACTGGTA
GATTACACGAGCTGTGCTCAGAACTGGATCTATGAATGA
Enzyme 7 GenBank Gene ID NM_000269.2 Link Image
Enzyme 7 GeneCard ID NME1 Link Image
Enzyme 7 GenAtlas ID NME1 Link Image
Enzyme 7 HGNC ID HGNC:7849 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 17q21.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Rosengard AM, Krutzsch HC, Shearn A, Biggs JR, Barker E, Margulies IM, King CR, Liotta LA, Steeg PS: Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development. Nature. 1989 Nov 9;342(6246):177-80. [PubMed Link Image]
  2. Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed Link Image]
  3. Wang L, Patel U, Ghosh L, Chen HC, Banerjee S: Mutation in the nm23 gene is associated with metastasis in colorectal cancer. Cancer Res. 1993 Feb 15;53(4):717-20. [PubMed Link Image]
  4. Dooley S, Seib T, Engel M, Theisinger B, Janz H, Piontek K, Zang KD, Welter C: Isolation and characterization of the human genomic locus coding for the putative metastasis control gene nm23-H1. Hum Genet. 1994 Jan;93(1):63-6. [PubMed Link Image]
  5. Ni X, Gu S, Dai J, Cheng H, Guo L, Li L, Ji C, Xie Y, Ying K, Mao Y: Isolation and characterization of a novel human NM23-H1B gene, a different transcript of NM23-H1. J Hum Genet. 2003;48(2):96-100. [PubMed Link Image]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  7. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed Link Image]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. Hailat N, Keim DR, Melhem RF, Zhu XX, Eckerskorn C, Brodeur GM, Reynolds CP, Seeger RC, Lottspeich F, Strahler JR, et al.: High levels of p19/nm23 protein in neuroblastoma are associated with advanced stage disease and with N-myc gene amplification. J Clin Invest. 1991 Jul;88(1):341-5. [PubMed Link Image]
  10. MacDonald NJ, Freije JM, Stracke ML, Manrow RE, Steeg PS: Site-directed mutagenesis of nm23-H1. Mutation of proline 96 or serine 120 abrogates its motility inhibitory activity upon transfection into human breast carcinoma cells. J Biol Chem. 1996 Oct 11;271(41):25107-16. [PubMed Link Image]
  11. Manda R, Kohno T, Matsuno Y, Takenoshita S, Kuwano H, Yokota J: Identification of genes (SPON2 and C20orf2) differentially expressed between cancerous and noncancerous lung cells by mRNA differential display. Genomics. 1999 Oct 1;61(1):5-14. [PubMed Link Image]
  12. Fan Z, Beresford PJ, Oh DY, Zhang D, Lieberman J: Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Cell. 2003 Mar 7;112(5):659-72. [PubMed Link Image]
  13. Valentijn LJ, Koster J, Versteeg R: Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene encodes a novel protein, NM23-LV. Genomics. 2006 Apr;87(4):483-9. Epub 2006 Jan 25. [PubMed Link Image]
  14. Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. Epub 2008 Sep 10. [PubMed Link Image]
  15. Garzia L, D'Angelo A, Amoresano A, Knauer SK, Cirulli C, Campanella C, Stauber RH, Steegborn C, Iolascon A, Zollo M: Phosphorylation of nm23-H1 by CKI induces its complex formation with h-prune and promotes cell motility. Oncogene. 2008 Mar 20;27(13):1853-64. Epub 2007 Oct 1. [PubMed Link Image]
  16. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  17. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  18. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  19. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  20. Min K, Song HK, Chang C, Kim SY, Lee KJ, Suh SW: Crystal structure of human nucleoside diphosphate kinase A, a metastasis suppressor. Proteins. 2002 Feb 15;46(3):340-2. [PubMed Link Image]
  21. Chen Y, Gallois-Montbrun S, Schneider B, Veron M, Morera S, Deville-Bonne D, Janin J: Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases. J Mol Biol. 2003 Sep 26;332(4):915-26. [PubMed Link Image]
  22. Chang CL, Zhu XX, Thoraval DH, Ungar D, Rawwas J, Hora N, Strahler JR, Hanash SM, Radany E: Nm23-H1 mutation in neuroblastoma. Nature. 1994 Aug 4;370(6488):335-6. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5342
Enzyme 8 Name Nucleoside diphosphate kinase 7
Enzyme 8 Synonyms
  1. NDK 7
  2. NDP kinase 7
  3. nm23-H7
Enzyme 8 Gene Name NME7
Enzyme 8 Protein Sequence >Nucleoside diphosphate kinase 7
MNHSERFVFIAEWYDPNASLLRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYDNLHLEDL
FIGNKVNVFSRQLVLIDYGDQYTARQLGSRKEKTLALIKPDAISKAGEIIEIINKAGFTI
TKLKMMMLSRKEALDFHVDHQSRPFFNELIQFITTGPIIAMEILRDDAICEWKRLLGPAN
SGVARTDASESIRALFGTDGIRNAAHGPDSFASAAREMELFFPSSGGCGPANTAKFTNCT
CCIVKPHAVSEGLLGKILMAIRDAGFEISAMQMFNMDRVNVEEFYEVYKGVVTEYHDMVT
EMYSGPCVAMEIQQNNATKTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLP
EDGLLEVQYFFKILDN
Enzyme 8 Number of Residues 376
Enzyme 8 Molecular Weight 42491.4
Enzyme 8 Theoretical pI 6.44
Enzyme 8 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 8 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 8 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 8 Pathways
Enzyme 8 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 4960169 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q9Y5B8 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name NDK7_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1131 bp
ATGAATCATAGTGAAAGATTCGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
Enzyme 8 GenBank Gene ID AF153191 Link Image
Enzyme 8 GeneCard ID NME7 Link Image
Enzyme 8 GenAtlas ID NME7 Link Image
Enzyme 8 HGNC ID HGNC:20461 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 1q24
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5344
Enzyme 9 Name Nucleoside diphosphate kinase B
Enzyme 9 Synonyms
  1. NDK B
  2. NDP kinase B
  3. C-myc purine-binding transcription factor PUF
  4. nm23-H2
Enzyme 9 Gene Name NME2
Enzyme 9 Protein Sequence >Nucleoside diphosphate kinase B
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
Enzyme 9 Number of Residues 152
Enzyme 9 Molecular Weight 17297.9
Enzyme 9 Theoretical pI 8.69
Enzyme 9 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 9 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 9 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically (PubMed:8392752)
Enzyme 9 Pathways
Enzyme 9 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 4467843 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P22392 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name NDKB_HUMAN Link Image
Enzyme 9 PDB ID 1NSK Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >459 bp
ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
Enzyme 9 GenBank Gene ID X58965 Link Image
Enzyme 9 GeneCard ID NME2 Link Image
Enzyme 9 GenAtlas ID NME2 Link Image
Enzyme 9 HGNC ID HGNC:7850 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 17q21.3
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Stahl JA, Leone A, Rosengard AM, Porter L, King CR, Steeg PS: Identification of a second human nm23 gene, nm23-H2. Cancer Res. 1991 Jan 1;51(1):445-9. [PubMed Link Image]
  2. Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed Link Image]
  3. Postel EH, Berberich SJ, Flint SJ, Ferrone CA: Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis. Science. 1993 Jul 23;261(5120):478-80. [PubMed Link Image]
  4. Valentijn LJ, Koster J, Versteeg R: Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene encodes a novel protein, NM23-LV. Genomics. 2006 Apr;87(4):483-9. Epub 2006 Jan 25. [PubMed Link Image]
  5. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Seifert M, Seib T, Engel M, Dooley S, Welter C: Characterization of the human nm23-H2 promoter region and localization of the microsatellite D17S396. Biochem Biophys Res Commun. 1995 Oct 24;215(3):910-4. [PubMed Link Image]
  8. Iwashita S, Fujii M, Mukai H, Ono Y, Miyamoto M: Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2. Biochem Biophys Res Commun. 2004 Aug 6;320(4):1063-8. [PubMed Link Image]
  9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  10. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  12. Webb PA, Perisic O, Mendola CE, Backer JM, Williams RL: The crystal structure of a human nucleoside diphosphate kinase, NM23-H2. J Mol Biol. 1995 Aug 25;251(4):574-87. [PubMed Link Image]
  13. Morera S, Lacombe ML, Xu Y, LeBras G, Janin J: X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution. Structure. 1995 Dec 15;3(12):1307-14. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5345
Enzyme 10 Name Nucleoside diphosphate kinase 3
Enzyme 10 Synonyms
  1. NDK 3
  2. NDP kinase 3
  3. DR-nm23
  4. Nucleoside diphosphate kinase C
  5. NDPKC
  6. nm23-H3
Enzyme 10 Gene Name NME3
Enzyme 10 Protein Sequence >Nucleoside diphosphate kinase 3
MICLVLTIFANLFPAACTGAHERTFLAVKPDGVQRRLVGEIVRRFERKGFKLVALKLVQA
SEELLREHYAELRERPFYGRLVKYMASGPVVAMVWQGLDVVRTSRALIGATNPADAPPGT
IRGDFCIEVGKNLIHGSDSVESARREIALWFRADELLCWEDSAGHWLYE
Enzyme 10 Number of Residues 169
Enzyme 10 Molecular Weight 19014.9
Enzyme 10 Theoretical pI 7.97
Enzyme 10 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 10 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 10 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Probably has a role in normal hematopoiesis by inhibition of granulocyte differentiation and induction of apoptosis
Enzyme 10 Pathways
Enzyme 10 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 14336763 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q13232 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name NDK3_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >510 bp
ATGATCTGCCTGGTGCTGACCATCTTCGCTAACCTCTTCCCCGCGGCCTGCACCGGCGCA
CACGAACGCACCTTCCTGGCCGTGAAGCCGGACGGCGTGCAGCGGCGGCTGGTGGGCGAG
ATTGTGCGGCGCTTCGAGAGGAAGGGCTTCAAGTTGGTGGCGCTGAAGCTGGTGCAGGCC
TCCGAGGAGCTGCTGCGTGAGCACTACGCCGAGCTGCGTGAACGCCCGTTCTACGGCCGC
CTTGTCAAGTATATGGCCTCCGGGCCGGTGGTGGCCATGGTTTGGCAGGGGCTGGACGTG
GTGCGCACCTCGCGGGCGCTCATCGGAGCCACGAACCCGGCCGACGCCCCGCCCGGCACC
ATCCGCGGGGATTTCTGCATCGAGGTTGGCAAGAACCTGATTCACGGCAGCGACTCGGTG
GAGAGTGCCCGCCGCGAGATCGCTCTCTGGTTCCGCGCAGACGAGCTCCTCTGCTGGGAG
GACAGCGCTGGGCACTGGCTGTATGAGTAG
Enzyme 10 GenBank Gene ID AE006639 Link Image
Enzyme 10 GeneCard ID NME3 Link Image
Enzyme 10 GenAtlas ID NME3 Link Image
Enzyme 10 HGNC ID HGNC:7851 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 16q13
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Venturelli D, Martinez R, Melotti P, Casella I, Peschle C, Cucco C, Spampinato G, Darzynkiewicz Z, Calabretta B: Overexpression of DR-nm23, a protein encoded by a member of the nm23 gene family, inhibits granulocyte differentiation and induces apoptosis in 32Dc13 myeloid cells. Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7435-9. [PubMed Link Image]
  2. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5346
Enzyme 11 Name Nucleoside diphosphate kinase 6
Enzyme 11 Synonyms
  1. NDK 6
  2. NDP kinase 6
  3. Inhibitor of p53-induced apoptosis-alpha
  4. IPIA-alpha
  5. nm23-H6
Enzyme 11 Gene Name NME6
Enzyme 11 Protein Sequence >Nucleoside diphosphate kinase 6
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA
Enzyme 11 Number of Residues 186
Enzyme 11 Molecular Weight 21142.0
Enzyme 11 Theoretical pI 8.49
Enzyme 11 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 11 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 11 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Inhibitor of p53-induced apoptosis
Enzyme 11 Pathways
Enzyme 11 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 3228530 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID O75414 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name NDK6_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >561 bp
ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA
Enzyme 11 GenBank Gene ID AF051941 Link Image
Enzyme 11 GeneCard ID NME6 Link Image
Enzyme 11 GenAtlas ID NME6 Link Image
Enzyme 11 HGNC ID HGNC:20567 Link Image
Enzyme 11 Chromosome Location 3
Enzyme 11 Locus 3p21
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Mehus JG, Deloukas P, Lambeth DO: NME6: a new member of the nm23/nucleoside diphosphate kinase gene family located on human chromosome 3p21.3. Hum Genet. 1999 Jun;104(6):454-9. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5351
Enzyme 12 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Enzyme 12 Synonyms
  1. E-NPP 1
  2. Membrane component chromosome 6 surface marker 1
  3. Phosphodiesterase I/nucleotide pyrophosphatase 1
  4. Plasma-cell membrane glycoprotein PC-1
  5. Alkaline phosphodiesterase I
  6. Nucleotide pyrophosphatase
  7. NPPase
Enzyme 12 Gene Name ENPP1
Enzyme 12 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPL
EKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNC
RCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINY
SSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKK
CGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEW
YKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLP
KDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLIL
ISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSC
REPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNV
FSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVY
TPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYG
RPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPL
SPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTL
LRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKD
TSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSF
YQQRKEPVSDILKLKTHLPTFSQED
Enzyme 12 Number of Residues 925
Enzyme 12 Molecular Weight 104923.6
Enzyme 12 Theoretical pI 7.14
Enzyme 12 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • ion binding
  • metal ion binding
  • molecular transducer activity
  • nucleic acid binding
  • pattern binding
  • polysaccharide binding
  • receptor activity
  • scavenger receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • immune response
  • immune system process
  • metabolic process
Component
Enzyme 12 General Function Involved in catalytic activity
Enzyme 12 Specific Function Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity
Enzyme 12 Pathways
Enzyme 12 Reactions
  • a dinucleotide + H2O = 2 mononucleotides [RN:R00056]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • 77-97
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 170650661 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P22413 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name ENPP1_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >2778 bp
ATGGAGCGCGACGGCTGCGCGGGGGGCGGGAGCCGCGGCGGCGAGGGCGGGCGCGCTCCC
CGGGAGGGCCCGGCGGGGAACGGCCGCGATCGGGGCCGCAGCCACGCTGCCGAGGCGCCC
GGGGACCCGCAGGCGGCCGCGTCCTTGCTGGCCCCTATGGACGTGGGGGAGGAGCCGCTG
GAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCCAACACCTATAAAGTACTCTCGCTG
GTATTGTCAGTATGTGTGTTAACAACAATACTTGGTTGTATATTTGGGTTGAAACCAAGC
TGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGTTTCGAGAGAACATTTGGGAACTGT
CGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGCTGTTTAGATTACCAGGAGACGTGC
ATAGAACCAGAACATATATGGACTTGCAACAAATTCAGGTGTGGTGAGAAAAGGTTGACC
AGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGACAAGGGCGACTGCTGCATCAACTAC
AGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAAGAACCATGTGAGAGCATTAATGAG
CCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACCCTCTTATTTTCTTTGGATGGATTC
AGGGCAGAATATTTACACACTTGGGGTGGACTTCTTCCTGTTATTAGCAAACTAAAAAAA
TGTGGAACATATACTAAAAACATGAGACCGGTATATCCAACAAAAACTTTCCCCAATCAC
TACAGCATTGTCACCGGATTGTATCCAGAATCTCATGGCATAATCGACAATAAAATGTAT
GATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGTAAAGAGAAATTTAATCCTGAGTGG
TACAAAGGAGAACCAATTTGGGTCACAGCTAAGTATCAAGGCCTCAAGTCTGGCACATTT
TTCTGGCCAGGATCAGATGTGGAAATTAACGGAATTTTCCCAGACATCTATAAAATGTAT
AATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCTGTTCTTCAGTGGCTACAGCTTCCT
AAAGATGAAAGACCACACTTTTACACTCTGTATTTAGAAGAACCAGATTCTTCAGGTCAT
TCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCCTTGCAGAGGGTTGATGGTATGGTT
GGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTGCACAGATGCCTGAACCTCATCCTT
ATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAGAAATACATATATCTGAATAAATAT
TTGGGGGATGTTAAAAATATTAAAGTTATCTATGGACCTGCAGCTCGATTGAGACCCTCT
GATGTCCCAGATAAATACTATTCATTTAACTATGAAGGCATTGCCCGAAATCTTTCTTGC
CGGGAACCAAACCAGCACTTCAAACCTTACCTGAAACATTTCTTACCTAAGCGTTTGCAC
TTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTCTATTTGGACCCTCAGTGGCAACTT
GCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGTGGATTTCATGGCTCTGACAATGTA
TTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGACCTGGATTCAAGCATGGCATTGAG
GCTGACACCTTTGAAAACATTGAAGTCTATAACTTAATGTGTGATTTACTGAATTTGACA
CCGGCTCCTAATAACGGAACTCATGGAAGTCTTAACCACCTTCTAAAGAATCCTGTTTAT
ACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTACAGTGCCCCTTCACAAGAAACCCC
AGAGATAACCTTGGCTGCTCATGTAACCCTTCGATTTTGCCGATTGAGGATTTTCAAACA
CAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATTAAGCATGAAACTTTACCCTATGGA
AGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGTCTTCTTTCCCAGCACCAGTTTATG
AGTGGATACAGCCAAGACATCTTAATGCCCCTTTGGACATCCTATACCGTGGACAGAAAT
GACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTGTACCAGGACTTTAGAATTCCTCTT
AGTCCTGTCCATAAATGTTCATTTTATAAAAATAACACCAAAGTGAGTTACGGGTTCCTC
TCCCCACCACAACTAAATAAAAATTCAAGTGGAATATATTCTGAAGCTTTGCTTACTACA
AATATAGTGCCAATGTACCAGAGTTTTCAAGTTATATGGCGCTACTTTCATGACACCCTA
CTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAATGTCGTCAGTGGTCCTGTGTTTGAC
TTTGATTATGATGGACGTTGTGATTCCTTAGAGAATCTGAGGCAAAAAAGAAGAGTCATC
CGTAACCAAGAAATTTTGATTCCAACTCACTTCTTTATTGTGCTAACAAGCTGTAAAGAT
ACATCTCAGACGCCTTTGCACTGTGAAAACCTAGACACCTTAGCTTTCATTTTGCCTCAC
AGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAGCATGACTCCTCATGGGTTGAAGAA
TTGTTAATGTTACACAGAGCACGGATCACAGATGTTGAGCACATCACTGGACTCAGCTTC
TATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTAAAGTTGAAAACACATTTGCCAACC
TTTAGCCAAGAAGACTGA
Enzyme 12 GenBank Gene ID NM_006208.2 Link Image
Enzyme 12 GeneCard ID ENPP1 Link Image
Enzyme 12 GenAtlas ID ENPP1 Link Image
Enzyme 12 HGNC ID HGNC:3356 Link Image
Enzyme 12 Chromosome Location 6
Enzyme 12 Locus 6q22-q23
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Buckley MF, Loveland KA, McKinstry WJ, Garson OM, Goding JW: Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. J Biol Chem. 1990 Oct 15;265(29):17506-11. [PubMed Link Image]
  2. Funakoshi I, Kato H, Horie K, Yano T, Hori Y, Kobayashi H, Inoue T, Suzuki H, Fukui S, Tsukahara M, et al.: Molecular cloning of cDNAs for human fibroblast nucleotide pyrophosphatase. Arch Biochem Biophys. 1992 May 15;295(1):180-7. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Pizzuti A, Frittitta L, Argiolas A, Baratta R, Goldfine ID, Bozzali M, Ercolino T, Scarlato G, Iacoviello L, Vigneri R, Tassi V, Trischitta V: A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding region is strongly associated with insulin resistance. Diabetes. 1999 Sep;48(9):1881-4. [PubMed Link Image]
  6. Belli SI, Goding JW: Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities. Eur J Biochem. 1994 Dec 1;226(2):433-43. [PubMed Link Image]
  7. Belli SI, Mercuri FA, Sali A, Goding JW: Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide pyrophosphatase) and analysis of the active site. Eur J Biochem. 1995 Mar 15;228(3):669-76. [PubMed Link Image]
  8. Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed Link Image]
  9. Bello V, Goding JW, Greengrass V, Sali A, Dubljevic V, Lenoir C, Trugnan G, Maurice M: Characterization of a di-leucine-based signal in the cytoplasmic tail of the nucleotide-pyrophosphatase NPP1 that mediates basolateral targeting but not endocytosis. Mol Biol Cell. 2001 Oct;12(10):3004-15. [PubMed Link Image]
  10. Yano Y, Hayashi Y, Sano K, Nagano H, Nakaji M, Seo Y, Ninomiya T, Yoon S, Yokozaki H, Kasuga M: Expression and localization of ecto-nucleotide pyrophosphatase/phosphodiesterase I-1 (E-NPP1/PC-1) and -3 (E-NPP3/CD203c/PD-Ibeta/B10/gp130(RB13-6)) in inflammatory and neoplastic bile duct diseases. Cancer Lett. 2004 Apr 30;207(2):139-47. [PubMed Link Image]
  11. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  12. Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed Link Image]
  13. Nakamura I, Ikegawa S, Okawa A, Okuda S, Koshizuka Y, Kawaguchi H, Nakamura K, Koyama T, Goto S, Toguchida J, Matsushita M, Ochi T, Takaoka K, Nakamura Y: Association of the human NPPS gene with ossification of the posterior longitudinal ligament of the spine (OPLL). Hum Genet. 1999 Jun;104(6):492-7. [PubMed Link Image]
  14. Rutsch F, Ruf N, Vaingankar S, Toliat MR, Suk A, Hohne W, Schauer G, Lehmann M, Roscioli T, Schnabel D, Epplen JT, Knisely A, Superti-Furga A, McGill J, Filippone M, Sinaiko AR, Vallance H, Hinrichs B, Smith W, Ferre M, Terkeltaub R, Nurnberg P: Mutations in ENPP1 are associated with 'idiopathic' infantile arterial calcification. Nat Genet. 2003 Aug;34(4):379-81. [PubMed Link Image]
  15. Cheng KS, Chen MR, Ruf N, Lin SP, Rutsch F: Generalized arterial calcification of infancy: different clinical courses in two affected siblings. Am J Med Genet A. 2005 Jul 15;136(2):210-3. [PubMed Link Image]
  16. Bacci S, Ludovico O, Prudente S, Zhang YY, Di Paola R, Mangiacotti D, Rauseo A, Nolan D, Duffy J, Fini G, Salvemini L, Amico C, Vigna C, Pellegrini F, Menzaghi C, Doria A, Trischitta V: The K121Q polymorphism of the ENPP1/PC-1 gene is associated with insulin resistance/atherogenic phenotypes, including earlier onset of type 2 diabetes and myocardial infarction. Diabetes. 2005 Oct;54(10):3021-5. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5486
Enzyme 13 Name Fucose-1-phosphate guanylyltransferase
Enzyme 13 Synonyms
  1. GDP-L-fucose diphosphorylase
  2. GDP-L-fucose pyrophosphorylase
Enzyme 13 Gene Name FPGT
Enzyme 13 Protein Sequence >Fucose-1-phosphate guanylyltransferase
MAAARDPPEVSLREATQRKLRRFSELRGKLVARGEFWDIVAITAADEKQELAYNQQLSEK
LKRKELPLGVQYHVFVDPAGAKIGNGGSTLCALQCLEKLYGDKWNSFTILLIHSGGYSQR
LPNASALGKIFTALPLGNPIYQMLELKLAMYIDFPLNMNPGILVTCADDIELYSIGEFEF
IRFDKPGFTALAHPSSLTIGTTHGVFVLDPFDDLKHRDLEYRSCHRFLHKPSIEKMYQFN
AVCRPGNFCQQDFAGGDIADLKLDSDYVYTDSLFYMDHKSAKMLLAFYEKIGTLSCEIDA
YGDFLQALGPGATVEYTRNTSNVIKEESELVEMRQRIFHLLKGTSLNVVVLNNSKFYHIG
TTEEYLFYFTSDNSLKSELGLQSITFSIFPDIPECSGKTSCIIQSILDSRCSVAPGSVVE
YSRLGPDVSVGENCIISGSYILTKAALPAHSFVCSLSLKMNRCLKYATMAFGVQDNLKKS
VKTLSDIKLLQFFGVCFLSCLDVWNLKVTEELFSGNKTCLSLWTARIFPVCSSLSDSVIT
SLKMLNAVKNKSAFSLNSYKLLSIEEMLIYKDVEDMITYREQIFLEISLKSSLM
Enzyme 13 Number of Residues 594
Enzyme 13 Molecular Weight 66598.1
Enzyme 13 Theoretical pI 6.44
Enzyme 13 GO Classification Not Available
Enzyme 13 General Function Involved in fucose-1-phosphate guanylyltransferase acti
Enzyme 13 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 13 Pathways
Enzyme 13 Reactions
  • GTP + beta-L-fucose 1-phosphate = diphosphate + GDP-L-fucose [RN:R01951]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 2582185 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID O14772 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name FPGT_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 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 13 GenBank Gene ID AF017445 Link Image
Enzyme 13 GeneCard ID FPGT Link Image
Enzyme 13 GenAtlas ID FPGT Link Image
Enzyme 13 HGNC ID HGNC:3825 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 1p31.1
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Pastuszak I, Ketchum C, Hermanson G, Sjoberg EJ, Drake R, Elbein AD: GDP-L-fucose pyrophosphorylase. Purification, cDNA cloning, and properties of the enzyme. J Biol Chem. 1998 Nov 13;273(46):30165-74. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5668
Enzyme 14 Name Inosine triphosphate pyrophosphatase
Enzyme 14 Synonyms
  1. ITPase
  2. Inosine triphosphatase
  3. Putative oncogene protein hlc14-06-p
Enzyme 14 Gene Name ITPA
Enzyme 14 Protein Sequence >Inosine triphosphate pyrophosphatase
MAASLVGKKIVFVTGNAKKLEEVVQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEA
VRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLKPEGLHQLLAGFEDKSAYALCTFAL
STGDPSQPVRLFRGRTSGRIVAPRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFR
ALLELQEYFGSLAA
Enzyme 14 Number of Residues 194
Enzyme 14 Molecular Weight 21445.5
Enzyme 14 Theoretical pI 5.34
Enzyme 14 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 14 General Function Involved in hydrolase activity
Enzyme 14 Specific Function Hydrolyzes ITP and dITP to their respective monophosphate derivatives. Xanthosine 5'-triphosphate (XTP) is also a potential substrate. May be the major enzyme responsible for regulating ITP concentration in cells
Enzyme 14 Pathways
Enzyme 14 Reactions
  • a nucleoside triphosphate + H2O = a nucleotide + diphosphate [RN:R01532]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 21104378 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q9BY32 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name ITPA_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >585 bp
ATGGCGGCCTCATTGGTGGGGAAGAAGATCGTGTTTGTAACGGGGAACGCCAAGAAGCTG
GAGGAGGTCGTTCAGATTCTAGGAGATAAGTTTCCATGCACTTTGGTGGCACAGAAAATT
GACCTGCCGGAGTACCAAGGGGAGCCGGATGAGATTTCCATACAGAAATGTCAGGAGGCA
GTTCGCCAGGTACAGGGGCCCGTGCTGGTTGAGGACACTTGTCTGTGCTTCAATGCCCTT
GGAGGGCTCCCCGGCCCCTACATAAAGTGGTTTCTGGAGAAGTTAAAGCCTGAAGGTCTC
CACCAGCTCCTGGCCGGGTTCGAGGACAAGTCAGCCTATGCGCTCTGCACGTTTGCACTC
AGCACCGGGGACCCAAGCCAGCCCGTGCGCCTGTTCAGGGGCCGGACCTCGGGCCGGATC
GTGGCACCCAGAGGCTGCCAGGACTTTGGCTGGGACCCCTGCTTTCAGCCTGATGGATAT
GAGCAGACGTACGCAGAGATGCCTAAGGCGGAGAAGAACGCTGTCTCCCATCGCTTCCGG
GCCCTGCTGGAGCTGCAGGAATACTTTGGCAGTTTGGCAGCTTGA
Enzyme 14 GenBank Gene ID AB062127 Link Image
Enzyme 14 GeneCard ID ITPA Link Image
Enzyme 14 GenAtlas ID ITPA Link Image
Enzyme 14 HGNC ID HGNC:6176 Link Image
Enzyme 14 Chromosome Location 2
Enzyme 14 Locus 20p
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Lin S, McLennan AG, Ying K, Wang Z, Gu S, Jin H, Wu C, Liu W, Yuan Y, Tang R, Xie Y, Mao Y: Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the itpa gene. J Biol Chem. 2001 Jun 1;276(22):18695-701. Epub 2001 Mar 13. [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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Stenmark P, Kursula P, Flodin S, Graslund S, Landry R, Nordlund P, Schuler H: Crystal structure of human inosine triphosphatase. Substrate binding and implication of the inosine triphosphatase deficiency mutation P32T. J Biol Chem. 2007 Feb 2;282(5):3182-7. Epub 2006 Nov 29. [PubMed Link Image]
  5. Sumi S, Marinaki AM, Arenas M, Fairbanks L, Shobowale-Bakre M, Rees DC, Thein SL, Ansari A, Sanderson J, De Abreu RA, Simmonds HA, Duley JA: Genetic basis of inosine triphosphate pyrophosphohydrolase deficiency. Hum Genet. 2002 Oct;111(4-5):360-7. Epub 2002 Aug 15. [PubMed Link Image]
  6. Cao H, Hegele RA: DNA polymorphisms in ITPA including basis of inosine triphosphatase deficiency. J Hum Genet. 2002;47(11):620-2. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5864
Enzyme 15 Name GMP synthase [glutamine-hydrolyzing]
Enzyme 15 Synonyms
  1. GMP synthetase
  2. Glutamine amidotransferase
Enzyme 15 Gene Name GMPS
Enzyme 15 Protein Sequence >GMP synthase [glutamine-hydrolyzing]
MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETP
AFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHK
KSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANE
SKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVL
VLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAA
HSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPE
EVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVR
ILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPH
TLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDW
ESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILR
ESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVE
VVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE
Enzyme 15 Number of Residues 693
Enzyme 15 Molecular Weight 76714.8
Enzyme 15 Theoretical pI 6.86
Enzyme 15 GO Classification
Function
  • ATP binding
  • GMP synthase (glutamine-hydrolyzing) activity
  • GMP synthase (glutamine-hydrolyzing) activity
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • carbon-nitrogen ligase activity, with glutamine as amido-N-donor
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleoside binding
  • purine nucleoside binding
Process
  • GMP biosynthetic process
  • biosynthetic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • cellular nitrogen compound metabolic process
  • glutamine family amino acid metabolic process
  • glutamine metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside monophosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside monophosphate biosynthetic process
Component
Enzyme 15 General Function Involved in catalytic activity
Enzyme 15 Specific Function Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division
Enzyme 15 Pathways
Enzyme 15 Reactions
  • ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate [RN:R01231]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID P49915 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name GUAA_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >2082 bp
ATGGCTCTGTGCAACGGAGACTCCAAGCTGGAGAATGCTGGAGGAGACCTTAAGGATGGC
CACCACCACTATGAAGGAGCTGTTGTCATTCTGGATGCTGGTGCTCAGTACGGGAAAGTC
ATAGACCGAAGAGTGAGGGAACTGTTCGTGCAGTCTGAAATTTTCCCCTTGGAAACACCA
GCATTTGCTATAAAGGAACAAGGATTCCGTGCTATTATCATCTCTGGAGGACCTAATTCT
GTGTATGCTGAAGATGCTCCCTGGTTTGATCCAGCAATATTCACTATTGGCAAGCCTGTT
CTTGGAATTTGCTATGGTATGCAGATGATGAATAAGGTATTTGGAGGTACTGTGCACAAA
AAAAGTGTCAGAGAAGATGGAGTTTTCAACATTAGTGTGGATAATACATGTTCATTATTC
AGGGGCCTTCAGAAGGAAGAAGTTGTTTTGCTTACACATGGAGATAGTGTAGACAAAGTA
GCTGATGGATTCAAGGTTGTGGCACGTTCTGGAAACATAGTAGCAGGCATAGCAAATGAA
TCTAAAAAGTTATATGGAGCACAGTTCCACCCTGAAGTTGGCCTTACAGAAAATGGAAAA
GTAATACTGAAGAATTTCCTTTATGATATAGCTGGATGCAGTGGAACCTTCACCGTGCAG
AACAGAGAACTTGAGTGTATTCGAGAGATCAAAGAGAGAGTAGGCACGTCAAAAGTTTTG
GTTTTACTCAGTGGTGGAGTAGACTCAACAGTTTGTACAGCTTTGCTAAATCGTGCTTTG
AACCAAGAACAAGTCATTGCTGTGCACATTGATAATGGCTTTATGAGAAAACGAGAAAGC
CAGTCTGTTGAAGAGGCCCTCAAAAAGCTTGGAATTCAGGTCAAAGTGATAAATGCTGCT
CATTCTTTCTACAATGGAACAACAACCCTACCAATATCAGATGAAGATAGAACCCCACGG
AAAAGAATTAGCAAAACGTTAAATATGACCACAAGTCCTGAAGAGAAAAGAAAAATCATT
GGGGATACTTTTGTTAAGATTGCCAATGAAGTAATTGGAGAAATGAACTTGAAACCAGAG
GAGGTTTTCCTTGCCCAAGGTACTTTACGGCCTGATCTAATTGAAAGTGCATCCCTTGTT
GCAAGTGGCAAAGCTGAACTCATCAAAACCCATCACAATGACACAGAGCTCATCAGAAAG
TTGAGAGAGGAGGGAAAAGTAATAGAACCTCTGAAAGATTTTCATAAAGATGAAGTGAGA
ATTTTGGGCAGAGAACTTGGACTTCCAGAAGAGTTAGTTTCCAGGCATCCATTTCCAGGT
CCTGGCCTGGCAATCAGAGTAATATGTGCTGAAGAACCTTATATTTGTAAGGACTTTCCT
GAAACCAACAATATTTTGAAAATAGTAGCTGATTTTTCTGCAAGTGTTAAAAAGCCACAT
ACCCTATTACAGAGAGTCAAAGCCTGCACAACAGAAGAGGATCAGGAGAAGCTGATGCAA
ATTACCAGTCTGCATTCACTGAATGCCTTCTTGCTGCCAATTAAAACTGTAGGTGTGCAG
GGTGACTGTCGTTCCTACAGTTACGTGTGTGGAATCTCCAGTAAAGATGAACCTGACTGG
GAATCACTTATTTTTCTGGCTAGGCTTATACCTCGCATGTGTCACAACGTTAACAGAGTT
GTTTATATATTTGGCCCACCAGTTAAAGAACCTCCTACAGATGTTACTCCCACTTTCTTG
ACAACAGGGGTGCTCAGTACTTTACGCCAAGCTGATTTTGAGGCCCATAACATTCTCAGG
GAGTCTGGGTATGCTGGGAAAATCAGCCAGATGCCGGTGATTTTGACACCATTACATTTT
GATCGGGACCCACTTCAAAAGCAGCCTTCATGCCAGAGATCTGTGGTTATTCGAACCTTT
ATTACTAGTGACTTCATGACTGGTATACCTGCAACACCTGGCAATGAGATCCCTGTAGAG
GTGGTATTAAAGATGGTCACTGAGATTAAGAAGATTCCTGGTATTTCTCGAATTATGTAT
GACTTAACATCAAAGCCCCCAGGAACTACTGAGTGGGAGTAA
Enzyme 15 GenBank Gene ID U10860 Link Image
Enzyme 15 GeneCard ID GMPS Link Image
Enzyme 15 GenAtlas ID GMPS Link Image
Enzyme 15 HGNC ID HGNC:4378 Link Image
Enzyme 15 Chromosome Location 3
Enzyme 15 Locus 3q24
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Hirst M, Haliday E, Nakamura J, Lou L: Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA. J Biol Chem. 1994 Sep 23;269(38):23830-7. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Pegram LD, Megonigal MD, Lange BJ, Nowell PC, Rowley JD, Rappaport EF, Felix CA: t(3;11) translocation in treatment-related acute myeloid leukemia fuses MLL with the GMPS (GUANOSINE 5' MONOPHOSPHATE SYNTHETASE) gene. Blood. 2000 Dec 15;96(13):4360-2. [PubMed Link Image]
  4. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  5. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  6. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5893
Enzyme 16 Name Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
Enzyme 16 Synonyms
  1. Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase
  2. Ap4A hydrolase
  3. Ap4Aase
  4. Diadenosine tetraphosphatase
  5. Nucleoside diphosphate-linked moiety X motif 2
  6. Nudix motif 2
Enzyme 16 Gene Name NUDT2
Enzyme 16 Protein Sequence >Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
MALRACGLIIFRRCLIPKVDNNAIEFLLLQASDGIHHWTPPKGHVEPGEDDLETALRETQ
EEAGIEAGQLTIIEGFKRELNYVARNKPKTVIYWLAEVKDYDVEIRLSHEHQAYRWLGLE
EACQLAQFKEMKAALQEGHQFLCSIEA
Enzyme 16 Number of Residues 147
Enzyme 16 Molecular Weight 16829.1
Enzyme 16 Theoretical pI 5.06
Enzyme 16 GO Classification
Function
  • bis(5'-nucleosyl)-tetraphosphatase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleotide diphosphatase activity
  • pyrophosphatase activity
Process
Component
Enzyme 16 General Function Involved in hydrolase activity
Enzyme 16 Specific Function Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis
Enzyme 16 Pathways
Enzyme 16 Reactions
  • P1,P4-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP [RN:R01232]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 55958893 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID P50583 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name AP4A_HUMAN Link Image
Enzyme 16 PDB ID 1XSC Link Image
Enzyme 16 PDB File Show
Enzyme 16 3D Structure
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >444 bp
ATGGCCTTGAGAGCATGTGGCTTGATCATCTTCCGAAGATGCCTCATTCCCAAAGTGGAC
AACAATGCAATTGAGTTTTTACTGCTGCAGGCATCAGATGGCATTCATCACTGGACTCCT
CCCAAAGGCCATGTGGAACCAGGAGAGGATGACTTGGAAACAGCCCTGAGGGAGACCCAA
GAGGAAGCAGGCATAGAAGCAGGCCAGCTGACCATTATTGAGGGGTTCAAAAGGGAACTC
AATTATGTGGCCAGGAACAAGCCTAAAACAGTCATTTACTGGCTGGCGGAGGTGAAGGAC
TATGACGTGGAGATCCGCCTCTCCCATGAGCACCAAGCCTACCGCTGGCTGGGGCTGGAG
GAGGCCTGCCAGTTGGCTCAGTTCAAGGAGATGAAGGCAGCGCTCCAAGAAGGACACCAG
TTTCTTTGCTCCATAGAGGCCTGA
Enzyme 16 GenBank Gene ID AL356494 Link Image
Enzyme 16 GeneCard ID NUDT2 Link Image
Enzyme 16 GenAtlas ID NUDT2 Link Image
Enzyme 16 HGNC ID HGNC:8049 Link Image
Enzyme 16 Chromosome Location 9
Enzyme 16 Locus 9p13
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Thorne NM, Hankin S, Wilkinson MC, Nunez C, Barraclough R, McLennan AG: Human diadenosine 5',5"'-P1,P4-tetraphosphate pyrophosphohydrolase is a member of the MutT family of nucleotide pyrophosphatases. Biochem J. 1995 Nov 1;311 ( Pt 3):717-21. [PubMed Link Image]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Swarbrick JD, Buyya S, Gunawardana D, Gayler KR, McLennan AG, Gooley PR: Structure and substrate-binding mechanism of human Ap4A hydrolase. J Biol Chem. 2005 Mar 4;280(9):8471-81. Epub 2004 Dec 13. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5924
Enzyme 17 Name Adenylate kinase isoenzyme 5
Enzyme 17 Synonyms
  1. AK 5
  2. ATP-AMP transphosphorylase 5
Enzyme 17 Gene Name AK5
Enzyme 17 Protein Sequence >Adenylate kinase isoenzyme 5
MNTNDAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVKELGGCDKVKWDTFV
SQEKKTLPPLNGGQSRRSFLRNVMPENSNFPYRRYDRLPPIHQFSIESDTDLSETAELIE
EYEVFDPTRPRPKIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKW
SLIAKIITTGELAPQETTITEIKQKLMQIPDEEGIVIDGFPRDVAQALSFEDQICTPDLV
VFLACANQRLKERLLKRAEQQGRPDDNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDA
DRDEDEVFYDISMAVDNKLFPNKEAAAGSSDLDPSMILDTGEIIDTGSDYEDQGDDQLNV
FGEDTMGGFMEDLRKCKIIFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESE
RSKLIRDIMERGDLVPSGIVLELLKEAMVASLGDTRGFLIDGYPREVKQGEEFGRRIGDP
QLVICMDCSADTMTNRLLQRSRSSLPVDDTTKTIAKRLEAYYRASIPVIAYYETKTQLHK
INAEGTPEDVFLQLCTAIDSIF
Enzyme 17 Number of Residues 562
Enzyme 17 Molecular Weight 63332.4
Enzyme 17 Theoretical pI 4.69
Enzyme 17 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • adenylate kinase activity
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleoside binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • ATP metabolic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate metabolic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 17 General Function Involved in ATP binding
Enzyme 17 Specific Function Active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP
Enzyme 17 Pathways
Enzyme 17 Reactions
  • ATP + AMP = 2 ADP [RN:R00127]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 28144897 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q9Y6K8 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name KAD5_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1689 bp
ATGAACACCAACGATGCCAAGGAGTATCTGGCCCGGAGGGAAATCCCTCAGCTTTTTGAG
AGCCTTTTGAATGGACTGATGTGTTCTAAGCCCGAAGATCCAGTAGAATACTTGGAAAGT
TGTTTACAAAAAGTAAAGGAACTGGGTGGCTGTGACAAGGTGAAATGGGATACATTTGTA
AGCCAGGAAAAGAAGACCTTACCTCCACTAAATGGAGGACAGTCACGGAGATCCTTTCTA
AGAAATGTAATGCCTGAAAACTCAAACTTTCCATATCGGCGGTATGACCGGCTCCCTCCA
ATCCATCAATTCTCCATAGAAAGTGACACGGATCTCTCTGAGACTGCAGAGTTGATTGAG
GAGTATGAGGTTTTTGATCCTACCAGACCTCGACCAAAAATCATTCTTGTTATAGGTGGT
CCAGGAAGTGGAAAGGGTACTCAGAGTTTGAAAATTGCAGAACGATATGGATTCCAATAC
ATTTCTGTGGGAGAATTATTAAGAAAGAAGATCCACAGTACCAGCAGCAATAGGAAATGG
AGTCTTATTGCCAAGATAATTACAACTGGAGAATTGGCCCCACAGGAAACAACAATTACA
GAGATAAAACAAAAATTGATGCAAATACCTGATGAAGAGGGCATTGTTATTGATGGATTT
CCAAGAGATGTTGCCCAGGCTCTATCTTTTGAGGACCAAATCTGTACCCCCGATTTGGTG
GTATTCCTGGCTTGTGCTAATCAGAGACTCAAAGAAAGATTACTGAAGCGTGCAGAACAG
CAGGGCCGACCAGACGACAATGTAAAAGCTACCCAAAGGAGACTAATGAACTTCAAGCAG
AATGCTGCTCCATTGGTTAAATACTTCCAGGAAAAGGGGCTCATCATGACATTTGATGCC
GACCGCGATGAGGATGAGGTGTTCTATGACATCAGCATGGCAGTTGACAACAAGTTATTT
CCAAACAAAGAGGCTGCAGCAGGTTCAAGTGACCTTGATCCTTCGATGATATTGGACACT
GGAGAGATCATTGATACAGGATCTGATTATGAAGATCAGGGTGATGACCAGTTAAATGTA
TTTGGAGAGGACACTATGGGAGGTTTCATGGAAGATTTGAGAAAGTGTAAAATTATTTTC
ATAATTGGTGGTCCTGGCTCTGGCAAAGGCACACAGTGTGAAAAGCTGGTGGAAAAATAT
GGATTTACACATCTCTCAACTGGCGAGCTCCTGCGTGAGGAACTGGCATCAGAATCTGAA
AGAAGCAAATTGATCAGAGACATTATGGAACGTGGAGACCTGGTGCCCTCAGGCATCGTT
TTGGAGCTCCTGAAGGAGGCCATGGTGGCCAGCCTCGGGGACACCAGGGGCTTCCTGATT
GACGGCTATCCTCGGGAGGTGAAGCAAGGGGAAGAGTTCGGACGCAGGATTGGAGACCCA
CAGTTGGTGATCTGTATGGACTGCTCGGCAGACACCATGACCAACCGCCTTCTCCAAAGG
AGCCGGAGCAGCCTGCCTGTGGACGACACCACCAAGACCATCGCCAAGCGCCTAGAAGCC
TACTACCGAGCGTCCATCCCCGTGATCGCCTACTACGAGACAAAAACACAGCTACACAAG
ATAAATGCAGAGGGAACACCAGAGGACGTTTTTCTTCAACTCTGCACAGCTATTGACTCT
ATTTTCTGA
Enzyme 17 GenBank Gene ID NM_174858.1 Link Image
Enzyme 17 GeneCard ID AK5 Link Image
Enzyme 17 GenAtlas ID AK5 Link Image
Enzyme 17 HGNC ID HGNC:365 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 1p31
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Van Rompay AR, Johansson M, Karlsson A: Identification of a novel human adenylate kinase. cDNA cloning, expression analysis, chromosome localization and characterization of the recombinant protein. Eur J Biochem. 1999 Apr;261(2):509-17. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5949
Enzyme 18 Name CTP synthase 1
Enzyme 18 Synonyms
  1. CTP synthetase 1
  2. UTP--ammonia ligase 1
Enzyme 18 Gene Name CTPS
Enzyme 18 Protein Sequence >CTP synthase 1
MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFV
LDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDA
IQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHV
SLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ
VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQPRKMLMKWKEMADRYDRLLETCS
IALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQK
LCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDAN
STEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHRH
RFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPY
FGLLLASVGRLSHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSINHD
Enzyme 18 Number of Residues 591
Enzyme 18 Molecular Weight 66689.9
Enzyme 18 Theoretical pI 6.42
Enzyme 18 GO Classification
Function
  • CTP synthase activity
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
Component
Enzyme 18 General Function Involved in CTP synthase activity
Enzyme 18 Specific Function Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen
Enzyme 18 Pathways
Enzyme 18 Reactions
  • ATP + UTP + NH3 = ADP + phosphate + CTP [RN:R00571]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 30293 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID P17812 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name PYRG1_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1776 bp
ATGAAGTACATTCTGGTTACTGGTGGTGTTATATCAGGAATTGGAAAAGGAATCATTGCC
AGCAGTGTGGGCACAATACTCAAGTCATGTGGTTTACATGTAACTTCAATCAAAATTGAC
CCCTACATTAACATTGATGCAGGAACATTCTCTCCTTATGAGCATGGTGAGGTTTTTGTG
CTGGATGATGGTGGGGAAGTAGACCTTGACCTGGGTAACTATGAGCGGTTCCTTGACATC
CGCCTCACCAAGGACAATAATCTGACCACTGGAAAGATATACCAGTATGTCATTAACAAG
GAACGGAAAGGAGATTACTTGGGGAAAACTGTCCAAGTTGTCCCTCATATCACAGATGCA
ATCCAGGAGTGGGTGATGAGACAGGCGTTAATACCTGTAGATGAAGATGGCCTGGAACCT
CAAGTGTGTGTTATTGAGCTTGGTGGAACCGTGGGGGACATAGAAAGCATGCCCTTTATT
GAGGCCTTCCGTCAGTTCCAATTCAAGGTCAAAAGAGAGAACTTTTGTAACATCCACGTC
AGTCTAGTTCCCCAGCCAAGTTCAACAGGGGAACAGAAGACTAAACCTACCCAGAATAGT
GTTCGGGAACTTAGAGGACTTGGGCTTTCCCCAGATCTGGTTGTATGCAGGTGCTCAAAT
CCACTTGACACATCAGTGAAGGAGAAAATATCAATGTTCTGCCATGTTGAGCCTGAACAA
GTGATCTGTGTCCACGATGTCTCATCCATCTACCGAGTCCCCTTGTTGTTAGAGGAGCAA
GGGGTTGTAGATTATTTTCTTCGAAGACTTGACCTTCCTATTGAGAGGCAGCCAAGAAAA
ATGCTGATGAAATGGAAAGAGATGGCTGACAGATATGATCGCTTGCTGGAGACCTGCTCT
ATTGCCCTTGTGGCGAAATACACCGAGTTCTCAGACTCCTATGCCTCTGTCATTAAGGCT
CTGGAGCATTCTGCACTGGCCATCAACCACAAATTGGAAATCAAGTACATAGATTCTGCG
GACTTGGAGCCCATCACCTCGCAAGAAGAGCCCGTGCGCTACCACGAAGCTTGGCAGAAG
CTCTGTAGTGCTCATGGAGTGCTGGTTCCAGGAGGATTTGGTGTTCGAGGAACAGAAGGA
AAAATCCAAGCAATTGCCTGGGCTCGGAATCAGAAAAAGCCTTTTTTGGGCGTGTGCTTA
GGGATGCAGTTGGCAGTGGTTGAATTCTCAAGAAACGTGCTGGGATGGCAAGATGCCAAT
TCTACAGAGTTTGACCCTACGACCAGTCATCCCGTGGTCGTAGACATGCCAGAACACAAC
CCAGGGCAGATGGGCGGAACCATGAGGCTGGGCAAGAGGAGAACCCTGTTCCAGACCAAG
AACTCAGTCATGAGGAAACTCTATGGAGACGCAGACTACTTGGAAGAGAGGCACCGCCAC
CGATTTGAGGTGAATCCAGTCTGGAAAAAGTGTTTGGAAGAACAAGGCTTGAAGTTTGTT
GGCCAAGATGTTGAAGGAGAGAGAATGGAAATTGTGGAGTTAGAAGATCATCCCTTTTTT
GTTGGGGTTCAGTACCACCCTGAGTTCCTGTCCAGGCCTATCAAGCCCTCCCCACCATAC
TTTGGCCTCCTCCTGGCCTCTGTGGGGCGGCTCTCACATTACCTCCAGAAAGGCTGCAGG
CTCTCACCCAGGGACACCTATAGTGACAGGAGTGGAAGCAGCTCCCCTGACTCTGAAATC
ACCGAACTGAAGTTTCCATCAATAAATCATGACTGA
Enzyme 18 GenBank Gene ID X52142 Link Image
Enzyme 18 GeneCard ID CTPS Link Image
Enzyme 18 GenAtlas ID CTPS Link Image
Enzyme 18 HGNC ID HGNC:2519 Link Image
Enzyme 18 Chromosome Location 1
Enzyme 18 Locus 1p34.1
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Yamauchi M, Yamauchi N, Meuth M: Molecular cloning of the human CTP synthetase gene by functional complementation with purified human metaphase chromosomes. EMBO J. 1990 Jul;9(7):2095-9. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  5. Han GS, Sreenivas A, Choi MG, Chang YF, Martin SS, Baldwin EP, Carman GM: Expression of Human CTP synthetase in Saccharomyces cerevisiae reveals phosphorylation by protein kinase A. J Biol Chem. 2005 Nov 18;280(46):38328-36. Epub 2005 Sep 22. [PubMed Link Image]
  6. Kim JE, Tannenbaum SR, White FM: Global phosphoproteome of HT-29 human colon adenocarcinoma cells. J Proteome Res. 2005 Jul-Aug;4(4):1339-46. [PubMed Link Image]
  7. Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J: Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC. Proteomics. 2005 Sep;5(14):3589-99. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  9. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  10. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  11. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  12. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  13. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  14. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  15. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  16. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5967
Enzyme 19 Name Glutamate dehydrogenase 1, mitochondrial
Enzyme 19 Synonyms
  1. GDH 1
Enzyme 19 Gene Name GLUD1
Enzyme 19 Protein Sequence >Glutamate dehydrogenase 1, mitochondrial
MYRYLGEALLLSRAGPAALGSASADSAALLGWARGQPAAAPQPGLALAARRHYSEAVADR
EDDPNFFKMVEGFFDRGASIVEDKLVEDLRTRESEEQKRNRVRGILRIIKPCNHVLSLSF
PIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFG
GAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREMSWIADTY
ASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFG
DKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILG
FPKAKPYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLER
NIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGK
HGGTIPIVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLDLRTAAYV
NAIEKVFKVYNEAGVTFT
Enzyme 19 Number of Residues 558
Enzyme 19 Molecular Weight 61397.3
Enzyme 19 Theoretical pI 7.91
Enzyme 19 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
  • oxidation reduction
Component
Enzyme 19 General Function Involved in oxidoreductase activity
Enzyme 19 Specific Function May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate
Enzyme 19 Pathways
Enzyme 19 Reactions
  • L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H + H+ [RN:R00243 R00248]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 31707 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID P00367 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name DHE3_HUMAN Link Image
Enzyme 19 PDB ID 1L1F Link Image
Enzyme 19 PDB File Show
Enzyme 19 3D Structure
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1677 bp
ATGTACCGCTACCTGGGCGAAGCGCTGTTGCTGTCCCGGGCCGGGCCCGCTGCCCTGGGC
TCGGCGTCCGCCGACTCGGCCGCGTTGCTGGGCTGGGCCCGGGGACAGCCCGCCGCCGCC
CCGCAGCCGGGGCTGGCATTGGCCGCCCGGCGCCACTACAGCGAGGCGGTGGCCGACCGC
GAGGACGACCCCAACTTCTTCAAGATGGTGGAGGGCTTCTTCGATCGCGGCGCCAGCATC
GTGGAGGACAAGCTGGTGGAGGACCTGAGGACCCGGGAGAGCGAGGAGCAGAAGCGGAAC
CGGGTGCGCGGCATCCTGCGGATCATCAAGCCCTGCAACCATGTGCTGAGTCTCTCCTTC
CCCATCCGGCGCGACGACGGCTCCTGGGAGGTCATCGAAGGCTACCGGGCCCAGCACAGC
CAGCACCGCACGCCCTGCAAGGGAGGTATCCGTTACAGCACTGATGTGAGTGTAGATGAA
GTAAAAGCTTTGGCTTCTCTGATGACATACAAGTGTGCAGTGGTTGATGTGCCGTTTGGG
GGTGCTAAAGCTGGTGTTAAGATCAATCCCAAGAACTATACTGATAATGAATTGGAAAAG
ATCACAAGGAGGTTCACCATGGAGCTAGCAAAAAAGGGCTTTATTGGTCCTGGCATTGAT
GTGCCTGCTCCAGACATGAGCACAGGTGAGCGGGAGATGTCCTGGATCGCTGATACCTAT
GCCAGCACCATAGGGCACTATGATATTAATGCACACGCCTGTGTTACTGGTAAACCCATC
AGCCAAGGGGGAATCCATGGACGCATCTCTGCTACTGGCCGTGGTGTCTTCCATGGGATT
GAAAATTTCATCAATGAAGCTTCTTACATGAGCATTTTAGGAATGACACCAGGGTTTGGA
GATAAAACATTTGTTGTTCAGGGATTTGGTAATGTGGGCCTACACTCTATGAGATATTTA
CATCGTTTTGGTGCTAAATGTATTGCTGTTGGTGAGTCTGATGGGAGTATATGGAATCCA
GATGGTATTGACCCAAAGGAACTGGAAGACTTCAAATTGCAACATGGGTCCATTCTGGGC
TTCCCCAAGGCAAAGCCCTATGAAGGAAGCATCTTGGAGGCCGACTGTGACATACTGATC
CCAGCTGCCAGTGAGAAGCAGTTGACCAAATCCAACGCACCCAGAGTCAAAGCCAAGATC
ATTGCTGAAGGTGCCAATGGGCCAACAACTCCAGAAGCTGACAAGATCTTCCTGGAGAGA
AACATTATGGTTATTCCAGATCTCTACTTGAATGCTGGAGGAGTGACAGTATCTTACTTT
GAGTGGCTGAAGAATCTAAATCATGTCAGCTATGGCCGTTTGACCTTCAAATATGAAAGG
GATTCTAACTACCACTTGCTCATGTCTGTTCAAGAGAGTTTAGAAAGAAAATTTGGAAAG
CATGGTGGAACTATTCCCATTGTACCCACGGCAGAGTTCCAAGACAGGATATCGGGTGCA
TCTGAGAAAGACATCGTGCACTCTGGCTTGGCATACACAATGGAGCGTTCTGCCAGGCAA
ATTATGCGCACAGCCATGAAGTATAACCTGGGATTGGACCTGAGAACAGCTGCCTATGTT
AATGCCATTGAGAAAGTCTTCAAAGTGTACAATGAAGCTGGTGTGACCTTCACATAG
Enzyme 19 GenBank Gene ID X07674 Link Image
Enzyme 19 GeneCard ID GLUD1 Link Image
Enzyme 19 GenAtlas ID GLUD1 Link Image
Enzyme 19 HGNC ID HGNC:4335 Link Image
Enzyme 19 Chromosome Location 1
Enzyme 19 Locus 10q23.3
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Nakatani Y, Banner C, von Herrath M, Schneider ME, Smith HH, Freese E: Comparison of human brain and liver glutamate dehydrogenase cDNAS. Biochem Biophys Res Commun. 1987 Dec 16;149(2):405-10. [PubMed Link Image]
  2. Amuro N, Yamaura M, Goto Y, Okazaki T: Molecular cloning and nucleotide sequence of the cDNA for human liver glutamate dehydrogenase precursor. Biochem Biophys Res Commun. 1988 May 16;152(3):1395-400. [PubMed Link Image]
  3. Nakatani Y, Schneider M, Banner C, Freese E: Complete nucleotide sequence of human glutamate dehydrogenase cDNA. Nucleic Acids Res. 1988 Jul 11;16(13):6237. [PubMed Link Image]
  4. Mavrothalassitis G, Tzimagiorgis G, Mitsialis A, Zannis V, Plaitakis A, Papamatheakis J, Moschonas N: Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family. Proc Natl Acad Sci U S A. 1988 May;85(10):3494-8. [PubMed Link Image]
  5. Michaelidis TM, Tzimagiorgis G, Moschonas NK, Papamatheakis J: The human glutamate dehydrogenase gene family: gene organization and structural characterization. Genomics. 1993 Apr;16(1):150-60. [PubMed Link Image]
  6. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Julliard JH, Smith EL: Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme. J Biol Chem. 1979 May 10;254(9):3427-38. [PubMed Link Image]
  9. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed Link Image]
  10. Banner C, Silverman S, Thomas JW, Lampel KA, Vitkovic L, Huie D, Wenthold RJ: Isolation of a human brain cDNA for glutamate dehydrogenase. J Neurochem. 1987 Jul;49(1):246-52. [PubMed Link Image]
  11. Tzimagiorgis G, Leversha MA, Chroniary K, Goulielmos G, Sargent CA, Ferguson-Smith M, Moschonas NK: Structure and expression analysis of a member of the human glutamate dehydrogenase (GLUD) gene family mapped to chromosome 10p11.2. Hum Genet. 1993 Jun;91(5):433-8. [PubMed Link Image]
  12. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  13. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  14. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  15. Smith TJ, Peterson PE, Schmidt T, Fang J, Stanley CA: Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation. J Mol Biol. 2001 Mar 23;307(2):707-20. [PubMed Link Image]
  16. Fang J, Hsu BY, MacMullen CM, Poncz M, Smith TJ, Stanley CA: Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations. Biochem J. 2002 Apr 1;363(Pt 1):81-7. [PubMed Link Image]
  17. Smith TJ, Schmidt T, Fang J, Wu J, Siuzdak G, Stanley CA: The structure of apo human glutamate dehydrogenase details subunit communication and allostery. J Mol Biol. 2002 May 3;318(3):765-77. [PubMed Link Image]
  18. Banerjee S, Schmidt T, Fang J, Stanley CA, Smith TJ: Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation. Biochemistry. 2003 Apr 1;42(12):3446-56. [PubMed Link Image]
  19. Meissner T, Beinbrech B, Mayatepek E: Congenital hyperinsulinism: molecular basis of a heterogeneous disease. Hum Mutat. 1999;13(5):351-61. [PubMed Link Image]
  20. Stanley CA, Lieu YK, Hsu BY, Burlina AB, Greenberg CR, Hopwood NJ, Perlman K, Rich BH, Zammarchi E, Poncz M: Hyperinsulinism and hyperammonemia in infants with regulatory mutations of the glutamate dehydrogenase gene. N Engl J Med. 1998 May 7;338(19):1352-7. [PubMed Link Image]
  21. Miki Y, Taki T, Ohura T, Kato H, Yanagisawa M, Hayashi Y: Novel missense mutations in the glutamate dehydrogenase gene in the congenital hyperinsulinism-hyperammonemia syndrome. J Pediatr. 2000 Jan;136(1):69-72. [PubMed Link Image]
  22. Santer R, Kinner M, Passarge M, Superti-Furga A, Mayatepek E, Meissner T, Schneppenheim R, Schaub J: Novel missense mutations outside the allosteric domain of glutamate dehydrogenase are prevalent in European patients with the congenital hyperinsulinism-hyperammonemia syndrome. Hum Genet. 2001 Jan;108(1):66-71. [PubMed Link Image]
  23. MacMullen C, Fang J, Hsu BY, Kelly A, de Lonlay-Debeney P, Saudubray JM, Ganguly A, Smith TJ, Stanley CA: Hyperinsulinism/hyperammonemia syndrome in children with regulatory mutations in the inhibitory guanosine triphosphate-binding domain of glutamate dehydrogenase. J Clin Endocrinol Metab. 2001 Apr;86(4):1782-7. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5977
Enzyme 20 Name Adenylate cyclase type 7
Enzyme 20 Synonyms
  1. ATP pyrophosphate-lyase 7
  2. Adenylate cyclase type VII
  3. Adenylyl cyclase 7
Enzyme 20 Gene Name ADCY7
Enzyme 20 Protein Sequence >Adenylate cyclase type 7
MPAKGRYFLNEGEEGPDQDALYEKYQLTSQHGPLLLTLLLVAATACVALIIIAFSQGDPS
RHQAILGMAFLVLAVFAALSVLMYVECLLRRWLRALALLTWACLVALGYVLVFDAWTKAA
CAWEQVPFFLFIVFVVYTLLPFSMRGAVAVGAVSTASHLLVLGSLMGGFTTPSVRVGLQL
LANAVIFLCGNLTGAFHKHQMQDASRDLFTYTVKCIQIRRKLRIEKRQQENLLLSVLPAH
ISMGMKLAIIERLKEHGDRRCMPDNNFHSLYVKRHQNVSILYADIVGFTQLASDCSPKEL
VVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDMCQAIKQ
VREATGVDINMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEAT
LKHLDKAYEVEDGHGQQRDPYLKEMNIRTYLVIDPRSQQPPPPSQHLPRPKGDAALKMRA
SVRMTRYLESWGAARPFAHLNHRESVSSGETHVPNGRRPKSVPQRHRRTPDRSMSPKGRS
EDDSYDDEMLSAIEGLSSTRPCCSKSDDFYTFGSIFLEKGFEREYRLAPIPRARHDFACA
SLIFVCILLVHVLLMPRTAALGVSFGLVACVLGLVLGLCFATKFSRCCPARGTLCTISER
VETQPLLRLTLAVLTIGSLLTVAIINLPLMPFQVPELPVGNETGLLAASSKTRALCEPLP
YYTCSCVLGFIACSVFLRMSLEPKVVLLTVALVAYLVLFNLSPCWQWDCCGQGLGNLTKP
NGTTSGTPSCSWKDLKTMTNFYLVLFYITLLTLSRQIDYYCRLDCLWKKKFKKEHEEFET
MENVNRLLLENVLPAHVAAHFIGDKLNEDWYHQSYDCVCVMFASVPDFKVFYTECDVNKE
GLECLRLLNEIIADFDELLLKPKFSGVEKIKTIGSTYMAAAGLSVASGHENQELERQHAH
IGVMVEFSIALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVAS
RMESTGELGKIQVTEETCTILQGLGYSCECRGLINVKGKGELRTYFVCTDTAKFQGLGLN
Enzyme 20 Number of Residues 1080
Enzyme 20 Molecular Weight 120307.2
Enzyme 20 Theoretical pI 8.16
Enzyme 20 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 20 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 20 Specific Function This is a membrane-bound, calcium-inhibitable adenylyl cyclase
Enzyme 20 Pathways
Enzyme 20 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • 34-54 63-83 95-117 122-142 147-167 176-196 595-615 620-640 669-688 718-737 746-773 794-814
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 116496681 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P51828 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name ADCY7_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >3243 bp
ATGCCAGCCAAGGGGCGCTACTTCCTCAACGAGGGCGAGGAGGGCCCTGACCAAGATGCG
CTCTACGAGAAGTACCAGCTCACCAGCCAGCATGGGCCGCTGCTGCTCACGCTCCTGCTG
GTGGCCGCCACTGCCTGCGTGGCCCTCATCATCATTGCCTTCAGCCAGGGGGACCCCTCC
AGACACCAGGCCATTCTGGGCATGGCGTTCCTGGTGCTGGCGGTGTTTGCGGCCCTCTCT
GTGCTGATGTACGTCGAGTGTCTCCTGCGGCGCTGGCTCAGGGCCTTGGCGCTGCTCACC
TGGGCCTGCTTGGTGGCGCTGGGCTATGTGCTGGTGTTCGACGCATGGACAAAGGCGGCC
TGTGCGTGGGAGCAGGTGCCCTTCTTCCTGTTCATTGTCTTCGTGGTGTACACACTACTG
CCCTTCAGCATGCGGGGCGCTGTCGCCGTTGGGGCCGTCTCCACTGCCTCCCACCTCCTG
GTGCTCGGTTCTTTGATGGGAGGCTTCACGACACCCAGTGTCCGGGTGGGGCTGCAGCTG
CTGGCCAACGCAGTCATCTTCCTGTGTGGGAACCTGACAGGCGCCTTCCACAAGCACCAA
ATGCAGGATGCGTCCCGGGACCTCTTCACCTACACTGTGAAGTGCATCCAGATCCGCCGG
AAGCTGCGCATCGAGAAGCGCCAGCAGGAGAACCTGCTGCTGTCAGTGCTTCCGGCCCAC
ATCTCCATGGGCATGAAGCTGGCCATCATCGAACGGCTCAAGGAGCATGGTGACCGTCGC
TGCATGCCTGACAACAACTTCCACAGCCTCTACGTCAAGAGGCACCAGAATGTCAGCATC
CTCTATGCGGACATCGTGGGCTTCACGCAGCTGGCCAGCGACTGTTCTCCCAAGGAGCTG
GTGGTGGTGCTGAATGAGCTCTTTGGCAAGTTCGACCAGATCGCCAAGGCCAACGAGTGC
ATGCGAATCAAGATCCTCGGCGACTGCTACTACTGTGTATCGGGCCTGCCCGTGTCGCTG
CCTACCCACGCCCGGAACTGCGTGAAGATGGGGCTGGACATGTGCCAGGCCATCAAGCAG
GTGCGGGAGGCCACGGGCGTGGACATCAACATGCGTGTGGGCATACACTCGGGGAATGTG
CTGTGCGGGGTCATCGGGCTGCGCAAGTGGCAGTATGACGTGTGGTCCCACGACGTGTCC
CTGGCCAACCGGATGGAGGCAGCCGGAGTACCCGGCCGGGTGCACATCACGGAGGCCACG
CTAAAGCACCTGGACAAGGCGTACGAGGTGGAGGATGGGCACGGGCAGCAGCGGGACCCC
TACCTCAAGGAGATGAACATCCGCACCTACCTGGTCATCGACCCCCGGAGCCAGCAGCCA
CCCCCGCCCAGCCAACACCTCCCCAGGCCCAAGGGGGACGCGGCCCTGAAGATGCGGGCG
TCAGTGCGCATGACCCGGTACCTCGAGTCCTGGGGGGCGGCACGGCCCTTTGCACATCTC
AACCACCGTGAGAGCGTGAGCAGTGGTGAGACCCACGTCCCCAACGGGCGGAGGCCTAAG
AGCGTTCCCCAGCGCCACCGCCGGACCCCAGACAGAAGCATGTCCCCCAAGGGGCGGTCG
GAGGATGACTCGTACGATGACGAGATGCTGTCAGCCATTGAGGGGCTCAGCTCCACGAGG
CCCTGCTGCTCCAAGTCCGATGACTTCTACACCTTTGGGTCCATCTTCCTGGAGAAGGGC
TTTGAGCGCGAGTACCGCCTGGCACCCATCCCCCGGGCCCGCCACGACTTTGCCTGCGCC
AGCCTGATCTTCGTCTGCATCCTGCTCGTCCATGTCCTGCTCATGCCCAGGACGGCGGCA
CTGGGTGTGTCCTTCGGGCTGGTGGCCTGTGTACTGGGGCTGGTGCTGGGCCTGTGCTTT
GCCACCAAGTTCTCGAGGTGCTGCCCAGCTCGGGGGACGCTCTGCACTATCTCTGAGAGG
GTGGAGACACAGCCCCTGCTGAGGCTGACCCTGGCCGTCCTGACCATCGGCAGCCTGCTC
ACTGTGGCCATCATCAACCTGCCCCTGATGCCTTTCCAAGTTCCAGAGCTGCCTGTTGGC
AATGAGACAGGCCTACTGGCCGCGAGCAGCAAGACAAGAGCCCTGTGTGAGCCCCTCCCG
TACTACACCTGCAGCTGTGTCCTGGGCTTCATCGCCTGCTCGGTCTTCCTGAGGATGAGC
CTGGAGCCAAAGGTTGTGCTGCTGACAGTGGCCCTGGTGGCCTACCTGGTGCTCTTCAAC
CTCTCCCCATGCTGGCAGTGGGACTGCTGCGGCCAAGGCCTGGGCAACCTCACCAAGCCC
AACGGCACCACCAGTGGCACCCCTAGCTGTTCCTGGAAGGACCTGAAGACCATGACCAAT
TTCTACCTGGTCCTGTTCTACATCACCCTGCTTACACTCTCCAGACAGATTGACTATTAC
TGCCGCTTGGACTGCCTATGGAAGAAGAAGTTCAAGAAGGAGCACGAGGAGTTTGAGACC
ATGGAGAACGTGAACCGCCTTCTTCTGGAGAACGTCCTGCCAGCCCACGTGGCTGCCCAC
TTTATCGGTGACAAGTTAAACGAGGACTGGTACCATCAGTCCTATGACTGCGTCTGTGTC
ATGTTTGCCTCCGTGCCGGACTTCAAAGTGTTCTACACAGAGTGCGATGTCAACAAAGAA
GGGCTGGAGTGCCTACGCCTGCTCAATGAGATCATTGCCGACTTCGACGAGCTCCTACTG
AAGCCCAAGTTCAGCGGCGTGGAGAAGATCAAGACCATCGGCAGCACGTACATGGCAGCT
GCAGGGCTCAGCGTCGCCTCAGGGCACGAGAACCAGGAGCTGGAGCGGCAGCATGCCCAC
ATTGGTGTCATGGTGGAGTTCAGCATCGCCCTGATGAGTAAGCTGGACGGCATCAACAGG
CACTCCTTCAACTCCTTCCGCCTCCGCGTCGGCATAAACCATGGGCCTGTGATTGCTGGA
GTGATTGGGGCCCGAAAACCTCAGTATGACATCTGGGGAAACACTGTCAATGTGGCCAGC
CGAATGGAAAGCACTGGAGAACTTGGGAAAATCCAGGTTACCGAGGAGACCTGCACCATC
CTCCAGGGCCTCGGGTACTCTTGTGAATGCCGTGGCCTGATCAACGTCAAAGGCAAAGGC
GAGCTGAGGACTTACTTTGTCTGTACGGACACTGCCAAGTTTCAGGGGCTGGGGCTGAAC
TGA
Enzyme 20 GenBank Gene ID BC126271 Link Image
Enzyme 20 GeneCard ID ADCY7 Link Image
Enzyme 20 GenAtlas ID ADCY7 Link Image
Enzyme 20 HGNC ID HGNC:238 Link Image
Enzyme 20 Chromosome Location 1
Enzyme 20 Locus 16q12.1
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5978
Enzyme 21 Name Adenylate cyclase type 4
Enzyme 21 Synonyms
  1. ATP pyrophosphate-lyase 4
  2. Adenylate cyclase type IV
  3. Adenylyl cyclase 4
Enzyme 21 Gene Name ADCY4
Enzyme 21 Protein Sequence >Adenylate cyclase type 4
MARLFSPRPPPSEDLFYETYYSLSQQYPLLLLLLGIVLCALAALLAVAWASGRELTSDPS
FLTTVLCALGGFSLLLGLASREQRLQRWTRPLSGLVWVALLALGHAFLFTGGVVSAWDQV
SYFLFVIFTAYAMLPLGMRDAAVAGLASSLSHLLVLGLYLGPQPDSRPALLPQLAANAVL
FLCGNVAGVYHKALMERALRATFREALSSLHSRRRLDTEKKHQEHLLLSILPAYLAREMK
AEIMARLQAGQGSRPESTNNFHSLYVKRHQGVSVLYADIVGFTRLASECSPKELVLMLNE
LFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRAIRKLRAATG
VDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAG
AYAVEDAGMEHRDPYLRELGEPTYLVIDPRAEEEDEKGTAGGLLSSLEGLKMRPSLLMTR
YLESWGAAKPFAHLSHGDSPVSTSTPLPEKTLASFSTQWSLDRSRTPRGLDDELDTGDAK
FFQVIEQLNSQKQWKQSKDFNPLTLYFREKEMEKEYRLSAIPAFKYYEACTFLVFLSNFI
IQMLVTNRPPALAITYSITFLLFLLILFVCFSEDLMRCVLKGPKMLHWLPALSGLVATRP
GLRIALGTATILLVFAMAITSLFFFPTSSDCPFQAPNVSSMISNLSWELPGSLPLISVPY
SMHCCTLGFLSCSLFLHMSFELKLLLLLLWLAASCSLFLHSHAWLSECLIVRLYLGPLDS
RPGVLKEPKLMGAISFFIFFFTLLVLARQNEYYCRLDFLWKKKLRQEREETETMENLTRL
LLENVLPAHVAPQFIGQNRRNEDLYHQSYECVCVLFASVPDFKEFYSESNINHEGLECLR
LLNEIIADFDELLSKPKFSGVEKIKTIGSTYMAATGLNATSGQDAQQDAERSCSHLGTMV
EFAVALGSKLDVINKHSFNNFRLRVGLNHGPVVAGVIGAQKPQYDIWGNTVNVASRMEST
GVLGKIQVTEETAWALQSLGYTCYSRGVIKVKGKGQLCTYFLNTDLTRTGPPSATLG
Enzyme 21 Number of Residues 1077
Enzyme 21 Molecular Weight 119792.9
Enzyme 21 Theoretical pI 7.50
Enzyme 21 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 21 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 21 Specific Function This is a membrane-bound, calmodulin-insensitive adenylyl cyclase
Enzyme 21 Pathways
Enzyme 21 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • 29-50 61-80 94-117 120-138 141-162 170-190 586-607 611-633 664-687 715-736 744-764 791-807
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 22212709 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q8NFM4 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name ADCY4_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >3234 bp
ATGGCCCGCCTCTTCAGCCCCCGGCCGCCCCCCAGCGAAGACCTCTTCTACGAGACCTAC
TACAGCCTGAGCCAGCAGTACCCGCTGCTGCTGCTGCTGCTGGGGATCGTGCTCTGTGCG
CTCGCGGCGCTGCTCGCAGTGGCCTGGGCCAGCGGCAGGGAGCTGACCTCAGACCCGAGC
TTCCTGACCACTGTGCTGTGCGCGCTGGGCGGCTTCTCGCTGCTGCTGGGCCTCGCTTCC
CGGGAGCAGCGACTGCAGCGCTGGACGCGTCCCCTGTCCGGCTTGGTATGGGTCGCGCTG
CTAGCGCTAGGCCACGCCTTCCTGTTCACCGGGGGCGTGGTGAGCGCCTGGGACCAGGTG
TCCTATTTTCTCTTCGTCATCTTCACGGCGTATGCCATGCTGCCCTTGGGCATGCGGGAC
GCCGCCGTCGCGGGCCTCGCCTCCTCACTCTCGCATCTGCTGGTCCTCGGGCTGTATCTT
GGGCCACAGCCGGACTCACGGCCTGCACTGCTGCCGCAGTTGGCAGCAAACGCAGTGCTG
TTCCTGTGCGGGAACGTGGCAGGAGTGTACCACAAGGCGCTGATGGAGCGCGCCCTGCGG
GCCACGTTCCGGGAGGCACTCAGCTCCCTGCACTCACGCCGGCGGCTGGACACCGAGAAG
AAGCACCAGGAACACCTTCTCTTGTCCATCCTTCCTGCCTACCTGGCCCGAGAGATGAAG
GCAGAGATCATGGCACGGCTGCAGGCAGGACAGGGGTCACGGCCAGAGAGCACTAACAAT
TTCCACAGCCTCTATGTCAAGAGGCACCAGGGAGTCAGCGTGCTGTATGCTGACATCGTG
GGCTTCACGCGGCTGGCCAGCGAGTGTTCCCCTAAGGAGCTGGTGCTCATGCTCAATGAG
CTCTTTGGCAAGTTCGACCAGATTGCCAAGGAGCATGAATGCATGCGGATCAAGATCCTG
GGGGACTGTTACTACTGTGTCTCTGGGCTGCCACTCTCACTGCCAGACCATGCCATCAAC
TGCGTGCGCATGGGCCTGGACATGTGCCGGGCCATCAGGAAACTGCGGGCAGCCACTGGC
GTGGACATCAACATGCGTGTGGGCGTGCACTCAGGCAGCGTACTGTGTGGAGTCATCGGG
CTGCAGAAGTGGCAGTACGACGTTTGGTCACATGATGTCACACTGGCTAACCACATGGAG
GCAGGCGGTGTACCAGGGCGAGTGCACATCACAGGGGCTACCCTGGCCCTGCTGGCAGGG
GCTTATGCTGTGGAGGACGCAGGCATGGAGCATCGGGACCCCTACCTTCGGGAGCTAGGG
GAGCCTACCTATCTGGTCATCGATCCACGGGCAGAGGAGGAGGATGAGAAGGGCACTGCA
GGAGGCTTGCTGTCCTCGCTTGAGGGCCTCAAGATGCGTCCATCACTGCTGATGACCCGT
TACCTGGAGTCCTGGGGCGCAGCCAAGCCTTTTGCCCACCTGAGCCACGGAGACAGCCCT
GTGTCCACCTCCACCCCTCTCCCGGAGAAGACCCTGGCTTCCTTCAGCACCCAGTGGAGC
CTGGATCGGAGCCGTACCCCCCGGGGACTAGATGATGAACTGGACACCGGGGATGCCAAG
TTCTTCCAGGTCATTGAGCAGCTCAACTCGCAGAAACAGTGGAAGCAGTCGAAGGACTTC
AACCCACTGACACTGTACTTCAGAGAGAAGGAGATGGAGAAAGAGTACCGACTCTCTGCA
ATCCCCGCCTTCAAATACTATGAAGCCTGCACCTTCCTGGTTTTTCTCTCCAACTTCATC
ATCCAGATGCTAGTGACAAACAGGCCCCCAGCTCTGGCCATCACGTATAGCATCACCTTC
CTCCTCTTCCTCCTCATCCTTTTTGTCTGCTTCTCAGAGGACCTGATGAGGTGTGTCCTG
AAAGGCCCCAAGATGCTGCACTGGCTGCCTGCACTGTCTGGCCTGGTGGCCACACGACCA
GGACTGAGAATAGCCTTGGGCACCGCCACCATCCTCCTTGTCTTTGCCATGGCCATTACC
AGCCTGTTCTTCTTCCCAACATCATCAGACTGCCCTTTCCAAGCTCCCAATGTGTCCTCC
ATGATTTCCAACCTCTCCTGGGAGCTCCCTGGGTCTCTGCCTCTCATCAGTGTCCCATAC
TCCATGCACTGCTGCACGCTGGGCTTCCTCTCCTGCTCCCTCTTTCTGCACATGAGCTTC
GAGCTGAAGCTGCTGCTGCTCCTGCTGTGGCTGGCGGCATCCTGCTCCCTCTTCCTGCAC
TCCCATGCCTGGCTGTCGGAATGCCTCATCGTCCGCCTCTATCTGGGCCCCTTGGACTCC
AGGCCCGGAGTGCTGAAGGAGCCCAAACTGATGGGTGCTATCTCCTTCTTCATCTTCTTC
TTCACCCTCCTTGTCCTGGCTCGCCAGAATGAGTACTACTGCCGCCTGGACTTCCTGTGG
AAGAAGAAGCTGAGGCAGGAGAGGGAGGAGACAGAGACGATGGAGAACCTGACTCGGCTG
CTCTTGGAGAACGTGCTCCCTGCACACGTGGCCCCCCAGTTCATTGGCCAGAACCGGCGC
AACGAGGATCTCTACCACCAGTCCTATGAATGCGTTTGTGTCCTCTTCGCCTCAGTCCCA
GACTTCAAGGAGTTCTACTCTGAATCCAACATCAATCATGAGGGCCTAGAGTGTCTGAGG
CTGCTCAATGAGATAATTGCTGATTTTGATGAGCTGCTCTCCAAGCCCAAGTTCAGTGGG
GTGGAGAAGATCAAGACCATCGGCAGCACCTACATGGCAGCCACAGGCTTAAATGCCACC
TCTGGACAGGATGCACAACAGGATGCTGAACGGAGCTGCAGCCACCTTGGCACTATGGTG
GAATTTGCCGTGGCCCTGGGGTCTAAGCTGGACGTCATCAACAAGCATTCATTCAACAAC
TTCCGCCTGCGAGTGGGGTTGAACCATGGACCCGTAGTAGCTGGAGTTATTGGGGCCCAG
AAGCCGCAATATGACATTTGGGGCAACACAGTGAACGTGGCCAGCCGCATGGAGAGTACA
GGAGTCCTTGGCAAAATCCAAGTGACTGAGGAGACAGCATGGGCCCTACAGTCCCTGGGC
TACACCTGCTACAGCCGGGGTGTCATCAAGGTGAAAGGCAAAGGGCAGCTCTGCACCTAC
TTCCTGAACACAGACTTGACACGAACTGGACCTCCTTCAGCTACCCTAGGCTGA
Enzyme 21 GenBank Gene ID AF497516 Link Image
Enzyme 21 GeneCard ID ADCY4 Link Image
Enzyme 21 GenAtlas ID ADCY4 Link Image
Enzyme 21 HGNC ID HGNC:235 Link Image
Enzyme 21 Chromosome Location 1
Enzyme 21 Locus 14q12
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Ludwig MG, Seuwen K: Characterization of the human adenylyl cyclase gene family: cDNA, gene structure, and tissue distribution of the nine isoforms. J Recept Signal Transduct Res. 2002 Feb-Nov;22(1-4):79-110. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5979
Enzyme 22 Name Adenylate cyclase type 6
Enzyme 22 Synonyms
  1. ATP pyrophosphate-lyase 6
  2. Adenylate cyclase type VI
  3. Adenylyl cyclase 6
  4. Ca(2+)-inhibitable adenylyl cyclase
Enzyme 22 Gene Name ADCY6
Enzyme 22 Protein Sequence >Adenylate cyclase type 6
MSWFSGLLVPKVDERKTAWGERNGQKRSRRRGTRAGGFCTPRYMSCLRDAEPPSPTPAGP
PRCPWQDDAFIRRGGPGKGKELGLRAVALGFEDTEVTTTAGGTAEVAPDAVPRSGRSCWR
RLVQVFQSKQFRSAKLERLYQRYFFQMNQSSLTLLMAVLVLLTAVLLAFHAAPARPQPAY
VALLACAAALFVGLMVVCNRHSFRQDSMWVVSYVVLGILAAVQVGGALAADPRSPSAGLW
CPVFFVYIAYTLLPIRMRAAVLSGLGLSTLHLILAWQLNRGDAFLWKQLGANVLLFLCTN
VIGICTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINT
KKEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHC
LRIKILGDCYYCVSGLPEARADHAHCCVEMGVDMIEAISLVREVTGVNVNMRVGIHSGRV
HCGVLGLRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYLNGDYEVEPGRGGERNA
YLKEQHIETFLILGASQKRKEEKAMLAKLQRTRANSMEGLMPRWVPDRAFSRTKDSKAFR
QMGIDDSSKDNRGTQDALNPEDEVDEFLSRAIDARSIDQLRKDHVRRFLLTFQREDLEKK
YSRKVDPRFGAYVACALLVFCFICFIQLLIFPHSTLMLGIYASIFLLLLITVLICAVYSC
GSLFPKALQRLSRSIVRSRAHSTAVGIFSVLLVFTSAIANMFTCNHTPIRSCAARMLNLT
PADITACHLQQLNYSLGLDAPLCEGTMPTCSFPEYFIGNMLLSLLASSVFLHISSIGKLA
MIFVLGLIYLVLLLLGPPATIFDNYDLLLGVHGLASSNETFDGLDCPAAGRVALKYMTPV
ILLVFALALYLHAQQVESTARLDFLWKLQATGEKEEMEELQAYNRRLLHNILPKDVAAHF
LARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIIS
EERFRQLEKIKTIGSTYMAASGLNASTYDQVGRSHITALADYAMRLMEQMKHINEHSFNN
FQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQVLAAKG
YQLECRGVVKVKGKGEMTTYFLNGGPSS
Enzyme 22 Number of Residues 1168
Enzyme 22 Molecular Weight 130614.1
Enzyme 22 Theoretical pI 8.27
Enzyme 22 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 22 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 22 Specific Function Membrane-bound, calcium-inhibitable adenylyl cyclase
Enzyme 22 Pathways
Enzyme 22 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • 152-168 181-197 214-230 239-255 259-275 289-305 674-691 702-718 743-759 820-836 839-855 897-913
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein Not Available
Enzyme 22 UniProtKB/Swiss-Prot ID O43306 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name ADCY6_HUMAN Link Image
Enzyme 22 PDB ID 1U0H Link Image
Enzyme 22 PDB File Show
Enzyme 22 3D Structure
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >3507 bp
ATGTCATGGTTTAGTGGCCTCCTGGTCCCTAAAGTGGATGAACGGAAAACAGCCTGGGGC
GAACGCAATGGGCAGAAGCGTTCGCGGCGCCGTGGCACTCGGGCAGGTGGCTTCTGCACG
CCCCGCTATATGAGCTGCCTCCGGGATGCAGAGCCACCCAGCCCCACCCCTGCCGGCCCC
CCTCGGTGCCCCTGGCAGGATGACGCCTTCATCCGGAGGGGCGGCCCAGGCAAGGGCAAG
GAGCTGGGGCTGCGGGCAGTGGCCCTGGGCTTCGAGGATACCGAGGTGACAACGACAGCG
GGCGGGACGGCTGAGGTGGCGCCCGACGCGGTGCCCAGGAGTGGGCGATCCTGCTGGCGC
CGTCTGGTGCAGGTGTTCCAGTCGAAGCAGTTCCGTTCGGCCAAGCTGGAGCGCCTGTAC
CAGCGGTACTTCTTCCAGATGAACCAGAGCAGCCTGACGCTGCTGATGGCGGTGCTGGTG
CTGCTCACAGCGGTGCTGCTGGCTTTCCACGCCGCACCCGCCCGCCCTCAGCCTGCCTAT
GTGGCACTGTTGGCCTGTGCCGCCGCCCTGTTCGTGGGGCTCATGGTGGTGTGTAACCGG
CATAGCTTCCGCCAGGACTCCATGTGGGTGGTGAGCTACGTGGTGCTGGGCATCCTGGCG
GCAGTGCAGGTCGGGGGCGCTCTCGCAGCAGACCCGCGCAGCCCCTCTGCGGGCCTCTGG
TGCCCTGTGTTCTTTGTCTACATCGCCTACACGCTCCTCCCCATCCGCATGCGGGCTGCC
GTCCTCAGCGGCCTGGGCCTCTCCACCTTGCATTTGATCTTGGCCTGGCAACTTAACCGT
GGTGATGCCTTCCTCTGGAAGCAGCTCGGTGCCAATGTGCTGCTGTTCCTCTGCACCAAC
GTCATTGGCATCTGCACACACTATCCAGCAGAGGTGTCTCAGCGCCAGGCCTTTCAGGAG
ACCCGCGGTTACATCCAGGCCCGGCTCCACCTGCAGCATGAGAATCGGCAGCAGGAGCGG
CTGCTGCTGTCGGTATTGCCCCAGCACGTTGCCATGGAGATGAAAGAAGACATCAACACA
AAAAAAGAAGACATGATGTTCCACAAGATCTACATACAGAAGCATGACAATGTCAGCATC
CTGTTTGCAGACATTGAGGGCTTCACCAGCCTGGCATCCCAGTGCACTGCGCAGGAGCTG
GTCATGACCCTGAATGAGCTCTTTGCCCGGTTTGACAAGCTGGCTGCGGAGAATCACTGC
CTGAGGATCAAGATCTTGGGGGACTGTTACTACTGTGTGTCAGGGCTGCCGGAGGCCCGG
GCCGACCATGCCCACTGCTGTGTGGAGATGGGGGTAGACATGATTGAGGCCATCTCGCTG
GTACGTGAGGTGACAGGTGTGAATGTGAACATGCGCGTGGGCATCCACAGCGGGCGCGTG
CACTGCGGCGTCCTTGGCTTGCGGAAATGGCAGTTCGATGTGTGGTCCAATGATGTGACC
CTGGCCAACCACATGGAGGCAGGAGGCCGGGCTGGCCGCATCCACATCACTCGGGCAACA
CTGCAGTACCTGAACGGGGACTACGAGGTGGAGCCAGGCCGTGGTGGCGAGCGCAACGCG
TACCTCAAGGAGCAGCACATTGAGACTTTCCTCATCCTGGGCGCCAGCCAGAAACGGAAA
GAGGAGAAGGCCATGCTGGCCAAGCTGCAGCGGACTCGGGCCAACTCCATGGAAGGGCTG
ATGCCGCGCTGGGTTCCTGATCGTGCCTTCTCCCGGACCAAGGACTCCAAGGCCTTCCGC
CAGATGGGCATTGATGATTCCAGCAAAGACAACCGGGGCACCCAAGATGCCCTGAACCCT
GAGGATGAGGTGGATGAGTTCCTGAGCCGTGCCATCGATGCCCGCAGCATTGATCAGCTG
CGGAAGGACCATGTGCGCCGGTTTCTGCTCACCTTCCAGAGAGAGGATCTTGAGAAGAAG
TACTCCCGGAAGGTGGATCCCCGCTTCGGAGCCTACGTTGCCTGTGCCCTGTTGGTCTTC
TGCTTCATCTGCTTCATCCAGCTTCTCATCTTCCCACACTCCACCCTGATGCTTGGGATC
TATGCCAGCATCTTCCTGCTGCTGCTAATCACCGTGCTGATCTGTGCTGTGTACTCCTGT
GGTTCTCTGTTCCCTAAGGCCCTGCAACGTCTGTCCCGCAGCATTGTCCGCTCACGGGCA
CATAGCACCGCAGTTGGCATCTTTTCCGTCCTGCTTGTGTTTACTTCTGCCATTGCCAAC
ATGTTCACCTGTAACCACACCCCCATACGGAGCTGTGCAGCCCGGATGCTGAATTTAACA
CCTGCTGACATCACTGCCTGCCACCTGCAGCAGCTCAATTACTCTCTGGGCCTGGATGCT
CCCCTGTGTGAGGGCACCATGCCCACCTGCAGCTTTCCTGAGTACTTCATCGGGAACATG
CTGCTGAGTCTCTTGGCCAGCTCTGTCTTCCTGCACATCAGCAGCATCGGGAAGTTGGCC
ATGATCTTTGTCTTGGGGCTCATCTATTTGGTGCTGCTTCTGCTGGGTCCCCCAGCCACC
ATCTTTGACAACTATGACCTACTGCTTGGCGTCCATGGCTTGGCTTCTTCCAATGAGACC
TTTGATGGGCTGGACTGTCCAGCTGCAGGGAGGGTGGCCCTCAAATATATGACCCCTGTG
ATTCTGCTGGTGTTTGCGCTGGCGCTGTATCTGCATGCTCAGCAGGTGGAGTCGACTGCC
CGCCTAGACTTCCTCTGGAAACTACAGGCAACAGGGGAGAAGGAGGAGATGGAGGAGCTA
CAGGCATACAACCGGAGGCTGCTGCATAACATTCTGCCCAAGGACGTGGCGGCCCACTTC
CTGGCCCGGGAGCGCCGCAATGATGAACTCTACTATCAGTCGTGTGAGTGTGTGGCTGTT
ATGTTTGCCTCCATTGCCAACTTCTCTGAGTTCTATGTGGAGCTGGAGGCAAACAATGAG
GGTGTCGAGTGCCTGCGGCTGCTCAACGAGATCATCGCTGACTTTGATGAGATTATCAGC
GAGGAGCGGTTCCGGCAGCTGGAAAAGATCAAGACGATTGGTAGCACCTACATGGCTGCC
TCAGGGCTGAACGCCAGCACCTACGATCAGGTGGGCCGCTCCCACATCACTGCCCTGGCT
GACTACGCCATGCGGCTCATGGAGCAGATGAAGCACATCAATGAGCACTCCTTCAACAAT
TTCCAGATGAAGATTGGGCTGAACATGGGCCCAGTCGTGGCAGGTGTCATCGGGGCTCGG
AAGCCACAGTATGACATCTGGGGGAACACAGTGAATGTCTCTAGTCGTATGGACAGCACG
GGGGTCCCCGACCGAATCCAGGTGACCACGGACCTGTACCAGGTTCTAGCTGCCAAGGGC
TACCAGCTGGAGTGTCGAGGGGTGGTCAAGGTGAAGGGCAAGGGGGAGATGACCACCTAC
TTCCTCAATGGGGGCCCCAGCAGTTAA
Enzyme 22 GenBank Gene ID AF250226 Link Image
Enzyme 22 GeneCard ID ADCY6 Link Image
Enzyme 22 GenAtlas ID ADCY6 Link Image
Enzyme 22 HGNC ID HGNC:237 Link Image
Enzyme 22 Chromosome Location 1
Enzyme 22 Locus 12q12-q13
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Wicker R, Catalan AG, Cailleux A, Starenki D, Stengel D, Sarasin A, Suarez HG: Cloning and expression of human adenylyl cyclase type VI in normal thyroid tissues. Biochim Biophys Acta. 2000 Sep 7;1493(1-2):279-83. [PubMed Link Image]
  2. Ishikawa K, Nagase T, Nakajima D, Seki N, Ohira M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1997 Oct 31;4(5):307-13. [PubMed Link Image]
  3. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Hellevuo K, Yoshimura M, Kao M, Hoffman PL, Cooper DM, Tabakoff B: A novel adenylyl cyclase sequence cloned from the human erythroleukemia cell line. Biochem Biophys Res Commun. 1993 Apr 15;192(1):311-8. [PubMed Link Image]
  6. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  7. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5980
Enzyme 23 Name Adenylate cyclase type 5
Enzyme 23 Synonyms
  1. ATP pyrophosphate-lyase 5
  2. Adenylate cyclase type V
  3. Adenylyl cyclase 5
Enzyme 23 Gene Name ADCY5
Enzyme 23 Protein Sequence >Adenylate cyclase type 5
MSGSKSVSPPGYAAQKTAAPAPRGGPEHRSAWGEADSRANGYPHAPGGSARGSTKKPGGA
VTPQQQQRLASRWRSDDDDDPPLSGDDPLAGGFGFSFRSKSAWQERGGDDCGRGSRRQRR
GAASGGSTRAPPAGGGGGSAAAAASAGGTEVRPRSVEVGLEERRGKGRAADELEAGAVEG
GEGSGDGGSSADSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQS
SLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGL
ACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSAL
HLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLH
SQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTS
LASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEM
GMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGK
AGRIHITKATLNYLNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAKMN
RQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFL
GRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQI
TIVPHSIFMLSFYLTCSLLLTLVVFVSVIYSCVKLFPSPLQTLSRKIVRSKMNSTLVGVF
TITLVFLAAFVNMFTCNSRDLLGCLAQEHNISASQVNACHVAESAVNYSLGDEQGFCGSP
WPNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIELIYVLIVEVPGVTLFDNADL
LVTANAIDFFNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKL
QATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANF
SEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTY
DKVGKTHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWG
NTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPL
S
Enzyme 23 Number of Residues 1261
Enzyme 23 Molecular Weight 138906.4
Enzyme 23 Theoretical pI 7.25
Enzyme 23 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 23 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 23 Specific Function This is a membrane-bound, calcium-inhibitable adenylyl cyclase
Enzyme 23 Pathways
Enzyme 23 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • 196-216 242-262 268-288 299-319 325-345 374-394 770-790 792-812 836-856 910-930 935-955 984-1004
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 34486092 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID O95622 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name ADCY5_HUMAN Link Image
Enzyme 23 PDB ID 1U0H Link Image
Enzyme 23 PDB File Show
Enzyme 23 3D Structure
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >3786 bp
ATGTCCGGCTCCAAAAGCGTGAGCCCCCCGGGCTACGCGGCGCAGAAGACTGCGGCGCCG
GCGCCCCGGGGAGGCCCCGAACACCGCTCTGCGTGGGGCGAGGCCGATTCCCGCGCGAAT
GGCTACCCCCATGCCCCCGGGGGCTCTGCCCGCGGCTCCACCAAGAAACCCGGGGGGGCG
GTGACCCCGCAGCAGCAGCAGCGCCTGGCCAGCCGCTGGCGCAGCGACGACGACGACGAT
CCTCCGCTGAGCGGTGACGACCCCCTGGCCGGGGGCTTCGGCTTCAGCTTCCGCTCCAAG
TCCGCCTGGCAGGAGCGCGGCGGCGACGACTGCGGTCGCGGCAGCCGCCGGCAGCGGCGG
GGCGCGGCCAGCGGGGGCAGCACCCGGGCGCCCCCTGCGGGCGGCGGCGGCGGCTCGGCG
GCGGCGGCTGCCTCGGCGGGCGGGACGGAGGTGCGCCCTCGCTCGGTGGAGGTGGGTCTG
GAGGAGCGGCGGGGCAAGGGGCGCGCGGCCGACGAGCTGGAGGCCGGCGCCGTCGAGGGC
GGCGAGGGGTCCGGGGATGGCGGCAGCTCGGCGGACTCGGGCTCGGGCGCGGGGCCCGGC
GCGGTGCTGTCCCTGGGCGCCTGCTGCCTGGCGTTGCTGCAGATATTCCGCTCCAAGAAG
TTCCCGTCGGACAAACTGGAGCGGCTGTACCAGCGCTACTTCTTCCGCCTGAACCAGAGC
AGCCTCACCATGCTCATGGCCGTGCTGGTGCTCGTGTGCCTGGTCATGTTGGCCTTCCAC
GCGGCGCGGCCCCCGCTCCAGCTGCCCTACCTGGCCGTGCTGGCGGCCGCCGTCGGCGTG
ATCCTCATCATGGCTGTGCTTTGCAACCGCGCCGCCTTCCACCAGGACCACATGGGCCTG
GCCTGCTATGCGCTCATCGCCGTGGTGCTGGCCGTCCAGGTGGTGGGCCTGCTGCTGCCG
CAGCCACGCAGCGCCTCTGAGGGCATCTGGTGGACCGTGTTCTTCATCTACACCATCTAC
ACGCTGCTGCCCGTGCGCATGCGGGCCGCAGTGCTCAGCGGGGTGCTCCTGTCCGCCCTC
CACCTGGCCATCGCCCTGCGCACCAACGCCCAGGACCAGTTCCTGCTGAAGCAGCTTGTC
TCCAATGTTCTCATTTTCTCCTGCACCAACATCGTGGGTGTCTGCACCCACTATCCGGCT
GAGGTCTCCCAGAGACAGGCTTTCCAGGAGACCCGAGAGTGCATCCAGGCGCGGCTCCAC
TCGCAGCGGGAGAACCAGCAGCAGGAACGGCTCCTGCTGTCTGTCCTTCCCCGTCATGTT
GCCATGGAGATGAAAGCAGACATCAACGCCAAGCAGGAGGATATGATGTTCCATAAGATT
TACATCCAGAAACATGACAACGTGAGCATCCTGTTTGCTGACATCGAGGGCTTCACCAGC
CTGGCGTCCCAGTGCACTGCACAGGAACTGGTCATGACCCTCAACGAGCTCTTCGCCCGC
TTTGACAAGCTGGCCGCAGAGAATCACTGTTTACGTATTAAGATCCTTGGGGATTGTTAT
TACTGCGTCTCGGGGCTGCCTGAAGCAAGGGCTGACCACGCCCACTGCTGTGTGGAGATG
GGCATGGACATGATCGAGGCCATCTCGTTGGTCCGGGAGGTGACAGGGGTGAACGTGAAC
ATGCGTGTGGGAATTCACAGCGGGCGAGTACACTGCGGTGTCCTTGGTCTCAGGAAGTGG
CAGTTCGACGTCTGGTCTAACGATGTCACGCTAGCCAACCACATGGAGGCTGGCGGCAAG
GCAGGACGCATCCACATCACCAAGGCTACACTCAACTACCTGAATGGGGACTACGAGGTG
GAGCCAGGCTGTGGGGGCGAGCGCAACGCCTACCTCAAGGAGCACAGTATCGAGACCTTC
CTCATCCTGCGCTGCACCCAGAAGCGGAAAGAAGAGAAGGCCATGATCGCCAAGATGAAC
CGCCAGAGAACCAACTCCATCGGGCACAACCCACCACACTGGGGGGCTGAGCGCCCCTTC
TACAACCACCTGGGTGGCAACCAGGTGTCCAAGGAGATGAAGCGGATGGGCTTTGAAGAC
CCCAAGGACAAGAACGCCCAGGAGAGTGCGAACCCTGAGGATGAAGTGGATGAGTTTCTG
GGCCGTGCCATTGACGCCAGGAGCATTGATAGGCTTCGGTCTGAGCACGTCCGCAAGTTC
CTCCTGACCTTCAGGGAGCCTGACTTAGAGAAGAAGTACTCCAAGCAGGTAGACGACCGA
TTTGGTGCCTATGTGGCGTGTGCCTCGCTCGTCTTCCTCTTCATCTGCTTTGTCCAGATC
ACCATCGTGCCCCACTCCATATTCATGCTCAGCTTCTACCTGACCTGTTCCCTGCTGCTG
ACCTTGGTGGTGTTTGTGTCTGTGATCTACTCCTGCGTAAAGCTCTTCCCCTCCCCACTG
CAGACCCTCTCCAGGAAGATCGTGCGGTCCAAGATGAACAGCACCCTGGTTGGGGTGTTC
ACCATCACCCTGGTGTTCCTGGCGGCTTTTGTCAACATGTTCACGTGCAACTCCAGGGAC
CTGCTGGGCTGCTTGGCACAGGAGCACAACATCAGCGCGAGCCAGGTCAACGCGTGTCAC
GTGGCGGAGTCGGCCGTCAACTACAGCCTGGGCGATGAGCAGGGCTTCTGTGGCAGCCCC
TGGCCCAACTGCAACTTCCCCGAGTACTTCACCTACAGCGTGCTGCTCAGCCTGCTGGCC
TGCTCCGTGTTCCTGCAGATCAGCTGCATCGGGAAGCTGGTGCTCATGCTGGCCATCGAG
CTCATCTACGTGCTCATCGTGGAGGTGCCAGGTGTCACGCTCTTCGACAACGCCGACCTG
CTGGTCACCGCCAACGCCATAGACTTCTTCAACAACGGGACCTCCCAGTGCCCTGAGCAT
GCAACCAAGGTGGCATTGAAGGTGGTGACGCCCATCATCATCTCAGTCTTTGTGCTGGCC
CTGTACCTGCACGCCCAGCAGGTGGAGTCCACTGCCCGCCTCGACTTCCTCTGGAAACTG
CAGGCCACAGAGGAGAAAGAGGAGATGGAGGAGCTGCAGGCCTACAACCGGCGGCTGCTG
CACAACATCCTGCCCAAGGACGTGGCCGCTCACTTCCTGGCCCGCGAGCGGCGCAATGAT
GAGCTCTACTATCAGTCCTGTGAGTGTGTGGCGGTCATGTTCGCCTCCATCGCCAACTTC
TCCGAGTTCTACGTTGAGCTGGAGGCCAACAACGAGGGTGTCGAGTGCCTGCGGCTACTC
AATGAGATCATCGCTGACTTTGATGAGATCATCAGCGAGGATCGGTTCCGGCAGCTGGAG
AAGATCAAGACCATCGGCAGCACCTACATGGCTGCCTCCGGCCTCAACGACTCTACCTAC
GACAAGGTGGGCAAGACCCACATCAAGGCACTGGCCGACTTTGCCATGAAGCTGATGGAC
CAGATGAAGTACATCAATGAGCACTCCTTCAACAACTTCCAGATGAAGATCGGGCTCAAC
ATCGGCCCCGTGGTGGCCGGGGTGATAGGGGCACGAAAGCCTCAGTACGACATCTGGGGC
AATACCGTGAACGTGGCCAGCCGCATGGACAGCACCGGTGTACCCGACCGCATCCAGGTC
ACCACAGACATGTACCAGGTGCTGGCTGCCAACACGTACCAGCTGGAGTGCCGGGGCGTG
GTCAAGGTCAAGGGCAAAGGCGAGATGATGACCTACTTCCTCAATGGAGGGCCCCCGCTC
AGTTAG
Enzyme 23 GenBank Gene ID NM_183357.1 Link Image
Enzyme 23 GeneCard ID ADCY5 Link Image
Enzyme 23 GenAtlas ID ADCY5 Link Image
Enzyme 23 HGNC ID HGNC:236 Link Image
Enzyme 23 Chromosome Location 3
Enzyme 23 Locus 3q13.2-q21
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  2. Ludwig MG, Seuwen K: Characterization of the human adenylyl cyclase gene family: cDNA, gene structure, and tissue distribution of the nine isoforms. J Recept Signal Transduct Res. 2002 Feb-Nov;22(1-4):79-110. [PubMed Link Image]
  3. Raimundo S, Giray J, Volff JN, Schwab M, Altenbuchner J, Ratge D, Wisser H: Cloning and sequence of partial cDNAs encoding the human type V and VI adenylyl cyclases and subsequent RNA-quantification in various tissues. Clin Chim Acta. 1999 Jul;285(1-2):155-61. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 5981
Enzyme 24 Name Adenylate cyclase type 8
Enzyme 24 Synonyms
  1. ATP pyrophosphate-lyase 8
  2. Adenylate cyclase type VIII
  3. Adenylyl cyclase 8
  4. Ca(2+)/calmodulin-activated adenylyl cyclase
Enzyme 24 Gene Name ADCY8
Enzyme 24 Protein Sequence >Adenylate cyclase type 8
MELSDVRCLTGSEELYTIHPTPPAGDGRSASRPQRLLWQTAVRHITEQRFIHGHRGGSGS
GSGGSGKASDPAGGGPNHHAPQLSGDSALPLYSLGPGERAHSTCGTKVFPERSGSGSASG
SGGGGDLGFLHLDCAPSNSDFFLNGGYSYRGVIFPTLRNSFKSRDLERLYQRYFLGQRRK
SEVVMNVLDVLTKLTLLVLHLSLASAPMDPLKGILLGFFTGIEVVICALVVVRKDTTSHT
YLQYSGVVTWVAMTTQILAAGLGYGLLGDGIGYVLFTLFATYSMLPLPLTWAILAGLGTS
LLQVILQVVIPRLAVISINQVVAQAVLFMCMNTAGIFISYLSDRAQRQAFLETRRCVEAR
LRLETENQRQERLVLSVLPRFVVLEMINDMTNVEDEHLQHQFHRIYIHRYENVSILFADV
KGFTNLSTTLSAQELVRMLNELFARFDRLAHEHHCLRIKILGDCYYCVSGLPEPRQDHAH
CCVEMGLSMIKTIRYVRSRTKHDVDMRIGIHSGSVLCGVLGLRKWQFDVWSWDVDIANKL
ESGGIPGRIHISKATLDCLNGDYNVEEGHGKERNEFLRKHNIETYLIKQPEDSLLSLPED
IVKESVSSSDRRNSGATFTEGSWSPELPFDNIVGKQNTLAALTRNSINLLPNHLAQALHV
QSGPEEINKRIEHTIDLRSGDKLRREHIKPFSLMFKDSSLEHKYSQMRDEVFKSNLVCAF
IVLLFITAIQSLLPSSRVMPMTIQFSILIMLHSALVLITTAEDYKCLPLILRKTCCWINE
TYLARNVIIFASILINFLGAILNILWCDFDKSIPLKNLTFNSSAVFTDICSYPEYFVFTG
VLAMVTCAVFLRLNSVLKLAVLLIMIAIYALLTETVYAGLFLRYDNLNHSGEDFLGTKEV
SLLLMAMFLLAVFYHGQQLEYTARLDFLWRVQAKEEINEMKELREHNENMLRNILPSHVA
RHFLEKDRDNEELYSQSYDAVGVMFASIPGFADFYSQTEMNNQGVECLRLLNEIIADFDE
LLGEDRFQDIEKIKTIGSTYMAVSGLSPEKQQCEDKWGHLCALADFSLALTESIQEINKH
SFNNFELRIGISHGSVVAGVIGAKKPQYDIWGKTVNLASRMDSTGVSGRIQVPEETYLIL
KDQGFAFDYRGEIYVKGISEQEGKIKTYFLLGRVQPNPFILPPRRLPGQYSLAAVVLGLV
QSLNRQRQKQLLNENNNTGIIKGHYNRRTLLSPSGTEPGAQAEGTDKSDLP
Enzyme 24 Number of Residues 1251
Enzyme 24 Molecular Weight 140120.8
Enzyme 24 Theoretical pI 6.99
Enzyme 24 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 24 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 24 Specific Function This is a membrane-bound, calcium-stimulable adenylyl cyclase. May be involved in learning, in memory and in drug dependence
Enzyme 24 Pathways
Enzyme 24 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • 183-203 212-232 247-267 274-294 296-316 321-341 716-736 738-758 787-807 831-851 861-881 894-914
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 516263 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID P40145 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name ADCY8_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >3756 bp
ATGGAGCTCTCCGATGTGCGCTGCCTTACAGGCAGCGAGGAACTCTACACCATCCACCCG
ACGCCCCCGGCCGGCGACGGCAGGAGCGCCTCCCGGCCGCAGCGGCTGCTGTGGCAGACG
GCGGTGCGACACATCACGGAGCAGCGCTTCATTCACGGGCACCGGGGAGGCAGCGGCAGC
GGGAGTGGAGGCTCGGGCAAAGCCTCGGACCCTGCGGGCGGCGGCCCCAACCACCACGCG
CCGCAGCTGTCAGGCGACTCGGCGCTGCCCCTCTACTCGCTGGGCCCGGGAGAGCGAGCG
CACAGCACCTGCGGCACCAAAGTCTTCCCGGAACGCAGCGGGAGCGGCAGTGCCAGCGGC
AGCGGAGGCGGGGGCGACCTGGGCTTCCTGCACCTTGACTGTGCCCCTAGCAACTCGGAT
TTCTTTCTTAATGGGGGCTATAGCTACCGAGGGGTCATTTTCCCCACCCTGCGCAACTCC
TTCAAATCTCGGGATTTGGAACGCCTCTACCAGCGCTATTTCTTGGGCCAAAGGCGCAAA
TCGGAAGTGGTGATGAACGTGCTGGACGTGCTGACCAAACTCACTCTCTTGGTCCTACAC
TTGAGCCTGGCCTCGGCCCCCATGGACCCGCTCAAGGGCATCCTGCTGGGCTTCTTCACC
GGCATTGAGGTAGTGATCTGCGCCCTGGTGGTGGTCAGGAAGGACACCACCTCCCACACG
TACCTGCAGTACAGCGGCGTGGTCACCTGGGTGGCCATGACCACCCAGATCCTGGCAGCA
GGCCTCGGCTACGGGCTCCTGGGCGACGGCATAGGCTACGTGCTCTTCACGCTCTTCGCC
ACCTACAGTATGCTGCCGCTGCCGCTCACCTGGGCCATCCTGGCCGGCCTGGGCACCTCG
CTGCTGCAGGTCATCCTCCAAGTGGTCATACCCCGGCTGGCGGTCATTTCCATCAACCAG
GTTGTGGCCCAGGCAGTGCTATTCATGTGTATGAACACAGCTGGAATCTTCATCAGTTAC
CTGTCAGACCGGGCCCAGCGCCAAGCTTTCCTGGAGACTCGGAGGTGTGTGGAGGCCAGG
CTGCGCCTGGAGACAGAGAACCAAAGACAGGAGCGGCTCGTGCTTTCTGTGCTCCCCCGG
TTTGTTGTCCTGGAAATGATCAACGACATGACCAATGTGGAAGATGAGCACCTGCAGCAC
CAGTTCCATCGGATCTACATCCATCGCTATGAGAACGTCAGTATTCTTTTTGCAGATGTT
AAAGGATTTACCAACCTCTCCACGACCTTGTCTGCTCAGGAGCTGGTCAGGATGCTCAAC
GAGCTCTTTGCCAGATTTGATCGACTGGCCCATGAGCATCACTGCCTTCGTATTAAAATC
CTGGGGGACTGCTACTACTGCGTGTCTGGACTTCCTGAGCCCCGCCAGGACCATGCCCAC
TGCTGTGTTGAAATGGGTCTCAGCATGATCAAAACCATCAGGTATGTGCGGTCAAGGACA
AAACACGATGTTGACATGAGGATTGGAATCCACTCCGGCTCGGTGCTGTGCGGTGTTTTG
GGACTACGGAAGTGGCAGTTTGATGTCTGGTCTTGGGATGTGGATATTGCAAACAAACTC
GAATCTGGAGGAATCCCCGGGAGGATTCACATTTCCAAAGCCACGCTGGACTGTCTCAAC
GGTGACTATAACGTGGAAGAGGGCCATGGTAAAGAGAGGAATGAATTCCTGAGGAAGCAT
AATATCGAAACTTACTTAATTAAGCAGCCTGAGGACAGTCTGCTGTCCTTGCCTGAAGAT
ATCGTCAAGGAGTCAGTGAGCTCCTCAGACCGGAGAAACAGTGGGGCCACATTCACTGAA
GGATCCTGGAGCCCTGAACTGCCCTTTGATAATATCGTGGGGAAACAGAATACTCTGGCT
GCCCTAACAAGAAATTCAATAAATCTGCTTCCAAACCATCTTGCACAAGCTTTGCATGTC
CAGTCTGGGCCTGAGGAAATTAACAAGAGAATAGAACATACCATCGACTTGCGGAGTGGC
GATAAATTGAGAAGAGAGCATATCAAGCCATTCTCACTGATGTTTAAAGACTCCAGCCTG
GAGCACAAGTATTCTCAAATGAGGGATGAAGTGTTCAAGTCAAACTTGGTCTGTGCATTT
ATCGTTCTTCTATTTATCACGGCAATACAAAGTTTGCTTCCTTCTTCAAGAGTGATGCCA
ATGACCATCCAGTTCTCCATTCTGATTATGCTGCACTCGGCTCTGGTCCTCATCACCACA
GCAGAGGATTATAAATGTTTGCCCCTCATCCTCCGGAAAACTTGCTGTTGGATTAATGAG
ACCTATTTGGCCCGGAACGTCATCATCTTTGCATCCATTTTGATTAATTTCCTGGGTGCC
ATCTTAAATATCCTGTGGTGTGATTTTGACAAGTCGATACCCTTGAAGAACCTGACTTTC
AATTCCTCAGCTGTGTTTACAGATATCTGCTCCTACCCAGAGTACTTTGTCTTCACGGGG
GTGTTGGCCATGGTGACCTGTGCAGTTTTCCTCCGGCTGAACTCCGTCCTGAAGCTGGCA
GTGCTGCTGATCATGATTGCCATCTATGCCCTGCTCACTGAGACCGTCTACGCAGGCCTC
TTTCTGCGTTATGACAACCTCAACCACAGTGGAGAAGATTTCCTGGGGACCAAGGAGGTA
TCACTGCTACTGATGGCCATGTTCCTCCTGGCTGTGTTCTACCATGGACAGCAGCTGGAG
TACACAGCCCGCCTGGACTTCCTTTGGCGAGTACAGGCCAAAGAGGAGATCAATGAGATG
AAGGAGCTGAGGGAACACAATGAGAACATGCTCCGGAATATCTTACCCAGCCATGTGGCC
CGCCATTTCCTAGAGAAGGACCGAGACAATGAGGAGCTGTATTCTCAATCCTATGATGCT
GTTGGGGTGATGTTTGCCTCCATCCCAGGATTTGCGGACTTTTACTCTCAGACTGAAATG
AATAACCAGGGAGTGGAATGCCTGCGCTTGCTCAATGAGATCATTGCTGACTTCGATGAG
TTGCTTGGTGAAGACCGATTTCAAGACATTGAAAAGATTAAGACCATTGGCAGCACCTAC
ATGGCCGTGTCAGGCCTGTCACCTGAAAAACAGCAATGTGAAGACAAGTGGGGACATTTG
TGTGCTCTGGCTGACTTCTCACTCGCCCTGACAGAAAGCATACAGGAGATCAACAAGCAT
TCATTCAACAATTTTGAACTCCGGATTGGCATCAGCCACGGCTCAGTGGTAGCTGGCGTT
ATCGGCGCTAAGAAACCACAGTATGACATTTGGGGCAAAACTGTGAACCTGGCAAGCCGA
ATGGACAGCACGGGGGTTAGTGGCCGGATCCAAGTCCCAGAGGAGACCTATCTCATCCTG
AAGGACCAGGGCTTTGCCTTTGATTACCGAGGGGAGATCTATGTGAAGGGTATCAGTGAA
CAGGAAGGAAAAATCAAAACGTACTTTCTTCTGGGAAGAGTCCAACCCAACCCATTCATC
TTGCCCCCAAGAAGACTGCCTGGGCAGTACTCCCTGGCCGCGGTTGTCCTGGGACTTGTC
CAGTCCCTCAATAGGCAAAGGCAGAAGCAGCTACTCAATGAGAACAACAACACAGGAATC
ATCAAGGGTCATTACAACCGGCGGACTTTGTTGTCACCCAGCGGCACAGAGCCTGGAGCC
CAGGCTGAAGGCACCGACAAATCTGATTTGCCATAA
Enzyme 24 GenBank Gene ID Z35309 Link Image
Enzyme 24 GeneCard ID ADCY8 Link Image
Enzyme 24 GenAtlas ID ADCY8 Link Image
Enzyme 24 HGNC ID HGNC:239 Link Image
Enzyme 24 Chromosome Location 8
Enzyme 24 Locus 8q24
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Defer N, Marinx O, Stengel D, Danisova A, Iourgenko V, Matsuoka I, Caput D, Hanoune J: Molecular cloning of the human type VIII adenylyl cyclase. FEBS Lett. 1994 Aug 29;351(1):109-13. [PubMed Link Image]
  2. Parma J, Stengel D, Gannage MH, Poyard M, Barouki R, Hanoune J: Sequence of a human brain adenylyl cyclase partial cDNA: evidence for a consensus cyclase specific domain. Biochem Biophys Res Commun. 1991 Aug 30;179(1):455-62. [PubMed Link Image]
  3. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 5983
Enzyme 25 Name Adenylate cyclase type 3
Enzyme 25 Synonyms
  1. ATP pyrophosphate-lyase 3
  2. Adenylate cyclase type III
  3. AC-III
  4. Adenylate cyclase, olfactive type
  5. Adenylyl cyclase 3
  6. AC3
Enzyme 25 Gene Name ADCY3
Enzyme 25 Protein Sequence >Adenylate cyclase type 3
MPRNQGFSEPEYSAEYSAEYSVSLPSDPDRGVGRTHEISVRNSGSCLCLPRFMRLTFVPE
SLENLYQTYFKRQRHETLLVLVVFAALFDCYVVVMCAVVFSSDKLASLAVAGIGLVLDII
LFVLCKKGLLPDRVTRRVLPYVLWLLITAQIFSYLGLNFARAHAASDTVGWQVFFVFSFF
ITLPLSLSPIVIISVVSCVVHTLVLGVTVAQQQQEELKGMQLLREILANVFLYLCAIAVG
IMSYYMADRKHRKAFLEARQSLEVKMNLEEQSQQQENLMLSILPKHVADEMLKDMKKDES
QKDQQQFNTMYMYRHENVSILFADIVGFTQLSSACSAQELVKLLNELFARFDKLAAKYHQ
LRIKILGDCYYCICGLPDYREDHAVCSILMGLAMVEAISYVREKTKTGVDMRVGVHTGTV
LGGVLGQKRWQYDVWSTDVTVANKMEAGGIPGRVHISQSTMDCLKGEFDVEPGDGGSRCD
YLEEKGIETYLIIASKPEVKKTATQNGLNGSALPNGAPASSKSSSPALIETKEPNGSAHS
SGSTSEKPEEQDAQADNPSFPNPRRRLRLQDLADRVVDASEDEHELNQLLNEALLERESA
QVVKKRNTFLLSMRFMDPEMETRYSVEKEKQSGAAFSCSCVVLLCTALVEILIDPWLMTN
YVTFMVGEILLLILTICSLAAIFPRAFPKKLVAFSTWIDRTRWARNTWAMLAIFILVMAN
VVDMLSCLQYYTGPSNATAGMETEGSCLENPKYYNYVAVLSLIATIMLVQVSHMVKLTLM
LLVAGAVATINLYAWRPVFDEYDHKRFREHDLPMVALEQMQGFNPGLNGTDRLPLVPSKY
SMTVMVFLMMLSFYYFSRHVEKLARTLFLWKIEVHDQKERVYEMRRWNEALVTNMLPEHV
ARHFLGSKKRDEELYSQTYDEIGVMFASLPNFADFYTEESINNGGIECLRFLNEIISDFD
SLLDNPKFRVITKIKTIGSTYMAASGVTPDVNTNGFASSNKEDKSERERWQHLADLADFA
LAMKDTLTNINNQSFNNFMLRIGMNKGGVLAGVIGARKPHYDIWGNTVNVASRMESTGVM
GNIQVVEETQVILREYGFRFVRRGPIFVKGKGELLTFFLKGRDKLATFPNGPSVTLPHQV
VDNS
Enzyme 25 Number of Residues 1144
Enzyme 25 Molecular Weight 128958.9
Enzyme 25 Theoretical pI 6.55
Enzyme 25 GO Classification
Function
  • catalytic activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
Enzyme 25 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 25 Specific Function Mediates odorant detection (possibly) via modulation of intracellular cAMP concentration
Enzyme 25 Pathways
Enzyme 25 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • 80-100 105-125 139-159 173-193 226-246 381-401 633-653 664-684 708-728 754-774 775-795 833-853
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 148536830 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID O60266 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name ADCY3_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >3435 bp
ATGCCGAGGAACCAGGGCTTCTCCGAGCCCGAATACTCGGCCGAGTACTCAGCCGAGTAC
TCCGTCAGCCTGCCCTCCGACCCTGACCGCGGGGTGGGCCGGACCCATGAAATCTCGGTC
CGGAACTCGGGCTCCTGCCTGTGCCTGCCTCGCTTCATGCGGCTGACTTTCGTGCCGGAG
TCCTTGGAGAACCTCTACCAGACCTACTTCAAAAGGCAGCGCCACGAGACCCTGCTGGTG
CTGGTGGTCTTTGCAGCCCTCTTTGACTGCTACGTGGTGGTCATGTGTGCTGTGGTCTTC
TCCAGCGACAAGCTGGCTTCCCTCGCCGTGGCTGGAATTGGACTGGTGTTGGACATCATC
CTCTTCGTGCTCTGCAAAAAGGGGCTGCTCCCGGACCGGGTCACCCGCAGAGTGCTGCCC
TACGTGCTGTGGCTGCTCATAACCGCCCAGATCTTCTCCTACCTGGGCCTGAACTTCGCG
CGTGCCCACGCGGCTAGTGACACGGTGGGCTGGCAGGTCTTCTTTGTCTTCTCCTTCTTC
ATCACGCTGCCCCTCAGCCTCAGCCCCATCGTGATCATCTCCGTGGTCTCCTGTGTGGTG
CACACGTTGGTCCTGGGGGTCACCGTGGCCCAGCAGCAGCAGGAGGAGCTCAAGGGGATG
CAGCTGCTGCGGGAGATCCTGGCCAACGTCTTCCTCTACCTGTGCGCCATCGCTGTGGGC
ATCATGTCCTACTACATGGCTGACCGCAAGCACCGCAAGGCCTTCCTGGAGGCCCGCCAG
TCGCTGGAGGTGAAGATGAACCTGGAAGAGCAGAGCCAGCAGCAGGAGAACCTCATGCTT
TCCATCCTGCCCAAGCACGTGGCTGACGAGATGCTGAAAGACATGAAGAAAGACGAGAGC
CAGAAGGACCAGCAGCAGTTCAACACCATGTACATGTACCGTCACGAGAACGTCAGCATC
CTCTTTGCCGACATCGTGGGCTTTACCCAGCTGTCTTCTGCCTGCAGTGCCCAGGAGCTT
GTGAAGCTGCTCAACGAGCTCTTTGCCCGCTTTGACAAGCTGGCAGCTAAATACCACCAG
CTGCGGATTAAGATCCTGGGCGACTGCTACTACTGCATCTGCGGCTTGCCCGACTACCGG
GAGGACCACGCCGTCTGCTCCATCCTCATGGGGCTGGCCATGGTGGAGGCCATCTCGTAT
GTGCGGGAGAAGACCAAGACTGGGGTGGACATGCGTGTGGGGGTGCACACGGGCACCGTG
CTGGGGGGCGTCCTGGGCCAGAAGCGCTGGCAGTACGACGTGTGGTCGACTGATGTCACT
GTAGCCAACAAGATGGAGGCCGGCGGCATCCCTGGGCGCGTGCACATCTCCCAGAGCACC
ATGGACTGCCTGAAAGGGGAGTTTGATGTGGAGCCAGGCGATGGGGGCAGCCGCTGTGAT
TACCTAGAAGAGAAGGGTATTGAAACCTACCTCATCATTGCCTCCAAGCCAGAGGTGAAG
AAAACAGCCACCCAGAATGGCCTCAATGGCTCGGCCCTGCCCAATGGAGCACCAGCTTCC
TCAAAGTCCAGCTCCCCTGCCCTCATTGAGACCAAGGAGCCCAACGGGAGTGCCCACAGC
AGTGGGTCCACGTCGGAGAAGCCCGAGGAGCAGGATGCCCAGGCCGACAACCCCTCATTC
CCCAACCCACGCCGGAGGCTGCGCCTGCAGGACCTGGCTGACCGAGTGGTGGATGCCTCT
GAAGATGAGCACGAGCTCAACCAGCTGCTCAACGAGGCCCTGCTTGAGCGAGAGTCCGCC
CAAGTAGTAAAGAAGAGAAACACCTTCCTCTTGTCCATGCGGTTCATGGACCCCGAGATG
GAAACCCGCTACTCGGTGGAGAAGGAGAAGCAGAGTGGGGCTGCCTTCAGCTGCTCCTGC
GTCGTCCTGCTCTGCACGGCCCTGGTCGAGATACTCATCGACCCCTGGCTAATGACAAAC
TATGTGACCTTCATGGTGGGGGAGATTCTGCTCCTCATCCTGACCATCTGCTCCCTGGCT
GCCATCTTTCCCCGGGCCTTTCCTAAGAAGCTTGTGGCCTTCTCAACTTGGATTGACCGG
ACCCGCTGGGCCAGGAACACCTGGGCCATGCTCGCCATCTTCATCCTGGTGATGGCAAAT
GTCGTGGACATGCTCAGCTGTCTCCAGTACTACACGGGACCCAGCAATGCAACGGCAGGG
ATGGAAACGGAGGGCAGCTGCCTGGAGAACCCCAAGTATTACAACTATGTGGCCGTGCTG
TCCCTCATCGCCACCATCATGCTGGTGCAGGTCAGCCACATGGTGAAGCTCACGCTCATG
CTGCTCGTCGCAGGCGCCGTGGCCACCATCAACCTCTATGCCTGGCGTCCCGTCTTTGAT
GAATACGACCACAAGCGTTTTCGGGAGCACGACTTACCTATGGTGGCCTTAGAGCAGATG
CAAGGATTCAACCCTGGGCTCAATGGCACTGACAGGCTGCCCCTGGTGCCTTCCAAGTAC
TCTATGACGGTGATGGTGTTCCTCATGATGCTCAGCTTCTACTACTTCTCCCGCCACGTA
GAAAAACTGGCACGGACACTTTTCTTGTGGAAGATTGAGGTCCACGACCAGAAGGAACGT
GTCTATGAGATGCGACGCTGGAACGAGGCCTTGGTCACCAACATGTTGCCTGAGCACGTG
GCACGCCATTTCCTGGGGTCCAAGAAGAGAGATGAGGAGCTGTATAGCCAGACGTATGAT
GAGATTGGAGTCATGTTTGCCTCCCTGCCCAACTTTGCTGACTTCTACACAGAGGAGAGC
ATCAACAATGGTGGTATTGAGTGTCTGCGTTTCCTCAATGAAATCATCTCAGATTTTGAC
TCTCTCCTGGACAATCCCAAGTTCCGGGTGATCACCAAGATCAAAACCATTGGCAGCACG
TATATGGCGGCTTCAGGAGTCACCCCCGATGTCAACACCAATGGCTTTGCCAGCTCCAAC
AAGGAAGACAAGTCCGAGAGAGAGCGCTGGCAGCACCTGGCTGACCTGGCCGACTTCGCG
CTGGCCATGAAGGATACGCTCACCAACATCAACAACCAGTCCTTCAATAACTTCATGCTG
CGCATAGGCATGAACAAAGGCGGGGTTCTGGCTGGGGTCATCGGAGCCCGGAAACCACAC
TACGACATCTGGGGCAATACAGTCAATGTAGCCAGCAGGATGGAGTCCACGGGGGTCATG
GGCAACATTCAGGTGGTAGAAGAAACCCAAGTCATCCTCCGAGAGTACGGCTTCCGCTTT
GTGAGGCGAGGCCCCATCTTTGTGAAGGGGAAGGGGGAGCTGCTGACCTTCTTCTTGAAG
GGGCGGGATAAGCTAGCCACCTTCCCCAATGGCCCCTCTGTCACACTGCCCCACCAGGTG
GTGGACAACTCCTGA
Enzyme 25 GenBank Gene ID NM_004036.3 Link Image
Enzyme 25 GeneCard ID ADCY3 Link Image
Enzyme 25 GenAtlas ID ADCY3 Link Image
Enzyme 25 HGNC ID HGNC:234 Link Image
Enzyme 25 Chromosome Location 2
Enzyme 25 Locus 2p23.3
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Yang B, He B, Abdel-Halim SM, Tibell A, Brendel MD, Bretzel RG, Efendic S, Hillert J: Molecular cloning of a full-length cDNA for human type 3 adenylyl cyclase and its expression in human islets. Biochem Biophys Res Commun. 1999 Jan 27;254(3):548-51. [PubMed Link Image]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
  5. Hellevuo K, Yoshimura M, Kao M, Hoffman PL, Cooper DM, Tabakoff B: A novel adenylyl cyclase sequence cloned from the human erythroleukemia cell line. Biochem Biophys Res Commun. 1993 Apr 15;192(1):311-8. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 5984
Enzyme 26 Name Adenylate cyclase type 1
Enzyme 26 Synonyms
  1. ATP pyrophosphate-lyase 1
  2. Adenylate cyclase type I
  3. Adenylyl cyclase 1
  4. Ca(2+)/calmodulin-activated adenylyl cyclase
Enzyme 26 Gene Name ADCY1
Enzyme 26 Protein Sequence >Adenylate cyclase type 1
MAGAPRGGGGGGGGAGEPGGAERAAGTSRRRGLRACDEEFACPELEALFRGYTLRLEQAA
TLKALAVLSLLAGALALAELLGAPGPAPGLAKGSHPVHCVLFLALLVVTNVRSLQVPQLQ
QVGQLALLFSLTFALLCCPFALGGPARGSAGAAGGPATAEQGVWQLLLVTFVSYALLPVR
SLLAIGFGLVVAASHLLVTATLVPAKRPRLWRTLGANALLFVGVNMYGVFVRILTERSQR
KAFLQARSCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDFLKPPERIFHKIYIQRHD
NVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGL
TQPKTDHAHCCVEMGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWS
NDVTLANVMEAAGLPGKVHITKTTLACLNGDYEVEPGYGHERNSFLKTHNIETFFIVPSH
RRKIFPGLILSDIKPAKRMKFKTVCYLLVQLMHCRKMFKAEIPFSNVMTCEDDDKRRALR
TASEKLRNRSSFSTNVVYTTPGTRVNRYISRLLEARQTELEMADLNFFTLKYKHVEREQK
YHQLQDEYFTSAVVLTLILAALFGLVYLLIFPQSVVVLLLLVFCICFLVACVLYLHITRV
QCFPGCLTIQIRTVLCIFIVVLIYSVAQGCVVGCLPWAWSSKPNSSLVVLSSGGQRTALP
TLPCESTHHALLCCLVGTLPLAIFFRVSSLPKMILLSGLTTSYILVLELSGYTRTGGGAV
SGRSYEPIVAILLFSCALALHARQVDIRLRLDYLWAAQAEEEREDMEKVKLDNRRILFNL
LPAHVAQHFLMSNPRNMDLYYQSYSQVGVMFASIPNFNDFYIELDGNNMGVECLRLLNEI
IADFDELMEKDFYKDIEKIKTIGSTYMAAVGLAPTSGTKAKKSISSHLSTLADFAIEMFD
VLDEINYQSYNDFVLRVGINVGPVVAGVIGARRPQYDIWGNTVNVASRMDSTGVQGRIQV
TEEVHRLLRRCPYHFVCRGKVSVKGKGEMLTYFLEGRTDGNGSQIRSLGLDRKMCPFGRA
GLQGRRPPVCPMPGVSVRAGLPPHSPGQYLPSAAAGKEA
Enzyme 26 Number of Residues 1119
Enzyme 26 Molecular Weight 123438.8
Enzyme 26 Theoretical pI 8.49
Enzyme 26 GO Classification
Function
  • catalytic activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
Enzyme 26 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 26 Specific Function This is a calmodulin-sensitive adenylyl cyclase. May be involved in regulatory processes in the central nervous system. It may play a role in memory acquisition and learning
Enzyme 26 Pathways
Enzyme 26 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • 64-84 88-108 125-145 158-178 183-203 214-234 611-631 635-655 674-694 725-745 753-773 775-794
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 31083193 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q08828 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name ADCY1_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >3360 bp
ATGGCGGGGGCGCCGCGCGGCGGAGGCGGCGGCGGAGGCGGCGCGGGCGAGCCCGGGGGC
GCCGAGCGGGCGGCCGGGACAAGCCGCCGGCGCGGGCTCCGGGCGTGCGACGAGGAGTTC
GCTTGCCCAGAGCTGGAGGCGCTGTTCCGCGGCTACACGCTGCGGCTGGAGCAGGCGGCC
ACGCTGAAGGCGCTGGCCGTTCTCAGCCTGCTGGCGGGCGCGCTGGCGCTGGCCGAGCTG
CTGGGCGCGCCGGGGCCCGCGCCCGGCCTGGCCAAGGGCTCACACCCGGTGCACTGCGTC
CTCTTCCTGGCGCTGCTCGTGGTAACCAACGTCCGGTCCCTGCAGGTGCCCCAGCTGCAG
CAGGTCGGCCAGCTGGCGCTGCTCTTCAGCCTCACCTTCGCGCTGCTCTGCTGTCCTTTC
GCGCTGGGCGGCCCCGCCCGGGGTTCCGCCGGGGCCGCTGGGGGGCCAGCGACCGCCGAA
CAAGGGGTTTGGCAGCTCCTTTTGGTCACCTTCGTGTCCTATGCCTTGCTGCCCGTGCGC
AGCCTGCTGGCCATAGGCTTTGGGCTCGTGGTGGCTGCGTCGCACTTGCTGGTCACAGCC
ACCTTGGTCCCCGCCAAGCGCCCACGTCTCTGGAGGACGCTCGGTGCCAATGCCTTGCTC
TTCGTCGGTGTGAACATGTATGGGGTCTTTGTGCGGATTCTGACTGAGCGTTCACAGAGG
AAGGCGTTCCTGCAGGCCCGGAGCTGCATTGAGGACCGACTGAGGCTGGAGGATGAGAAC
GAGAAGCAGGAGCGGCTCCTCATGAGCCTCCTGCCCCGGAACGTTGCCATGGAGATGAAG
GAGGACTTCCTGAAGCCCCCTGAGAGGATTTTCCACAAGATTTACATCCAGAGGCACGAC
AATGTGAGCATCCTGTTTGCTGACATCGTGGGTTTCACGGGCTTGGCATCCCAGTGCACA
GCCCAGGAGCTGGTGAAACTCCTCAATGAGCTCTTCGGCAAGTTCGATGAATTAGCCACG
GAGAACCACTGTCGCCGCATCAAGATTCTCGGGGACTGCTACTACTGCGTGTCGGGCCTC
ACCCAGCCCAAGACTGACCATGCCCACTGCTGTGTGGAGATGGGACTCGACATGATTGAT
ACCATCACATCTGTGGCTGAAGCCACCGAGGTGGATCTGAACATGCGTGTGGGTCTGCAC
ACGGGCAGGGTCCTCTGTGGTGTCCTGGGCTTGCGCAAGTGGCAGTACGACGTGTGGTCC
AATGATGTGACCTTGGCCAATGTCATGGAAGCCGCTGGCCTGCCAGGGAAGGTTCATATC
ACAAAGACGACCCTAGCGTGCTTGAATGGGGACTACGAGGTAGAACCGGGTTACGGACAT
GAGAGGAACAGTTTCTTGAAAACTCATAACATCGAAACCTTTTTTATTGTGCCATCCCAT
CGCCGAAAGATATTTCCAGGCCTGATTCTCTCAGATATAAAACCGGCCAAAAGGATGAAG
TTCAAGACTGTCTGCTACCTGCTGGTGCAGCTCATGCACTGCCGGAAAATGTTCAAGGCC
GAGATCCCCTTCTCCAATGTCATGACCTGCGAGGACGATGACAAGCGGAGGGCATTAAGA
ACAGCCTCGGAAAAACTCAGAAACCGCTCATCTTTTTCTACCAACGTTGTCTACACCACC
CCGGGCACTCGCGTCAACAGGTACATCAGCCGCCTCTTAGAAGCCCGCCAGACAGAGCTG
GAGATGGCAGACCTGAACTTCTTTACCCTGAAGTACAAACATGTCGAACGGGAGCAAAAG
TACCACCAGCTTCAGGACGAGTATTTCACCAGCGCCGTTGTCCTCACCCTCATCCTGGCT
GCCTTATTTGGCCTTGTCTACCTTCTAATATTCCCACAGAGTGTGGTCGTCCTGCTCCTG
CTAGTATTCTGCATCTGCTTCCTGGTGGCCTGTGTCCTGTACCTGCACATCACCCGGGTC
CAGTGTTTTCCAGGGTGCCTGACGATTCAGATTCGCACTGTCCTGTGTATTTTCATAGTG
GTCTTAATCTACTCAGTAGCCCAAGGTTGTGTGGTGGGCTGCCTGCCTTGGGCCTGGAGC
TCCAAGCCCAACAGTTCCCTGGTGGTCCTTTCGTCTGGGGGCCAGCGCACAGCCCTGCCC
ACCCTGCCCTGCGAGTCTACACACCATGCCCTGCTCTGCTGCCTGGTGGGCACCCTCCCG
CTAGCCATATTTTTCCGGGTGTCCTCCTTGCCAAAAATGATCCTGCTCTCCGGGCTCACC
ACGTCCTACATCCTCGTTCTGGAGCTCAGCGGATACACCAGGACTGGGGGTGGTGCCGTC
TCCGGGCGCAGCTACGAGCCGATTGTGGCCATCCTGCTCTTCTCCTGTGCGCTGGCCCTG
CATGCCAGGCAGGTGGACATCAGGCTGAGGCTGGACTACCTCTGGGCCGCACAGGCAGAG
GAGGAGCGAGAGGACATGGAGAAGGTGAAGCTGGACAACAGGCGCATCCTCTTCAACCTC
CTGCCGGCCCACGTCGCCCAGCACTTCCTCATGTCCAACCCTCGGAACATGGACCTCTAC
TACCAGTCCTACTCCCAGGTGGGCGTCATGTTTGCCTCCATCCCCAACTTCAATGACTTC
TACATCGAGCTGGACGGCAACAACATGGGGGTGGAGTGTCTGCGGCTTCTCAACGAGATC
ATCGCCGACTTTGACGAGCTCATGGAAAAAGACTTTTACAAGGACATAGAGAAGATCAAG
ACCATCGGGAGCACCTACATGGCCGCTGTGGGGCTAGCGCCCACCTCGGGGACCAAGGCT
AAGAAGTCCATCTCCTCCCACCTGAGCACGCTGGCGGACTTTGCCATTGAGATGTTTGAC
GTTCTGGATGAAATCAACTACCAGTCTTACAACGACTTTGTCCTCCGAGTTGGCATCAAT
GTTGGCCCTGTGGTGGCTGGAGTGATTGGCGCTCGCAGGCCCCAGTACGACATCTGGGGA
AACACAGTCAACGTGGCCAGTCGGATGGATAGCACAGGGGTCCAGGGCAGAATCCAGGTG
ACTGAGGAAGTCCACCGGCTGCTGAGAAGGTGCCCCTACCACTTTGTGTGCCGAGGCAAA
GTCAGTGTCAAGGGCAAAGGCGAGATGTTGACATACTTTCTAGAAGGCAGGACTGATGGA
AACGGCTCCCAAATCAGGTCCCTGGGCTTGGATCGGAAAATGTGTCCATTTGGGAGAGCT
GGCCTTCAGGGCAGACGTCCCCCCGTGTGCCCCATGCCTGGCGTCTCAGTCAGGGCTGGG
CTCCCTCCACACTCCCCAGGCCAGTACCTGCCCTCTGCAGCAGCTGGGAAGGAGGCTTAG
Enzyme 26 GenBank Gene ID NM_021116.2 Link Image
Enzyme 26 GeneCard ID ADCY1 Link Image
Enzyme 26 GenAtlas ID ADCY1 Link Image
Enzyme 26 HGNC ID HGNC:232 Link Image
Enzyme 26 Chromosome Location 7
Enzyme 26 Locus 7p13-p12
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. 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]
  2. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  3. Villacres EC, Xia Z, Bookbinder LH, Edelhoff S, Disteche CM, Storm DR: Cloning, chromosomal mapping, and expression of human fetal brain type I adenylyl cyclase. Genomics. 1993 May;16(2):473-8. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 6011
Enzyme 27 Name DNA-directed RNA polymerase III subunit RPC4
Enzyme 27 Synonyms
  1. RNA polymerase III subunit C4
  2. DNA-directed RNA polymerase III subunit D
  3. Protein BN51
  4. RNA polymerase III 47 kDa subunit
  5. RPC53 homolog
Enzyme 27 Gene Name POLR3D
Enzyme 27 Protein Sequence >DNA-directed RNA polymerase III subunit RPC4
MSEGNAAGEPSTPGGPRPLLTGARGLIGRRPAPPLTPGRLPSIRSRDLTLGGVKKKTFTP
NIISRKIKEEPKEEVTVKKEKRERDRDRQREGHGRGRGRPEVIQSHSIFEQGPAEMMKKK
GNWDKTVDVSDMGPSHIINIKKEKRETDEETKQILRMLEKDDFLDDPGLRNDTRNMPVQL
PLAHSGWLFKEENDEPDVKPWLAGPKEEDMEVDIPAVKVKEEPRDEEEEAKMKAPPKAAR
KTPGLPKDVSVAELLRELSLTKEEELLFLQLPDTLPGQPPTQDIKPIKTEVQGEDGQVVL
IKQEKDREAKLAENACTLADLTEGQVGKLLIRKSGRVQLLLGKVTLDVTMGTACSFLQEL
VSVGLGDSRTGEMTVLGHVKHKLVCSPDFESLLDHKHR
Enzyme 27 Number of Residues 398
Enzyme 27 Molecular Weight 44395.5
Enzyme 27 Theoretical pI 6.97
Enzyme 27 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
  • transcription from RNA polymerase III promoter
  • transcription, DNA-dependent
Component
  • DNA-directed RNA polymerase III complex
  • intracellular organelle part
  • nuclear part
  • nucleoplasm part
  • organelle part
Enzyme 27 General Function Involved in DNA binding
Enzyme 27 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway
Enzyme 27 Pathways
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 55769552 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID P05423 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name RPC4_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >1197 bp
ATGTCGGAAGGAAACGCCGCCGGCGAGCCCAGCACGCCGGGAGGGCCCCGACCTCTCCTG
ACTGGGGCCCGGGGGCTCATCGGGCGGCGGCCGGCGCCTCCCCTCACCCCCGGCCGCCTT
CCCTCCATCCGTTCCAGGGACCTCACCCTCGGGGGAGTCAAGAAGAAAACCTTCACCCCA
AATATCATCAGTCGGAAGATCAAGGAAGAGCCCAAGGAAGAAGTAACTGTCAAGAAGGAG
AAGCGTGAAAGGGACAGAGACCGACAACGAGAGGGGCATGGACGAGGGCGAGGCCGTCCA
GAAGTGATCCAGTCTCACTCCATCTTTGAGCAGGGCCCAGCTGAAATGATGAAGAAAAAA
GGGAACTGGGATAAGACAGTGGATGTGTCAGACATGGGACCTTCTCATATCATCAACATC
AAAAAAGAGAAGAGAGAGACAGACGAAGAAACTAAACAGATCTTGCGTATGCTGGAGAAG
GACGATTTCCTCGATGACCCCGGCCTGAGGAACGACACTCGAAATATGCCTGTGCAGCTG
CCGCTGGCTCACTCAGGATGGCTTTTTAAGGAAGAAAATGACGAACCAGATGTTAAACCT
TGGCTGGCTGGCCCCAAGGAAGAGGACATGGAGGTGGACATACCTGCTGTGAAAGTGAAA
GAGGAGCCACGAGATGAGGAGGAAGAGGCCAAGATGAAGGCTCCTCCCAAAGCAGCCAGG
AAGACTCCAGGCCTCCCGAAGGATGTATCTGTGGCAGAGCTGCTGAGGGAGCTGAGCCTC
ACCAAGGAAGAGGAACTGCTGTTTCTGCAGCTGCCAGACACCCTCCCTGGCCAGCCACCC
ACCCAGGACATCAAGCCTATCAAGACAGAGGTGCAGGGCGAGGACGGACAGGTGGTGCTC
ATCAAGCAGGAGAAAGACCGAGAAGCCAAATTGGCAGAGAATGCTTGTACCCTGGCTGAC
CTGACAGAGGGTCAGGTTGGCAAGCTACTCATCCGCAAGTCTGGAAGGGTGCAACTCCTC
TTGGGCAAGGTGACTCTGGACGTGACCATGGGAACTGCCTGCTCCTTCCTGCAGGAGCTG
GTGTCCGTGGGCCTTGGAGACAGTAGGACAGGGGAGATGACAGTCCTGGGACACGTGAAG
CACAAACTTGTATGTTCCCCTGATTTTGAATCCCTCTTGGATCACAAACACCGGTAA
Enzyme 27 GenBank Gene ID NM_001722.2 Link Image
Enzyme 27 GeneCard ID POLR3D Link Image
Enzyme 27 GenAtlas ID POLR3D Link Image
Enzyme 27 HGNC ID HGNC:1080 Link Image
Enzyme 27 Chromosome Location 8
Enzyme 27 Locus 8q21
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Ittmann M, Greco A, Basilico C: Isolation of the human gene that complements a temperature-sensitive cell cycle mutation in BHK cells. Mol Cell Biol. 1987 Oct;7(10):3386-93. [PubMed Link Image]
  2. Hu P, Wu S, Sun Y, Yuan CC, Kobayashi R, Myers MP, Hernandez N: Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits. Mol Cell Biol. 2002 Nov;22(22):8044-55. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Chong SS, Hu P, Hernandez N: Reconstitution of transcription from the human U6 small nuclear RNA promoter with eight recombinant polypeptides and a partially purified RNA polymerase III complex. J Biol Chem. 2001 Jun 8;276(23):20727-34. Epub 2001 Feb 27. [PubMed Link Image]
  5. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  6. Chiu YH, Macmillan JB, Chen ZJ: RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell. 2009 Aug 7;138(3):576-91. Epub 2009 Jul 23. [PubMed Link Image]
  7. Ablasser A, Bauernfeind F, Hartmann G, Latz E, Fitzgerald KA, Hornung V: RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat Immunol. 2009 Oct;10(10):1065-72. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 6012
Enzyme 28 Name DNA-directed RNA polymerase II subunit RPB2
Enzyme 28 Synonyms
  1. DNA-directed RNA polymerase II 140 kDa polypeptide
  2. DNA-directed RNA polymerase II subunit B
  3. RNA polymerase II subunit 2
  4. RNA polymerase II subunit B2
Enzyme 28 Gene Name POLR2B
Enzyme 28 Protein Sequence >DNA-directed RNA polymerase II subunit RPB2
MYDADEDMQYDEDDDEITPDLWQEACWIVISSYFDEKGLVRQQLDSFDEFIQMSVQRIVE
DAPPIDLQAEAQHASGEVEEPPRYLLKFEQIYLSKPTHWERDGAPSPMMPNEARLRNLTY
SAPLYVDITKTVIKEGEEQLQTQHQKTFIGKIPIMLRSTYCLLNGLTDRDLCELNECPLD
PGGYFIINGSEKVLIAQEKMATNTVYVFAKKDSKYAYTGECRSCLENSSRPTSTIWVSML
ARGGQGAKKSAIGQRIVATLPYIKQEVPIIIVFRALGFVSDRDILEHIIYDFEDPEMMEM
VKPSLDEAFVIQEQNVALNFIGSRGAKPGVTKEKRIKYAKEVLQKEMLPHVGVSDFCETK
KAYFLGYMVHRLLLAALGRRELDDRDHYGNKRLDLAGPLLAFLFRGMFKNLLKEVRIYAQ
KFIDRGKDFNLELAIKTRIISDGLKYSLATGNWGDQKKAHQARAGVSQVLNRLTFASTLS
HLRRLNSPIGRDGKLAKPRQLHNTLWGMVCPAETPEGHAVGLVKNLALMAYISVGSQPSP
ILEFLEEWSMENLEEISPAAIADATKIFVNGCWVGIHKDPEQLMNTLRKLRRQMDIIVSE
VSMIRDIREREIRIYTDAGRICRPLLIVEKQKLLLKKRHIDQLKEREYNNYSWQDLVASG
VVEYIDTLEEETVMLAMTPDDLQEKEVAYCSTYTHCEIHPSMILGVCASIIPFPDHNQSP
RNTYQSAMGKQAMGVYITNFHVRMDTLAHVLYYPQKPLVTTRSMEYLRFRELPAGINSIV
AIASYTGYNQEDSVIMNRSAVDRGFFRSVFYRSYKEQESKKGFDQEEVFEKPTRETCQGM
RHAIYDKLDDDGLIAPGVRVSGDDVIIGKTVTLPENEDELESTNRRYTKRDCSTFLRTSE
TGIVDQVMVTLNQEGYKFCKIRVRSVRIPQIGDKFASRHGQKGTCGIQYRQEDMPFTCEG
ITPDIIINPHAIPSRMTIGHLIECLQGKVSANKGEIGDATPFNDAVNVQKISNLLSDYGY
HLRGNEVLYNGFTGRKITSQIFIGPTYYQRLKHMVDDKIHSRARGPIQILNRQPMEGRSR
DGGLRFGEMERDCQIAHGAAQFLRERLFEASDPYQVHVCNLCGIMAIANTRTHTYECRGC
RNKTQISLVRMPYACKLLFQELMSMSIAPRMMSV
Enzyme 28 Number of Residues 1174
Enzyme 28 Molecular Weight 133895.4
Enzyme 28 Theoretical pI 6.87
Enzyme 28 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleoside binding
  • nucleotidyltransferase activity
  • ribonucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
Component
Enzyme 28 General Function Involved in DNA-directed RNA polymerase activity
Enzyme 28 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB2 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template
Enzyme 28 Pathways
Enzyme 28 Reactions
  • nucleoside triphosphate + RNAn = diphosphate + RNAn+1 [RN:R00444]
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 36122 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID P30876 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name RPB2_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >3525 bp
ATGTACGACGCGGATGAGGATATGCAATATGATGAGGATGATGATGAAATCACCCCGGAT
TTGTGGCAAGAAGCATGCTGGATTGTAATCAGTTCCTATTTTGACGAGAAAGGCTTGGTT
AGACAACAGCTGGATTCTTTTGATGAGTTTATTCAGATGTCTGTTCAAAGAATTGTGGAA
GACGCTCCTCCTATAGACCTACAGGCTGAAGCTCAGCATGCTAGTGGAGAAGTTGAAGAA
CCGCCACGATATTTGCTGAAGTTTGAACAAATTTATCTTTCCAAGCCTACCCATTGGGAA
AGAGATGGTGCTCCTTCACCAATGATGCCCAATGAAGCTAGATTAAGGAATCTCACGTAT
TCTGCTCCGCTTTATGTTGATATAACAAAAACAGTCATTAAAGAAGGTGAAGAACAACTT
CAGACTCAGCATCAGAAAACTTTTATAGGAAAAATTCCAATTATGTTGCGGTCAACTTAC
TGCCTTTTGAATGGCTTGACAGATCGTGATCTTTGTGAGTTAAATGAATGCCCTTTGGAT
CCTGGTGGCTATTTCATTATTAATGGATCAGAAAAGGTTCTGATTGCCCAAGAGAAAATG
GCAACAAACACAGTTTATGTGTTTGCCAAAAAGGATTCTAAATATGCCTACACAGGAGAG
TGTAGATCATGTCTTGAGAATTCTTCCCGACCCACCAGTACTATATGGGTTAGCATGCTG
GCAAGAGGAGGACAGGGTGCCAAGAAGAGTGCTATTGGTCAGCGCATTGTGGCAACTCTA
CCATATATCAAGCAAGAAGTTCCCATCATTATTGTGTTCAGAGCATTAGGTTTTGTGTCC
GACAGAGATATTTTAGAACATATTATTTATGATTTTGAAGATCCAGAGATGATGGAAATG
GTTAAACCTTCTCTCGATGAAGCTTTTGTCATCCAAGAACAGAATGTTGCACTAAATTTC
ATTGGTTCACGAGGAGCAAAGCCTGGTGTTACTAAAGAGAAAAGAATTAAATATGCAAAG
GAAGTTTTACAAAAAGAAATGCTCCCTCATGTTGGTGTCAGTGATTTTTGTGAGACCAAA
AAAGCCTATTTCTTGGGATACATGGTTCATAGGTTACTTCTGGCAGCTTTGGGTAGAAGA
GAACTAGATGACAGAGATCACTATGGAAACAAGAGATTGGATCTTGCTGGGCCGCTGCTT
GCATTCTTATTTAGAGGTATGTTTAAGAATTTGCTTAAAGAAGTGCGGATCTATGCACAG
AAATTTATTGATCGAGGAAAGGATTTTAACTTGGAGTTGGCAATTAAAACACGGATCATA
TCTGATGGCCTAAAATACTCTTTAGCTACTGGAAACTGGGGTGATCAAAAGAAAGCTCAT
CAAGCCAGAGCTGGAGTATCTCAGGTGTTAAACCGCCTGACTTTTGCGTCTACTCTTTCT
CACCTGCGTCGTTTAAATTCTCCTATTGGTAGAGACGGCAAGCTAGCAAAACCAAGACAG
TTGCATAATACGTTGTGGGGAATGGTGTGTCCTGCCGAGACCCCAGAGGGCCATGCTGTA
GGACTTGTGAAGAATTTAGCCTTGATGGCGTATATTTCAGTTGGATCTCAACCATCTCCA
ATTCTGGAATTTTTAGAAGAATGGAGTATGGAAAATTTAGAAGAAATTTCTCCTGCAGCT
ATTGCTGATGCAACCAAGATTTTTGTTAATGGCTGCTGGGTTGGAATACATAAAGATCCC
GAACAACTTATGAACACCCTAAGGAAATTGAGACGTCAGATGGACATCATTGTGTCTGAA
GTTTCTATGATCAGAGATATTCGAGAGAGGGAGATTCGGATCTATACGGATGCAGGCCGT
ATTTGTAGACCACTTCTGATTGTGGAAAAACAAAAGCTACTTTTGAAGAAGAGGCATATT
GACCAATTGAAAGAGAGAGAATATAACAACTATAGTTGGCAGGATCTTGTGGCCAGTGGG
GTAGTGGAGTATATTGATACCCTGGAAGAAGAAACAGTGATGCTTGCAATGACTCCAGAT
GATTTACAGGAGAAAGAAGTAGCTTATTGTTCCACATATACACACTGTGAGATTCATCCC
TCAATGATCCTTGGTGTCTGTGCATCTATTATTCCCTTTCCTGATCATAACCAGTCCCCT
AGAAACACATACCAGTCTGCTATGGGTAAGCAGGCTATGGGAGTTTACATCACCAACTTC
CATGTTCGCATGGACACATTGGCCCATGTTCTCTATTATCCTCAAAAGCCACTTGTGACT
ACACGGTCTATGGAATATCTACGATTTAGAGAGCTGCCAGCAGGCATCAACTCAATTGTG
GCCATTGCATCATACACTGGATATAATCAGGAAGACTCTGTTATCATGAATCGTTCAGCT
GTAGACCGCGGCTTCTTCAGGTCTGTTTTCTATCGCTCATACAAAGAACAGGAGTCTAAA
AAAGGATTTGATCAAGAAGAAGTTTTTGAGAAGCCTACACGTGAAACATGCCAGGGCATG
AGGCATGCCATTTACGACAAGCTGGATGATGATGGTTTGATAGCTCCAGGGGTTCGTGTA
TCAGGAGATGATGTTATTATAGGCAAAACAGTCACCTTGCCTGAAAATGAAGATGAATTG
GAGAGCACCAATAGACGCTATACCAAGAGAGACTGTAGCACTTTTCTCAGAACTAGTGAG
ACGGGCATTGTGGATCAGGTTATGGTAACTCTCAATCAGGAAGGATATAAATTTTGTAAA
ATAAGGGTACGCTCTGTTAGGATTCCACAGATTGGAGACAAATTTGCTAGTCGACATGGT
CAAAAGGGTACTTGTGGTATTCAGTATAGACAAGAGGATATGCCTTTCACCTGTGAAGGT
ATCACCCCTGATATCATCATCAATCCCCATGCCATCCCCTCTCGTATGACTATTGGTCAC
TTAATTGAATGCCTTCAAGGGAAGGTATCGGCTAACAAGGGTGAAATTGGTGATGCCACT
CCATTTAATGATGCTGTTAACGTGCAGAAGATTTCTAATCTTTTATCTGATTATGGCTAT
CATCTCAGAGGAAATGAGGTCCTGTACAATGGGTTCACTGGTCGAAAAATCACATCACAA
ATATTTATTGGCCCCACTTATTACCAGCGTTTGAAGCATATGGTGGATGATAAGATTCAC
TCTCGTGCTAGGGGACCTATTCAGATCCTCAATAGACAGCCCATGGAGGGTAGATCTCGT
GATGGTGGCCTGCGTTTTGGAGAAATGGAACGAGATTGTCAGATTGCCCATGGAGCAGCC
CAGTTTTTAAGGGAAAGATTGTTTGAGGCATCAGATCCATATCAGGTTCATGTTTGCAAT
CTTTGTGGAATAATGGCGATTGCCAACACCAGGACCCATACATATGAATGCAGGGGCTGC
CGCAATAAAACCCAGATTTCTTTGGTGCGAATGCCTTACGCATGCAAACTATTGTTTCAG
GAACTTATGTCTATGAGTATTGCACCGCGAATGATGAGTGTTTAG
Enzyme 28 GenBank Gene ID X63563 Link Image
Enzyme 28 GeneCard ID POLR2B Link Image
Enzyme 28 GenAtlas ID POLR2B Link Image
Enzyme 28 HGNC ID HGNC:9188 Link Image
Enzyme 28 Chromosome Location 4
Enzyme 28 Locus 4q12
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Acker J, Wintzerith M, Vigneron M, Kedinger C: Primary structure of the second largest subunit of human RNA polymerase II (or B). J Mol Biol. 1992 Aug 20;226(4):1295-9. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed Link Image]
  5. Kershnar E, Wu SY, Chiang CM: Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes. J Biol Chem. 1998 Dec 18;273(51):34444-53. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 6014
Enzyme 29 Name DNA-directed RNA polymerase II subunit RPB1
Enzyme 29 Synonyms
  1. RNA polymerase II subunit B1
  2. DNA-directed RNA polymerase II subunit A
  3. DNA-directed RNA polymerase III largest subunit
  4. RNA-directed RNA polymerase II subunit RPB1
Enzyme 29 Gene Name POLR2A
Enzyme 29 Protein Sequence >DNA-directed RNA polymerase II subunit RPB1
MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDP
RQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVD
SNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKG
HGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEP
RYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAA
HVIAEDVKLLQFHVATMVDNELPGLPRAMQKSGRPLKSLKQRLKGKEGRVRGNLMGKRVD
FSARTVITPDPNLSIDQVGVPRSIAANMTFAEIVTPFNIDRLQELVRRGNSQYPGAKYII
RDNGDRIDLRFHPKPSDLHLQTGYKVERHMCDGDIVIFNRQPTLHKMSMMGHRVRILPWS
TFRLNLSVTTPYNADFDGDEMNLHLPQSLETRAEIQELAMVPRMIVTPQSNRPVMGIVQD
TLTAVRKFTKRDVFLERGEVMNLLMFLSTWDGKVPQPAILKPRPLWTGKQIFSLIIPGHI
NCIRTHSTHPDDEDSGPYKHISPGDTKVVVENGELIMGILCKKSLGTSAGSLVHISYLEM
GHDITRLFYSNIQTVINNWLLIEGHTIGIGDSIADSKTYQDIQNTIKKAKQDVIEVIEKA
HNNELEPTPGNTLRQTFENQVNRILNDARDKTGSSAQKSLSEYNNFKSMVVSGAKGSKIN
ISQVIAVVGQQNVEGKRIPFGFKHRTLPHFIKDDYGPESRGFVENSYLAGLTPTEFFFHA
MGGREGLIDTAVKTAETGYIQRRLIKSMESVMVKYDATVRNSINQVVQLRYGEDGLAGES
VEFQNLATLKPSNKAFEKKFRFDYTNERALRRTLQEDLVKDVLSNAHIQNELEREFERMR
EDREVLRVIFPTGDSKVVLPCNLLRMIWNAQKIFHINPRLPSDLHPIKVVEGVKELSKKL
VIVNGDDPLSRQAQENATLLFNIHLRSTLCSRRMAEEFRLSGEAFDWLLGEIESKFNQAI
AHPGEMVGALAAQSLGEPATQMTLNTFHYAGVSAKNVTLGVPRLKELINISKKPKTPSLT
VFLLGQSARDAERAKDILCRLEHTTLRKVTANTAIYYDPNPQSTVVAEDQEWVNVYYEMP
DFDVARISPWLLRVELDRKHMTDRKLTMEQIAEKINAGFGDDLNCIFNDDNAEKLVLRIR
IMNSDENKMQEEEEVVDKMDDDVFLRCIESNMLTDMTLQGIEQISKVYMHLPQTDNKKKI
IITEDGEFKALQEWILETDGVSLMRVLSEKDVDPVRTTSNDIVEIFTVLGIEAVRKALER
ELYHVISFDGSYVNYRHLALLCDTMTCRGHLMAITRHGVNRQDTGPLMKCSFEETVDVLM
EAAAHGESDPMKGVSENIMLGQLAPAGTGCFDLLLDAEKCKYGMEIPTNIPGLGAAGPTG
MFFGSAPSPMGGISPAMTPWNQGATPAYGAWSPSVGSGMTPGAAGFSPSAASDASGFSPG
YSPAWSPTPGSPGSPGPSSPYIPSPGGAMSPSYSPTSPAYEPRSPGGYTPQSPSYSPTSP
SYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSP
TSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPS
YSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPT
SPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPASPKYTPTSPSYSPSSPEYTPTSPKY
SPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTS
PKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSPAISPDDSDEEN
Enzyme 29 Number of Residues 1970
Enzyme 29 Molecular Weight 217174.2
Enzyme 29 Theoretical pI 7.38
Enzyme 29 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
  • transcription from RNA polymerase II promoter
  • transcription, DNA-dependent
Component
  • DNA-directed RNA polymerase II, core complex
  • intracellular organelle part
  • nuclear part
  • nucleoplasm part
  • organelle part
Enzyme 29 General Function Involved in DNA binding
Enzyme 29 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing. Acts as a RNA- dependent RNA polymerase when associated with small delta antigen of Hepatitis delta virus, acting both as a replicate and transcriptase for the viral RNA circular genome
Enzyme 29 Pathways
Enzyme 29 Reactions
  • nucleoside triphosphate + RNAn = diphosphate + RNAn+1 [RN:R00444]
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 36124 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID P24928 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name RPB1_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >5913 bp
ATGCACGGGGGTGGCCCCCCCTCGGGGGACAGCGCATGCCCGCTGCGCACCATCAAGAGA
GTCCAGTTCGGAGTCCTGAGTCCGGATGAACTGAAGCGAATGTCTGTGACGGAGGGTGGC
ATCAAATACCCAGAGACGACTGAGGGAGGCCGCCCCAAGCTTGGGGGGCTGATGGACCCG
AGGCAGGGGGTGATTGAGCGGACTGGCCGCTGCCAAACATGTGCAGGAAACATGACAGAG
TGTCCTGGCCACTTTGGCCACATTGAACTGGCCAAGCCTGTGTTTCACGTGGGCTTCCTG
GTGAAGACAATGAAAGTTTTGCGCTGTGTCTGCTTCTTCTGCTCCAAACTGCTTGTGGAC
TCTAACAACCCAAAGATCAAGGATATCCTGGCTAAGTCCAAGGGACAGCCCAAGAAGCGG
CTCACACATGTCTACGACCTTTGCAAGGGCAAAAACATATGCGAGGGTGGGGAGGAGATG
GACAACAAGTTCGGTGTGGAACAACCTGAGGGTGACGAGGATCTGACCAAAGAAAAGGGC
CATGGTGGCTGTGGGCGGTACCAGCCCAGGATCCGGCGTTCTGGCCTAGAGCTGTATGCG
GAATGGAAGCACGTTAATGAGGACTCTCAGGAGAAGAAGATCCTGCTGAGTCCAGAGCGA
GTGCATGAGATCTTCAAACGCATCTCAGATGAGGAGTGTTTTGTGCTGGGCATGGAGCCC
CGCTATGCACGGCCAGAGTGGATGATTGTCACAGTGCTGCCTGTGCCCCCGCTCTCCGTG
CGGCCTGCTGTTGTGATGCAGGGCTCTGCCCGTAACCAGGATGACCTGACTCACAAACTG
GCTGACATCGTGAAGATCAACAATCAGCTGCGGCGCAATGAGCAGAACGGCGCAGCGGCC
CATGTCATTGCAGAGGATGTGAAGCTCCTCCAGTTCCATGTGGCCACCATGGTGGACAAT
GAGCTGCCTGGCTTGCCCCGTGCCATGCAGAAGTCTGGGCGTCCCCTCAAGTCCCTGAAG
CAGCGGTTGAAGGGCAAGGAAGGCCGGGTGCGAGGGAACCTGATGGGCAAAAGAGTGGAC
TTCTCGGCCCGTACTGTCATCACCCCCGACCCCAACCTCTCCATTGACCAGGTTGGCGTG
CCCCGCTCCATTGCTGCCAACATGACCTTTGCGGAGATTGTCACCCCCTTCAACATTGAC
AGACTTCAAGAACTAGTGCGCAGGGGGAACAGTCAGTACCCAGGCGCCAAGTACATCATC
CGAGACAATGGTGATCGCATTGACTTGCGTTTCCACCCCAAGCCCAGTGACCTTCACCTG
CAGACCGGCTATAAGGTGGAACGGCACATGTGTGATGGGGACATTGTTATCTTCAACCGG
CAGCCAACTCTGCACAAAATGTCCATGATGGGGCATCGGGTCCGCATTCTCCCATGGTCT
ACCTTTCGCTTGAATCTTAGCGTGACAACTCCGTACAATGCAGACTTTGACGGGGATGAG
ATGAACTTGCACCTGCCACAGTCTCTGGAGACGCGAGCAGAGATCCAGGAGCTGGCCATG
GTTCCTCGCATGATTGTCACCCCCCAGAGCAATCGGCCTGTCATGGGTATTGTGCAGGAC
ACACTCACAGCAGTGCGCAAATTCACCAAGAGAGACGTCTTCCTGGAGCGGGGTGAAGTG
ATGAACCTCCTGATGTTCCTGTCGACGTGGGATGGGAAGGTCCCACAGCCGGCCATCCTA
AAGCCCCGGCCCCTGTGGACAGGCAAGCAAATCTTCTCCCTCATCATACCTGGTCACATC
AATTGTATCCGTACCCACAGCACCCATCCCGATGATGAAGACAGTGGCCCTTACAAGCAC
ATCTCTCCTGGGGACACCAAGGTGGTGGTGGAGAATGGGGAGCTGATCATGGGCATCCTG
TGTAAGAAGTCTCTGGGCACGTCAGCTGGCTCCCTGGTCCACATCTCCTACCTAGAGATG
GGTCATGACATCACTCGCCTCTTCTACTCCAACATTCAGACTGTCATTAACAACTGGCTC
CTCATCGAGGGTCATACTATTGGCATTGGGGACTCCATTGCTGATTCTAAGACTTACCAG
GACATTCAGAACACTATTAAGAAGGCCAAGCAGGACGTAATAGAGGTCATCGAGAAGGCA
CACAACAATGAGCTGGAGCCCACCCCAGGGAACACTCTGCGGCAGACGTTTGAGAATCAG
GTGAACCGCATTCTTAACGATGCCCGAGACAAGACTGGCTCCTCTGCTCAGAAATCCCTG
TCTGAATACAACAACTTCAAGTCTATGGTCGTGTCCGGAGCTAAAGGTTCCAAGATTAAC
ATCTCCCAGGTCATTGCTGTCGTTGGACAGCAGAACGTCGAGGGCAAGCGGATTCCATTT
GGCTTCAAGCACCGGACTCTGCCTCACTTCATCAAGGATGACTACGGGCCTGAGAGCCGT
GGCTTTGTGGAGAACTCCTACCTAGCCGGCCTCACACCCACTGAGTTCTTTTTCCACGCC
ATGGGGGGTCGTGAGGGGCTCATTGACACGGCTGTCAAGACTGCTGAGACTGGATACATC
CAGCGGCGGCTGATCAAGTCCATGGAGTCAGTGATGGTGAAGTACGACGCGACTGTGCGG
AACTCCATCAACCAGGTGGTGCAGCTGCGCTACGGCGAAGACGGCCTGGCAGGCGAGAGC
GTTGAGTTCCAGAACCTGGCTACGCTTAAGCCTTCCAACAAGGCTTTTGAGAAGAAGTTC
CGCTTTGATTATACCAATGAGAGGGCCCTGCGGCGCACTCTGCAGGAGGACCTGGTGAAG
GACGTGCTGAGCAACGCACACATCCAGAACGAGTTGGAGCGGGAATTTGAGCGGATGCGG
GAGGATCGGGAGGTGCTCAGGGTCATCTTCCCAACTGGAGACAGCAAGGTCGTCCTCCCC
TGTAACCTGCTGCGGATGATCTGGAATGCTCAGAAAATCTTCCACATCAACCCACGCCTT
CCCTCCGACCTGCACCCCATCAAAGTGGTGGAGGGAGTCAAGGAATTGAGCAAGAAGCTG
GTGATTGTGAATGGGGATGACCCACTAAGTCGACAGGCCCAGGAAAATGCCACGCTGCTC
TTCAACATCCACCTGCGGTCCACGTTGTGTTCCCGCCGCATGGCAGAGGAGTTTCGGCTC
AGTGGGGAGGCCTTCGACTGGCTGCTTGGGGAGATTGAGTCCAAGTTCAACCAAGCCATT
GCGCATCCCGGGGAAATGGTGGGGGCTCTGGCTGCGCAGTCCCTTGGAGAACCTGCCACC
CAGATGACCTTGAATACCTTCCACTATGCTGGTGTGTCTGCCAAGAATGTGACGCTGGGT
GTGCCCCGACTTAAGGAGCTCATCAACATTTCCAAGAAGCCAAAGACTCCTTCGCTTACT
GTCTTCCTGTTGGGCCAGTCCGCTCGAGATGCTGAGAGAGCCAAGGATATTCTGTGCCGT
CTGGAGCATACAACGTTGAGGAAGGTGACTGCCAACACAGCCATCTACTATGACCCCAAC
CCCCAGAGCACGGTGGTGGCAGAGGATCAGGAATGGGTGAATGTCTACTATGAAATGCCT
GACTTTGATGTGGCCCGAATCTCCCCCTGGCTGTTGCGGGTGGAGCTGGATCGGAAGCAC
ATGACTGACCGGAAGCTCACCATGGAGCAGATTGCTGAAAAGATCAATGCTGGTTTTGGT
GACGACTTGAACTGCATCTTTAATGATGACAATGCAGAGAAGCTGGTGCTCCGTATTCGC
ATCATGAACAGCGATGAGAACAAGATGCAAGAGGAGGAAGAGGTGGTGGACAAGATGGAT
GATGATGTCTTCCTGCGCTGCATCGAGTCCAACATGCTGACAGATATGACCCTGCAGGGC
ATCGAGCAGATCAGCAAGGTGTACATGCACTTGCCACAGACAGACAACAAGAAGAAGATC
ATCATCACGGAGGATGGGGAATTCAAGGCCCTGCAGGAGTGGATCCTGGAGACGGACGGC
GTGAGCTTGATGCGGGTGCTGAGTGAGAAGGACGTGGACCCCGTACGCACCACGTCCAAT
GACATTGTGGAGATCTTCACGGTGCTGGGCATTGAAGCCGTGCGGAAGGCCCTGGAGCGG
GAGCTGTACCACGTCATCTCCTTTGATGGCTCCTATGTCAATTACCGACACTTGGCTCTC
TTGTGTGATACCATGACCTGTCGTGGCCACTTGATGGCCATCACCCGACACGGAGTCAAC
CGCCAGGACACAGGACCACTCATGAAGTGTTCCTTTGAGGAAACGGTGGACGTGCTTATG
GAAGCAGCCGCACACGGTGAGAGTGACCCCATGAAGGGGGTCTCTGAGAATATCATGCTG
GGCCAGCTGGCTCCGGCCGGCACTGGCTGCTTTGACCTCCTGCTTGATGCAGAGAAGTGC
AAGTATGGCATGGAGATCCCCACCAATATCCCCGGCCTGGGGGCTGCTGGACCCACCGGC
ATGTTCTTTGGTTCAGCACCCAGTCCCATGGGTGGAATCTCTCCTGCCATGACACCTTGG
AACCAGGGTGCAACCCCTGCCTATGGCGCCTGGTCCCCCAGTGTTGGGAGTGGAATGACC
CCAGGGGCAGCCGGTTTCTCTCCCAGTGCTGCGTCAGATGCCAGCGGCTTCAGCCCAGGT
TACTCCCCTGCCTGGTCTCCCACACCGGGCTCCCCGGGGTCCCCAGGTCCCTCAAGCCCC
TACATCCCTTCACCAGGTGGCGCCATGTCTCCCAGCTACTCGCCAACGTCACCTGCCTAC
GAGCCCCGCTCTCCTGGGGGCTACACACCCCAGAGTCCCTCTTATTCCCCCACTTCACCC
TCCTACTCCCCTACCTCTCCATCCTATTCTCCAACCAGTCCCAACTATAGTCCCACATCA
CCCAGCTATTCGCCAACGTCACCCAGCTACTCACCGACCTCTCCCAGCTACTCACCCACC
TCTCCCAGCTACTCGCCCACCTCTCCCAGCTATTCGCCCACCTCTCCCAGCTACTCACCC
ACTTCCCCTAGCTATTCGCCCACTTCCCCTAGCTACTCGCCAACGTCTCCCAGCTACTCG
CCGACATCTCCCAGCTACTCGCCAACTTCACCCAGCTATTCTCCCACTTCTCCCAGCTAC
TCACCTACCTCTCCAAGCTATTCACCCACCTCCCCCAGCTACTCACCCACTTCCCCAAGT
TACTCACCCACCAGCCCGAACTATTCTCCAACCAGTCCCAATTACACCCCAACATCACCC
AGCTACAGCCCGACATCACCCAGCTATTCCCCTACTAGTCCCAACTACACACCTACCAGC
CCTAACTACAGCCCAACCTCTCCAAGCTACTCTCCAACATCACCCAGCTATTCCCCGACC
TCACCAAGTTACTCCCCTTCCAGCCCACGATACACACCACAGTCTCCAACCTATACCCCA
AGCTCACCCAGCTACAGCCCCAGTTCGCCCAGCTACAGCCCAACCTCACCCAAGTACACC
CCAACCAGTCCTTCTTATAGTCCCAGCTCCCCAGAGTATACCCCAACCTCTCCCAAGTAC
TCACCTACCAGTCCCAAATATTCACCCACCTCTCCCAAGTACTCGCCTACCAGTCCCACC
TATTCACCCACCACCCCAAAATACTCCCCAACATCTCCTACTTATTCCCCAACCTCTCCA
GTCTACACCCCAACCTCTCCCAAGTACTCACCTACTAGCCCCACTTACTCGCCCACTTCC
CCCAAGTACTCGCCCACCAGCCCCACCTACTCGCCCACCTCCCCCAAAGGCTCAACCTAC
TCTCCCACTTCCCCTGGTTACTCGCCCACCAGCCCCACCTACAGTCTCACAAGCCCGGCT
ATCAGCCCGGATGACAGTGACGAGGAGAACTGA
Enzyme 29 GenBank Gene ID X63564 Link Image
Enzyme 29 GeneCard ID POLR2A Link Image
Enzyme 29 GenAtlas ID POLR2A Link Image
Enzyme 29 HGNC ID HGNC:9187 Link Image
Enzyme 29 Chromosome Location 1
Enzyme 29 Locus 17p13.1
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Wintzerith M, Acker J, Vicaire S, Vigneron M, Kedinger C: Complete sequence of the human RNA polymerase II largest subunit. Nucleic Acids Res. 1992 Feb 25;20(4):910. [PubMed Link Image]
  2. Mita K, Tsuji H, Morimyo M, Takahashi E, Nenoi M, Ichimura S, Yamauchi M, Hongo E, Hayashi A: The human gene encoding the largest subunit of RNA polymerase II. Gene. 1995 Jul 4;159(2):285-6. [PubMed Link Image]
  3. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Kershnar E, Wu SY, Chiang CM: Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes. J Biol Chem. 1998 Dec 18;273(51):34444-53. [PubMed Link Image]
  6. Nayler O, Stratling W, Bourquin JP, Stagljar I, Lindemann L, Jasper H, Hartmann AM, Fackelmayer FO, Ullrich A, Stamm S: SAF-B protein couples transcription and pre-mRNA splicing to SAR/MAR elements. Nucleic Acids Res. 1998 Aug 1;26(15):3542-9. [PubMed Link Image]
  7. Parada CA, Roeder RG: A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription. EMBO J. 1999 Jul 1;18(13):3688-701. [PubMed Link Image]
  8. Kim JB, Yamaguchi Y, Wada T, Handa H, Sharp PA: Tat-SF1 protein associates with RAP30 and human SPT5 proteins. Mol Cell Biol. 1999 Sep;19(9):5960-8. [PubMed Link Image]
  9. Allen M, Friedler A, Schon O, Bycroft M: The structure of an FF domain from human HYPA/FBP11. J Mol Biol. 2002 Oct 25;323(3):411-6. [PubMed Link Image]
  10. Carty SM, Greenleaf AL: Hyperphosphorylated C-terminal repeat domain-associating proteins in the nuclear proteome link transcription to DNA/chromatin modification and RNA processing. Mol Cell Proteomics. 2002 Aug;1(8):598-610. [PubMed Link Image]
  11. Yang L, Li N, Wang C, Yu Y, Yuan L, Zhang M, Cao X: Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved in pre-mRNA splicing and induces apoptosis of human hepatocellular carcinoma cells. J Biol Chem. 2004 Mar 19;279(12):11639-48. Epub 2003 Dec 17. [PubMed Link Image]
  12. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  13. Katsarou ME, Papakyriakou A, Katsaros N, Scorilas A: Expression of the C-terminal domain of novel human SR-A1 protein: interaction with the CTD domain of RNA polymerase II. Biochem Biophys Res Commun. 2005 Aug 19;334(1):61-8. [PubMed Link Image]
  14. Sun XJ, Wei J, Wu XY, Hu M, Wang L, Wang HH, Zhang QH, Chen SJ, Huang QH, Chen Z: Identification and characterization of a novel human histone H3 lysine 36-specific methyltransferase. J Biol Chem. 2005 Oct 21;280(42):35261-71. Epub 2005 Aug 22. [PubMed Link Image]
  15. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  16. Li M, Phatnani HP, Guan Z, Sage H, Greenleaf AL, Zhou P: Solution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1. Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17636-41. Epub 2005 Nov 28. [PubMed Link Image]
  17. Moniaux N, Nemos C, Schmied BM, Chauhan SC, Deb S, Morikane K, Choudhury A, Vanlith M, Sutherlin M, Sikela JM, Hollingsworth MA, Batra SK: The human homologue of the RNA polymerase II-associated factor 1 (hPaf1), localized on the 19q13 amplicon, is associated with tumorigenesis. Oncogene. 2006 Jun 1;25(23):3247-57. Epub 2006 Feb 20. [PubMed Link Image]
  18. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  19. Haline-Vaz T, Silva TC, Zanchin NI: The human interferon-regulated ISG95 protein interacts with RNA polymerase II and shows methyltransferase activity. Biochem Biophys Res Commun. 2008 Aug 8;372(4):719-24. Epub 2008 Jun 3. [PubMed Link Image]
  20. Becker R, Loll B, Meinhart A: Snapshots of the RNA processing factor SCAF8 bound to different phosphorylated forms of the carboxyl-terminal domain of RNA polymerase II. J Biol Chem. 2008 Aug 15;283(33):22659-69. Epub 2008 Jun 11. [PubMed Link Image]
  21. Chang J, Nie X, Chang HE, Han Z, Taylor J: Transcription of hepatitis delta virus RNA by RNA polymerase II. J Virol. 2008 Feb;82(3):1118-27. Epub 2007 Nov 21. [PubMed Link Image]
  22. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  23. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  24. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  25. Zhang Y, Kim Y, Genoud N, Gao J, Kelly JW, Pfaff SL, Gill GN, Dixon JE, Noel JP: Determinants for dephosphorylation of the RNA polymerase II C-terminal domain by Scp1. Mol Cell. 2006 Dec 8;24(5):759-70. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 6017
Enzyme 30 Name DNA-directed RNA polymerase, mitochondrial
Enzyme 30 Synonyms
  1. MtRPOL
Enzyme 30 Gene Name POLRMT
Enzyme 30 Protein Sequence >DNA-directed RNA polymerase, mitochondrial
MSALCWGRGAAGLKRALRPCGRPGLPGKEGTAGGVCGPRRSSSASPQEQDQDRRKDWGHV
ELLEVLQARVRQLQAESVSEVVVNRVDVARLPECGSGDGSLQPPRKVQMGAKDATPVPCG
RWAKILEKDKRTQQMRMQRLKAKLQMPFQSGEFKALTRRLQVEPRLLSKQMAGCLEDCTR
QAPESPWEEQLARLLQEAPGKLSLDVEQAPSGQHSQAQLSGQQQRLLAFFKCCLLTDQLP
LAHHLLVVHHGQRQKRKLLTLDMYNAVMLGWARQGAFKELVYVLFMVKDAGLTPDLLSYA
AALQCMGRQDQDAGTIERCLEQMSQEGLKLQALFTAVLLSEEDRATVLKAVHKVKPTFSL
PPQLPPPVNTSKLLRDVYAKDGRVSYPKLHLPLKTLQCLFEKQLHMELASRVCVVSVEKP
TLPSKEVKHARKTLKTLRDQWEKALCRALRETKNRLEREVYEGRFSLYPFLCLLDEREVV
RMLLQVLQALPAQGESFTTLARELSARTFSRHVVQRQRVSGQVQALQNHYRKYLCLLASD
AEVPEPCLPRQYWEELGAPEALREQPWPLPVQMELGKLLAEMLVQATQMPCSLDKPHRSS
RLVPVLYHVYSFRNVQQIGILKPHPAYVQLLEKAAEPTLTFEAVDVPMLCPPLPWTSPHS
GAFLLSPTKLMRTVEGATQHQELLETCPPTALHGALDALTQLGNCAWRVNGRVLDLVLQL
FQAKGCPQLGVPAPPSEAPQPPEAHLPHSAAPARKAELRRELAHCQKVAREMHSLRAEAL
YRLSLAQHLRDRVFWLPHNMDFRGRTYPCPPHFNHLGSDVARALLEFAQGRPLGPHGLDW
LKIHLVNLTGLKKREPLRKRLAFAEEVMDDILDSADQPLTGRKWWMGAEEPWQTLACCME
VANAVRASDPAAYVSHLPVHQDGSCNGLQHYAALGRDSVGAASVNLEPSDVPQDVYSGVA
AQVEVFRRQDAQRGMRVAQVLEGFITRKVVKQTVMTVVYGVTRYGGRLQIEKRLRELSDF
PQEFVWEASHYLVRQVFKSLQEMFSGTRAIQHWLTESARLISHMGSVVEWVTPLGVPVIQ
PYRLDSKVKQIGGGIQSITYTHNGDISRKPNTRKQKNGFPPNFIHSLDSSHMMLTALHCY
RKGLTFVSVHDCYWTHAADVSVMNQVCREQFVRLHSEPILQDLSRFLVKRFCSEPQKILE
ASQLKETLQAVPKPGAFDLEQVKRSTYFFS
Enzyme 30 Number of Residues 1230
Enzyme 30 Molecular Weight 138619.3
Enzyme 30 Theoretical pI 9.25
Enzyme 30 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
Component
Enzyme 30 General Function Involved in DNA binding
Enzyme 30 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Enzyme 30 Pathways
Enzyme 30 Reactions
  • nucleoside triphosphate + RNAn = diphosphate + RNAn+1 [RN:R00444]
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 2979529 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID O00411 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name RPOM_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >3693 bp
ATGTCGGCACTTTGCTGGGGCCGCGGAGCGGCGGGGCTCAAACGAGCCCTACGGCCTTGC
GGCCGCCCGGGACTCCCCGGCAAAGAAGGGACCGCCGGTGGCGTCTGCGGCCCCAGGAGG
AGCTCGTCCGCCAGCCCCCAGGAGCAAGACCAAGACCGCAGGAAGGACTGGGGCCACGTG
GAGCTGCTGGAGGTGCTCCAGGCGCGGGTGCGGCAGCTGCAGGCTGAGAGCGTGTCGGAG
GTGGTGGTGAACAGGGTGGATGTGGCGCGGCTCCCAGAATGTGGCAGTGGAGATGGTAGC
CTCCAGCCACCCAGGAAGGTCCAGATGGGGGCCAAGGATGCCACCCCGGTGCCCTGTGGC
CGCTGGGCAAAGATACTGGAGAAGGATAAGCGGACCCAGCAGATGCGTATGCAGCGGTTG
AAGGCGAAGCTGCAGATGCCATTCCAGAGCGGGGAGTTCAAGGCGCTGACCAGGCGCCTG
CAGGTGGAGCCCCGGCTCCTGAGCAAGCAGATGGCCGGGTGCCTGGAGGACTGCACGCGC
CAGGCCCCCGAGAGCCCCTGGGAGGAGCAGCTGGCCCGGCTGCTGCAGGAGGCCCCTGGG
AAGCTGAGCCTCGATGTGGAGCAGGCCCCGTCGGGGCAGCACTCGCAGGCCCAGCTCTCA
GGTCAGCAGCAGAGGCTCCTGGCCTTCTTCAAGTGCTGCCTGCTCACTGACCAGCTGCCC
CTCGCCCACCACCTGCTGGTCGTCCACCACGGCCAGCGGCAGAAGCGGAAGCTGCTCACG
CTGGACATGTACAACGCCGTGATGCTTGGCTGGGCGCGGCAGGGTGCCTTCAAGGAGCTG
GTATATGTGTTATTCATGGTGAAGGATGCCGGCTTGACTCCGGACCTGCTGTCCTATGCG
GCTGCCCTCCAGTGCATGGGGAGGCAGGACCAGGACGCCGGGACCATCGAAAGGTGTCTG
GAACAGATGAGCCAGGAGGGGCTGAAGCTGCAGGCACTCTTCACCGCCGTTCTGCTGTCT
GAGGAGGATCGGGCCACTGTTCTGAAGGCCGTGCACAAGGTGAAGCCCACCTTCAGCCTC
CCGCCGCAGCTGCCGCCCCCGGTCAACACCTCCAAGCTGCTCAGGGACGTGTATGCCAAG
GATGGGCGTGTGTCCTACCCGAAGCTGCACCTGCCCTTGAAGACCCTGCAGTGCCTCTTT
GAGAAGCAGCTCCACATGGAGCTGGCCAGCAGGGTGTGCGTGGTGTCCGTGGAGAAGCCC
ACGTTGCCAAGCAAGGAGGTCAAGCACGCGCGGAAGACCCTGAAGACCCTGCGGGACCAA
TGGGAGAAAGCACTGTGCCGGGCGCTGCGGGAGACCAAGAACCGCCTAGAGCGCGAGGTG
TACGAGGGCCGGTTCTCACTTTACCCCTTCCTGTGCCTGCTGGACGAGCGCGAGGTGGTG
CGGATGCTCCTGCAGGTCCTGCAGGCGCTGCCCGCCCAAGGTGAGTCCTTCACCACCCTG
GCCCGGGAGCTGAGTGCGCGCACTTTCAGCCGGCACGTGGTGCAGAGGCAGCGGGTCAGT
GGCCAGGTGCAGGCGCTGCAGAACCACTACAGGAAGTACCTCTGCTTGCTGGCCTCCGAC
GCCGAGGTGCCCGAGCCCTGCCTGCCGCGGCAGTACTGGGAGGAGCTGGGGGCGCCCGAG
GCCCTGCGGGAGCAGCCCTGGCCCCTGCCAGTGCAGATGGAGCTGGGCAAGCTGCTGGCG
GAGATGCTGGTGCAGGCTACGCAGATGCCATGCAGCCTGGACAAGCCGCATCGTTCCTCT
CGGCTTGTCCCCGTGCTCTACCACGTGTATTCCTTCCGCAACGTCCAGCAGATCGGCATC
CTGAAGCCGCACCCGGCCTACGTGCAGCTGCTGGAGAAGGCCGCGGAGCCCACGCTGACC
TTCGAGGCGGTGGATGTACCCATGCTTTGCCCCCCGCTGCCCTGGACATCGCCGCACTCT
GGTGCTTTCCTGCTCAGCCCCACCAAGCTGATGCGCACGGTGGAAGGCGCCACGCAGCAC
CAGGAGCTGCTGGAAACCTGCCCGCCCACCGCGCTGCATGGCGCACTGGACGCCCTCACC
CAACTGGGCAACTGCGCCTGGCGCGTCAACGGGCGCGTGCTGGACCTGGTGCTGCAGCTC
TTCCAGGCCAAGGGCTGCCCCCAGCTAGGCGTGCCGGCCCCGCCCTCCGAGGCGCCCCAG
CCGCCCGAGGCCCACCTGCCGCACAGCGCCGCGCCCGCCCGCAAGGCCGAGCTGCGCCGT
GAGCTGGCGCACTGCCAGAAGGTGGCCCGGGAGATGCACAGCCTGCGGGCGGAGGCGCTG
TACCGCCTCTCGCTGGCGCAGCACCTGCGGGACCGCGTCTTCTGGCTGCCGCACAACATG
GACTTCCGCGGCCGCACCTACCCCTGCCCGCCGCACTTCAACCACCTGGGCAGCGACGTG
GCGCGGGCCCTGCTGGAGTTCGCCCAGGGCCGCCCGCTCGGCCCGCACGGCCTGGATTGG
CTCAAGATCCACCTGGTCAATCTCACGGGGTTGAAGAAGCGGGAGCCGCTGCGGAAGCGC
CTGGCCTTTGCGGAGGAGGTGATGGATGACATCCTGGACTCCGCGGACCAACCCTTGACG
GGCCGAAAGTGGTGGATGGGCGCGGAGGAACCCTGGCAGACGCTGGCCTGCTGTATGGAG
GTGGCGAACGCTGTGCGCGCCTCCGACCCTGCCGCCTATGTCTCCCACCTCCCCGTCCAT
CAGGACGGCTCTTGCAACGGCCTGCAGCATTATGCTGCTCTGGGCCGCGACAGCGTGGGC
GCCGCCTCCGTCAACCTGGAGCCCTCGGATGTGCCGCAGGACGTGTACAGCGGCGTGGCC
GCGCAGGTGGAGGTGTTCCGTAGGCAGGACGCCCAGCGGGGCATGCGGGTGGCACAGGTG
CTGGAAGGTTTCATCACCCGCAAGGTGGTGAAGCAGACGGTGATGACGGTGGTGTACGGG
GTCACGCGCTATGGCGGGCGCCTGCAGATTGAGAAGCGCCTCCGGGAGCTGAGCGACTTT
CCCCAGGAGTTCGTGTGGGAGGCCTCTCACTATCTCGTACGCCAGGTCTTCAAGAGTCTA
CAGGAGATGTTCTCGGGGACCCGGGCCATCCAGCACTGGCTGACCGAGAGTGCCCGCCTC
ATCTCCCACATGGGCTCTGTGGTGGAGTGGGTCACACCCCTGGGCGTCCCCGTCATCCAG
CCCTATCGCCTGGACTCCAAGGTCAAGCAAATAGGAGGTGGAATTCAGAGCATCACCTAC
ACCCACAACGGAGACATCAGCCGAAAGCCCAACACACGTAAGCAGAAGAACGGCTTCCCG
CCCAACTTCATCCACTCGCTGGACTCCTCCCACATGATGCTCACCGCCCTGCACTGCTAC
AGGAAGGGCCTGACCTTCGTCTCTGTGCACGACTGTTACTGGACTCACGCAGCTGATGTC
TCCGTCATGAACCAGGTGTGCCGGGAGCAGTTTGTCCGCTTGCACAGCGAGCCCATCCTG
CAGGACCTGTCCAGATTCCTGGTCAAGCGGTTCTGCTCTGAGCCCCAGAAGATCTTGGAG
GCCAGCCAGCTGAAGGAGACACTGCAGGCGGTGCCCAAGCCAGGGGCCTTCGACCTGGAG
CAGGTGAAGCGTTCCACCTACTTCTTCAGCTGA
Enzyme 30 GenBank Gene ID AC004449 Link Image
Enzyme 30 GeneCard ID POLRMT Link Image
Enzyme 30 GenAtlas ID POLRMT Link Image
Enzyme 30 HGNC ID HGNC:9200 Link Image
Enzyme 30 Chromosome Location 1
Enzyme 30 Locus 19p13.3
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Tiranti V, Savoia A, Forti F, D'Apolito MF, Centra M, Rocchi M, Zeviani M: Identification of the gene encoding the human mitochondrial RNA polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence Tags database. Hum Mol Genet. 1997 Apr;6(4):615-25. [PubMed Link Image]
  2. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  3. Falkenberg M, Gaspari M, Rantanen A, Trifunovic A, Larsson NG, Gustafsson CM: Mitochondrial transcription factors B1 and B2 activate transcription of human mtDNA. Nat Genet. 2002 Jul;31(3):289-94. Epub 2002 Jun 17. [PubMed Link Image]
  4. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 6018
Enzyme 31 Name DNA-directed RNA polymerase I subunit RPA2
Enzyme 31 Synonyms
  1. RNA polymerase I subunit 2
  2. DNA-directed RNA polymerase I 135 kDa polypeptide
  3. RPA135
Enzyme 31 Gene Name POLR1B
Enzyme 31 Protein Sequence >DNA-directed RNA polymerase I subunit RPA2
MDPGSRWRNLPSGPSLKHLTDPSYGIPREQQKAALQELTRAHVESFNYAVHEGLGLAVQA
IPPFEFAFKDERISFTILDAVISPPTVPKGTICKEANVYPAECRGRRSTYRGKLTADINW
AVNGISKGIIKQFLGYVPIMVKSKLCNLRNLPPQALIEHHEEAEEMGGYFIINGIEKVIR
MLIMPRRNFPIAMIRPKWKTRGPGYTQYGVSMHCVREEHSAVNMNLHYLENGTVMLNFIY
RKELFFLPLGFALKALVSFSDYQIFQELIKGKEDDSFLRNSVSQMLRIVMEEGCSTQKQV
LNYLGECFRVKLNVPDWYPNEQAAEFLFNQCICIHLKSNTEKFYMLCLMTRKLFALAKGE
CMEDNPDSLVNQEVLTPGQLFLMFLKEKLEGWLVSIKIAFDKKAQKTSVSMNTDNLMRIF
TMGIDLTKPFEYLFATGNLRSKTGLGLLQDSGLCVVADKLNFIRYLSHFRCVHRGADFAK
MRTTTVRRLLPESWGFLCPVHTPDGEPCGLMNHLTAVCEVVTQFVYTASIPALLCNLGVT
PIDGAPHRSYSECYPVLLDGVMVGWVDKDLAPGIADSLRHFKVLREKRIPPWMEVVLIPM
TGKPSLYPGLFLFTTPCRLVRPVQNLALGKEELIGTMEQIFMNVAIFEDEVFAGVTTHQE
LFPHSLLSVIANFIPFSDHNQSPRNMYQCQMGKQTMGFPLLTYQDRSDNKLYRLQTPQSP
LVRPSMYDYYDMDNYPIGTNAIVAVISYTGYDMEDAMIVNKASWERGFAHGSVYKSEFID
LSEKIKQGDSSLVFGIKPGDPRVLQKLDDDGLPFIGAKLQYGDPYYSYLNLNTGESFVMY
YKSKENCVVDNIKVCSNDTGSGKFKCVCITMRVPRNPTIGDKFASRHGQKGILSRLWPAE
DMPFTESGMVPDILFNPHGFPSRMTIGMLIESMAGKSAALHGLCHDATPFIFSEENSALE
YFGEMLKAAGYNFYGTERLYSGISGLELEADIFIGVVYYQRLRHMVSDKFQVRTTGARDR
VTNQPIGGRNVQGGIRFGEMERDALLAHGTSFLLHDRLFNCSDRSVAHVCVKCGSLLSPL
LEKPPPSWSAMRNRKYNCTLCSRSDTIDTVSVPYVFRYFVAELAAMNIKVKLDVV
Enzyme 31 Number of Residues 1135
Enzyme 31 Molecular Weight 128228.4
Enzyme 31 Theoretical pI 7.88
Enzyme 31 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleoside binding
  • nucleotidyltransferase activity
  • ribonucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 31 General Function Involved in DNA-directed RNA polymerase activity
Enzyme 31 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol I is composed of mobile elements and RPA2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft
Enzyme 31 Pathways
Enzyme 31 Reactions
  • nucleoside triphosphate + RNAn = diphosphate + RNAn+1 [RN:R00444]
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 62420281 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q9H9Y6 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name RPA2_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >3408 bp
ATGGATCCTGGCAGCCGGTGGCGGAACCTGCCCAGCGGGCCTAGCCTAAAGCACTTGACT
GACCCCTCTTATGGAATCCCGCGGGAACAGCAAAAGGCAGCGTTGCAGGAGCTGACGCGG
GCGCACGTGGAGTCCTTCAACTACGCTGTGCACGAGGGTCTCGGCCTCGCGGTGCAGGCT
ATACCTCCCTTTGAATTTGCTTTCAAAGATGAGCGTATCTCTTTTACTATTCTGGATGCT
GTTATCAGTCCACCTACAGTTCCAAAAGGGACCATCTGCAAAGAGGCCAATGTTTATCCA
GCAGAATGCCGGGGCCGAAGGAGTACCTACCGTGGGAAGTTGACAGCTGATATCAACTGG
GCAGTGAATGGAATCTCAAAAGGAATCATTAAGCAGTTTCTTGGCTATGTTCCCATCATG
GTGAAATCCAAGCTTTGCAACTTACGTAACCTTCCCCCACAAGCCCTCATTGAGCACCAT
GAGGAGGCAGAGGAAATGGGGGGCTATTTTATAATCAATGGCATTGAAAAAGTCATCCGA
ATGTTGATTATGCCTCGGAGAAATTTTCCCATTGCAATGATAAGACCAAAATGGAAAACC
AGAGGGCCTGGTTATACTCAGTATGGAGTTTCAATGCACTGTGTGAGGGAAGAACATTCC
GCTGTCAATATGAACCTCCACTACTTGGAAAATGGCACTGTTATGTTGAACTTTATTTAC
CGAAAAGAACTGTTCTTTCTTCCTTTGGGATTTGCACTTAAGGCACTTGTCAGCTTTTCT
GATTATCAGATCTTTCAGGAGCTCATCAAAGGAAAAGAGGATGATTCTTTCCTTAGGAAC
TCTGTTTCTCAGATGTTAAGGATTGTAATGGAAGAGGGTTGTTCGACACAAAAACAGGTC
CTTAACTACCTAGGTGAATGCTTCAGAGTAAAACTCAATGTTCCTGACTGGTACCCAAAT
GAGCAAGCTGCGGAGTTCCTGTTTAACCAGTGCATCTGTATCCACTTGAAATCCAATACT
GAAAAGTTTTATATGCTTTGTCTCATGACGCGAAAGCTCTTTGCTTTAGCCAAAGGAGAG
TGCATGGAGGACAATCCTGATAGTTTGGTGAACCAGGAAGTCCTCACACCGGGTCAGCTC
TTCCTTATGTTCCTGAAGGAAAAACTGGAAGGTTGGTTAGTGTCTATTAAAATAGCTTTT
GATAAGAAGGCTCAGAAGACCAGTGTTTCCATGAACACTGACAATTTGATGAGGATTTTT
ACAATGGGCATAGACCTTACAAAACCATTTGAATACCTTTTTGCTACTGGGAATCTGCGT
TCTAAAACAGGTCTTGGCCTCCTACAAGATTCTGGACTTTGTGTTGTGGCTGACAAGCTG
AACTTCATACGCTACCTCTCCCATTTCCGCTGCGTGCACAGAGGGGCTGATTTTGCCAAG
ATGAGGACCACCACAGTACGCAGGCTGCTGCCAGAGTCCTGGGGCTTCCTTTGTCCCGTG
CATACCCCAGACGGGGAGCCCTGTGGCCTGATGAACCACCTAACTGCCGTATGTGAGGTT
GTCACACAGTTTGTGTATACGGCATCTATTCCAGCTTTACTGTGCAACTTGGGGGTCACT
CCCATTGATGGAGCTCCCCACCGATCATACAGTGAGTGCTACCCTGTCCTGCTGGACGGT
GTCATGGTTGGCTGGGTGGATAAGGATCTTGCTCCAGGCATCGCAGATTCTCTTCGTCAT
TTTAAGGTGTTGAGAGAGAAAAGAATTCCTCCCTGGATGGAAGTGGTCCTTATACCCATG
ACAGGAAAACCAAGTCTGTACCCAGGATTGTTCCTTTTTACCACTCCTTGTAGACTGGTA
CGGCCTGTGCAGAACTTAGCATTGGGCAAAGAAGAGCTAATTGGAACTATGGAACAGATC
TTCATGAATGTCGCTATCTTTGAGGATGAAGTTTTTGCTGGAGTTACCACACACCAGGAA
CTCTTTCCACACAGCCTGCTGAGTGTGATTGCCAACTTCATCCCTTTCTCTGATCACAAC
CAGAGTCCACGGAACATGTACCAATGCCAGATGGGTAAGCAAACTATGGGCTTTCCACTT
CTCACTTATCAAGACCGATCGGATAACAAACTGTATCGTCTTCAGACTCCTCAGAGTCCC
TTGGTGAGACCCTCCATGTATGATTATTATGACATGGATAACTATCCAATTGGGACCAAT
GCCATCGTTGCTGTGATTTCTTACACTGGCTATGATATGGAAGATGCCATGATTGTGAAT
AAGGCCTCTTGGGAACGAGGCTTTGCCCATGGAAGTGTCTACAAGTCTGAGTTCATAGAC
CTCTCTGAAAAAATTAAACAAGGAGATAGTAGCCTGGTGTTTGGCATCAAACCTGGTGAC
CCACGCGTTCTGCAGAAGTTAGATGACGATGGATTGCCGTTTATAGGAGCAAAACTGCAG
TACGGAGATCCGTATTACAGCTACCTCAACCTCAACACCGGGGAAAGTTTTGTGATGTAC
TATAAGAGTAAAGAAAATTGTGTTGTGGATAACATCAAAGTGTGCAGTAATGACACTGGG
AGTGGAAAATTCAAGTGTGTTTGCATCACTATGAGAGTGCCTCGGAACCCAACTATCGGA
GATAAATTTGCCAGTCGCCATGGGCAGAAGGGCATTTTAAGCAGATTGTGGCCGGCTGAG
GACATGCCTTTTACTGAGAGTGGGATGGTCCCAGACATTCTGTTCAATCCCCATGGTTTT
CCATCCCGCATGACCATTGGGATGTTAATTGAGAGTATGGCCGGGAAGTCTGCAGCTTTG
CATGGTCTCTGCCATGATGCTACACCCTTCATCTTCTCAGAGGAGAACTCGGCCTTAGAA
TACTTTGGTGAGATGTTAAAGGCTGCTGGCTACAATTTCTATGGCACCGAGAGGTTATAT
AGTGGCATCAGTGGGCTAGAACTGGAAGCAGACATCTTCATAGGAGTGGTTTATTATCAG
CGCTTACGCCATATGGTCTCAGACAAATTTCAAGTAAGGACAACTGGAGCCCGAGACAGA
GTCACCAACCAGCCTATTGGGGGAAGAAATGTCCAGGGTGGAATCCGTTTTGGGGAGATG
GAACGGGATGCGCTTTTAGCTCATGGTACATCTTTTCTCCTTCATGACCGCCTCTTCAAC
TGCTCAGATCGGTCGGTAGCCCATGTGTGTGTGAAGTGTGGCAGTTTACTCTCTCCACTG
TTGGAGAAGCCACCCCCTTCTTGGTCTGCCATGCGCAACAGAAAATACAACTGTACTCTG
TGTAGTCGCAGTGACACTATCGATACTGTTTCTGTGCCTTATGTTTTTCGGTATTTTGTA
GCTGAACTGGCAGCTATGAACATCAAAGTGAAACTGGATGTTGTTTAA
Enzyme 31 GenBank Gene ID AC012442 Link Image
Enzyme 31 GeneCard ID POLR1B Link Image
Enzyme 31 GenAtlas ID POLR1B Link Image
Enzyme 31 HGNC ID HGNC:20454 Link Image
Enzyme 31 Chromosome Location 2
Enzyme 31 Locus 2q13
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  3. Miller G, Panov KI, Friedrich JK, Trinkle-Mulcahy L, Lamond AI, Zomerdijk JC: hRRN3 is essential in the SL1-mediated recruitment of RNA Polymerase I to rRNA gene promoters. EMBO J. 2001 Mar 15;20(6):1373-82. [PubMed Link Image]
  4. Panov KI, Panova TB, Gadal O, Nishiyama K, Saito T, Russell J, Zomerdijk JC: RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor. Mol Cell Biol. 2006 Jul;26(14):5436-48. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 6019
Enzyme 32 Name DNA-directed RNA polymerase III subunit RPC7
Enzyme 32 Synonyms
  1. RNA polymerase III subunit C7
  2. DNA-directed RNA polymerase III subunit G
  3. RNA polymerase III 32 kDa subunit
  4. RPC32
Enzyme 32 Gene Name POLR3G
Enzyme 32 Protein Sequence >DNA-directed RNA polymerase III subunit RPC7
MAGNKGRGRAAYTFNIEAVGFSKGEKLPDVVLKPPPLFPDTDYKPVPLKTGEGEEYMLAL
KQELRETMKRMPYFIETPEERQDIERYSKRYMKVYKEEWIPDWRRLPREMMPRNKCKKAG
PKPKKAKDAGKGTPLTNTEDVLKKMEELEKRGDGEKSDEENEEKEGSKEKSKEGDDDDDD
DAAEQEEYDEEEQEEENDYINSYFEDGDDFGADSDDNMDEATY
Enzyme 32 Number of Residues 223
Enzyme 32 Molecular Weight 25914.3
Enzyme 32 Theoretical pI 4.26
Enzyme 32 GO Classification Not Available
Enzyme 32 General Function Involved in DNA-directed RNA polymerase activity
Enzyme 32 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. May direct with other members of the RPC3/POLR3C-RPC6/POLR3F- RPC7/POLR3G subcomplex RNA Pol III binding to the TFIIIB-DNA complex via the interactions between TFIIIB and POLR3F. May be involved either in the recruitment and stabilization of the subcomplex within RNA polymerase III, or in stimulating catalytic functions of other subunits during initiation. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway
Enzyme 32 Pathways
Enzyme 32 Reactions Not Available
Enzyme 32 Pfam Domain Function Not Available
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 115529475 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID O15318 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name RPC7_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >672 bp
ATGGCTGGGAATAAAGGAAGAGGACGTGCTGCTTATACCTTTAATATTGAGGCTGTTGGA
TTTAGCAAAGGTGAAAAGTTACCTGATGTAGTGTTGAAACCACCCCCACTATTTCCTGAT
ACAGATTATAAACCAGTGCCACTGAAAACAGGAGAAGGTGAAGAATATATGCTGGCTTTG
AAACAGGAGTTGAGAGAAACAATGAAAAGAATGCCTTATTTTATTGAAACACCTGAAGAA
AGACAAGATATTGAAAGGTATAGTAAAAGATACATGAAGGTATACAAGGAAGAATGGATA
CCAGATTGGAGAAGACTTCCAAGAGAGATGATGCCAAGAAATAAATGTAAAAAAGCAGGC
CCAAAACCCAAAAAGGCAAAAGACGCAGGCAAAGGCACACCACTCACTAATACTGAAGAT
GTGTTGAAAAAAATGGAGGAATTGGAAAAAAGAGGTGATGGTGAAAAATCAGATGAGGAA
AATGAAGAGAAAGAAGGAAGCAAAGAGAAAAGTAAAGAAGGTGATGATGACGATGACGAT
GATGCCGCAGAACAGGAGGAATATGATGAAGAAGAGCAAGAAGAGGAAAATGACTACATT
AATTCATACTTTGAAGATGGAGATGATTTTGGCGCAGACAGTGATGACAACATGGATGAG
GCAACCTATTAG
Enzyme 32 GenBank Gene ID NM_006467.2 Link Image
Enzyme 32 GeneCard ID POLR3G Link Image
Enzyme 32 GenAtlas ID POLR3G Link Image
Enzyme 32 HGNC ID HGNC:30075 Link Image
Enzyme 32 Chromosome Location 5
Enzyme 32 Locus 5q14.3
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Wang Z, Roeder RG: Three human RNA polymerase III-specific subunits form a subcomplex with a selective function in specific transcription initiation. Genes Dev. 1997 May 15;11(10):1315-26. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed Link Image]
  4. Hu P, Wu S, Sun Y, Yuan CC, Kobayashi R, Myers MP, Hernandez N: Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits. Mol Cell Biol. 2002 Nov;22(22):8044-55. [PubMed Link Image]
  5. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  7. Chiu YH, Macmillan JB, Chen ZJ: RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell. 2009 Aug 7;138(3):576-91. Epub 2009 Jul 23. [PubMed Link Image]
  8. Ablasser A, Bauernfeind F, Hartmann G, Latz E, Fitzgerald KA, Hornung V: RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat Immunol. 2009 Oct;10(10):1065-72. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 6027
Enzyme 33 Name DNA-directed RNA polymerase III subunit RPC2
Enzyme 33 Synonyms
  1. RNA polymerase III subunit C2
  2. C128
  3. DNA-directed RNA polymerase III 127.6 kDa polypeptide
  4. DNA-directed RNA polymerase III subunit B
Enzyme 33 Gene Name POLR3B
Enzyme 33 Protein Sequence >DNA-directed RNA polymerase III subunit RPC2
MDVLAEEFGNLTPEQLAAPIPTVEEKWRLLPAFLKVKGLVKQHIDSFNYFINVEIKKIMK
ANEKVTSDADPMWYLKYLNIYVGLPDVEESFNVTRPVSPHECRLRDMTYSAPITVDIEYT
RGSQRIIRNALPIGRMPIMLRSSNCVLTGKTPAEFAKLNECPLDPGGYFIVKGVEKVILI
QEQLSKNRIIVEADRKGAVGASVTSSTHEKKSRTNMAVKQGRFYLRHNTLSEDIPIVIIF
KAMGVESDQEIVQMIGTEEHVMAAFGPSLEECQKAQIFTQMQALKYIGNKVRRQRMWGGG
PKKTKIEEARELLASTILTHVPVKEFNFRAKCIYTAVMVRRVILAQGDNKVDDRDYYGNK
RLELAGQLLSLLFEDLFKKFNSEMKKIADQVIPKQRAAQFDVVKHMRQDQITNGMVNAIS
TGNWSLKRFKMDRQGVTQVLSRLSYISALGMMTRISSQFEKTRKVSGPRSLQPSQWGMLC
PSDTPEGEACGLVKNLALMTHITTDMEDGPIVKLASNLGVEDVNLLCGEELSYPNVFLVF
LNGNILGVIRDHKKLVNTFRLMRRAGYINEFVSISTNLTDRCVYISSDGGRLCRPYIIVK
KQKPAVTNKHMEELAQGYRNFEDFLHESLVEYLDVNEENDCNIALYEHTINKDTTHLEIE
PFTLLGVCAGLIPYPHHNQSPRNTYQCAMGKQAMGTIGYNQRNRIDTLMYLLAYPQKPMV
KTKTIELIEFEKLPAGQNATVAVMSYSGYDIEDALVLNKASLDRGFGRCLVYKNAKCTLK
RYTNQTFDKVMGPMLDAATRKPIWRHEILDADGICSPGEKVENKQVLVNKSMPTVTQIPL
EGSNVPQQPQYKDVPITYKGATDSYIEKVMISSNAEDAFLIKMLLRQTRRPEIGDKFSSR
HGQKGVCGLIVPQEDMPFCDSGICPDIIMNPHGFPSRMTVGKLIELLAGKAGVLDGRFHY
GTAFGGSKVKDVCEDLVRHGYNYLGKDYVTSGITGEPLEAYIYFGPVYYQKLKHMVLDKM
HARARGPRAVLTRQPTEGRSRDGGLRLGEMERDCLIGYGASMLLLERLMISSDAFEVDVC
GQCGLLGYSGWCHYCKSSCHVSSLRIPYACKLLFQELQSMNIIPRLKLSKYNE
Enzyme 33 Number of Residues 1133
Enzyme 33 Molecular Weight 127784.0
Enzyme 33 Theoretical pI 8.64
Enzyme 33 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleoside binding
  • nucleotidyltransferase activity
  • ribonucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
Component
Enzyme 33 General Function Involved in DNA-directed RNA polymerase activity
Enzyme 33 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol III is composed of mobile elements and RPC2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway
Enzyme 33 Pathways
Enzyme 33 Reactions
  • nucleoside triphosphate + RNAn = diphosphate + RNAn+1 [RN:R00444]
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 238908503 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q9NW08 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name RPC2_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >3402 bp
ATGGACGTGCTAGCGGAGGAGTTTGGGAACCTGACTCCGGAGCAGCTGGCGGCGCCGATC
CCGACTGTAGAGGAAAAATGGAGGCTGCTTCCAGCATTTTTAAAGGTGAAAGGCCTTGTG
AAACAGCATATAGATTCATTTAACTATTTCATTAATGTAGAGATAAAGAAGATAATGAAA
GCCAATGAAAAGGTTACAAGTGACGCTGACCCTATGTGGTACTTAAAATATCTTAATATC
TATGTTGGGCTTCCTGATGTTGAAGAAAGCTTCAATGTAACTAGACCAGTGTCCCCTCAT
GAGTGCCGTTTGAGAGACATGACATACTCTGCCCCTATTACAGTGGATATTGAATATACC
CGAGGCAGCCAGAGGATCATCCGCAATGCCTTACCTATCGGCAGAATGCCCATAATGCTA
CGTAGTTCAAACTGTGTTCTTACAGGAAAAACGCCAGCAGAATTTGCCAAACTGAACGAA
TGTCCCTTAGATCCAGGTGGCTACTTCATTGTTAAAGGAGTAGAAAAAGTTATTCTTATC
CAAGAGCAGCTGTCTAAGAACAGGATCATCGTGGAGGCTGATAGAAAAGGGGCTGTTGGA
GCTTCAGTTACCAGCTCTACCCATGAGAAAAAAAGCAGAACCAATATGGCTGTGAAACAA
GGACGATTTTATTTGAGGCATAATACTTTGTCAGAAGATATACCCATTGTCATCATATTT
AAGGCCATGGGTGTTGAGAGTGACCAGGAAATTGTGCAGATGATTGGAACAGAGGAGCAC
GTGATGGCTGCATTTGGGCCCAGTCTGGAAGAGTGCCAGAAAGCTCAGATTTTCACACAG
ATGCAGGCATTAAAATATATAGGGAACAAAGTAAGAAGGCAAAGGATGTGGGGAGGTGGA
CCAAAGAAAACCAAAATAGAAGAAGCAAGAGAGCTCCTGGCTTCCACCATTCTGACCCAT
GTCCCAGTTAAGGAATTCAATTTCCGAGCCAAATGTATCTATACTGCAGTGATGGTGCGA
AGAGTTATTCTGGCCCAAGGAGATAATAAAGTTGACGACAGAGATTATTATGGTAACAAG
CGACTGGAATTGGCAGGACAGCTTTTATCTCTTCTTTTTGAAGACTTGTTCAAAAAATTT
AATTCTGAAATGAAAAAGATTGCCGACCAGGTGATTCCTAAGCAAAGAGCAGCCCAGTTT
GATGTTGTCAAACACATGCGCCAAGACCAGATCACCAATGGCATGGTGAATGCTATTTCT
ACCGGAAATTGGTCTTTAAAGAGATTTAAAATGGACCGCCAGGGTGTAACCCAAGTGCTG
TCTCGCTTGTCATATATATCCGCACTGGGCATGATGACAAGAATCTCTTCCCAGTTTGAA
AAAACGAGAAAAGTGAGTGGTCCTCGCTCCCTCCAGCCATCTCAGTGGGGAATGCTGTGT
CCTTCGGACACTCCTGAAGGAGAGGCATGTGGTTTGGTTAAAAACTTGGCCCTTATGACA
CACATCACAACTGATATGGAAGATGGACCCATTGTTAAATTAGCCAGTAACTTGGGAGTA
GAAGATGTGAATTTATTATGTGGGGAAGAGCTCTCTTACCCAAATGTGTTTCTTGTCTTT
CTTAATGGTAACATCTTAGGTGTCATTCGAGACCACAAAAAGCTAGTGAATACATTTCGA
CTCATGAGAAGAGCAGGATATATCAATGAATTTGTTTCCATCTCAACAAATCTTACAGAT
CGATGTGTCTATATTTCTTCTGATGGGGGAAGGCTATGCAGACCCTACATAATTGTCAAG
AAACAGAAGCCAGCAGTCACAAATAAACATATGGAAGAGCTGGCCCAAGGGTACAGGAAT
TTTGAAGATTTCTTACATGAGAGTCTGGTTGAATATTTAGATGTGAATGAAGAAAATGAT
TGTAACATTGCACTGTACGAACACACAATTAATAAAGACACCACCCACTTGGAGATTGAA
CCCTTCACTCTTCTCGGCGTGTGTGCTGGACTTATCCCATACCCTCACCATAACCAGTCA
CCGAGAAACACTTATCAGTGTGCCATGGGGAAACAAGCCATGGGTACTATAGGATACAAC
CAGCGAAACAGAATTGATACTCTCATGTATCTACTAGCATATCCACAAAAACCCATGGTT
AAGACAAAAACCATTGAATTGATAGAATTTGAGAAACTGCCAGCTGGACAGAATGCAACA
GTTGCTGTGATGAGCTATAGTGGCTATGATATTGAAGATGCTCTTGTTTTAAACAAGGCC
TCTTTAGACAGAGGCTTTGGGCGTTGCCTTGTATATAAAAATGCTAAATGTACGTTGAAA
CGATACACCAATCAGACTTTTGATAAAGTGATGGGGCCCATGTTGGATGCTGCTACAAGG
AAACCTATCTGGCGACATGAAATCTTAGATGCAGATGGTATTTGTTCTCCAGGTGAGAAA
GTAGAAAACAAACAAGTGCTTGTAAATAAGTCCATGCCCACAGTGACTCAGATTCCTTTG
GAAGGAAGTAATGTACCACAGCAACCACAGTACAAAGATGTACCCATAACCTACAAAGGA
GCAACAGACTCATATATTGAAAAAGTGATGATATCTTCAAATGCTGAAGATGCTTTTCTG
ATCAAAATGCTGCTGAGACAGACAAGGCGTCCAGAAATTGGAGACAAATTCAGCAGTCGT
CATGGGCAAAAAGGTGTTTGTGGCTTGATCGTCCCCCAGGAAGACATGCCATTTTGTGAT
TCTGGCATCTGTCCGGACATCATCATGAACCCACACGGCTTCCCATCACGAATGACGGTG
GGGAAGCTCATTGAGCTGCTGGCTGGCAAGGCCGGTGTGCTGGACGGCAGATTCCACTAC
GGCACTGCGTTTGGAGGCAGTAAAGTGAAGGATGTGTGTGAGGACCTCGTTCGCCATGGT
TATAACTACTTGGGGAAAGACTATGTTACATCCGGCATCACAGGTGAGCCCTTAGAAGCA
TACATCTATTTTGGCCCCGTGTACTATCAGAAGCTGAAACACATGGTGCTAGATAAAATG
CATGCCCGGGCCCGGGGCCCACGAGCCGTCCTTACCAGGCAACCCACTGAAGGACGGTCT
CGTGATGGTGGCTTGCGTCTCGGGGAAATGGAACGTGACTGTTTAATCGGTTATGGAGCC
AGTATGCTTTTGCTAGAGAGACTAATGATTTCAAGTGATGCCTTTGAGGTTGATGTCTGT
GGGCAGTGTGGACTTCTGGGGTATTCTGGCTGGTGCCATTACTGCAAGTCATCCTGCCAC
GTGTCTTCCCTCCGTATTCCGTATGCCTGCAAGCTGCTCTTCCAGGAACTACAGTCTATG
AACATCATCCCCAGGTTAAAACTGTCCAAGTACAATGAATGA
Enzyme 33 GenBank Gene ID NM_018082.5 Link Image
Enzyme 33 GeneCard ID POLR3B Link Image
Enzyme 33 GenAtlas ID POLR3B Link Image
Enzyme 33 HGNC ID HGNC:30348 Link Image
Enzyme 33 Chromosome Location 1
Enzyme 33 Locus 12q23.3
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Hu P, Wu S, Sun Y, Yuan CC, Kobayashi R, Myers MP, Hernandez N: Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits. Mol Cell Biol. 2002 Nov;22(22):8044-55. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  5. Chiu YH, Macmillan JB, Chen ZJ: RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell. 2009 Aug 7;138(3):576-91. Epub 2009 Jul 23. [PubMed Link Image]
  6. Ablasser A, Bauernfeind F, Hartmann G, Latz E, Fitzgerald KA, Hornung V: RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat Immunol. 2009 Oct;10(10):1065-72. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 6031
Enzyme 34 Name DNA-directed RNA polymerase I subunit RPA49
Enzyme 34 Synonyms
  1. RNA polymerase I subunit A49
  2. DNA-directed RNA polymerase I subunit E
  3. RNA polymerase I-associated factor 1
  4. RNA polymerase I-associated factor 53
Enzyme 34 Gene Name POLR1E
Enzyme 34 Protein Sequence >DNA-directed RNA polymerase I subunit RPA49
MYQASAVSLLPRDIPSCHSPSPGFSHLPTSSSQLAPDLLQFPLGQDPSFLAIPILTLPPS
DSLVPPYIVWYIVWPSALISFLGCTLTVQFSNGKLQSPGNMRFTLYENKDSTNPRKRNQR
ILAAETDRLSYVGNNFGTGALKCNTLCRHFVGILNKTSGQMEVYDAELFNMQPLFSDVSV
ESELALESQTKTYREKMDSCIEAFGTTKQKRALNTRRMNRVGNESLNRAVAKAAETIIDT
KGVTALVSDAIHNDLQDDSLYLPPCYDDAAKPEDVYKFEDLLSPAEYEALQSPSEAFRNV
TSEEILKMIEENSHCTFVIEALKSLPSDVESRDRQARCIWFLDTLIKFRAHRVVKRKSAL
GPGVPHIINTKLLKHFTCLTYNNGRLRNLISDSMKAKITAYVIILALHIHDFQIDLTVLQ
RDLKLSEKRMMEIAKAMRLKISKRRVSVAAGSEEDHKLGTLSLPLPPAQTSDRLAKRRKI
T
Enzyme 34 Number of Residues 481
Enzyme 34 Molecular Weight 53961.4
Enzyme 34 Theoretical pI 8.74
Enzyme 34 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 34 General Function Involved in DNA binding
Enzyme 34 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Appears to be involved in the formation of the initiation complex at the promoter by mediating the interaction between Pol I and UBTF/UBF
Enzyme 34 Pathways
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 21749630 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q9GZS1 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name RPA49_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >1446 bp
ATGTACCAGGCCTCTGCTGTCAGCCTCCTTCCGCGAGACATTCCCTCCTGTCACAGCCCC
TCCCCAGGGTTCTCCCACCTCCCTACCTCCTCTTCTCAGCTGGCCCCGGATCTCCTCCAG
TTCCCTTTGGGTCAGGACCCGAGCTTCCTTGCCATCCCCATTCTGGCACTCCCTCCCAGT
GACAGTCTAGTCCCACCGTACATTGTGTGGTACATTGTGTGGCCTTCTGCTCTCATCTCA
TTCTTGGGCTGCACTCTTACAGTCCAGTTCTCCAACGGGAAGCTACAGAGTCCAGGCAAC
ATGCGCTTTACCTTGTATGAGAACAAAGATTCCACCAACCCCAGGAAGAGGAATCAACGG
ATCCTGGCAGCTGAAACAGATAGGCTCTCCTATGTGGGAAACAATTTTGGGACTGGAGCC
CTCAAATGCAACACTTTGTGCAGGCACTTTGTGGGAATTTTGAACAAGACCTCTGGCCAA
ATGGAAGTATATGATGCTGAATTGTTCAACATGCAGCCACTATTTTCAGATGTATCAGTC
GAGAGTGAACTGGCGCTAGAGAGTCAGACCAAAACTTACAGAGAAAAGATGGATTCTTGT
ATTGAAGCCTTTGGTACCACCAAACAGAAGCGAGCTCTGAACACCAGGAGAATGAACAGA
GTTGGCAATGAATCTTTGAATCGTGCAGTGGCTAAAGCTGCAGAGACTATCATTGATACG
AAGGGTGTGACTGCTCTGGTCAGCGATGCTATCCACAATGACTTGCAAGATGACTCCCTC
TACCTTCCTCCCTGCTATGATGATGCAGCCAAGCCTGAAGACGTGTATAAATTTGAAGAT
CTTCTTTCCCCTGCGGAGTATGAAGCTCTTCAGAGCCCATCTGAAGCTTTCAGGAACGTC
ACGTCAGAAGAAATACTGAAGATGATTGAGGAGAACAGCCATTGCACCTTTGTCATAGAA
GCGTTGAAGTCTTTGCCATCAGATGTGGAGAGCCGAGACCGCCAGGCCCGATGCATATGG
TTTCTGGATACCCTCATCAAATTTCGAGCTCATAGGGTAGTTAAGCGGAAAAGTGCTCTG
GGACCTGGAGTTCCCCACATCATCAACACCAAACTGCTGAAGCACTTTACTTGCTTGACC
TACAACAATGGCAGATTACGGAACTTAATTTCGGATTCTATGAAGGCGAAGATTACCGCA
TATGTGATCATACTTGCCTTGCACATACATGACTTCCAAATTGACCTGACAGTGTTACAG
AGGGACTTGAAGCTCAGTGAGAAAAGGATGATGGAGATAGCCAAAGCCATGAGGCTGAAG
ATCTCCAAAAGAAGGGTGTCTGTGGCCGCCGGCAGTGAAGAAGATCACAAACTGGGCACC
CTGTCCCTCCCGCTGCCTCCAGCCCAGACCTCAGACCGCCTGGCAAAGCGGAGGAAGATT
ACCTAG
Enzyme 34 GenBank Gene ID AK091294 Link Image
Enzyme 34 GeneCard ID POLR1E Link Image
Enzyme 34 GenAtlas ID POLR1E Link Image
Enzyme 34 HGNC ID HGNC:17631 Link Image
Enzyme 34 Chromosome Location 9
Enzyme 34 Locus 9p13.2
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Scherl A, Coute Y, Deon C, Calle A, Kindbeiter K, Sanchez JC, Greco A, Hochstrasser D, Diaz JJ: Functional proteomic analysis of human nucleolus. Mol Biol Cell. 2002 Nov;13(11):4100-9. [PubMed Link Image]
  5. Panov KI, Panova TB, Gadal O, Nishiyama K, Saito T, Russell J, Zomerdijk JC: RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor. Mol Cell Biol. 2006 Jul;26(14):5436-48. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 6035
Enzyme 35 Name DNA-directed RNA polymerase III subunit RPC8
Enzyme 35 Synonyms
  1. RNA polymerase III subunit C8
  2. DNA-directed RNA polymerase III subunit H
  3. RNA polymerase III subunit 22.9 kDa subunit
  4. RPC22.9
Enzyme 35 Gene Name POLR3H
Enzyme 35 Protein Sequence >DNA-directed RNA polymerase III subunit RPC8
MFVLVEMVDTVRIPPWQFERKLNDSIAEELNKKLANKVVYNVGLCICLFDITKLEDAYVF
PGDGASHTKVHFRCVVFHPFLDEILIGKIKGCSPEGVHVSLGFFDDILIPPESLQQPAKF
DEAEQVWVWEYETEEGAHDLYMDTGEEIRFRVVDESFVDTSPTGPSSADATTSSEELPKK
EAPYTLVGSISEPGLGLLSWWTSN
Enzyme 35 Number of Residues 204
Enzyme 35 Molecular Weight 22917.7
Enzyme 35 Theoretical pI 4.21
Enzyme 35 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • transcription
Component
Enzyme 35 General Function Involved in DNA-directed RNA polymerase activity
Enzyme 35 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway
Enzyme 35 Pathways
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 65301161 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID Q9Y535 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name RPC8_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >615 bp
ATGTTCGTCCTGGTGGAAATGGTGGACACCGTCCGGATCCCCCCTTGGCAGTTTGAGAGG
AAGCTCAACGACTCCATTGCCGAGGAGCTGAACAAGAAGTTGGCCAACAAGGTCGTGTAC
AACGTGGGACTCTGCATTTGTCTGTTTGATATCACCAAACTGGAGGATGCCTATGTATTC
CCTGGGGATGGCGCATCACACACCAAAGTCCATTTTCGCTGCGTGGTGTTTCATCCATTC
CTAGATGAGATTCTCATTGGGAAGATCAAAGGCTGCAGCCCAGAAGGAGTGCACGTCTCT
CTAGGCTTCTTCGATGACATTCTCATCCCCCCAGAGTCACTGCAGCAGCCAGCCAAGTTC
GACGAAGCGGAGCAGGTGTGGGTGTGGGAGTACGAGACGGAGGAAGGAGCACACGACCTC
TACATGGACACCGGCGAGGAGATCCGCTTCCGGGTGGTGGACGAGAGCTTTGTTGACACG
TCCCCCACAGGGCCCAGCTCAGCAGATGCCACCACTTCCAGTGAGGAGCTGCCAAAGAAG
GAGGCTCCGTACACGCTTGTGGGATCCATCAGTGAGCCAGGCCTGGGCCTTCTCTCCTGG
TGGACCAGCAACTAG
Enzyme 35 GenBank Gene ID NM_001018050.2 Link Image
Enzyme 35 GeneCard ID POLR3H Link Image
Enzyme 35 GenAtlas ID POLR3H Link Image
Enzyme 35 HGNC ID HGNC:30349 Link Image
Enzyme 35 Chromosome Location 2
Enzyme 35 Locus 22q13.2
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Hu P, Wu S, Sun Y, Yuan CC, Kobayashi R, Myers MP, Hernandez N: Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits. Mol Cell Biol. 2002 Nov;22(22):8044-55. [PubMed Link Image]
  2. Hirosawa M, Nagase T, Murahashi Y, Kikuno R, Ohara O: Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping. DNA Res. 2001 Feb 28;8(1):1-9. [PubMed Link Image]
  3. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  4. 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]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Chiu YH, Macmillan JB, Chen ZJ: RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell. 2009 Aug 7;138(3):576-91. Epub 2009 Jul 23. [PubMed Link Image]
  7. Ablasser A, Bauernfeind F, Hartmann G, Latz E, Fitzgerald KA, Hornung V: RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat Immunol. 2009 Oct;10(10):1065-72. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 6036
Enzyme 36 Name DNA-directed RNA polymerase III subunit RPC10
Enzyme 36 Synonyms
  1. RNA polymerase III subunit C10
  2. DNA-directed RNA polymerase III subunit K
  3. RNA polymerase III 12.5 kDa subunit
  4. RPC12.5
  5. RNA polymerase III subunit C11
  6. HsC11p
  7. RPC11
  8. hRPC11
Enzyme 36 Gene Name POLR3K
Enzyme 36 Protein Sequence >DNA-directed RNA polymerase III subunit RPC10
MLLFCPGCGNGLIVEEGQRCHRFSCNTCPYVHNITRKVTNRKYPKLKEVDDVLGGAAAWE
NVDSTAESCPKCEHPRAYFMQLQTRSADEPMTTFYKCCNAQCGHRWRD
Enzyme 36 Number of Residues 108
Enzyme 36 Molecular Weight 12336.0
Enzyme 36 Theoretical pI 7.89
Enzyme 36 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • RNA polymerase activity
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transcription regulator activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • transcription
Component
Enzyme 36 General Function Involved in DNA binding
Enzyme 36 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway
Enzyme 36 Pathways
Enzyme 36 Reactions Not Available
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 14336676 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q9Y2Y1 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name RPC10_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >327 bp
ATGCTGCTGTTCTGCCCCGGCTGCGGGAACGGGCTGATCGTGGAGGAGGGACAACGCTGC
CACCGCTTCTCCTGCAACACGTGCCCCTACGTGCACAACATCACCCGCAAGGTAACAAAT
CGGAAGTACCCAAAACTGAAAGAAGTGGATGATGTGCTTGGTGGAGCAGCTGCCTGGGAG
AATGTTGACTCTACTGCAGAGTCGTGTCCCAAATGCGAACATCCTCGTGCTTACTTCATG
CAGCTTCAGACCCGCTCTGCAGATGAGCCGATGACCACCTTCTACAAGTGCTGCAATGCT
CAGTGTGGACACCGCTGGAGGGATTAG
Enzyme 36 GenBank Gene ID AE006462 Link Image
Enzyme 36 GeneCard ID POLR3K Link Image
Enzyme 36 GenAtlas ID POLR3K Link Image
Enzyme 36 HGNC ID HGNC:14121 Link Image
Enzyme 36 Chromosome Location 1
Enzyme 36 Locus 16p13.3
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Chedin S, Riva M, Schultz P, Sentenac A, Carles C: The RNA cleavage activity of RNA polymerase III is mediated by an essential TFIIS-like subunit and is important for transcription termination. Genes Dev. 1998 Dec 15;12(24):3857-71. [PubMed Link Image]
  2. Spakovskii GV, Lebedenko EN: [Molecular identification and characteristics of hRPC11, the smallest specific subunit of human RNA polymerase III] Bioorg Khim. 1998 Nov;24(11):877-80. [PubMed Link Image]
  3. De Gobbi M, Viprakasit V, Hughes JR, Fisher C, Buckle VJ, Ayyub H, Gibbons RJ, Vernimmen D, Yoshinaga Y, de Jong P, Cheng JF, Rubin EM, Wood WG, Bowden D, Higgs DR: A regulatory SNP causes a human genetic disease by creating a new transcriptional promoter. Science. 2006 May 26;312(5777):1215-7. [PubMed Link Image]
  4. 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]
  5. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Hu P, Wu S, Sun Y, Yuan CC, Kobayashi R, Myers MP, Hernandez N: Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits. Mol Cell Biol. 2002 Nov;22(22):8044-55. [PubMed Link Image]
  8. Chiu YH, Macmillan JB, Chen ZJ: RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell. 2009 Aug 7;138(3):576-91. Epub 2009 Jul 23. [PubMed Link Image]
  9. Ablasser A, Bauernfeind F, Hartmann G, Latz E, Fitzgerald KA, Hornung V: RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat Immunol. 2009 Oct;10(10):1065-72. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 6039
Enzyme 37 Name Pyruvate kinase isozymes M1/M2
Enzyme 37 Synonyms
  1. Cytosolic thyroid hormone-binding protein
  2. CTHBP
  3. Opa-interacting protein 3
  4. OIP-3
  5. Pyruvate kinase 2/3
  6. Pyruvate kinase muscle isozyme
  7. Thyroid hormone-binding protein 1
  8. THBP1
  9. Tumor M2-PK
  10. p58
Enzyme 37 Gene Name PKM2
Enzyme 37 Protein Sequence >Pyruvate kinase isozymes M1/M2
MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVET
LKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIR
TGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGL
ISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMV
FASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIE
IPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIM
LSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEAS
FKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQE
AWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP
Enzyme 37 Number of Residues 531
Enzyme 37 Molecular Weight 57936.4
Enzyme 37 Theoretical pI 7.94
Enzyme 37 GO Classification
Function
  • alkali metal ion binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • kinase activity
  • magnesium ion binding
  • metal ion binding
  • potassium ion binding
  • pyruvate kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 37 General Function Involved in magnesium ion binding
Enzyme 37 Specific Function Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival
Enzyme 37 Pathways
Enzyme 37 Reactions
  • ATP + pyruvate = ADP + phosphoenolpyruvate [RN:R00200]
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • None
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 33286418 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID P14618 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name KPYM_HUMAN Link Image
Enzyme 37 PDB ID 1F3X Link Image
Enzyme 37 PDB File Show
Enzyme 37 3D Structure
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >1596 bp
ATGTCGAAGCCCCATAGTGAAGCCGGGACTGCCTTCATTCAGACCCAGCAGCTGCACGCA
GCCATGGCTGACACATTCCTGGAGCACATGTGCCGCCTGGACATTGATTCACCACCCATC
ACAGCCCGGAACACTGGCATCATCTGTACCATTGGCCCAGCTTCCCGATCAGTGGAGACG
TTGAAGGAGATGATTAAGTCTGGAATGAATGTGGCTCGTCTGAACTTCTCTCATGGAACT
CATGAGTACCATGCGGAGACCATCAAGAATGTGCGCACAGCCACGGAAAGCTTTGCTTCT
GACCCCATCCTCTACCGGCCCGTTGCTGTGGCTCTAGACACTAAAGGACCTGAGATCCGA
ACTGGGCTCATCAAGGGCAGCGGCACTGCAGAGGTGGAGCTGAAGAAGGGAGCCACTCTC
AAAATCACGCTGGATAACGCCTACATGGAAAAGTGTGACGAGAACATCCTGTGGCTGGAC
TACAAGAACATCTGCAAGGTGGTGGAAGTGGGCAGCAAGATCTACGTGGATGATGGGCTT
ATTTCTCTCCAGGTGAAGCAGAAAGGTGCCGACTTCCTGGTGACGGAGGTGGAAAATGGT
GGCTCCTTGGGCAGCAAGAAGGGTGTGAACCTTCCTGGGGCTGCTGTGGACTTGCCTGCT
GTGTCGGAGAAGGACATCCAGGATCTGAAGTTTGGGGTCGAGCAGGATGTTGATATGGTG
TTTGCGTCATTCATCCGCAAGGCATCTGATGTCCATGAAGTTAGGAAGGTCCTGGGAGAG
AAGGGAAAGAACATCAAGATTATCAGCAAAATCGAGAATCATGAGGGGGTTCGGAGGTTT
GATGAAATCCTGGAGGCCAGTGATGGGATCATGGTGGCTCGTGGTGATCTAGGCATTGAG
ATTCCTGCAGAGAAGGTCTTCCTTGCTCAGAAGATGATGATTGGACGGTGCAACCGAGCT
GGGAAGCCTGTCATCTGTGCTACTCAGATGCTGGAGAGCATGATCAAGAAGCCCCGCCCC
ACTCGGGCTGAAGGCAGTGATGTGGCCAATGCAGTCCTGGATGGAGCCGACTGCATCATG
CTGTCTGGAGAAACAGCCAAAGGGGACTATCCTCTGGAGGCTGTGCGCATGCAGCACCTG
ATTGCCCGTGAGGCAGAGGCTGCCATCTACCACTTGCAATTATTTGAGGAACTCCGCCGC
CTGGCGCCCATTACCAGCGACCCCACAGAAGCCACCGCCGTGGGTGCCGTGGAGGCCTCC
TTCAAGTGCTGCAGTGGGGCCATAATCGTCCTCACCAAGTCTGGCAGGTCTGCTCACCAG
GTGGCCAGATACCGCCCACGTGCCCCCATCATTGCTGTGACCCGGAATCCCCAGACAGCT
CGTCAGGCCCACCTGTACCGTGGCATCTTCCCTGTGCTGTGCAAGGACCCAGTCCAGGAG
GCCTGGGCTGAGGACGTGGACCTCCGGGTGAACTTTGCCATGAATGTTGGCAAGGCCCGA
GGCTTCTTCAAGAAGGGAGATGTGGTCATTGTGCTGACCGGATGGCGCCCTGGCTCCGGC
TTCACCAACACCATGCGTGTTGTTCCTGTGCCGTGA
Enzyme 37 GenBank Gene ID NM_002654.3 Link Image
Enzyme 37 GeneCard ID PKM2 Link Image
Enzyme 37 GenAtlas ID PKM2 Link Image
Enzyme 37 HGNC ID HGNC:9021 Link Image
Enzyme 37 Chromosome Location 1
Enzyme 37 Locus 15q22
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Tani K, Yoshida MC, Satoh H, Mitamura K, Noguchi T, Tanaka T, Fujii H, Miwa S: Human M2-type pyruvate kinase: cDNA cloning, chromosomal assignment and expression in hepatoma. Gene. 1988 Dec 20;73(2):509-16. [PubMed Link Image]
  2. Kato H, Fukuda T, Parkison C, McPhie P, Cheng SY: Cytosolic thyroid hormone-binding protein is a monomer of pyruvate kinase. Proc Natl Acad Sci U S A. 1989 Oct;86(20):7861-5. [PubMed Link Image]
  3. Takenaka M, Noguchi T, Sadahiro S, Hirai H, Yamada K, Matsuda T, Imai E, Tanaka T: Isolation and characterization of the human pyruvate kinase M gene. Eur J Biochem. 1991 May 23;198(1):101-6. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Ashizawa K, McPhie P, Lin KH, Cheng SY: An in vitro novel mechanism of regulating the activity of pyruvate kinase M2 by thyroid hormone and fructose 1, 6-bisphosphate. Biochemistry. 1991 Jul 23;30(29):7105-11. [PubMed Link Image]
  8. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  9. Williams JM, Chen GC, Zhu L, Rest RF: Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth. Mol Microbiol. 1998 Jan;27(1):171-86. [PubMed Link Image]
  10. Garcia-Gonzalo FR, Cruz C, Munoz P, Mazurek S, Eigenbrodt E, Ventura F, Bartrons R, Rosa JL: Interaction between HERC1 and M2-type pyruvate kinase. FEBS Lett. 2003 Mar 27;539(1-3):78-84. [PubMed Link Image]
  11. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  12. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  13. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  14. Stetak A, Veress R, Ovadi J, Csermely P, Keri G, Ullrich A: Nuclear translocation of the tumor marker pyruvate kinase M2 induces programmed cell death. Cancer Res. 2007 Feb 15;67(4):1602-8. [PubMed Link Image]
  15. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  16. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  17. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  18. Shimada N, Shinagawa T, Ishii S: Modulation of M2-type pyruvate kinase activity by the cytoplasmic PML tumor suppressor protein. Genes Cells. 2008 Mar;13(3):245-54. [PubMed Link Image]
  19. Lee J, Kim HK, Han YM, Kim J: Pyruvate kinase isozyme type M2 (PKM2) interacts and cooperates with Oct-4 in regulating transcription. Int J Biochem Cell Biol. 2008;40(5):1043-54. Epub 2007 Nov 29. [PubMed Link Image]
  20. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  21. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  22. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  23. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  24. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  25. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  26. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  27. Dombrauckas JD, Santarsiero BD, Mesecar AD: Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis. Biochemistry. 2005 Jul 12;44(27):9417-29. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 6041
Enzyme 38 Name Pyruvate kinase isozymes R/L
Enzyme 38 Synonyms
  1. Pyruvate kinase 1
  2. R-type/L-type pyruvate kinase
  3. Red cell/liver pyruvate kinase
Enzyme 38 Gene Name PKLR
Enzyme 38 Protein Sequence >Pyruvate kinase isozymes R/L
MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQ
LPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFS
HGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKG
SQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQV
ENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAA
LGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRC
NLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKM
QHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRS
AQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESG
KLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
Enzyme 38 Number of Residues 574
Enzyme 38 Molecular Weight 61829.6
Enzyme 38 Theoretical pI 7.83
Enzyme 38 GO Classification
Function
  • alkali metal ion binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • kinase activity
  • magnesium ion binding
  • metal ion binding
  • potassium ion binding
  • pyruvate kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 38 General Function Involved in magnesium ion binding
Enzyme 38 Specific Function Plays a key role in glycolysis
Enzyme 38 Pathways
Enzyme 38 Reactions
  • ATP + pyruvate = ADP + phosphoenolpyruvate [RN:R00200]
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein Not Available
Enzyme 38 UniProtKB/Swiss-Prot ID P30613 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name KPYR_HUMAN Link Image
Enzyme 38 PDB ID 1LIU Link Image
Enzyme 38 PDB File Show
Enzyme 38 3D Structure
Enzyme 38 Cellular Location Not Available
Enzyme 38 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 38 GenBank Gene ID AB015983 Link Image
Enzyme 38 GeneCard ID PKLR Link Image
Enzyme 38 GenAtlas ID PKLR Link Image
Enzyme 38 HGNC ID HGNC:9020 Link Image
Enzyme 38 Chromosome Location 1
Enzyme 38 Locus 1q21
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Kanno H, Fujii H, Hirono A, Miwa S: cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384----Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia. Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):8218-21. [PubMed Link Image]
  2. Tani K, Fujii H, Nagata S, Miwa S: Human liver type pyruvate kinase: complete amino acid sequence and the expression in mammalian cells. Proc Natl Acad Sci U S A. 1988 Mar;85(6):1792-5. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Tani K, Fujii H, Tsutsumi H, Sukegawa J, Toyoshima K, Yoshida MC, Noguchi T, Tanaka T, Miwa S: Human liver type pyruvate kinase: cDNA cloning and chromosomal assignment. Biochem Biophys Res Commun. 1987 Mar 13;143(2):431-8. [PubMed Link Image]
  5. Kanno H, Fujii H, Tsujino G, Miwa S: Molecular basis of impaired pyruvate kinase isozyme conversion in erythroid cells: a single amino acid substitution near the active site and decreased mRNA content of the R-type PK. Biochem Biophys Res Commun. 1993 Apr 15;192(1):46-52. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Beutler E, Baronciani L: Mutations in pyruvate kinase. Hum Mutat. 1996;7(1):1-6. [PubMed Link Image]
  8. Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase. Blood Cells Mol Dis. 1996;22(1):85-9. [PubMed Link Image]
  9. Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (1st update). Blood Cells Mol Dis. 1996;22(3):259-64. [PubMed Link Image]
  10. Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (2nd update). Blood Cells Mol Dis. 1998 Sep;24(3):273-9. [PubMed Link Image]
  11. Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (Third update). Blood Cells Mol Dis. 2000 Feb;26(1):47-53. [PubMed Link Image]
  12. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  13. Valentini G, Chiarelli LR, Fortin R, Dolzan M, Galizzi A, Abraham DJ, Wang C, Bianchi P, Zanella A, Mattevi A: Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia. J Biol Chem. 2002 Jun 28;277(26):23807-14. Epub 2002 Apr 17. [PubMed Link Image]
  14. Neubauer B, Lakomek M, Winkler H, Parke M, Hofferbert S, Schroter W: Point mutations in the L-type pyruvate kinase gene of two children with hemolytic anemia caused by pyruvate kinase deficiency. Blood. 1991 May 1;77(9):1871-5. [PubMed Link Image]
  15. Kanno H, Fujii H, Hirono A, Omine M, Miwa S: Identical point mutations of the R-type pyruvate kinase (PK) cDNA found in unrelated PK variants associated with hereditary hemolytic anemia. Blood. 1992 Mar 1;79(5):1347-50. [PubMed Link Image]
  16. Kanno H, Fujii H, Miwa S: Low substrate affinity of pyruvate kinase variant (PK Sapporo) caused by a single amino acid substitution (426 Arg-->Gln) associated with hereditary hemolytic anemia. Blood. 1993 May 1;81(9):2439-41. [PubMed Link Image]
  17. Baronciani L, Beutler E: Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia. Proc Natl Acad Sci U S A. 1993 May 1;90(9):4324-7. [PubMed Link Image]
  18. Kanno H, Ballas SK, Miwa S, Fujii H, Bowman HS: Molecular abnormality of erythrocyte pyruvate kinase deficiency in the Amish. Blood. 1994 Apr 15;83(8):2311-6. [PubMed Link Image]
  19. Lenzner C, Nurnberg P, Thiele BJ, Reis A, Brabec V, Sakalova A, Jacobasch G: Mutations in the pyruvate kinase L gene in patients with hereditary hemolytic anemia. Blood. 1994 May 15;83(10):2817-22. [PubMed Link Image]
  20. Baronciani L, Beutler E: Molecular study of pyruvate kinase deficient patients with hereditary nonspherocytic hemolytic anemia. J Clin Invest. 1995 Apr;95(4):1702-9. [PubMed Link Image]
  21. Beutler E, Westwood B, van Zwieten R, Roos D: G-->T transition at cDNA nt 110 (K37Q) in the PKLR (pyruvate kinase) gene is the molecular basis of a case of hereditary increase of red blood cell ATP. Hum Mutat. 1997;9(3):282-5. [PubMed Link Image]
  22. Zarza R, Alvarez R, Pujades A, Nomdedeu B, Carrera A, Estella J, Remacha A, Sanchez JM, Morey M, Cortes T, Perez Lungmus G, Bureo E, Vives Corrons JL: Molecular characterization of the PK-LR gene in pyruvate kinase deficient Spanish patients. Red Cell Pathology Group of the Spanish Society of Haematology (AEHH). Br J Haematol. 1998 Nov;103(2):377-82. [PubMed Link Image]
  23. Cohen-Solal M, Prehu C, Wajcman H, Poyart C, Bardakdjian-Michau J, Kister J, Prome D, Valentin C, Bachir D, Galacteros F: A new sickle cell disease phenotype associating Hb S trait, severe pyruvate kinase deficiency (PK Conakry), and an alpha2 globin gene variant (Hb Conakry). Br J Haematol. 1998 Dec;103(4):950-6. [PubMed Link Image]
  24. Pastore L, Della Morte R, Frisso G, Alfinito F, Vitale D, Calise RM, Ferraro F, Zagari A, Rotoli B, Salvatore F: Novel mutations and structural implications in R-type pyruvate kinase-deficient patients from Southern Italy. Hum Mutat. 1998;11(2):127-34. [PubMed Link Image]
  25. Zanella A, Bianchi P, Fermo E, Iurlo A, Zappa M, Vercellati C, Boschetti C, Baronciani L, Cotton F: Molecular characterization of the PK-LR gene in sixteen pyruvate kinase-deficient patients. Br J Haematol. 2001 Apr;113(1):43-8. [PubMed Link Image]
  26. van Wijk R, Huizinga EG, van Wesel AC, van Oirschot BA, Hadders MA, van Solinge WW: Fifteen novel mutations in PKLR associated with pyruvate kinase (PK) deficiency: structural implications of amino acid substitutions in PK. Hum Mutat. 2009 Mar;30(3):446-53. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 6159
Enzyme 39 Name Ectonucleoside triphosphate diphosphohydrolase 4
Enzyme 39 Synonyms
  1. NTPDase 4
  2. Lysosomal apyrase-like protein of 70 kDa
  3. Uridine-diphosphatase
  4. UDPase
Enzyme 39 Gene Name ENTPD4
Enzyme 39 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 4
MGRIGISCLFPASWHFSISPVGCPRILNTNLRQIMVISVLAAAVSLLYFSVVIIRNKYGR
LTRDKKFQRYLARVTDIEATDTNNPNVNYGIVVDCGSSGSRVFVYCWPRHNGNPHDLLDI
RQMRDKNRKPVVMKIKPGISEFATSPEKVSDYISPLLNFAAEHVPRAKHKETPLYILCTA
GMRILPESQQKAILEDLLTDIPVHFDFLFSDSHAEVISGKQEGVYAWIGINFVLGRFEHI
EDDDEAVVEVNIPGSESSEAIVRKRTAGILDMGGVSTQIAYEVPKTVSFASSQQEEVAKN
LLAEFNLGCDVHQTEHVYRVYVATFLGFGGNAARQRYEDRIFANTIQKNRLLGKQTGLTP
DMPYLDPCLPLDIKDEIQQNGQTIYLRGTGDFDLCRETIQPFMNKTNETQTSLNGVYQPP
IHFQNSEFYGFSEFYYCTEDVLRMGGDYNAAKFTKAAKDYCATKWSILRERFDRGLYASH
ADLHRLKYQCFKSAWMFEVFHRGFSFPVNYKSLKTALQVYDKEVQWTLGAILYRTRFLPL
RDIQQEAFRASHTHWRGVSFVYNHYLFSGCFLVVLLAILLYLLRLRRIHRRTPRSSSAAA
LWMEEGLPAQNAPGTL
Enzyme 39 Number of Residues 616
Enzyme 39 Molecular Weight 70254.8
Enzyme 39 Theoretical pI 8.39
Enzyme 39 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 39 General Function Involved in hydrolase activity
Enzyme 39 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 39 Pathways
Enzyme 39 Reactions
  • a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • 34-54 560-580
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 4758662 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID Q9Y227 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name ENTP4_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >1851 bp
ATGGGGAGGATTGGCATCTCCTGTCTTTTTCCTGCTTCTTGGCATTTTAGCATATCTCCA
GTAGGGTGTCCTCGAATTCTGAATACCAATTTACGCCAAATTATGGTCATTAGTGTCCTG
GCTGCTGCTGTTTCACTTTTATATTTTTCTGTTGTCATAATCCGAAATAAGTATGGGCGA
CTAACCAGAGACAAGAAATTTCAAAGGTACCTGGCACGAGTTACCGACATTGAAGCTACA
GACACCAATAACCCCAATGTGAACTATGGGATCGTGGTGGACTGTGGTAGCAGTGGGTCT
CGAGTATTTGTTTACTGCTGGCCAAGGCATAATGGCAATCCACATGATCTGTTGGATATC
AGGCAAATGAGGGATAAAAACCGAAAGCCAGTGGTCATGAAGATAAAACCGGGCATTTCA
GAATTTGCTACCTCTCCAGAGAAAGTCAGTGATTACATTTCTCCACTTTTGAACTTTGCT
GCAGAGCATGTGCCACGGGCAAAACACAAAGAGACACCTCTCTACATTCTCTGCACGGCT
GGAATGAGAATCCTCCCCGAAAGCCAGCAGAAAGCTATTCTGGAAGACCTTCTGACCGAT
ATCCCCGTGCACTTTGACTTTCTGTTTTCTGACTCTCATGCAGAAGTAATTTCTGGGAAA
CAAGAAGGTGTGTATGCTTGGATTGGCATTAATTTTGTCCTTGGACGATTTGAGCATATT
GAAGATGATGATGAGGCCGTTGTGGAAGTTAACATTCCTGGAAGTGAAAGCAGCGAAGCC
ATTGTCCGTAAAAGGACAGCGGGCATTCTCGACATGGGCGGCGTGTCGACTCAGATAGCG
TACGAAGTCCCCAAAACTGTAAGCTTTGCGTCCTCACAGCAGGAAGAAGTAGCTAAAAAC
TTGTTAGCTGAATTTAACTTGGGATGTGATGTTCACCAAACTGAGCATGTGTATCGAGTC
TATGTGGCCACGTTTCTTGGGTTTGGTGGCAATGCTGCTCGACAGAGATACGAAGACAGA
ATATTTGCCAACACCATTCAAAAGAACAGGCTCCTGGGTAAACAGACTGGTCTGACTCCT
GATATGCCGTACTTGGACCCCTGCCTACCCCTAGACATTAAAGATGAAATCCAGCAAAAT
GGACAAACCATATACCTACGAGGGACTGGAGACTTTGACCTGTGTCGAGAGACTATCCAG
CCTTTCATGAATAAAACAAACGAGACCCAGACTTCCCTCAATGGGGTCTACCAGCCCCCA
ATTCACTTCCAGAACAGTGAATTCTATGGCTTCTCCGAATTCTACTACTGCACCGAGGAT
GTGTTACGAATGGGGGGAGACTACAATGCTGCTAAATTTACTAAAGCTGCAAAGGATTAT
TGTGCAACAAAGTGGTCCATTTTGCGGGAACGCTTTGACCGAGGACTGTACGCCTCTCAT
GCTGACCTCCACAGGCTTAAGTATCAGTGCTTCAAATCGGCCTGGATGTTTGAGGTGTTT
CATAGGGGCTTTTCGTTTCCTGTCAACTATAAAAGCTTAAAGACTGCCTTGCAAGTTTAC
GACAAGGAGGTTCAGTGGACCCTTGGAGCCATCCTCTACAGGACCCGCTTTCTACCATTA
AGAGACATCCAGCAGGAGGCCTTCCGAGCCAGTCACACCCACTGGCGGGGCGTTTCCTTT
GTCTACAACCACTACCTGTTCTCTGGCTGCTTCCTGGTGGTGCTGCTGGCCATCCTGCTG
TACCTGCTGCGGCTGCGGCGCATCCACAGGCGCACTCCCCGGAGCAGCTCGGCCGCCGCC
CTCTGGATGGAGGAGGGCCTTCCCGCCCAGAATGCCCCGGGGACCTTGTGA
Enzyme 39 GenBank Gene ID NM_004901.3 Link Image
Enzyme 39 GeneCard ID ENTPD4 Link Image
Enzyme 39 GenAtlas ID ENTPD4 Link Image
Enzyme 39 HGNC ID HGNC:14573 Link Image
Enzyme 39 Chromosome Location 8
Enzyme 39 Locus 8p21.3
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Wang TF, Guidotti G: Golgi localization and functional expression of human uridine diphosphatase. J Biol Chem. 1998 May 1;273(18):11392-9. [PubMed Link Image]
  2. Biederbick A, Rose S, Elsasser HP: A human intracellular apyrase-like protein, LALP70, localizes to lysosomal/autophagic vacuoles. J Cell Sci. 1999 Aug;112 ( Pt 15):2473-84. [PubMed Link Image]
  3. Biederbick A, Kosan C, Kunz J, Elsasser HP: First apyrase splice variants have different enzymatic properties. J Biol Chem. 2000 Jun 23;275(25):19018-24. [PubMed Link Image]
  4. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
  5. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 6162
Enzyme 40 Name Adenylosuccinate synthetase isozyme 2
Enzyme 40 Synonyms
  1. AMPSase 2
  2. AdSS 2
  3. Adenylosuccinate synthetase, acidic isozyme
  4. Adenylosuccinate synthetase, liver isozyme
  5. L-type adenylosuccinate synthetase
  6. IMP--aspartate ligase 2
Enzyme 40 Gene Name ADSS
Enzyme 40 Protein Sequence >Adenylosuccinate synthetase isozyme 2
MAFAETYPAASSLPNGDCGRPRARPGGNRVTVVLGAQWGDEGKGKVVDLLAQDADIVCRC
QGGNNAGHTVVVDSVEYDFHLLPSGIINPNVTAFIGNGVVIHLPGLFEEAEKNVQKGKGL
EGWEKRLIISDRAHIVFDFHQAADGIQEQQRQEQAGKNLGTTKKGIGPVYSSKAARSGLR
MCDLVSDFDGFSERFKVLANQYKSIYPTLEIDIEGELQKLKGYMEKIKPMVRDGVYFLYE
ALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGMPPQNVGEVYGVVKAY
TTRVGIGAFPTEQDNEIGELLQTRGREFGVTTGRKRRCGWLDLVLLKYAHMINGFTALAL
TKLDILDMFTEIKVGVAYKLDGEIIPHIPANQEVLNKVEVQYKTLPGWNTDISNARAFKE
LPVNAQNYVRFIEDELQIPVKWIGVGKSRESMIQLF
Enzyme 40 Number of Residues 456
Enzyme 40 Molecular Weight 50097.1
Enzyme 40 Theoretical pI 6.52
Enzyme 40 GO Classification
Function
  • GTP binding
  • adenylosuccinate synthase activity
  • binding
  • catalytic activity
  • cation binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • ion binding
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • magnesium ion binding
  • metal ion binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 40 General Function Involved in adenylosuccinate synthase activity
Enzyme 40 Specific Function Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP
Enzyme 40 Pathways
Enzyme 40 Reactions
  • GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP [RN:R01135]
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 34577063 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID P30520 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name PURA2_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >1371 bp
ATGGCGTTCGCCGAGACCTACCCGGCGGCATCCTCCCTGCCCAACGGCGATTGCGGCCGC
CCCAGGGCGCGGCCCGGAGGAAACCGGGTGACGGTGGTGCTCGGTGCGCAGTGGGGCGAC
GAAGGCAAAGGGAAGGTGGTGGACCTGCTGGCGCAGGACGCCGACATCGTGTGCCGCTGC
CAGGGAGGAAATAATGCTGGCCATACAGTTGTTGTGGATTCTGTGGAATATGATTTTCAT
CTCTTACCCAGTGGAATAATTAATCCAAATGTCACTGCATTCATTGGAAATGGTGTGGTA
ATTCATCTACCTGGATTGTTTGAAGAAGCAGAGAAAAATGTTCAAAAAGGAAAAGGACTA
GAAGGCTGGGAAAAAAGGCTTATTATATCTGACAGAGCTCATATTGTATTTGATTTTCAT
CAAGCAGCTGATGGTATCCAGGAACAACAGAGACAAGAACAAGCAGGAAAAAATTTGGGT
ACAACAAAAAAGGGCATTGGCCCAGTTTATTCGTCCAAAGCTGCTCGGAGTGGACTCAGG
ATGTGCGACCTTGTTTCTGACTTTGATGGCTTCTCTGAGAGGTTTAAAGTTCTAGCTAAC
CAATACAAATCTATATACCCCACTTTGGAAATAGACATTGAAGGTGAATTACAAAAACTC
AAGGGTTATATGGAAAAGATTAAACCAATGGTGAGAGATGGAGTTTATTTTCTATATGAG
GCCCTACATGGACCACCAAAGAAAATCTTGGTAGAAGGTGCAAATGCAGCACTATTAGAT
ATTGATTTTGGGACTTACCCTTTTGTAACCTCTTCAAATTGTACTGTTGGAGGTGTTTGT
ACTGGTTTGGGTATGCCACCTCAAAATGTTGGAGAAGTGTATGGAGTTGTGAAAGCTTAT
ACAACTAGAGTTGGTATTGGTGCCTTTCCTACAGAGCAAGACAATGAAATTGGAGAATTA
TTACAAACAAGGGGTAGAGAGTTTGGTGTAACTACTGGAAGGAAAAGAAGATGTGGCTGG
TTGGACCTCGTTTTGCTCAAATATGCTCATATGATCAATGGATTTACTGCGTTGGCACTT
ACCAAGTTGGATATTTTGGACATGTTTACGGAAATCAAAGTTGGAGTTGCTTACAAGTTA
GATGGTGAAATCATACCTCATATCCCAGCAAACCAAGAAGTCTTAAATAAAGTTGAAGTT
CAATATAAGACTCTCCCAGGATGGAACACAGACATATCAAATGCAAGGGCGTTTAAAGAA
CTACCTGTTAATGCACAAAACTATGTTCGATTTATTGAAGATGAGCTTCAAATTCCAGTT
AAGTGGATTGGTGTTGGTAAATCCAGAGAATCTATGATTCAACTCTTTTAA
Enzyme 40 GenBank Gene ID NM_001126 Link Image
Enzyme 40 GeneCard ID ADSS Link Image
Enzyme 40 GenAtlas ID ADSS Link Image
Enzyme 40 HGNC ID HGNC:292 Link Image
Enzyme 40 Chromosome Location 1
Enzyme 40 Locus 1cen-q12
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Powell SM, Zalkin H, Dixon JE: Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase. FEBS Lett. 1992 May 25;303(1):4-10. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 6166
Enzyme 41 Name Adenylosuccinate synthetase isozyme 1
Enzyme 41 Synonyms
  1. AMPSase 1
  2. AdSS 1
  3. Adenylosuccinate synthetase, basic isozyme
  4. Adenylosuccinate synthetase, muscle isozyme
  5. M-type adenylosuccinate synthetase
  6. IMP--aspartate ligase 1
Enzyme 41 Gene Name ADSSL1
Enzyme 41 Protein Sequence >Adenylosuccinate synthetase isozyme 1
MSGTRASNDRPPGAGGVKRGRLQQEAAATGSRVTVVLGAQWGDEGKGKVVDLLATDADII
SRCQGGNNAGHTVVVDGKEYDFHLLPSGIINTKAVSFIGNGVVIHLPGLFEEAEKNEKKG
LKDWEKRLIISDRAHLVFDFHQAVDGLQEVQRQAQEGKNIGTTKKGIGPTYSSKAARTGL
RICDLLSDFDEFSSRFKNLAHQHQSMFPTLEIDIEGQLKRLKGFAERIRPMVRDGVYFMY
EALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDVYGVVKA
YTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALA
LTKLDILDVLGEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWE
DLPPQAQNYIRFVENHVGVAVKWVGVGKSRESMIQLF
Enzyme 41 Number of Residues 457
Enzyme 41 Molecular Weight 50208.2
Enzyme 41 Theoretical pI 8.85
Enzyme 41 GO Classification
Function
  • GTP binding
  • adenylosuccinate synthase activity
  • binding
  • catalytic activity
  • cation binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • ion binding
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • magnesium ion binding
  • metal ion binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 41 General Function Involved in adenylosuccinate synthase activity
Enzyme 41 Specific Function Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP
Enzyme 41 Pathways
Enzyme 41 Reactions
  • GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP [RN:R01135]
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein Not Available
Enzyme 41 UniProtKB/Swiss-Prot ID Q8N142 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name PURA1_HUMAN Link Image
Enzyme 41 PDB ID 1MF1 Link Image
Enzyme 41 PDB File Show
Enzyme 41 3D Structure
Enzyme 41 Cellular Location Not Available
Enzyme 41 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 41 GenBank Gene ID AY037159 Link Image
Enzyme 41 GeneCard ID ADSSL1 Link Image
Enzyme 41 GenAtlas ID ADSSL1 Link Image
Enzyme 41 HGNC ID HGNC:20093 Link Image
Enzyme 41 Chromosome Location 1
Enzyme 41 Locus 14q32.33
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Sun H, Li N, Wang X, Chen T, Shi L, Zhang L, Wang J, Wan T, Cao X: Molecular cloning and characterization of a novel muscle adenylosuccinate synthetase, AdSSL1, from human bone marrow stromal cells. Mol Cell Biochem. 2005 Jan;269(1-2):85-94. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 6171
Enzyme 42 Name Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial
Enzyme 42 Synonyms
  1. Succinyl-CoA synthetase subunit alpha
  2. SCS-alpha
Enzyme 42 Gene Name SUCLG1
Enzyme 42 Protein Sequence >Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial
MTATLAAAADIATMVSGSSGLAAARLLSRSFLLPQNGIRHCSYTASRQHLYVDKNTKIIC
QGFTGKQGTFHSQQALEYGTKLVGGTTPGKGGQTHLGLPVFNTVKEAKEQTGATASVIYV
PPPFAAAAINEAIEAEIPLVVCITEGIPQQDMVRVKHKLLRQEKTRLIGPNCPGVINPGE
CKIGIMPGHIHKKGRIGIVSRSGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFIDCL
EIFLNDSATEGIILIGEIGGNAEENAAEFLKQHNSGPNSKPVVSFIAGLTAPPGRRMGHA
GAIIAGGKGGAKEKISALQSAGVVVSMSPAQLGTTIYKEFEKRKML
Enzyme 42 Number of Residues 346
Enzyme 42 Molecular Weight 36249.5
Enzyme 42 Theoretical pI 9.04
Enzyme 42 GO Classification
Function
  • ATP citrate synthase activity
  • CoA-ligase activity
  • binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-sulfur bonds
  • succinate-CoA ligase (ADP-forming) activity
  • succinate-CoA ligase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
Process
  • metabolic process
Component
Enzyme 42 General Function Involved in catalytic activity
Enzyme 42 Specific Function GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
Enzyme 42 Pathways
Enzyme 42 Reactions
  • GTP + succinate + CoA = GDP + phosphate + succinyl-CoA [RN:R00432]
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 109452591 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID P53597 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name SUCA_HUMAN Link Image
Enzyme 42 PDB ID 1EUC Link Image
Enzyme 42 PDB File Show
Enzyme 42 3D Structure
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >1041 bp
ATGACCGCAACCCTTGCCGCTGCCGCTGACATCGCTACCATGGTCTCCGGCAGCAGCGGC
CTCGCCGCCGCCCGTCTCCTGTCGCGCAGCTTCCTCCTGCCGCAGAATGGAATTCGGCAT
TGTTCCTACACAGCTTCTCGGCAACATCTCTATGTTGATAAAAATACAAAGATTATTTGC
CAGGGTTTCACTGGCAAACAGGGCACCTTTCACAGCCAGCAGGCATTGGAATATGGCACC
AAACTCGTTGGAGGAACCACTCCAGGGAAAGGAGGCCAGACACATCTGGGCTTACCTGTC
TTTAATACTGTGAAGGAGGCCAAAGAACAGACAGGAGCAACGGCTTCTGTCATTTATGTT
CCTCCGCCTTTTGCTGCTGCTGCCATTAATGAAGCTATTGAGGCAGAAATTCCCTTGGTT
GTGTGTATCACTGAAGGAATTCCCCAGCAGGACATGGTACGAGTCAAGCACAAACTGCTG
CGCCAGGAAAAGACAAGGCTAATTGGGCCCAACTGCCCTGGAGTCATCAATCCTGGAGAA
TGTAAAATTGGCATCATGCCTGGCCATATTCACAAAAAAGGAAGGATTGGCATTGTGTCC
AGATCTGGCACCCTGACTTATGAAGCAGTTCACCAAACAACGCAAGTTGGATTGGGGCAG
TCTTTGTGCGTTGGCATTGGAGGTGATCCTTTTAATGGAACAGATTTTATTGACTGCCTC
GAAATCTTTTTGAACGATTCTGCCACAGAAGGCATCATATTGATTGGTGAAATTGGTGGT
AATGCAGAAGAGAATGCTGCAGAATTTTTGAAGCAACATAATTCAGGTCCAAATTCCAAG
CCTGTAGTGTCCTTCATTGCTGGTTTAACTGCTCCTCCTGGGAGAAGAATGGGTCATGCC
GGGGCAATTATTGCTGGAGGAAAAGGTGGAGCTAAAGAGAAGATCTCTGCCCTTCAGAGT
GCAGGAGTTGTGGTCAGTATGTCTCCTGCACAGCTGGGAACCACGATCTACAAGGAATTT
GAAAAGAGGAAGATGCTATGA
Enzyme 42 GenBank Gene ID NM_003849.3 Link Image
Enzyme 42 GeneCard ID SUCLG1 Link Image
Enzyme 42 GenAtlas ID SUCLG1 Link Image
Enzyme 42 HGNC ID HGNC:11449 Link Image
Enzyme 42 Chromosome Location 2
Enzyme 42 Locus 2p11.2
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. James M, Man NT, Edwards YH, Morris GE: The molecular basis for cross-reaction of an anti-dystrophin antibody with alpha-actinin. Biochim Biophys Acta. 1997 Apr 12;1360(2):169-76. [PubMed Link Image]
  4. Ostergaard E, Christensen E, Kristensen E, Mogensen B, Duno M, Shoubridge EA, Wibrand F: Deficiency of the alpha subunit of succinate-coenzyme A ligase causes fatal infantile lactic acidosis with mitochondrial DNA depletion. Am J Hum Genet. 2007 Aug;81(2):383-7. Epub 2007 Jun 4. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 6172
Enzyme 43 Name Phosphoenolpyruvate carboxykinase [GTP], mitochondrial
Enzyme 43 Synonyms
  1. PEPCK-M
  2. Phosphoenolpyruvate carboxylase
Enzyme 43 Gene Name PCK2
Enzyme 43 Protein Sequence >Phosphoenolpyruvate carboxykinase [GTP], mitochondrial
MAALYRPGLRLNWHGLSPLGWPSCRSIQTLRVLSGDLGQLPTGIRDFVEHSARLCQPEGI
HICDGTEAENTATLTLLEQQGLIRKLPKYNNCWLARTDPKDVARVESKTVIVTPSQRDTV
QLPPGGARGQLGNWMSPADFQRAVDERFPGCMQGRTMYVLPFSMGPVGSPLSRIGVQLTD
SAYVVASMRIMTRLGTPVLQALGDGDFVKCLHSVGQPLTGQGEPVSQWPCNPEKTLIGHV
PDQREIISFGSGYGGNSLLGKKCFALRIASRLARDEGWLAEHMLILGITSPAGKKRYVAA
AFPSACGKTNLAMMRPALPGWKVECVGDDIAWMRFDSEGRLRAINPENGFFGVAPGTSAT
TNPNAMATIQSNTIFTNVAETSDGGVYWEGIDQPLPPGVTVTSWLGKPWKPGDKEPCAHP
NSRFCAPARQCPIMDPAWEAPEGVPIDAIIFGGRRPKGVPLVYEAFNWRHGVFVGSAMRS
ESTAAAEHKGKIIMHDPFAMRPFFGYNFGHYLEHWLSMEGRKGAQLPRIFHVNWFRRDEA
GHFLWPGFGENARVLDWICRRLEGEDSARETPIGLVPKEGALDLSGLRAIDTTQLFSLPK
DFWEQEVRDIRSYLTEQVNQDLPKEVLAELEALERRVHKM
Enzyme 43 Number of Residues 640
Enzyme 43 Molecular Weight 70729.4
Enzyme 43 Theoretical pI 7.67
Enzyme 43 GO Classification
Function
  • GTP binding
  • binding
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • lyase activity
  • nucleotide binding
  • phosphoenolpyruvate carboxykinase activity
  • purine nucleotide binding
Process
  • alcohol metabolic process
  • gluconeogenesis
  • glucose metabolic process
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 43 General Function Involved in phosphoenolpyruvate carboxykinase activity
Enzyme 43 Specific Function Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle
Enzyme 43 Pathways
Enzyme 43 Reactions
  • GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2 [RN:R00431]
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 66346721 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID Q16822 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name PCKGM_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >1923 bp
ATGGCCGCATTGTACCGCCCTGGCCTGCGGCTTAACTGGCATGGGCTGAGCCCCTTGGGC
TGGCCATCATGCCGTAGCATCCAGACCCTGCGAGTGCTTAGTGGAGATCTGGGCCAGCTT
CCCACTGGCATTCGAGATTTTGTAGAGCACAGTGCCCGCCTGTGCCAACCAGAGGGCATC
CACATCTGTGATGGAACTGAGGCTGAGAATACTGCCACACTGACCCTGCTGGAGCAGCAG
GGCCTCATCCGAAAGCTCCCCAAGTACAATAACTGCTGGCTGGCCCGCACAGACCCCAAG
GATGTGGCACGAGTAGAGAGCAAGACGGTGATTGTAACTCCTTCTCAGCGGGACACGGTA
CAACTCCCGCCTGGTGGGGCCCGTGGGCAGCTGGGCAACTGGATGTCCCCAGCTGATTTC
CAGCGAGCTGTGGATGAGAGGTTTCCAGGCTGCATGCAGGGCCGCACCATGTATGTGCTT
CCATTCAGCATGGGTCCTGTGGGCTCCCCGCTGTCCCGCATCGGGGTGCAGCTCACTGAC
TCAGCCTATGTGGTGGCAAGCATGCGTATTATGACCCGACTGGGGACACCTGTGCTTCAG
GCCCTGGGAGATGGTGACTTTGTCAAGTGTCTGCACTCCGTGGGCCAGCCCCTGACAGGA
CAAGGGGAGCCAGTGAGCCAGTGGCCGTGCAACCCAGAGAAAACCCTGATTGGCCACGTG
CCCGACCAGCGGGAGATCATCTCCTTCGGCAGCGGCTATGGTGGCAACTCCCTGCTGGGC
AAGAAGTGCTTTGCCCTACGCATCGCCTCTCGGCTGGCCCGGGATGAGGGCTGGCTGGCA
GAGCACATGCTGATCCTGGGCATCACCAGCCCTGCAGGGAAGAAGCGCTATGTGGCAGCC
GCCTTCCCTAGTGCCTGTGGCAAGACCAACCTGGCTATGATGCGGCCTGCACTGCCAGGC
TGGAAAGTGGAGTGTGTGGGGGATGATATTGCTTGGATGAGGTTTGACAGTGAAGGTCGA
CTCCGGGCCATCAACCCTGAGAACGGCTTCTTTGGGGTTGCCCCTGGTACCTCTGCCACC
ACCAATCCCAACGCCATGGCTACAATCCAGAGTAACACTATTTTTACCAATGTGGCTGAG
ACCAGTGATGGTGGCGTGTACTGGGAGGGCATTGACCAGCCTCTTCCACCTGGTGTTACT
GTGACCTCCTGGCTGGGCAAACCCTGGAAACCTGGTGACAAGGAGCCCTGTGCACATCCC
AACTCTCGATTTTGTGCCCCGGCTCGCCAGTGCCCCATCATGGACCCAGCCTGGGAGGCC
CCAGAGGGTGTCCCCATTGACGCCATCATCTTTGGTGGCCGCAGACCCAAAGGGGTACCC
CTGGTATACGAGGCCTTCAACTGGCGTCATGGGGTGTTTGTGGGCAGCGCCATGCGCTCT
GAGTCCACTGCTGCAGCAGAACACAAAGGGAAGATCATCATGCACGACCCATTTGCCATG
CGGCCCTTTTTTGGCTACAACTTCGGGCACTACCTGGAACACTGGCTGAGCATGGAAGGG
CGCAAGGGGGCCCAGCTGCCCCGTATCTTCCATGTCAACTGGTTCCGGCGTGACGAGGCA
GGGCACTTCCTGTGGCCAGGCTTTGGGGAGAATGCTCGGGTGCTAGACTGGATCTGCCGG
CGGTTAGAGGGGGAGGACAGTGCCCGAGAGACACCCATTGGGCTGGTGCCAAAGGAAGGA
GCCTTGGATCTCAGCGGCCTCAGAGCTATAGACACCACTCAGCTGTTCTCCCTCCCCAAG
GACTTCTGGGAACAGGAGGTTCGTGACATTCGGAGCTACCTGACAGAGCAGGTCAACCAG
GATCTGCCCAAAGAGGTGTTGGCTGAGCTTGAGGCCCTGGAGAGACGTGTGCACAAAATG
TGA
Enzyme 43 GenBank Gene ID NM_004563.2 Link Image
Enzyme 43 GeneCard ID PCK2 Link Image
Enzyme 43 GenAtlas ID PCK2 Link Image
Enzyme 43 HGNC ID HGNC:8725 Link Image
Enzyme 43 Chromosome Location 1
Enzyme 43 Locus 14q11.2
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Modaressi S, Christ B, Bratke J, Zahn S, Heise T, Jungermann K: Molecular cloning, sequencing and expression of the cDNA of the mitochondrial form of phosphoenolpyruvate carboxykinase from human liver. Biochem J. 1996 May 1;315 ( Pt 3):807-14. [PubMed Link Image]
  2. Modaressi S, Brechtel K, Christ B, Jungermann K: Human mitochondrial phosphoenolpyruvate carboxykinase 2 gene. Structure, chromosomal localization and tissue-specific expression. Biochem J. 1998 Jul 15;333 ( Pt 2):359-66. [PubMed Link Image]
  3. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 6173
Enzyme 44 Name Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial
Enzyme 44 Synonyms
  1. GTP-specific succinyl-CoA synthetase subunit beta
  2. Succinyl-CoA synthetase beta-G chain
  3. SCS-betaG
Enzyme 44 Gene Name SUCLG2
Enzyme 44 Protein Sequence >Succinyl-CoA ligase [GDP-forming] subunit beta, mitochondrial
MASPVAAQAGKLLRALALRPRFLAAGSQAVQLTSRRWLNLQEYQSKKLMSDNGVRVQRFF
VADTANEALEAAKRLNAKEIVLKAQILAGGRGKGVFNSGLKGGVHLTKDPNVVGQLAKQM
IGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSCNGPVLVGSPQGGVDIEEV
AASNPELIFKEQIDIFEGIKDSQAQRMAENLGFVGPLKSQAADQITKLYNLFLKIDATQV
EVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAAKYDLKYIGLD
GNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKEAQVYQAFKLLTADPKVEAILV
NIFGGIVNCAIIANGITKACRELELKVPLVVRLEGTNVQEAQKILNNSGLPITSAIDLED
AAKKAVASVAKK
Enzyme 44 Number of Residues 432
Enzyme 44 Molecular Weight 46510.2
Enzyme 44 Theoretical pI 6.18
Enzyme 44 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • purine nucleoside binding
Process
  • metabolic process
Component
Enzyme 44 General Function Involved in catalytic activity
Enzyme 44 Specific Function GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
Enzyme 44 Pathways
Enzyme 44 Reactions
  • GTP + succinate + CoA = GDP + phosphate + succinyl-CoA [RN:R00432]
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 157779135 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID Q96I99 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name SUCB2_HUMAN Link Image
Enzyme 44 PDB ID 1EUC Link Image
Enzyme 44 PDB File Show
Enzyme 44 3D Structure
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence >1299 bp
ATGGCGTCCCCCGTAGCAGCGCAGGCCGGGAAGCTTCTGCGAGCCCTAGCGCTGCGGCCC
CGCTTCCTGGCGGCCGGGTCCCAGGCAGTTCAATTAACCTCCAGAAGATGGCTGAACCTG
CAGGAATACCAGAGCAAGAAACTGATGTCTGACAACGGAGTGAGAGTTCAAAGATTCTTT
GTAGCAGACACTGCAAATGAAGCTCTCGAGGCTGCTAAGAGACTAAATGCAAAAGAAATT
GTTTTAAAAGCCCAGATCTTAGCTGGAGGAAGAGGAAAAGGTGTCTTCAATAGTGGTTTG
AAAGGAGGTGTTCATTTAACAAAAGACCCTAATGTTGTGGGACAGCTGGCTAAACAGATG
ATTGGGTACAATCTAGCGACAAAACAAACTCCAAAAGAAGGTGTGAAAGTTAACAAGGTG
ATGGTTGCTGAAGCCTTGGATATTTCCAGAGAAACCTACCTGGCAATTCTGATGGACCGG
TCCTGCAATGGCCCCGTGCTGGTGGGCAGCCCCCAGGGGGGCGTCGACATTGAAGAGGTG
GCTGCTTCAAACCCGGAGCTCATTTTTAAGGAGCAAATTGACATTTTTGAAGGAATAAAG
GACAGCCAAGCTCAGCGGATGGCCGAAAATCTAGGCTTCGTTGGGCCTTTGAAAAGCCAG
GCTGCAGATCAAATTACGAAGCTGTATAATCTCTTCCTGAAAATTGATGCTACTCAGGTG
GAAGTGAATCCCTTTGGTGAAACTCCAGAAGGACAAGTTGTCTGTTTTGATGCCAAGATA
AACTTTGATGACAACGCAGAATTCCGACAAAAAGACATATTTGCTATGGACGACAAATCA
GAGAATGAGCCCATTGAAAATGAAGCTGCCAAATATGATCTAAAATACATAGGACTAGAT
GGGAACATTGCCTGCTTTGTGAATGGTGCTGGGCTCGCCATGGCTACTTGTGATATCATT
TTCCTTAATGGTGGGAAGCCAGCCAACTTCTTGGATCTTGGAGGTGGTGTAAAGGAAGCT
CAAGTATATCAAGCATTCAAATTGCTCACAGCTGATCCTAAGGTTGAAGCCATCCTTGTC
AATATATTTGGTGGTATCGTCAACTGTGCCATCATTGCCAATGGGATCACCAAAGCCTGC
CGGGAGCTAGAACTCAAGGTGCCCCTGGTGGTCCGGCTTGAAGGAACCAACGTCCAAGAG
GCCCAGAAGATACTCAACAACAGCGGACTCCCCATTACTTCAGCCATTGACCTGGAGGAT
GCAGCCAAGAAGGCTGTGGCCAGTGTGGCCAAGAAGTGA
Enzyme 44 GenBank Gene ID NM_003848.3 Link Image
Enzyme 44 GeneCard ID SUCLG2 Link Image
Enzyme 44 GenAtlas ID SUCLG2 Link Image
Enzyme 44 HGNC ID HGNC:11450 Link Image
Enzyme 44 Chromosome Location 3
Enzyme 44 Locus 3p14.1
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  2. Johnson JD, Mehus JG, Tews K, Milavetz BI, Lambeth DO: Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes. J Biol Chem. 1998 Oct 16;273(42):27580-6. [PubMed Link Image]
  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 6174
Enzyme 45 Name Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
Enzyme 45 Synonyms
  1. PEPCK-C
  2. Phosphoenolpyruvate carboxylase
Enzyme 45 Gene Name PCK1
Enzyme 45 Protein Sequence >Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
MPPQLQNGLNLSAKVVQGSLDSLPQAVREFLENNAELCQPDHIHICDGSEEENGRLLGQM
EEEGILRRLKKYDNCWLALTDPRDVARIESKTVIVTQEQRDTVPIPKTGLSQLGRWMSEE
DFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLSKIGIELTDSPYVVASMRIMTRMGTPV
LEAVGDGEFVKCLHSVGCPLPLQKPLVNNWPCNPELTLIAHLPDRREIISFGSGYGGNSL
LGKKCFALRMASRLAKEEGWLAEHMLILGITNPEGEKKYLAAAFPSACGKTNLAMMNPSL
PGWKVECVGDDIAWMKFDAQGHLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNV
AETSDGGVYWEGIDEPLASGVTITSWKNKEWSSEDGEPCAHPNSRFCTPASQCPIIDAAW
ESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKIIMHDPF
AMRPFFGYNFGKYLAHWLSMAQHPAAKLPKIFHVNWFRKDKEGKFLWPGFGENSRVLEWM
FNRIDGKASTKLTPIGYIPKEDALNLKGLGHINMMELFSISKEFWEKEVEDIEKYLEDQV
NADLPCEIEREILALKQRISQM
Enzyme 45 Number of Residues 622
Enzyme 45 Molecular Weight 69194.0
Enzyme 45 Theoretical pI 6.05
Enzyme 45 GO Classification
Function
  • GTP binding
  • binding
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • lyase activity
  • nucleotide binding
  • phosphoenolpyruvate carboxykinase activity
  • purine nucleotide binding
Process
  • alcohol metabolic process
  • gluconeogenesis
  • glucose metabolic process
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 45 General Function Involved in phosphoenolpyruvate carboxykinase activity
Enzyme 45 Specific Function Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle
Enzyme 45 Pathways
Enzyme 45 Reactions
  • GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2 [RN:R00431]
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 189945 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID P35558 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name PCKGC_HUMAN Link Image
Enzyme 45 PDB ID 1NHX Link Image
Enzyme 45 PDB File Show
Enzyme 45 3D Structure
Enzyme 45 Cellular Location Not Available
Enzyme 45 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 45 GenBank Gene ID L05144 Link Image
Enzyme 45 GeneCard ID PCK1 Link Image
Enzyme 45 GenAtlas ID PCK1 Link Image
Enzyme 45 HGNC ID HGNC:8724 Link Image
Enzyme 45 Chromosome Location 2
Enzyme 45 Locus 20q13.31
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References
  1. Stoffel M, Xiang KS, Espinosa R 3rd, Cox NJ, Le Beau MM, Bell GI: cDNA sequence and localization of polymorphic human cytosolic phosphoenolpyruvate carboxykinase gene (PCK1) to chromosome 20, band q13.31: PCK1 is not tightly linked to maturity-onset diabetes of the young. Hum Mol Genet. 1993 Jan;2(1):1-4. [PubMed Link Image]
  2. Ting CN, Burgess DL, Chamberlain JS, Keith TP, Falls K, Meisler MH: Phosphoenolpyruvate carboxykinase (GTP): characterization of the human PCK1 gene and localization distal to MODY on chromosome 20. Genomics. 1993 Jun;16(3):698-706. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. O'Brien RM, Printz RL, Halmi N, Tiesinga JJ, Granner DK: Structural and functional analysis of the human phosphoenolpyruvate carboxykinase gene promoter. Biochim Biophys Acta. 1995 Dec 27;1264(3):284-8. [PubMed Link Image]
  7. Liu J, Hanson RW: Regulation of phosphoenolpyruvate carboxykinase (GTP) gene transcription. Mol Cell Biochem. 1991 May 29-Jun 12;104(1-2):89-100. [PubMed Link Image]
  8. Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL: Regulation of cellular metabolism by protein lysine acetylation. Science. 2010 Feb 19;327(5968):1000-4. [PubMed Link Image]
  9. Dunten P, Belunis C, Crowther R, Hollfelder K, Kammlott U, Levin W, Michel H, Ramsey GB, Swain A, Weber D, Wertheimer SJ: Crystal structure of human cytosolic phosphoenolpyruvate carboxykinase reveals a new GTP-binding site. J Mol Biol. 2002 Feb 15;316(2):257-64. [PubMed Link Image]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 6209
Enzyme 46 Name Adenylate cyclase type 2
Enzyme 46 Synonyms
  1. ATP pyrophosphate-lyase 2
  2. Adenylate cyclase type II
  3. Adenylyl cyclase 2
Enzyme 46 Gene Name ADCY2
Enzyme 46 Protein Sequence >Adenylate cyclase type 2
MWQEAMRRRRYLRDRSEEAAGGGDGLPRSRDWLYESYYCMSQQHPLIVFLLLIVMGSCLA
LLAVFFALGLEVEDHVAFLITVPTALAIFFAIFILVCIESVFKKLLRLFSLVIWICLVAM
GYLFMCFGGTVSPWDQVSFFLFIIFVVYTMLPFNMRDAIIASVLTSSSHTIVLSVCLSAT
PGGKEHLVWQILANVIIFICGNLAGAYHKHLMELALQQTYQDTCNCIKSRIKLEFEKRQQ
ERLLLSLLPAHIAMEMKAEIIQRLQGPKAGQMENTNNFHNLYVKRHTNVSILYADIVGFT
RLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVK
MGLDMCEAIKKVRDATGVDINMRVGVHSGNVLCGVIGLQKWQYDVWSHDVTLANHMEAGG
VPGRVHISSVTLEHLNGAYKVEEGDGDIRDPYLKQHLVKTYFVINPKGERRSPQHLFRPR
HTLDGAKMRASVRMTRYLESWGAAKPFAHLHHRDSMTTENGKISTTDVPMGQHNFQNRTL
RTKSQKKRFEEELNERMIQAIDGINAQKQWLKSEDIQRISLLFYNKVLEKEYRATALPAF
KYYVTCACLIFFCIFIVQILVLPKTSVLGISFGAAFLLLAFILFVCFAGQLLQCSKKASP
LLMWLLKSSGIIANRPWPRISLTIITTAIILMMAVFNMFFLSDSEETIPPTANTTNTSFS
ASNNQVAILRAQNLFFLPYFIYSCILGLISCSVFLRVNYELKMLIMMVALVGYNTILLHT
HAHVLGDYSQVLFERPGIWKDLKTMGSVSLSIFFITLLVLGRQNEYYCRLDFLWKNKFKK
EREEIETMENLNRVLLENVLPAHVAEHFLARSLKNEELYHQSYDCVCVMFASIPDFKEFY
TESDVNKEGLECLRLLNEIIADFDDLLSKPKFSGVEKIKTIGSTYMAATGLSAVPSQEHS
QEPERQYMHIGTMVEFAFALVGKLDAINKHSFNDFKLRVGINHGPVIAGVIGAQKPQYDI
WGNTVNVASRMDSTGVLDKIQVTEETSLVLQTLGYTCTCRGIINVKGKGDLKTYFVNTEM
SRSLSQSNVAS
Enzyme 46 Number of Residues 1091
Enzyme 46 Molecular Weight 123602.2
Enzyme 46 Theoretical pI 8.15
Enzyme 46 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 46 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 46 Specific Function This is a membrane-bound, calmodulin-insensitive adenylyl cyclase
Enzyme 46 Pathways
Enzyme 46 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • 46-66 76-96 108-128 133-153 159-179 187-207 602-622 628-652 680-701 734-755 763-780 801-821
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 115387102 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID Q08462 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name ADCY2_HUMAN Link Image
Enzyme 46 PDB ID 1AB8 Link Image
Enzyme 46 PDB File Show
Enzyme 46 3D Structure
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >3276 bp
ATGTGGCAGGAGGCGATGCGGCGCCGCCGCTACCTGCGGGACCGCTCCGAGGAGGCGGCG
GGCGGCGGAGACGGGCTGCCGCGGTCCCGGGACTGGCTCTACGAGTCCTACTACTGCATG
AGCCAGCAGCACCCGCTCATCGTCTTCCTGCTGCTCATCGTCATGGGCTCCTGCCTCGCC
CTGCTCGCCGTCTTCTTCGCGCTCGGGCTGGAAGTTGAAGACCATGTGGCGTTTCTAATA
ACAGTTCCAACTGCCCTGGCGATTTTCTTTGCGATATTTATCCTGGTCTGCATCGAGTCT
GTGTTTAAGAAGCTGCTGCGCCTCTTCTCGTTGGTGATATGGATATGCCTTGTTGCCATG
GGATACCTGTTCATGTGTTTTGGAGGCACCGTCTCTCCCTGGGACCAGGTATCGTTCTTC
CTCTTCATCATCTTCGTGGTGTACACCATGCTGCCCTTCAACATGCGAGACGCCATCATT
GCCAGCGTCCTCACCTCCTCCTCCCACACCATCGTGCTTAGCGTCTGCCTGTCTGCAACA
CCGGGAGGCAAGGAGCACCTGGTCTGGCAGATCCTGGCCAATGTGATCATTTTCATCTGT
GGGAACCTGGCGGGAGCCTACCATAAGCACCTCATGGAACTCGCTCTTCAGCAAACATAT
CAGGACACCTGTAATTGCATCAAGTCGCGGATCAAGTTGGAATTTGAAAAACGTCAACAG
GAGCGGCTTCTGCTCTCCCTGCTGCCGGCCCACATCGCCATGGAGATGAAAGCGGAGATC
ATCCAGAGGCTGCAGGGCCCCAAGGCGGGCCAGATGGAGAACACAAATAACTTCCACAAC
CTGTATGTGAAGCGGCATACAAACGTGAGCATCTTATACGCTGACATCGTTGGCTTTACC
CGGCTGGCAAGTGACTGCTCCCCGGGAGAACTAGTCCACATGCTGAATGAGCTCTTTGGA
AAGTTTGATCAAATTGCAAAGGAGAATGAATGCATGAGAATTAAAATTTTAGGAGACTGC
TACTACTGTGTATCTGGACTCCCTATATCTCTCCCTAACCATGCCAAGAACTGTGTGAAA
ATGGGGCTGGACATGTGTGAAGCCATAAAGAAAGTGAGGGATGCTACTGGAGTTGATATC
AACATGCGCGTGGGCGTGCATTCTGGGAATGTCCTGTGTGGCGTGATTGGTCTGCAGAAG
TGGCAATATGATGTGTGGTCACATGATGTGACCTTGGCCAACCACATGGAAGCTGGAGGG
GTCCCTGGACGTGTTCACATTTCTTCTGTCACCCTGGAGCACTTGAATGGCGCTTATAAA
GTGGAGGAGGGAGATGGTGACATTAGGGACCCATATTTAAAACAGCACCTGGTGAAAACC
TACTTTGTGATCAACCCCAAGGGAGAACGACGGAGCCCCCAGCATCTCTTCAGACCTCGC
CACACCCTTGATGGAGCCAAAATGAGGGCCTCGGTCCGCATGACCCGGTACTTGGAGTCC
TGGGGGGCAGCCAAGCCCTTTGCACACCTACATCACAGGGACAGCATGACCACAGAGAAC
GGCAAGATCAGCACCACGGATGTACCCATGGGTCAGCATAATTTTCAAAATCGCACCTTA
AGAACCAAGTCACAAAAGAAGAGATTTGAAGAAGAATTGAATGAAAGGATGATTCAAGCA
ATTGATGGGATTAATGCACAGAAGCAATGGCTCAAGTCTGAAGACATTCAGAGAATCTCA
CTGCTTTTCTATAACAAAGTACTAGAAAAAGAGTACCGGGCCACGGCACTGCCAGCGTTC
AAGTATTATGTGACTTGTGCCTGTCTCATATTCTTCTGCATCTTCATTGTGCAGATTCTC
GTGCTGCCAAAAACGTCCGTCCTGGGCATCTCCTTTGGGGCTGCGTTTCTCTTGCTGGCC
TTCATCCTCTTCGTCTGCTTTGCTGGACAGCTTCTGCAATGCAGCAAAAAAGCCTCTCCC
CTGCTCATGTGGCTTTTGAAGTCCTCGGGCATCATTGCCAACCGCCCCTGGCCACGGATC
TCTCTCACGATCATCACCACAGCCATCATATTAATGATGGCCGTGTTCAACATGTTTTTC
CTGAGTGACTCAGAGGAAACAATCCCTCCAACTGCCAACACAACAAACACAAGCTTTTCA
GCCTCAAATAATCAGGTGGCGATTCTGCGTGCGCAGAATTTATTTTTCCTCCCGTACTTT
ATCTACAGCTGCATTCTGGGACTGATATCCTGTTCCGTGTTCCTGCGGGTAAACTATGAG
CTGAAGATGTTGATCATGATGGTGGCCTTGGTGGGCTACAACACCATCCTACTCCACACC
CACGCCCACGTCCTGGGCGACTACAGCCAGGTCTTATTTGAGAGACCAGGCATTTGGAAA
GACCTGAAGACCATGGGCTCTGTGTCTCTCTCTATATTCTTCATCACACTGCTTGTTCTG
GGTAGACAGAATGAATATTACTGTAGGTTAGACTTCTTATGGAAGAACAAATTCAAAAAA
GAGCGGGAGGAGATAGAGACCATGGAGAACCTGAACCGCGTGCTGCTGGAGAACGTGCTT
CCCGCGCACGTGGCTGAGCACTTCCTGGCCAGGAGCCTGAAGAATGAGGAGCTATACCAC
CAGTCCTATGACTGCGTCTGCGTCATGTTTGCCTCCATTCCGGATTTCAAAGAATTTTAT
ACAGAATCCGACGTGAACAAGGAGGGCTTGGAATGCCTTCGGCTCCTGAACGAGATCATC
GCTGACTTTGATGATCTTCTTTCCAAGCCAAAATTCAGTGGAGTTGAAAAGATTAAGACC
ATTGGCAGCACATACATGGCAGCAACAGGTCTGAGCGCTGTGCCCAGCCAGGAGCACTCC
CAGGAGCCCGAGCGGCAGTACATGCACATTGGCACCATGGTGGAGTTTGCTTTTGCCCTG
GTAGGGAAGCTGGATGCCATCAACAAGCACTCCTTCAACGACTTCAAATTGCGAGTGGGT
ATTAACCATGGACCTGTGATAGCTGGTGTGATTGGAGCTCAGAAGCCACAATATGATATC
TGGGGCAACACTGTCAATGTGGCCAGTAGGATGGACAGCACCGGAGTCCTGGACAAAATA
CAGGTTACCGAGGAGACGAGCCTCGTCCTGCAGACCCTCGGATACACGTGCACCTGTCGA
GGAATAATCAACGTGAAAGGAAAGGGGGACCTGAAGACGTACTTTGTAAACACAGAAATG
TCAAGGTCCCTTTCCCAGAGCAACGTGGCATCCTGA
Enzyme 46 GenBank Gene ID NM_020546.2 Link Image
Enzyme 46 GeneCard ID ADCY2 Link Image
Enzyme 46 GenAtlas ID ADCY2 Link Image
Enzyme 46 HGNC ID HGNC:233 Link Image
Enzyme 46 Chromosome Location 5
Enzyme 46 Locus 5p15.3
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  2. Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [PubMed Link Image]
  3. Stengel D, Parma J, Gannage MH, Roeckel N, Mattei MG, Barouki R, Hanoune J: Different chromosomal localization of two adenylyl cyclase genes expressed in human brain. Hum Genet. 1992 Sep-Oct;90(1-2):126-30. [PubMed Link Image]
  4. Hellevuo K, Yoshimura M, Kao M, Hoffman PL, Cooper DM, Tabakoff B: A novel adenylyl cyclase sequence cloned from the human erythroleukemia cell line. Biochem Biophys Res Commun. 1993 Apr 15;192(1):311-8. [PubMed Link Image]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 6226
Enzyme 47 Name GTP cyclohydrolase 1
Enzyme 47 Synonyms
  1. GTP cyclohydrolase I
  2. GTP-CH-I
Enzyme 47 Gene Name GCH1
Enzyme 47 Protein Sequence >GTP cyclohydrolase 1
MEKGPVRAPAEKPRGARCSNGFPERDPPRPGPSRPAEKPPRPEAKSAQPADGWKGERPRS
EEDNELNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETISDVLNDA
IFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQ
VQERLTKQIAVAITEALRPAGVGVVVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKT
REEFLTLIRS
Enzyme 47 Number of Residues 250
Enzyme 47 Molecular Weight 27902.9
Enzyme 47 Theoretical pI 8.82
Enzyme 47 GO Classification
Function
  • GTP cyclohydrolase I activity
  • GTP cyclohydrolase activity
  • catalytic activity
  • cyclohydrolase activity
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
Process
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • folic acid and derivative biosynthetic process
  • folic acid and derivative metabolic process
  • metabolic process
  • tetrahydrofolate biosynthetic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 47 General Function Involved in GTP cyclohydrolase I activity
Enzyme 47 Specific Function Positively regulates nitric oxide synthesis in umbilical vein endothelial cells (HUVECs). May be involved in dopamine synthesis. May modify pain sensitivity and persistence. Isoform GCH-1 is the functional enzyme, the potential function of the enzymatically inactive isoforms remains unknown
Enzyme 47 Pathways
Enzyme 47 Reactions
  • GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate [RN:R00424]
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 19343964 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID P30793 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name GCH1_HUMAN Link Image
Enzyme 47 PDB ID 1IS8 Link Image
Enzyme 47 PDB File Show
Enzyme 47 3D Structure
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence >753 bp
ATGGAGAAGGGCCCTGTGCGGGCACCGGCGGAGAAGCCGCGGGGCGCCAGGTGCAGCAAT
GGGTTCCCCGAGCGGGATCCGCCGCGGCCCGGGCCCAGCAGGCCGGCGGAGAAGCCCCCG
CGGCCCGAGGCCAAGAGCGCGCAGCCCGCGGACGGCTGGAAGGGCGAGCGGCCCCGCAGC
GAGGAGGATAACGAGCTGAACCTCCCTAACCTGGCAGCCGCCTACTCGTCCATCCTGAGC
TCGCTGGGCGAGAACCCCCAGCGGCAAGGGCTGCTCAAGACGCCCTGGAGGGCGGCCTCG
GCCATGCAGTTCTTCACCAAGGGCTACCAGGAGACCATCTCAGATGTCCTAAACGATGCT
ATATTTGATGAAGATCATGATGAGATGGTGATTGTGAAGGACATAGACATGTTTTCCATG
TGTGAGCATCACTTGGTTCCATTTGTTGGAAAGGTCCATATTGGTTATCTTCCTAACAAG
CAAGTCCTTGGCCTCAGCAAACTTGCGAGGATTGTAGAAATCTATAGTAGAAGACTACAA
GTTCAGGAGCGCCTTACAAAACAAATTGCTGTAGCAATCACGGAAGCCTTGCGGCCTGCT
GGAGTCGGGGTAGTGGTTGAAGCAACACACATGTGTATGGTAATGCGAGGTGTACAGAAA
ATGAACAGCAAAACTGTGACCAGCACAATGTTGGGTGTGTTCCGGGAGGATCCAAAGACT
CGGGAAGAGTTCCTGACTCTCATTAGGAGCTGA
Enzyme 47 GenBank Gene ID BC025415 Link Image
Enzyme 47 GeneCard ID GCH1 Link Image
Enzyme 47 GenAtlas ID GCH1 Link Image
Enzyme 47 HGNC ID HGNC:4193 Link Image
Enzyme 47 Chromosome Location 1
Enzyme 47 Locus 14q22.1-q22.2
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References
  1. Togari A, Ichinose H, Matsumoto S, Fujita K, Nagatsu T: Multiple mRNA forms of human GTP cyclohydrolase I. Biochem Biophys Res Commun. 1992 Aug 31;187(1):359-65. [PubMed Link Image]
  2. Gutlich M, Jaeger E, Rucknagel KP, Werner T, Rodl W, Ziegler I, Bacher A: Human GTP cyclohydrolase I: only one out of three cDNA isoforms gives rise to the active enzyme. Biochem J. 1994 Aug 15;302 ( Pt 1):215-21. [PubMed Link Image]
  3. Nomura T, Ohtsuki M, Matsui S, Sumi-Ichinose C, Nomura H, Hagino Y, Iwase K, Ichinose H, Fujita K, Nagatsu T: Isolation of a full-length cDNA clone for human GTP cyclohydrolase I type 1 from pheochromocytoma. J Neural Transm Gen Sect. 1995;101(1-3):237-42. [PubMed Link Image]
  4. Golderer G, Werner ER, Heufler C, Strohmaier W, Grobner P, Werner-Felmayer G: GTP cyclohydrolase I mRNA: novel splice variants in the slime mould Physarum polycephalum and in human monocytes (THP-1) indicate conservation of mRNA processing. Biochem J. 2001 Apr 15;355(Pt 2):499-507. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Witter K, Werner T, Blusch JH, Schneider EM, Riess O, Ziegler I, Rodl W, Bacher A, Gutlich M: Cloning, sequencing and functional studies of the gene encoding human GTP cyclohydrolase I. Gene. 1996 Jun 1;171(2):285-90. [PubMed Link Image]
  7. Gutlich M, Schott K, Werner T, Bacher A, Ziegler I: Species and tissue specificity of mammalian GTP cyclohydrolase I messenger RNA. Biochim Biophys Acta. 1992 Dec 29;1171(2):133-40. [PubMed Link Image]
  8. Ichinose H, Ohye T, Matsuda Y, Hori T, Blau N, Burlina A, Rouse B, Matalon R, Fujita K, Nagatsu T: Characterization of mouse and human GTP cyclohydrolase I genes. Mutations in patients with GTP cyclohydrolase I deficiency. J Biol Chem. 1995 Apr 28;270(17):10062-71. [PubMed Link Image]
  9. Blau N, Niederwieser A: The application of 8-aminoguanosine triphosphate, a new inhibitor of GTP cyclohydrolase I, to the purification of the enzyme from human liver. Biochim Biophys Acta. 1986 Jan 15;880(1):26-31. [PubMed Link Image]
  10. Shen RS, Alam A, Zhang YX: Human liver GTP cyclohydrolase I: purification and some properties. Biochimie. 1989 Mar;71(3):343-9. [PubMed Link Image]
  11. Schoedon G, Redweik U, Curtius HC: Purification of GTP cyclohydrolase I from human liver and production of specific monoclonal antibodies. Eur J Biochem. 1989 Jan 2;178(3):627-34. [PubMed Link Image]
  12. Werner-Felmayer G, Werner ER, Fuchs D, Hausen A, Reibnegger G, Schmidt K, Weiss G, Wachter H: Pteridine biosynthesis in human endothelial cells. Impact on nitric oxide-mediated formation of cyclic GMP. J Biol Chem. 1993 Jan 25;268(3):1842-6. [PubMed Link Image]
  13. Thony B, Blau N: Mutations in the GTP cyclohydrolase I and 6-pyruvoyl-tetrahydropterin synthase genes. Hum Mutat. 1997;10(1):11-20. [PubMed Link Image]
  14. Katusic ZS, Stelter A, Milstien S: Cytokines stimulate GTP cyclohydrolase I gene expression in cultured human umbilical vein endothelial cells. Arterioscler Thromb Vasc Biol. 1998 Jan;18(1):27-32. [PubMed Link Image]
  15. Cai S, Alp NJ, McDonald D, Smith I, Kay J, Canevari L, Heales S, Channon KM: GTP cyclohydrolase I gene transfer augments intracellular tetrahydrobiopterin in human endothelial cells: effects on nitric oxide synthase activity, protein levels and dimerisation. Cardiovasc Res. 2002 Sep;55(4):838-49. [PubMed Link Image]
  16. Ohtsuki M, Shiraishi H, Kato T, Kuroda R, Tazawa M, Sumi-Ichinose C, Tada S, Udagawa Y, Itoh M, Hishida H, Ichinose H, Nagatsu T, Hagino Y, Nomura T: cAMP inhibits cytokine-induced biosynthesis of tetrahydrobiopterin in human umbilical vein endothelial cells. Life Sci. 2002 Mar 22;70(18):2187-98. [PubMed Link Image]
  17. Gesierich A, Niroomand F, Tiefenbacher CP: Role of human GTP cyclohydrolase I and its regulatory protein in tetrahydrobiopterin metabolism. Basic Res Cardiol. 2003 Mar;98(2):69-75. [PubMed Link Image]
  18. Shiraishi H, Kato T, Atsuta K, Sumi-Ichinose C, Ohtsuki M, Itoh M, Hishida H, Tada S, Udagawa Y, Nagatsu T, Hagino Y, Ichinose H, Nomura T: cGMP inhibits GTP cyclohydrolase I activity and biosynthesis of tetrahydrobiopterin in human umbilical vein endothelial cells. J Pharmacol Sci. 2003 Nov;93(3):265-71. [PubMed Link Image]
  19. Suzuki T, Kurita H, Ichinose H: GTP cyclohydrolase I utilizes metal-free GTP as its substrate. Eur J Biochem. 2004 Jan;271(2):349-55. [PubMed Link Image]
  20. Duan CL, Su Y, Zhao CL, Lu LL, Xu QY, Yang H: The assays of activities and function of TH, AADC, and GCH1 and their potential use in ex vivo gene therapy of PD. Brain Res Brain Res Protoc. 2005 Dec;16(1-3):37-43. [PubMed Link Image]
  21. Huang A, Zhang YY, Chen K, Hatakeyama K, Keaney JF Jr: Cytokine-stimulated GTP cyclohydrolase I expression in endothelial cells requires coordinated activation of nuclear factor-kappaB and Stat1/Stat3. Circ Res. 2005 Feb 4;96(2):164-71. Epub 2004 Dec 16. [PubMed Link Image]
  22. Kalivendi S, Hatakeyama K, Whitsett J, Konorev E, Kalyanaraman B, Vasquez-Vivar J: Changes in tetrahydrobiopterin levels in endothelial cells and adult cardiomyocytes induced by LPS and hydrogen peroxide--a role for GFRP? Free Radic Biol Med. 2005 Feb 15;38(4):481-91. [PubMed Link Image]
  23. Pandya MJ, Golderer G, Werner ER, Werner-Felmayer G: Interaction of human GTP cyclohydrolase I with its splice variants. Biochem J. 2006 Nov 15;400(1):75-80. [PubMed Link Image]
  24. Chavan B, Gillbro JM, Rokos H, Schallreuter KU: GTP cyclohydrolase feedback regulatory protein controls cofactor 6-tetrahydrobiopterin synthesis in the cytosol and in the nucleus of epidermal keratinocytes and melanocytes. J Invest Dermatol. 2006 Nov;126(11):2481-9. Epub 2006 Jun 15. [PubMed Link Image]
  25. Swick L, Kapatos G: A yeast 2-hybrid analysis of human GTP cyclohydrolase I protein interactions. J Neurochem. 2006 Jun;97(5):1447-55. [PubMed Link Image]
  26. Tegeder I, Costigan M, Griffin RS, Abele A, Belfer I, Schmidt H, Ehnert C, Nejim J, Marian C, Scholz J, Wu T, Allchorne A, Diatchenko L, Binshtok AM, Goldman D, Adolph J, Sama S, Atlas SJ, Carlezon WA, Parsegian A, Lotsch J, Fillingim RB, Maixner W, Geisslinger G, Max MB, Woolf CJ: GTP cyclohydrolase and tetrahydrobiopterin regulate pain sensitivity and persistence. Nat Med. 2006 Nov;12(11):1269-77. Epub 2006 Oct 22. [PubMed Link Image]
  27. Widder JD, Chen W, Li L, Dikalov S, Thony B, Hatakeyama K, Harrison DG: Regulation of tetrahydrobiopterin biosynthesis by shear stress. Circ Res. 2007 Oct 12;101(8):830-8. Epub 2007 Aug 17. [PubMed Link Image]
  28. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  29. Auerbach G, Herrmann A, Bracher A, Bader G, Gutlich M, Fischer M, Neukamm M, Garrido-Franco M, Richardson J, Nar H, Huber R, Bacher A: Zinc plays a key role in human and bacterial GTP cyclohydrolase I. Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13567-72. [PubMed Link Image]
  30. Ichinose H, Ohye T, Takahashi E, Seki N, Hori T, Segawa M, Nomura Y, Endo K, Tanaka H, Tsuji S, et al.: Hereditary progressive dystonia with marked diurnal fluctuation caused by mutations in the GTP cyclohydrolase I gene. Nat Genet. 1994 Nov;8(3):236-42. [PubMed Link Image]
  31. Ichinose H, Ohye T, Segawa M, Nomura Y, Endo K, Tanaka H, Tsuji S, Fujita K, Nagatsu T: GTP cyclohydrolase I gene in hereditary progressive dystonia with marked diurnal fluctuation. Neurosci Lett. 1995 Aug 18;196(1-2):5-8. [PubMed Link Image]
  32. Hirano M, Tamaru Y, Ito H, Matsumoto S, Imai T, Ueno S: Mutant GTP cyclohydrolase I mRNA levels contribute to dopa-responsive dystonia onset. Ann Neurol. 1996 Nov;40(5):796-8. [PubMed Link Image]
  33. Bandmann O, Nygaard TG, Surtees R, Marsden CD, Wood NW, Harding AE: Dopa-responsive dystonia in British patients: new mutations of the GTP-cyclohydrolase I gene and evidence for genetic heterogeneity. Hum Mol Genet. 1996 Mar;5(3):403-6. [PubMed Link Image]
  34. Beyer K, Lao-Villadoniga JI, Vecino-Bilbao B, Cacabelos R, De la Fuente-Fernandez R: A novel point mutation in the GTP cyclohydrolase I gene in a Spanish family with hereditary progressive and dopa responsive dystonia. J Neurol Neurosurg Psychiatry. 1997 Apr;62(4):420-1. [PubMed Link Image]
  35. Jarman PR, Bandmann O, Marsden CD, Wood NW: GTP cyclohydrolase I mutations in patients with dystonia responsive to anticholinergic drugs. J Neurol Neurosurg Psychiatry. 1997 Sep;63(3):304-8. [PubMed Link Image]
  36. Furukawa Y, Kish SJ, Bebin EM, Jacobson RD, Fryburg JS, Wilson WG, Shimadzu M, Hyland K, Trugman JM: Dystonia with motor delay in compound heterozygotes for GTP-cyclohydrolase I gene mutations. Ann Neurol. 1998 Jul;44(1):10-6. [PubMed Link Image]
  37. Bandmann O, Valente EM, Holmans P, Surtees RA, Walters JH, Wevers RA, Marsden CD, Wood NW: Dopa-responsive dystonia: a clinical and molecular genetic study. Ann Neurol. 1998 Oct;44(4):649-56. [PubMed Link Image]
  38. Hwu WL, Wang PJ, Hsiao KJ, Wang TR, Chiou YW, Lee YM: Dopa-responsive dystonia induced by a recessive GTP cyclohydrolase I mutation. Hum Genet. 1999 Sep;105(3):226-30. [PubMed Link Image]
  39. Suzuki T, Ohye T, Inagaki H, Nagatsu T, Ichinose H: Characterization of wild-type and mutants of recombinant human GTP cyclohydrolase I: relationship to etiology of dopa-responsive dystonia. J Neurochem. 1999 Dec;73(6):2510-6. [PubMed Link Image]
  40. Brique S, Destee A, Lambert JC, Mouroux V, Delacourte A, Amouyel P, Chartier-Harlin MC: A new GTP-cyclohydrolase I mutation in an unusual dopa-responsive dystonia, familial form. Neuroreport. 1999 Feb 25;10(3):487-91. [PubMed Link Image]
  41. Hirano M, Komure O, Ueno S: A novel missense mutant inactivates GTP cyclohydrolase I in dopa-responsive dystonia. Neurosci Lett. 1999 Feb 5;260(3):181-4. [PubMed Link Image]
  42. Tassin J, Durr A, Bonnet AM, Gil R, Vidailhet M, Lucking CB, Goas JY, Durif F, Abada M, Echenne B, Motte J, Lagueny A, Lacomblez L, Jedynak P, Bartholome B, Agid Y, Brice A: Levodopa-responsive dystonia. GTP cyclohydrolase I or parkin mutations? Brain. 2000 Jun;123 ( Pt 6):1112-21. [PubMed Link Image]
  43. Steinberger D, Korinthenberg R, Topka H, Berghauser M, Wedde R, Muller U: Dopa-responsive dystonia: mutation analysis of GCH1 and analysis of therapeutic doses of L-dopa. German Dystonia Study Group. Neurology. 2000 Dec 12;55(11):1735-7. [PubMed Link Image]
  44. Leuzzi V, Carducci C, Carducci C, Cardona F, Artiola C, Antonozzi I: Autosomal dominant GTP-CH deficiency presenting as a dopa-responsive myoclonus-dystonia syndrome. Neurology. 2002 Oct 22;59(8):1241-3. [PubMed Link Image]
  45. Ohta E, Funayama M, Ichinose H, Toyoshima I, Urano F, Matsuo M, Tomoko N, Yukihiko K, Yoshino S, Yokoyama H, Shimazu H, Maeda K, Hasegawa K, Obata F: Novel mutations in the guanosine triphosphate cyclohydrolase 1 gene associated with DYT5 dystonia. Arch Neurol. 2006 Nov;63(11):1605-10. [PubMed Link Image]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 6259
Enzyme 48 Name Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial
Enzyme 48 Synonyms
  1. ATP-specific succinyl-CoA synthetase subunit beta
  2. Renal carcinoma antigen NY-REN-39
  3. Succinyl-CoA synthetase beta-A chain
  4. SCS-betaA
Enzyme 48 Gene Name SUCLA2
Enzyme 48 Protein Sequence >Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial
MAASMFYGRLVAVATLRNHRPRTAQRAAAQVLGSSGLFNNHGLQVQQQQQRNLSLHEYMS
MELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVK
IVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGP
VLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENM
VKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDER
DKDAAKANLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEA
FKLITSDKKVLAILVNIFGGIMRCDVIAQGIVMAVKDLEIKIPVVVRLQGTRVDDAKALI
ADSGLKILACDDLDEAARMVVKLSEIVTLAKQAHVDVKFQLPI
Enzyme 48 Number of Residues 463
Enzyme 48 Molecular Weight 50316.9
Enzyme 48 Theoretical pI 7.50
Enzyme 48 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • purine nucleoside binding
Process
  • metabolic process
Component
Enzyme 48 General Function Involved in catalytic activity
Enzyme 48 Specific Function ATP + succinate + CoA = ADP + phosphate + succinyl-CoA
Enzyme 48 Pathways
Enzyme 48 Reactions
  • ATP + succinate + CoA = ADP + phosphate + succinyl-CoA [RN:R00405]
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein Not Available
Enzyme 48 UniProtKB/Swiss-Prot ID Q9P2R7 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name SUCB1_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence >1392 bp
ATGGCGGCCTCCATGTTCTACGGCAGGCTAGTGGCCGTGGCCACCCTTCGGAACCACCGG
CCTCGGACGGCCCAGCGGGCTGCTGCTCAGGTTCTGGGAAGTTCTGGATTGTTTAATAAC
CATGGACTCCAAGTACAGCAGCAACAGCAAAGGAATCTCTCACTACATGAATACATGAGT
ATGGAATTATTGCAAGAAGCTGGTGTCTCCGTTCCCAAAGGATATGTGGCAAAGTCACCA
GATGAAGCTTATGCAATTGCCAAAAAATTAGGTTCAAAAGATGTCGTGATAAAGGCACAG
GTTTTAGCTGGTGGTAGAGGAAAAGGAACATTTGAAAGTGGCCTCAAAGGAGGAGTGAAG
ATAGTTTTCTCTCCAGAAGAAGCAAAAGCTGTTTCTTCACAAATGATTGGGAAAAAATTG
TTTACCAAGCAAACGGGAGAAAAGGGCAGAATATGCAATCAAGTATTGGTCTGTGAGCGA
AAATATCCCAGGAGAGAATACTACTTTGCAATAACAATGGAAAGGTCATTTCAAGGTCCT
GTATTAATAGGAAGTTCACATGGTGGTGTCAACATTGAAGATGTTGCTGCTGAGTCTCCT
GAAGCAATAATTAAAGAACCTATTGATATTGAAGAAGGCATCAAAAAGGAACAAGCTCTC
CAGCTTGCACAGAAGATGGGATTTCCACCTAATATTGTGGAATCAGCAGCAGAAAACATG
GTCAAGCTTTACAGCCTTTTTCTGAAATACGATGCAACCATGATAGAAATAAATCCAATG
GTGGAAGATTCAGATGGAGCTGTATTGTGTATGGATGCAAAGATCAATTTTGACTCTAAT
TCAGCCTATCGCCAAAAGAAAATCTTTGATCTACAGGACTGGACCCAGGAAGATGAAAGG
GACAAAGATGCTGCTAAGGCAAATCTCAACTACATTGGCCTCGATGGAAATATAGGCTGC
CTAGTAAATGGTGCTGGTTTGGCTATGGCCACAATGGATATAATAAAACTTCATGGAGGG
ACTCCAGCCAACTTCCTTGATGTTGGTGGTGGTGCTACAGTCCATCAAGTAACAGAAGCA
TTTAAGCTTATCACTTCAGATAAAAAGGTACTGGCTATTCTGGTCAACATTTTTGGAGGA
ATCATGCGCTGTGATGTTATTGCACAGGGTATAGTCATGGCAGTAAAAGACTTGGAAATT
AAAATACCTGTTGTGGTACGGTTACAAGGTACACGAGTCGATGATGCTAAGGCACTGATA
GCGGACAGTGGACTTAAAATACTTGCTTGTGATGACTTGGATGAAGCTGCTAGAATGGTT
GTAAAGCTCTCTGAAATAGTGACCTTAGCGAAGCAAGCACATGTGGATGTGAAATTTCAG
TTGCCAATATGA
Enzyme 48 GenBank Gene ID AB035863 Link Image
Enzyme 48 GeneCard ID SUCLA2 Link Image
Enzyme 48 GenAtlas ID SUCLA2 Link Image
Enzyme 48 HGNC ID HGNC:11448 Link Image
Enzyme 48 Chromosome Location 1
Enzyme 48 Locus 13q12.2-q13.3
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References
  1. Furuyama K, Sassa S: Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia. J Clin Invest. 2000 Mar;105(6):757-64. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Johnson JD, Mehus JG, Tews K, Milavetz BI, Lambeth DO: Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes. J Biol Chem. 1998 Oct 16;273(42):27580-6. [PubMed Link Image]
  6. Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed Link Image]
  7. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  8. Elpeleg O, Miller C, Hershkovitz E, Bitner-Glindzicz M, Bondi-Rubinstein G, Rahman S, Pagnamenta A, Eshhar S, Saada A: Deficiency of the ADP-forming succinyl-CoA synthase activity is associated with encephalomyopathy and mitochondrial DNA depletion. Am J Hum Genet. 2005 Jun;76(6):1081-6. Epub 2005 Apr 22. [PubMed Link Image]
  9. Ostergaard E, Hansen FJ, Sorensen N, Duno M, Vissing J, Larsen PL, Faeroe O, Thorgrimsson S, Wibrand F, Christensen E, Schwartz M: Mitochondrial encephalomyopathy with elevated methylmalonic acid is caused by SUCLA2 mutations. Brain. 2007 Mar;130(Pt 3):853-61. Epub 2007 Feb 7. [PubMed Link Image]
  10. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  11. Carrozzo R, Dionisi-Vici C, Steuerwald U, Lucioli S, Deodato F, Di Giandomenico S, Bertini E, Franke B, Kluijtmans LA, Meschini MC, Rizzo C, Piemonte F, Rodenburg R, Santer R, Santorelli FM, van Rooij A, Vermunt-de Koning D, Morava E, Wevers RA: SUCLA2 mutations are associated with mild methylmalonic aciduria, Leigh-like encephalomyopathy, dystonia and deafness. Brain. 2007 Mar;130(Pt 3):862-74. Epub 2007 Feb 14. [PubMed Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 6352
Enzyme 49 Name Atrial natriuretic peptide receptor 2
Enzyme 49 Synonyms
  1. Atrial natriuretic peptide receptor type B
  2. ANP-B
  3. ANPR-B
  4. NPR-B
  5. Guanylate cyclase B
  6. GC-B
Enzyme 49 Gene Name NPR2
Enzyme 49 Protein Sequence >Atrial natriuretic peptide receptor 2
MALPSLLLLVAALAGGVRPPGARNLTLAVVLPEHNLSYAWAWPRVGPAVALAVEALGRAL
PVDLRFVSSELEGACSEYLAPLSAVDLKLYHDPDLLLGPGCVYPAASVARFASHWRLPLL
TAGAVASGFSAKNDHYRTLVRTGPSAPKLGEFVVTLHGHFNWTARAALLYLDARTDDRPH
YFTIEGVFEALQGSNLSVQHQVYAREPGGPEQATHFIRANGRIVYICGPLEMLHEILLQA
QRENLTNGDYVFFYLDVFGESLRAGPTRATGRPWQDNRTREQAQALREAFQTVLVITYRE
PPNPEYQEFQNRLLIRAREDFGVELGPSLMNLIAGCFYDGILLYAEVLNETIQEGGTRED
GLRIVEKMQGRRYHGVTGLVVMDKNNDRETDFVLWAMGDLDSGDFQPAAHYSGAEKQIWW
TGRPIPWVKGAPPSDNPPCAFDLDDPSCDKTPLSTLAIVALGTGITFIMFGVSSFLIFRK
LMLEKELASMLWRIRWEELQFGNSERYHKGAGSRLTLSLRGSSYGSLMTAHGKYQIFANT
GHFKGNVVAIKHVNKKRIELTRQVLFELKHMRDVQFNHLTRFIGACIDPPNICIVTEYCP
RGSLQDILENDSINLDWMFRYSLINDLVKGMAFLHNSIISSHGSLKSSNCVVDSRFVLKI
TDYGLASFRSTAEPDDSHALYAKKLWTAPELLSGNPLPTTGMQKADVYSFGIILQEIALR
SGPFYLEGLDLSPKEIVQKVRNGQRPYFRPSIDRTQLNEELVLLMERCWAQDPAERPDFG
QIKGFIRRFNKEGGTSILDNLLLRMEQYANNLEKLVEERTQAYLEEKRKAEALLYQILPH
SVAEQLKRGETVQAEAFDSVTIYFSDIVGFTALSAESTPMQVVTLLNDLYTCFDAIIDNF
DVYKVETIGDAYMVVSGLPGRNGQRHAPEIARMALALLDAVSSFRIRHRPHDQLRLRIGV
HTGPVCAGVVGLKMPRYCLFGDTVNTASRMESNGQALKIHVSSTTKDALDELGCFQLELR
GDVEMKGKGKMRTYWLLGERKGPPGLL
Enzyme 49 Number of Residues 1047
Enzyme 49 Molecular Weight 117021.0
Enzyme 49 Theoretical pI 6.86
Enzyme 49 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • lyase activity
  • molecular transducer activity
  • nucleoside binding
  • peptide receptor activity
  • peptide receptor activity, G-protein coupled
  • phosphorus-oxygen lyase activity
  • protein kinase activity
  • purine nucleoside binding
  • receptor activity
  • signal transducer activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
  • cell part
  • membrane
Enzyme 49 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 49 Specific Function Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth
Enzyme 49 Pathways
Enzyme 49 Reactions
  • GTP = 3',5'-cyclic GMP + diphosphate [RN:R00434]
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • 1-22
Enzyme 49 Transmembrane Regions
  • 459-478
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 5139790 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID P20594 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name ANPRB_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >3144 bp
ATGGCGCTGCCATCACTTCTGCTGTTGGTGGCAGCCCTGGCAGGTGGGGTGCGTCCTCCC
GGGGCGCGGAACCTGACGCTGGCGGTGGTGCTGCCAGAACACAACCTGAGCTATGCCTGG
GCCTGGCCACGGGTGGGACCCGCTGTGGCACTAGCTGTGGAGGCTCTGGGCCGGGCACTG
CCCGTGGACCTGCGGTTTGTCAGCTCCGAACTGGAAGGCGCCTGCTCTGAGTACCTGGCA
CCGCTGAGCGCTGTGGACCTCAAGCTGTACCATGACCCCGACCTGCTGTTAGGTCCCGGT
TGCGTGTACCCTGCTGCCTCTGTGGCCCGCTTTGCCTCCCACTGGCGCCTTCCCCTGCTG
ACTGCGGGTGCTGTGGCCTCTGGTTTTTCGGCTAAGAATGACCATTATCGTACCCTGGTT
CGCACTGGCCCCTCTGCTCCCAAGCTGGGTGAGTTTGTGGTGACACTACACGGGCACTTC
AATTGGACTGCCCGTGCTGCCTTGCTGTACCTGGATGCTCGCACAGATGACCGGCCTCAC
TACTTCACCATCGAGGGCGTCTTTGAGGCCCTGCAGGGCAGCAACCTCAGTGTGCAGCAC
CAGGTGTATGCCCGAGAGCCAGGGGGCCCCGAGCAGGCCACCCACTTCATCCGGGCCAAC
GGGCGCATTGTGTATATCTGCGGCCCTCTGGAGATGCTGCATGAGATCCTGCTTCAGGCC
CAGAGGGAGAATCTGACCAATGGGGATTATGTCTTCTTTTACCTGGATGTCTTTGGGGAG
AGTCTCCGTGCAGGCCCCACACGTGCTACAGGCCGGCCCTGGCAGGACAATCGCACCCGG
GAACAGGCCCAGGCCCTCAGAGAGGCCTTTCAGACTGTATTGGTGATCACGTACCGAGAA
CCCCCAAATCCTGAGTATCAGGAATTCCAGAATCGTCTGCTGATAAGAGCCCGGGAAGAC
TTTGGTGTGGAGCTGGGCCCTTCCCTGATGAACCTCATCGCTGGCTGCTTCTATGATGGG
ATCCTGCTATATGCTGAAGTCCTGAATGAGACAATACAGGAAGGAGGCACCCGGGAGGAT
GGACTTCGAATTGTGGAAAAGATGCAGGGACGAAGATATCACGGTGTAACTGGGCTGGTT
GTCATGGACAAGAACAATGACCGAGAGACTGACTTTGTCCTCTGGGCCATGGGAGACCTG
GATTCTGGGGACTTTCAGCCTGCAGCCCACTACTCGGGAGCTGAGAAGCAGATTTGGTGG
ACGGGACGGCCTATTCCCTGGGTGAAGGGGGCTCCTCCCTCGGACAATCCCCCCTGTGCC
TTTGACTTGGACGACCCATCCTGTGATAAAACTCCACTTTCAACCCTGGCAATTGTGGCT
CTGGGCACAGGAATCACCTTCATCATGTTTGGTGTTTCCAGCTTCCTAATTTTCCGAAAG
CTGATGCTGGAGAAGGAGCTGGCTAGCATGTTGTGGCGTATTCGCTGGGAAGAACTGCAG
TTTGGCAACTCAGAGCGTTATCACAAAGGTGCAGGCAGTCGCCTCACACTGTCGCTGCGG
GGATCCAGTTACGGCTCGCTCATGACAGCCCATGGGAAATACCAGATCTTTGCCAACACC
GGTCACTTCAAGGGAAATGTTGTCGCCATCAAACATGTGAATAAGAAGCGCATTGAGCTG
ACCCGGCAGGTTCTGTTTGAACTCAAACATATGAGAGATGTTCAGTTCAACCATCTCACT
CGCTTCATTGGCGCCTGCATAGACCCTCCCAACATTTGCATTGTCACTGAATACTGTCCT
CGTGGGAGTTTACAGGATATTCTAGAAAATGACAGCATCAACTTGGACTGGATGTTTCGT
TATTCACTCATTAATGACCTTGTTAAGGGCATGGCCTTTCTCCACAACAGCATTATTTCA
TCGCATGGGAGTCTCAAGTCCTCCAACTGTGTGGTGGATAGTCGTTTTGTGCTCAAAATC
ACAGACTATGGCCTGGCCAGCTTCCGATCAACTGCTGAACCTGATGACAGCCATGCCCTC
TATGCCAAGAAGCTGTGGACTGCCCCAGAACTGCTCAGTGGGAACCCCTTGCCAACCACA
GGCATGCAGAAGGCTGACGTCTATAGCTTTGGGATCATCCTGCAGGAGATAGCACTTCGC
AGTGGTCCTTTCTACTTGGAGGGCCTGGACCTCAGCCCCAAAGAGATTGTCCAGAAGGTA
CGAAATGGTCAGCGGCCATATTTCCGGCCAAGCATTGACCGGTCCCAACTGAATGAAGAG
CTAGTTTTGCTGATGGAGCGATGTTGGGCTCAGGACCCAGCTGAGCGGCCAGACTTTGGA
CAGATTAAGGGCTTCATTCGGCGCTTTAACAAGGAGGGTGGCACCAGCATATTGGACAAC
CTCCTGCTGCGCATGGAACAGTATGCCAATAACTTGGAGAAGCTGGTGGAGGAACGCACA
CAGGCCTATCTGGAGGAAAAACGCAAGGCTGAAGCTCTGCTCTACCAAATCCTACCCCAT
TCAGTGGCAGAGCAGTTAAAACGGGGAGAGACTGTACAGGCTGAGGCCTTTGACAGTGTT
ACCATCTACTTCAGTGACATTGTTGGCTTCACAGCATTGTCAGCAGAGAGCACCCCCATG
CAGGTAGTGACACTTCTTAATGACCTGTATACCTGCTTTGATGCCATAATTGACAACTTT
GATGTCTACAAGGTGGAGACGATTGGGGATGCTTACATGGTGGTATCTGGCCTCCCAGGC
CGAAATGGTCAACGCCATGCACCAGAAATTGCTCGTATGGCCCTAGCATTACTAGATGCA
GTTTCTTCCTTTCGCATCCGCCACCGACCCCATGACCAGCTGAGGCTACGCATAGGGGTC
CATACTGGGCCAGTCTGTGCTGGGGTTGTTGGCCTGAAGATGCCCCGTTATTGTCTTTTT
GGAGACACAGTGAACACTGCTTCTCGAATGGAGTCTAATGGTCAAGCGCTGAAGATCCAT
GTCTCCTCTACCACCAAGGATGCCCTAGATGAGCTAGGATGCTTCCAGCTAGAGCTTCGG
GGGGATGTGGAAATGAAGGGAAAAGGAAAGATGCGAACATACTGGCTCTTAGGAGAGCGG
AAAGGACCTCCTGGACTCCTGTAA
Enzyme 49 GenBank Gene ID AB005647 Link Image
Enzyme 49 GeneCard ID NPR2 Link Image
Enzyme 49 GenAtlas ID NPR2 Link Image
Enzyme 49 HGNC ID HGNC:7944 Link Image
Enzyme 49 Chromosome Location 9
Enzyme 49 Locus 9p21-p12
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References
  1. Chang MS, Lowe DG, Lewis M, Hellmiss R, Chen E, Goeddel DV: Differential activation by atrial and brain natriuretic peptides of two different receptor guanylate cyclases. Nature. 1989 Sep 7;341(6237):68-72. [PubMed Link Image]
  2. Rehemudula D, Nakayama T, Soma M, Takahashi Y, Uwabo J, Sato M, Izumi Y, Kanmatsuse K, Ozawa Y: Structure of the type B human natriuretic peptide receptor gene and association of a novel microsatellite polymorphism with essential hypertension. Circ Res. 1999 Mar 19;84(5):605-10. [PubMed Link Image]
  3. Hirsch JR, Meyer M, Magert HJ, Forssmann WG, Mollerup S, Herter P, Weber G, Cermak R, Ankorina-Stark I, Schlatter E, Kruhoffer M: cGMP-dependent and -independent inhibition of a K+ conductance by natriuretic peptides: molecular and functional studies in human proximal tubule cells. J Am Soc Nephrol. 1999 Mar;10(3):472-80. [PubMed Link Image]
  4. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Bennett BD, Bennett GL, Vitangcol RV, Jewett JR, Burnier J, Henzel W, Lowe DG: Extracellular domain-IgG fusion proteins for three human natriuretic peptide receptors. Hormone pharmacology and application to solid phase screening of synthetic peptide antisera. J Biol Chem. 1991 Dec 5;266(34):23060-7. [PubMed Link Image]
  7. Koller KJ, Lowe DG, Bennett GL, Minamino N, Kangawa K, Matsuo H, Goeddel DV: Selective activation of the B natriuretic peptide receptor by C-type natriuretic peptide (CNP). Science. 1991 Apr 5;252(5002):120-3. [PubMed Link Image]
  8. Hillman RT, Green RE, Brenner SE: An unappreciated role for RNA surveillance. Genome Biol. 2004;5(2):R8. Epub 2004 Feb 2. [PubMed Link Image]
  9. Bartels CF, Bukulmez H, Padayatti P, Rhee DK, van Ravenswaaij-Arts C, Pauli RM, Mundlos S, Chitayat D, Shih LY, Al-Gazali LI, Kant S, Cole T, Morton J, Cormier-Daire V, Faivre L, Lees M, Kirk J, Mortier GR, Leroy J, Zabel B, Kim CA, Crow Y, Braverman NE, van den Akker F, Warman ML: Mutations in the transmembrane natriuretic peptide receptor NPR-B impair skeletal growth and cause acromesomelic dysplasia, type Maroteaux. Am J Hum Genet. 2004 Jul;75(1):27-34. Epub 2004 May 14. [PubMed Link Image]
  10. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 6353
Enzyme 50 Name Guanylate cyclase soluble subunit beta-1
Enzyme 50 Synonyms
  1. GCS-beta-1
  2. Guanylate cyclase soluble subunit beta-3
  3. GCS-beta-3
  4. Soluble guanylate cyclase small subunit
Enzyme 50 Gene Name GUCY1B3
Enzyme 50 Protein Sequence >Guanylate cyclase soluble subunit beta-1
MYGFVNHALELLVIRNYGPEVWEDIKKEAQLDEEGQFLVRIIYDDSKTYDLVAAASKVLN
LNAGEILQMFGKMFFVFCQESGYDTILRVLGSNVREFLQNLDALHDHLATIYPGMRAPSF
RCTDAEKGKGLILHYYSEREGLQDIVIGIIKTVAQQIHGTEIDMKVIQQRNEECDHTQFL
IEEKESKEEDFYEDLDRFEENGTQESRISPYTFCKAFPFHIIFDRDLVVTQCGNAIYRVL
PQLQPGNCSLLSVFSLVRPHIDISFHGILSHINTVFVLRSKEGLLDVEKLECEDELTGTE
ISCLRLKGQMIYLPEADSILFLCSPSVMNLDDLTRRGLYLSDIPLHDATRDLVLLGEQFR
EEYKLTQELEILTDRLQLTLRALEDEKKKTDTLLYSVLPPSVANELRHKRPVPAKRYDNV
TILFSGIVGFNAFCSKHASGEGAMKIVNLLNDLYTRFDTLTDSRKNPFVYKVETVGDKYM
TVSGLPEPCIHHARSICHLALDMMEIAGQVQVDGESVQITIGIHTGEVVTGVIGQRMPRY
CLFGNTVNLTSRTETTGEKGKINVSEYTYRCLMSPENSDPQFHLEHRGPVSMKGKKEPMQ
VWFLSRKNTGTEETKQDDD
Enzyme 50 Number of Residues 619
Enzyme 50 Molecular Weight 70513.9
Enzyme 50 Theoretical pI 5.02
Enzyme 50 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • cyclase activity
  • guanylate cyclase activity
  • heme binding
  • ion binding
  • iron ion binding
  • lyase activity
  • metal ion binding
  • phosphorus-oxygen lyase activity
  • transition metal ion binding
Process
  • cGMP biosynthetic process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • signaling
  • signaling pathway
Component
Enzyme 50 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 50 Specific Function GTP = 3',5'-cyclic GMP + diphosphate
Enzyme 50 Pathways
Enzyme 50 Reactions
  • GTP = 3',5'-cyclic GMP + diphosphate [RN:R00434]
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • None
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 4504215 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID Q02153 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name GCYB1_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence >1860 bp
ATGTACGGATTTGTGAATCACGCCCTGGAGTTGCTGGTGATCCGCAATTACGGCCCCGAG
GTGTGGGAAGACATCAAAAAAGAGGCACAGTTAGATGAAGAAGGACAGTTTCTTGTCAGA
ATAATATATGATGACTCCAAAACTTATGATTTGGTTGCTGCTGCAAGCAAAGTCCTCAAT
CTCAATGCTGGAGAAATCCTCCAAATGTTTGGGAAGATGTTTTTCGTCTTTTGCCAAGAA
TCTGGTTATGATACAATCTTGCGTGTCCTGGGCTCTAATGTCAGAGAATTTCTACAGAAC
CTTGATGCTCTGCACGACCACCTTGCTACCATCTACCCAGGAATGCGTGCACCTTCCTTT
AGGTGCACTGATGCAGAAAAGGGCAAAGGACTCATTTTGCACTACTACTCAGAGAGAGAA
GGACTTCAGGATATTGTCATTGGAATCATCAAAACAGTGGCACAACAAATCCATGGCACT
GAAATAGACATGAAGGTTATTCAGCAAAGAAATGAAGAATGTGATCATACTCAATTTTTA
ATTGAAGAAAAAGAGTCAAAAGAAGAGGATTTTTATGAAGATCTTGACAGATTTGAAGAA
AATGGTACCCAGGAATCACGCATCAGCCCATATACATTCTGCAAAGCTTTTCCTTTTCAT
ATAATATTTGACCGGGACCTAGTGGTCACTCAGTGTGGCAATGCTATATACAGAGTTCTC
CCCCAGCTCCAGCCTGGGAATTGCAGCCTTCTGTCTGTCTTCTCGCTGGTTCGTCCTCAT
ATTGATATTAGTTTCCATGGGATCCTTTCTCACATCAATACTGTTTTTGTATTGAGAAGC
AAGGAAGGATTGTTGGATGTGGAGAAATTAGAATGTGAGGATGAACTGACTGGGACTGAG
ATCAGCTGCTTACGTCTCAAGGGTCAAATGATCTACTTACCTGAAGCAGATAGCATACTT
TTTCTATGTTCACCAAGTGTCATGAACCTGGACGATTTGACAAGGAGAGGGCTGTATCTA
AGTGACATCCCTCTGCATGATGCCACGCGCGATCTTGTTCTTTTGGGAGAACAATTTAGA
GAGGAATACAAACTCACCCAAGAACTGGAAATCCTCACTGACAGGCTACAGCTCACGTTA
AGAGCCCTGGAAGATGAAAAGAAAAAGACAGACACATTGCTGTATTCTGTCCTTCCTCCG
TCTGTTGCCAATGAGCTGCGGCACAAGCGTCCAGTGCCTGCCAAAAGATATGACAATGTG
ACCATCCTCTTTAGTGGCATTGTGGGCTTCAATGCTTTCTGTAGCAAGCATGCATCTGGA
GAAGGAGCCATGAAGATCGTCAACCTCCTCAACGACCTCTACACCAGATTTGACACACTG
ACTGATTCCCGGAAAAACCCATTTGTTTATAAGGTGGAGACTGTTGGTGACAAGTATATG
ACAGTGAGTGGTTTACCAGAGCCATGCATTCACCATGCACGATCCATCTGCCACCTGGCC
TTGGACATGATGGAAATTGCTGGCCAGGTTCAAGTAGATGGTGAATCTGTTCAGATAACA
ATAGGGATACACACTGGAGAGGTAGTTACAGGTGTCATAGGACAGCGGATGCCTCGATAC
TGTCTTTTTGGGAATACTGTCAACCTCACAAGCCGAACAGAAACCACAGGAGAAAAGGGA
AAAATAAATGTGTCTGAATATACATACAGATGTCTTATGTCTCCAGAAAATTCAGATCCA
CAATTCCACTTGGAGCACAGAGGCCCAGTGTCCATGAAGGGCAAAAAAGAACCAATGCAA
GTTTGGTTTCTATCCAGAAAAAATACAGGAACAGAGGAAACAAAGCAGGATGATGACTGA
Enzyme 50 GenBank Gene ID NM_000857.2 Link Image
Enzyme 50 GeneCard ID GUCY1B3 Link Image
Enzyme 50 GenAtlas ID GUCY1B3 Link Image
Enzyme 50 HGNC ID HGNC:4687 Link Image
Enzyme 50 Chromosome Location 4
Enzyme 50 Locus 4q31.3-q33
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 General References
  1. Giuili G, Scholl U, Bulle F, Guellaen G: Molecular cloning of the cDNAs coding for the two subunits of soluble guanylyl cyclase from human brain. FEBS Lett. 1992 Jun 8;304(1):83-8. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Chhajlani V, Frandberg PA, Ahlner J, Axelsson KL, Wikberg JE: Heterogeneity in human soluble guanylate cyclase due to alternative splicing. FEBS Lett. 1991 Sep 23;290(1-2):157-8. [PubMed Link Image]
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 6356
Enzyme 51 Name Retinal guanylyl cyclase 1
Enzyme 51 Synonyms
  1. RETGC-1
  2. Guanylate cyclase 2D, retinal
  3. Rod outer segment membrane guanylate cyclase
  4. ROS-GC
Enzyme 51 Gene Name GUCY2D
Enzyme 51 Protein Sequence >Retinal guanylyl cyclase 1
MTACARRAGGLPDPGLCGPAWWAPSLPRLPRALPRLPLLLLLLLLQPPALSAVFTVGVLG
PWACDPIFSRARPDLAARLAAARLNRDPGLAGGPRFEVALLPEPCRTPGSLGAVSSALAR
VSGLVGPVNPAACRPAELLAEEAGIALVPWGCPWTQAEGTTAPAVTPAADALYALLRAFG
WARVALVTAPQDLWVEAGRSLSTALRARGLPVASVTSMEPLDLSGAREALRKVRDGPRVT
AVIMVMHSVLLGGEEQRYLLEAAEELGLTDGSLVFLPFDTIHYALSPGPEALAALANSSQ
LRRAHDAVLTLTRHCPSEGSVLDSLRRAQERRELPSDLNLQQVSPLFGTIYDAVFLLARG
VAEARAAAGGRWVSGAAVARHIRDAQVPGFCGDLGGDEEPPFVLLDTDAAGDRLFATYML
DPARGSFLSAGTRMHFPRGGSAPGPDPSCWFDPNNICGGGLEPGLVFLGFLLVVGMGLAG
AFLAHYVRHRLLHMQMVSGPNKIILTVDDITFLHPHGGTSRKVAQGSRSSLGARSMSDIR
SGPSQHLDSPNIGVYEGDRVWLKKFPGDQHIAIRPATKTAFSKLQELRHENVALYLGLFL
ARGAEGPAALWEGNLAVVSEHCTRGSLQDLLAQREIKLDWMFKSSLLLDLIKGIRYLHHR
GVAHGRLKSRNCIVDGRFVLKITDHGHGRLLEAQKVLPEPPRAEDQLWTAPELLRDPALE
RRGTLAGDVFSLAIIMQEVVCRSAPYAMLELTPEEVVQRVRSPPPLCRPLVSMDQAPVEC
ILLMKQCWAEQPELRPSMDHTFDLFKNINKGRKTNIIDSMLRMLEQYSSNLEDLIRERTE
ELELEKQKTDRLLTQMLPPSVAEALKTGTPVEPEYFEQVTLYFSDIVGFTTISAMSEPIE
VVDLLNDLYTLFDAIIGSHDVYKVETIGDAYMVASGLPQRNGQRHAAEIANMSLDILSAV
GTFRMRHMPEVPVRIRIGLHSGPCVAGVVGLTMPRYCLFGDTVNTASRMESTGLPYRIHV
NLSTVGILRALDSGYQVELRGRTELKGKGAEDTFWLVGRRGFNKPIPKPPDLQPGSSNHG
ISLQEIPPERRRKLEKARPGQFS
Enzyme 51 Number of Residues 1103
Enzyme 51 Molecular Weight 120057.2
Enzyme 51 Theoretical pI 7.47
Enzyme 51 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cyclase activity
  • guanylate cyclase activity
  • kinase activity
  • lyase activity
  • nucleoside binding
  • phosphorus-oxygen lyase activity
  • protein kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cGMP biosynthetic process
  • cellular metabolic process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • signaling
  • signaling pathway
Component
Enzyme 51 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 51 Specific Function Probably plays a specific functional role in the rods and/or cones of photoreceptors. It may be the enzyme involved in the resynthesis of cGMP required for recovery of the dark state after phototransduction
Enzyme 51 Pathways
Enzyme 51 Reactions
  • GTP = 3',5'-cyclic GMP + diphosphate [RN:R00434]
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • 1-51
Enzyme 51 Transmembrane Regions
  • 463-487
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 2695890 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID Q02846 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name GUC2D_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence >3312 bp
ATGACCGCCTGCGCCCGCCGAGCGGGTGGGCTTCCGGACCCCGGGCTCTGCGGTCCCGCG
TGGTGGGCTCCGTCCCTGCCCCGCCTCCCCCGGGCCCTGCCCCGGCTCCCGCTCCTGCTG
CTCCTGCTTCTGCTGCAGCCCCCCGCCCTCTCCGCCGTGTTCACGGTGGGGGTCCTGGGC
CCCTGGGCTTGCGACCCCATCTTCTCTCGGGCTCGCCCGGACCTGGCCGCCCGCCTGGCC
GCCGCCCGCCTGAACCGCGACCCCGGCCTGGCAGGCGGTCCCCGCTTCGAGGTAGCGCTG
CTGCCCGAGCCTTGCCGGACGCCGGGCTCGCTGGGGGCCGTGTCCTCCGCGCTGGCCCGC
GTGTCGGGCCTCGTGGGTCCGGTGAACCCTGCGGCCTGCCGGCCAGCCGAGCTGCTCGCC
GAAGAAGCCGGGATCGCGCTGGTGCCCTGGGGCTGCCCCTGGACGCAGGCGGAGGGCACC
ACGGCCCCTGCCGTGACCCCCGCCGCGGATGCCCTCTACGCCCTGCTTCGCGCATTCGGC
TGGGCGCGCGTGGCCCTGGTCACCGCCCCCCAGGACCTGTGGGTGGAGGCGGGACGCTCA
CTGTCCACGGCACTCAGGGCCCGGGGCCTGCCTGTCGCCTCCGTGACTTCCATGGAGCCC
TTGGACCTGTCTGGAGCCCGGGAGGCCCTGAGGAAGGTTCGGGACGGGCCCAGGGTCACA
GCAGTGATCATGGTGATGCACTCGGTGCTGCTGGGTGGCGAGGAGCAGCGCTACCTCCTG
GAGGCCGCAGAGGAGCTGGGCCTGACCGATGGCTCCCTGGTCTTCCTGCCCTTCGACACG
ATCCACTACGCCTTGTCCCCAGGCCCGGAGGCCTTGGCCGCACTCGCCAACAGCTCCCAG
CTTCGCAGGGCCCACGATGCCGTGCTCACCCTCACGCGCCACTGTCCCTCTGAAGGCAGC
GTGCTGGACAGCCTGCGCAGGGCTCAAGAGCGCCGCGAGCTGCCCTCTGACCTCAATCTG
CAGCAGGTCTCCCCACTCTTTGGCACCATCTATGACGCGGTCTTCTTGCTGGCAAGGGGC
GTGGCAGAAGCGCGGGCTGCCGCAGGTGGCAGATGGGTGTCCGGAGCAGCTGTGGCCCGC
CACATCCGGGATGCGCAGGTCCCTGGCTTCTGCGGGGACCTAGGAGGAGACGAGGAGCCC
CCATTCGTGCTGCTAGACACGGACGCGGCGGGAGACCGGCTTTTTGCCACATACATGCTG
GATCCTGCCCGGGGCTCCTTCCTCTCCGCCGGTACCCGGATGCACTTCCCGCGTGGGGGA
TCAGCACCCGGACCTGACCCCTCGTGCTGGTTCGATCCAAACAACATCTGCGGTGGAGGA
CTGGAGCCGGGCCTCGTCTTTCTTGGCTTCCTCCTGGTGGTTGGGATGGGGCTGGCTGGG
GCCTTCCTGGCCCATTATGTGAGGCACCGGCTACTTCACATGCAAATGGTCTCCGGCCCC
AACAAGATCATCCTGACCGTGGACGACATCACCTTTCTCCACCCACATGGGGGCACCTCT
CGAAAGGTGGCCCAGGGGAGTCGATCAAGTCTGGGTGCCCGCAGCATGTCAGACATTCGC
AGCGGCCCCAGCCAACACTTGGACAGCCCCAACATTGGTGTCTATGAGGGAGACAGGGTT
TGGCTGAAGAAATTCCCAGGGGATCAGCACATAGCTATCCGCCCAGCAACCAAGACGGCC
TTCTCCAAGCTCCAGGAGCTCCGGCATGAGAACGTGGCCCTCTACCTGGGGCTTTTCCTG
GCTCGGGGAGCAGAAGGCCCTGCGGCCCTCTGGGAGGGCAACCTGGCTGTGGTCTCAGAG
CACTGCACGCGGGGCTCTCTTCAGGACCTCCTCGCTCAGAGAGAAATAAAGCTGGACTGG
ATGTTCAAGTCCTCCCTCCTGCTGGACCTTATCAAGGGAATAAGGTATCTGCACCATCGA
GGCGTGGCTCATGGGCGGCTGAAGTCACGGAACTGCATAGTGGATGGCAGATTCGTACTC
AAGATCACTGACCACGGCCACGGGAGACTGCTGGAAGCACAGAAGGTGCTACCGGAGCCT
CCCAGAGCGGAGGACCAGCTGTGGACAGCCCCGGAGCTGCTTAGGGACCCAGCCCTGGAG
CGCCGGGGAACGCTGGCCGGCGACGTCTTTAGCTTGGCCATCATCATGCAAGAAGTAGTG
TGCCGCAGTGCCCCTTATGCCATGCTGGAGCTCACTCCCGAGGAAGTGGTGCAGAGGGTG
CGGAGCCCCCCTCCACTGTGTCGGCCCTTGGTGTCCATGGACCAGGCACCTGTCGAGTGT
ATCCTCCTGATGAAGCAGTGCTGGGCAGAGCAGCCGGAACTTCGGCCCTCCATGGACCAC
ACCTTCGACCTGTTCAAGAACATCAACAAGGGCCGGAAGACGAACATCATTGACTCGATG
CTTCGGATGCTGGAGCAGTACTCTAGTAACCTGGAGGATCTGATCCGGGAGCGCACGGAG
GAGCTGGAGCTGGAAAAGCAGAAGACAGACCGGCTGCTTACACAGATGCTGCCTCCGTCT
GTGGCTGAGGCCTTGAAGACGGGGACACCAGTGGAGCCCGAGTACTTTGAGCAAGTGACA
CTGTACTTTAGTGACATTGTGGGCTTCACCACCATCTCTGCCATGAGTGAGCCCATTGAG
GTTGTGGACCTGCTCAACGATCTCTACACACTCTTTGATGCCATCATTGGTTCCCACGAT
GTCTACAAGGTGGAGACAATAGGGGACGCCTATATGGTGGCCTCGGGGCTGCCCCAGCGG
AATGGGCAGCGACACGCGGCAGAGATCGCCAACATGTCACTGGACATCCTCAGTGCCGTG
GGCACTTTCCGCATGCGCCATATGCCTGAGGTTCCCGTGCGCATCCGCATAGGCCTGCAC
TCGGGTCCATGCGTGGCAGGCGTGGTGGGCCTCACCATGCCGCGGTACTGCCTGTTTGGG
GACACGGTCAACACCGCCTCGCGCATGGAGTCCACCGGGCTGCCTTACCGCATCCACGTG
AACTTGAGCACTGTGGGGATTCTCCGTGCTCTGGACTCGGGCTACCAGGTGGAGCTGCGA
GGCCGCACGGAGCTGAAGGGCAAGGGCGCCGAGGACACTTTCTGGCTAGTGGGCAGACGC
GGCTTCAACAAGCCCATCCCCAAACCGCCTGACCTGCAACCGGGGTCCAGCAACCACGGC
ATCAGCCTGCAGGAGATCCCACCCGAGCGGCGACGGAAGCTGGAGAAGGCGCGGCCGGGC
CAGTTCTCTTGA
Enzyme 51 GenBank Gene ID AJ222657 Link Image
Enzyme 51 GeneCard ID GUCY2D Link Image
Enzyme 51 GenAtlas ID GUCY2D Link Image
Enzyme 51 HGNC ID HGNC:4689 Link Image
Enzyme 51 Chromosome Location 1
Enzyme 51 Locus 17p13.1
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 General References
  1. Shyjan AW, de Sauvage FJ, Gillett NA, Goeddel DV, Lowe DG: Molecular cloning of a retina-specific membrane guanylyl cyclase. Neuron. 1992 Oct;9(4):727-37. [PubMed Link Image]
  2. Oliveira L, Miniou P, Viegas-Pequignot E, Rozet JM, Dollfus H, Pittler SJ: Human retinal guanylate cyclase (GUC2D) maps to chromosome 17p13.1. Genomics. 1994 Jul 15;22(2):478-81. [PubMed Link Image]
  3. Liu Y, Ruoho AE, Rao VD, Hurley JH: Catalytic mechanism of the adenylyl and guanylyl cyclases: modeling and mutational analysis. Proc Natl Acad Sci U S A. 1997 Dec 9;94(25):13414-9. [PubMed Link Image]
  4. Perrault I, Rozet JM, Calvas P, Gerber S, Camuzat A, Dollfus H, Chatelin S, Souied E, Ghazi I, Leowski C, Bonnemaison M, Le Paslier D, Frezal J, Dufier JL, Pittler S, Munnich A, Kaplan J: Retinal-specific guanylate cyclase gene mutations in Leber's congenital amaurosis. Nat Genet. 1996 Dec;14(4):461-4. [PubMed Link Image]
  5. Perrault I, Rozet JM, Gerber S, Kelsell RE, Souied E, Cabot A, Hunt DM, Munnich A, Kaplan J: A retGC-1 mutation in autosomal dominant cone-rod dystrophy. Am J Hum Genet. 1998 Aug;63(2):651-4. [PubMed Link Image]
  6. Kelsell RE, Gregory-Evans K, Payne AM, Perrault I, Kaplan J, Yang RB, Garbers DL, Bird AC, Moore AT, Hunt DM: Mutations in the retinal guanylate cyclase (RETGC-1) gene in dominant cone-rod dystrophy. Hum Mol Genet. 1998 Jul;7(7):1179-84. [PubMed Link Image]
  7. Duda T, Venkataraman V, Goraczniak R, Lange C, Koch KW, Sharma RK: Functional consequences of a rod outer segment membrane guanylate cyclase (ROS-GC1) gene mutation linked with Leber's congenital amaurosis. Biochemistry. 1999 Jan 12;38(2):509-15. [PubMed Link Image]
  8. Dharmaraj SR, Silva ER, Pina AL, Li YY, Yang JM, Carter CR, Loyer MK, El-Hilali HK, Traboulsi EK, Sundin OK, Zhu DK, Koenekoop RK, Maumenee IH: Mutational analysis and clinical correlation in Leber congenital amaurosis. Ophthalmic Genet. 2000 Sep;21(3):135-50. [PubMed Link Image]
  9. Koenekoop RK, Fishman GA, Iannaccone A, Ezzeldin H, Ciccarelli ML, Baldi A, Sunness JS, Lotery AJ, Jablonski MM, Pittler SJ, Maumenee I: Electroretinographic abnormalities in parents of patients with Leber congenital amaurosis who have heterozygous GUCY2D mutations. Arch Ophthalmol. 2002 Oct;120(10):1325-30. [PubMed Link Image]
  10. Udar N, Yelchits S, Chalukya M, Yellore V, Nusinowitz S, Silva-Garcia R, Vrabec T, Hussles Maumenee I, Donoso L, Small KW: Identification of GUCY2D gene mutations in CORD5 families and evidence of incomplete penetrance. Hum Mutat. 2003 Feb;21(2):170-1. [PubMed Link Image]
  11. Tucker CL, Ramamurthy V, Pina AL, Loyer M, Dharmaraj S, Li Y, Maumenee IH, Hurley JB, Koenekoop RK: Functional analyses of mutant recessive GUCY2D alleles identified in Leber congenital amaurosis patients: protein domain comparisons and dominant negative effects. Mol Vis. 2004 Apr 20;10:297-303. [PubMed Link Image]
  12. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 6357
Enzyme 52 Name Guanylate cyclase soluble subunit alpha-3
Enzyme 52 Synonyms
  1. GCS-alpha-3
  2. GCS-alpha-1
  3. Soluble guanylate cyclase large subunit
Enzyme 52 Gene Name GUCY1A3
Enzyme 52 Protein Sequence >Guanylate cyclase soluble subunit alpha-3
MFCTKLKDLKITGECPFSLLAPGQVPNESSEEAAGSSESCKATVPICQDIPEKNIQESLP
QRKTSRSRVYLHTLAESICKLIFPEFERLNVALQRTLAKHKIKESRKSLEREDFEKTIAE
QAVAAGVPVEVIKESLGEEVFKICYEEDENILGVVGGTLKDFLNSFSTLLKQSSHCQEAG
KRGRLEDASILCLDKEDDFLHVYYFFPKRTTSLILPGIIKAAAHVLYETEVEVSLMPPCF
HNDCSEFVNQPYLLYSVHMKSTKPSLSPSKPQSSLVIPTSLFCKTFPFHFMFDKDMTILQ
FGNGIRRLMNRRDFQGKPNFEEYFEILTPKINQTFSGIMTMLNMQFVVRVRRWDNSVKKS
SRVMDLKGQMIYIVESSAILFLGSPCVDRLEDFTGRGLYLSDIPIHNALRDVVLIGEQAR
AQDGLKKRLGKLKATLEQAHQALEEEKKKTVDLLCSIFPCEVAQQLWQGQVVQAKKFSNV
TMLFSDIVGFTAICSQCSPLQVITMLNALYTRFDQQCGELDVYKVETIGDAYCVAGGLHK
ESDTHAVQIALMALKMMELSDEVMSPHGEPIKMRIGLHSGSVFAGVVGVKMPRYCLFGNN
VTLANKFESCSVPRKINVSPTTYRLLKDCPGFVFTPRSREELPPNFPSEIPGICHFLDAY
QQGTNSKPCFQKKDVEDGNANFLGKASGID
Enzyme 52 Number of Residues 690
Enzyme 52 Molecular Weight 77451.8
Enzyme 52 Theoretical pI 7.12
Enzyme 52 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • cyclase activity
  • guanylate cyclase activity
  • heme binding
  • ion binding
  • iron ion binding
  • lyase activity
  • metal ion binding
  • phosphorus-oxygen lyase activity
  • transition metal ion binding
Process
  • cGMP biosynthetic process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • signaling
  • signaling pathway
Component
Enzyme 52 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 52 Specific Function GTP = 3',5'-cyclic GMP + diphosphate
Enzyme 52 Pathways
Enzyme 52 Reactions
  • GTP = 3',5'-cyclic GMP + diphosphate [RN:R00434]
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • None
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein 20306359 Link Image
Enzyme 52 UniProtKB/Swiss-Prot ID Q02108 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name GCYA3_HUMAN Link Image
Enzyme 52 PDB ID Not Available
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence >2073 bp
ATGTTCTGCACGAAGCTCAAGGATCTCAAGATCACAGGAGAGTGTCCTTTCTCCTTACTG
GCACCAGGTCAAGTTCCTAACGAGTCTTCAGAGGAGGCAGCAGGAAGCTCAGAGAGCTGC
AAAGCAACCATGCCCATCTGTCAAGACATTCCTGAGAAGAACATACAAGAAAGTCTTCCT
CAAAGAAAAACCAGTCGGAGCCGAGTCTATCTTCACACTTTGGCAGAGAGTATTTGCAAA
CTGATTTTCCCAGAGTTTGAACGGCTGAATGTTGCACTTCAGAGAACATTGGCAAAGCAC
AAAATAAAAGAAAGCAGGAAATCTTTGGAAAGAGAAGACTTTGAAAAAACAATTGCAGAG
CAAGCAGTTGCAGCAGGAGTTCCAGTGGAGGTTATCAAAGAATCTCTTGGTGAAGAGGTT
TTTAAAATATGTTACGAGGAAGATGAAAACATCCTTGGGGTGGTTGGAGGCACCCTTAAA
GATTTTTTAAACAGCTTCAGTACCCTTCTGAAACAGAGCAGCCATTGCCAAGAAGCAGGA
AAAAGGGGCAGGCTTGAGGACGCCTCCATTCTATGCCTGGATAAGGAGGATGATTTTCTA
CATGTTTACTACTTCTTCCCTAAGAGAACCACCTCCCTGATTCTTCCCGGCATCATAAAG
GCAGCTGCTCACGTATTATATGAAACGGAAGTGGAAGTGTCGTTAATGCCTCCCTGCTTC
CATAATGATTGCAGCGAGTTTGTGAATCAGCCCTACTTGTTGTACTCCGTTCACATGAAA
AGCACCAAGCCATCCCTGTCCCCCAGCAAACCCCAGTCCTCGCTGGTGATTCCCACATCG
CTATTCTGCAAGACATTTCCATTCCATTTCATGTTTGACAAAGATATGACAATTCTGCAA
TTTGGCAATGGCATCAGAAGGCTGATGAACAGGAGAGACTTTCAAGGAAAGCCTAATTTT
GAAGAATACTTTGAAATTCTGACTCCAAAAATCAACCAGACGTTTAGCGGGATCATGACT
ATGTTGAATATGCAGTTTGTTGTACGAGTGAGGAGATGGGACAACTCTGTGAAGAAATCT
TCAAGGGTTATGGACCTCAAAGGCCAAATGATCTACATTGTTGAATCCAGTGCAATCTTG
TTTTTGGGGTCACCCTGTGTGGACAGATTAGAAGATTTTACAGGACGAGGGCTCTACCTC
TCAGACATCCCAATTCACAATGCACTGAGGGATGTGGTCTTAATAGGGGAACAAGCCCGA
GCTCAAGATGGCCTGAAGAAGAGGCTGGGGAAGCTGAAGGCTACCCTTGAGCAAGCCCAC
CAAGCCCTGGAGGAGGAGAAGAAAAAGACAGTAGACCTTCTGTGCTCCATATTTCCCTGT
GAGGTTGCTCAGCAGCTGTGGCAAGGGCAAGTTGTGCAAGCCAAGAAGTTCAGTAATGTC
ACCATGCTCTTCTCAGACATCGTTGGGTTCACTGCCATCTGCTCCCAGTGCTCACCGCTG
CAGGTCATCACCATGCTCAATGCACTGTACACTCGCTTCGACCAGCAGTGTGGAGAGCTG
GATGTCTACAAGGTGGAGACCATTGGCGATGCCTATTGTGTAGCTGGGGGATTACACAAA
GAGAGTGATACTCATGCTGTTCAGATAGCGCTGATGGCCGTGAAGATGATGGAGCTCTCT
GATGAAGTTATGTCTCCCCATGGAGAACCTATCAAGATGCGAATTGGACTGCACTCTGGA
TCAGTTTTTGCTGGCGTCGTTGGAGTTAAAATGCCCCGTTACTGTCTTTTTGGAAACAAT
GTCACTCTGGCTAACAAATTTGAGTCCTGCAGTGTACCACGAAAAATCAATGTCAGCCCA
ACAACTTACAGATTACTCAAAGACTGTCCTGGTTTCGTGTTTACCCCTCGATCAAGGGAG
GAACTTCCACCAAACTTCCCTAGTGAAATCCCCGGAATCTGCCATTTTCTGGATGCTTAC
CAACAAGGAACAAACTCAAAACCATGCTTCCAAAAGAAAGATGTGGAAGATGGCAATGCC
AATTTTTTAGGCAAAGCATCAGGAATAGATTAG
Enzyme 52 GenBank Gene ID BC028384 Link Image
Enzyme 52 GeneCard ID GUCY1A3 Link Image
Enzyme 52 GenAtlas ID GUCY1A3 Link Image
Enzyme 52 HGNC ID HGNC:4685 Link Image
Enzyme 52 Chromosome Location 4
Enzyme 52 Locus 4q31.3-q33|4q31.1-q31.2
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 General References
  1. Giuili G, Scholl U, Bulle F, Guellaen G: Molecular cloning of the cDNAs coding for the two subunits of soluble guanylyl cyclase from human brain. FEBS Lett. 1992 Jun 8;304(1):83-8. [PubMed Link Image]
  2. Zabel U, Weeger M, La M, Schmidt HH: Human soluble guanylate cyclase: functional expression and revised isoenzyme family. Biochem J. 1998 Oct 1;335 ( Pt 1):51-7. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 6358
Enzyme 53 Name Atrial natriuretic peptide receptor 1
Enzyme 53 Synonyms
  1. Atrial natriuretic peptide receptor type A
  2. ANP-A
  3. ANPR-A
  4. NPR-A
  5. Guanylate cyclase A
  6. GC-A
Enzyme 53 Gene Name NPR1
Enzyme 53 Protein Sequence >Atrial natriuretic peptide receptor 1
MPGPRRPAGSRLRLLLLLLLPPLLLLLRGSHAGNLTVAVVLPLANTSYPWSWARVGPAVE
LALAQVKARPDLLPGWTVRTVLGSSENALGVCSDTAAPLAAVDLKWEHNPAVFLGPGCVY
AAAPVGRFTAHWRVPLLTAGAPALGFGVKDEYALTTRAGPSYAKLGDFVAALHRRLGWER
QALMLYAYRPGDEEHCFFLVEGLFMRVRDRLNITVDHLEFAEDDLSHYTRLLRTMPRKGR
VIYICSSPDAFRTLMLLALEAGLCGEDYVFFHLDIFGQSLQGGQGPAPRRPWERGDGQDV
SARQAFQAAKIITYKDPDNPEYLEFLKQLKHLAYEQFNFTMEDGLVNTIPASFHDGLLLY
IQAVTETLAHGGTVTDGENITQRMWNRSFQGVTGYLKIDSSGDRETDFSLWDMDPENGAF
RVVLNYNGTSQELVAVSGRKLNWPLGYPPPDIPKCGFDNEDPACNQDHLSTLEVLALVGS
LSLLGILIVSFFIYRKMQLEKELASELWRVRWEDVEPSSLERHLRSAGSRLTLSGRGSNY
GSLLTTEGQFQVFAKTAYYKGNLVAVKRVNRKRIELTRKVLFELKHMRDVQNEHLTRFVG
ACTDPPNICILTEYCPRGSLQDILENESITLDWMFRYSLTNDIVKGMLFLHNGAICSHGN
LKSSNCVVDGRFVLKITDYGLESFRDLDPEQGHTVYAKKLWTAPELLRMASPPVRGSQAG
DVYSFGIILQEIALRSGVFHVEGLDLSPKEIIERVTRGEQPPFRPSLALQSHLEELGLLM
QRCWAEDPQERPPFQQIRLTLRKFNRENSSNILDNLLSRMEQYANNLEELVEERTQAYLE
EKRKAEALLYQILPHSVAEQLKRGETVQAEAFDSVTIYFSDIVGFTALSAESTPMQVVTL
LNDLYTCFDAVIDNFDVYKVETIGDAYMVVSGLPVRNGRLHACEVARMALALLDAVRSFR
IRHRPQEQLRLRIGIHTGPVCAGVVGLKMPRYCLFGDTVNTASRMESNGEALKIHLSSET
KAVLEEFGGFELELRGDVEMKGKGKVRTYWLLGERGSSTRG
Enzyme 53 Number of Residues 1061
Enzyme 53 Molecular Weight 118918.1
Enzyme 53 Theoretical pI 6.61
Enzyme 53 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • lyase activity
  • molecular transducer activity
  • nucleoside binding
  • peptide receptor activity
  • peptide receptor activity, G-protein coupled
  • phosphorus-oxygen lyase activity
  • protein kinase activity
  • purine nucleoside binding
  • receptor activity
  • signal transducer activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
  • cell part
  • membrane
Enzyme 53 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 53 Specific Function Receptor for the atrial natriuretic peptide NPPA/ANP and the brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones playing a key role in cardiovascular homeostasis. Has guanylate cyclase activity upon binding of the ligand
Enzyme 53 Pathways
Enzyme 53 Reactions
  • GTP = 3',5'-cyclic GMP + diphosphate [RN:R00434]
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • 1-32
Enzyme 53 Transmembrane Regions
  • 474-494
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein 3297986 Link Image
Enzyme 53 UniProtKB/Swiss-Prot ID P16066 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name ANPRA_HUMAN Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence >3186 bp
ATGCCGGGGCCCCGGCGCCCCGCTGGCTCCCGCCTGCGCCTGCTCCTGCTCCTGCTGCTG
CCGCCGCTGCTGCTGCTGCTCCGGGGCAGCCACGCGGGCAACCTGACGGTAGCCGTGGTA
CTGCCGCTGGCCAATACCTCGTACCCCTGGTCGTGGGCGCGCGTGGGACCCGCCGTGGAG
CTGGCCTTGGCCCAGGTGAAGGCGCGCCCCGACTTGCTGCCGGGCTGGACGGTCCGCACG
GTGCTGGGCAGCAGCGAAAACGCGCTGGGCGTCTGCTCCGACACCGCAGCGCCCCTGGCC
GCGGTGGACCTCAAGTGGGAGCACAACCCCGCTGTGTTCCTGGGCCCCGGCTGCGTGTAC
GCCGCCGCCCCAGTGGGGCGCTTCACCGCGCACTGGCGGGTCCCGCTGCTGACCGCCGGC
GCCCCGGCGCTGGGCTTCGGTGTCAAGGACGAGTATGCGCTGACCACCCGCGCGGGGCCC
AGCTACGCCAAGCTGGGGGACTTCGTGGCGGCGCTGCACCGACGGCTGGGCTGGGAGCGC
CAAGCGCTCATGCTCTACGCCTACCGGCCGGGTGACGAAGAGCACTGCTTCTTCCTCGTG
GAGGGGCTGTTCATGCGGGTCCGCGACCGCCTCAATATTACGGTGGACCACCTGGAGTTC
GCCGAGGACGACCTCAGCCACTACACCAGGCTGCTGCGGACCATGCCGCGCAAAGGCCGA
GTTATCTACATCTGCAGCTCCCCTGATGCCTTCAGAACCCTCATGCTCCTGGCCCTGGAA
GCTGGCTTGTGTGGGGAGGACTACGTTTTCTTCCACCTGGATATCTTTGGGCAAAGCCTG
CAAGGTGGACAGGGCCCTGCTCCCCGCAGGCCCTGGGAGAGAGGGGATGGGCAGGATGTC
AGTGCCCGCCAGGCCTTTCAGGCTGCCAAAATCATTACATATAAAGACCCAGATAATCCC
GAGTACTTGGAATTCCTGAAGCAGTTAAAACACCTGGCCTATGAGCAGTTCAACTTCACC
ATGGAGGATGGCCTGGTGAACACCATCCCAGCATCCTTCCACGACGGGCTCCTGCTCTAT
ATCCAGGCAGTGACGGAGACTCTGGCACATGGGGGAACTGTTACTGATGGGGAGAACATC
ACTCAGCGGATGTGGAACCGAAGCTTTCAAGGTGTGACAGGATACCTGAAAATTGATAGC
AGTGGCGATCGGGAAACAGACTTCTCCCTCTGGGATATGGATCCCGAGAATGGTGCCTTC
AGGGTTGTACTGAACTACAATGGGACTTCCCAAGAGCTGGTGGCTGTGTCGGGGCGCAAA
CTGAACTGGCCCCTGGGGTACCCTCCTCCTGACATCCCCAAATGTGGCTTTGACAACGAA
GACCCAGCATGCAACCAAGATCACCTTTCCACCCTGGAGGTGCTGGCTTTGGTGGGCAGC
CTCTCCTTGCTCGGCATTCTGATTGTCTCCTTCTTCATATACAGGAAGATGCAGCTGGAG
AAGGAACTGGCCTCGGAGCTGTGGCGGGTGCGCTGGGAGGACGTTGAGCCCAGTAGCCTT
GAGAGGCACCTGCGGAGTGCAGGCAGCCGGCTGACCCTGAGCGGGAGAGGCTCCAATTAC
GGCTCCCTGCTAACCACAGAGGGCCAGTTCCAAGTCTTTGCCAAGACAGCATATTATAAG
GGCAACCTCGTGGCTGTGAAACGTGTGAACCGTAAACGCATTGAGCTGACACGAAAAGTC
CTGTTTGAACTGAAGCATATGCGGGATGTGCAGAATGAACACCTGACCAGGTTTGTGGGA
GCCTGCACCGACCCCCCCAATATCTGCATCCTCACAGAGTACTGTCCCCGTGGGAGCCTG
CAGGACATTCTGGAGAATGAGAGCATCACCCTGGACTGGATGTTCCGGTACTCACTCACC
AATGACATCGTCAAGGGCATGCTGTTTCTACACAATGGGGCTATCTGTTCCCATGGGAAC
CTCAAGTCATCCAACTGCGTGGTAGATGGGCGCTTTGTGCTCAAGATCACCGACTATGGG
CTGGAGAGCTTCAGGGACCTGGACCCAGAGCAAGGACACACCGTTTATGCCAAAAAGCTG
TGGACGGCCCCTGAGCTCCTGCGAATGGCTTCACCCCCTGTGCGGGGCTCCCAGGCTGGT
GACGTATACAGCTTTGGGATCATCCTTCAGGAGATTGCCCTGAGGAGTGGGGTCTTCCAC
GTGGAAGGTTTGGACCTGAGCCCCAAAGAGATCATCGAGCGGGTGACTCGGGGTGAGCAG
CCCCCCTTCCGGCCCTCCCTGGCCCTGCAGAGTCACCTGGAGGAGTTGGGGCTGCTCATG
CAGCGGTGCTGGGCTGAGGACCCACAGGAGAGGCCACCATTCCAGCAGATCCGCCTGACG
TTGCGCAAATTTAACAGGGAGAACAGCAGCAACATCCTGGACAACCTGCTGTCCCGCATG
GAGCAGTACGCGAACAATCTGGAGGAACTGGTGGAGGAGCGGACCCAGGCATACCTGGAG
GAGAAGCGCAAGGCTGAGGCCCTGCTCTACCAGATCCTGCCTCACTCAGTGGCTGAGCAG
CTGAAGCGTGGGGAGACGGTGCAGGCCGAAGCCTTTGACAGTGTTACCATCTACTTCAGT
GACATTGTGGGTTTCACAGCGCTGTCGGCGGAGAGCACACCCATGCAGGTGGTGACCCTG
CTCAATGACCTGTACACTTGCTTTGATGCTGTCATAGACAACTTTGATGTGTACAAGGTG
GAGACAATTGGCGATGCCTACATGGTGGTGTCAGGGCTCCCTGTGCGGAACGGGCGGCTA
CACGCCTGCGAGGTAGCCCGCATGGCCCTGGCACTGCTGGATGCTGTGCGCTCCTTCCGA
ATCCGCCACCGGCCCCAGGAGCAGCTGCGCTTGCGCATTGGCATCCACACAGGACCTGTG
TGTGCTGGAGTGGTGGGACTGAAGATGCCCCGTTACTGTCTCTTTGGGGATACAGTCAAC
ACAGCCTCAAGAATGGAGTCTAATGGGGAAGCCCTGAAGATCCACTTGTCTTCTGAGACC
AAGGCTGTCCTGGAGGAGTTTGGTGGTTTCGAGCTGGAGCTTCGAGGGGATGTAGAAATG
AAGGGCAAAGGCAAGGTTCGGACCTACTGGCTCCTTGGGGAGAGGGGGAGTAGCACCCGA
GGCTGA
Enzyme 53 GenBank Gene ID AB010491 Link Image
Enzyme 53 GeneCard ID NPR1 Link Image
Enzyme 53 GenAtlas ID NPR1 Link Image
Enzyme 53 HGNC ID HGNC:7943 Link Image
Enzyme 53 Chromosome Location 1
Enzyme 53 Locus 1q21-q22
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 General References
  1. Lowe DG, Chang MS, Hellmiss R, Chen E, Singh S, Garbers DL, Goeddel DV: Human atrial natriuretic peptide receptor defines a new paradigm for second messenger signal transduction. EMBO J. 1989 May;8(5):1377-84. [PubMed Link Image]
  2. Takahashi Y, Nakayama T, Soma M, Izumi Y, Kanmatsuse K: Organization of the human natriuretic peptide receptor A gene. Biochem Biophys Res Commun. 1998 May 29;246(3):736-9. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Pardhasaradhi K, Kutty RK, Gentleman S, Krishna G: Expression of mRNA for atrial natriuretic peptide receptor guanylate cyclase (ANPRA) in human retina. Cell Mol Neurobiol. 1994 Feb;14(1):1-7. [PubMed Link Image]
  6. Bennett BD, Bennett GL, Vitangcol RV, Jewett JR, Burnier J, Henzel W, Lowe DG: Extracellular domain-IgG fusion proteins for three human natriuretic peptide receptors. Hormone pharmacology and application to solid phase screening of synthetic peptide antisera. J Biol Chem. 1991 Dec 5;266(34):23060-7. [PubMed Link Image]
  7. Koller KJ, Lowe DG, Bennett GL, Minamino N, Kangawa K, Matsuo H, Goeddel DV: Selective activation of the B natriuretic peptide receptor by C-type natriuretic peptide (CNP). Science. 1991 Apr 5;252(5002):120-3. [PubMed Link Image]
  8. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 6359
Enzyme 54 Name Heat-stable enterotoxin receptor
Enzyme 54 Synonyms
  1. STA receptor
  2. hSTAR
  3. Guanylyl cyclase C
  4. GC-C
  5. Intestinal guanylate cyclase
Enzyme 54 Gene Name GUCY2C
Enzyme 54 Protein Sequence >Heat-stable enterotoxin receptor
MKTLLLDLALWSLLFQPGWLSFSSQVSQNCHNGSYEISVLMMGNSAFAEPLKNLEDAVNE
GLEIVRGRLQNAGLNVTVNATFMYSDGLIHNSGDCRSSTCEGLDLLRKISNAQRMGCVLI
GPSCTYSTFQMYLDTELSYPMISAGSFGLSCDYKETLTRLMSPARKLMYFLVNFWKTNDL
PFKTYSWSTSYVYKNGTETEDCFWYLNALEASVSYFSHELGFKVVLRQDKEFQDILMDHN
RKSNVIIMCGGPEFLYKLKGDRAVAEDIVIILVDLFNDQYLEDNVTAPDYMKNVLVLTLS
PGNSLLNSSFSRNLSPTKRDFALAYLNGILLFGHMLKIFLENGENITTPKFAHAFRNLTF
EGYDGPVTLDDWGDVDSTMVLLYTSVDTKKYKVLLTYDTHVNKTYPVDMSPTFTWKNSKL
PNDITGRGPQILMIAVFTLTGAVVLLLLVALLMLRKYRKDYELRQKKWSHIPPENIFPLE
TNETNHVSLKIDDDKRRDTIQRLRQCKYDKKRVILKDLKHNDGNFTEKQKIELNKLLQID
YYNLTKFYGTVKLDTMIFGVIEYCERGSLREVLNDTISYPDGTFMDWEFKISVLYDIAKG
MSYLHSSKTEVHGRLKSTNCVVDSRMVVKITDFGCNSILPPKKDLWTAPEHLRQANISQK
GDVYSYGIIAQEIILRKETFYTLSCRDRNEKIFRVENSNGMKPFRPDLFLETAEEKELEV
YLLVKNCWEEDPEKRPDFKKIETTLAKIFGLFHDQKNESYMDTLIRRLQLYSRNLEHLVE
ERTQLYKAERDRADRLNFMLLPRLVVKSLKEKGFVEPELYEEVTIYFSDIVGFTTICKYS
TPMEVVDMLNDIYKSFDHIVDHHDVYKVETIGDAYMVASGLPKRNGNRHAIDIAKMALEI
LSFMGTFELEHLPGLPIWIRIGVHSGPCAAGVVGIKMPRYCLFGDTVNTASRMESTGLPL
RIHVSGSTIAILKRTECQFLYEVRGETYLKGRGNETTYWLTGMKDQKFNLPTPPTVENQQ
RLQAEFSDMIANSLQKRQAAGIRSQKPRRVASYKKGTLEYLQLNTTDKESTYF
Enzyme 54 Number of Residues 1073
Enzyme 54 Molecular Weight 123367.7
Enzyme 54 Theoretical pI 7.18
Enzyme 54 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • lyase activity
  • nucleoside binding
  • phosphorus-oxygen lyase activity
  • protein kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 54 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 54 Specific Function Receptor for the E.coli heat-stable enterotoxin (E.coli enterotoxin markedly stimulates the accumulation of cGMP in mammalian cells expressing GC-C). Also activated by the endogenous peptide guanylin
Enzyme 54 Pathways
Enzyme 54 Reactions
  • GTP = 3',5'-cyclic GMP + diphosphate [RN:R00434]
Enzyme 54 Pfam Domain Function
Enzyme 54 Signals
  • 1-23
Enzyme 54 Transmembrane Regions
  • 431-454
Enzyme 54 Essentiality Not Available
Enzyme 54 GenBank ID Protein 222080083 Link Image
Enzyme 54 UniProtKB/Swiss-Prot ID P25092 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name GUC2C_HUMAN Link Image
Enzyme 54 PDB ID Not Available
Enzyme 54 Cellular Location Not Available
Enzyme 54 Gene Sequence >3222 bp
ATGAAGACGTTGCTGTTGGACTTGGCTTTGTGGTCACTGCTCTTCCAGCCCGGGTGGCTG
TCCTTTAGTTCCCAGGTGAGTCAGAACTGCCACAATGGCAGCTATGAAATCAGCGTCCTG
ATGATGGGCAACTCAGCCTTTGCAGAGCCCCTGAAAAACTTGGAAGATGCGGTGAATGAG
GGGCTGGAAATAGTGAGAGGACGTCTGCAAAATGCTGGCCTAAATGTGACTGTGAACGCT
ACTTTCATGTATTCGGATGGTCTGATTCATAACTCAGGCGACTGCCGGAGTAGCACCTGT
GAAGGCCTCGACCTACTCAGGAAAATTTCAAATGCACAACGGATGGGCTGTGTCCTCATA
GGGCCCTCATGTACATACTCCACCTTCCAGATGTACCTTGACACAGAATTGAGCTACCCC
ATGATCTCAGCTGGAAGTTTTGGATTGTCATGTGACTATAAAGAAACCTTAACCAGGCTG
ATGTCTCCAGCTAGAAAGTTGATGTACTTCTTGGTTAACTTTTGGAAAACCAACGATCTG
CCCTTCAAAACTTATTCCTGGAGCACTTCGTATGTTTACAAGAATGGTACAGAAACTGAG
GACTGTTTCTGGTACCTTAATGCTCTGGAGGCTAGCGTTTCCTATTTCTCCCACGAACTC
GGCTTTAAGGTGGTGTTAAGACAAGATAAGGAGTTTCAGGATATCTTAATGGACCACAAC
AGGAAAAGCAATGTGATTATTATGTGTGGTGGTCCAGAGTTCCTCTACAAGCTGAAGGGT
GACCGAGCAGTGGCTGAAGACATTGTCATTATTCTAGTGGATCTTTTCAATGACCAGTAC
TTTGAGGACAATGTCACAGCCCCTGACTATATGAAAAATGTCCTTGTTCTGACGCTGTCT
CCTGGGAATTCCCTTCTAAATAGCTCTTTCTCCAGGAATCTATCACCAACAAAACGAGAC
TTTGCTCTTGCCTATTTGAATGGAATCCTGCTCTTTGGACATATGCTGAAGATATTTCTT
GAAAATGGAGAAAATATTACCACCCCCAAATTTGCTCATGCTTTCAGGAATCTCACTTTT
GAAGGGTATGACGGTCCAGTGACCTTGGATGACTGGGGGGATGTTGACAGTACCATGGTG
CTTCTGTATACCTCTGTGGACACCAAGAAATACAAGGTTCTTTTGACCTATGATACCCAC
GTAAATAAGACCTATCCTGTGGATATGAGCCCCACATTCACTTGGAAGAACTCTAAACTT
CCTAATGATATTACAGGCCGGGGCCCTCAGATCCTGATGATTGCAGTCTTCACCCTCACT
GGAGCTGTGGTGCTGCTCCTGCTCGTCGCTCTCCTGATGCTCAGAAAATATAGAAAAGAT
TATGAACTTCGTCAGAAAAAATGGTCCCACATTCCTCCTGAAAATATCTTTCCTCTGGAG
ACCAATGAGACCAATCATGTTAGCCTCAAGATCGATGATGACAAAAGACGAGATACAATC
CAGAGACTACGACAGTGCAAATACGACAAAAAGCGAGTGATTCTCAAAGATCTCAAGCAC
AATGATGGTAATTTCACTGAAAAACAGAAGATAGAATTGAACAAGTTGCTTCAGATTGAC
TATTACAACCTGACCAAGTTCTACGGCACAGTGAAACTTGATACCATGATCTTCGGGGTG
ATAGAATACTGTGAGAGAGGATCCCTCCGGGAAGTTTTAAATGACACAATTTCCTACCCT
GATGGCACATTCATGGATTGGGAGTTTAAGATCTCTGTCTTGTATGACATTGCTAAGGGA
ATGTCATATCTGCACTCCAGTAAGACAGAAGTCCATGGTCGTCTGAAATCTACCAACTGC
GTAGTGGACAGTAGAATGGTGGTGAAGATCACTGATTTTGGCTGCAATTCCATTTTACCT
CCAAAAAAGGACCTGTGGACAGCTCCAGAGCACCTCCGCCAAGCCAACATCTCTCAGAAA
GGAGATGTGTACAGCTATGGGATCATCGCACAGGAGATCATCCTGCGGAAAGAAACCTTC
TACACTTTGAGCTGTCGGGACCGGAATGAGAAGATTTTCAGAGTGGAAAATTCCAATGGA
ATGAAACCCTTCCGCCCAGATTTATTCTTGGAAACAGCAGAGGAAAAAGAGCTAGAAGTG
TACCTACTTGTAAAAAACTGTTGGGAGGAAGATCCAGAAAAGAGACCAGATTTCAAAAAA
ATTGAGACTACACTTGCCAAGATATTTGGACTTTTTCATGACCAAAAAAATGAAAGCTAT
ATGGATACCTTGATCCGACGTCTACAGCTATATTCTCGAAACCTGGAACATCTGGTAGAG
GAAAGGACACAGCTGTACAAGGCAGAGAGGGACAGGGCTGACAGACTTAACTTTATGTTG
CTTCCAAGGCTAGTGGTAAAGTCTCTGAAGGAGAAAGGCTTTGTGGAGCCGGAACTATAT
GAGGAAGTTACAATCTACTTCAGTGACATTGTAGGTTTCACTACTATCTGCAAATACAGC
ACCCCCATGGAAGTGGTGGACATGCTTAATGACATCTATAAGAGTTTTGACCACATTGTT
GATCATCATGATGTCTACAAGGTGGAAACCATCGGTGATGCGTACATGGTGGCTAGTGGT
TTGCCTAAGAGAAATGGCAATCGGCATGCAATAGACATTGCCAAGATGGCCTTGGAAATC
CTCAGCTTCATGGGGACCTTTGAGCTGGAGCATCTTCCTGGCCTCCCAATATGGATTCGC
ATTGGAGTTCACTCTGGTCCCTGTGCTGCTGGAGTTGTGGGAATCAAGATGCCTCGTTAT
TGTCTATTTGGAGATACGGTCAACACAGCCTCTAGGATGGAATCCACTGGCCTCCCTTTG
AGAATTCACGTGAGTGGCTCCACCATAGCCATCCTGAAGAGAACTGAGTGCCAGTTCCTT
TATGAAGTGAGAGGAGAAACATACTTAAAGGGAAGAGGAAATGAGACTACCTACTGGCTG
ACTGGGATGAAGGACCAGAAATTCAACCTGCCAACCCCTCCTACTGTGGAGAATCAACAG
CGTTTGCAAGCAGAATTTTCAGACATGATTGCCAACTCTTTACAGAAAAGACAGGCAGCA
GGGATAAGAAGCCAAAAACCCAGACGGGTAGCCAGCTATAAAAAAGGCACTCTGGAATAC
TTGCAGCTGAATACCACAGACAAGGAGAGCACCTATTTTTAA
Enzyme 54 GenBank Gene ID NM_004963.3 Link Image
Enzyme 54 GeneCard ID GUCY2C Link Image
Enzyme 54 GenAtlas ID GUCY2C Link Image
Enzyme 54 HGNC ID HGNC:4688 Link Image
Enzyme 54 Chromosome Location 1
Enzyme 54 Locus 12p12
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 General References
  1. de Sauvage FJ, Camerato TR, Goeddel DV: Primary structure and functional expression of the human receptor for Escherichia coli heat-stable enterotoxin. J Biol Chem. 1991 Sep 25;266(27):17912-8. [PubMed Link Image]
  2. Singh S, Singh G, Heim JM, Gerzer R: Isolation and expression of a guanylate cyclase-coupled heat stable enterotoxin receptor cDNA from a human colonic cell line. Biochem Biophys Res Commun. 1991 Sep 30;179(3):1455-63. [PubMed Link Image]
  3. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Mann EA, Jump ML, Glenella RA: Cell line-specific transcriptional activation of the promoter of the human guanylyl cyclase C/heat-stable enterotoxin/receptor gene. Biochim Biophys Acta. 1996 Feb 7;1305(1-2):7-10. [PubMed Link Image]
  6. Mann EA, Cohen MB, Giannella RA: Comparison of receptors for Escherichia coli heat-stable enterotoxin: novel receptor present in IEC-6 cells. Am J Physiol. 1993 Jan;264(1 Pt 1):G172-8. [PubMed Link Image]
  7. Scott RO, Thelin WR, Milgram SL: A novel PDZ protein regulates the activity of guanylyl cyclase C, the heat-stable enterotoxin receptor. J Biol Chem. 2002 Jun 21;277(25):22934-41. Epub 2002 Apr 11. [PubMed Link Image]
  8. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 6361
Enzyme 55 Name Guanylate cyclase soluble subunit alpha-2
Enzyme 55 Synonyms
  1. GCS-alpha-2
Enzyme 55 Gene Name GUCY1A2
Enzyme 55 Protein Sequence >Guanylate cyclase soluble subunit alpha-2
MSRRKISSESFSSLGSDYLETSPEEEGECPLSRLCWNGSRSPPGPLEPSPAAAAAAAAPA
PTPAASAAAAAATAGARRVQRRRRVNLDSLGESISRLTAPSPQTIQQTLKRTLQYYEHQV
IGYRDAEKNFHNISNRCSYADHSNKEEIEDVSGILQCTANILGLKFEEIQKRFGEEFFNI
CFHENERVLRAVGGTLQDFFNGFDALLEHIRTSFGKQATLESPSFLCKELPEGTLMLHYF
HPHHIVGFAMLGMIKAAGKKIYRLDVEVEQVANEKLCSDVSNPGNCSCLTFLIKECENTN
IMKNLPQGTSQVPADLRISINTFCRAFPFHLMFDPSMSVLQLGEGLRKQLRCDTHKVLKF
EDCFEIVSPKVNATFERVLLRLSTPFVIRTKPEASGSENKDKVMEVKGQMIHVPESNSIL
FLGSPCVDKLDELMGRGLHLSDIPIHDATRDVILVGEQAKAQDGLKKRMDKLKATLERTH
QALEEEKKKTVDLLYSIFPGDVAQQLWQGQQVQARKFDDVTMLFSDIVGFTAICAQCTPM
QVISMLNELYTRFDHQCGFLDIYKVETIGDAYCVAAGLHRKSLCHAKPIALMALKMMELS
EEVLTPDGRPIQMRIGIHSGSVLAGVVGVRMPRYCLFGNNVTLASKFESGSHPRRINVSP
TTYQLLKREESFTFIPRSREELPDNFPKEIPGICYFLEVRTGPKPPKPSLSSSRIKKVSY
NIGTMFLRETSL
Enzyme 55 Number of Residues 732
Enzyme 55 Molecular Weight 81749.2
Enzyme 55 Theoretical pI 7.72
Enzyme 55 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • cyclase activity
  • guanylate cyclase activity
  • heme binding
  • ion binding
  • iron ion binding
  • lyase activity
  • metal ion binding
  • phosphorus-oxygen lyase activity
  • transition metal ion binding
Process
  • cGMP biosynthetic process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • signaling
  • signaling pathway
Component
Enzyme 55 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 55 Specific Function Isoform 2 acts as a negative regulator of guanylyl cyclase activity as it forms non-functional heterodimers with the beta subunits
Enzyme 55 Pathways
Enzyme 55 Reactions
  • GTP = 3',5'-cyclic GMP + diphosphate [RN:R00434]
Enzyme 55 Pfam Domain Function
Enzyme 55 Signals
  • None
Enzyme 55 Transmembrane Regions
  • None
Enzyme 55 Essentiality Not Available
Enzyme 55 GenBank ID Protein 120659898 Link Image
Enzyme 55 UniProtKB/Swiss-Prot ID P33402 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name GCYA2_HUMAN Link Image
Enzyme 55 PDB ID Not Available
Enzyme 55 Cellular Location Not Available
Enzyme 55 Gene Sequence >2199 bp
ATGTCTCGAAGGAAGATTTCGTCCGAGTCCTTCAGCTCCCTGGGCTCCGACTACCTGGAG
ACCAGCCCGGAGGAGGAGGGGGAGTGCCCCCTGTCTAGGCTCTGCTGGAATGGCAGCCGG
AGCCCGCCCGGGCCGCTGGAGCCCAGCCCGGCCGCAGCTGCCGCTGCCGCCGCTCCGGCC
CCGACCCCGGCTGCTTCTGCCGCCGCCGCCGCTGCCACTGCCGGGGCCAGGAGGGTGCAG
CGCCGGAGGCGGGTCAACCTGGACTCGCTGGGCGAGAGCATCAGCCGCCTGACGGCGCCC
TCGCCTCAGACGATACAGCAGACTCTCAAGAGGACACTGCAGTATTATGAACATCAAGTT
ATTGGTTACAGGGATGCAGAAAAGAATTTCCACAATATCTCTAACAGATGCTCCTATGCA
GACCACTCCAATAAAGAAGAAATTGAAGATGTCTCAGGAATTCTTCAGTGTACTGCTAAT
ATACTCGGTTTGAAGTTTGAGGAAATTCAAAAAAGATTTGGTGAAGAGTTCTTTAATATA
TGCTTTCATGAGAATGAGAGAGTCCTTCGAGCTGTAGGTGGCACTTTGCAGGACTTTTTT
AACGGCTTTGATGCTTTGTTGGAACACATTAGAACTTCTTTTGGAAAACAGGCCACTCTG
GAGTCACCATCTTTCCTATGCAAAGAGCTCCCTGAAGGTACTCTCATGCTCCACTACTTC
CACCCTCACCATATTGTGGGGTTTGCAATGCTGGGGATGATTAAGGCTGCAGGAAAGAAG
ATCTATCGGCTGGATGTGGAAGTGGAACAGGTTGCAAATGAGAAGCTATGCTCTGATGTT
TCAAACCCAGGCAATTGTAGCTGTCTTACTTTCCTTATCAAAGAATGTGAAAATACTAAT
ATCATGAAGAACCTTCCACAGGGAACCTCCCAAGTTCCTGCGGACCTCAGAATTAGCATC
AACACCTTCTGTAGAGCCTTCCCTTTCCACTTGATGTTTGATCCCAGCATGTCAGTCCTT
CAGTTGGGGGAAGGTCTAAGGAAGCAGCTTCGATGTGACACTCACAAAGTGCTCAAGTTT
GAGGACTGCTTCGAGATTGTATCTCCAAAGGTTAATGCCACCTTTGAAAGGGTCCTGCTG
CGACTGTCTACCCCGTTTGTGATTAGAACCAAGCCTGAGGCTTCTGGCTCTGAAAATAAA
GACAAGGTGATGGAAGTCAAAGGACAAATGATCCATGTTCCAGAATCAAATTCCATTTTA
TTTTTGGGCTCTCCATGTGTGGACAAGTTGGATGAACTCATGGGCCGAGGGCTACATCTC
TCAGACATCCCTATCCATGATGCCACCCGAGATGTCATTTTGGTTGGTGAGCAGGCAAAG
GCCCAAGATGGGTTGAAGAAAAGGATGGATAAATTAAAGGCAACTTTAGAAAGAACTCAC
CAGGCCCTGGAAGAAGAGAAAAAGAAGACAGTGGATCTTCTATATTCTATTTTCCCTGGT
GATGTAGCCCAGCAATTATGGCAAGGGCAGCAAGTACAGGCCAGAAAGTTTGATGATGTC
ACCATGCTCTTTTCAGACATTGTTGGCTTCACAGCCATATGTGCCCAGTGTACTCCCATG
CAAGTAATCAGCATGCTGAATGAACTGTACACCAGATTTGACCACCAGTGTGGATTTTTG
GATATTTATAAGGTGGAAACAATAGGTGATGCCTACTGTGTTGCAGCAGGGCTCCACAGA
AAAAGCCTCTGCCATGCTAAACCCATTGCTCTGATGGCCTTGAAGATGATGGAACTTTCA
GAAGAGGTGCTGACACCTGATGGAAGACCGATTCAGATGAGGATAGGAATTCACTCAGGC
TCCGTGCTGGCTGGAGTTGTTGGGGTGCGAATGCCACGTTATTGCCTGTTTGGAAATAAT
GTCACACTGGCAAGCAAATTCGAGTCGGGAAGTCACCCTCGGCGCATCAATGTCAGCCCA
ACCACTTACCAATTATTAAAACGAGAAGAAAGTTTCACATTCATTCCGCGGTCTCGTGAA
GAGCTTCCAGACAACTTTCCAAAGGAAATTCCTGGGATCTGCTATTTCCTGGAGGTAAGG
ACTGGTCCAAAGCCACCAAAGCCTTCTCTTTCTTCGTCGAGAATAAAAAAGGTTTCCTAC
AACATCGGCACCATGTTCCTCCGGGAGACAAGCCTCTGA
Enzyme 55 GenBank Gene ID BC130484 Link Image
Enzyme 55 GeneCard ID GUCY1A2 Link Image
Enzyme 55 GenAtlas ID GUCY1A2 Link Image
Enzyme 55 HGNC ID HGNC:4684 Link Image
Enzyme 55 Chromosome Location 1
Enzyme 55 Locus 11q21-q22
Enzyme 55 SNPs SNPJam Report Link Image
Enzyme 55 General References
  1. Harteneck C, Wedel B, Koesling D, Malkewitz J, Bohme E, Schultz G: Molecular cloning and expression of a new alpha-subunit of soluble guanylyl cyclase. Interchangeability of the alpha-subunits of the enzyme. FEBS Lett. 1991 Nov 4;292(1-2):217-22. [PubMed Link Image]
  2. Behrends S, Harteneck C, Schultz G, Koesling D: A variant of the alpha 2 subunit of soluble guanylyl cyclase contains an insert homologous to a region within adenylyl cyclases and functions as a dominant negative protein. J Biol Chem. 1995 Sep 8;270(36):21109-13. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 55 Metabolite References Not Available
Enzyme 56 [top]
Enzyme 56 ID 6365
Enzyme 56 Name Retinal guanylyl cyclase 2
Enzyme 56 Synonyms
  1. RETGC-2
  2. Guanylate cyclase 2F, retinal
  3. Guanylate cyclase F
  4. GC-F
  5. Rod outer segment membrane guanylate cyclase 2
  6. ROS-GC2
Enzyme 56 Gene Name GUCY2F
Enzyme 56 Protein Sequence >Retinal guanylyl cyclase 2
MFLGLGRFSRLVLWFAAFRKLLGHHGLASAKFLWCLCLLSVMSLPQQVWTLPYKIGVVGP
WACDSLFSKALPEVAARLAIERINRDPSFDLSYSFEYVILNEDCQTSRALSSFISHHQMA
SGFIGPTNPGYCEAASLLGNSWDKGIFSWACVNYELDNKISYPTFSRTLPSPIRVLVTVM
KYFQWAHAGVISSDEDIWVHTANRVASALRSHGLPVGVVLTTGQDSQSMRKALQRIHQAD
RIRIIIMCMHSALIGGETQMHLLECAHDLKMTDGTYVFVPYDALLYSLPYKHTPYQVLRN
NPKLREAYDAVLTITVESQEKTFYQAFTEAAARGEIPEKLEFDQVSPLFGTIYNSIYFIA
QAMNNAMKENGQAGAASLVQHSRNMQFHGFNQLMRTDSNGNGISEYVILDTNLKEWELHS
TYTVDMEMELLRFGGTPIHFPGGRPPRADAKCWFAEGKICHGGIDPAFAMMVCLTLLIAL
LSINGFAYFIRRRINKIQLIKGPNRILLTLEDVTFINPHFGSKRGSRASVSFQITSEVQS
GRSPRLSFSSGSLTPATYENSNIAIYEGDWVWLKKFSLGDFGDLKSIKSRASDVFEMMKD
LRHENINPLLGFFYDSGMFAIVTEFCSRGSLEDILTNQDVKLDWMFKSSLLLDLIKGMKY
LHHREFVHGRLKSRNCVVDGRFVLKVTDYGFNDILEMLRLSEEESSMEELLWTAPELLRA
PRGSRLGSFAGDVYSFAIIMQEVMVRGTPFCMMDLPAQEIINRLKKPPPVYRPVVPPEHA
PPECLQLMKQCWAEAAEQRPTFDEIFNQFKTFNKGKKTNIIDSMLRMLEQYSSNLEDLIR
ERTEELEIEKQKTEKLLTQMLPPSVAESLKKGCTVEPEGFDLVTLYFSDIVGFTTISAMS
EPIEVVDLLNDLYTLFDAIIGSHDVYKVETIGDAYMVASGLPKRNGSRHAAEIANMSLDI
LSSVGTFKMRHMPEVPVRIRIGLHSGPVVAGVVGLTMPRYCLFGDTVNTASRMESTGLPY
RIHVSLSTVTILQNLSEGYEVELRGRTELKGKGTEETFWLIGKKGFMKPLPVPPPVDKDG
QVGHGLQPVEIAAFQRRKAERQLVRNKP
Enzyme 56 Number of Residues 1108
Enzyme 56 Molecular Weight 124820.9
Enzyme 56 Theoretical pI 7.20
Enzyme 56 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cyclase activity
  • guanylate cyclase activity
  • kinase activity
  • lyase activity
  • nucleoside binding
  • phosphorus-oxygen lyase activity
  • protein kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cGMP biosynthetic process
  • cellular metabolic process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • signaling
  • signaling pathway
Component
Enzyme 56 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 56 Specific Function Probably plays a specific functional role in the rods and/or cones of photoreceptors. It may be the enzyme involved in the resynthesis of cGMP required for recovery of the dark state after phototransduction
Enzyme 56 Pathways
Enzyme 56 Reactions
  • GTP = 3',5'-cyclic GMP + diphosphate [RN:R00434]
Enzyme 56 Pfam Domain Function
Enzyme 56 Signals
  • 1-50
Enzyme 56 Transmembrane Regions
  • 468-490
Enzyme 56 Essentiality Not Available
Enzyme 56 GenBank ID Protein 4680397 Link Image
Enzyme 56 UniProtKB/Swiss-Prot ID P51841 Link Image
Enzyme 56 UniProtKB/Swiss-Prot Entry Name GUC2F_HUMAN Link Image
Enzyme 56 PDB ID Not Available
Enzyme 56 Cellular Location Not Available
Enzyme 56 Gene Sequence >3327 bp
ATGTTCCTGGGACTCGGGCGCTTTTCTCGCCTTGTTCTCTGGTTTGCGGCTTTCAGGAAA
CTGCTGGGACACCATGGCCTTGCATCTGCCAAGTTCCTGTGGTGCTTGTGCCTTCTGTCT
GTCATGTCCCTTCCGCAGCAGGTGTGGACACTCCCCTACAAGATAGGGGTGGTGGGCCCT
TGGGCTTGTGATTCGCTGTTTTCAAAGGCCCTGCCTGAGGTTGCTGCGCGATTAGCCATT
GAGCGAATCAACCGGGACCCATCTTTTGACCTGAGTTATTCTTTTGAATACGTGATTCTC
AATGAAGACTGCCAGACTTCGAGGGCTCTCTCCAGTTTCATTTCCCACCACCAGATGGCC
TCAGGATTTATTGGACCTACCAACCCTGGCTACTGCGAGGCAGCCTCGCTCCTGGGAAAC
AGCTGGGACAAAGGAATTTTCTCTTGGGCTTGTGTGAATTATGAATTAGACAATAAAATT
AGCTACCCGACCTTTTCTCGGACACTCCCTTCTCCCATCCGGGTGCTTGTAACTGTCATG
AAATATTTCCAGTGGGCTCATGCTGGAGTCATTTCCTCAGATGAAGACATTTGGGTGCAT
ACAGCCAATCGAGTCGCAAGTGCTCTTCGGAGCCACGGCTTACCTGTAGGGGTCGTCCTG
ACCACAGGACAAGACAGCCAAAGCATGCGGAAAGCCCTCCAGAGGATTCACCAGGCAGAC
AGAATTCGCATAATCATCATGTGTATGCATTCAGCTTTGATTGGGGGAGAGACTCAGATG
CATCTCTTGGAATGTGCTCATGATCTGAAAATGACTGATGGAACCTACGTCTTTGTTCCT
TATGATGCCCTGCTCTACAGTTTACCTTATAAGCACACCCCCTACCGGGTCCTAAGGAAC
AACCCAAAGCTCCGGGAAGCCTATGATGCAGTGTTGACCATTACAGTGGAGTCCCAAGAA
AAGACCTTCTATCAAGCCTTCACAGAGGCAGCAGCAAGAGGTGAAATTCCTGAGAAGCTG
GAGTTCGATCAAGTTTCACCGTTGTTTGGAACCATCTACAATTCAATTTACTTTATCGCA
CAAGCCATGAATAATGCTATGAAAGAAAATGGACAGGCTGGTGCTGCCAGCCTGGTTCAG
CATTCCAGAAACATGCAGTTCCATGGATTCAACCAGTTGATGAGGACAGATTCAAATGGA
AATGGAATTTCAGAATATGTAATCCTGGACACCAACTTGAAAGAATGGGAACTCCATAGC
ACCTACACTGTGGACATGGAAATGGAGCTGCTACGTTTCGGAGGGACCCCTATTCACTTC
CCTGGTGGCAGGCCCCCTAGAGCAGATGCAAAATGCTGGTTTGCAGAAGGGAAGATCTGC
CATGGAGGCATCGACCCTGCCTTTGCCATGATGGTCTGCCTTACTTTGCTTATAGCCCTG
CTGTCTATTAATGGATTTGCTTACTTTATAAGGCGTCGTATAAATAAAATCCAGTTGATC
AAAGGACCCAATAGAATTCTACTGACTTTGGAGGATGTAACGTTTATCAATCCCCACTTT
GGCAGTAAGAGAGGAAGTCGTGCCAGTGTAAGCTTCCAGATTACCTCAGAGGTCCAAAGT
GGGAGGTCCCCAAGACTCTCCTTTTCTTCAGGGAGTCTAACTCCAGCTACCTATGAAAAC
TCCAACATAGCGATTTATGAGGGTGATTGGGTGTGGCTGAAAAAGTTCTCCCTTGGAGAT
TTTGGAGACCTTAAGTCCATCAAATCAAGAGCAAGTGATGTGTTCGAAATGATGAAGGAC
TTGCGTCATGAGAATATTAACCCTTTATTGGGTTTCTTCTATGATTCGGGGATGTTTGCC
ATTGTGACAGAATTCTGTTCCCGAGGGAGCCTAGAAGACATACTGACAAATCAAGATGTG
AAACTTGACTGGATGTTTAAATCATCACTCTTGCTGGATCTCATAAAGGGCATGAAGTAC
TTACACCACAGAGAGTTTGTTCATGGGAGGCTAAAGTCTCGAAACTGTGTGGTAGATGGG
CGTTTTGTACTAAAAGTGACAGATTATGGCTTTAACGACATCTTAGAAATGCTGAGACTC
TCTGAAGAGGAATCTTCTATGGAAGAGCTGCTGTGGACGGCCCCTGAACTGTTGAGAGCT
CCAAGAGGCAGCAGGTTAGGTTCTTTTGCAGGAGATGTCTATAGCTTTGCCATCATCATG
CAAGAAGTGATGGTCCGGGGTACCCCATTCTGCATGATGGATCTGCCAGCTCAAGAAATC
ATAAACAGACTTAAGAAGCCTCCTCCTGTGTACAGACCAGTAGTTCCTCCTGAGCATGCC
CCTCCAGAATGTCTCCAGCTGATGAAGCAGTGCTGGGCTGAGGCTGCAGAACAACGACCA
ACTTTTGATGAAATATTTAACCAGTTTAAAACTTTTAATAAAGGGAAGAAGACCAATATT
ATTGATTCTATGCTTCGGATGTTGGAGCAATATTCTAGCAACTTGGAAGATTTGATTCGG
GAGCGGACTGAAGAGCTGGAAATTGAAAAACAGAAAACGGAAAAGCTTCTAACACAGATG
CTACCACCATCAGTTGCTGAATCTCTCAAAAAGGGCTGCACAGTTGAACCTGAGGGCTTT
GACTTGGTCACCTTGTACTTCAGCGACATTGTGGGCTTCACAACCATTTCAGCCATGAGT
GAGCCCATTGAGGTCGTGGATCTTCTGAATGACCTGTACACACTCTTTGATGCAATAATT
GGCAGTCATGATGTCTACAAGGTAGAGACCATTGGAGATGCCTACATGGTGGCTTCAGGC
CTCCCAAAGAGGAATGGCAGTAGGCATGCAGCTGAGATTGCAAACATGTCCTTAGATATC
CTGAGCTCTGTGGGCACTTTCAAGATGCGGCACATGCCAGAAGTGCCGGTCCGAATTCGA
ATTGGCCTTCACTCAGGGCCGGTTGTTGCTGGAGTGGTGGGCCTCACCATGCCCAGATAC
TGCTTGTTTGGAGACACTGTGAACACAGCTTCTCGGATGGAATCTACAGGCTTACCTTAT
CGCATTCATGTCAGTCTCAGCACTGTTACAATTCTTCAAAATCTGAGTGAGGGCTATGAA
GTGGAGCTTCGAGGAAGAACAGAGCTCAAGGGCAAAGGCACAGAGGAAACCTTCTGGCTG
ATTGGGAAAAAAGGCTTCATGAAGCCCCTTCCTGTGCCCCCACCAGTGGACAAAGATGGG
CAAGTGGGCCATGGCCTGCAACCAGTGGAGATTGCAGCCTTCCAAAGAAGAAAAGCAGAA
AGGCAGTTGGTGAGAAACAAGCCATAA
Enzyme 56 GenBank Gene ID AL031387 Link Image
Enzyme 56 GeneCard ID GUCY2F Link Image
Enzyme 56 GenAtlas ID GUCY2F Link Image
Enzyme 56 HGNC ID HGNC:4691 Link Image
Enzyme 56 Chromosome Location Not Available
Enzyme 56 Locus Not Available
Enzyme 56 SNPs SNPJam Report Link Image
Enzyme 56 General References
  1. Lowe DG, Dizhoor AM, Liu K, Gu Q, Spencer M, Laura R, Lu L, Hurley JB: Cloning and expression of a second photoreceptor-specific membrane retina guanylyl cyclase (RetGC), RetGC-2. Proc Natl Acad Sci U S A. 1995 Jun 6;92(12):5535-9. [PubMed Link Image]
  2. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  3. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
  4. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 56 Metabolite References Not Available
Enzyme 57 [top]
Enzyme 57 ID 6366
Enzyme 57 Name Guanylate cyclase soluble subunit beta-2
Enzyme 57 Synonyms
  1. GCS-beta-2
Enzyme 57 Gene Name GUCY1B2
Enzyme 57 Protein Sequence >Guanylate cyclase soluble subunit beta-2
MSGYDRMLRTLGGNLMEFIENLDALHSYLALSYQEMNAPSFRVERGADGKMFLHYYSDRS
GLCHIVPGIIEAVAKDFFDIDVIMDILDMNEEVERTGKKEHVVFLIVQKAHRKMRKTKPK
RLQDSQGMERDQEALQAAFLKMKEKYLNVSACPVKKSHWDVVRSIVMFGKGHLMNTFEPI
YPERLWIEEKTFCNAFPFHIVFDESLQVKQARVNIQKYVPGLQTQNIQLDEYFSIIHPQV
TFNIFSIRRFINSQFVLKTRREMMPVAWQSRTTLKLQGQMIWMESMWCMVYLCSPKLRSL
QELEELNMHLSDIAPNDTTRDLILLNQQRLAEIELSNQLERKKEELQVLSKHLAIEKKKT
ETLLYAMLPKHVANQLREGKKVAAGEFKSCTILFSDVVTFTNICTACEPIQIVNVLNSMY
SKFDRLTSVHAVYKVETIGDAYMVVGGVPVPIGNHAQRVANFALGMRISAKEVTNPVTGE
PIQLRVGIHTGPVLADVVGDKMPRYCLFGDTVNTASRMESHGLPNKVHLSPTAYRALKNQ
GFKIIERGEIEVKGKGRMTTYFLIQNLNATEDEIMGRSKTPVDHKGSTQKASLPTTKLQG
SVQPSCPEHSSLASWLL
Enzyme 57 Number of Residues 617
Enzyme 57 Molecular Weight 70367.2
Enzyme 57 Theoretical pI 8.86
Enzyme 57 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • cyclase activity
  • guanylate cyclase activity
  • heme binding
  • ion binding
  • iron ion binding
  • lyase activity
  • metal ion binding
  • phosphorus-oxygen lyase activity
  • transition metal ion binding
Process
  • cGMP biosynthetic process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • signaling
  • signaling pathway
Component
Enzyme 57 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 57 Specific Function GTP = 3',5'-cyclic GMP + diphosphate
Enzyme 57 Pathways
Enzyme 57 Reactions
  • GTP = 3',5'-cyclic GMP + diphosphate [RN:R00434]
Enzyme 57 Pfam Domain Function
Enzyme 57 Signals
  • None
Enzyme 57 Transmembrane Regions
  • None
Enzyme 57 Essentiality Not Available
Enzyme 57 GenBank ID Protein 8081019 Link Image
Enzyme 57 UniProtKB/Swiss-Prot ID O75343 Link Image
Enzyme 57 UniProtKB/Swiss-Prot Entry Name GCYB2_HUMAN Link Image
Enzyme 57 PDB ID Not Available
Enzyme 57 Cellular Location Not Available
Enzyme 57 Gene Sequence >1854 bp
ATGTCTGGCTATGACAGGATGCTACGGACACTGGGAGGAAATCTCATGGAGTTTATTGAA
AACCTGGATGCCCTCCACAGTTACCTGGCACTCTCTTATCAGGAGATGAATGCACCATCG
TTTCGTGTGGAGAGAGGAGCAGATGGGAAAATGTTTCTCCATTACTACTCGGATAGAAGT
GGTCTGTGCCACATTGTACCAGGTATCATTGAGGCTGTGGCCAAAGACTTCTTTGATATT
GATGTAATCATGGACATTCTTGACATGAATGAAGAAGTGGAGAGGACAGGGAAGAAGGAG
CATGTTGTGTTTCTGATTGTACAGAAGGCTCACAGGAAGATGAGAAAGACNAAGCCAAAA
AGGTTACAAGACAGTCAGGGCATGGAGAGAGACCAAGAGGCCCTCCAGGCAGCTTTCCTC
AAGATGAAGGAGAAATATTTGAATGTCTCTGCTTGTCCTGTGAAAAAATCCCACTGGGAT
GTTGTGAGAAGCATAGTCATGTTTGGAAAAGGGCATCTCATGAACACCTTTGAGCCAATT
TATCCTGAGAGACTCTGGATTGAAGAGAAGACATTCTGCAACGCTTTTCCTTTCCACATT
GTATTCGATGAATCACTACAGGTGAAGCAAGCCAGAGTGAACATTCAGAAGTACGTACCA
GGACTCCAAACCCAGAATATTCAACTGGATGAGTATTTCTCCATCATTCATCCTCAAGTT
ACCTTCAACATTTTCAGCATCCGCAGATTTATCAACAGTCAATTTGTCCTGAAGACACGA
AGAGAAATGATGCCTGTAGCATGGCAAAGTCGGACTACACTCAAACTTCAAGGCCAGATG
ATCTGGATGGAGTCCATGTGGTGCATGGTGTACCTGTGCTCTCCGAAGCTCCGCAGCCTG
CAAGAGCTGGAAGAACTCAATATGCATCTTTCTGACATCGCCCCCAACGACACCACCAGG
GATCTCATCCTCCTGAACCAGCAGCGGCTGGCTGAGATAGAGCTGTCCAACCAGCTGGAA
AGGAAGAAGGAGGAGCTACAGGTCCTCTCCAAGCACTTGGCCATTGAAAAGAAGAAAACA
GAGACCTTACTTTATGCCATGCTGCCCAAACACGTGGCCAACCAGCTGAGGGAGGGCAAA
AAGGTGGCTGCAGGAGAATTTAAAAGCTGCACGATTCTTTTCAGCGATGTAGTGACATTT
ACTAACATCTGTACTGCCTGTGAACCTATACAAATAGTGAACGTGCTGAATTCCATGTAC
TCCAAGTTTGACAGATTAACCAGTGTGCACGCAGTCTATAAAGTAGAAACAATAGGAGAT
GCTTATATGGTGGTAGGAGGTGTACCAGTGCCTATTGGAAACCATGCTCAAAGAGTGGCT
AATTTTGCCTTGGGGATGAGAATTTCTGCAAAGGAAGTGACGAATCCTGTTACTGGAGAA
CCCATCCAGCTCAGAGTGGGGATCCATACTGGACCAGTCTTAGCAGATGTTGTAGGAGAC
AAGATGCCACGGTACTGCTTGTTTGGTGACACTGTGAACACAGCTTCTAGGATGGAAAGT
CATGGGCTTCCCAACAAAGTGCACCTCAGTCCCACAGCCTACAGAGCCTTGAAAAATCAA
GGGTTTAAAATCATTGAGAGGGGTGAAATTGAAGTGAAAGGTAAAGGGAGAATGACCACA
TACTTTTTGATCCAGAACTTGAATGCCACAGAGGATGAGATCATGGGGAGATCTAAAACC
CCAGTTGATCACAAGGGGTCAACACAGAAAGCATCCTTGCCCACCACCAAGCTCCAGGGC
TCAGTTCAACCATCTTGCCCTGAACACTCTTCTCTTGCATCCTGGTTATTATGA
Enzyme 57 GenBank Gene ID AF038499 Link Image
Enzyme 57 GeneCard ID GUCY1B2 Link Image
Enzyme 57 GenAtlas ID GUCY1B2 Link Image
Enzyme 57 HGNC ID HGNC:4686 Link Image
Enzyme 57 Chromosome Location 1
Enzyme 57 Locus 13q14.3
Enzyme 57 SNPs SNPJam Report Link Image
Enzyme 57 General References
  1. Behrends S, Vehse K: The beta(2) subunit of soluble guanylyl cyclase contains a human-specific frameshift and is expressed in gastric carcinoma. Biochem Biophys Res Commun. 2000 Apr 29;271(1):64-9. [PubMed Link Image]
  2. Behrends S, Kazmierczak B, Steenpa A, Knauf B, Bullerdiek J, Scholz H, Eiberg H: Assignment of GUCY1B2, the gene coding for the beta2 subunit of human guanylyl cyclase to chromosomal band 13q14.3 between markers D13S168 and D13S155. Genomics. 1999 Jan 1;55(1):126-7. [PubMed Link Image]
Enzyme 57 Metabolite References Not Available
Enzyme 58 [top]
Enzyme 58 ID 6369
Enzyme 58 Name mRNA-capping enzyme
Enzyme 58 Synonyms
  1. HCAP1
  2. HCE
  3. Polynucleotide 5'-triphosphatase
  4. mRNA 5'-triphosphatase
  5. TPase
  6. mRNA guanylyltransferase
  7. GTP--RNA guanylyltransferase
  8. GTase
Enzyme 58 Gene Name RNGTT
Enzyme 58 Protein Sequence >mRNA-capping enzyme
MAHNKIPPRWLNCPRRGQPVAGRFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKVK
MGLLVDLTNTSRFYDRNDIEKEGIKYIKLQCKGHGECPTTENTETFIRLCERFNERNPPE
LIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKGDYLKELFRRYGDI
EEAPPPPLLPDWCFEDDEDEDEDEDGKKESEPGSSASFGKRRKERLKLGAIFLEGVTVKG
VTQVTTQPKLGEVQQKCHQFCGWEGSGFPGAQPVSMDKQNIKLLDLKPYKVSWKADGTRY
MMLIDGTNEVFMIDRDNSVFHVSNLEFPFRKDLRMHLSNTLLDGEMIIDRVNGQAVPRYL
IYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRNKPFFDICT
SRKLLEGNFAKEVSHEMDGLIFQPTGKYKPGRCDDILKWKPPSLNSVDFRLKITRMGGEG
LLPQNVGLLYVGGYERPFAQIKVTKELKQYDNKIIECKFENNSWVFMRQRTDKSFPNAYN
TAMAVCNSISNPVTKEMLFEFIDRCTAASQGQKRKHHLDPDTELMPPPPPKRPRPLT
Enzyme 58 Number of Residues 597
Enzyme 58 Molecular Weight 68556.2
Enzyme 58 Theoretical pI 8.23
Enzyme 58 GO Classification
Function
  • RNA guanylyltransferase activity
  • catalytic activity
  • guanylyltransferase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • mRNA guanylyltransferase activity
  • nucleotide phosphatase activity
  • nucleotidyltransferase activity
  • phosphatase activity
  • phosphoprotein phosphatase activity
  • phosphoric ester hydrolase activity
  • polynucleotide 5'-phosphatase activity
  • protein tyrosine phosphatase activity
  • protein tyrosine/serine/threonine phosphatase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • RNA metabolic process
  • RNA processing
  • cellular macromolecule metabolic process
  • cellular metabolic process
  • dephosphorylation
  • mRNA capping
  • mRNA processing
  • macromolecule metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • protein amino acid dephosphorylation
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 58 General Function Involved in phosphatase activity
Enzyme 58 Specific Function Bifunctional mRNA-capping enzyme exhibiting RNA 5'- triphosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation:by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the gmp moiety of GTP to the 5'-diphosphate terminus
Enzyme 58 Pathways Not Available
Enzyme 58 Reactions
  • a 5'-phosphopolynucleotide + H2O = a polynucleotide + phosphate [RN:R02249]
Enzyme 58 Pfam Domain Function
Enzyme 58 Signals
  • None
Enzyme 58 Transmembrane Regions
  • None
Enzyme 58 Essentiality Not Available
Enzyme 58 GenBank ID Protein 3097308 Link Image
Enzyme 58 UniProtKB/Swiss-Prot ID O60942 Link Image
Enzyme 58 UniProtKB/Swiss-Prot Entry Name MCE1_HUMAN Link Image
Enzyme 58 PDB ID 1I9S Link Image
Enzyme 58 PDB File Show
Enzyme 58 3D Structure
Enzyme 58 Cellular Location Not Available
Enzyme 58 Gene Sequence >1794 bp
ATGGCTCACAACAAGATCCCGCCGCGGTGGCTGAACTGTCCCCGGCGCGGCCAGCCGGTG
GCAGGAAGATTCTTACCTCTGAAGACAATGTTAGGACCAAGATATGATAGTCAAGTTGCT
GAAGAAAATCGGTTCCATCCCAGCATGCTCTCAAATTACCTAAAGAGCCTAAAGGTTAAA
ATGGGCTTGTTGGTGGACCTGACAAATACTTCAAGGTTCTATGACCGAAATGACATAGAA
AAAGAAGGAATCAAATATATAAAACTTCAGTGTAAAGGACATGGTGAGTGCCCTACCACT
GAGAATACTGAGACCTTTATTCGTCTGTGTGAGCGGTTTAATGAAAGAAATCCACCTGAA
CTTATAGGTGTTCATTGTACTCATGGCTTCAATCGCACTGGTTTCCTCATATGTGCCTTT
TTGGTGGAGAAAATGGATTGGAGTATCGAAGCAGCAGTTGCTACTTTTGCCCAAGCCAGA
CCACCAGGAATCTACAAGGGTGATTATTTGAAGGAACTTTTTCGTCGGTATGGTGACATA
GAGGAAGCACCACCCCCACCTCTATTGCCAGATTGGTGTTTTGAGGATGATGAAGACGAA
GATGAGGATGAGGATGGAAAGAAGGAATCAGAACCCGGGTCAAGTGCTTCTTTTGGCAAA
AGGAGAAAAGAACGGTTAAAACTGGGCGCTATTTTCTTGGAAGGTGTTACTGTTAAAGGT
GTAACTCAAGTAACAACACAACCAAAGTTAGGAGAGGTACAGCAGAAGTGTCATCAATTC
TGTGGCTGGGAAGGGTCTGGATTCCCTGGAGCACAGCCTGTTTCCATGGACAAGCAAAAT
ATTAAACTTTTAGACCTGAAGCCATACAAAGTAAGCTGGAAAGCAGATGGTACTCGGTAC
ATGATGTTGATTGATGGCACAAATGAAGTTTTTATGATTGATAGAGACAATTCAGTATTT
CATGTTTCAAATCTGGAATTTCCATTTCGTAAAGATCTTCGTATGCATTTATCAAATACT
CTCTTGGATGGCGAGATGATTATTGACAGAGTAAATGGACAGGCTGTTCCTAGATATTTG
ATATATGACATAATTAAATTCAATTCACAGCCCGTTGGAGATTGTGATTTTAATGTTCGT
CTGCAGTGTATAGAACGAGAAATTATAAGTCCTCGACACGAAAAAATGAAGACTGGGCTC
ATTGACAAAACACAGGAACCATTTAGCGTCAGAAATAAGCCGTTTTTTGACATCTGTACT
TCAAGAAAGCTACTTGAAGGAAATTTTGCCAAAGAAGTGAGCCATGAAATGGATGGACTT
ATTTTTCAGCCTACTGGAAAATACAAACCTGGTCGATGTGATGATATTTTGAAATGGAAG
CCTCCCAGTCTGAATTCTGTGGATTTTCGTCTAAAAATAACAAGAATGGGAGGAGAAGGG
TTACTTCCTCAGAATGTTGGCCTCCTGTATGTTGGAGGTTATGAAAGACCCTTTGCACAA
ATCAAGGTGACAAAAGAGCTGAAACAGTATGACAACAAAATTATAGAATGCAAATTTGAG
AACAACAGCTGGGTCTTCATGAGACAGAGAACAGACAAAAGTTTTCCTAATGCCTACAAC
ACTGCCATGGCTGTGTGTAACAGCATCTCAAACCCTGTCACCAAGGAGATGCTGTTTGAG
TTCATCGACAGATGTACTGCAGCTTCTCAAGGACAGAAGCGAAAACATCATCTGGACCCT
GACACGGAGCTCATGCCACCACCACCTCCCAAAAGACCACGCCCTTTAACCTAA
Enzyme 58 GenBank Gene ID AB009022 Link Image
Enzyme 58 GeneCard ID RNGTT Link Image
Enzyme 58 GenAtlas ID RNGTT Link Image
Enzyme 58 HGNC ID HGNC:10073 Link Image
Enzyme 58 Chromosome Location 6
Enzyme 58 Locus 6q16
Enzyme 58 SNPs SNPJam Report Link Image
Enzyme 58 General References
  1. Yue Z, Maldonado E, Pillutla R, Cho H, Reinberg D, Shatkin AJ: Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II. Proc Natl Acad Sci U S A. 1997 Nov 25;94(24):12898-903. [PubMed Link Image]
  2. Yamada-Okabe T, Doi R, Shimmi O, Arisawa M, Yamada-Okabe H: Isolation and characterization of a human cDNA for mRNA 5'-capping enzyme. Nucleic Acids Res. 1998 Apr 1;26(7):1700-6. [PubMed Link Image]
  3. Tsukamoto T, Shibagaki Y, Murakoshi T, Suzuki M, Nakamura A, Gotoh H, Mizumoto K: Cloning and characterization of two human cDNAs encoding the mRNA capping enzyme. Biochem Biophys Res Commun. 1998 Feb 4;243(1):101-8. [PubMed Link Image]
  4. 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]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Pillutla RC, Yue Z, Maldonado E, Shatkin AJ: Recombinant human mRNA cap methyltransferase binds capping enzyme/RNA polymerase IIo complexes. J Biol Chem. 1998 Aug 21;273(34):21443-6. [PubMed Link Image]
  7. Wen Y, Shatkin AJ: Transcription elongation factor hSPT5 stimulates mRNA capping. Genes Dev. 1999 Jul 15;13(14):1774-9. [PubMed Link Image]
  8. Chiu YL, Coronel E, Ho CK, Shuman S, Rana TM: HIV-1 Tat protein interacts with mammalian capping enzyme and stimulates capping of TAR RNA. J Biol Chem. 2001 Apr 20;276(16):12959-66. Epub 2001 Jan 18. [PubMed Link Image]
  9. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
Enzyme 58 Metabolite References Not Available
Enzyme 59 [top]
Enzyme 59 ID 6417
Enzyme 59 Name Rap guanine nucleotide exchange factor 2
Enzyme 59 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 59 Gene Name RAPGEF2
Enzyme 59 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 59 Number of Residues 1499
Enzyme 59 Molecular Weight 167415.5
Enzyme 59 Theoretical pI 6.64
Enzyme 59 GO Classification
Function
  • GTPase regulator activity
  • binding
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • protein binding
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 59 General Function Involved in protein binding
Enzyme 59 Specific Function Guanine nucleotide exchange factor (GEF) for Rap1A, Rap1B and Rap2B GTPases. Does not interact with cAMP or cGMP
Enzyme 59 Pathways Not Available
Enzyme 59 Reactions Not Available
Enzyme 59 Pfam Domain Function
Enzyme 59 Signals
  • None
Enzyme 59 Transmembrane Regions
  • None
Enzyme 59 Essentiality Not Available
Enzyme 59 GenBank ID Protein 7657261 Link Image
Enzyme 59 UniProtKB/Swiss-Prot ID Q9Y4G8 Link Image
Enzyme 59 UniProtKB/Swiss-Prot Entry Name RPGF2_HUMAN Link Image
Enzyme 59 PDB ID Not Available
Enzyme 59 Cellular Location Not Available
Enzyme 59 Gene Sequence >4500 bp
ATGAAACCACTAGCAATCCCAGCTAACCATGGAGTTATGGGCCAGCAGGAGAAACACTCA
CTTCCTGCAGATTTCACAAAACTGCATCTTACTGACAGTCTCCACCCACAGGTGACCCAC
GTTTCTTCTAGCCATTCAGGATGTAGTATCACTAGTGATTCTGGGAGCAGCAGTCTTTCT
GATATCTACCAGGCCACAGAAAGCGAGGCTGGTGATATGGACCTGAGTGGGTTGCCAGAA
ACAGCAGTGGATTCCGAAGACGACGACGATGAAGAAGACATTGAGAGAGCATCAGATCCT
CTGATGAGCAGGGACATTGTGAGAGACTGCCTAGAGAAGGACCCAATTGACCGGACAGAT
GATGACATTGAACAACTCTTGGAATTTATGCACCAGTTGCCTGCTTTTGCCAATATGACA
ATGTCAGTGAGGCGAGAACTCTGTGCTGTGATGGTGTTCGCAGTGGTGGAAAGAGCAGGG
ACCATAGTGTTAAATGATGGTGAAGAGCTGGACTCCTGGTCAGTGATTCTCAATGGATCT
GTGGAAGTGACTTATCCAGATGGAAAAGCAGAAATACTGTGCATGGGAAATAGTTTTGGT
GTCTCTCCTACCATGGACAAAGAATACATGAAAGGAGTGATGAGAACAAAGGTGGATGAC
TGCCAGTTTGTCTGCATAGCCCAGCAAGATTACTGCCGTATTCTCAATCAAGTAGAAAAG
AACATGCAAAAAGTTGAAGAGGAAGGAGAGATTGTTATGGTGAAAGAACACCGAGAACTT
GATCGAACTGGAACAAGAAAGGGACACATTGTCATCAAGGGTACCTCAGAAAGGTTAACA
ATGCATTTGGTGGAAGAGCATTCAGTAGTAGATCCAACATTCATAGAAGACTTTCTGTTG
ACCTATAGGACTTTTCTTTCTAGCCCAATGGAAGTGGGCAAAAAGTTATTGGAGTGGTTT
AATGACCCGAGCCTCAGGGATAAGGTTACACGGGTAGTATTATTGTGGGTAAATAATCAC
TTCAATGACTTTGAAGGAGATCCTGCAATGACTCGATTTTTAGAAGAATTTGAAAACAAT
CTGGAAAGAGAGAAAATGGGTGGACACCTAAGGCTGTTGAATATCGCGTGTGCTGCTAAA
GCAAAAAGAAGATTGATGACGTTAACAAAACCATCCCGAGAAGCTCCTTTGCCTTTTATC
TTACTTGGAGGCTCTGAGAAGGGATTTGGAATCTTTGTTGACAGTGTAGATTCAGGTAGC
AAAGCAACTGAAGCAGGCTTGAAACGGGGGGATCAGATATTAGAAGTAAATGGCCAAAAC
TTTGAAAACATTCAGCTGTCAAAAGCTATGGAAATTCTTAGAAATAACACACATTTATCT
ATCACTGTGAAAACCAATTTATTTGTATTTAAAGAACTTCTAACAAGATTGTCAGAAGAG
AAAAGAAATGGTGCCCCCCACCTTCCTAAAATTGGTGACATTAAAAAGGCCAGTCGCTAC
TCCATTCCAGATCTTGCTGTAGATGTAGAACAGGTGATAGGACTTGAAAAAGTGAACAAA
AAAAGTAAAGCCAACACTGTGGGAGGAAGGAACAAGCTGAAAAAGATACTCGACAAGACT
CGGATCAGTATCTTGCCACAGAAACCATACAATGATATTGGGATTGGTCAGTCTCAAGAT
GACAGCATAGTAGGATTAAGGCAGACAAAGCACATCCCAACTGCATTGCCTGTCAGTGGA
ACCTTATCATCCAGTAATCCTGATTTATTGCAGTCACATCATCGCATTTTAGACTTCAGT
GCTACTCCTGACTTGCCAGATCAAGTGCTAAGGGTTTTTAAGGCTGATCAGCAAAGCCGC
TACATCATGATCAGTAAGGACACTACAGCAAAGGAAGTGGTCATTCAGGCTATCAGGGAG
TTTGCTGTTACTGCCACCCCGGATCAATATTCACTATGTGAGGTCTCTGTCACACCTGAG
GGAGTAATCAAACAAAGAAGACTTCCAGATCAGCTTTCCAAACTTGCAGACAGAATACAA
CTGAGTGGAAGGTATTATCTGAAAAACAACATGGAAACAGAAACTCTTTGTTCAGATGAA
GATGCTCAGGAGTTGTTGAGAGAGAGTCAAATTTCCCTCCTTCAGCTCAGCACTGTGGAA
GTTGCAACACAGCTCTCTATGCGAAATTTTGAACTCTTTCGCAACATTGAACCTACTGAA
TATATAGATGATTTATTTAAACTCAGATCAAAAACCAGCTGTGCCAACCTGAAGAGATTT
GAAGAAGTCATTAACCAGGAAACATTTTGGGTAGCATCTGAAATTCTCAGAGAAACAAAC
CAGCTGAAGAGGATGAAGATCATTAAGCATTTCATCAAGATAGCACTGCACTGTAGGGAA
TGCAAGAATTTTAACTCAATGTTTGCAATCATCAGTGGCCTAAACCTGGCACCAGTGGCA
AGACTGCGAACGACCTGGGAGAAACTTCCCAATAAATACGAAAAACTATTTCAAGATCTC
CAAGACCTGTTTGATCCTTCCAGAAACATGGCAAAATATCGTAATGTTCTCAATAGTCAA
AATCTACAACCTCCCATAATCCCTCTATTCCCAGTTATCAAAAAGGATCTCACCTTCCTT
CACGAAGGAAATGACTCAAAAGTAGACGGGCTGGTCAATTTTGAGAAGCTAAGGATGATT
GCAAAAGAAATTCGTCACGTTGGCCGAATGGCTTCAGTGAACATGGACCCTGCCCTCATG
TTCAGGACTCGGAAGAAGAAATGGCGGAGTTTGGGGTCTCTCAGCCAGGGTAGTACAAAT
GCAACAGTGCTAGATGTTGCTCAGACAGGTGGTCATAAAAAGCGGGTACGTCGTAGTTCC
TTTCTCAATGCCAAAAAGCTTTATGAAGATGCCCAAATGGCTCGAAAAGTGAAGCAGTAC
CTTTCCAATTTGGAGCTAGAAATGGACGAGGAGAGTCTTCAGACATTATCTCTGCAGTGT
GAGCCAGCAACCAACACATTGCCTAAGAATCCTGGTGACAAAAAGCCTGTCAAATCCGAG
ACCTCTCCAGTAGCTCCAAGGGCAGGGTCACAACAGAAAGCTCAGTCCCTGCCACAGCCC
CAGCAGCAGCCACCACCAGCACATAAAATCAACCAGGGACTACAGGTTCCCGCCGTGTCC
CTTTATCCTTCACGGAAGAAAGTGCCCGTAAAGGATCTCCCACCTTTTGGCATAAACTCT
CCACAAGCTTTAAAAAAAATTCTTTCTTTGTCTGAAGAAGGAAGTTTGGAACGTCACAAG
AAACAGGCTGAAGATACAATATCAAATGCATCTTCGCAGCTTTCTTCTCCTCCTACTTCT
CCACAGAGTTCTCCAAGGAAAGGCTATACTTTGGCTCCCAGTGGTACTGTGGATAATTTT
TCAGATTCTGGTCACAGTGAAATTTCTTCACGATCCAGTATTGTTAGCAATTCGTCTTTT
GACTCAGTGCCAGTCTCACTGCACGATGAGAGGCGCCAGAGGCATTCTGTCAGCATCGTG
GAAACAAACCTAGGGATGGGCAGGATGGAGAGGCGGACCATGATTGAACCTGATCAGTAT
AGCTTGGGGTCCTATGCACCAATGTCCGAGGGCCGAGGCTTATATGCTACAGCTACAGTA
ATTTCTTCTCCAAGCACAGAGGAACTTTCCCAGGATCAGGGGGATCGCGCGTCACTTGAT
GCTGCTGACAGTGGCCGTGGGAGCTGGACGTCATGCTCAAGTGGCTCCCATGATAATATA
CAGACGATCCAGCACCAGAGAAGCTGGGAGACTCTTCCATTCGGGCATACTCACTTTGAT
TATTCAGGGGATCCTGCAGGTTTATGGGCATCAAGCAGCCATATGGACCAAATTATGTTT
TCTGATCATAGCACAAAGTATAACAGGCAAAATCAAAGTAGAGAGAGCCTTGAACAAGCC
CAGTCCCGAGCAAGCTGGGCGTCTTCCACAGGTTACTGGGGAGAAGACTCAGAAGGTGAC
ACAGGCACAATAAAGCGGAGGGGTGGAAAGGATGTTTCCATTGAAGCCGAAAGCAGTAGC
CTAACGTCTGTGACTACGGAAGAAACCAAGCCTGTCCCCATGCCTGCCCACATAGCTGTG
GCATCAAGTACTACAAAGGGGCTCATTGCACGAAAGGAGGGCAGGTATCGAGAGCCCCCG
CCCACCCCTCCCGGCTACATTGGAATTCCCATTACTGACTTTCCAGAAGGGCACTCCCAT
CCAGCCAGGAAACCGCCGGACTACAACGTGGCCCTTCAGAGATCGCGGATGGTCGCACGA
TCCTCCGACACAGCTGGGCCTTCATCCGTACAGCAGCCACATGGGCATCCCACCAGCAGC
AGGCCTGTGAACAAACCTCAGTGGCATAAACCGAACGAGTCTGACCCGCGCCTCGCCCCC
TATCAGTCCCAAGGGTTTTCCACCGAGGAGGATGAAGATGAACAAGTTTCTGCTGTTTGA
Enzyme 59 GenBank Gene ID NM_014247.2 Link Image
Enzyme 59 GeneCard ID RAPGEF2 Link Image
Enzyme 59 GenAtlas ID RAPGEF2 Link Image
Enzyme 59 HGNC ID HGNC:16854 Link Image
Enzyme 59 Chromosome Location 4
Enzyme 59 Locus 4q32.1
Enzyme 59 SNPs SNPJam Report Link Image
Enzyme 59 General References
  1. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
  2. Ohtsuka T, Hata Y, Ide N, Yasuda T, Inoue E, Inoue T, Mizoguchi A, Takai Y: nRap GEP: a novel neural GDP/GTP exchange protein for rap1 small G protein that interacts with synaptic scaffolding molecule (S-SCAM). Biochem Biophys Res Commun. 1999 Nov;265(1):38-44. [PubMed Link Image]
  3. de Rooij J, Boenink NM, van Triest M, Cool RH, Wittinghofer A, Bos JL: PDZ-GEF1, a guanine nucleotide exchange factor specific for Rap1 and Rap2. J Biol Chem. 1999 Dec 31;274(53):38125-30. [PubMed Link Image]
  4. Rebhun JF, Castro AF, Quilliam LA: Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction. J Biol Chem. 2000 Nov 10;275(45):34901-8. [PubMed Link Image]
  5. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  6. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 59 Metabolite References Not Available
Enzyme 60 [top]
Enzyme 60 ID 6466
Enzyme 60 Name Serine/threonine-protein kinase PAK 7
Enzyme 60 Synonyms
  1. p21-activated kinase 5
  2. PAK-5
  3. p21-activated kinase 7
  4. PAK-7
Enzyme 60 Gene Name PAK7
Enzyme 60 Protein Sequence >Serine/threonine-protein kinase PAK 7
MFGKKKKKIEISGPSNFEHRVHTGFDPQEQKFTGLPQQWHSLLADTANRPKPMVDPSCIT
PIQLAPMKTIVRGNKPCKETSINGLLEDFDNISVTRSNSLRKESPPTPDQGASSHGPGHA
EENGFITFSQYSSESDTTADYTTEKYREKSLYGDDLDPYYRGSHAAKQNGHVMKMKHGEA
YYSEVKPLKSDFARFSADYHSHLDSLSKPSEYSDLKWEYQRASSSSPLDYSFQFTPSRTA
GTSGCSKESLAYSESEWGPSLDDYDRRPKSSYLNQTSPQPTMRQRSRSGSGLQEPMMPFG
ASAFKTHPQGHSYNSYTYPRLSEPTMCIPKVDYDRAQMVLSPPLSGSDTYPRGPAKLPQS
QSKSGYSSSSHQYPSGYHKATLYHHPSLQSSSQYISTASYLSSLSLSSSTYPPPSWGSSS
DQQPSRVSHEQFRAALQLVVSPGDPREYLANFIKIGEGSTGIVCIATEKHTGKQVAVKKM
DLRKQQRRELLFNEVVIMRDYHHDNVVDMYSSYLVGDELWVVMEFLEGGALTDIVTHTRM
NEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKR
KSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDSLP
PRVKDLHKVSSVLRGFLDLMLVREPSQRATAQELLGHPFLKLAGPPSCIVPLMRQYRHH
Enzyme 60 Number of Residues 719
Enzyme 60 Molecular Weight 80744.2
Enzyme 60 Theoretical pI 8.20
Enzyme 60 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
Enzyme 60 General Function Involved in protein kinase activity
Enzyme 60 Specific Function The activated kinase acts on a variety of targets
Enzyme 60 Pathways Not Available
Enzyme 60 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 60 Pfam Domain Function
Enzyme 60 Signals
  • None
Enzyme 60 Transmembrane Regions
  • None
Enzyme 60 Essentiality Not Available
Enzyme 60 GenBank ID Protein 24308191 Link Image
Enzyme 60 UniProtKB/Swiss-Prot ID Q9P286 Link Image
Enzyme 60 UniProtKB/Swiss-Prot Entry Name PAK7_HUMAN Link Image
Enzyme 60 PDB ID Not Available
Enzyme 60 Cellular Location Not Available
Enzyme 60 Gene Sequence >2160 bp
ATGTTTGGGAAGAAAAAGAAAAAGATTGAAATATCTGGCCCGTCCAACTTTGAACACAGG
GTTCATACTGGGTTTGATCCACAAGAGCAGAAGTTTACCGGCCTTCCCCAGCAGTGGCAC
AGCCTGTTAGCAGATACGGCCAACAGGCCAAAGCCTATGGTGGACCCTTCATGCATCACA
CCCATCCAGCTGGCTCCTATGAAGACAATCGTTAGAGGAAACAAACCCTGCAAGGAAACC
TCCATCAACGGCCTGCTAGAGGATTTTGACAACATCTCGGTGACTCGCTCCAACTCCCTA
AGGAAAGAAAGCCCACCCACCCCAGATCAGGGAGCCTCCAGCCACGGTCCAGGCCACGCG
GAAGAAAATGGCTTCATCACCTTCTCCCAGTATTCCAGCGAATCCGATACTACTGCTGAC
TACACGACCGAAAAGTACAGGGAGAAGAGTCTCTATGGAGATGATCTGGATCCGTATTAT
AGAGGCAGCCACGCAGCCAAGCAAAATGGGCACGTAATGAAAATGAAGCACGGGGAGGCC
TACTATTCTGAGGTGAAGCCTTTGAAATCCGATTTTGCCAGATTTTCTGCCGATTATCAC
TCACATTTGGACTCACTGAGCAAACCAAGTGAATACAGTGACCTCAAGTGGGAGTATCAG
AGAGCCTCGAGTAGCTCCCCTCTGGATTATTCATTCCAATTCACACCTTCTAGAACTGCA
GGGACCAGCGGGTGCTCCAAGGAGAGCCTGGCGTACAGTGAAAGTGAATGGGGACCCAGC
CTGGATGACTATGACAGGAGGCCAAAGTCTTCGTACCTGAATCAGACAAGCCCTCAGCCC
ACCATGCGGCAGAGGTCCAGGTCAGGCTCGGGACTCCAGGAACCGATGATGCCATTTGGA
GCAAGTGCATTTAAAACCCATCCCCAAGGACACTCCTACAACTCCTACACCTACCCTCGC
TTGTCCGAGCCCACAATGTGCATTCCAAAGGTGGATTACGATCGAGCACAGATGGTCCTC
AGCCCTCCACTGTCAGGGTCTGACACCTACCCCAGGGGCCCTGCCAAACTACCTCAAAGT
CAAAGCAAATCGGGCTATTCCTCAAGCAGTCACCAGTACCCGTCTGGGTACCACAAAGCC
ACCTTGTACCATCACCCCTCCCTGCAGAGCAGTTCGCAGTACATCTCCACGGCTTCCTAC
CTGAGCTCCCTCAGCCTCTCATCCAGCACCTACCCGCCGCCCAGCTGGGGCTCCTCCTCC
GACCAGCAGCCCTCCAGGGTGTCCCATGAACAGTTTCGGGCGGCCCTGCAGCTGGTGGTC
AGCCCAGGAGACCCCAGGGAATACTTGGCCAACTTTATCAAAATCGGGGAAGGCTCAACC
GGCATCGTATGCATCGCCACCGAGAAACACACAGGGAAACAAGTTGCAGTGAAGAAAATG
GACCTCCGGAAGCAACAGAGACGAGAACTGCTTTTCAATGAGGTCGTGATCATGCGGGAT
TACCACCATGACAATGTGGTTGACATGTACAGCAGCTACCTTGTCGGCGATGAGCTCTGG
GTGGTCATGGAGTTTCTAGAAGGTGGTGCCTTGACAGACATTGTGACTCACACCAGAATG
AATGAAGAACAGATAGCTACTGTCTGCCTGTCAGTTCTGAGAGCTCTCTCCTACCTTCAT
AACCAAGGAGTGATTCACAGGGACATAAAAAGTGACTCCATCCTCCTGACAAGCGATGGC
CGGATAAAGTTGTCTGATTTTGGTTTCTGTGCTCAAGTTTCCAAAGAGGTGCCGAAGAGG
AAATCATTGGTTGGCACTCCCTACTGGATGGCCCCTGAGGTGATTTCTAGGCTACCTTAT
GGGACAGAGGTGGACATCTGGTCCCTCGGGATCATGGTGATAGAAATGATTGATGGCGAG
CCCCCCTACTTCAATGAGCCTCCCCTCCAGGCGATGCGGAGGATCCGGGACAGTTTACCT
CCAAGAGTGAAGGACCTACACAAGGTTTCTTCAGTGCTCCGGGGATTCCTAGACTTGATG
TTGGTGAGGGAGCCCTCTCAGAGAGCAACAGCCCAGGAACTCCTCGGACATCCATTCTTA
AAACTAGCAGGTCCACCGTCTTGCATCGTCCCCCTCATGAGACAATACAGGCATCACTGA
Enzyme 60 GenBank Gene ID NM_020341.3 Link Image
Enzyme 60 GeneCard ID PAK7 Link Image
Enzyme 60 GenAtlas ID PAK7 Link Image
Enzyme 60 HGNC ID HGNC:15916 Link Image
Enzyme 60 Chromosome Location 2
Enzyme 60 Locus 20p12
Enzyme 60 SNPs SNPJam Report Link Image
Enzyme 60 General References
  1. Pandey A, Dan I, Kristiansen TZ, Watanabe NM, Voldby J, Kajikawa E, Khosravi-Far R, Blagoev B, Mann M: Cloning and characterization of PAK5, a novel member of mammalian p21-activated kinase-II subfamily that is predominantly expressed in brain. Oncogene. 2002 May 30;21(24):3939-48. [PubMed Link Image]
  2. Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Oct 29;6(5):337-45. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  5. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 60 Metabolite References Not Available
Enzyme 61 [top]
Enzyme 61 ID 6549
Enzyme 61 Name Serine/threonine-protein kinase PAK 6
Enzyme 61 Synonyms
  1. PAK-5
  2. p21-activated kinase 6
  3. PAK-6
Enzyme 61 Gene Name PAK6
Enzyme 61 Protein Sequence >Serine/threonine-protein kinase PAK 6
MFRKKKKKRPEISAPQNFQHRVHTSFDPKEGKFVGLPPQWQNILDTLRRPKPVVDPSRIT
RVQLQPMKTVVRGSAMPVDGYISGLLNDIQKLSVISSNTLRGRSPTSRRRAQSLGLLGDE
HWATDPDMYLQSPQSERTDPHGLYLSCNGGTPAGHKQMPWPEPQSPRVLPNGLAAKAQSL
GPAEFQGASQRCLQLGACLQSSPPGASPPTGTNRHGMKAAKHGSEEARPQSCLVGSATGR
PGGEGSPSPKTRESSLKRRLFRSMFLSTAATAPPSSSKPGPPPQSKPNSSFRPPQKDNPP
SLVAKAQSLPSDQPVGTFSPLTTSDTSSPQKSLRTAPATGQLPGRSSPAGSPRTWHAQIS
TSNLYLPQDPTVAKGALAGEDTGVVTHEQFKAALRMVVDQGDPRLLLDSYVKIGEGSTGI
VCLAREKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQHFNVVEMYKSYLVGEELWVL
MEFLQGGALTDIVSQVRLNEEQIATVCEAVLQALAYLHAQGVIHRDIKSDSILLTLDGRV
KLSDFGFCAQISKDVPKRKSLVGTPYWMAPEVISRSLYATEVDIWSLGIMVIEMVDGEPP
YFSDSPVQAMKRLRDSPPPKLKNSHKVSPVLRDFLERMLVRDPQERATAQELLDHPFLLQ
TGLPECLVPLIQLYRKQTSTC
Enzyme 61 Number of Residues 681
Enzyme 61 Molecular Weight 74868.1
Enzyme 61 Theoretical pI 10.06
Enzyme 61 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
Enzyme 61 General Function Involved in protein kinase activity
Enzyme 61 Specific Function The activated kinase acts on a variety of targets
Enzyme 61 Pathways Not Available
Enzyme 61 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 61 Pfam Domain Function
Enzyme 61 Signals
  • None
Enzyme 61 Transmembrane Regions
  • None
Enzyme 61 Essentiality Not Available
Enzyme 61 GenBank ID Protein 9082306 Link Image
Enzyme 61 UniProtKB/Swiss-Prot ID Q9NQU5 Link Image
Enzyme 61 UniProtKB/Swiss-Prot Entry Name PAK6_HUMAN Link Image
Enzyme 61 PDB ID Not Available
Enzyme 61 Cellular Location Not Available
Enzyme 61 Gene Sequence >2046 bp
ATGTTCCGCAAGAAAAAGAAGAAACGCCCTGAGATCTCAGCGCCACAGAACTTCCAGCAC
CGTGTCCACACCTCCTTCGACCCCAAAGAAGGCAAGTTTGTGGGCCTCCCCCCACAATGG
CAGAACATCCTGGACACACTGCGGCGCCCCAAGCCCGTGGTGGACCCTTCGCGAATCACA
CGGGTGCAGCTCCAGCCCATGAAGACAGTGGTGCGGGGCAGCGCGATGCCTGTGGATGGC
TACATCTCGGGGCTGCTCAACGACATCCAGAAGTTGTCAGTCATCAGCTCCAACACCCTG
CGTGGTCGCAGCCCCACCAGCCGGCGGCGGGCACAGTCCCTGGGGCTGCTGGGGGATGAG
CACTGGGCCACCGACCCAGACATGTACCTCCAGAGCCCCCAGTCTGAGCGCACTGACCCC
CACGGCCTCTACCTCAGCTGCAACGGGGGCACACCAGCAGGCCACAAGCAGATGCCGTGG
CCCGAGCCACAGAGCCCACGGGTCCTGCCCAATGGGCTGGCTGCAAAGGCACAGTCCCTG
GGCCCCGCCGAGTTTCAGGGTGCCTCGCAGCGCTGTCTGCAGCTGGGTGCCTGCCTGCAG
AGCTCCCCACCAGGAGCCTCGCCCCCCACGGGCACCAATAGGCATGGAATGAAGGCTGCC
AAGCATGGCTCTGAGGAGGCCCGGCCACAGTCCTGCCTGGTGGGCTCAGCCACAGGCAGG
CCAGGTGGGGAAGGCAGCCCTAGCCCTAAGACCCGGGAGAGCAGCCTGAAGCGCAGGCTA
TTCCGAAGCATGTTCCTGTCCACTGCTGCCACAGCCCCTCCAAGCAGCAGCAAGCCAGGC
CCTCCACCACAGAGCAAGCCCAACTCCTCTTTCCGACCGCCGCAGAAAGACAACCCCCCA
AGCCTGGTGGCCAAGGCCCAGTCCTTGCCCTCGGACCAGCCGGTGGGGACCTTCAGCCCT
CTGACCACTTCGGATACCAGCAGCCCCCAGAAGTCCCTCCGCACAGCCCCGGCCACAGGC
CAGCTTCCAGGCCGGTCTTCCCCAGCGGGATCCCCCCGCACCTGGCACGCCCAGATCAGC
ACCAGCAACCTGTACCTGCCCCAGGACCCCACGGTTGCCAAGGGTGCCCTGGCTGGTGAG
GACACAGGTGTTGTGACACATGAGCAGTTCAAGGCTGCGCTCAGGATGGTGGTGGACCAG
GGTGACCCCCGGCTGCTGCTGGACAGCTACGTGAAGATTGGCGAGGGCTCCACCGGCATC
GTCTGCTTGGCCCGGGAGAAGCACTCGGGCCGCCAGGTGGCCGTCAAGATGATGGACCTC
AGGAAGCAGCAGCGCAGGGAGCTGCTCTTCAACGAGGTGGTGATCATGCGGGACTACCAG
CACTTCAACGTGGTGGAGATGTACAAGAGCTACCTGGTGGGAGAGGAGCTGTGGGTGCTC
ATGGAGTTCCTGCAGGGAGGAGCCCTCACAGACATCGTCTCCCAAGTCAGGCTGAATGAG
GAGCAGATTGCCACTGTGTGTGAGGCTGTGCTGCAGGCCCTGGCCTACCTGCATGCTCAG
GGTGTCATCCACCGGGACATCAAGAGTGACTCCATCCTGCTGACCCTCGATGGCAGGGTG
AAGCTCTCGGACTTCGGATTCTGTGCTCAGATCAGCAAAGACGTCCCTAAGAGGAAGTCC
CTGGTGGGAACCCCCTACTGGATGGCTCCTGAAGTGATCTCCAGGTCTTTGTATGCCACT
GAGGTGGATATCTGGTCTCTGGGCATCATGGTGATTGAGATGGTAGATGGGGAGCCACCG
TACTTCAGTGACTCCCCAGTGCAAGCCATGAAGAGGCTCCGGGACAGCCCCCCACCCAAG
CTGAAAAACTCTCACAAGGTCTCCCCAGTGCTGCGAGACTTCCTGGAGCGGATGCTGGTG
CGGGACCCCCAAGAGAGAGCCACAGCCCAGGAGCTCCTAGACCACCCCTTCCTGCTGCAG
ACAGGGCTACCTGAGTGCCTGGTGCCCCTGATCCAGCTCTACCGAAAGCAGACCTCCACC
TGCTGA
Enzyme 61 GenBank Gene ID AF276893 Link Image
Enzyme 61 GeneCard ID PAK6 Link Image
Enzyme 61 GenAtlas ID PAK6 Link Image
Enzyme 61 HGNC ID HGNC:16061 Link Image
Enzyme 61 Chromosome Location 1
Enzyme 61 Locus 15q14
Enzyme 61 SNPs SNPJam Report Link Image
Enzyme 61 General References
  1. Yang F, Li X, Sharma M, Zarnegar M, Lim B, Sun Z: Androgen receptor specifically interacts with a novel p21-activated kinase, PAK6. J Biol Chem. 2001 May 4;276(18):15345-53. Epub 2001 Jan 25. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  4. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  5. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
  6. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 61 Metabolite References Not Available
Enzyme 62 [top]
Enzyme 62 ID 6563
Enzyme 62 Name Serine/threonine-protein kinase PAK 4
Enzyme 62 Synonyms
  1. p21-activated kinase 4
  2. PAK-4
Enzyme 62 Gene Name PAK4
Enzyme 62 Protein Sequence >Serine/threonine-protein kinase PAK 4
MFGKRKKRVEISAPSNFEHRVHTGFDQHEQKFTGLPRQWQSLIEESARRPKPLVDPACIT
SIQPGAPKTIVRGSKGAKDGALTLLLDEFENMSVTRSNSLRRDSPPPPARARQENGMPEE
PATTARGGPGKAGSRGRFAGHSEAGGGSGDRRRAGPEKRPKSSREGSGGPQESSRDKRPL
SGPDVGTPQPAGLASGAKLAAGRPFNTYPRADTDHPSRGAQGEPHDVAPNGPSAGGLAIP
QSSSSSSRPPTRARGAPSPGVLGPHASEPQLAPPACTPAAPAVPGPPGPRSPQREPQRVS
HEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRR
ELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAV
CLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPY
WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHK
VSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR
Enzyme 62 Number of Residues 591
Enzyme 62 Molecular Weight 64071.5
Enzyme 62 Theoretical pI 10.35
Enzyme 62 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
Enzyme 62 General Function Involved in protein kinase activity
Enzyme 62 Specific Function Activates the JNK pathway. Plays a role in the reorganization of the actin cytoskeleton and in the formation of filopodia. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates ARHGEF2
Enzyme 62 Pathways Not Available
Enzyme 62 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 62 Pfam Domain Function
Enzyme 62 Signals
  • None
Enzyme 62 Transmembrane Regions
  • None
Enzyme 62 Essentiality Not Available
Enzyme 62 GenBank ID Protein 62422554 Link Image
Enzyme 62 UniProtKB/Swiss-Prot ID O96013 Link Image
Enzyme 62 UniProtKB/Swiss-Prot Entry Name PAK4_HUMAN Link Image
Enzyme 62 PDB ID Not Available
Enzyme 62 Cellular Location Not Available
Enzyme 62 Gene Sequence >1776 bp
ATGTTTGGGAAGAGGAAGAAGCGGGTGGAGATCTCCGCGCCGTCCAACTTCGAGCACCGC
GTGCACACGGGCTTCGACCAGCACGAGCAGAAGTTCACGGGGCTGCCCCGCCAGTGGCAG
AGCCTGATCGAGGAGTCGGCTCGCCGGCCCAAGCCCCTCGTCGACCCCGCCTGCATCACC
TCCATCCAGCCCGGGGCCCCCAAGACCATCGTGCGGGGCAGCAAAGGTGCCAAAGATGGG
GCCCTCACGCTGCTGCTGGACGAGTTTGAGAACATGTCGGTGACACGCTCCAACTCCCTG
CGGAGAGACAGCCCGCCGCCGCCCGCCCGTGCCCGCCAGGAAAATGGGATGCCAGAGGAG
CCGGCCACCACGGCCAGAGGGGGCCCAGGGAAGGCAGGCAGCCGAGGCCGGTTCGCCGGT
CACAGCGAGGCGGGTGGCGGCAGTGGTGACAGGCGACGGGCGGGGCCAGAGAAGAGGCCC
AAGTCTTCCAGGGAGGGCTCAGGGGGTCCCCAGGAGTCCTCCCGGGACAAACGCCCCCTC
TCCGGGCCTGATGTCGGCACCCCCCAGCCTGCTGGTCTGGCCAGTGGGGCGAAACTGGCA
GCTGGCCGGCCCTTTAACACCTACCCGAGGGCTGACACGGACCACCCATCCCGGGGTGCC
CAGGGGGAGCCTCATGACGTGGCCCCTAACGGGCCATCAGCGGGGGGCCTGGCCATCCCC
CAGTCCTCCTCCTCCTCCTCCCGGCCTCCCACCCGAGCCCGAGGTGCCCCCAGCCCTGGA
GTGCTGGGACCCCACGCCTCAGAGCCCCAGCTGGCCCCTCCAGCCTGCACCCCCGCCGCC
CCTGCTGTTCCTGGGCCCCCTGGCCCCCGCTCACCACAGCGGGAGCCACAGCGAGTATCC
CATGAGCAGTTCCGGGCTGCCCTGCAGCTGGTGGTGGACCCAGGCGACCCCCGCTCCTAC
CTGGACAACTTCATCAAGATTGGCGAGGGCTCCACGGGCATCGTGTGCATCGCCACCGTG
CGCAGCTCGGGCAAGCTGGTGGCCGTCAAGAAGATGGACCTGCGCAAGCAGCAGAGGCGC
GAGCTGCTCTTCAACGAGGTGGTAATCATGAGGGACTACCAGCACGAGAATGTGGTGGAG
ATGTACAACAGCTACCTGGTGGGGGACGAGCTCTGGGTGGTCATGGAGTTCCTGGAAGGA
GGCGCCCTCACCGACATCGTCACCCACACCAGGATGAACGAGGAGCAGATCGCGGCCGTG
TGCCTTGCAGTGCTGCAGGCCCTGTCGGTGCTCCACGCCCAGGGCGTCATCCACCGGGAC
ATCAAGAGCGACTCGATCCTGCTGACCCATGATGGCAGGGTGAAGCTGTCAGACTTTGGG
TTCTGCGCCCAGGTGAGCAAGGAAGTGCCCCGAAGGAAGTCGCTGGTCGGCACGCCCTAC
TGGATGGCCCCAGAGCTCATCTCCCGCCTTCCCTACGGGCCAGAGGTAGACATCTGGTCG
CTGGGGATAATGGTGATTGAGATGGTGGACGGAGAGCCCCCCTACTTCAACGAGCCACCC
CTCAAAGCCATGAAGATGATTCGGGACAACCTGCCACCCCGACTGAAGAACCTGCACAAG
GTGTCGCCATCCCTGAAGGGCTTCCTGGACCGCCTGCTGGTGCGAGACCCTGCCCAGCGG
GCCACGGCAGCCGAGCTGCTGAAGCACCCATTCCTGGCCAAGGCAGGGCCGCCTGCCAGC
ATCGTGCCCCTCATGCGCCAGAACCGCACCAGATGA
Enzyme 62 GenBank Gene ID NM_001014831.2 Link Image
Enzyme 62 GeneCard ID PAK4 Link Image
Enzyme 62 GenAtlas ID PAK4 Link Image
Enzyme 62 HGNC ID HGNC:16059 Link Image
Enzyme 62 Chromosome Location 1
Enzyme 62 Locus 19q13.2
Enzyme 62 SNPs SNPJam Report Link Image
Enzyme 62 General References
  1. Abo A, Qu J, Cammarano MS, Dan C, Fritsch A, Baud V, Belisle B, Minden A: PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia. EMBO J. 1998 Nov 16;17(22):6527-40. [PubMed Link Image]
  2. Hirosawa M, Nagase T, Ishikawa K, Kikuno R, Nomura N, Ohara O: Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain. DNA Res. 1999 Oct 29;6(5):329-36. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Soosairajah J, Maiti S, Wiggan O, Sarmiere P, Moussi N, Sarcevic B, Sampath R, Bamburg JR, Bernard O: Interplay between components of a novel LIM kinase-slingshot phosphatase complex regulates cofilin. EMBO J. 2005 Feb 9;24(3):473-86. Epub 2005 Jan 20. [PubMed Link Image]
  7. Callow MG, Zozulya S, Gishizky ML, Jallal B, Smeal T: PAK4 mediates morphological changes through the regulation of GEF-H1. J Cell Sci. 2005 May 1;118(Pt 9):1861-72. Epub 2005 Apr 12. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  9. Wissing J, Jansch L, Nimtz M, Dieterich G, Hornberger R, Keri G, Wehland J, Daub H: Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics. 2007 Mar;6(3):537-47. Epub 2006 Dec 27. [PubMed Link Image]
  10. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  11. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  12. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  13. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  14. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 62 Metabolite References Not Available
Enzyme 63 [top]
Enzyme 63 ID 6596
Enzyme 63 Name Serine/threonine-protein kinase Nek9
Enzyme 63 Synonyms
  1. Nercc1 kinase
  2. Never in mitosis A-related kinase 9
  3. NimA-related protein kinase 9
  4. NimA-related kinase 8
  5. Nek8
Enzyme 63 Gene Name NEK9
Enzyme 63 Protein Sequence >Serine/threonine-protein kinase Nek9
MSVLGEYERHCDSINSDFGSESGGCGDSSPGPSASQGPRAGGGAAEQEELHYIPIRVLGR
GAFGEATLYRRTEDDSLVVWKEVDLTRLSEKERRDALNEIVILALLQHDNIIAYYNHFMD
NTTLLIELEYCNGGNLYDKILRQKDKLFEEEMVVWYLFQIVSAVSCIHKAGILHRDIKTL
NIFLTKANLIKLGDYGLAKKLNSEYSMAETLVGTPYYMSPELCQGVKYNFKSDIWAVGCV
IFELLTLKRTFDATNPLNLCVKIVQGIRAMEVDSSQYSLELIQMVHSCLDQDPEQRPTAD
ELLDRPLLRKRRREMEEKVTLLNAPTKRPRSSTVTEAPIAVVTSRTSEVYVWGGGKSTPQ
KLDVIKSGCSARQVCAGNTHFAVVTVEKELYTWVNMQGGTKLHGQLGHGDKASYRQPKHV
EKLQGKAIRQVSCGDDFTVCVTDEGQLYAFGSDYYGCMGVDKVAGPEVLEPMQLNFFLSN
PVEQVSCGDNHVVVLTRNKEVYSWGCGEYGRLGLDSEEDYYTPQKVDVPKALIIVAVQCG
CDGTFLLTQSGKVLACGLNEFNKLGLNQCMSGIINHEAYHEVPYTTSFTLAKQLSFYKIR
TIAPGKTHTAAIDERGRLLTFGCNKCGQLGVGNYKKRLGINLLGGPLGGKQVIRVSCGDE
FTIAATDDNHIFAWGNGGNGRLAMTPTERPHGSDICTSWPRPIFGSLHHVPDLSCRGWHT
ILIVEKVLNSKTIRSNSSGLSIGTVFQSSSPGGGGGGGGGEEEDSQQESETPDPSGGFRG
TMEADRGMEGLISPTEAMGNSNGASSSCPGWLRKELENAEFIPMPDSPSPLSAAFSESEK
DTLPYEELQGLKVASEAPLEHKPQVEASSPRLNPAVTCAGKGTPLTPPACACSSLQVEVE
RLQGLVLKCLAEQQKLQQENLQIFTQLQKLNKKLEGGQQVGMHSKGTQTAKEEMEMDPKP
DLDSDSWCLLGTDSCRPSL
Enzyme 63 Number of Residues 979
Enzyme 63 Molecular Weight 107167.7
Enzyme 63 Theoretical pI 5.50
Enzyme 63 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
Enzyme 63 General Function Involved in protein kinase activity
Enzyme 63 Specific Function Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation. Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2. Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues. Important for G1/S transition and S phase progression
Enzyme 63 Pathways Not Available
Enzyme 63 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 63 Pfam Domain Function
Enzyme 63 Signals
  • None
Enzyme 63 Transmembrane Regions
  • None
Enzyme 63 Essentiality Not Available
Enzyme 63 GenBank ID Protein 222136641 Link Image
Enzyme 63 UniProtKB/Swiss-Prot ID Q8TD19 Link Image
Enzyme 63 UniProtKB/Swiss-Prot Entry Name NEK9_HUMAN Link Image
Enzyme 63 PDB ID Not Available
Enzyme 63 Cellular Location Not Available
Enzyme 63 Gene Sequence >2940 bp
ATGTCGGTGCTGGGCGAGTACGAGCGACACTGCGATTCCATCAACTCGGACTTTGGGAGC
GAGTCCGGGGGTTGCGGGGACTCGAGTCCGGGGCCTAGCGCCAGTCAGGGGCCGCGAGCC
GGCGGCGGCGCGGCGGAGCAGGAGGAACTGCACTACATCCCCATCCGCGTCCTGGGCCGC
GGCGCCTTCGGGGAAGCCACGCTGTACCGCCGCACCGAGGATGACTCACTGGTTGTGTGG
AAGGAAGTCGATTTGACCCGGCTGTCTGAGAAGGAACGTCGTGATGCCTTGAATGAGATT
GTTATTCTGGCACTGCTGCAGCACGACAACATTATTGCCTACTACAATCACTTCATGGAC
AATACCACGCTGCTGATTGAGCTGGAATATTGTAATGGAGGGAACCTGTATGACAAAATC
CTTCGTCAGAAGGACAAGTTGTTTGAGGAAGAGATGGTGGTGTGGTACCTATTTCAGATT
GTTTCAGCAGTGAGCTGCATCCATAAAGCTGGAATCCTTCATAGAGATATAAAGACATTA
AATATTTTTCTGACCAAGGCAAACCTGATAAAACTTGGAGATTATGGCCTAGCAAAGAAA
CTTAATTCTGAGTATTCCATGGCTGAGACGCTTGTGGGAACCCCATATTACATGTCTCCA
GAGCTCTGTCAAGGAGTAAAGTACAATTTCAAGTCTGATATCTGGGCAGTTGGCTGCGTC
ATTTTTGAACTGCTTACCTTAAAGAGGACGTTTGATGCTACAAACCCACTTAACCTGTGT
GTGAAGATCGTGCAAGGAATTCGGGCCATGGAAGTTGACTCTAGCCAGTACTCTTTGGAA
TTGATCCAAATGGTTCATTCGTGCCTTGACCAGGATCCTGAGCAGAGACCTACTGCAGAT
GAACTTCTAGATCGCCCTCTTCTCAGGAAACGCAGGAGAGAGATGGAGGAAAAAGTCACT
CTGCTTAATGCACCTACAAAGAGACCAAGGTCAAGCACTGTGACTGAAGCACCCATTGCT
GTAGTAACATCACGAACCAGTGAAGTCTATGTTTGGGGTGGTGGAAAATCCACCCCCCAG
AAACTGGATGTTATCAAGAGTGGCTGTAGTGCCCGGCAGGTCTGTGCAGGGAATACCCAC
TTTGCTGTGGTCACAGTGGAGAAGGAACTGTACACTTGGGTGAACATGCAAGGAGGCACT
AAACTCCATGGTCAGCTGGGCCATGGAGACAAAGCCTCCTATCGACAGCCAAAGCATGTG
GAAAAGTTGCAAGGCAAAGCTATCCGTCAGGTGTCATGTGGTGATGATTTCACTGTCTGT
GTGACTGATGAGGGTCAGCTCTATGCCTTCGGATCAGATTATTATGGCTGCATGGGGGTG
GACAAAGTTGCTGGCCCTGAAGTGCTAGAACCCATGCAGCTGAACTTCTTCCTCAGCAAT
CCAGTGGAGCAGGTCTCCTGTGGAGATAATCATGTGGTGGTTCTGACACGAAACAAGGAA
GTCTATTCTTGGGGCTGTGGCGAATATGGACGACTGGGTTTGGATTCAGAAGAGGATTAT
TATACACCACAAAAGGTGGATGTTCCCAAGGCCTTGATTATTGTTGCAGTTCAATGTGGC
TGTGATGGGACATTTCTGTTGACCCAGTCAGGCAAAGTGCTGGCCTGTGGACTCAATGAA
TTCAATAAGCTGGGTCTGAATCAGTGCATGTCGGGAATTATCAACCATGAAGCATACCAT
GAAGTTCCCTACACAACGTCCTTTACCTTGGCCAAACAGTTGTCCTTTTATAAGATCCGT
ACCATTGCCCCAGGCAAGACTCACACAGCTGCTATTGATGAGCGAGGCCGGCTGCTGACC
TTTGGCTGCAACAAGTGTGGGCAGCTGGGCGTTGGGAACTACAAGAAGCGTCTGGGAATC
AACCTGTTGGGGGGACCCCTTGGTGGGAAGCAAGTGATCAGGGTCTCCTGCGGTGATGAG
TTTACCATTGCTGCCACTGATGATAATCACATTTTTGCCTGGGGCAATGGTGGTAATGGC
CGCCTGGCAATGACCCCCACAGAGAGACCACATGGCTCTGATATCTGTACCTCATGGCCT
CGGCCTATTTTTGGATCTCTGCATCATGTCCCGGACCTGTCTTGCCGTGGATGGCATACC
ATTCTCATCGTTGAGAAAGTATTGAATTCTAAGACCATCCGTTCCAATAGCAGTGGCTTA
TCCATTGGAACTGTGTTTCAGAGCTCTAGCCCGGGAGGAGGCGGCGGGGGCGGCGGTGGT
GAAGAAGAGGACAGTCAGCAGGAATCTGAAACTCCTGACCCAAGTGGAGGCTTCCGAGGA
ACAATGGAAGCAGACCGAGGAATGGAAGGTTTAATCAGTCCCACAGAGGCCATGGGGAAC
AGTAATGGGGCCAGCAGCTCCTGTCCTGGCTGGCTTCGAAAGGAGCTGGAAAATGCAGAA
TTTATCCCCATGCCTGACAGCCCATCTCCTCTCAGTGCAGCGTTTTCAGAATCTGAGAAA
GATACCCTGCCCTATGAAGAGCTGCAAGGACTCAAAGTGGCCTCTGAAGCTCCTTTGGAA
CACAAACCCCAAGTAGAAGCCTCGTCACCTCGGCTGAATCCTGCAGTAACCTGTGCTGGG
AAGGGAACACCACTGACTCCTCCTGCGTGTGCGTGCAGCTCTCTGCAGGTGGAGGTTGAG
AGATTGCAGGGTCTGGTGTTAAAGTGTCTGGCTGAACAACAGAAGCTACAGCAAGAAAAC
CTCCAGATTTTTACCCAACTGCAGAAGTTGAACAAGAAATTAGAAGGAGGGCAGCAGGTG
GGGATGCATTCCAAAGGAACTCAGACAGCAAAGGAAGAGATGGAAATGGATCCAAAGCCT
GACTTAGATTCAGATTCCTGGTGCCTCCTGGGAACAGACTCCTGTAGACCCAGCCTCTAG
Enzyme 63 GenBank Gene ID NM_033116.4 Link Image
Enzyme 63 GeneCard ID NEK9 Link Image
Enzyme 63 GenAtlas ID NEK9 Link Image
Enzyme 63 HGNC ID HGNC:18591 Link Image
Enzyme 63 Chromosome Location 1
Enzyme 63 Locus 14q24.3
Enzyme 63 SNPs SNPJam Report Link Image
Enzyme 63 General References
  1. Holland PM, Milne A, Garka K, Johnson RS, Willis C, Sims JE, Rauch CT, Bird TA, Virca GD: Purification, cloning, and characterization of Nek8, a novel NIMA-related kinase, and its candidate substrate Bicd2. J Biol Chem. 2002 May 3;277(18):16229-40. Epub 2002 Feb 25. [PubMed Link Image]
  2. Roig J, Mikhailov A, Belham C, Avruch J: Nercc1, a mammalian NIMA-family kinase, binds the Ran GTPase and regulates mitotic progression. Genes Dev. 2002 Jul 1;16(13):1640-58. [PubMed Link Image]
  3. Ohara O, Nagase T, Mitsui G, Kohga H, Kikuno R, Hiraoka S, Takahashi Y, Kitajima S, Saga Y, Koseki H: Characterization of size-fractionated cDNA libraries generated by the in vitro recombination-assisted method. DNA Res. 2002 Apr 30;9(2):47-57. [PubMed Link Image]
  4. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Tan BC, Lee SC: Nek9, a novel FACT-associated protein, modulates interphase progression. J Biol Chem. 2004 Mar 5;279(10):9321-30. Epub 2003 Dec 2. [PubMed Link Image]
  7. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  8. Wissing J, Jansch L, Nimtz M, Dieterich G, Hornberger R, Keri G, Wehland J, Daub H: Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics. 2007 Mar;6(3):537-47. Epub 2006 Dec 27. [PubMed Link Image]
  9. Rapley J, Nicolas M, Groen A, Regue L, Bertran MT, Caelles C, Avruch J, Roig J: The NIMA-family kinase Nek6 phosphorylates the kinesin Eg5 at a novel site necessary for mitotic spindle formation. J Cell Sci. 2008 Dec 1;121(Pt 23):3912-21. Epub 2008 Nov 11. [PubMed Link Image]
  10. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  11. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  12. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  13. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  14. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  15. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  16. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 63 Metabolite References Not Available
Enzyme 64 [top]
Enzyme 64 ID 6633
Enzyme 64 Name Citron Rho-interacting kinase
Enzyme 64 Synonyms
  1. CRIK
  2. Serine/threonine-protein kinase 21
Enzyme 64 Gene Name CIT
Enzyme 64 Protein Sequence >Citron Rho-interacting kinase
MLKFKYGARNPLDAGAAEPIASRASRLNLFFQGKPPFMTQQQMSPLSREGILDALFVLFE
ECSQPALMKIKHVSNFVRKYSDTIAELQELQPSAKDFEVRSLVGCGHFAEVQVVREKATG
DIYAMKVMKKKALLAQEQVSFFEEERNILSRSTSPWIPQLQYAFQDKNHLYLVMEYQPGG
DLLSLLNRYEDQLDENLIQFYLAELILAVHSVHLMGYVHRDIKPENILVDRTGHIKLVDF
GSAAKMNSNKMVNAKLPIGTPDYMAPEVLTVMNGDGKGTYGLDCDWWSVGVIAYEMIYGR
SPFAEGTSARTFNNIMNFQRFLKFPDDPKVSSDFLDLIQSLLCGQKERLKFEGLCCHPFF
SKIDWNNIRNSPPPFVPTLKSDDDTSNFDEPEKNSWVSSSPCQLSPSGFSGEELPFVGFS
YSKALGILGRSESVVSGLDSPAKTSSMEKKLLIKSKELQDSQDKCHKMEQEMTRLHRRVS
EVEAVLSQKEVELKASETQRSLLEQDLATYITECSSLKRSLEQARMEVSQEDDKALQLLH
DIREQSRKLQEIKEQEYQAQVEEMRLMMNQLEEDLVSARRRSDLYESELRESRLAAEEFK
RKATECQHKLLKAKDQGKPEVGEYAKLEKINAEQQLKIQELQEKLEKAVKASTEATELLQ
NIRQAKERAERELEKLQNREDSSEGIRKKLVEAEELEEKHREAQVSAQHLEVHLKQKEQH
YEEKIKVLDNQIKKDLADKETLENMMQRHEEEAHEKGKILSEQKAMINAMDSKIRSLEQR
IVELSEANKLAANSSLFTQRNMKAQEEMISELRQQKFYLETQAGKLEAQNRKLEEQLEKI
SHQDHSDKNRLLELETRLREVSLEHEEQKLELKRQLTELQLSLQERESQLTALQAARAAL
ESQLRQAKTELEETTAEAEEEIQALTAHRDEIQRKFDALRNSCTVITDLEEQLNQLTEDN
AELNNQNFYLSKQLDEASGANDEIVQLRSEVDHLRREITEREMQLTSQKQTMEALKTTCT
MLEEQVMDLEALNDELLEKERQWEAWRSVLGDEKSQFECRVRELQRMLDTEKQSRARADQ
RITESRQVVELAVKEHKAEILALQQALKEQKLKAESLSDKLNDLEKKHAMLEMNARSLQQ
KLETERELKQRLLEEQAKLQQQMDLQKNHIFRLTQGLQEALDRADLLKTERSDLEYQLEN
IQVLYSHEKVKMEGTISQQTKLIDFLQAKMDQPAKKKKGLFSRRKEDPALPTQVPLQYNE
LKLALEKEKARCAELEEALQKTRIELRSAREEAAHRKATDHPHPSTPATARQQIAMSAIV
RSPEHQPSAMSLLAPPSSRRKESSTPEEFSRRLKERMHHNIPHRFNVGLNMRATKCAVCL
DTVHFGRQASKCLECQVMCHPKCSTCLPATCGLPAEYATHFTEAFCRDKMNSPGLQTKEP
SSSLHLEGWMKVPRNNKRGQQGWDRKYIVLEGSKVLIYDNEAREAGQRPVEEFELCLPDG
DVSIHGAVGASELANTAKADVPYILKMESHPHTTCWPGRTLYLLAPSFPDKQRWVTALES
VVAGGRVSREKAEADAKLLGNSLLKLEGDDRLDMNCTLPFSDQVVLVGTEEGLYALNVLK
NSLTHVPGIGAVFQIYIIKDLEKLLMIAGEERALCLVDVKKVKQSLAQSHLPAQPDISPN
IFEAVKGCHLFGAGKIENGLCICAAMPSKVVILRYNENLSKYCIRKEIETSEPCSCIHFT
NYSILIGTNKFYEIDMKQYTLEEFLDKNDHSLAPAVFAASSNSFPVSIVQVNSAGQREEY
LLCFHEFGVFVDSYGRRSRTDDLKWSRLPLAFAYREPYLFVTHFNSLEVIEIQARSSAGT
PARAYLDIPNPRYLGPAISSGAIYLASSYQDKLRVICCKGNLVKESGTEHHRGPSTSRSS
PNKRGPPTYNEHITKRVASSPAPPEGPSHPREPSTPHRYREGRTELRRDKSPGRPLEREK
SPGRMLSTRRERSPGRLFEDSSRGRLPAGAVRTPLSQVNKVWDQSSV
Enzyme 64 Number of Residues 2027
Enzyme 64 Molecular Weight 231428.9
Enzyme 64 Theoretical pI 6.54
Enzyme 64 GO Classification
Function
  • ATP binding
  • GTPase regulator activity
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • enzyme regulator activity
  • kinase activity
  • nucleoside binding
  • nucleoside-triphosphatase regulator activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • small GTPase regulator activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 64 General Function Involved in protein serine/threonine kinase activity
Enzyme 64 Specific Function Required for KIF14 localization to the central spindle and midbody. May play a role in cytokinesis. Putative RHO/RAC effector that binds to the GTP-bound forms of RHO and RAC1. It probably binds p21 with a tighter specificity in vivo. Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Plays an important role in the regulation of cytokinesis and the development of the central nervous system
Enzyme 64 Pathways Not Available
Enzyme 64 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 64 Pfam Domain Function
Enzyme 64 Signals
  • None
Enzyme 64 Transmembrane Regions
  • None
Enzyme 64 Essentiality Not Available
Enzyme 64 GenBank ID Protein 32698688 Link Image
Enzyme 64 UniProtKB/Swiss-Prot ID O14578 Link Image
Enzyme 64 UniProtKB/Swiss-Prot Entry Name CTRO_HUMAN Link Image
Enzyme 64 PDB ID Not Available
Enzyme 64 Cellular Location Not Available
Enzyme 64 Gene Sequence >6084 bp
ATGTTGAAGTTCAAATATGGAGCGCGGAATCCTTTGGATGCTGGTGCTGCTGAACCCATT
GCCAGCCGGGCCTCCAGGCTGAATCTGTTCTTCCAGGGGAAACCACCCTTTATGACTCAA
CAGCAGATGTCTCCTCTTTCCCGAGAAGGGATATTAGATGCCCTCTTTGTTCTCTTTGAA
GAATGCAGTCAGCCTGCTCTGATGAAGATTAAGCACGTGAGCAACTTTGTCCGGAAGTAT
TCCGACACCATAGCTGAGTTACAGGAGCTCCAGCCTTCGGCAAAGGACTTCGAAGTCAGA
AGTCTTGTAGGTTGTGGTCACTTTGCTGAAGTGCAGGTGGTAAGAGAGAAAGCAACCGGG
GACATCTATGCTATGAAAGTGATGAAGAAGAAGGCTTTATTGGCCCAGGAGCAGGTTTCA
TTTTTTGAGGAAGAGCGGAACATATTATCTCGAAGCACAAGCCCGTGGATCCCCCAATTA
CAGTATGCCTTTCAGGACAAAAATCACCTTTATCTGGTCATGGAATATCAGCCTGGAGGG
GACTTGCTGTCACTTTTGAATAGATATGAGGACCAGTTAGATGAAAACCTGATACAGTTT
TACCTAGCTGAGCTGATTTTGGCTGTTCACAGCGTTCATCTGATGGGATACGTGCATCGA
GACATCAAGCCTGAGAACATTCTCGTTGACCGCACAGGACACATCAAGCTGGTGGATTTT
GGATCTGCCGCGAAAATGAATTCAAACAAGATGGTGAATGCCAAACTCCCGATTGGGACC
CCAGATTACATGGCTCCTGAAGTGCTGACTGTGATGAACGGGGATGGAAAAGGCACCTAC
GGCCTGGACTGTGACTGGTGGTCAGTGGGCGTGATTGCCTATGAGATGATTTATGGGAGA
TCCCCCTTCGCAGAGGGAACCTCTGCCAGAACCTTCAATAACATTATGAATTTCCAGCGG
TTTTTGAAATTTCCAGATGACCCCAAAGTGAGCAGTGACTTTCTTGATCTGATTCAAAGC
TTGTTGTGCGGCCAGAAAGAGAGACTGAAGTTTGAAGGTCTTTGCTGCCATCCTTTCTTC
TCTAAAATTGACTGGAACAACATTCGTAACTCTCCTCCCCCCTTCGTTCCCACCCTCAAG
TCTGACGATGACACCTCCAATTTTGATGAACCAGAGAAGAATTCGTGGGTTTCATCCTCT
CCGTGCCAGCTGAGCCCCTCAGGCTTCTCGGGTGAAGAACTGCCGTTTGTGGGGTTTTCG
TACAGCAAGGCACTGGGGATTCTTGGTAGATCTGAGTCTGTTGTGTCGGGTCTGGACTCC
CCTGCCAAGACTAGCTCCATGGAAAAGAAACTTCTCATCAAAAGCAAAGAGCTACAAGAC
TCTCAGGACAAGTGTCACAAGATGGAGCAGGAAATGACCCGGTTACATCGGAGAGTGTCA
GAGGTGGAGGCTGTGCTTAGTCAGAAGGAGGTGGAGCTGAAGGCCTCTGAGACTCAGAGA
TCCCTCCTGGAGCAGGACCTTGCTACCTACATCACAGAATGCAGTAGCTTAAAGCGAAGT
TTGGAGCAAGCACGGATGGAGGTGTCCCAGGAGGATGACAAAGCACTGCAGCTTCTCCAT
GATATCAGAGAGCAGAGCCGGAAGCTCCAAGAAATCAAAGAGCAGGAGTACCAGGCTCAA
GTGGAAGAAATGAGGTTGATGATGAATCAGTTGGAAGAGGATCTTGTCTCAGCAAGAAGA
CGGAGTGATCTCTACGAATCTGAGCTGAGAGAGTCTCGGCTTGCTGCTGAAGAATTCAAG
CGGAAAGCGACAGAATGTCAGCATAAACTGTTGAAGGCTAAGGATCAAGGGAAGCCTGAA
GTGGGAGAATATGCGAAACTGGAGAAGATCAATGCTGAGCAGCAGCTCAAAATTCAGGAG
CTCCAAGAGAAACTGGAGAAGGCTGTAAAAGCCAGCACGGAGGCCACCGAGCTGCTGCAG
AATATCCGCCAGGCAAAGGAGCGAGCCGAGAGGGAGCTGGAGAAGCTGCAGAACCGAGAG
GATTCTTCTGAAGGCATCAGAAAGAAGCTGGTGGAAGCTGAGGAGCTCGAAGAGAAACAT
CGGGAGGCCCAAGTCTCAGCCCAGCACCTAGAAGTGCACCTGAAACAGAAAGAGCAGCAC
TATGAGGAAAAGATTAAAGTGTTGGACAATCAGATAAAGAAAGACCTGGCTGACAAGGAG
ACACTGGAGAACATGATGCAGAGACACGAGGAGGAGGCCCATGAGAAGGGCAAAATTCTC
AGCGAACAGAAGGCGATGATCAATGCTATGGATTCCAAGATCAGATCCCTGGAACAGAGG
ATTGTGGAACTGTCTGAAGCCAATAAACTTGCAGCAAATAGCAGTCTTTTTACCCAAAGG
AACATGAAGGCCCAAGAAGAGATGATTTCTGAACTCAGGCAACAGAAATTTTACCTGGAG
ACACAGGCTGGGAAGTTGGAGGCCCAGAACCGAAAACTGGAGGAGCAGCTGGAGAAGATC
AGCCACCAAGACCACAGTGACAAGAATCGGCTGCTGGAACTGGAGACAAGATTGCGGGAG
GTCAGTCTAGAGCACGAGGAGCAGAAACTGGAGCTCAAGCGCCAGCTCACAGAGCTACAG
CTCTCCCTGCAGGAGCGCGAGTCACAGTTGACAGCCCTGCAGGCTGCACGGGCGGCCCTG
GAGAGCCAGCTTCGCCAGGCGAAGACAGAGCTGGAAGAGACCACAGCAGAAGCTGAAGAG
GAGATCCAGGCACTCACGGCACATAGAGATGAAATCCAGCGCAAATTTGATGCTCTTCGT
AACAGCTGTACTGTAATCACAGACCTGGAGGAGCAGCTAAACCAGCTGACCGAGGACAAC
GCTGAACTCAACAACCAAAACTTCTACTTGTCCAAACAACTCGATGAGGCTTCTGGCGCC
AACGACGAGATTGTACAACTGCGAAGTGAAGTGGACCATCTCCGCCGGGAGATCACGGAA
CGAGAGATGCAGCTTACCAGCCAGAAGCAAACGATGGAGGCTCTGAAGACCACGTGCACC
ATGCTGGAGGAACAGGTCATGGATTTGGAGGCCCTAAACGATGAGCTGCTAGAAAAAGAG
CGGCAGTGGGAGGCCTGGAGGAGCGTCCTGGGTGATGAGAAATCCCAGTTTGAGTGTCGG
GTTCGAGAGCTGCAGAGAATGCTGGACACCGAGAAACAGAGCAGGGCGAGAGCCGATCAG
CGGATCACCGAGTCTCGCCAGGTGGTGGAGCTGGCAGTGAAGGAGCACAAGGCTGAGATT
CTCGCTCTGCAGCAGGCTCTCAAAGAGCAGAAGCTGAAGGCCGAGAGCCTCTCTGACAAG
CTCAATGACCTGGAGAAGAAGCATGCTATGCTTGAAATGAATGCCCGAAGCTTACAGCAG
AAGCTGGAGACTGAACGAGAGCTCAAACAGAGGCTTCTGGAAGAGCAAGCCAAATTACAG
CAGCAGATGGACCTGCAGAAAAATCACATTTTCCGTCTGACTCAAGGACTGCAAGAAGCT
CTAGATCGGGCTGATCTACTGAAGACAGAAAGAAGTGACTTGGAGTATCAGCTGGAAAAC
ATTCAGGTTCTCTATTCTCATGAAAAGGTGAAAATGGAAGGCACTATTTCTCAACAAACC
AAACTCATTGATTTTCTGCAAGCCAAAATGGACCAACCTGCTAAAAAGAAAAAGGGTTTA
TTTAGTCGACGGAAAGAGGACCCTGCTTTACCCACACAGGTTCCTCTGCAGTACAATGAG
CTGAAGCTGGCCCTGGAGAAGGAGAAAGCTCGCTGTGCAGAGCTAGAGGAAGCCCTTCAG
AAGACCCGCATCGAGCTCCGGTCCGCCCGGGAGGAAGCTGCCCACCGCAAAGCAACGGAC
CACCCACACCCATCCACGCCAGCCACCGCGAGGCAGCAGATCGCCATGTCCGCCATCGTG
CGGTCGCCAGAGCACCAGCCCAGTGCCATGAGCCTGCTGGCCCCGCCATCCAGCCGCAGA
AAGGAGTCTTCAACTCCAGAGGAATTTAGTCGGCGTCTTAAGGAACGCATGCACCACAAT
ATTCCTCACCGATTCAACGTAGGACTGAACATGCGAGCCACAAAGTGTGCTGTGTGTCTG
GATACCGTGCACTTTGGACGCCAGGCATCCAAATGTCTCGAATGTCAGGTGATGTGTCAC
CCCAAGTGCTCCACGTGCTTGCCAGCCACCTGCGGCTTGCCTGCTGAATATGCCACACAC
TTCACCGAGGCCTTCTGCCGTGACAAAATGAACTCCCCAGGTCTCCAGACCAAGGAGCCC
AGCAGCAGCTTGCACCTGGAAGGGTGGATGAAGGTGCCCAGGAATAACAAACGAGGACAG
CAAGGCTGGGACAGGAAGTACATTGTCCTGGAGGGATCAAAAGTCCTCATTTATGACAAT
GAAGCCAGAGAAGCTGGACAGAGGCCGGTGGAAGAATTTGAGCTGTGCCTTCCCGACGGG
GATGTATCTATTCATGGTGCCGTTGGTGCTTCCGAACTCGCAAATACAGCCAAAGCAGAT
GTCCCATACATACTGAAGATGGAATCTCACCCGCACACCACCTGCTGGCCCGGGAGAACC
CTCTACTTGCTAGCTCCCAGCTTCCCTGACAAACAGCGCTGGGTCACCGCCTTAGAATCA
GTTGTCGCAGGTGGGAGAGTTTCTAGGGAAAAAGCAGAAGCTGATGCTAAACTGCTTGGA
AACTCCCTGCTGAAACTGGAAGGTGATGACCGTCTAGACATGAACTGCACGCTGCCCTTC
AGTGACCAGGTGGTGTTGGTGGGCACCGAGGAAGGGCTCTACGCCCTGAATGTCTTGAAA
AACTCCCTAACCCATGTCCCAGGAATTGGAGCAGTCTTCCAAATTTATATTATCAAGGAC
CTGGAGAAGCTACTCATGATAGCAGGAGAAGAGCGGGCACTGTGTCTTGTGGACGTGAAG
AAAGTGAAACAGTCCCTGGCCCAGTCCCACCTGCCTGCCCAGCCCGACATCTCACCCAAC
ATTTTTGAAGCTGTCAAGGGCTGCCACTTGTTTGGGGCAGGCAAGATTGAGAACGGGCTC
TGCATCTGTGCAGCCATGCCCAGCAAAGTCGTCATTCTCCGCTACAACGAAAACCTCAGC
AAATACTGCATCCGGAAAGAGATAGAGACCTCAGAGCCCTGCAGCTGTATCCACTTCACC
AATTACAGTATCCTCATTGGAACCAATAAATTCTACGAAATCGACATGAAGCAGTACACG
CTCGAGGAATTCCTGGATAAGAATGACCATTCCTTGGCACCTGCTGTGTTTGCCGCCTCT
TCCAACAGCTTCCCTGTCTCAATCGTGCAGGTGAACAGCGCAGGGCAGCGAGAGGAGTAC
TTGCTGTGTTTCCACGAATTTGGAGTGTTCGTGGATTCTTACGGAAGACGTAGCCGCACA
GACGATCTCAAGTGGAGTCGCTTACCTTTGGCCTTTGCCTACAGAGAACCCTATCTGTTT
GTGACCCACTTCAACTCACTCGAAGTAATTGAGATCCAGGCACGCTCCTCAGCAGGGACC
CCTGCCCGAGCGTACCTGGACATCCCGAACCCGCGCTACCTGGGCCCTGCCATTTCCTCA
GGAGCGATTTACTTGGCGTCCTCATACCAGGATAAATTAAGGGTCATTTGCTGCAAGGGA
AACCTCGTGAAGGAGTCCGGCACTGAACACCACCGGGGCCCGTCCACCTCCCGCAGCAGC
CCCAACAAGCGAGGCCCACCCACGTACAACGAGCACATCACCAAGCGCGTGGCCTCCAGC
CCAGCGCCGCCCGAAGGCCCCAGCCACCCGCGAGAGCCAAGCACACCCCACCGCTACCGC
GAGGGGCGGACCGAGCTGCGCAGGGACAAGTCTCCTGGCCGCCCCCTGGAGCGAGAGAAG
TCCCCCGGCCGGATGCTCAGCACGCGGAGAGAGCGGTCCCCCGGGAGGCTGTTTGAAGAC
AGCAGCAGGGGCCGGCTGCCTGCGGGAGCCGTGAGGACCCCGCTGTCCCAGGTGAACAAG
GTCTGGGACCAGTCTTCAGTATAA
Enzyme 64 GenBank Gene ID NM_007174.1 Link Image
Enzyme 64 GeneCard ID CIT Link Image
Enzyme 64 GenAtlas ID CIT Link Image
Enzyme 64 HGNC ID HGNC:1985 Link Image
Enzyme 64 Chromosome Location 1
Enzyme 64 Locus 12q24
Enzyme 64 SNPs SNPJam Report Link Image
Enzyme 64 General References
  1. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Feb 26;6(1):63-70. [PubMed Link Image]
  2. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  3. Gruneberg U, Neef R, Li X, Chan EH, Chalamalasetty RB, Nigg EA, Barr FA: KIF14 and citron kinase act together to promote efficient cytokinesis. J Cell Biol. 2006 Jan 30;172(3):363-72. Epub 2006 Jan 23. [PubMed Link Image]
  4. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  5. Nousiainen M, Sillje HH, Sauer G, Nigg EA, Korner R: Phosphoproteome analysis of the human mitotic spindle. Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5391-6. Epub 2006 Mar 24. [PubMed Link Image]
  6. Berto G, Camera P, Fusco C, Imarisio S, Ambrogio C, Chiarle R, Silengo L, Di Cunto F: The Down syndrome critical region protein TTC3 inhibits neuronal differentiation via RhoA and Citron kinase. J Cell Sci. 2007 Jun 1;120(Pt 11):1859-67. Epub 2007 May 8. [PubMed Link Image]
  7. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  8. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  9. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  10. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  11. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  12. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  13. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 64 Metabolite References Not Available
Enzyme 65 [top]
Enzyme 65 ID 6696
Enzyme 65 Name Serine/threonine-protein kinase PAK 3
Enzyme 65 Synonyms
  1. Beta-PAK
  2. Oligophrenin-3
  3. p21-activated kinase 3
  4. PAK-3
Enzyme 65 Gene Name PAK3
Enzyme 65 Protein Sequence >Serine/threonine-protein kinase PAK 3
MSDGLDNEEKPPAPPLRMNSNNRDSSALNHSSKPLPMAPEEKNKKARLRSIFPGGGDKTN
KKKEKERPEISLPSDFEHTIHVGFDAVTGEFTPDLYGSQMCPGKLPEGIPEQWARLLQTS
NITKLEQKKNPQAVLDVLKFYDSKETVNNQKYMSFTSGDKSAHGYIAAHPSSTKTASEPP
LAPPVSEEEDEEEEEEEDENEPPPVIAPRPEHTKSIYTRSVVESIASPAVPNKEVTPPSA
ENANSSTLYRNTDRQRKKSKMTDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTA
LDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL
AGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTD
FGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNE
NPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPL
SSLTPLIIAAKEAIKNSSR
Enzyme 65 Number of Residues 559
Enzyme 65 Molecular Weight 62309.1
Enzyme 65 Theoretical pI 5.12
Enzyme 65 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
Enzyme 65 General Function Involved in protein kinase activity
Enzyme 65 Specific Function Key regulator of synapse formation and plasticity in the hippocampus
Enzyme 65 Pathways Not Available
Enzyme 65 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 65 Pfam Domain Function
Enzyme 65 Signals
  • None
Enzyme 65 Transmembrane Regions
  • None
Enzyme 65 Essentiality Not Available
Enzyme 65 GenBank ID Protein 189491759 Link Image
Enzyme 65 UniProtKB/Swiss-Prot ID O75914 Link Image
Enzyme 65 UniProtKB/Swiss-Prot Entry Name PAK3_HUMAN Link Image
Enzyme 65 PDB ID 1F3M Link Image
Enzyme 65 PDB File Show
Enzyme 65 3D Structure
Enzyme 65 Cellular Location Not Available
Enzyme 65 Gene Sequence >1680 bp
ATGTCTGACGGTCTGGATAATGAAGAGAAACCCCCGGCTCCTCCACTGAGGATGAATAGT
AACAACCGGGATTCTTCAGCACTCAACCACAGCTCCAAACCACTTCCCATGGCCCCTGAA
GAGAAGAATAAGAAAGCCAGGCTTCGCTCTATCTTCCCAGGAGGAGGGGATAAAACCAAT
AAGAAGAAGGAGAAAGAGCGCCCAGAGATCTCTCTTCCTTCAGACTTTGAGCATACGATT
CATGTGGGGTTTGATGCAGTCACCGGGGAATTCACTCCAGATCTCTATGGCTCACAGATG
TGCCCAGGGAAGCTCCCAGAGGGAATTCCAGAGCAATGGGCACGATTACTCCAAACTTCC
AACATAACAAAATTGGAACAGAAGAAGAACCCACAAGCTGTTCTAGATGTTCTCAAATTC
TATGATTCCAAAGAAACAGTCAACAACCAGAAATACATGAGCTTTACATCAGGAGATAAA
AGTGCACATGGATACATAGCAGCCCATCCTTCGAGTACAAAAACAGCATCTGAGCCTCCA
TTGGCCCCTCCTGTGTCTGAAGAAGAAGATGAAGAGGAAGAAGAAGAAGAAGATGAAAAT
GAGCCACCACCAGTTATCGCACCAAGACCAGAGCATACAAAATCAATCTATACTCGTTCT
GTGGTTGAATCCATTGCTTCACCAGCAGTACCAAATAAAGAGGTCACACCACCCTCTGCT
GAAAATGCCAATTCCAGTACTTTGTACAGGAACACAGATCGGCAAAGAAAAAAATCCAAG
ATGACAGATGAGGAGATCTTAGAGAAGCTAAGAAGCATTGTGAGTGTTGGGGACCCAAAG
AAAAAATACACAAGATTTGAAAAAATTGGTCAAGGGGCATCAGGTACTGTTTATACAGCA
CTAGACATTGCAACAGGACAAGAGGTGGCCATAAAGCAGATGAACCTTCAACAGCAACCC
AAGAAGGAATTAATTATTAATGAAATTCTGGTCATGAGGGAAAATAAGAACCCTAATATT
GTTAATTATTTAGATAGCTACTTGGTGGGTGATGAACTATGGGTAGTCATGGAATACTTG
GCTGGTGGCTCTCTGACTGATGTGGTCACAGAGACCTGTATGGATGAAGGACAGATAGCA
GCTGTCTGCAGAGAGTGCCTGCAAGCTTTGGATTTCCTGCACTCAAACCAGGTGATCCAT
AGAGATATAAAGAGTGACAATATTCTTCTCGGGATGGATGGCTCTGTTAAATTGACTGAC
TTTGGGTTCTGTGCCCAGATCACTCCTGAGCAAAGTAAACGAAGCACTATGGTGGGAACC
CCATATTGGATGGCACCTGAGGTGGTGACTCGAAAAGCTTATGGTCCGAAAGTTGATATC
TGGTCTCTTGGAATTATGGCAATTGAAATGGTGGAAGGTGAACCCCCTTACCTTAATGAA
AATCCACTCAGGGCATTGTATCTGATAGCCACTAATGGAACTCCAGAGCTCCAGAATCCT
GAGAGACTGTCAGCTGTATTCCGTGACTTTTTAAATCGCTGTCTTGAGATGGATGTGGAT
AGGCGAGGATCTGCCAAGGAGCTTTTGCAGCATCCATTTTTAAAATTAGCCAAGCCTCTC
TCCAGCCTGACTCCTCTGATTATCGCTGCAAAGGAAGCAATTAAGAACAGCAGCCGCTAA
Enzyme 65 GenBank Gene ID NM_001128173.1 Link Image
Enzyme 65 GeneCard ID PAK3 Link Image
Enzyme 65 GenAtlas ID PAK3 Link Image
Enzyme 65 HGNC ID HGNC:8592 Link Image
Enzyme 65 Chromosome Location Not Available
Enzyme 65 Locus Not Available
Enzyme 65 SNPs SNPJam Report Link Image
Enzyme 65 General References
  1. Allen KM, Gleeson JG, Bagrodia S, Partington MW, MacMillan JC, Cerione RA, Mulley JC, Walsh CA: PAK3 mutation in nonsyndromic X-linked mental retardation. Nat Genet. 1998 Sep;20(1):25-30. [PubMed Link Image]
  2. 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]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  6. Bienvenu T, des Portes V, McDonell N, Carrie A, Zemni R, Couvert P, Ropers HH, Moraine C, van Bokhoven H, Fryns JP, Allen K, Walsh CA, Boue J, Kahn A, Chelly J, Beldjord C: Missense mutation in PAK3, R67C, causes X-linked nonspecific mental retardation. Am J Med Genet. 2000 Aug 14;93(4):294-8. [PubMed Link Image]
  7. Gedeon AK, Nelson J, Gecz J, Mulley JC: X-linked mild non-syndromic mental retardation with neuropsychiatric problems and the missense mutation A365E in PAK3. Am J Med Genet A. 2003 Aug 1;120A(4):509-17. [PubMed Link Image]
  8. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 65 Metabolite References Not Available
Enzyme 66 [top]
Enzyme 66 ID 6751
Enzyme 66 Name Rho-associated protein kinase 1
Enzyme 66 Synonyms
  1. Renal carcinoma antigen NY-REN-35
  2. Rho-associated, coiled-coil-containing protein kinase 1
  3. p160 ROCK-1
  4. p160ROCK
Enzyme 66 Gene Name ROCK1
Enzyme 66 Protein Sequence >Rho-associated protein kinase 1
MSTGDSFETRFEKMDNLLRDPKSEVNSDCLLDGLDALVYDLDFPALRKNKNIDNFLSRYK
DTINKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAF
FWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTA
EVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDY
ISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFP
DDNDISKEAKNLICAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLS
SDIDTSNFDDLEEDKGEEETFPIPKAFVGNQLPFVGFTYYSNRRYLSSANPNDNRTSSNA
DKSLQESLQKTIYKLEEQLHNEMQLKDEMEQKCRTSNIKLDKIMKELDEEGNQRRNLEST
VSQIEKEKMLLQHRINEYQRKAEQENEKRRNVENEVSTLKDQLEDLKKVSQNSQLANEKL
SQLQKQLEEANDLLRTESDTAVRLRKSHTEMSKSISQLESLNRELQERNRILENSKSQTD
KDYYQLQAILEAERRDRGHDSEMIGDLQARITSLQEEVKHLKHNLEKVEGERKEAQDMLN
HSEKEKNNLEIDLNYKLKSLQQRLEQEVNEHKVTKARLTDKHQSIEEAKSVAMCEMEKKL
KEEREAREKAENRVVQIEKQCSMLDVDLKQSQQKLEHLTGNKERMEDEVKNLTLQLEQES
NKRLLLQNELKTQAFEADNLKGLEKQMKQEINTLLEAKRLLEFELAQLTKQYRGNEGQMR
ELQDQLEAEQYFSTLYKTQVKELKEEIEEKNRENLKKIQELQNEKETLATQLDLAETKAE
SEQLARGLLEEQYFELTQESKKAASRNRQEITDKDHTVSRLEEANSMLTKDIEILRRENE
ELTEKMKKAEEEYKLEKEEEISNLKAAFEKNINTERTLKTQAVNKLAEIMNRKDFKIDRK
KANTQDLRKKEKENRKLQLELNQEREKFNQMVVKHQKELNDMQAQLVEECAHRNELQMQL
ASKESDIEQLRAKLLDLSDSTSVASFPSADETDGNLPESRIEGWLSVPNRGNIKRYGWKK
QYVVVSSKKILFYNDEQDKEQSNPSMVLDIDKLFHVRPVTQGDVYRAETEEIPKIFQILY
ANEGECRKDVEMEPVQQAEKTNFQNHKGHEFIPTLYHFPANCDACAKPLWHVFKPPPALE
CRRCHVKCHRDHLDKKEDLICPCKVSYDVTSARDMLLLACSQDEQKKWVTHLVKKIPKNP
PSGFVRASPRTLSTRSTANQSFRKVVKNTSGKTS
Enzyme 66 Number of Residues 1354
Enzyme 66 Molecular Weight 158173.5
Enzyme 66 Theoretical pI 5.67
Enzyme 66 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biological regulation
  • cell division
  • cellular metabolic process
  • cellular process
  • cytokinesis
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
  • cell part
  • intracellular
Enzyme 66 General Function Involved in protein serine/threonine kinase activity
Enzyme 66 Specific Function Phosphorylates and activates DAPK3, which then regulates myosin light chain phosphatase through phosphorylation of MYPT1 thereby regulating the assembly of the actin cytoskeleton, cell migration, invasiveness of tumor cells, smooth muscle contraction and neurite outgrowth. Required for centromere positioning and centromere-dependent exit from mitosis. Necessary for apoptotic membrane blebbing
Enzyme 66 Pathways Not Available
Enzyme 66 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 66 Pfam Domain Function
Enzyme 66 Signals
  • None
Enzyme 66 Transmembrane Regions
  • None
Enzyme 66 Essentiality Not Available
Enzyme 66 GenBank ID Protein Not Available
Enzyme 66 UniProtKB/Swiss-Prot ID Q13464 Link Image
Enzyme 66 UniProtKB/Swiss-Prot Entry Name ROCK1_HUMAN Link Image
Enzyme 66 PDB ID Not Available
Enzyme 66 Cellular Location Not Available
Enzyme 66 Gene Sequence >4065 bp
ATGTCGACTGGGGACAGTTTTGAGACTCGATTTGAAAAAATGGACAACCTGCTGCGGGAT
CCCAAATCGGAAGTGAATTCGGATTGTTTGCTGGATGGATTGGATGCTTTGGTATATGAT
TTGGATTTTCCTGCCTTAAGAAAAAACAAAAATATTGACAACTTTTTAAGCAGATATAAA
GACACAATAAATAAAATCAGAGATTTACGAATGAAAGCTGAAGATTATGAAGTAGTGAAG
GTGATTGGTAGAGGTGCATTTGGAGAAGTTCAATTGGTAAGGCATAAATCCACCAGGAAG
GTATATGCTATGAAGCTTCTCAGCAAATTTGAAATGATAAAGAGATCTGATTCTGCTTTT
TTCTGGGAAGAAAGGGACATCATGGCTTTTGCCAACAGTCCTTGGGTTGTTCAGCTTTTT
TATGCATTCCAAGATGATCGTTATCTCTACATGGTGATGGAATACATGCCTGGTGGAGAT
CTTGTAAACTTAATGAGCAACTATGATGTGCCTGAAAAATGGGCACGATTCTATACTGCA
GAAGTAGTTCTTGCATTGGATGCAATCCATTCCATGGGTTTTATTCACAGAGATGTGAAG
CCTGATAACATGCTGCTGGATAAATCTGGACATTTGAAGTTAGCAGATTTTGGTACTTGT
ATGAAGATGAATAAGGAAGGCATGGTACGATGTGATACAGCGGTTGGAACACCTGATTAT
ATTTCCCCTGAAGTATTAAAATCCCAAGGTGGTGATGGTTATTATGGAAGAGAATGTGAC
TGGTGGTCGGTTGGGGTATTTTTATACGAAATGCTTGTAGGTGATACACCTTTTTATGCA
GATTCTTTGGTTGGAACTTACAGTAAAATTATGAACCATAAAAATTCACTTACCTTTCCT
GATGATAATGACATATCAAAAGAAGCAAAAAACCTTATTTGTGCCTTCCTTACTGACAGG
GAAGTGAGGTTAGGGCGAAATGGTGTAGAAGAAATCAAACGACATCTCTTCTTCAAAAAT
GACCAGTGGGCTTGGGAAACGCTCCGAGACACTGTAGCACCAGTTGTACCCGATTTAAGT
AGTGACATTGATACTAGTAATTTTGATGACTTGGAAGAAGATAAAGGAGAGGAAGAAACA
TTCCCTATTCCTAAAGCTTTCGTTGGCAATCAACTACCTTTTGTAGGATTTACATATTAT
AGCAATCGTAGATACTTATCTTCAGCAAATCCTAATGATAACAGAACTAGCTCCAATGCA
GATAAAAGCTTGCAGGAAAGTTTGCAAAAAACAATCTATAAGCTGGAAGAACAGCTGCAT
AATGAAATGCAGTTAAAAGATGAAATGGAGCAGAAGTGCAGAACCTCAAACATAAAACTA
GACAAGATAATGAAAGAATTGGATGAAGAGGGAAATCAAAGAAGAAATCTAGAATCTACA
GTGTCTCAGATTGAGAAGGAGAAAATGTTGCTACAGCATAGAATTAATGAGTACCAAAGA
AAAGCTGAACAGGAAAATGAGAAGAGAAGAAATGTAGAAAATGAAGTTTCTACATTAAAG
GATCAGTTGGAAGACTTAAAGAAAGTCAGTCAGAATTCACAGCTTGCTAATGAGAAGCTG
TCCCAGTTACAAAAGCAGCTAGAAGAAGCCAATGACTTACTTAGGACAGAATCGGACACA
GCTGTAAGATTGAGGAAGAGTCACACAGAGATGAGCAAGTCAATTAGTCAGTTAGAGTCC
CTGAACAGAGAGTTGCAAGAGAGAAATCGAATTTTAGAGAATTCTAAGTCACAAACAGAC
AAAGATTATTACCAGCTGCAAGCTATATTAGAAGCTGAACGAAGAGACAGAGGTCATGAT
TCTGAGATGATTGGAGACCTTCAAGCTCGAATTACATCTTTACAAGAGGAGGTGAAGCAT
CTCAAACATAATCTCGAAAAAGTGGAAGGAGAAAGAAAAGAGGCTCAAGACATGCTTAAT
CACTCAGAAAAGGAAAAGAATAATTTAGAGATAGATTTAAACTACAAACTTAAATCATTA
CAACAACGGTTAGAACAAGAGGTAAATGAACACAAAGTAACCAAAGCTCGTTTAACTGAC
AAACATCAATCTATTGAAGAGGCAAAGTCTGTGGCAATGTGTGAGATGGAAAAAAAGCTG
AAAGAAGAAAGAGAAGCTCGAGAGAAGGCTGAAAATCGGGTTGTTCAGATTGAGAAACAG
TGTTCCATGCTAGACGTTGATCTGAAGCAATCTCAGCAGAAACTAGAACATTTGACTGGA
AATAAAGAAAGGATGGAGGATGAAGTTAAGAATCTAACCCTGCAACTGGAGCAGGAATCA
AATAAGCGGCTGTTGTTACAAAATGAATTGAAGACTCAAGCATTTGAGGCAGACAATTTA
AAAGGTTTAGAAAAGCAGATGAAACAGGAAATAAATACTTTATTGGAAGCAAAGAGATTA
TTAGAATTTGAGTTAGCTCAGCTTACGAAACAGTATAGAGGAAATGAAGGACAGATGCGG
GAGCTACAAGATCAGCTTGAAGCTGAGCAATATTTCTCGACACTTTATAAAACCCAGGTA
AAGGAACTTAAAGAAGAAATTGAAGAAAAAAACAGAGAAAATTTAAAGAAAATACAGGAA
CTACAAAATGAAAAAGAAACTCTTGCTACTCAGTTGGATCTAGCAGAAACAAAAGCTGAG
TCTGAGCAGTTGGCGCGAGGCCTTCTGGAAGAACAGTATTTTGAATTGACGCAAGAAAGC
AAGAAAGCTGCTTCAAGAAATAGACAAGAGATTACAGATAAAGATCACACTGTTAGTCGG
CTTGAAGAAGCAAACAGCATGCTAACCAAAGATATTGAAATATTAAGAAGAGAGAATGAA
GAGCTAACAGAGAAAATGAAGAAGGCAGAGGAAGAATATAAACTGGAGAAGGAGGAGGAG
ATCAGTAATCTTAAGGCTGCCTTTGAAAAGAATATCAACACTGAACGAACCCTTAAAACA
CAGGCTGTTAACAAATTGGCAGAAATAATGAATCGAAAAGATTTTAAAATTGATAGAAAG
AAAGCTAATACACAAGATTTGAGAAAGAAAGAAAAGGAAAATCGAAAGCTGCAACTGGAA
CTCAACCAAGAAAGAGAGAAATTCAACCAGATGGTAGTGAAACATCAGAAGGAACTGAAT
GACATGCAAGCGCAATTGGTAGAAGAATGTGCACATAGGAATGAGCTTCAGATGCAGTTG
GCCAGCAAAGAGAGTGATATTGAGCAATTGCGTGCTAAACTTTTGGACCTCTCGGATTCT
ACAAGTGTTGCTAGTTTTCCTAGTGCTGATGAAACTGATGGTAACCTCCCAGAGTCAAGA
ATTGAAGGTTGGCTTTCAGTACCAAATAGAGGAAATATCAAACGATATGGCTGGAAGAAA
CAGTATGTTGTGGTAAGCAGCAAAAAAATTTTGTTCTATAATGACGAACAAGATAAGGAG
CAATCCAATCCATCTATGGTATTGGACATAGATAAACTGTTTCACGTTAGACCTGTAACC
CAAGGAGATGTGTATAGAGCTGAAACTGAAGAAATTCCTAAAATATTCCAGATACTATAT
GCAAATGAAGGTGAATGTAGAAAAGATGTAGAGATGGAACCAGTACAACAAGCTGAAAAA
ACTAATTTCCAAAATCACAAAGGCCATGAGTTTATTCCTACACTCTACCACTTTCCTGCC
AATTGTGATGCCTGTGCCAAACCTCTCTGGCATGTTTTTAAGCCACCCCCTGCCCTAGAG
TGTCGAAGATGCCATGTTAAGTGCCACAGAGATCACTTAGATAAGAAAGAGGACTTAATT
TGTCCATGTAAAGTAAGTTATGATGTAACATCAGCAAGAGATATGCTGCTGTTAGCATGT
TCTCAGGATGAACAAAAAAAATGGGTAACTCATTTAGTAAAGAAAATCCCTAAGAATCCA
CCATCTGGTTTTGTTCGTGCTTCCCCTCGAACGCTTTCTACAAGATCCACTGCAAATCAG
TCTTTCCGGAAAGTGGTCAAAAATACATCTGGAAAAACTAGTTAA
Enzyme 66 GenBank Gene ID U43195 Link Image
Enzyme 66 GeneCard ID ROCK1 Link Image
Enzyme 66 GenAtlas ID ROCK1 Link Image
Enzyme 66 HGNC ID HGNC:10251 Link Image
Enzyme 66 Chromosome Location 1
Enzyme 66 Locus 18q11.1
Enzyme 66 SNPs SNPJam Report Link Image
Enzyme 66 General References
  1. Ishizaki T, Maekawa M, Fujisawa K, Okawa K, Iwamatsu A, Fujita A, Watanabe N, Saito Y, Kakizuka A, Morii N, Narumiya S: The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase. EMBO J. 1996 Apr 15;15(8):1885-93. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Van Eyk JE, Arrell DK, Foster DB, Strauss JD, Heinonen TY, Furmaniak-Kazmierczak E, Cote GP, Mak AS: Different molecular mechanisms for Rho family GTPase-dependent, Ca2+-independent contraction of smooth muscle. J Biol Chem. 1998 Sep 4;273(36):23433-9. [PubMed Link Image]
  4. Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed Link Image]
  5. Kawano Y, Fukata Y, Oshiro N, Amano M, Nakamura T, Ito M, Matsumura F, Inagaki M, Kaibuchi K: Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by Rho-kinase in vivo. J Cell Biol. 1999 Nov 29;147(5):1023-38. [PubMed Link Image]
  6. Maekawa M, Ishizaki T, Boku S, Watanabe N, Fujita A, Iwamatsu A, Obinata T, Ohashi K, Mizuno K, Narumiya S: Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Science. 1999 Aug 6;285(5429):895-8. [PubMed Link Image]
  7. Sumi T, Matsumoto K, Nakamura T: Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase. J Biol Chem. 2001 Jan 5;276(1):670-6. [PubMed Link Image]
  8. Sebbagh M, Renvoize C, Hamelin J, Riche N, Bertoglio J, Breard J: Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing. Nat Cell Biol. 2001 Apr;3(4):346-52. [PubMed Link Image]
  9. Riento K, Guasch RM, Garg R, Jin B, Ridley AJ: RhoE binds to ROCK I and inhibits downstream signaling. Mol Cell Biol. 2003 Jun;23(12):4219-29. [PubMed Link Image]
  10. Riento K, Ridley AJ: Rocks: multifunctional kinases in cell behaviour. Nat Rev Mol Cell Biol. 2003 Jun;4(6):446-56. [PubMed Link Image]
  11. Morita E, Sandrin V, Chung HY, Morham SG, Gygi SP, Rodesch CK, Sundquist WI: Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis. EMBO J. 2007 Oct 3;26(19):4215-27. Epub 2007 Sep 13. [PubMed Link Image]
  12. Hagerty L, Weitzel DH, Chambers J, Fortner CN, Brush MH, Loiselle D, Hosoya H, Haystead TA: ROCK1 phosphorylates and activates zipper-interacting protein kinase. J Biol Chem. 2007 Feb 16;282(7):4884-93. Epub 2006 Dec 8. [PubMed Link Image]
  13. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  14. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  15. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  16. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  17. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  18. Dvorsky R, Blumenstein L, Vetter IR, Ahmadian MR: Structural insights into the interaction of ROCKI with the switch regions of RhoA. J Biol Chem. 2004 Feb 20;279(8):7098-104. Epub 2003 Dec 2. [PubMed Link Image]
  19. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 66 Metabolite References Not Available
Enzyme 67 [top]
Enzyme 67 ID 6753
Enzyme 67 Name Serine/threonine-protein kinase PAK 2
Enzyme 67 Synonyms
  1. Gamma-PAK
  2. PAK65
  3. S6/H4 kinase
  4. p21-activated kinase 2
  5. PAK-2
  6. p58
  7. PAK-2p27
  8. p27
  9. PAK-2p34
  10. p34
  11. C-t-PAK2
Enzyme 67 Gene Name PAK2
Enzyme 67 Protein Sequence >Serine/threonine-protein kinase PAK 2
MSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSLKPLPSVPEEKKPRHKIISIFSGT
EKGSKKKEKERPEISPPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNP
QAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGTPALNAKGTEAPAVVTEEEDDDEETAP
PVIAPRPDHTKSIYTRSVIDPVPAPVGDSHVDGAAKSLDKQKKKTKMTDEEIMEKLRTIV
SIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKE
LKNPNIVNFLDSYLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLH
ANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAY
GPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRC
LEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLIMAAKEAMKSNR
Enzyme 67 Number of Residues 524
Enzyme 67 Molecular Weight 58042.1
Enzyme 67 Theoretical pI 5.76
Enzyme 67 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
Enzyme 67 General Function Involved in protein kinase activity
Enzyme 67 Specific Function The activated kinase acts on a variety of targets. Phosphorylates ribosomal protein S6, histone H4 and myelin basic protein. Full length PAK 2 stimulates cell survival and cell growth. The process is, at least in part, mediated by phosphorylation and inhibition of pro-apoptotic BAD. Caspase- activated PAK-2p34 is involved in cell death response, probably involving the JNK signaling pathway. Cleaved PAK-2p34 seems to have a higher activity than the CDC42-activated form
Enzyme 67 Pathways Not Available
Enzyme 67 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 67 Pfam Domain Function
Enzyme 67 Signals
  • None
Enzyme 67 Transmembrane Regions
  • None
Enzyme 67 Essentiality Not Available
Enzyme 67 GenBank ID Protein 47482156 Link Image
Enzyme 67 UniProtKB/Swiss-Prot ID Q13177 Link Image
Enzyme 67 UniProtKB/Swiss-Prot Entry Name PAK2_HUMAN Link Image
Enzyme 67 PDB ID 1F3M Link Image
Enzyme 67 PDB File Show
Enzyme 67 3D Structure
Enzyme 67 Cellular Location Not Available
Enzyme 67 Gene Sequence >1575 bp
ATGTCTGATAACGGAGAACTGGAAGATAAGCCTCCAGCACCTCCTGTGCGAATGAGCAGC
ACCATCTTTAGCACTGGAGGCAAAGACCCTTTGTCAGCCAATCACAGTTTGAAACCTTTG
CCCTCTGTTCCAGAAGAGAAAAAGCCCAGGCATAAAATCATCTCCATATTCTCAGGCACA
GAGAAAGGAAGTAAAAAGAAGGAAAAGGAACGGCCAGAAATTTCTCCTCCATCTGATTTT
GAGCACACCATCCATGTTGGTTTTGATGCTGTTACTGGAGAATTCACTGGCATGCCAGAA
CAGTGGGCTCGATTACTACAGACCTCCAATATCACCAAACTAGAGCAAAAGAAGAACCCT
CAGGCTGTGCTGGATGTCCTAAAGTTCTACGACTCCAACACAGTGAAGCAGAAATATCTG
AGCTTTACTCCTCCTGAGAAAGATGGCTTTCCTTCTGGAACACCAGCACTGAATGCCAAG
GGAACAGAAGCACCCGCAGTAGTGACAGAGGAGGAGGATGATGATGAAGAGACTGCTCCT
CCCGTTATTGCCCCGCGACCGGATCATACGAAATCAATTTACACACGGTCTGTAATTGAC
CCTGTTCCTGCACCAGTTGGTGATTCACATGTTGATGGTGCTGCCAAGTCTTTAGACAAA
CAGAAAAAGAAGACTAAGATGACAGATGAAGAGATTATGGAGAAATTAAGAACTATCGTG
AGCATAGGTGACCCTAAGAAAAAATATACAAGATATGAAAAAATTGGACAAAGGGCTTCT
GGTACAGTTTTCACTGCTACTGACGTTGCACTGGGACAGGAGGTTGCTATCAAACAAATT
AATTTACAGAAACAGCCAAAGAAGGAACTGATCATTAACGAGATTCTGGTGATGAAAGAA
TTGAAAAATCCCAACATCGTTAACTTTTTGGACAGTTACCTGGTAGGAGATGAATTGTTT
GTGGTCATGGAATACCTTGCTGGGGGGTCACTCACTGATGTGGTAACAGAAACGTGCATG
GATGAAGCACAGATTGCTGCTGTATGCAGAGAGTGTTTACAGGCATTGGAGTTTTTACAT
GCTAATCAAGTGATCCACAGAGACATCAAAAGTGACAATGTACTTTTGGGAATGGAAGGA
TCTGTTAAGCTCACTGACTTTGGTTTCTGTGCCCAGATCACCCCTGAGCAGAGCAAACGC
AGTACCATGGTCGGAACGCCATACTGGATGGCACCAGAGGTGGTTACACGGAAAGCTTAT
GGCCCTAAAGTCGACATATGGTCTCTGGGTATCATGGCTATTGAGATGGTAGAAGGAGAG
CCTCCATACCTCAATGAAAATCCCTTGAGGGCCTTGTACCTAATAGCAACTAATGGAACC
CCAGAACTTCAGAATCCAGAGAAACTTTCCCCAATATTTCGGGATTTCTTAAATCGATGT
TTGGAAATGGATGTGGAAAAAAGGGGTTCAGCCAAAGAATTATTACAGCATCCTTTCCTG
AAACTGGCCAAACCGTTATCTAGCTTGACACCACTGATCATGGCAGCTAAAGAAGCAATG
AAGAGTAACCGTTAA
Enzyme 67 GenBank Gene ID BC069613 Link Image
Enzyme 67 GeneCard ID PAK2 Link Image
Enzyme 67 GenAtlas ID PAK2 Link Image
Enzyme 67 HGNC ID HGNC:8591 Link Image
Enzyme 67 Chromosome Location 3
Enzyme 67 Locus 3q29
Enzyme 67 SNPs SNPJam Report Link Image
Enzyme 67 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  2. Martin GA, Bollag G, McCormick F, Abo A: A novel serine kinase activated by rac1/CDC42Hs-dependent autophosphorylation is related to PAK65 and STE20. EMBO J. 1995 May 1;14(9):1970-8. [PubMed Link Image]
  3. Martin GA, Bollag G, McCormick F, Abo A: A novel serine kinase activated by rac1/CDC42Hs-dependent autophosphorylation is related to PAK65 and STE20. EMBO J. 1995 Sep 1;14(17):4385. [PubMed Link Image]
  4. Benner GE, Dennis PB, Masaracchia RA: Activation of an S6/H4 kinase (PAK 65) from human placenta by intramolecular and intermolecular autophosphorylation. J Biol Chem. 1995 Sep 8;270(36):21121-8. [PubMed Link Image]
  5. Rudel T, Bokoch GM: Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2. Science. 1997 Jun 6;276(5318):1571-4. [PubMed Link Image]
  6. Walter BN, Huang Z, Jakobi R, Tuazon PT, Alnemri ES, Litwack G, Traugh JA: Cleavage and activation of p21-activated protein kinase gamma-PAK by CPP32 (caspase 3). Effects of autophosphorylation on activity. J Biol Chem. 1998 Oct 30;273(44):28733-9. [PubMed Link Image]
  7. Arora VK, Molina RP, Foster JL, Blakemore JL, Chernoff J, Fredericksen BL, Garcia JV: Lentivirus Nef specifically activates Pak2. J Virol. 2000 Dec;74(23):11081-7. [PubMed Link Image]
  8. Jakobi R, McCarthy CC, Koeppel MA, Stringer DK: Caspase-activated PAK-2 is regulated by subcellular targeting and proteasomal degradation. J Biol Chem. 2003 Oct 3;278(40):38675-85. Epub 2003 Jul 9. [PubMed Link Image]
  9. Koeppel MA, McCarthy CC, Moertl E, Jakobi R: Identification and characterization of PS-GAP as a novel regulator of caspase-activated PAK-2. J Biol Chem. 2004 Dec 17;279(51):53653-64. Epub 2004 Oct 7. [PubMed Link Image]
  10. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  11. Karkkainen S, Hiipakka M, Wang JH, Kleino I, Vaha-Jaakkola M, Renkema GH, Liss M, Wagner R, Saksela K: Identification of preferred protein interactions by phage-display of the human Src homology-3 proteome. EMBO Rep. 2006 Feb;7(2):186-91. [PubMed Link Image]
  12. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  13. Vilas GL, Corvi MM, Plummer GJ, Seime AM, Lambkin GR, Berthiaume LG: Posttranslational myristoylation of caspase-activated p21-activated protein kinase 2 (PAK2) potentiates late apoptotic events. Proc Natl Acad Sci U S A. 2006 Apr 25;103(17):6542-7. Epub 2006 Apr 14. [PubMed Link Image]
  14. Nola S, Sebbagh M, Marchetto S, Osmani N, Nourry C, Audebert S, Navarro C, Rachel R, Montcouquiol M, Sans N, Etienne-Manneville S, Borg JP, Santoni MJ: Scrib regulates PAK activity during the cell migration process. Hum Mol Genet. 2008 Nov 15;17(22):3552-65. Epub 2008 Aug 20. [PubMed Link Image]
  15. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  16. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  17. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  18. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  19. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 67 Metabolite References Not Available
Enzyme 68 [top]
Enzyme 68 ID 6760
Enzyme 68 Name Ectonucleoside triphosphate diphosphohydrolase 2
Enzyme 68 Synonyms
  1. NTPDase 2
  2. CD39 antigen-like 1
  3. Ecto-ATP diphosphohydrolase 2
  4. Ecto-ATPDase 2
  5. Ecto-ATPase 2
Enzyme 68 Gene Name ENTPD2
Enzyme 68 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 2
MAGKVRSLLPPLLLAAAGLAGLLLLCVPTRDVREPPALKYGIVLDAGSSHTSMFIYKWPA
DKENDTGIVGQHSSCDVPGGGISSYADNPSGASQSLVGCLEQALQDVPKERHAGTPLYLG
ATAGMRLLNLTNPEASTSVLMAVTHTLTQYPFDFRGARILSGQEEGVFGWVTANYLLENF
IKYGWVGRWFRPRKGTLGAMDLGGASTQITFETTSPAEDRASEVQLHLYGQHYRVYTHSF
LCYGRDQVLQRLLASALQTHGFHPCWPRGFSTQVLLGDVYQSPCTMAQRPQNFNSSARVS
LSGSSDPHLCRDLVSGLFSFSSCPFSRCSFNGVFQPPVAGNFVAFSAFFYTVDFLRTSMG
LPVATLQQLEAAAVNVCNQTWAQLQARVPGQRARLADYCAGAMFVQQLLSRGYGFDERAF
GGVIFQKKAADTAVGWALGYMLNLTNLIPADPPGLRKGTDFSSWVVLLLLFASALLAALV
LLLRQVHSAKLPSTI
Enzyme 68 Number of Residues 495
Enzyme 68 Molecular Weight 53665.0
Enzyme 68 Theoretical pI 8.34
Enzyme 68 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 68 General Function Involved in ATP binding
Enzyme 68 Specific Function In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Hydrolyzes ADP only to a marginal extent. The order of activity with different substrates is ATP > GTP > CTP = ITP > UTP >> ADP = UDP
Enzyme 68 Pathways Not Available
Enzyme 68 Reactions Not Available
Enzyme 68 Pfam Domain Function
Enzyme 68 Signals
  • None
Enzyme 68 Transmembrane Regions
  • 8-28 463-483
Enzyme 68 Essentiality Not Available
Enzyme 68 GenBank ID Protein 5114239 Link Image
Enzyme 68 UniProtKB/Swiss-Prot ID Q9Y5L3 Link Image
Enzyme 68 UniProtKB/Swiss-Prot Entry Name ENTP2_HUMAN Link Image
Enzyme 68 PDB ID Not Available
Enzyme 68 Cellular Location Not Available
Enzyme 68 Gene Sequence >1488 bp
ATGGCCGGGAAGGTGCGGTCACTGCTGCCGCCGCTGCTGCTGGCCGCCGCGGGCCTCGCC
GGCCTCCTACTGCTGTGCGTCCCCACCCGCGACGTCCGGGAGCCGCCCGCCCTCAAGTAT
GGCATCGTCCTGGACGCTGGTTCTTCACACACGTCCATGTTTATCTACAAGTGGCCGGCA
GACAAGGAGAACGACACAGGCATTGTGGGCCAGCACAGCTCCTGTGATGTTCCAGGTGGG
GGCATCTCCAGCTATGCAGACAACCCTTCTGGGGCCAGCCAGAGTCTTGTTGGATGCCTC
GAACAGGCGCTTCAGGATGTGCCCAAAGAGAGACACGCGGGCACACCCCTCTACCTGGGA
GCCACAGCGGGTATGCGCCTGCTCAACCTGACCAATCCAGAGGCCTCGACCAGTGTGCTC
ATGGCAGTGACTCACACACTGACCCAGTACCCCTTTGACTTCCGGGGTGCACGCATCCTC
TCGGGCCAGGAAGAGGGGGTGTTTGGCTGGGTGACTGCCAACTACCTGCTGGAGAACTTC
ATCAAGTACGGCTGGGTGGGCCGGTGGTTCCGGCCACGGAAGGGGACACTGGGGGCCATG
GACCTGGGGGGTGCCTCTACCCAGATCACTTTTGAGACAACCAGTCCAGCTGAGGACAGA
GCCAGCGAGGTCCAGCTGCATCTCTACGGCCAGCACTACCGAGTCTACACCCACAGCTTC
CTCTGCTATGGCCGTGACCAGGTCCTCCAGAGGCTGCTGGCCAGCGCCCTCCAGACCCAC
GGCTTCCACCCCTGCTGGCCGAGGGGCTTTTCCACCCAAGTGCTGCTCGGGGATGTGTAC
CAGTCACCATGCACCATGGCCCAGCGGCCCCAGAACTTCAACAGCAGTGCCAGGGTCAGC
CTGTCAGGGAGCAGTGACCCCCACCTCTGCCGAGATCTGGTTTCTGGGCTCTTCAGCTTC
TCCTCCTGCCCCTTCTCCCGATGCTCTTTCAATGGGGTCTTCCAGCCCCCAGTGGCTGGG
AACTTTGTGGCCTTCTCTGCCTTCTTCTACACTGTGGACTTTTTGCGGACTTCGATGGGG
CTGCCCGTGGCCACCCTGCAGCAGCTGGAGGCAGCCGCAGTGAATGTCTGCAACCAGACC
TGGGCTCAGCTGCAAGCTCGGGTGCCAGGGCAACGGGCCCGCCTGGCCGACTACTGCGCC
GGGGCCATGTTCGTGCAGCAGCTGCTGAGTCGCGGCTACGGCTTCGACGAGCGCGCCTTC
GGCGGCGTGATCTTCCAGAAGAAGGCCGCGGACACTGCAGTGGGCTGGGCGCTCGGCTAC
ATGCTGAACCTGACCAACCTGATCCCCGCCGACCCGCCGGGGCTGCGCAAGGGCACAGAC
TTCAGCTCCTGGGTCGTCCTCCTGCTGCTCTTCGCCTCCGCGCTCCTGGCTGCGCTTGTC
CTGCTGCTGCGTCAGGTGCACTCCGCCAAGCTGCCAAGCACCATTTAG
Enzyme 68 GenBank Gene ID AF144748 Link Image
Enzyme 68 GeneCard ID ENTPD2 Link Image
Enzyme 68 GenAtlas ID Not Available
Enzyme 68 HGNC ID Not Available
Enzyme 68 Chromosome Location 9
Enzyme 68 Locus 9q34
Enzyme 68 SNPs SNPJam Report Link Image
Enzyme 68 General References
  1. Chadwick BP, Frischauf AM: Cloning and mapping of a human and mouse gene with homology to ecto-ATPase genes. Mamm Genome. 1997 Sep;8(9):668-72. [PubMed Link Image]
  2. Mateo J, Harden TK, Boyer JL: Functional expression of a cDNA encoding a human ecto-ATPase. Br J Pharmacol. 1999 Sep;128(2):396-402. [PubMed Link Image]
  3. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 68 Metabolite References Not Available
Enzyme 69 [top]
Enzyme 69 ID 6814
Enzyme 69 Name Rho-associated protein kinase 2
Enzyme 69 Synonyms
  1. Rho kinase 2
  2. Rho-associated, coiled-coil-containing protein kinase 2
  3. p164 ROCK-2
Enzyme 69 Gene Name ROCK2
Enzyme 69 Protein Sequence >Rho-associated protein kinase 2
MSRPPPTGKMPGAPETAPGDGAGASRQRKLEALIRDPRSPINVESLLDGLNSLVLDLDFP
ALRKNKNIDNFLNRYEKIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAM
KLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNL
MSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKHGHLKLADFGTCMKMD
ETGMVHCDTAVGTPDYISPEVLKSQGGDGFYGRECDWWSVGVFLYEMLVGDTPFYADSLV
GTYSKIMDHKNSLCFPEDAEISKHAKNLICAFLTDREVRLGRNGVEEIRQHPFFKNDQWH
WDNIRETAAPVVPELSSDIDSSNFDDIEDDKGDVETFPIPKAFVGNQLPFIGFTYYRENL
LLSDSPSCRETDSIQSRKNEESQEIQKKLYTLEEHLSNEMQAKEELEQKCKSVNTRLEKT
AKELEEEITLRKSVESALRQLEREKALLQHKNAEYQRKADHEADKKRNLENDVNSLKDQL
EDLKKRNQNSQISTEKVNQLQRQLDETNALLRTESDTAARLRKTQAESSKQIQQLESNNR
DLQDKNCLLETAKLKLEKEFINLQSALESERRDRTHGSEIINDLQGRICGLEEDLKNGKI
LLAKVELEKRQLQERFTDLEKEKSNMEIDMTYQLKVIQQSLEQEEAEHKATKARLADKNK
IYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLK
QKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMN
LEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQK
KQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQE
LTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQF
EKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQ
MIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHIGLDSSSIGSGPG
DAEADDGFPESRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVL
DIDKLFHVRPVTQTDVYRADAKEIPRIFQILYANEGESKKEQEFPVEPVGEKSNYICHKG
HEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYD
ISTAKNLLLLANSTEEQQKWVSRLVKKIPKKPPAPDPFARSSPRTSMKIQQNQSIRRPSR
QLAPNKPS
Enzyme 69 Number of Residues 1388
Enzyme 69 Molecular Weight 160898.6
Enzyme 69 Theoretical pI 5.84
Enzyme 69 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cell division
  • cellular metabolic process
  • cellular process
  • cytokinesis
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
Enzyme 69 General Function Involved in protein serine/threonine kinase activity
Enzyme 69 Specific Function Regulates the assembly of the actin cytoskeleton. Promotes formation of stress fibers and of focal adhesion complexes. Plays a role in smooth muscle contraction
Enzyme 69 Pathways Not Available
Enzyme 69 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 69 Pfam Domain Function
Enzyme 69 Signals
  • None
Enzyme 69 Transmembrane Regions
  • None
Enzyme 69 Essentiality Not Available
Enzyme 69 GenBank ID Protein 41872583 Link Image
Enzyme 69 UniProtKB/Swiss-Prot ID O75116 Link Image
Enzyme 69 UniProtKB/Swiss-Prot Entry Name ROCK2_HUMAN Link Image
Enzyme 69 PDB ID Not Available
Enzyme 69 Cellular Location Not Available
Enzyme 69 Gene Sequence >4167 bp
ATGAGCCGGCCCCCGCCGACGGGGAAAATGCCCGGCGCCCCCGAGACCGCGCCGGGGGAC
GGGGCAGGCGCGAGCCGCCAGAGGAAGCTGGAGGCGCTGATCCGAGACCCTCGCTCCCCC
ATCAACGTGGAGAGCTTGCTGGATGGCTTAAATTCCTTGGTCCTTGATTTAGATTTTCCT
GCTTTGAGGAAAAACAAGAACATAGATAATTTCTTAAATAGATATGAGAAAATTGTGAAA
AAAATCAGAGGTCTACAGATGAAGGCAGAAGACTATGATGTTGTAAAAGTTATTGGAAGA
GGTGCTTTTGGTGAAGTGCAGTTGGTTCGTCACAAGGCATCGCAGAAGGTTTATGCTATG
AAGCTTCTTAGTAAGTTTGAAATGATAAAAAGATCAGATTCTGCCTTTTTTTGGGAAGAA
AGAGATATTATGGCCTTTGCCAATAGCCCCTGGGTGGTTCAGCTTTTTTATGCCTTTCAA
GATGATAGGTATCTGTACATGGTAATGGAGTACATGCCTGGTGGAGACCTTGTAAACCTT
ATGAGTAATTATGATGTGCCTGAAAAATGGGCCAAATTTTACACTGCTGAAGTTGTTCTT
GCTCTGGATGCAATACACTCCATGGGTTTAATACACAGAGATGTGAAGCCTGACAACATG
CTCTTGGATAAACATGGACATCTAAAATTAGCAGATTTTGGCACGTGTATGAAGATGGAT
GAAACAGGCATGGTACATTGTGATACAGCAGTTGGAACACCGGATTATATATCACCTGAG
GTTCTGAAATCACAAGGGGGTGATGGTTTCTATGGGCGAGAATGTGATTGGTGGTCTGTA
GGTGTTTTCCTTTATGAGATGCTAGTGGGGGATACTCCATTTTATGCGGATTCACTTGTA
GGAACATATAGCAAAATTATGGATCATAAGAATTCACTGTGTTTCCCTGAAGATGCAGAA
ATTTCCAAACATGCAAAGAATCTCATCTGTGCTTTCTTAACAGATAGGGAGGTACGACTT
GGGAGAAATGGGGTGGAAGAAATCAGACAGCATCCTTTCTTTAAGAATGATCAGTGGCAT
TGGGATAACATAAGAGAAACGGCAGCTCCTGTAGTACCTGAACTCAGCAGTGACATAGAC
AGCAGCAATTTCGATGACATTGAAGATGACAAAGGAGATGTAGAAACCTTCCCAATTCCT
AAAGCTTTTGTTGGAAATCAGCTGCCTTTCATCGGATTTACCTACTATAGAGAAAATTTA
TTATTAAGTGACTCTCCATCTTGTAGAGAAACTGATTCCATACAATCAAGGAAAAATGAA
GAAAGTCAAGAGATTCAGAAAAAACTGTATACATTAGAAGAACATCTTAGCAATGAGATG
CAAGCCAAAGAGGAACTGGAACAGAAGTGCAAATCTGTTAATACTCGCCTAGAAAAAACA
GCAAAGGAGCTAGAAGAGGAGATTACCTTACGGAAAAGTGTGGAATCAGCATTAAGACAG
TTAGAAAGAGAAAAGGCGCTTCTTCAGCACAAAAATGCAGAATATCAGAGGAAAGCTGAT
CATGAAGCAGACAAAAAACGAAATTTGGAAAATGATGTTAACAGCTTAAAAGATCAACTT
GAAGATTTGAAAAAAAGAAATCAAAACTCTCAAATATCCACTGAGAAAGTGAATCAACTC
CAGAGACAACTGGATGAAACCAATGCTTTACTGCGAACAGAGTCTGATACTGCAGCCCGG
TTAAGGAAAACCCAGGCAGAAAGTTCAAAACAGATTCAGCAGCTGGAATCTAACAATAGA
GATCTACAAGATAAAAACTGCCTGCTGGAGACTGCCAAGTTAAAACTTGAAAAGGAATTT
ATCAATCTTCAGTCAGCTCTAGAATCTGAAAGGAGGGATCGAACCCATGGATCAGAGATA
ATTAATGATTTACAAGGTAGAATATGTGGCCTAGAAGAAGATTTAAAGAACGGCAAAATC
TTACTAGCGAAAGTAGAACTGGAGAAGAGACAACTTCAGGAGAGATTTACTGATTTGGAA
AAGGAAAAAAGCAACATGGAAATAGATATGACATACCAACTAAAAGTTATACAGCAGAGC
CTAGAACAAGAAGAAGCTGAACATAAGGCCACAAAGGCACGACTAGCAGATAAAAATAAG
ATCTATGAGTCCATCGAAGAAGCCAAATCAGAAGCCATGAAAGAAATGGAGAAGAAGCTC
TTGGAGGAAAGAACTTTAAAACAGAAAGTGGAGAACCTATTGCTAGAAGCTGAGAAAAGA
TGTTCTCTATTAGACTGTGACCTCAAACAGTCACAGCAGAAAATAAATGAGCTCCTTAAA
CAGAAAGATGTGCTAAATGAGGATGTTAGAAACCTGACATTAAAAATAGAGCAAGAAACT
CAGAAGCGCTGCCTTACACAAAATGACCTGAAGATGCAAACACAACAGGTTAACACACTA
AAAATGTCAGAAAAGCAGTTAAAGCAAGAAAATAACCATCTCATGGAAATGAAAATGAAC
TTGGAAAAACAAAATGCTGAACTTCGAAAAGAACGTCAGGATGCAGATGGGCAAATGAAA
GAGCTCCAGGATCAGCTCGAAGCAGAACAGTATTTCTCAACCCTTTATAAAACACAAGTT
AGGGAGCTTAAAGAAGAATGTGAAGAAAAGACCAAACTTGGTAAAGAATTGCAGCAGAAG
AAACAGGAATTACAGGATGAACGGGACTCTTTGGCTGCCCAACTGGAGATCACCTTGACC
AAAGCAGATTCTGAGCAACTGGCTCGTTCAATTGCTGAAGAACAATATTCTGATTTGGAA
AAAGAGAAGATCATGAAAGAGCTGGAGATCAAAGAGATGATGGCTAGACACAAACAGGAA
CTTACGGAAAAAGATGCTACAATTGCTTCTCTTGAGGAAACTAATAGGACACTAACTAGT
GATGTTGCCAATCTTGCAAATGAGAAAGAAGAATTAAATAACAAATTGAAAGATGTTCAA
GAGCAACTGTCAAGATTGAAAGATGAAGAAATAAGCGCAGCAGCTATTAAAGCACAGTTT
GAGAAGCAGCTATTAACAGAAAGAACACTCAAAACTCAAGCTGTGAATAAGTTGGCTGAG
ATCATGAATCGAAAAGAACCTGTCAAGCGTGGTAATGACACAGATGTGCGGAGAAAAGAG
AAGGAGAATAGAAAGCTACATATGGAGCTTAAATCTGAACGTGAGAAATTGACCCAGCAG
ATGATCAAGTATCAGAAAGAACTGAATGAAATGCAGGCACAAATAGCTGAAGAGAGCCAG
ATTCGAATTGAACTGCAGATGACATTGGACAGTAAAGACAGTGACATTGAGCAGCTGCGG
TCACAACTCCAAGCCTTGCATATTGGTCTGGATAGTTCCAGTATAGGCAGTGGACCAGGG
GATGCTGAGGCAGATGATGGGTTTCCAGAATCAAGATTAGAAGGATGGCTTTCATTGCCT
GTACGAAACAACACTAAGAAATTTGGATGGGTTAAAAAGTATGTGATTGTAAGCAGTAAG
AAGATTCTTTTCTATGACAGTGAACAAGATAAAGAACAATCCAATCCTTACATGGTTTTA
GATATAGACAAGTTATTTCATGTCCGACCAGTTACACAGACAGATGTGTATAGAGCAGAT
GCTAAAGAAATTCCAAGGATATTCCAGATTCTGTATGCCAATGAAGGAGAAAGTAAGAAG
GAACAAGAATTTCCAGTGGAGCCAGTTGGAGAAAAATCTAATTATATTTGCCACAAGGGA
CATGAGTTTATTCCTACTCTTTATCATTTCCCAACCAACTGTGAGGCTTGTATGAAGCCC
CTGTGGCACATGTTTAAGCCTCCTCCTGCTTTGGAGTGCCGCCGTTGCCATATTAAGTGT
CATAAAGATCATATGGACAAAAAGGAGGAGATTATAGCACCTTGCAAAGTATATTATGAT
ATTTCAACGGCAAAGAATCTGTTATTACTAGCAAATTCTACAGAAGAGCAGCAGAAGTGG
GTTAGTCGGTTGGTGAAAAAGATACCTAAAAAGCCCCCAGCTCCAGACCCTTTTGCCCGA
TCATCTCCTAGAACTTCAATGAAGATACAGCAAAACCAGTCTATTAGACGGCCAAGTCGA
CAGCTTGCCCCAAACAAACCTAGCTAA
Enzyme 69 GenBank Gene ID NM_004850.3 Link Image
Enzyme 69 GeneCard ID ROCK2 Link Image
Enzyme 69 GenAtlas ID ROCK2 Link Image
Enzyme 69 HGNC ID HGNC:10252 Link Image
Enzyme 69 Chromosome Location 2
Enzyme 69 Locus 2p24
Enzyme 69 SNPs SNPJam Report Link Image
Enzyme 69 General References
  1. Takahashi N, Tuiki H, Saya H, Kaibuchi K: Localization of the gene coding for ROCK II/Rho kinase on human chromosome 2p24. Genomics. 1999 Jan 15;55(2):235-7. [PubMed Link Image]
  2. Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Jun 30;5(3):169-76. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  5. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  6. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  7. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  8. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  9. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  10. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  11. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 69 Metabolite References Not Available
Enzyme 70 [top]
Enzyme 70 ID 6926
Enzyme 70 Name Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2
Enzyme 70 Synonyms
  1. AGAP-2
  2. Centaurin-gamma-1
  3. Cnt-g1
  4. GTP-binding and GTPase-activating protein 2
  5. GGAP2
  6. Phosphatidylinositol-3-kinase enhancer
  7. PIKE
Enzyme 70 Gene Name AGAP2
Enzyme 70 Protein Sequence >Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2
MSRGAGALQRRTTTYLISLTLVKLESVPPPPPSPSAAAVGAPGARGSEPRDPGSPRGAEE
PGKKRHERLFHRQDALWISTSSAGAGGAEPPALSPAPASPARPVSPAPGRRLSLWAAPPG
PPLSGGLSPDSKPGGAPSSSRRPLLSSPSWGGPEPEGRTGGGVPGSSSPHPGTGSRRLKV
APPPPAPKPCKTVTTSGAKAGGGKGAGSRLSWPESEGKPRVKGSKSSAGTGASVSAAATA
AAAGGGGSTASTSGGVGAGAGARGKLSPRKGKSKTLDNSDLHPGPPAGSPPPLTLPPTPS
PATAVTAASAQPPGPAPPITLEPPAPGLKRGREGGRASTRDRKMLKFISGIFTKSTGGPP
GSGPLPGPPSLSSGSGSRELLGAELRASPKAVINSQEWTLSRSIPELRLGVLGDARSGKS
SLIHRFLTGSYQVLEKTESEQYKKEMLVDGQTHLVLIREEAGAPDAKFSGWADAVIFVFS
LEDENSFQAVSRLHGQLSSLRGEGRGGLALALVGTQDRISASSPRVVGDARARALCADMK
RCSYYETCATYGLNVDRVFQEVAQKVVTLRKQQQLLAACKSLPSSPSHSAASTPVAGQAS
NGGHTSDYSSSLPSSPNVGHRELRAEAAAVAGLSTPGSLHRAAKRRTSLFANRRGSDSEK
RSLDSRGETTGSGRAIPIKQSFLLKRSGNSLNKEWKKKYVTLSSNGFLLYHPSINDYIHS
THGKEMDLLRTTVKVPGKRPPRAISAFGPSASINGLVKDMSTVQMGEGLEATTPMPSPSP
SPSSLQPPPDQTSKHLLKPDRNLARALSTDCTPSGDLSPLSREPPPSPMVKKQRRKKLTT
PSKTEGSAGQAEAKRKMWKLKSFGSLRNIYKAEENFEFLIVSSTGQTWHFEAASFEERDA
WVQAIESQILASLQCCESSKVKLRTDSQSEAVAIQAIRNAKGNSICVDCGAPNPTWASLN
LGALICIECSGIHRNLGTHLSRVRSLDLDDWPRELTLVLTAIGNDTANRVWESDTRGRAK
PSRDSSREERESWIRAKYEQLLFLAPLSTSEEPLGRQLWAAVQAQDVATVLLLLAHARHG
PLDTSVEDPQLRSPLHLAAELAHVVITQLLLWYGADVAARDAQGRTALFYARQAGSQLCA
DILLQHGCPGEGGSAATTPSAATTPSITATPSPRRRSSAASVGRADAPVALV
Enzyme 70 Number of Residues 1192
Enzyme 70 Molecular Weight 124672.3
Enzyme 70 Theoretical pI 10.54
Enzyme 70 GO Classification
Function
  • ARF GTPase activator activity
  • GTP binding
  • GTPase regulator activity
  • binding
  • cation binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • ion binding
  • metal ion binding
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • purine nucleotide binding
  • small GTPase regulator activity
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of ARF GTPase activity
  • regulation of GTP catabolic process
  • regulation of GTPase activity
  • regulation of Ras GTPase activity
  • regulation of biological process
  • regulation of cellular metabolic process
  • regulation of cellular process
  • regulation of metabolic process
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • regulation of nucleotide catabolic process
  • regulation of nucleotide metabolic process
  • regulation of purine nucleotide catabolic process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 70 General Function Involved in ARF GTPase activator activity
Enzyme 70 Specific Function GTPase-activating protein (GAP) for ARF1 and ARF5, which also shows strong GTPase activity. Isoform 1 participates in the prevention of neuronal apoptosis by enhancing PI3 kinase activity. It aids the coupling of metabotropic glutamate receptor 1 (GRM1) to cytoplasmic PI3 kinase by interacting with Homer scaffolding proteins, and also seems to mediate anti-apoptotic effects of NGF by activating nuclear PI3 kinase. Isoform 2 does not stimulate PI3 kinase but may protect cells from apoptosis by stimulating Akt. It also regulates the adapter protein 1 (AP-1)-dependent trafficking of proteins in the endosomal system. It seems to be oncogenic. It is overexpressed in cancer cells, prevents apoptosis and promotes cancer cell invasion
Enzyme 70 Pathways Not Available
Enzyme 70 Reactions Not Available
Enzyme 70 Pfam Domain Function
Enzyme 70 Signals
  • None
Enzyme 70 Transmembrane Regions
  • None
Enzyme 70 Essentiality Not Available
Enzyme 70 GenBank ID Protein 170650694 Link Image
Enzyme 70 UniProtKB/Swiss-Prot ID Q99490 Link Image
Enzyme 70 UniProtKB/Swiss-Prot Entry Name AGAP2_HUMAN Link Image
Enzyme 70 PDB ID 2BMJ Link Image
Enzyme 70 PDB File Show
Enzyme 70 3D Structure
Enzyme 70 Cellular Location Not Available
Enzyme 70 Gene Sequence >3579 bp
ATGAGCCGGGGCGCGGGCGCGCTTCAGCGCCGGACAACGACCTACCTCATCTCGCTGACC
CTGGTTAAGCTCGAGTCGGTGCCTCCGCCGCCGCCTTCTCCGTCTGCGGCCGCGGCCGGC
GCCGCCGGTGCCAGAGGCTCCGAGACTGGGGATCCTGGCAGCCCCCGAGGCGCGGAGGAG
CCGGGCAAGAAGCGGCACGAACGTCTCTTCCACCGGCAGGATGCGCTGTGGATCAGCACG
AGCAGCGCGGGCACCGGGGGCGCGGAGCCCCCAGCCCTGTCCCCGGCTCCGGCCAGTCCG
GCCCGCCCAGTCTCCCCCGCTCCCGGCCGCCGCCTCTCCCTCTGGGCCGTCCCTCCGGGA
CCCCCGCTCTCCGGGGGACTGAGCCCCGACCCCAAGCCTGGGGGCGCCCCCACCTCCTCC
CGGCGCCCCCTGCTCAGCAGCCCGAGCTGGGGCGGCCCGGAGCCCGAAGGCCGGGCGGGC
GGCGGCATCCCTGGCTCATCCTCTCCGCACCCTGGCACCGGCAGCCGGAGGCTCAAGGTG
GCGCCTCCTCCGCCGGCTCCCAAGCCTTGCAAGACCGTGACCACGAGTGGAGCCAAAGCC
GGCGGGGGCAAGGGCGCGGGTAGCCGCCTGTCATGGCCCGAAAGCGAGGGCAAGCCCAGG
GTCAAGGGGTCAAAGAGCAGCGCCGGGACTGGAGCTTCGGTCTCTGCCGCCGCCACCGCC
GCCGCCGCCGGGGGAGGGGGCTCTACAGCTTCGACCTCTGGTGGGGTCGGGGCTGGGGCT
GGAGCCCGAGGGAAGTTGTCCCCTCGGAAAGGCAAGAGTAAGACCTTGGACAACAGTGAC
TTGCATCCGGGACCGCCTGCCGGCTCTCCTCCTCCGCTAACCCTCCCACCAACTCCGAGT
CCAGCCACTGCTGTCACCGCTGCTTCCGCGCAGCCCCCCGGGCCTGCACCTCCAATCACT
CTGGAGCCTCCAGCTCCGGGGCTGAAACGGGGCCGGGAGGGGGGCCGAGCATCCACTCGT
GACCGCAAGATGCTCAAGTTTATCAGCGGCATCTTCACCAAGAGCACAGGAGGGCCTCCT
GGCTCCGGGCCCCTTCCCGGACCCCCCAGCCTGTCTTCTGGCAGCGGGTCCAGGGAGCTG
CTGGGCGCCGAGCTCCGCGCTTCCCCTAAGGCTGTGATCAATAGCCAGGAATGGACTTTG
AGCCGCTCCATTCCTGAACTGCGCCTGGGTGTGCTGGGCGATGCCAGGAGTGGGAAGTCA
TCGCTCATCCACCGATTCCTGACTGGCTCATACCAGGTGCTGGAGAAGACAGAGAGTGAG
CAGTACAAGAAAGAAATGTTGGTGGATGGACAGACACATCTGGTGCTAATCCGAGAGGAA
GCTGGGGCACCTGATGCCAAGTTCTCAGGCTGGGCAGATGCTGTGATCTTCGTCTTCAGC
CTGGAGGATGAGAACAGTTTCCAGGCTGTGAGCCGTCTCCATGGGCAGCTGAGTTCCCTT
CGCGGGGAGGGACGAGGAGGCCTGGCCTTGGCACTGGTGGGGACACAAGACAGGATCAGT
GCTTCCTCCCCTCGGGTGGTGGGAGATGCTCGTGCCAGAGCTCTGTGCGCGGACATGAAA
CGCTGCAGCTACTATGAGACTTGTGCAACCTATGGGCTCAATGTGGATCGGGTCTTCCAG
GAGGTGGCCCAGAAGGTGGTGACCTTGCGCAAGCAGCAACAGCTTCTGGCTGCCTGCAAG
TCCCTGCCCAGCTCCCCAAGCCACTCAGCTGCATCCACTCCGGTAGCTGGCCAGGCTAGT
AACGGGGGCCACACTAGCGACTACTCTTCTTCCCTCCCGTCCTCACCGAATGTTGGTCAC
CGGGAGCTCCGAGCCGAGGCAGCTGCAGTGGCTGGATTGAGCACCCCAGGGTCCCTGCAC
CGGGCAGCCAAGCGCAGGACCAGCCTTTTTGCGAATCGTCGGGGTAGTGACTCCGAGAAA
CGAAGCTTGGATAGTCGGGGAGAGACAACAGGGAGTGGGCGAGCCATCCCCATCAAACAG
AGCTTCCTACTAAAACGAAGTGGCAATTCCTTGAACAAAGAATGGAAGAAGAAATATGTA
ACCCTGTCCAGTAATGGCTTTCTACTCTACCACCCCAGTATTAACGATTACATCCACAGT
ACCCACGGCAAGGAGATGGACTTGCTGCGAACAACAGTCAAAGTCCCGGGCAAGCGGCCC
CCGAGGGCCATCTCTGCCTTTGGCCCCTCAGCCAGCATTAACGGGCTCGTCAAGGACATG
AGCACTGTCCAGATGGGTGAAGGCCTGGAAGCCACTACTCCCATGCCAAGCCCTAGCCCC
AGCCCCAGTTCCCTGCAGCCACCACCAGATCAGACATCCAAACACCTGCTGAAGCCAGAC
CGGAATTTGGCCCGAGCCCTCAGCACGGACTGTACCCCATCTGGAGACCTGAGCCCCCTG
AGTCGGGAACCCCCTCCTTCTCCCATGGTGAAGAAGCAGAGGAGGAAAAAATTGACAACA
CCATCCAAGACTGAAGGCTCGGCTGGGCAGGCTGAAGCCAAGCGCAAAATGTGGAAACTA
AAATCCTTTGGTAGTTTAAGAAATATTTATAAAGCAGAGGAAAACTTTGAGTTCCTGATC
GTGTCCAGCACGGGTCAGACGTGGCACTTTGAGGCAGCCAGTTTTGAGGAGCGGGATGCC
TGGGTCCAGGCCATCGAGAGTCAGATCCTAGCCAGTCTGCAATGCTGTGAGAGCAGCAAG
GTCAAGCTGCGCACAGACAGCCAAAGCGAGGCCGTGGCCATCCAGGCGATCCGGAACGCC
AAGGGGAATTCAATCTGCGTGGACTGCGGGGCCCCCAACCCCACGTGGGCCAGCTTGAAC
CTGGGCGCCCTCATCTGCATCGAGTGTTCTGGCATCCACCGCAACCTGGGCACACACCTG
TCCCGCGTTCGCTCGCTGGACTTGGACGACTGGCCACGGGAGCTGACCCTGGTGCTGACG
GCTATTGGCAACGACACGGCCAACCGCGTGTGGGAAAGCGACACGCGAGGCCGTGCCAAG
CCCTCGCGGGACTCTTCGCGGGAGGAGCGCGAGTCGTGGATTCGCGCCAAGTACGAGCAG
CTACTGTTCCTGGCGCCGCTGAGCACCTCGGAGGAGCCGCTGGGCCGCCAGCTGTGGGCC
GCCGTGCAGGCCCAGGACGTGGCTACCGTTCTCCTGCTTTTGGCCCATGCGCGACACGGG
CCGCTCGACACCAGCGTAGAGGACCCACAGCTGCGCTCCCCACTCCACCTGGCGGCCGAG
CTCGCCCACGTCGTCATCACGCAACTGCTGCTGTGGTACGGCGCGGACGTGGCGGCCCGT
GACGCCCAGGGCCGCACGGCGCTGTTCTACGCCCGCCAGGCTGGAAGCCAGCTGTGCGCC
GACATCCTTCTCCAGCACGGCTGCCCGGGTGAGGGCGGCAGCGCGGCCACCACGCCCAGC
GCGGCCACCACGCCCAGCATCACCGCCACGCCCAGCCCCCGCCGCCGGAGCAGCGCCGCT
AGCGTGGGCCGCGCCGACGCCCCGGTTGCGCTGGTATAG
Enzyme 70 GenBank Gene ID NM_001122772.1 Link Image
Enzyme 70 GeneCard ID AGAP2 Link Image
Enzyme 70 GenAtlas ID AGAP2 Link Image
Enzyme 70 HGNC ID HGNC:16921 Link Image
Enzyme 70 Chromosome Location 1
Enzyme 70 Locus 12q14.1
Enzyme 70 SNPs SNPJam Report Link Image
Enzyme 70 General References
  1. Elkahloun AG, Krizman DB, Wang Z, Hofmann TA, Roe B, Meltzer PS: Transcript mapping in a 46-kb sequenced region at the core of 12q13.3 amplification in human cancers. Genomics. 1997 Jun 1;42(2):295-301. [PubMed Link Image]
  2. Xia C, Ma W, Stafford LJ, Liu C, Gong L, Martin JF, Liu M: GGAPs, a new family of bifunctional GTP-binding and GTPase-activating proteins. Mol Cell Biol. 2003 Apr;23(7):2476-88. [PubMed Link Image]
  3. Rong R, Ahn JY, Huang H, Nagata E, Kalman D, Kapp JA, Tu J, Worley PF, Snyder SH, Ye K: PI3 kinase enhancer-Homer complex couples mGluRI to PI3 kinase, preventing neuronal apoptosis. Nat Neurosci. 2003 Nov;6(11):1153-61. Epub 2003 Oct 5. [PubMed Link Image]
  4. Nagase T, Seki N, Ishikawa K, Tanaka A, Nomura N: Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1996 Feb 29;3(1):17-24. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Ahn JY, Rong R, Kroll TG, Van Meir EG, Snyder SH, Ye K: PIKE (phosphatidylinositol 3-kinase enhancer)-A GTPase stimulates Akt activity and mediates cellular invasion. J Biol Chem. 2004 Apr 16;279(16):16441-51. Epub 2004 Feb 3. [PubMed Link Image]
  8. Ahn JY, Hu Y, Kroll TG, Allard P, Ye K: PIKE-A is amplified in human cancers and prevents apoptosis by up-regulating Akt. Proc Natl Acad Sci U S A. 2004 May 4;101(18):6993-8. Epub 2004 Apr 26. [PubMed Link Image]
  9. Nie Z, Fei J, Premont RT, Randazzo PA: The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein complexes AP-1 and AP-3. J Cell Sci. 2005 Aug 1;118(Pt 15):3555-66. [PubMed Link Image]
  10. Knobbe CB, Trampe-Kieslich A, Reifenberger G: Genetic alteration and expression of the phosphoinositol-3-kinase/Akt pathway genes PIK3CA and PIKE in human glioblastomas. Neuropathol Appl Neurobiol. 2005 Oct;31(5):486-90. [PubMed Link Image]
  11. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  12. Hu Y, Liu Z, Ye K: Phosphoinositol lipids bind to phosphatidylinositol 3 (PI3)-kinase enhancer GTPase and mediate its stimulatory effect on PI3-kinase and Akt signalings. Proc Natl Acad Sci U S A. 2005 Nov 15;102(46):16853-8. Epub 2005 Nov 1. [PubMed Link Image]
  13. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 70 Metabolite References Not Available
Enzyme 71 [top]
Enzyme 71 ID 7002
Enzyme 71 Name Rho guanine nucleotide exchange factor 1
Enzyme 71 Synonyms
  1. 115 kDa guanine nucleotide exchange factor
  2. p115-RhoGEF
  3. p115RhoGEF
  4. Sub1.5
Enzyme 71 Gene Name ARHGEF1
Enzyme 71 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 71 Number of Residues 912
Enzyme 71 Molecular Weight 102434.3
Enzyme 71 Theoretical pI 5.37
Enzyme 71 GO Classification
Function
  • GTPase regulator activity
  • Ras guanyl-nucleotide exchange factor activity
  • Rho guanyl-nucleotide exchange factor activity
  • enzyme regulator activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
  • biological regulation
  • regulation of Ras protein signal transduction
  • regulation of Rho protein signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
Component
  • cell part
  • cytoplasm
  • intracellular
  • intracellular part
Enzyme 71 General Function Involved in GTPase activator activity
Enzyme 71 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 71 Pathways Not Available
Enzyme 71 Reactions Not Available
Enzyme 71 Pfam Domain Function
Enzyme 71 Signals
  • None
Enzyme 71 Transmembrane Regions
  • None
Enzyme 71 Essentiality Not Available
Enzyme 71 GenBank ID Protein 15011972 Link Image
Enzyme 71 UniProtKB/Swiss-Prot ID Q92888 Link Image
Enzyme 71 UniProtKB/Swiss-Prot Entry Name ARHG1_HUMAN Link Image
Enzyme 71 PDB ID 1SHZ Link Image
Enzyme 71 PDB File Show
Enzyme 71 3D Structure
Enzyme 71 Cellular Location Not Available
Enzyme 71 Gene Sequence >2739 bp
ATGGAAGACTTCGCCCGAGGGGCGGCCTCCCCAGGCCCCTCCCGGCCTGGCCTGGTTCCC
GTCAGCATCATCGGGGCTGAGGATGAGGATTTTGAGAACGAGCTGGAGACAAACTCAGAA
GAGCAAAACAGCCAGTTCCAGAGCCTGGAGCAGGTGAAGCGGCGCCCAGCCCACCTCATG
GCCCTCCTGCAGCACGTGGCCCTGCAGTTTGAGCCAGGACCCCTGCTTTGCTGTCTGCAT
GCCGACATGCTGGGCTCACTGGGCCCCAAGGAGGCCAAGAAGGCCTTCCTGGACTTCTAC
CACAGCTTCCTGGAGAAGACAGCGGTTCTCCGGGTGCCGGTCCCTCCCAACGTCGCCTTT
GAACTTGACCGCACTAGGGCTGACCTCATCTCCGAGGATGTCCAGCGGCGGTTCGTGCAG
GAGGTGGTGCAAAGCCAGCAGGTAGCCGTGGGCCGGCAGCTGGAGGACTTCCGTTCCAAG
CGGCTCATGGGCATGACGCCCTGGGAGCAGGAGCTGGCCCAGCTGGAGGCTTGGGTTGGG
CGGGACCGAGCCAGCTACGAGGCCCGGGAGCGGCACGTGGCGGAGCGGCTGCTCATGCAC
CTGGAGGAGATGCAACATACCATCTCTACCGACGAAGAAAAGAGTGCTGCCGTGGTCAAC
GCCATTGGCCTGTACATGCGCCACCTTGGGGTGCGGACCAAGAGTGGAGACAAGAAGTCG
GGGAGGAACTTCTTCCGGAAAAAGGTGATGGGGAACCGGCGGTCGGACGAGCCTGCCAAG
ACCAAGAAGGGGCTGAGCAGCATCCTGGATGCCGCCCGCTGGAACCGGGGAGAGCCCCAG
GTTCCAGATTTTCGACACCTCAAAGCAGAGGTTGATGCCGAGAAGCCAGGTGCTACAGAC
CGGAAGGGAGGCGTGGGGATGCCCTCTCGGGACCGGAATATCGGGGCTCCTGGGCAGGAC
ACCCCTGGAGTCTCTCTGCACCCTCTGTCCCTGGACAGCCCAGACCGGGAACCAGGTGCT
GACGCCCCCCTGGAGCTGGGGGACTCATCCCCGCAGGGCCCAATGAGCCTGGAGTCCTTG
GCGCCCCCAGAGAGTACCGACGAGGGGGCCGAAACCGAGAGCCCCGAGCCTGGAGATGAG
GGGGAGCCGGGGCGGTCGGGACTGGAGCTTGAACCAGAAGAGCCTCCCGGCTGGCGGGAA
CTCGTCCCCCCAGACACCCTGCACAGCCTGCCCAAGAGCCAGGTGAAGCGGCAGGAGGTC
ATCAGCGAGCTGCTGGTGACAGAGGCGGCCCACGTGCGCATGCTGCGGGTGCTGCACGAC
CTCTTCTTCCAGCCCATGGCAGAATGCCTGTTCTTCCCCTTGGAGGAGCTGCAGAACATC
TTCCCCAGCCTGGACGAGCTCATCGAGGTGCATTCCCTGTTCCTCGATCGCCTGATGAAG
CGGAGGCAGGAGAGTGGCTACCTCATCGAGGAGATCGGAGACGTGCTGCTGGCCCGGTTT
GATGGTGCTGAGGGCTCCTGGTTCCAGAAAATCTCCTCCCGCTTCTGCAGCCGCCAGTCA
TTTGCCTTAGAGCAGCTCAAAGCCAAGCAACGCAAGGACCCTCGGTTCTGTGCCTTCGTG
CAGGAAGCTGAGAGCCGCCCGCGGTGCCGCCGCCTGCAGCTGAAGGACATGATCCCCACG
GAGATGCAGCGGCTGACCAAGTACCCCCTGCTCCTGCAGAGCATCGGGCAGAACACAGAA
GAGCCCACAGAACGGGAGAAAGTGGAGCTGGCAGCCGAGTGCTGCCGGGAAATTCTACAC
CACGTCAACCAAGCCGTGCGTGACATGGAGGACCTGCTGAGGCTCAAGGACTATCAGCGG
CGCCTGGACTTGTCCCACCTTCGGCAGAGCAGCGACCCTATGCTGAGCGAGTTCAAGAAC
CTGGACATCACCAAGAAGAAATTGGTCCACGAGGGCCCACTGACGTGGCGGGTGACTAAG
GACAAGGCAGTGGAGGTGCATGTGCTGCTGCTGGACGACCTGCTGCTGCTGCTCCAGCGC
CAGGACGAGCGGCTGCTGCTCAAGTCCCATAGCCGGACACTGACGCCCACGCCCGATGGC
AAGACCATGCTGCGGCCCGTGCTGCGGCTCACCTCCGCCATGACCCGCGAGGTGGCCACC
GATCACAAAGCCTTCTACGTCCTTTTTACCTGGGACCAGGAGGCCCAGATATACGAGCTG
GTGGCACAGACTGTGTCGGAGCGGAAAAACTGGTGTGCTCTCATCACTGAGACTGCCGGA
TCCCTGAAAGTCCCTGCCCCTGCCTCTCGCCCTAAGCCCCGGCCCAGCCCGAGCAGCACC
CGAGAACCCCTCCTCAGCAGCTCTGAGAACGGCAATGGTGGCCGAGAGACGTCTCCAGCT
GATGCCCGGACCGAGAGAATCCTCAGTGACCTCCTGCCCTTCTGCAGACCAGGCCCCGAG
GGCCAGCTCGCTGCCACGGCCCTTCGGAAAGTGCTGTCCCTGAAGCAGCTTCTGTTTCCG
GCGGAGGAAGACAATGGGGCGGGGCCTCCTCGAGATGGGGATGGGGTCCCAGGGGGCGGC
CCCCTGAGCCCAGCACGGACCCAGGAAATCCAGGAGAACCTGCTCAGCTTGGAGGAGACC
ATGAAGCAGCTGGAGGAGTTGGAGGAGGAATTTTGCCGCCTGAGACCCCTCCTGTCTCAG
CTTGGGGGGAACTCTGTCCCCCAGCCTGGCTGCACTTGA
Enzyme 71 GenBank Gene ID NM_004706.3 Link Image
Enzyme 71 GeneCard ID ARHGEF1 Link Image
Enzyme 71 GenAtlas ID Not Available
Enzyme 71 HGNC ID Not Available
Enzyme 71 Chromosome Location 1
Enzyme 71 Locus 19q13.13
Enzyme 71 SNPs SNPJam Report Link Image
Enzyme 71 General References
  1. Hart MJ, Sharma S, elMasry N, Qiu RG, McCabe P, Polakis P, Bollag G: Identification of a novel guanine nucleotide exchange factor for the Rho GTPase. J Biol Chem. 1996 Oct 11;271(41):25452-8. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Aasheim HC, Pedeutour F, Smeland EB: Characterization, expression and chromosomal localization of a human gene homologous to the mouse Lsc oncogene, with strongest expression in hematopoetic tissues. Oncogene. 1997 Apr 10;14(14):1747-52. [PubMed Link Image]
  4. Kozasa T, Jiang X, Hart MJ, Sternweis PM, Singer WD, Gilman AG, Bollag G, Sternweis PC: p115 RhoGEF, a GTPase activating protein for Galpha12 and Galpha13. Science. 1998 Jun 26;280(5372):2109-11. [PubMed Link Image]
  5. Hart MJ, Jiang X, Kozasa T, Roscoe W, Singer WD, Gilman AG, Sternweis PC, Bollag G: Direct stimulation of the guanine nucleotide exchange activity of p115 RhoGEF by Galpha13. Science. 1998 Jun 26;280(5372):2112-4. [PubMed Link Image]
  6. Bhattacharyya R, Wedegaertner PB: Galpha 13 requires palmitoylation for plasma membrane localization, Rho-dependent signaling, and promotion of p115-RhoGEF membrane binding. J Biol Chem. 2000 May 19;275(20):14992-9. [PubMed Link Image]
  7. Park B, Nguyen NT, Dutt P, Merdek KD, Bashar M, Sterpetti P, Tosolini A, Testa JR, Toksoz D: Association of Lbc Rho guanine nucleotide exchange factor with alpha-catenin-related protein, alpha-catulin/CTNNAL1, supports serum response factor activation. J Biol Chem. 2002 Nov 22;277(47):45361-70. Epub 2002 Sep 20. [PubMed Link Image]
  8. Holinstat M, Mehta D, Kozasa T, Minshall RD, Malik AB: Protein kinase Calpha-induced p115RhoGEF phosphorylation signals endothelial cytoskeletal rearrangement. J Biol Chem. 2003 Aug 1;278(31):28793-8. Epub 2003 May 16. [PubMed Link Image]
  9. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  10. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  11. Chen Z, Wells CD, Sternweis PC, Sprang SR: Structure of the rgRGS domain of p115RhoGEF. Nat Struct Biol. 2001 Sep;8(9):805-9. [PubMed Link Image]
  12. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 71 Metabolite References Not Available
Enzyme 72 [top]
Enzyme 72 ID 7035
Enzyme 72 Name Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
Enzyme 72 Synonyms
  1. Development and differentiation-enhancing factor 2
  2. Paxillin-associated protein with ARF GAP activity 3
  3. PAG3
  4. Pyk2 C-terminus-associated protein
  5. PAP
Enzyme 72 Gene Name ASAP2
Enzyme 72 Protein Sequence >Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2
MPDQISVSEFVAETHEDYKAPTASSFTTRTAQCRNTVAAIEEALDVDRMVLYKMKKSVKA
INSSGLAHVENEEQYTQALEKFGGNCVCRDDPDLGSAFLKFSVFTKELTALFKNLIQNMN
NIISFPLDSLLKGDLKGVKGDLKKPFDKAWKDYETKITKIEKEKKEHAKLHGMIRTEISG
AEIAEEMEKERRFFQLQMCEYLLKVNEIKIKKGVDLLQNLIKYFHAQCNFFQDGLKAVES
LKPSIETLSTDLHTIKQAQDEERRQLIQLRDILKSALQVEQKEDSQIRQSTAYSLHQPQG
NKEHGTERNGSLYKKSDGIRKVWQKRKCSVKNGFLTISHGTANRPPAKLNLLTCQVKTNP
EEKKCFDLISHDRTYHFQAEDEQECQIWMSVLQNSKEEALNNAFKGDDNTGENNIVQELT
KEIISEVQRMTGNDVCCDCGAPDPTWLSTNLGILTCIECSGIHRELGVHYSRMQSLTLDV
LGTSELLLAKNIGNAGFNEIMECCLPAEDSVKPNPGSDMNARKDYITAKYIERRYARKKH
ADNAAKLHSLCEAVKTRDIFGLLQAYADGVDLTEKIPLANGHEPDETALHLAVRSVDRTS
LHIVDFLVQNSGNLDKQTGKGSTALHYCCLTDNAECLKLLLRGKASIEIANESGETPLDI
AKRLKHEHCEELLTQALSGRFNSHVHVEYEWRLLHEDLDESDDDMDEKLQPSPNRREDRP
ISFYQLGSNQLQSNAVSLARDAANLAKEKQRAFMPSILQNETYGALLSGSPPPAQPAAPS
TTSAPPLPPRNVGKVQTASSANTLWKTNSVSVDGGSRQRSSSDPPAVHPPLPPLRVTSTN
PLTPTPPPPVAKTPSVMEALSQPSKPAPPGISQIRPPPLPPQPPSRLPQKKPAPGADKST
PLTNKGQPRGPVDLSATEALGPLSNAMVLQPPAPMPRKSQATKLKPKRVKALYNCVADNP
DELTFSEGDVIIVDGEEDQEWWIGHIDGDPGRKGAFPVSFVHFIAD
Enzyme 72 Number of Residues 1006
Enzyme 72 Molecular Weight 111649.6
Enzyme 72 Theoretical pI 6.66
Enzyme 72 GO Classification
Function
  • ARF GTPase activator activity
  • GTPase regulator activity
  • binding
  • cation binding
  • enzyme regulator activity
  • ion binding
  • metal ion binding
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • regulation of ARF GTPase activity
  • regulation of GTP catabolic process
  • regulation of GTPase activity
  • regulation of Ras GTPase activity
  • regulation of biological process
  • regulation of cellular metabolic process
  • regulation of metabolic process
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • regulation of nucleotide catabolic process
  • regulation of nucleotide metabolic process
  • regulation of purine nucleotide catabolic process
Component
Enzyme 72 General Function Involved in ARF GTPase activator activity
Enzyme 72 Specific Function Activates the small GTPases ARF1, ARF5 and ARF6. Regulates the formation of post-Golgi vesicles and modulates constitutive secretion. Modulates phagocytosis mediated by Fc gamma receptor and ARF6. Modulates PXN recruitment to focal contacts and cell migration
Enzyme 72 Pathways Not Available
Enzyme 72 Reactions Not Available
Enzyme 72 Pfam Domain Function
Enzyme 72 Signals
  • None
Enzyme 72 Transmembrane Regions
  • None
Enzyme 72 Essentiality Not Available
Enzyme 72 GenBank ID Protein 4502249 Link Image
Enzyme 72 UniProtKB/Swiss-Prot ID O43150 Link Image
Enzyme 72 UniProtKB/Swiss-Prot Entry Name ASAP2_HUMAN Link Image
Enzyme 72 PDB ID 1DCQ Link Image
Enzyme 72 PDB File Show
Enzyme 72 3D Structure
Enzyme 72 Cellular Location Not Available
Enzyme 72 Gene Sequence >3021 bp
ATGCCGGACCAGATCTCCGTGTCGGAATTCGTGGCCGAGACCCATGAGGACTACAAGGCG
CCCACGGCCTCCAGCTTCACCACCCGCACGGCGCAGTGCCGGAACACTGTGGCGGCCATC
GAGGAGGCTTTGGACGTGGACCGGATGGTTCTTTACAAAATGAAGAAATCCGTGAAAGCA
ATCAACAGCTCTGGGCTGGCTCACGTGGAAAATGAAGAGCAGTACACCCAGGCTCTGGAG
AAGTTTGGCGGCAACTGTGTATGCAGAGATGACCCAGATTTAGGAAGTGCGTTCCTGAAG
TTCTCAGTGTTTACAAAGGAGTTGACAGCACTTTTCAAAAACCTGATTCAGAATATGAAC
AACATAATCTCCTTCCCTTTGGACAGTTTGCTGAAGGGGGACCTGAAAGGAGTGAAAGGG
GATCTGAAAAAGCCTTTTGATAAAGCTTGGAAGGACTATGAAACAAAAATAACCAAGATA
GAAAAGGAGAAAAAGGAACACGCCAAGCTCCATGGGATGATTCGGACTGAAATAAGCGGA
GCGGAAATTGCCGAAGAGATGGAAAAGGAGAGGCGCTTCTTCCAGCTACAGATGTGCGAG
TATCTGCTGAAGGTCAACGAAATCAAGATTAAAAAGGGAGTAGATTTACTTCAGAATCTG
ATCAAATACTTTCATGCCCAATGCAATTTTTTTCAGGATGGACTCAAAGCCGTGGAAAGC
CTCAAACCTTCCATTGAAACGCTGTCTACGGATCTTCACACGATCAAACAGGCCCAGGAT
GAAGAAAGAAGGCAGTTGATACAGCTTCGAGATATTTTGAAATCCGCATTGCAGGTTGAA
CAGAAAGAGGACTCCCAAATTCGTCAGAGCACAGCTTATAGCTTACATCAGCCTCAGGGA
AACAAGGAACATGGGACCGAGCGGAACGGCAGCCTCTACAAGAAGAGTGACGGGATCCGA
AAAGTGTGGCAGAAAAGGAAATGTTCAGTTAAAAATGGTTTTCTGACCATATCCCATGGT
ACCGCTAACCGGCCTCCTGCAAAGCTCAACCTGCTAACCTGCCAGGTGAAGACCAACCCT
GAGGAGAAGAAGTGCTTTGACCTCATTTCACATGACAGAACTTACCACTTTCAAGCTGAA
GATGAACAGGAATGTCAAATATGGATGTCTGTGCTGCAAAATAGCAAAGAAGAAGCTTTA
AACAATGCATTTAAGGGGGATGACAATACTGGAGAAAATAACATCGTCCAAGAACTGACA
AAGGAGATCATCTCAGAAGTGCAGAGGATGACGGGCAATGACGTCTGCTGTGACTGTGGG
GCGCCAGATCCTACATGGCTTTCCACCAACCTGGGCATCCTGACCTGCATCGAGTGTTCC
GGAATCCACCGAGAGCTGGGGGTTCATTATTCCAGGATGCAGTCCCTGACCTTAGATGTA
CTGGGAACATCTGAGCTGCTGCTCGCCAAGAATATTGGGAATGCAGGCTTTAATGAGATC
ATGGAATGTTGCCTACCAGCTGAGGACTCAGTCAAACCCAACCCAGGCAGCGACATGAAT
GCAAGAAAGGACTACATCACAGCCAAGTACATCGAGAGGAGATACGCAAGGAAGAAGCAC
GCGGATAACGCGGCGAAGCTTCACAGTCTTTGCGAGGCCGTCAAAACGAGAGATATTTTT
GGATTGCTCCAAGCTTATGCTGATGGTGTGGATCTTACGGAAAAAATCCCACTGGCCAAC
GGACATGAGCCGGATGAAACGGCCCTCCACCTTGCAGTCAGATCCGTGGATCGAACCTCT
CTTCACATTGTAGACTTTTTAGTTCAGAACAGTGGGAACCTGGATAAACAGACAGGGAAA
GGCAGCACAGCCCTGCACTACTGCTGCCTGACCGACAATGCCGAGTGCCTCAAGTTGCTC
CTGCGGGGGAAGGCCTCCATCGAGATAGCAAACGAGTCAGGAGAGACTCCGCTGGACATT
GCCAAGCGCCTCAAGCACGAGCACTGTGAGGAGCTGCTGACCCAAGCCTTATCTGGAAGA
TTTAATTCTCACGTTCACGTTGAATATGAATGGCGACTACTCCACGAAGACCTGGATGAA
AGTGATGACGACATGGATGAGAAATTGCAGCCCAGTCCCAACCGGCGGGAAGACCGGCCC
ATCAGCTTCTACCAGCTGGGCTCCAACCAGCTTCAGTCTAACGCTGTATCTTTGGCCAGA
GATGCTGCAAACCTTGCCAAGGAGAAGCAGAGGGCTTTCATGCCCAGCATCTTGCAGAAT
GAGACTTACGGAGCCCTCCTGAGTGGCAGCCCACCTCCCGCCCAGCCTGCAGCCCCCAGC
ACCACCAGCGCCCCCCCGCTTCCTCCACGGAATGTTGGCAAAGTTCAGACAGCCTCCTCT
GCTAACACCCTGTGGAAGACAAACTCTGTAAGTGTGGACGGTGGAAGCCGGCAGCGATCT
TCGTCAGATCCGCCAGCTGTCCATCCACCGCTGCCCCCTCTTCGCGTGACATCTACCAAT
CCCCTGACCCCCACGCCGCCCCCACCCGTTGCCAAGACGCCCAGCGTAATGGAAGCCTTG
AGCCAGCCGAGCAAGCCTGCCCCGCCTGGGATCTCACAGATCAGGCCCCCACCTCTGCCC
CCACAGCCGCCCAGCCGCCTCCCGCAGAAGAAGCCTGCGCCGGGGGCTGACAAGTCCACC
CCACTGACCAACAAAGGCCAACCGAGAGGACCTGTGGATCTCTCTGCAACGGAAGCTCTG
GGTCCTCTGTCCAATGCTATGGTCCTGCAGCCCCCTGCACCCATGCCTAGGAAGTCGCAG
GCAACCAAGTTGAAGCCTAAGCGGGTGAAAGCGCTCTATAACTGTGTGGCTGACAACCCC
GATGAGCTCACCTTCTCCGAGGGGGATGTGATCATCGTGGACGGGGAGGAGGACCAGGAG
TGGTGGATTGGCCACATTGATGGAGATCCTGGTCGCAAAGGCGCATTCCCGGTGTCATTT
GTGCACTTTATCGCTGACTGA
Enzyme 72 GenBank Gene ID NM_003887.2 Link Image
Enzyme 72 GeneCard ID ASAP2 Link Image
Enzyme 72 GenAtlas ID ASAP2 Link Image
Enzyme 72 HGNC ID HGNC:2721 Link Image
Enzyme 72 Chromosome Location 2
Enzyme 72 Locus 2p25|2p24
Enzyme 72 SNPs SNPJam Report Link Image
Enzyme 72 General References
  1. Ishikawa K, Nagase T, Nakajima D, Seki N, Ohira M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1997 Oct 31;4(5):307-13. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Andreev J, Simon JP, Sabatini DD, Kam J, Plowman G, Randazzo PA, Schlessinger J: Identification of a new Pyk2 target protein with Arf-GAP activity. Mol Cell Biol. 1999 Mar;19(3):2338-50. [PubMed Link Image]
  4. Kondo A, Hashimoto S, Yano H, Nagayama K, Mazaki Y, Sabe H: A new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an ADP-ribosylation factor GTPase-activating protein activity, is involved in paxillin recruitment to focal adhesions and cell migration. Mol Biol Cell. 2000 Apr;11(4):1315-27. [PubMed Link Image]
  5. Uchida H, Kondo A, Yoshimura Y, Mazaki Y, Sabe H: PAG3/Papalpha/KIAA0400, a GTPase-activating protein for ADP-ribosylation factor (ARF), regulates ARF6 in Fcgamma receptor-mediated phagocytosis of macrophages. J Exp Med. 2001 Apr 16;193(8):955-66. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 72 Metabolite References Not Available
Enzyme 73 [top]
Enzyme 73 ID 7120
Enzyme 73 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
Enzyme 73 Synonyms
  1. G gamma-I
Enzyme 73 Gene Name GNG2
Enzyme 73 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL
Enzyme 73 Number of Residues 71
Enzyme 73 Molecular Weight 7850.0
Enzyme 73 Theoretical pI 8.22
Enzyme 73 GO Classification
Function
  • molecular transducer activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • extrinsic to membrane
  • extrinsic to plasma membrane
  • heterotrimeric G-protein complex
  • membrane part
Enzyme 73 General Function Involved in signal transducer activity
Enzyme 73 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 73 Pathways Not Available
Enzyme 73 Reactions Not Available
Enzyme 73 Pfam Domain Function
Enzyme 73 Signals
  • None
Enzyme 73 Transmembrane Regions
  • None
Enzyme 73 Essentiality Not Available
Enzyme 73 GenBank ID Protein 20147633 Link Image
Enzyme 73 UniProtKB/Swiss-Prot ID P59768 Link Image
Enzyme 73 UniProtKB/Swiss-Prot Entry Name GBG2_HUMAN Link Image
Enzyme 73 PDB ID 1GP2 Link Image
Enzyme 73 PDB File Show
Enzyme 73 3D Structure
Enzyme 73 Cellular Location Not Available
Enzyme 73 Gene Sequence >216 bp
ATGGCCAGCAACAACACCGCCAGCATAGCACAAGCCAGGAAGCTGGTAGAGCAGCTTAAG
ATGGAAGCCAATATCGACAGGATAAAGGTGTCCAAGGCAGCTGCAGATTTGATGGCCTAC
TGTGAAGCACATGCCAAGGAAGACCCCCTCCTGACCCCTGTTCCGGCTTCAGAAAACCCG
TTTAGGGAGAAGAAGTTTTTCTGTGCCATCCTTTAA
Enzyme 73 GenBank Gene ID AF493870 Link Image
Enzyme 73 GeneCard ID GNG2 Link Image
Enzyme 73 GenAtlas ID GNG2 Link Image
Enzyme 73 HGNC ID HGNC:4404 Link Image
Enzyme 73 Chromosome Location 1
Enzyme 73 Locus 14q21
Enzyme 73 SNPs SNPJam Report Link Image
Enzyme 73 General References
  1. Modarressi MH, Taylor KE, Wolfe J: Cloning, characterization, and mapping of the gene encoding the human G protein gamma 2 subunit. Biochem Biophys Res Commun. 2000 Jun 7;272(2):610-5. [PubMed Link Image]
  2. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 73 Metabolite References Not Available
Enzyme 74 [top]
Enzyme 74 ID 7122
Enzyme 74 Name GTP-binding nuclear protein Ran
Enzyme 74 Synonyms
  1. Androgen receptor-associated protein 24
  2. GTPase Ran
  3. Ras-like protein TC4
  4. Ras-related nuclear protein
Enzyme 74 Gene Name RAN
Enzyme 74 Protein Sequence >GTP-binding nuclear protein Ran
MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIK
FNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC
GNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP
ALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
Enzyme 74 Number of Residues 216
Enzyme 74 Molecular Weight 24423.0
Enzyme 74 Theoretical pI 7.59
Enzyme 74 GO Classification
Function
  • GTP binding
  • GTPase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
  • pyrophosphatase activity
Process
  • biological regulation
  • establishment of localization
  • intracellular protein transport
  • intracellular transport
  • nuclear transport
  • nucleocytoplasmic transport
  • protein transport
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • transport
Component
Enzyme 74 General Function Involved in GTPase activity
Enzyme 74 Specific Function Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases
Enzyme 74 Pathways Not Available
Enzyme 74 Reactions Not Available
Enzyme 74 Pfam Domain Function
Enzyme 74 Signals
  • None
Enzyme 74 Transmembrane Regions
  • None
Enzyme 74 Essentiality Not Available
Enzyme 74 GenBank ID Protein Not Available
Enzyme 74 UniProtKB/Swiss-Prot ID P62826 Link Image
Enzyme 74 UniProtKB/Swiss-Prot Entry Name RAN_HUMAN Link Image
Enzyme 74 PDB ID 1IBR Link Image
Enzyme 74 PDB File Show
Enzyme 74 3D Structure
Enzyme 74 Cellular Location Not Available
Enzyme 74 Gene Sequence >651 bp
ATGGCTGCGCAGGGAGAGCCCCAGGTCCAGTTCAAACTTGTATTGGTTGGTGATGGTGGT
ACTGGAAAAACGACCTTCGTGAAACGTCATTTGACTGGTGAATTTGAGAAGAAGTATGTA
GCCACCTTGGGTGTTGAGGTTCATCCCCTAGTGTTCCACACCAACAGAGGACCTATTAAG
TTCAATGTATGGGACACAGCCGGCCAGGAGAAATTCGGTGGACTGAGAGATGGCTATTAT
ATCCAAGCCCAGTGTGCCATCATAATGTTTGATGTAACATCGAGAGTTACTTACAAGAAT
GTGCCTAACTGGCATAGAGATCTGGTACGAGTGTGTGAAAACATCCCCATTGTGTTGTGT
GGCAACAAAGTGGATATTAAGGACAGGAAAGTGAAGGCGAAATCCATTGTCTTCCACCGA
AAGAAGAATCTTCAGTACTACGACATTTCTGCCAAAAGTAACTACAACTTTGAAAAGCCC
TTCCTCTGGCTTGCTAGGAAGCTCATTGGAGACCCTAACTTGGAATTTGTTGCCATGCCT
GCTCTCGCCCCACCAGAAGTTGTCATGGACCCAGCTTTGGCAGCACAGTATGAGCACGAC
TTAGAGGTTGCTCAGACAACTGCTCTCCCGGATGAGGATGATGACCTGTGA
Enzyme 74 GenBank Gene ID M31469 Link Image
Enzyme 74 GeneCard ID RAN Link Image
Enzyme 74 GenAtlas ID RAN Link Image
Enzyme 74 HGNC ID HGNC:9846 Link Image
Enzyme 74 Chromosome Location 1
Enzyme 74 Locus 12q24.3
Enzyme 74 SNPs SNPJam Report Link Image
Enzyme 74 General References
  1. Drivas GT, Shih A, Coutavas E, Rush MG, D'Eustachio P: Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line. Mol Cell Biol. 1990 Apr;10(4):1793-8. [PubMed Link Image]
  2. Matsumoto T, Beach D: Premature initiation of mitosis in yeast lacking RCC1 or an interacting GTPase. Cell. 1991 Jul 26;66(2):347-60. [PubMed Link Image]
  3. Ren M, Drivas G, D'Eustachio P, Rush MG: Ran/TC4: a small nuclear GTP-binding protein that regulates DNA synthesis. J Cell Biol. 1993 Jan;120(2):313-23. [PubMed Link Image]
  4. Hsiao PW, Lin DL, Nakao R, Chang C: The linkage of Kennedy's neuron disease to ARA24, the first identified androgen receptor polyglutamine region-associated coactivator. J Biol Chem. 1999 Jul 16;274(29):20229-34. [PubMed Link Image]
  5. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Bischoff FR, Ponstingl H: Mitotic regulator protein RCC1 is complexed with a nuclear ras-related polypeptide. Proc Natl Acad Sci U S A. 1991 Dec 1;88(23):10830-4. [PubMed Link Image]
  8. Moroianu J, Blobel G, Radu A: Nuclear protein import: Ran-GTP dissociates the karyopherin alphabeta heterodimer by displacing alpha from an overlapping binding site on beta. Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):7059-62. [PubMed Link Image]
  9. Fornerod M, Ohno M, Yoshida M, Mattaj IW: CRM1 is an export receptor for leucine-rich nuclear export signals. Cell. 1997 Sep 19;90(6):1051-60. [PubMed Link Image]
  10. Askjaer P, Jensen TH, Nilsson J, Englmeier L, Kjems J: The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP. J Biol Chem. 1998 Dec 11;273(50):33414-22. [PubMed Link Image]
  11. Paraskeva E, Izaurralde E, Bischoff FR, Huber J, Kutay U, Hartmann E, Luhrmann R, Gorlich D: CRM1-mediated recycling of snurportin 1 to the cytoplasm. J Cell Biol. 1999 Apr 19;145(2):255-64. [PubMed Link Image]
  12. Englmeier L, Fornerod M, Bischoff FR, Petosa C, Mattaj IW, Kutay U: RanBP3 influences interactions between CRM1 and its nuclear protein export substrates. EMBO Rep. 2001 Oct;2(10):926-32. Epub 2001 Sep 24. [PubMed Link Image]
  13. Lindsay ME, Holaska JM, Welch K, Paschal BM, Macara IG: Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export. J Cell Biol. 2001 Jun 25;153(7):1391-402. [PubMed Link Image]
  14. Zou Y, Lim S, Lee K, Deng X, Friedman E: Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M. J Biol Chem. 2003 Dec 5;278(49):49573-81. Epub 2003 Sep 18. [PubMed Link Image]
  15. Haendeler J, Hoffmann J, Brandes RP, Zeiher AM, Dimmeler S: Hydrogen peroxide triggers nuclear export of telomerase reverse transcriptase via Src kinase family-dependent phosphorylation of tyrosine 707. Mol Cell Biol. 2003 Jul;23(13):4598-610. [PubMed Link Image]
  16. Hakata Y, Yamada M, Shida H: A multifunctional domain in human CRM1 (exportin 1) mediates RanBP3 binding and multimerization of human T-cell leukemia virus type 1 Rex protein. Mol Cell Biol. 2003 Dec;23(23):8751-61. [PubMed Link Image]
  17. Wang D, Li Z, Schoen SR, Messing EM, Wu G: A novel MET-interacting protein shares high sequence similarity with RanBPM, but fails to stimulate MET-induced Ras/Erk signaling. Biochem Biophys Res Commun. 2004 Jan 9;313(2):320-6. [PubMed Link Image]
  18. Petosa C, Schoehn G, Askjaer P, Bauer U, Moulin M, Steuerwald U, Soler-Lopez M, Baudin F, Mattaj IW, Muller CW: Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex. Mol Cell. 2004 Dec 3;16(5):761-75. [PubMed Link Image]
  19. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  20. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed Link Image]
  21. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  22. Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. Epub 2008 Sep 10. [PubMed Link Image]
  23. Xia F, Canovas PM, Guadagno TM, Altieri DC: A survivin-ran complex regulates spindle formation in tumor cells. Mol Cell Biol. 2008 Sep;28(17):5299-311. Epub 2008 Jun 30. [PubMed Link Image]
  24. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  25. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  26. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  27. Scheffzek K, Klebe C, Fritz-Wolf K, Kabsch W, Wittinghofer A: Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form. Nature. 1995 Mar 23;374(6520):378-81. [PubMed Link Image]
  28. Chook YM, Blobel G: Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp. Nature. 1999 May 20;399(6733):230-7. [PubMed Link Image]
  29. Vetter IR, Nowak C, Nishimoto T, Kuhlmann J, Wittinghofer A: Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport. Nature. 1999 Mar 4;398(6722):39-46. [PubMed Link Image]
Enzyme 74 Metabolite References Not Available
Enzyme 75 [top]
Enzyme 75 ID 7131
Enzyme 75 Name Ras-related C3 botulinum toxin substrate 1
Enzyme 75 Synonyms
  1. Cell migration-inducing gene 5 protein
  2. Ras-like protein TC25
  3. p21-Rac1
Enzyme 75 Gene Name RAC1
Enzyme 75 Protein Sequence >Ras-related C3 botulinum toxin substrate 1
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAG
QEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLR
DDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPP
PVKKRKRKCLLL
Enzyme 75 Number of Residues 192
Enzyme 75 Molecular Weight 21449.9
Enzyme 75 Theoretical pI 8.65
Enzyme 75 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 75 General Function Involved in GTP binding
Enzyme 75 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 75 Pathways Not Available
Enzyme 75 Reactions Not Available
Enzyme 75 Pfam Domain Function
Enzyme 75 Signals
  • None
Enzyme 75 Transmembrane Regions
  • None
Enzyme 75 Essentiality Not Available
Enzyme 75 GenBank ID Protein Not Available
Enzyme 75 UniProtKB/Swiss-Prot ID P63000 Link Image
Enzyme 75 UniProtKB/Swiss-Prot Entry Name RAC1_HUMAN Link Image
Enzyme 75 PDB ID 1I4L Link Image
Enzyme 75 PDB File Show
Enzyme 75 3D Structure
Enzyme 75 Cellular Location Not Available
Enzyme 75 Gene Sequence >579 bp
ATGCAGGCCATCAAGTGTGTGGTGGTGGGAGACGGAGCTGTAGGTAAAACTTGCCTACTG
ATCAGTTACACAACCAATGCATTTCCTGGAGAATATATCCCTACTGTCTTTGACAATTAT
TCTGCCAATGTTATGGTAGATGGAAAACCGGTGAATCTGGGCTTATGGGATACAGCTGGA
CAAGAAGATTATGACAGATTACGCCCCCTATCCTATCCGCAAACAGATGTGTTCTTAATT
TGCTTTTCCCTTGTGAGTCCTGCATCATTTGAAAATGTCCGTGCAAAGTGGTATCCTGAG
GTGCGGCACCACTGTCCCAACACTCCCATCATCCTAGTGGGAACTAAACTTGATCTTAGG
GATGATAAAGACACGATCGAGAAACTGAAGGAGAAGAAGCTGACTCCCATCACCTATCCG
CAGGGTCTAGCCATGGCTAAGGAGATTGGTGCTGTAAAATACCTGGAGTGCTCGGCGCTC
ACACAGCGAGGCCTCAAGACAGTGTTTGACGAAGCGATCCGAGCAGTCCTCTGCCCGCCT
CCCGTGAAGAAGAGGAAGAGAAAATGCCTGCTGTTGTAA
Enzyme 75 GenBank Gene ID M29870 Link Image
Enzyme 75 GeneCard ID RAC1 Link Image
Enzyme 75 GenAtlas ID RAC1 Link Image
Enzyme 75 HGNC ID HGNC:9801 Link Image
Enzyme 75 Chromosome Location 7
Enzyme 75 Locus 7p22
Enzyme 75 SNPs SNPJam Report Link Image
Enzyme 75 General References
  1. Didsbury J, Weber RF, Bokoch GM, Evans T, Snyderman R: rac, a novel ras-related family of proteins that are botulinum toxin substrates. J Biol Chem. 1989 Oct 5;264(28):16378-82. [PubMed Link Image]
  2. Drivas GT, Shih A, Coutavas E, Rush MG, D'Eustachio P: Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line. Mol Cell Biol. 1990 Apr;10(4):1793-8. [PubMed Link Image]
  3. Matos P, Skaug J, Marques B, Beck S, Verissimo F, Gespach C, Boavida MG, Scherer SW, Jordan P: Small GTPase Rac1: structure, localization, and expression of the human gene. Biochem Biophys Res Commun. 2000 Nov 2;277(3):741-51. [PubMed Link Image]
  4. Jordan P, Brazao R, Boavida MG, Gespach C, Chastre E: Cloning of a novel human Rac1b splice variant with increased expression in colorectal tumors. Oncogene. 1999 Nov 18;18(48):6835-9. [PubMed Link Image]
  5. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Kinsella BT, Erdman RA, Maltese WA: Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA. J Biol Chem. 1991 May 25;266(15):9786-94. [PubMed Link Image]
  8. Ridley AJ, Paterson HF, Johnston CL, Diekmann D, Hall A: The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell. 1992 Aug 7;70(3):401-10. [PubMed Link Image]
  9. Jullien-Flores V, Dorseuil O, Romero F, Letourneur F, Saragosti S, Berger R, Tavitian A, Gacon G, Camonis JH: Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity. J Biol Chem. 1995 Sep 22;270(38):22473-7. [PubMed Link Image]
  10. Ren Y, Li R, Zheng Y, Busch H: Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases. J Biol Chem. 1998 Dec 25;273(52):34954-60. [PubMed Link Image]
  11. Nishihara H, Kobayashi S, Hashimoto Y, Ohba F, Mochizuki N, Kurata T, Nagashima K, Matsuda M: Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins. Biochim Biophys Acta. 1999 Nov 11;1452(2):179-87. [PubMed Link Image]
  12. Johansson A, Driessens M, Aspenstrom P: The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1. J Cell Sci. 2000 Sep;113 ( Pt 18):3267-75. [PubMed Link Image]
  13. Miki H, Yamaguchi H, Suetsugu S, Takenawa T: IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature. 2000 Dec 7;408(6813):732-5. [PubMed Link Image]
  14. Vikis HG, Li W, He Z, Guan KL: The semaphorin receptor plexin-B1 specifically interacts with active Rac in a ligand-dependent manner. Proc Natl Acad Sci U S A. 2000 Nov 7;97(23):12457-62. [PubMed Link Image]
  15. Noda Y, Takeya R, Ohno S, Naito S, Ito T, Sumimoto H: Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C. Genes Cells. 2001 Feb;6(2):107-19. [PubMed Link Image]
  16. Welch HC, Coadwell WJ, Ellson CD, Ferguson GJ, Andrews SR, Erdjument-Bromage H, Tempst P, Hawkins PT, Stephens LR: P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-nucleotide exchange factor for Rac. Cell. 2002 Mar 22;108(6):809-21. [PubMed Link Image]
  17. Brugnera E, Haney L, Grimsley C, Lu M, Walk SF, Tosello-Trampont AC, Macara IG, Madhani H, Fink GR, Ravichandran KS: Unconventional Rac-GEF activity is mediated through the Dock180-ELMO complex. Nat Cell Biol. 2002 Aug;4(8):574-82. [PubMed Link Image]
  18. Takeya R, Ueno N, Kami K, Taura M, Kohjima M, Izaki T, Nunoi H, Sumimoto H: Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases. J Biol Chem. 2003 Jul 4;278(27):25234-46. Epub 2003 Apr 25. [PubMed Link Image]
  19. Masuda-Robens JM, Kutney SN, Qi H, Chou MM: The TRE17 oncogene encodes a component of a novel effector pathway for Rho GTPases Cdc42 and Rac1 and stimulates actin remodeling. Mol Cell Biol. 2003 Mar;23(6):2151-61. [PubMed Link Image]
  20. Li W, Guan KL: The Down syndrome cell adhesion molecule (DSCAM) interacts with and activates Pak. J Biol Chem. 2004 Jul 30;279(31):32824-31. Epub 2004 May 28. [PubMed Link Image]
  21. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed Link Image]
  22. Watabe-Uchida M, John KA, Janas JA, Newey SE, Van Aelst L: The Rac activator DOCK7 regulates neuronal polarity through local phosphorylation of stathmin/Op18. Neuron. 2006 Sep 21;51(6):727-39. [PubMed Link Image]
  23. Oka T, Ihara S, Fukui Y: Cooperation of DEF6 with activated Rac in regulating cell morphology. J Biol Chem. 2007 Jan 19;282(3):2011-8. Epub 2006 Nov 22. [PubMed Link Image]
  24. Millard TH, Dawson J, Machesky LM: Characterisation of IRTKS, a novel IRSp53/MIM family actin regulator with distinct filament bundling properties. J Cell Sci. 2007 May 1;120(Pt 9):1663-72. Epub 2007 Apr 12. [PubMed Link Image]
  25. Lores P, Visvikis O, Luna R, Lemichez E, Gacon G: The SWI/SNF protein BAF60b is ubiquitinated through a signalling process involving Rac GTPase and the RING finger protein Unkempt. FEBS J. 2010 Mar;277(6):1453-64. Epub 2010 Feb 8. [PubMed Link Image]
  26. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  27. Worby CA, Mattoo S, Kruger RP, Corbeil LB, Koller A, Mendez JC, Zekarias B, Lazar C, Dixon JE: The fic domain: regulation of cell signaling by adenylylation. Mol Cell. 2009 Apr 10;34(1):93-103. [PubMed Link Image]
  28. Yarbrough ML, Li Y, Kinch LN, Grishin NV, Ball HL, Orth K: AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science. 2009 Jan 9;323(5911):269-72. Epub 2008 Nov 27. [PubMed Link Image]
  29. Frasa MA, Maximiano FC, Smolarczyk K, Francis RE, Betson ME, Lozano E, Goldenring J, Seabra MC, Rak A, Ahmadian MR, Braga VM: Armus is a Rac1 effector that inactivates Rab7 and regulates E-cadherin degradation. Curr Biol. 2010 Feb 9;20(3):198-208. Epub 2010 Jan 28. [PubMed Link Image]
  30. Hirshberg M, Stockley RW, Dodson G, Webb MR: The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue. Nat Struct Biol. 1997 Feb;4(2):147-52. [PubMed Link Image]
  31. Lapouge K, Smith SJ, Walker PA, Gamblin SJ, Smerdon SJ, Rittinger K: Structure of the TPR domain of p67phox in complex with Rac.GTP. Mol Cell. 2000 Oct;6(4):899-907. [PubMed Link Image]
  32. Worthylake DK, Rossman KL, Sondek J: Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1. Nature. 2000 Dec 7;408(6813):682-8. [PubMed Link Image]
  33. Stebbins CE, Galan JE: Modulation of host signaling by a bacterial mimic: structure of the Salmonella effector SptP bound to Rac1. Mol Cell. 2000 Dec;6(6):1449-60. [PubMed Link Image]
  34. Wurtele M, Wolf E, Pederson KJ, Buchwald G, Ahmadian MR, Barbieri JT, Wittinghofer A: How the Pseudomonas aeruginosa ExoS toxin downregulates Rac. Nat Struct Biol. 2001 Jan;8(1):23-6. [PubMed Link Image]
  35. Grizot S, Faure J, Fieschi F, Vignais PV, Dagher MC, Pebay-Peyroula E: Crystal structure of the Rac1-RhoGDI complex involved in nadph oxidase activation. Biochemistry. 2001 Aug 28;40(34):10007-13. [PubMed Link Image]
  36. Tarricone C, Xiao B, Justin N, Walker PA, Rittinger K, Gamblin SJ, Smerdon SJ: The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways. Nature. 2001 May 10;411(6834):215-9. [PubMed Link Image]
  37. Fiegen D, Haeusler LC, Blumenstein L, Herbrand U, Dvorsky R, Vetter IR, Ahmadian MR: Alternative splicing of Rac1 generates Rac1b, a self-activating GTPase. J Biol Chem. 2004 Feb 6;279(6):4743-9. Epub 2003 Nov 18. [PubMed Link Image]
  38. Prehna G, Ivanov MI, Bliska JB, Stebbins CE: Yersinia virulence depends on mimicry of host Rho-family nucleotide dissociation inhibitors. Cell. 2006 Sep 8;126(5):869-80. [PubMed Link Image]
  39. Jezyk MR, Snyder JT, Gershberg S, Worthylake DK, Harden TK, Sondek J: Crystal structure of Rac1 bound to its effector phospholipase C-beta2. Nat Struct Mol Biol. 2006 Dec;13(12):1135-40. Epub 2006 Nov 19. [PubMed Link Image]
Enzyme 75 Metabolite References Not Available
Enzyme 76 [top]
Enzyme 76 ID 7132
Enzyme 76 Name Rap1 GTPase-GDP dissociation stimulator 1
Enzyme 76 Synonyms
  1. Exchange factor smgGDS
  2. SMG GDS protein
  3. SMG P21 stimulatory GDP/GTP exchange protein
Enzyme 76 Gene Name RAP1GDS1
Enzyme 76 Protein Sequence >Rap1 GTPase-GDP dissociation stimulator 1
MDNLSDTLKKLKITAVDKTEDSLEGCLDCLLQALAQNNTETSEKIQASGILQLFASLLTP
QSSCKAKVANIIAEVAKNEFMRIPCVDAGLISPLVQLLNSKDQEVLLQTGRALGNICYDS
HEGRSAVDQAGGAQIVIDHLRSLCSITDPANEKLLTVFCGMLMNYSNENDSLQAQLINMG
VIPTLVKLLGIHCQNAALTEMCLVAFGNLAELESSKEQFASTNIAEELVKLFKKQIEHDK
REMIFEVLAPLAENDAIKLQLVEAGLVECLLEIVQQKVDSDKEDDITELKTGSDLMVLLL
LGDESMQKLFEGGKGSVFQRVLSWIPSNNHQLQLAGALAIANFARNDANCIHMVDNGIVE
KLMDLLDRHVEDGNVTVQHAALSALRNLAIPVINKAKMLSAGVTEAVLKFLKSEMPPVQF
KLLGTLRMLIDAQAEAAEQLGKNVKLVERLVEWCEAKDHAGVMGESNRLLSALIRHSKSK
DVIKTIVQSGGIKHLVTMATSEHVIMQNEALVALALIAALELGTAEKDLESAKLVQILHR
LLADERSAPEIKYNSMVLICALMGSECLHKEVQDLAFLDVVSKLRSHENKSVAQQASLTE
QRLTVES
Enzyme 76 Number of Residues 607
Enzyme 76 Molecular Weight 66316.2
Enzyme 76 Theoretical pI 4.97
Enzyme 76 GO Classification
Function
  • binding
Process
Component
Enzyme 76 General Function Involved in binding
Enzyme 76 Specific Function Stimulates GDP/GTP exchange reaction of a group of small GTP-binding proteins (G proteins) including Rap1a/Rap1b, RhoA, RhoB and KRas, by stimulating the dissociation of GDP from and the subsequent binding of GTP to each small G protein
Enzyme 76 Pathways Not Available
Enzyme 76 Reactions Not Available
Enzyme 76 Pfam Domain Function
Enzyme 76 Signals
  • None
Enzyme 76 Transmembrane Regions
  • None
Enzyme 76 Essentiality Not Available
Enzyme 76 GenBank ID Protein 155030196 Link Image
Enzyme 76 UniProtKB/Swiss-Prot ID P52306 Link Image
Enzyme 76 UniProtKB/Swiss-Prot Entry Name GDS1_HUMAN Link Image
Enzyme 76 PDB ID Not Available
Enzyme 76 Cellular Location Not Available
Enzyme 76 Gene Sequence >1824 bp
ATGGATAATCTCAGTGATACCTTGAAGAAGCTGAAGATAACAGCTGTTGACAAGACTGAG
GATAGTTTAGAAGGATGCTTGGATTGTCTGCTTCAAGCCCTGGCTCAAAATAATACGGAA
ACAAGTGAAAAAATCCAAGCAAGTGGAATACTTCAGCTGTTTGCAAGTCTGTTGACTCCA
CAGTCTTCCTGCAAAGCCAAAGTAGCTAACATCATAGCAGAAGTAGCCAAAAATGAGTTT
ATGCGAATTCCATGTGTGGATGCTGGATTGATTTCACCACTGGTGCAGCTGCTAAATAGC
AAAGACCAGGAAGTGCTGCTTCAAACGGGCAGGGCTCTAGGAAACATATGTTACGATAGC
CATGAGGGCAGAAGTGCAGTTGACCAAGCAGGTGGTGCACAGATTGTAATTGACCATTTA
AGGTCACTGTGCAGTATAACAGATCCCGCCAATGAGAAGCTCTTGACTGTCTTTTGTGGC
ATGCTGATGAACTATAGCAATGAGAATGATTCGCTTCAAGCTCAGCTTATCAATATGGGT
GTTATTCCTACCTTAGTGAAATTACTGGGCATCCACTGCCAAAATGCAGCTCTTACAGAA
ATGTGTCTTGTTGCATTTGGTAATTTAGCAGAACTTGAGTCAAGTAAAGAACAGTTTGCC
AGTACAAACATTGCTGAAGAGCTAGTAAAACTCTTCAAGAAACAAATAGAACATGATAAG
AGAGAAATGATTTTTGAAGTTCTTGCTCCATTGGCAGAAAATGATGCTATTAAACTACAG
CTGGTTGAAGCAGGCCTAGTAGAGTGTCTACTAGAGATTGTTCAGCAAAAAGTGGATAGT
GACAAAGAAGATGATATTACTGAGCTCAAAACTGGTTCAGATCTCATGGTTTTATTACTT
CTTGGAGATGAATCCATGCAGAAGTTATTTGAAGGAGGAAAAGGTAGTGTATTTCAAAGG
GTACTCTCTTGGATCCCATCAAATAACCACCAGCTACAGCTTGCTGGAGCATTGGCAATT
GCAAATTTTGCCAGAAATGATGCAAATTGTATTCATATGGTAGACAATGGGATTGTAGAA
AAACTTATGGATTTACTGGACAGACATGTAGAAGATGGAAATGTAACAGTACAGCATGCA
GCACTAAGTGCCCTCAGAAACCTGGCCATTCCAGTTATAAATAAAGCAAAGATGTTATCA
GCTGGGGTCACAGAGGCAGTTTTGAAATTTCTTAAATCTGAAATGCCTCCTGTTCAGTTC
AAACTTCTGGGAACATTAAGAATGTTAATAGATGCACAAGCAGAAGCTGCTGAACAATTG
GGAAAGAATGTTAAGTTAGTGGAGCGTTTGGTGGAATGGTGTGAAGCCAAAGATCATGCT
GGTGTGATGGGGGAGTCAAACAGACTGCTGTCTGCCCTTATACGACACAGTAAATCAAAA
GATGTAATTAAAACCATTGTGCAGAGTGGTGGCATCAAGCATCTAGTTACCATGGCAACT
AGTGAACATGTAATAATGCAGAATGAAGCTCTTGTTGCTTTGGCATTAATAGCAGCTTTA
GAATTGGGCACTGCTGAGAAAGATCTAGAAAGTGCTAAACTTGTACAGATTTTACATAGA
CTGCTAGCAGATGAGAGAAGTGCTCCTGAAATCAAATATAATTCCATGGTCCTGATATGT
GCTCTTATGGGATCTGAATGTCTACACAAGGAAGTACAGGATTTGGCTTTTCTAGATGTC
GTATCCAAACTTCGCAGTCATGAGAACAAAAGTGTTGCCCAGCAGGCCTCTCTCACAGAG
CAGAGACTTACTGTGGAAAGCTGA
Enzyme 76 GenBank Gene ID NM_001100427.1 Link Image
Enzyme 76 GeneCard ID RAP1GDS1 Link Image
Enzyme 76 GenAtlas ID RAP1GDS1 Link Image
Enzyme 76 HGNC ID HGNC:9859 Link Image
Enzyme 76 Chromosome Location 4
Enzyme 76 Locus 4q23-q25
Enzyme 76 SNPs SNPJam Report Link Image
Enzyme 76 General References
  1. Kikuchi A, Kaibuchi K, Hori Y, Nonaka H, Sakoda T, Kawamura M, Mizuno T, Takai Y: Molecular cloning of the human cDNA for a stimulatory GDP/GTP exchange protein for c-Ki-ras p21 and smg p21. Oncogene. 1992 Feb;7(2):289-93. [PubMed Link Image]
  2. Vikis HG, Stewart S, Guan KL: SmgGDS displays differential binding and exchange activity towards different Ras isoforms. Oncogene. 2002 Apr 4;21(15):2425-32. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 76 Metabolite References Not Available
Enzyme 77 [top]
Enzyme 77 ID 7133
Enzyme 77 Name Rho GDP-dissociation inhibitor 3
Enzyme 77 Synonyms
  1. Rho GDI 3
  2. Rho-GDI gamma
Enzyme 77 Gene Name ARHGDIG
Enzyme 77 Protein Sequence >Rho GDP-dissociation inhibitor 3
MLGLDACELGAQLLELLRLALCARVLLADKEGGPPAVDEVLDEAVPEYRAPGRKSLLEIR
QLDPDDRSLAKYKRVLLGPLPPAVDPSLPNVQVTRLTLLSEQAPGPVVMDLTGDLAVLKD
QVFVLKEGVDYRVKISFKVHREIVSGLKCLHHTYRRGLRVDKTVYMVGSYGPSAQEYEFV
TPVEEAPRGALVRGPYLVVSLFTDDDRTHHLSWEWGLCICQDWKD
Enzyme 77 Number of Residues 225
Enzyme 77 Molecular Weight 25097.8
Enzyme 77 Theoretical pI 5.37
Enzyme 77 GO Classification
Function
  • GDP-dissociation inhibitor activity
  • GTPase regulator activity
  • Rho GDP-dissociation inhibitor activity
  • enzyme regulator activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 77 General Function Involved in Rho GDP-dissociation inhibitor activity
Enzyme 77 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 77 Pathways Not Available
Enzyme 77 Reactions Not Available
Enzyme 77 Pfam Domain Function
Enzyme 77 Signals
  • None
Enzyme 77 Transmembrane Regions
  • None
Enzyme 77 Essentiality Not Available
Enzyme 77 GenBank ID Protein 82941188 Link Image
Enzyme 77 UniProtKB/Swiss-Prot ID Q99819 Link Image
Enzyme 77 UniProtKB/Swiss-Prot Entry Name GDIR3_HUMAN Link Image
Enzyme 77 PDB ID Not Available
Enzyme 77 Cellular Location Not Available
Enzyme 77 Gene Sequence >678 bp
ATGCTGGGCCTGGACGCGTGCGAGCTGGGGGCGCAGCTGCTGGAGCTGCTCCGGCTGGCG
CTGTGCGCCCGAGTCCTCCTGGCTGACAAGGAGGGTGGGCCGCCGGCAGTGGACGAGGTG
TTGGATGAGGCTGTGCCCGAGTACCGGGCGCCGGGGAGGAAGAGCCTCTTGGAGATCCGG
CAGCTGGACCCGGACGACAGGAGCCTGGCCAAGTACAAGCGGGTGCTGCTGGGGCCCCTG
CCACCGGCCGTGGACCCAAGCCTGCCCAATGTGCAGGTGACCAGGCTGACACTCCTGTCG
GAACAGGCTCCGGGGCCCGTCGTCATGGATCTCACAGGGGACCTGGCTGTTCTGAAGGAC
CAGGTGTTTGTCCTGAAGGAAGGTGTTGATTACAGAGTGAAGATCTCCTTCAAGGTCCAC
AGGGAGATTGTCAGCGGCCTCAAGTGTCTGCACCACACCTACCGCCGGGGCCTGCGCGTG
GACAAGACCGTCTACATGGTGGGCAGCTATGGCCCGAGCGCCCAGGAGTATGAGTTTGTG
ACTCCGGTGGAGGAAGCGCCGAGGGGTGCGCTGGTGCGGGGCCCCTATCTGGTGGTGTCC
CTCTTCACCGACGATGACAGGACGCACCACCTGTCCTGGGAGTGGGGTCTCTGCATCTGC
CAGGACTGGAAGGACTGA
Enzyme 77 GenBank Gene ID AB127078 Link Image
Enzyme 77 GeneCard ID ARHGDIG Link Image
Enzyme 77 GenAtlas ID ARHGDIG Link Image
Enzyme 77 HGNC ID HGNC:680 Link Image
Enzyme 77 Chromosome Location 1
Enzyme 77 Locus 16p13.3
Enzyme 77 SNPs SNPJam Report Link Image
Enzyme 77 General References
  1. Adra CN, Manor D, Ko JL, Zhu S, Horiuchi T, Van Aelst L, Cerione RA, Lim B: RhoGDIgamma: a GDP-dissociation inhibitor for Rho proteins with preferential expression in brain and pancreas. Proc Natl Acad Sci U S A. 1997 Apr 29;94(9):4279-84. [PubMed Link Image]
  2. Adra CN, Iyengar AR, Syed FA, Kanaan IN, Rilo HL, Yu W, Kheraj R, Lin SR, Horiuchi T, Khan S, Weremowicz S, Lim B, Morton CC, Higgs DR: Human ARHGDIG, a GDP-dissociation inhibitor for Rho proteins: genomic structure, sequence, expression analysis, and mapping to chromosome 16p13.3. Genomics. 1998 Oct 1;53(1):104-9. [PubMed Link Image]
  3. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  4. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 77 Metabolite References Not Available
Enzyme 78 [top]
Enzyme 78 ID 7134
Enzyme 78 Name Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Enzyme 78 Synonyms
  1. Adenylate cyclase-stimulating G alpha protein
Enzyme 78 Gene Name GNAS
Enzyme 78 Protein Sequence >Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQM
RILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELA
NPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLD
KIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFND
VTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEK
VLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCY
PHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL
Enzyme 78 Number of Residues 394
Enzyme 78 Molecular Weight 45664.2
Enzyme 78 Theoretical pI 5.56
Enzyme 78 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • molecular transducer activity
  • nucleotide binding
  • purine nucleotide binding
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • biological regulation
  • cell surface receptor linked signaling pathway
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 78 General Function Involved in signal transducer activity
Enzyme 78 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 78 Pathways Not Available
Enzyme 78 Reactions Not Available
Enzyme 78 Pfam Domain Function
Enzyme 78 Signals
  • None
Enzyme 78 Transmembrane Regions
  • None
Enzyme 78 Essentiality Not Available
Enzyme 78 GenBank ID Protein 31915 Link Image
Enzyme 78 UniProtKB/Swiss-Prot ID P63092 Link Image
Enzyme 78 UniProtKB/Swiss-Prot Entry Name GNAS2_HUMAN Link Image
Enzyme 78 PDB ID 1U0H Link Image
Enzyme 78 PDB File Show
Enzyme 78 3D Structure
Enzyme 78 Cellular Location Not Available
Enzyme 78 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 78 GenBank Gene ID X04408 Link Image
Enzyme 78 GeneCard ID GNAS Link Image
Enzyme 78 GenAtlas ID GNAS Link Image
Enzyme 78 HGNC ID HGNC:4392 Link Image
Enzyme 78 Chromosome Location 2
Enzyme 78 Locus 20q13.3
Enzyme 78 SNPs SNPJam Report Link Image
Enzyme 78 General References
  1. Mattera R, Codina J, Crozat A, Kidd V, Woo SL, Birnbaumer L: Identification by molecular cloning of two forms of the alpha-subunit of the human liver stimulatory (GS) regulatory component of adenylyl cyclase. FEBS Lett. 1986 Sep 29;206(1):36-42. [PubMed Link Image]
  2. Harris BA: Complete cDNA sequence of a human stimulatory GTP-binding protein alpha subunit. Nucleic Acids Res. 1988 Apr 25;16(8):3585. [PubMed Link Image]
  3. Kozasa T, Itoh H, Tsukamoto T, Kaziro Y: Isolation and characterization of the human Gs alpha gene. Proc Natl Acad Sci U S A. 1988 Apr;85(7):2081-5. [PubMed Link Image]
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Bray P, Carter A, Simons C, Guo V, Puckett C, Kamholz J, Spiegel A, Nirenberg M: Human cDNA clones for four species of G alpha s signal transduction protein. Proc Natl Acad Sci U S A. 1986 Dec;83(23):8893-7. [PubMed Link Image]
  7. Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed Link Image]
  8. Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. Epub 2008 Sep 10. [PubMed Link Image]
  9. Miric A, Vechio JD, Levine MA: Heterogeneous mutations in the gene encoding the alpha-subunit of the stimulatory G protein of adenylyl cyclase in Albright hereditary osteodystrophy. J Clin Endocrinol Metab. 1993 Jun;76(6):1560-8. [PubMed Link Image]
  10. Schwindinger WF, Francomano CA, Levine MA: Identification of a mutation in the gene encoding the alpha subunit of the stimulatory G protein of adenylyl cyclase in McCune-Albright syndrome. Proc Natl Acad Sci U S A. 1992 Jun 1;89(11):5152-6. [PubMed Link Image]
  11. Weinstein LS, Shenker A, Gejman PV, Merino MJ, Friedman E, Spiegel AM: Activating mutations of the stimulatory G protein in the McCune-Albright syndrome. N Engl J Med. 1991 Dec 12;325(24):1688-95. [PubMed Link Image]
  12. Landis CA, Masters SB, Spada A, Pace AM, Bourne HR, Vallar L: GTPase inhibiting mutations activate the alpha chain of Gs and stimulate adenylyl cyclase in human pituitary tumours. Nature. 1989 Aug 31;340(6236):692-6. [PubMed Link Image]
  13. Schwindinger WF, Miric A, Zimmerman D, Levine MA: A novel Gs alpha mutant in a patient with Albright hereditary osteodystrophy uncouples cell surface receptors from adenylyl cyclase. J Biol Chem. 1994 Oct 14;269(41):25387-91. [PubMed Link Image]
  14. Iiri T, Herzmark P, Nakamoto JM, van Dop C, Bourne HR: Rapid GDP release from Gs alpha in patients with gain and loss of endocrine function. Nature. 1994 Sep 8;371(6493):164-8. [PubMed Link Image]
  15. Gorelov VN, Dumon K, Barteneva NS, Palm D, Roher HD, Goretzki PE: Overexpression of Gs alpha subunit in thyroid tumors bearing a mutated Gs alpha gene. J Cancer Res Clin Oncol. 1995;121(4):219-24. [PubMed Link Image]
  16. Williamson EA, Ince PG, Harrison D, Kendall-Taylor P, Harris PE: G-protein mutations in human pituitary adrenocorticotrophic hormone-secreting adenomas. Eur J Clin Invest. 1995 Feb;25(2):128-31. [PubMed Link Image]
  17. Yang I, Park S, Ryu M, Woo J, Kim S, Kim J, Kim Y, Choi Y: Characteristics of gsp-positive growth hormone-secreting pituitary tumors in Korean acromegalic patients. Eur J Endocrinol. 1996 Jun;134(6):720-6. [PubMed Link Image]
  18. Farfel Z, Iiri T, Shapira H, Roitman A, Mouallem M, Bourne HR: Pseudohypoparathyroidism, a novel mutation in the betagamma-contact region of Gsalpha impairs receptor stimulation. J Biol Chem. 1996 Aug 16;271(33):19653-5. [PubMed Link Image]
  19. Candeliere GA, Roughley PJ, Glorieux FH: Polymerase chain reaction-based technique for the selective enrichment and analysis of mosaic arg201 mutations in G alpha s from patients with fibrous dysplasia of bone. Bone. 1997 Aug;21(2):201-6. [PubMed Link Image]
  20. Warner DR, Gejman PV, Collins RM, Weinstein LS: A novel mutation adjacent to the switch III domain of G(S alpha) in a patient with pseudohypoparathyroidism. Mol Endocrinol. 1997 Oct;11(11):1718-27. [PubMed Link Image]
  21. Iiri T, Farfel Z, Bourne HR: Conditional activation defect of a human Gsalpha mutant. Proc Natl Acad Sci U S A. 1997 May 27;94(11):5656-61. [PubMed Link Image]
  22. Warner DR, Weng G, Yu S, Matalon R, Weinstein LS: A novel mutation in the switch 3 region of Gsalpha in a patient with Albright hereditary osteodystrophy impairs GDP binding and receptor activation. J Biol Chem. 1998 Sep 11;273(37):23976-83. [PubMed Link Image]
  23. Riminucci M, Fisher LW, Majolagbe A, Corsi A, Lala R, De Sanctis C, Robey PG, Bianco P: A novel GNAS1 mutation, R201G, in McCune-albright syndrome. J Bone Miner Res. 1999 Nov;14(11):1987-9. [PubMed Link Image]
  24. Warner DR, Weinstein LS: A mutation in the heterotrimeric stimulatory guanine nucleotide binding protein alpha-subunit with impaired receptor-mediated activation because of elevated GTPase activity. Proc Natl Acad Sci U S A. 1999 Apr 13;96(8):4268-72. [PubMed Link Image]
  25. Liu J, Litman D, Rosenberg MJ, Yu S, Biesecker LG, Weinstein LS: A GNAS1 imprinting defect in pseudohypoparathyroidism type IB. J Clin Invest. 2000 Nov;106(9):1167-74. [PubMed Link Image]
  26. Bastepe M, Lane AH, Juppner H: Paternal uniparental isodisomy of chromosome 20q--and the resulting changes in GNAS1 methylation--as a plausible cause of pseudohypoparathyroidism. Am J Hum Genet. 2001 May;68(5):1283-9. Epub 2001 Apr 9. [PubMed Link Image]
  27. Wu WI, Schwindinger WF, Aparicio LF, Levine MA: Selective resistance to parathyroid hormone caused by a novel uncoupling mutation in the carboxyl terminus of G alpha(s). A cause of pseudohypoparathyroidism type Ib. J Biol Chem. 2001 Jan 5;276(1):165-71. [PubMed Link Image]
  28. Ishikawa Y, Tajima T, Nakae J, Nagashima T, Satoh K, Okuhara K, Fujieda K: Two mutations of the Gsalpha gene in two Japanese patients with sporadic pseudohypoparathyroidism type Ia. J Hum Genet. 2001;46(7):426-30. [PubMed Link Image]
  29. Ahrens W, Hiort O, Staedt P, Kirschner T, Marschke C, Kruse K: Analysis of the GNAS1 gene in Albright's hereditary osteodystrophy. J Clin Endocrinol Metab. 2001 Oct;86(10):4630-4. [PubMed Link Image]
  30. Linglart A, Carel JC, Garabedian M, Le T, Mallet E, Kottler ML: GNAS1 lesions in pseudohypoparathyroidism Ia and Ic: genotype phenotype relationship and evidence of the maternal transmission of the hormonal resistance. J Clin Endocrinol Metab. 2002 Jan;87(1):189-97. [PubMed Link Image]
  31. Lim SH, Poh LK, Cowell CT, Tey BH, Loke KY: Mutational analysis of the GNAS1 exons encoding the stimulatory G protein in five patients with pseudohypoparathyroidism type 1a. J Pediatr Endocrinol Metab. 2002 Mar;15(3):259-68. [PubMed Link Image]
  32. Jan de Beur S, Ding C, Germain-Lee E, Cho J, Maret A, Levine MA: Discordance between genetic and epigenetic defects in pseudohypoparathyroidism type 1b revealed by inconsistent loss of maternal imprinting at GNAS1. Am J Hum Genet. 2003 Aug;73(2):314-22. Epub 2003 Jul 11. [PubMed Link Image]
  33. Rickard SJ, Wilson LC: Analysis of GNAS1 and overlapping transcripts identifies the parental origin of mutations in patients with sporadic Albright hereditary osteodystrophy and reveals a model system in which to observe the effects of splicing mutations on translated and untranslated messenger RNA. Am J Hum Genet. 2003 Apr;72(4):961-74. Epub 2003 Mar 6. [PubMed Link Image]
  34. Pohlenz J, Ahrens W, Hiort O: A new heterozygous mutation (L338N) in the human Gsalpha (GNAS1) gene as a cause for congenital hypothyroidism in Albright's hereditary osteodystrophy. Eur J Endocrinol. 2003 Apr;148(4):463-8. [PubMed Link Image]
  35. Fragoso MC, Domenice S, Latronico AC, Martin RM, Pereira MA, Zerbini MC, Lucon AM, Mendonca BB: Cushing's syndrome secondary to adrenocorticotropin-independent macronodular adrenocortical hyperplasia due to activating mutations of GNAS1 gene. J Clin Endocrinol Metab. 2003 May;88(5):2147-51. [PubMed Link Image]
  36. Bastepe M, Frohlich LF, Hendy GN, Indridason OS, Josse RG, Koshiyama H, Korkko J, Nakamoto JM, Rosenbloom AL, Slyper AH, Sugimoto T, Tsatsoulis A, Crawford JD, Juppner H: Autosomal dominant pseudohypoparathyroidism type Ib is associated with a heterozygous microdeletion that likely disrupts a putative imprinting control element of GNAS. J Clin Invest. 2003 Oct;112(8):1255-63. [PubMed Link Image]
  37. Chan I, Hamada T, Hardman C, McGrath JA, Child FJ: Progressive osseous heteroplasia resulting from a new mutation in the GNAS1 gene. Clin Exp Dermatol. 2004 Jan;29(1):77-80. [PubMed Link Image]
  38. Linglart A, Gensure RC, Olney RC, Juppner H, Bastepe M: A novel STX16 deletion in autosomal dominant pseudohypoparathyroidism type Ib redefines the boundaries of a cis-acting imprinting control element of GNAS. Am J Hum Genet. 2005 May;76(5):804-14. Epub 2005 Mar 30. [PubMed Link Image]
  39. Riepe FG, Ahrens W, Krone N, Folster-Holst R, Brasch J, Sippell WG, Hiort O, Partsch CJ: Early manifestation of calcinosis cutis in pseudohypoparathyroidism type Ia associated with a novel mutation in the GNAS gene. Eur J Endocrinol. 2005 Apr;152(4):515-9. [PubMed Link Image]
  40. Bastepe M, Frohlich LF, Linglart A, Abu-Zahra HS, Tojo K, Ward LM, Juppner H: Deletion of the NESP55 differentially methylated region causes loss of maternal GNAS imprints and pseudohypoparathyroidism type Ib. Nat Genet. 2005 Jan;37(1):25-7. Epub 2004 Dec 12. [PubMed Link Image]
Enzyme 78 Metabolite References Not Available
Enzyme 79 [top]
Enzyme 79 ID 7135
Enzyme 79 Name Rab GDP dissociation inhibitor alpha
Enzyme 79 Synonyms
  1. Rab GDI alpha
  2. Guanosine diphosphate dissociation inhibitor 1
  3. GDI-1
  4. Oligophrenin-2
  5. Protein XAP-4
Enzyme 79 Gene Name GDI1
Enzyme 79 Protein Sequence >Rab GDP dissociation inhibitor alpha
MDEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDRNPYYGGESSSITPLEELYKRFQLLE
GPPESMGRGRDWNVDLIPKFLMANGQLVKMLLYTEVTRYLDFKVVEGSFVYKGGKIYKVP
STETEALASNLMGMFEKRRFRKFLVFVANFDENDPKTFEGVDPQTTSMRDVYRKFDLGQD
VIDFTGHALALYRTDDYLDQPCLETVNRIKLYSESLARYGKSPYLYPLYGLGELPQGFAR
LSAIYGGTYMLNKPVDDIIMENGKVVGVKSEGEVARCKQLICDPSYIPDRVRKAGQVIRI
ICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISYAHNVAAQGKYIAIASTTVETT
DPEKEVEPALELLEPIDQKFVAISDLYEPIDDGCESQVFCSCSYDATTHFETTCNDIKDI
YKRMAGTAFDFENMKRKQNDVFGEAEQ
Enzyme 79 Number of Residues 447
Enzyme 79 Molecular Weight 50582.3
Enzyme 79 Theoretical pI 4.75
Enzyme 79 GO Classification
Function
  • GDP-dissociation inhibitor activity
  • GTPase regulator activity
  • Rab GDP-dissociation inhibitor activity
  • enzyme regulator activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
  • biological regulation
  • establishment of localization
  • protein transport
  • regulation of GTP catabolic process
  • regulation of GTPase activity
  • regulation of biological process
  • regulation of cellular metabolic process
  • regulation of metabolic process
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • regulation of nucleotide catabolic process
  • regulation of nucleotide metabolic process
  • regulation of purine nucleotide catabolic process
  • transport
Component
Enzyme 79 General Function Involved in regulation of GTPase activity
Enzyme 79 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 79 Pathways Not Available
Enzyme 79 Reactions Not Available
Enzyme 79 Pfam Domain Function
Enzyme 79 Signals
  • None
Enzyme 79 Transmembrane Regions
  • None
Enzyme 79 Essentiality Not Available
Enzyme 79 GenBank ID Protein 695585 Link Image
Enzyme 79 UniProtKB/Swiss-Prot ID P31150 Link Image
Enzyme 79 UniProtKB/Swiss-Prot Entry Name GDIA_HUMAN Link Image
Enzyme 79 PDB ID 1GND Link Image
Enzyme 79 PDB File Show
Enzyme 79 3D Structure
Enzyme 79 Cellular Location Not Available
Enzyme 79 Gene Sequence >1344 bp
ATGGACGAGGAATACGATGTGATCGTGCTGGGGACCGGTCTCACCGAATGCATCCTGTCG
GGCATCATGTCTGTGAACGGGAAGAAGGTGCTGCACATGGACCGGAACCCCTACTACGGG
GGCGAGAGCTCCTCCATCACACCCCTGGAGGAGCTGTATAAGCGTTTTCAGTTGCTGGAG
GGGCCCCCTGAGTCGATGGGCCGAGGCCGAGACTGGAATGTTGACCTGATTCCCAAATTC
CTCATGGCTAACGGGCAGCTGGTAAAGATGCTACTGTATACAGAGGTGACTCGCTACCTG
GACTTCAAGGTGGTGGAGGGCAGCTTTGTCTACAAGGGGGGCAAGATCTACAAAGTGCCG
TCCACTGAGACTGAGGCCTTGGCTTCCAATCTGATGGGCATGTTTGAGAAACGGCGCTTC
CGCAAGTTCCTGGTGTTTGTGGCAAACTTCGATGAGAATGACCCCAAGACCTTTGAGGGC
GTTGACCCCCAGACTACCAGCATGCGTGACGTCTACCGGAAGTTTGATCTGGGCCAGGAT
GTCATCGATTTCACTGGCCATGCCCTGGCGCTCTACCGCACTGATGACTACCTGGACCAG
CCCTGCCTTGAGACCGTCAACCGCATCAAGTTGTACAGTGAGTCCCTGGCCCGGTATGGC
AAGAGCCCATATTTATACCCGCTCTACGGCTTGGGCGAGCTGCCCCAGGGTTTTGCAAGA
TTGAGTGCCATCTATGGGGGGACATATATGCTGAACAAACCTGTGGATGACATCATCATG
GAGAACGGCAAGGTGGTGGGCGTGAAGTCTGAGGGAGAGGTGGCCCGCTGCAAGCAGCTG
ATCTGTGACCCCAGCTACATCCCGGACCGTGTGCGGAAGGCTGGCCAGGTTATCCGCATC
ATCTGTATCCTTAGCCACCCCATCAAGAACACCAACGACGCCAACTCCTGCCAAATAATC
ATCCCCCAGAACCAGGTCAACAGGAAGTCAGACATCTACGTGTGCATGATCTCCTATGCA
CACAACGTGGCGGCCCAGGGCAAGTACATAGCTATTGCCAGCACTACTGTGGAGACCACG
GACCCTGAAAAGGAGGTGGAGCCGGCTCTGGAGCTGTTGGAGCCCATTGACCAGAAGTTT
GTGGCTATCAGTGACTTGTATGAGCCCATTGATGATGGTTGTGAGAGCCAGGTGTTCTGT
TCCTGCTCCTACGATGCCACCACACACTTTGAGACAACCTGCAACGACATCAAAGACATC
TACAAACGCATGGCTGGCACGGCCTTTGACTTTGAGAACATGAAGCGCAAACAGAACGAC
GTCTTTGGAGAAGCTGAGCAGTGA
Enzyme 79 GenBank Gene ID X79353 Link Image
Enzyme 79 GeneCard ID GDI1 Link Image
Enzyme 79 GenAtlas ID GDI1 Link Image
Enzyme 79 HGNC ID HGNC:4226 Link Image
Enzyme 79 Chromosome Location Not Available
Enzyme 79 Locus Not Available
Enzyme 79 SNPs SNPJam Report Link Image
Enzyme 79 General References
  1. Sedlacek Z, Konecki DS, Korn B, Klauck SM, Poustka A: Evolutionary conservation and genomic organization of XAP-4, an Xq28 located gene coding for a human rab GDP-dissociation inhibitor (GDI). Mamm Genome. 1994 Oct;5(10):633-9. [PubMed Link Image]
  2. Nishimura N, Goji J, Nakamura H, Orita S, Takai Y, Sano K: Cloning of a brain-type isoform of human Rab GDI and its expression in human neuroblastoma cell lines and tumor specimens. Cancer Res. 1995 Nov 15;55(22):5445-50. [PubMed Link Image]
  3. Chen EY, Zollo M, Mazzarella R, Ciccodicola A, Chen CN, Zuo L, Heiner C, Burough F, Repetto M, Schlessinger D, D'Urso M: Long-range sequence analysis in Xq28: thirteen known and six candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci. Hum Mol Genet. 1996 May;5(5):659-68. [PubMed Link Image]
  4. Kitano T, Schwarz C, Nickel B, Paabo S: Gene diversity patterns at 10 X-chromosomal loci in humans and chimpanzees. Mol Biol Evol. 2003 Aug;20(8):1281-9. Epub 2003 May 30. [PubMed Link Image]
  5. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. Electrophoresis. 1992 Dec;13(12):960-9. [PubMed Link Image]
  8. Bachner D, Sedlacek Z, Korn B, Hameister H, Poustka A: Expression patterns of two human genes coding for different rab GDP-dissociation inhibitors (GDIs), extremely conserved proteins involved in cellular transport. Hum Mol Genet. 1995 Apr;4(4):701-8. [PubMed Link Image]
  9. Li X, Bu X, Lu B, Avraham H, Flavell RA, Lim B: The hematopoiesis-specific GTP-binding protein RhoH is GTPase deficient and modulates activities of other Rho GTPases by an inhibitory function. Mol Cell Biol. 2002 Feb;22(4):1158-71. [PubMed Link Image]
  10. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  11. D'Adamo P, Menegon A, Lo Nigro C, Grasso M, Gulisano M, Tamanini F, Bienvenu T, Gedeon AK, Oostra B, Wu SK, Tandon A, Valtorta F, Balch WE, Chelly J, Toniolo D: Mutations in GDI1 are responsible for X-linked non-specific mental retardation. Nat Genet. 1998 Jun;19(2):134-9. [PubMed Link Image]
  12. Bienvenu T, des Portes V, Saint Martin A, McDonell N, Billuart P, Carrie A, Vinet MC, Couvert P, Toniolo D, Ropers HH, Moraine C, van Bokhoven H, Fryns JP, Kahn A, Beldjord C, Chelly J: Non-specific X-linked semidominant mental retardation by mutations in a Rab GDP-dissociation inhibitor. Hum Mol Genet. 1998 Aug;7(8):1311-5. [PubMed Link Image]
Enzyme 79 Metabolite References Not Available
Enzyme 80 [top]
Enzyme 80 ID 7136
Enzyme 80 Name Proto-oncogene DBL
Enzyme 80 Synonyms
  1. Proto-oncogene MCF-2
  2. MCF2-transforming protein
  3. DBL-transforming protein
Enzyme 80 Gene Name MCF2
Enzyme 80 Protein Sequence >Proto-oncogene DBL
MAEANPRRGKMRFRRNAASFPGNLHLVLVLRPTSFLQRTFTDIGFWFSQEDFMLKLPVVM
LSSVSDLLTYIDDKQLTPELGGTLQYCHSEWIIFRNAIENFALTVKEMAQMLQSFGTELA
ETELPDDIPSIEEILAIRAERYHLLKNDITAVTKEGKILLTNLEVPDTEGAVSSRLECHR
QISGDWQTINKLLTQVHDMETAFDGFWEKHQLKMEQYLQLWKFEQDFQQLVTEVEFLLNQ
QAELADVTGTIAQVKQKIKKLENLDENSQELLSKAQFVILHGHKLAANHHYALDLICQRC
NELRYLSDILVNEIKAKRIQLSRTFKMHKLLQQARQCCDEGECLLANQEIDKFQSKEDAQ
KALQDIENFLEMALPFINYEPETLQYEFDVILSPELKVQMKTIQLKLENIRSIFENQQAG
FRNLADKHVRPIQFVVPTPENLVTSGTPFFSSKQGKKTWRQNQSNLKIEVVPDCQEKRSS
GPSSSLDNGNSLDVLKNHVLNELIQTERVYVRELYTVLLGYRAEMDNPEMFDLMPPLLRN
KKDILFGNMAEIYEFHNDIFLSSLENCAHAPERVGPCFLERKDDFQMYAKYCQNKPRSET
IWRKYSECAFFQECQRKLKHRLRLDSYLLKPVQRITKYQLLLKELLKYSKDCEGSALLKK
ALDAMLDLLKSVNDSMHQIAINGYIGNLNELGKMIMQGGFSVWIGHKKGATKMKDLARFK
PMQRHLFLYEKAIVFCKRRVESGEGSDRYPSYSFKHCWKMDEVGITEYVKGDNRKFEIWY
GEKEEVYIVQASNVDVKMTWLKEIRNILLKQQELLTVKKRKQQDQLTERDKFQISLQQND
EKQQGAFISTEETELEHTSTVVEVCEAIASVQAEANTVWTEASQSAEISEEPAEWSSNYF
YPTYDENEEENRPLMRPVSEMALLY
Enzyme 80 Number of Residues 925
Enzyme 80 Molecular Weight 107672.4
Enzyme 80 Theoretical pI 5.87
Enzyme 80 GO Classification
Function
  • GTPase regulator activity
  • Ras guanyl-nucleotide exchange factor activity
  • Rho guanyl-nucleotide exchange factor activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
  • biological regulation
  • intracellular signaling pathway
  • regulation of Ras protein signal transduction
  • regulation of Rho protein signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signaling
  • signaling pathway
Component
  • cell part
  • intracellular
Enzyme 80 General Function Involved in protein binding
Enzyme 80 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 80 Pathways Not Available
Enzyme 80 Reactions Not Available
Enzyme 80 Pfam Domain Function
Enzyme 80 Signals
  • None
Enzyme 80 Transmembrane Regions
  • None
Enzyme 80 Essentiality Not Available
Enzyme 80 GenBank ID Protein 153791325 Link Image
Enzyme 80 UniProtKB/Swiss-Prot ID P10911 Link Image
Enzyme 80 UniProtKB/Swiss-Prot Entry Name MCF2_HUMAN Link Image
Enzyme 80 PDB ID Not Available
Enzyme 80 Cellular Location Not Available
Enzyme 80 Gene Sequence >2778 bp
ATGGCAGAAGCAAATCCCCGGAGAGGCAAGATGAGGTTCAGAAGGAATGCGGCTTCCTTC
CCTGGGAACTTGCACTTGGTTTTGGTTTTACGTCCTACCAGCTTTCTTCAACGAACGTTC
ACAGACATTGGATTTTGGTTTAGTCAGGAGGATTTTATGCTTAAATTACCAGTTGTTATG
CTGAGCTCAGTTAGTGATTTGCTGACATACATTGATGACAAGCAATTAACCCCTGAGTTA
GGCGGCACCTTGCAGTACTGCCACAGTGAATGGATCATCTTCAGAAATGCTATAGAAAAT
TTTGCCCTCACAGTGAAAGAAATGGCTCAGATGTTACAGTCCTTTGGAACTGAACTGGCT
GAGACAGAACTACCAGATGATATTCCCTCAATAGAAGAAATTCTGGCAATTCGTGCTGAA
AGGTATCATCTGTTGAAGAATGATATTACAGCTGTAACCAAAGAAGGAAAAATTCTGCTA
ACAAATCTGGAAGTGCCTGACACTGAAGGAGCTGTCAGTTCAAGACTAGAATGTCATCGG
CAAATAAGTGGTGACTGGCAAACTATTAATAAGTTGCTGACTCAAGTACATGATATGGAA
ACAGCTTTTGATGGATTTTGGGAAAAACATCAATTAAAAATGGAGCAGTATCTGCAACTA
TGGAAGTTTGAGCAGGATTTTCAACAGCTTGTGACTGAAGTTGAATTTCTATTAAACCAA
CAAGCAGAACTGGCTGATGTAACAGGGACTATAGCTCAAGTAAAACAAAAAATAAAAAAA
TTGGAAAACTTAGATGAAAATTCTCAGGAGCTATTATCAAAGGCCCAGTTTGTGATATTA
CATGGACACAAGCTTGCAGCAAATCACCATTATGCACTTGATTTAATCTGCCAGAGGTGC
AATGAGCTACGTTACCTTTCTGATATTTTGGTTAATGAGATAAAAGCAAAACGGATACAA
CTCAGCAGGACCTTCAAAATGCATAAACTCCTACAGCAGGCTCGTCAATGCTGTGATGAA
GGGGAATGTCTTCTAGCTAATCAGGAAATAGATAAGTTTCAGTCTAAAGAAGATGCTCAG
AAAGCTCTCCAAGACATTGAAAATTTTCTTGAAATGGCTCTACCCTTTATAAATTATGAA
CCTGAAACACTGCAGTATGAATTTGATGTAATATTATCTCCTGAGCTTAAGGTTCAAATG
AAGACTATACAACTCAAGCTTGAAAACATTCGAAGTATATTTGAGAACCAGCAGGCTGGT
TTCAGGAACCTGGCAGATAAGCATGTGAGGCCAATCCAATTTGTGGTACCCACACCTGAA
AATTTGGTCACATCTGGGACACCATTTTTTTCATCTAAACAAGGGAAGAAGACTTGGAGA
CAAAATCAGAGCAACTTAAAAATTGAAGTGGTGCCTGATTGTCAGGAGAAGAGAAGTTCT
GGTCCATCCTCCAGTTTGGACAATGGCAATAGCTTGGATGTTTTAAAGAACCACGTACTA
AATGAACTGATACAGACTGAGAGAGTTTATGTTCGAGAACTGTATACTGTTTTGTTGGGT
TATAGAGCGGAGATGGATAATCCAGAGATGTTTGATCTTATGCCACCTCTCCTGAGAAAT
AAAAAGGACATTCTCTTTGGAAACATGGCAGAAATATATGAATTCCATAACGACATTTTC
TTGAGCAGCCTGGAAAATTGTGCTCATGCTCCAGAAAGAGTGGGACCTTGTTTCCTGGAA
AGGAAGGATGATTTTCAGATGTATGCAAAATATTGTCAGAATAAGCCCAGATCAGAAACA
ATTTGGAGGAAGTATTCAGAATGCGCATTTTTCCAGGAATGTCAAAGAAAGTTAAAACAC
AGACTTAGACTGGATTCCTATTTACTCAAACCAGTGCAACGAATCACTAAATATCAGTTA
TTGTTGAAGGAGCTATTAAAATATAGCAAAGACTGTGAAGGATCTGCTCTGTTGAAGAAG
GCACTCGATGCAATGCTGGATTTACTGAAGTCAGTTAATGATTCTATGCATCAGATTGCA
ATAAATGGCTATATTGGAAACTTAAATGAACTGGGCAAGATGATAATGCAAGGTGGATTC
AGCGTTTGGATAGGGCACAAGAAAGGTGCTACAAAAATGAAGGATTTGGCTAGATTCAAA
CCAATGCAGCGACACCTTTTCTTGTATGAAAAAGCCATTGTTTTTTGCAAAAGGCGTGTT
GAAAGTGGAGAAGGCTCTGACAGATACCCGTCATACAGTTTTAAACACTGTTGGAAAATG
GATGAAGTTGGAATCACTGAATATGTAAAAGGTGATAACCGCAAGTTTGAAATCTGGTAT
GGTGAAAAGGAAGAAGTTTATATTGTCCAGGCTTCTAATGTAGATGTGAAGATGACGTGG
CTAAAAGAAATAAGAAATATTTTGTTGAAGCAGCAGGAACTTTTGACAGTTAAAAAAAGA
AAGCAACAGGATCAATTAACAGAACGGGATAAGTTTCAGATTTCTCTTCAGCAGAATGAT
GAAAAGCAACAGGGAGCTTTTATAAGTACTGAGGAAACTGAATTGGAACACACCAGCACT
GTGGTGGAGGTCTGTGAGGCAATTGCGTCAGTTCAGGCAGAAGCAAATACAGTTTGGACT
GAGGCATCACAATCTGCAGAAATCTCTGAAGAACCTGCGGAATGGTCAAGCAACTATTTC
TACCCTACTTATGATGAAAATGAAGAAGAAAATAGGCCCCTCATGAGACCTGTGTCGGAG
ATGGCTCTCCTATATTGA
Enzyme 80 GenBank Gene ID NM_005369.4 Link Image
Enzyme 80 GeneCard ID MCF2 Link Image
Enzyme 80 GenAtlas ID Not Available
Enzyme 80 HGNC ID Not Available
Enzyme 80 Chromosome Location Not Available
Enzyme 80 Locus Not Available
Enzyme 80 SNPs SNPJam Report Link Image
Enzyme 80 General References
  1. Ron D, Tronick SR, Aaronson SA, Eva A: Molecular cloning and characterization of the human dbl proto-oncogene: evidence that its overexpression is sufficient to transform NIH/3T3 cells. EMBO J. 1988 Aug;7(8):2465-73. [PubMed Link Image]
  2. Komai K, Okayama R, Kitagawa M, Yagi H, Chihara K, Shiozawa S: Alternative splicing variants of the human DBL (MCF-2) proto-oncogene. Biochem Biophys Res Commun. 2002 Dec 6;299(3):455-8. [PubMed Link Image]
  3. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  4. Eva A, Vecchio G, Rao CD, Tronick SR, Aaronson SA: The predicted DBL oncogene product defines a distinct class of transforming proteins. Proc Natl Acad Sci U S A. 1988 Apr;85(7):2061-5. [PubMed Link Image]
  5. Noguchi T, Galland F, Batoz M, Mattei MG, Birnbaum D: Activation of a mcf.2 oncogene by deletion of amino-terminal coding sequences. Oncogene. 1988 Dec;3(6):709-15. [PubMed Link Image]
  6. Ron D, Zannini M, Lewis M, Wickner RB, Hunt LT, Graziani G, Tronick SR, Aaronson SA, Eva A: A region of proto-dbl essential for its transforming activity shows sequence similarity to a yeast cell cycle gene, CDC24, and the human breakpoint cluster gene, bcr. New Biol. 1991 Apr;3(4):372-9. [PubMed Link Image]
  7. Hart MJ, Eva A, Zangrilli D, Aaronson SA, Evans T, Cerione RA, Zheng Y: Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product. J Biol Chem. 1994 Jan 7;269(1):62-5. [PubMed Link Image]
  8. Ueda S, Kataoka T, Satoh T: Role of the Sec14-like domain of Dbl family exchange factors in the regulation of Rho family GTPases in different subcellular sites. Cell Signal. 2004 Aug;16(8):899-906. [PubMed Link Image]
  9. Kostenko EV, Olabisi OO, Sahay S, Rodriguez PL, Whitehead IP: Ccpg1, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs. Mol Cell Biol. 2006 Dec;26(23):8964-75. Epub 2006 Sep 25. [PubMed Link Image]
Enzyme 80 Metabolite References Not Available
Enzyme 81 [top]
Enzyme 81 ID 7137
Enzyme 81 Name Cell division control protein 42 homolog
Enzyme 81 Synonyms
  1. G25K GTP-binding protein
Enzyme 81 Gene Name CDC42
Enzyme 81 Protein Sequence >Cell division control protein 42 homolog
MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAG
QEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLR
DDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQRGLKNVFDEAILAALEPP
ETQPKRKCCIF
Enzyme 81 Number of Residues 191
Enzyme 81 Molecular Weight 21310.4
Enzyme 81 Theoretical pI 5.83
Enzyme 81 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 81 General Function Involved in GTP binding
Enzyme 81 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 81 Pathways Not Available
Enzyme 81 Reactions Not Available
Enzyme 81 Pfam Domain Function
Enzyme 81 Signals
  • None
Enzyme 81 Transmembrane Regions
  • None
Enzyme 81 Essentiality Not Available
Enzyme 81 GenBank ID Protein 182857 Link Image
Enzyme 81 UniProtKB/Swiss-Prot ID P60953 Link Image
Enzyme 81 UniProtKB/Swiss-Prot Entry Name CDC42_HUMAN Link Image
Enzyme 81 PDB ID 1GRN Link Image
Enzyme 81 PDB File Show
Enzyme 81 3D Structure
Enzyme 81 Cellular Location Not Available
Enzyme 81 Gene Sequence >576 bp
ATGCAGACAATTAAGTGTGTTGTTGTGGGCGATGGTGCTGTTGGTAAAACATGTCTCCTG
ATATCCTACACAACAAACAAATTTCCATCGGAATATGTACCGACTGTTTTTGACAACTAT
GCAGTCACAGTTATGATTGGTGGAGAACCATATACTCTTGGACTTTTTGATACTGCAGGG
CAAGAGGATTATGACAGATTACGACCGCTGAGTTATCCACAAACAGATGTATTTCTAGTC
TGTTTTTCAGTGGTCTCTCCATCTTCATTTGAAAACGTGAAAGAAAAGTGGGTGCCTGAG
ATAACTCACCACTGTCCAAAGACTCCTTTCTTGCTTGTTGGGACTCAAATTGATCTCAGA
GATGACCCCTCTACTATTGAGAAACTTGCCAAGAACAAACAGAAGCCTATCACTCCAGAG
ACTGCTGAAAAGCTGGCCCGTGACCTGAAGGCTGTCAAGTATGTGGAGTGTTCTGCACTT
ACACAGAGAGGTCTGAAGAATGTGTTTGATGAGGCTATCCTAGCTGCCCTCGAGCCTCCG
GAAACTCAACCCAAAAGGAAGTGCTGTATATTCTAA
Enzyme 81 GenBank Gene ID M35543 Link Image
Enzyme 81 GeneCard ID CDC42 Link Image
Enzyme 81 GenAtlas ID CDC42 Link Image
Enzyme 81 HGNC ID HGNC:1736 Link Image
Enzyme 81 Chromosome Location 1
Enzyme 81 Locus 1p36.1
Enzyme 81 SNPs SNPJam Report Link Image
Enzyme 81 General References
  1. Munemitsu S, Innis MA, Clark R, McCormick F, Ullrich A, Polakis P: Molecular cloning and expression of a G25K cDNA, the human homolog of the yeast cell cycle gene CDC42. Mol Cell Biol. 1990 Nov;10(11):5977-82. [PubMed Link Image]
  2. Shinjo K, Koland JG, Hart MJ, Narasimhan V, Johnson DI, Evans T, Cerione RA: Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42. Proc Natl Acad Sci U S A. 1990 Dec;87(24):9853-7. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Kwong CH, Malech HL, Rotrosen D, Leto TL: Regulation of the human neutrophil NADPH oxidase by rho-related G-proteins. Biochemistry. 1993 Jun 1;32(21):5711-7. [PubMed Link Image]
  6. Polakis PG, Snyderman R, Evans T: Characterization of G25K, a GTP-binding protein containing a novel putative nucleotide binding domain. Biochem Biophys Res Commun. 1989 Apr 14;160(1):25-32. [PubMed Link Image]
  7. Yamane HK, Farnsworth CC, Xie HY, Evans T, Howald WN, Gelb MH, Glomset JA, Clarke S, Fung BK: Membrane-binding domain of the small G protein G25K contains an S-(all-trans-geranylgeranyl)cysteine methyl ester at its carboxyl terminus. Proc Natl Acad Sci U S A. 1991 Jan 1;88(1):286-90. [PubMed Link Image]
  8. Joberty G, Perlungher RR, Macara IG: The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins. Mol Cell Biol. 1999 Oct;19(10):6585-97. [PubMed Link Image]
  9. Eisenmann KM, McCarthy JB, Simpson MA, Keely PJ, Guan JL, Tachibana K, Lim L, Manser E, Furcht LT, Iida J: Melanoma chondroitin sulphate proteoglycan regulates cell spreading through Cdc42, Ack-1 and p130cas. Nat Cell Biol. 1999 Dec;1(8):507-13. [PubMed Link Image]
  10. Pirone DM, Fukuhara S, Gutkind JS, Burbelo PD: SPECs, small binding proteins for Cdc42. J Biol Chem. 2000 Jul 28;275(30):22650-6. [PubMed Link Image]
  11. Johansson A, Driessens M, Aspenstrom P: The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1. J Cell Sci. 2000 Sep;113 ( Pt 18):3267-75. [PubMed Link Image]
  12. Miki H, Yamaguchi H, Suetsugu S, Takenawa T: IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature. 2000 Dec 7;408(6813):732-5. [PubMed Link Image]
  13. Noda Y, Takeya R, Ohno S, Naito S, Ito T, Sumimoto H: Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C. Genes Cells. 2001 Feb;6(2):107-19. [PubMed Link Image]
  14. Meller N, Irani-Tehrani M, Kiosses WB, Del Pozo MA, Schwartz MA: Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho proteins. Nat Cell Biol. 2002 Sep;4(9):639-47. [PubMed Link Image]
  15. Masuda-Robens JM, Kutney SN, Qi H, Chou MM: The TRE17 oncogene encodes a component of a novel effector pathway for Rho GTPases Cdc42 and Rac1 and stimulates actin remodeling. Mol Cell Biol. 2003 Mar;23(6):2151-61. [PubMed Link Image]
  16. Worby CA, Mattoo S, Kruger RP, Corbeil LB, Koller A, Mendez JC, Zekarias B, Lazar C, Dixon JE: The fic domain: regulation of cell signaling by adenylylation. Mol Cell. 2009 Apr 10;34(1):93-103. [PubMed Link Image]
  17. Yarbrough ML, Li Y, Kinch LN, Grishin NV, Ball HL, Orth K: AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science. 2009 Jan 9;323(5911):269-72. Epub 2008 Nov 27. [PubMed Link Image]
  18. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  19. Feltham JL, Dotsch V, Raza S, Manor D, Cerione RA, Sutcliffe MJ, Wagner G, Oswald RE: Definition of the switch surface in the solution structure of Cdc42Hs. Biochemistry. 1997 Jul 22;36(29):8755-66. [PubMed Link Image]
  20. Guo W, Sutcliffe MJ, Cerione RA, Oswald RE: Identification of the binding surface on Cdc42Hs for p21-activated kinase. Biochemistry. 1998 Oct 6;37(40):14030-7. [PubMed Link Image]
  21. Rittinger K, Walker PA, Eccleston JF, Nurmahomed K, Owen D, Laue E, Gamblin SJ, Smerdon SJ: Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP. Nature. 1997 Aug 14;388(6643):693-7. [PubMed Link Image]
  22. Rudolph MG, Wittinghofer A, Vetter IR: Nucleotide binding to the G12V-mutant of Cdc42 investigated by X-ray diffraction and fluorescence spectroscopy: two different nucleotide states in one crystal. Protein Sci. 1999 Apr;8(4):778-87. [PubMed Link Image]
Enzyme 81 Metabolite References Not Available
Enzyme 82 [top]
Enzyme 82 ID 7138
Enzyme 82 Name Rab GDP dissociation inhibitor beta
Enzyme 82 Synonyms
  1. Rab GDI beta
  2. Guanosine diphosphate dissociation inhibitor 2
  3. GDI-2
Enzyme 82 Gene Name GDI2
Enzyme 82 Protein Sequence >Rab GDP dissociation inhibitor beta
MNEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDRNPYYGGESASITPLEDLYKRFKIPG
SPPESMGRGRDWNVDLIPKFLMANGQLVKMLLYTEVTRYLDFKVTEGSFVYKGGKIYKVP
STEAEALASSLMGLFEKRRFRKFLVYVANFDEKDPRTFEGIDPKKTTMRDVYKKFDLGQD
VIDFTGHALALYRTDDYLDQPCYETINRIKLYSESLARYGKSPYLYPLYGLGELPQGFAR
LSAIYGGTYMLNKPIEEIIVQNGKVIGVKSEGEIARCKQLICDPSYVKDRVEKVGQVIRV
ICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISFAHNVAAQGKYIAIVSTTVETK
EPEKEIRPALELLEPIEQKFVSISDLLVPKDLGTESQIFISRTYDATTHFETTCDDIKNI
YKRMTGSEFDFEEMKRKKNDIYGED
Enzyme 82 Number of Residues 445
Enzyme 82 Molecular Weight 50662.8
Enzyme 82 Theoretical pI 6.39
Enzyme 82 GO Classification
Function
  • GDP-dissociation inhibitor activity
  • GTPase regulator activity
  • Rab GDP-dissociation inhibitor activity
  • enzyme regulator activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
  • biological regulation
  • establishment of localization
  • protein transport
  • regulation of GTP catabolic process
  • regulation of GTPase activity
  • regulation of biological process
  • regulation of cellular metabolic process
  • regulation of metabolic process
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • regulation of nucleotide catabolic process
  • regulation of nucleotide metabolic process
  • regulation of purine nucleotide catabolic process
  • transport
Component
Enzyme 82 General Function Involved in regulation of GTPase activity
Enzyme 82 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 82 Pathways Not Available
Enzyme 82 Reactions Not Available
Enzyme 82 Pfam Domain Function
Enzyme 82 Signals
  • None
Enzyme 82 Transmembrane Regions
  • None
Enzyme 82 Essentiality Not Available
Enzyme 82 GenBank ID Protein 6598323 Link Image
Enzyme 82 UniProtKB/Swiss-Prot ID P50395 Link Image
Enzyme 82 UniProtKB/Swiss-Prot Entry Name GDIB_HUMAN Link Image
Enzyme 82 PDB ID Not Available
Enzyme 82 Cellular Location Not Available
Enzyme 82 Gene Sequence >1338 bp
ATGAATGAGGAGTACGACGTGATCGTGCTGGGCACCGGCCTGACGGAATGTATCCTGTCA
GGTATAATGTCAGTGAATGGCAAGAAAGTTCTTCATATGGATCGAAACCCTTACTACGGA
GGAGAGAGTGCATCTATAACACCATTGGAAGATTTATACAAAAGATTTAAAATACCAGGA
TCACCACCCGAGTCAATGGGGAGAGGAAGAGACTGGAATGTTGACTTGATTCCCAAGTTC
CTTATGGCTAATGGTCAGCTGGTTAAGATGCTGCTTTATACAGAGGTAACTCGCTATCTG
GATTTTAAAGTGACTGAAGGGAGCTTTGTCTATAAGGGTGGAAAAATCTACAAGGTTCCT
TCCACTGAAGCAGAAGCCCTGGCATCTAGCCTAATGGGATTGTTTGAAAAACGTCGCTTC
AGGAAATTCCTAGTGTATGTTGCCAACTTCGATGAAAAAGATCCAAGAACTTTTGAAGGC
ATTGATCCTAAGAAGACCACAATGCGAGATGTGTATAAGAAATTTGATTTGGGTCAAGAC
GTTATAGATTTTACTGGTCATGCTCTTGCACTTTACAGAACTGATGATTACTTAGATCAA
CCGTGTTATGAAACCATTAATAGAATTAAACTTTACAGTGAATCTTTGGCAAGATATGGC
AAAAGCCCATACCTTTATCCACTCTATGGCCTTGGAGAACTGCCCCAAGGATTTGCAAGG
CTAAGTGCTATTTATGGAGGTACCTATATGCTGAATAAACCCATTGAAGAAATCATTGTA
CAGAATGGAAAAGTAATTGGTGTAAAATCTGAAGGAGAAATTGCTCGCTGTAAGCAGCTC
ATCTGTGACCCCAGCTACGTAAAAGATCGGGTAGAAAAAGTGGGCCAGGTGATCAGAGTT
ATTTGCATCCTCAGCCACCCCATCAAGAACACCAATGATGCCAACTCCTGCCAGATCATT
ATTCCACAGAACCAAGTCAATCGAAAGTCAGATATCTACGTCTGCATGATCTCCTTTGCG
CACAATGTAGCAGCACAAGGGAAGTACATTGCTATAGTTAGTACAACTGTGGAAACCAAG
GAGCCTGAGAAGGAAATCAGACCAGCTTTGGAGCTCTTGGAACCAATTGAACAGAAATTT
GTTAGCATCAGTGACCTCCTGGTACCAAAAGACTTGGGAACAGAAAGCCAGATCTTTATT
TCCCGCACATATGATGCCACCACTCATTTTGAGACAACGTGTGATGACATTAAAAACATC
TATAAGAGGATGACAGGATCAGAGTTTGACTTTGAGGAAATGAAGCGCAAGAAGAATGAC
ATCTATGGGGAAGACTAA
Enzyme 82 GenBank Gene ID NM_001494.3 Link Image
Enzyme 82 GeneCard ID GDI2 Link Image
Enzyme 82 GenAtlas ID GDI2 Link Image
Enzyme 82 HGNC ID HGNC:4227 Link Image
Enzyme 82 Chromosome Location 1
Enzyme 82 Locus 10p15
Enzyme 82 SNPs SNPJam Report Link Image
Enzyme 82 General References
  1. Sedlacek Z, Munstermann E, Mincheva A, Lichter P, Poustka A: The human rab GDI beta gene with long retroposon-rich introns maps to 10p15 and its pseudogene to 7p11-p13. Mamm Genome. 1998 Jan;9(1):78-80. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Caillol N, Pasqualini E, Lloubes R, Lombardo D: Impairment of bile salt-dependent lipase secretion in human pancreatic tumoral SOJ-6 cells. J Cell Biochem. 2000 Sep 14;79(4):628-47. [PubMed Link Image]
  4. Bachner D, Sedlacek Z, Korn B, Hameister H, Poustka A: Expression patterns of two human genes coding for different rab GDP-dissociation inhibitors (GDIs), extremely conserved proteins involved in cellular transport. Hum Mol Genet. 1995 Apr;4(4):701-8. [PubMed Link Image]
  5. Li X, Bu X, Lu B, Avraham H, Flavell RA, Lim B: The hematopoiesis-specific GTP-binding protein RhoH is GTPase deficient and modulates activities of other Rho GTPases by an inhibitory function. Mol Cell Biol. 2002 Feb;22(4):1158-71. [PubMed Link Image]
  6. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 82 Metabolite References Not Available
Enzyme 83 [top]
Enzyme 83 ID 7139
Enzyme 83 Name Rho GDP-dissociation inhibitor 1
Enzyme 83 Synonyms
  1. Rho GDI 1
  2. Rho-GDI alpha
Enzyme 83 Gene Name ARHGDIA
Enzyme 83 Protein Sequence >Rho GDP-dissociation inhibitor 1
MAEQEPTAEQLAQIAAENEEDEHSVNYKPPAQKSIQEIQELDKDDESLRKYKEALLGRVA
VSADPNVPNVVVTGLTLVCSSAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNR
EIVSGMKYIQHTYRKGVKIDKTDYMVGSYGPRAEEYEFLTPVEEAPKGMLARGSYSIKSR
FTDDDKTDHLSWEWNLTIKKDWKD
Enzyme 83 Number of Residues 204
Enzyme 83 Molecular Weight 23206.9
Enzyme 83 Theoretical pI 4.74
Enzyme 83 GO Classification
Function
  • GDP-dissociation inhibitor activity
  • GTPase regulator activity
  • Rho GDP-dissociation inhibitor activity
  • enzyme regulator activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 83 General Function Involved in GTPase activator activity
Enzyme 83 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 83 Pathways Not Available
Enzyme 83 Reactions Not Available
Enzyme 83 Pfam Domain Function
Enzyme 83 Signals
  • None
Enzyme 83 Transmembrane Regions
  • None
Enzyme 83 Essentiality Not Available
Enzyme 83 GenBank ID Protein 20379028 Link Image
Enzyme 83 UniProtKB/Swiss-Prot ID P52565 Link Image
Enzyme 83 UniProtKB/Swiss-Prot Entry Name GDIR1_HUMAN Link Image
Enzyme 83 PDB ID 1HH4 Link Image
Enzyme 83 PDB File Show
Enzyme 83 3D Structure
Enzyme 83 Cellular Location Not Available
Enzyme 83 Gene Sequence >615 bp
ATGGCTGAGCAGGAGCCCACAGCCGAGCAGCTGGCCCAGATTGCAGCGGAGAACGAGGAG
GATGAGCACTCGGTCAACTACAAGCCCCCGGCCCAGAAGAGCATCCAGGAGATCCAGGAG
CTGGACAAGGACGACGAGAGCCTGCGAAAGTACAAGGAGGCCCTGCTGGGCCGCGTGGCC
GTTTCCGCAGACCCCAACGTCCCCAACGTCGTGGTGACTGGCCTGACCCTGGTGTGCAGC
TCGGCCCCGGGCCCCCTGGAGCTGGACCTGACGGGCGACCTGGAGAGCTTCAAGAAGCAG
TCGTTTGTGCTGAAGGAGGGTGTGGAGTACCGGATAAAAATCTCTTTCCGGGTTAACCGA
GAGATAGTGTCCGGCATGAAGTACATCCAGCATACGTACAGGAAAGGCGTCAAGATTGAC
AAGACTGACTACATGGTAGGCAGCTATGGGCCCCGGGCCGAGGAGTACGAGTTCCTGACC
CCCGTGGAGGAGGCACCCAAGGGTATGCTGGCCCGGGGCAGCTACAGCATCAAGTCCCGC
TTCACAGACGACGACAAGACCGACCACCTGTCCTGGGAGTGGAATCTCACCATCAAGAAG
GACTGGAAGGACTGA
Enzyme 83 GenBank Gene ID AF498926 Link Image
Enzyme 83 GeneCard ID ARHGDIA Link Image
Enzyme 83 GenAtlas ID Not Available
Enzyme 83 HGNC ID Not Available
Enzyme 83 Chromosome Location 1
Enzyme 83 Locus 17q25.3
Enzyme 83 SNPs SNPJam Report Link Image
Enzyme 83 General References
  1. Leffers H, Nielsen MS, Andersen AH, Honore B, Madsen P, Vandekerckhove J, Celis JE: Identification of two human Rho GDP dissociation inhibitor proteins whose overexpression leads to disruption of the actin cytoskeleton. Exp Cell Res. 1993 Dec;209(2):165-74. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Kwong CH, Malech HL, Rotrosen D, Leto TL: Regulation of the human neutrophil NADPH oxidase by rho-related G-proteins. Biochemistry. 1993 Jun 1;32(21):5711-7. [PubMed Link Image]
  5. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed Link Image]
  6. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  8. Keep NH, Barnes M, Barsukov I, Badii R, Lian LY, Segal AW, Moody PC, Roberts GC: A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm. Structure. 1997 May 15;5(5):623-33. [PubMed Link Image]
Enzyme 83 Metabolite References Not Available
Enzyme 84 [top]
Enzyme 84 ID 7140
Enzyme 84 Name Rho GDP-dissociation inhibitor 2
Enzyme 84 Synonyms
  1. Rho GDI 2
  2. Ly-GDI
  3. Rho-GDI beta
Enzyme 84 Gene Name ARHGDIB
Enzyme 84 Protein Sequence >Rho GDP-dissociation inhibitor 2
MTEKAPEPHVEEDDDDELDSKLNYKPPPQKSLKELQEMDKDDESLIKYKKTLLGDGPVVT
DPKAPNVVVTRLTLVCESAPGPITMDLTGDLEALKKETIVLKEGSEYRVKIHFKVNRDIV
SGLKYVQHTYRTGVKVDKATFMVGSYGPRPEEYEFLTPVEEAPKGMLARGTYHNKSFFTD
DDKQDHLSWEWNLSIKKEWTE
Enzyme 84 Number of Residues 201
Enzyme 84 Molecular Weight 22987.9
Enzyme 84 Theoretical pI 4.84
Enzyme 84 GO Classification
Function
  • GDP-dissociation inhibitor activity
  • GTPase regulator activity
  • Rho GDP-dissociation inhibitor activity
  • enzyme regulator activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 84 General Function Involved in GTPase activator activity
Enzyme 84 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 84 Pathways Not Available
Enzyme 84 Reactions Not Available
Enzyme 84 Pfam Domain Function
Enzyme 84 Signals
  • None
Enzyme 84 Transmembrane Regions
  • None
Enzyme 84 Essentiality Not Available
Enzyme 84 GenBank ID Protein 197692331 Link Image
Enzyme 84 UniProtKB/Swiss-Prot ID P52566 Link Image
Enzyme 84 UniProtKB/Swiss-Prot Entry Name GDIR2_HUMAN Link Image
Enzyme 84 PDB ID 1DS6 Link Image
Enzyme 84 PDB File Show
Enzyme 84 3D Structure
Enzyme 84 Cellular Location Not Available
Enzyme 84 Gene Sequence >606 bp
ATGACTGAAAAAGCCCCAGAGCCACATGTGGAGGAGGATGACGATGATGAGCTGGACAGC
AAGCTCAATTATAAGCCTCCACCACAGAAGTCCCTGAAAGAGCTGCAGGAAATGGACAAA
GATGATGAGAGTCTAATTAAGTACAAGAAAACGCTGCTGGGAGATGGTCCTGTGGTGACA
GATCCGAAAGCCCCCAATGTCGTTGTCACCCGGCTCACCCTGGTTTGTGAGAGTGCCCCG
GGACCAATCACCATGGACCTTACTGGAGATCTGGAAGCCCTCAAAAAGGAAACCATTGTG
TTAAAGGAAGGTTCTGAATATAGAGTCAAAATTCACTTCAAAGTGAACAGGGATATTGTG
TCAGGCCTGAAATACGTTCAGCACACCTACAGGACTGGGGTGAAAGTGGATAAAGCAACA
TTTATGGTTGGCAGCTATGGACCTCGGCCTGAGGAGTATGAGTTCCTCACTCCAGTTGAG
GAGGCTCCCAAGGGCATGCTGGCGCGAGGCACGTACCACAACAAGTCCTTCTTCACCGAC
GATGACAAGCAAGACCACCTCAGCTGGGAGTGGAACCTGTCGATTAAGAAGGAGTGGACA
GAATAA
Enzyme 84 GenBank Gene ID AB451315 Link Image
Enzyme 84 GeneCard ID ARHGDIB Link Image
Enzyme 84 GenAtlas ID Not Available
Enzyme 84 HGNC ID Not Available
Enzyme 84 Chromosome Location 1
Enzyme 84 Locus 12p12.3
Enzyme 84 SNPs SNPJam Report Link Image
Enzyme 84 General References
  1. Scherle P, Behrens T, Staudt LM: Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein, is expressed preferentially in lymphocytes. Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7568-72. [PubMed Link Image]
  2. Leffers H, Nielsen MS, Andersen AH, Honore B, Madsen P, Vandekerckhove J, Celis JE: Identification of two human Rho GDP dissociation inhibitor proteins whose overexpression leads to disruption of the actin cytoskeleton. Exp Cell Res. 1993 Dec;209(2):165-74. [PubMed Link Image]
  3. Lelias JM, Adra CN, Wulf GM, Guillemot JC, Khagad M, Caput D, Lim B: cDNA cloning of a human mRNA preferentially expressed in hematopoietic cells and with homology to a GDP-dissociation inhibitor for the rho GTP-binding proteins. Proc Natl Acad Sci U S A. 1993 Feb 15;90(4):1479-83. [PubMed Link Image]
  4. Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Aebersold R, Leavitt J: Sequence analysis of proteins separated by polyacrylamide gel electrophoresis: towards an integrated protein database. Electrophoresis. 1990 Jul;11(7):517-27. [PubMed Link Image]
  7. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  8. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  10. Scheffzek K, Stephan I, Jensen ON, Illenberger D, Gierschik P: The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI. Nat Struct Biol. 2000 Feb;7(2):122-6. [PubMed Link Image]
Enzyme 84 Metabolite References Not Available
Enzyme 85 [top]
Enzyme 85 ID 7141
Enzyme 85 Name Ras-related C3 botulinum toxin substrate 2
Enzyme 85 Synonyms
  1. GX
  2. Small G protein
  3. p21-Rac2
Enzyme 85 Gene Name RAC2
Enzyme 85 Protein Sequence >Ras-related C3 botulinum toxin substrate 2
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDSKPVNLGLWDTAG
QEDYDRLRPLSYPQTDVFLICFSLVSPASYENVRAKWFPEVRHHCPSTPIILVGTKLDLR
DDKDTIEKLKEKKLAPITYPQGLALAKEIDSVKYLECSALTQRGLKTVFDEAIRAVLCPQ
PTRQQKRACSLL
Enzyme 85 Number of Residues 192
Enzyme 85 Molecular Weight 21428.6
Enzyme 85 Theoretical pI 7.70
Enzyme 85 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 85 General Function Involved in GTP binding
Enzyme 85 Specific Function Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as secretory processes, phagocytose of apoptotic cells and epithelial cell polarization. Augments the production of reactive oxygen species (ROS) by NADPH oxidase
Enzyme 85 Pathways Not Available
Enzyme 85 Reactions Not Available
Enzyme 85 Pfam Domain Function
Enzyme 85 Signals
  • None
Enzyme 85 Transmembrane Regions
  • None
Enzyme 85 Essentiality Not Available
Enzyme 85 GenBank ID Protein Not Available
Enzyme 85 UniProtKB/Swiss-Prot ID P15153 Link Image
Enzyme 85 UniProtKB/Swiss-Prot Entry Name RAC2_HUMAN Link Image
Enzyme 85 PDB ID 1DS6 Link Image
Enzyme 85 PDB File Show
Enzyme 85 3D Structure
Enzyme 85 Cellular Location Not Available
Enzyme 85 Gene Sequence >579 bp
ATGCAGGCCATCAAGTGTGTGGTGGTGGGAGATGGGGCCGTGGGCAAGACCTGCCTTCTC
ATCAGCTACACCACCAACGCCTTTCCCGGAGAGTACATCCCCACCGTGTTTGACAACTAT
TCAGCCAATGTGATGGTGGACAGCAAGCCAGTGAACCTGGGGCTGTGGGACACTGCTGGG
CAGGAGGACTACGACCGTCTCCGGCCGCTCTCCTATCCACAGACGGACGTCTTCCTCATC
TGCTTCTCCCTCGTCAGCCCAGCCTCTTATGAGAACGTCCGCGCCAAGTGGTTCCCAGAA
GTGCGGCACCACTGCCCCAGCACACCCATCATCCTGGTGGGCACCAAGCTGGACCTGCGG
GACGACAAGGACACCATCGAGAAACTGAAGGAGAAGAAGCTGGCTCCCATCACCTACCCG
CAGGGCCTGGCACTGGCCAAGGAGATTGACTCGGTGAAATACCTGGAGTGCTCAGCCCTC
ACCCAGAGAGGCCTGAAAACCGTGTTCGACGAGGCCATCCGGGCCGTGCTGTGCCCTCAG
CCCACGCGGCAGCAGAAGCGCGCCTGCAGCCTCCTCTAG
Enzyme 85 GenBank Gene ID M29871 Link Image
Enzyme 85 GeneCard ID RAC2 Link Image
Enzyme 85 GenAtlas ID RAC2 Link Image
Enzyme 85 HGNC ID HGNC:9802 Link Image
Enzyme 85 Chromosome Location 2
Enzyme 85 Locus 22q13.1
Enzyme 85 SNPs SNPJam Report Link Image
Enzyme 85 General References
  1. Didsbury J, Weber RF, Bokoch GM, Evans T, Snyderman R: rac, a novel ras-related family of proteins that are botulinum toxin substrates. J Biol Chem. 1989 Oct 5;264(28):16378-82. [PubMed Link Image]
  2. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  3. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Mizuno T, Kaibuchi K, Ando S, Musha T, Hiraoka K, Takaishi K, Asada M, Nunoi H, Matsuda I, Takai Y: Regulation of the superoxide-generating NADPH oxidase by a small GTP-binding protein and its stimulatory and inhibitory GDP/GTP exchange proteins. J Biol Chem. 1992 May 25;267(15):10215-8. [PubMed Link Image]
  6. Knaus UG, Heyworth PG, Evans T, Curnutte JT, Bokoch GM: Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2. Science. 1991 Dec 6;254(5037):1512-5. [PubMed Link Image]
  7. Reibel L, Dorseuil O, Stancou R, Bertoglio J, Gacon G: A hemopoietic specific gene encoding a small GTP binding protein is overexpressed during T cell activation. Biochem Biophys Res Commun. 1991 Mar 15;175(2):451-8. [PubMed Link Image]
  8. Kwong CH, Malech HL, Rotrosen D, Leto TL: Regulation of the human neutrophil NADPH oxidase by rho-related G-proteins. Biochemistry. 1993 Jun 1;32(21):5711-7. [PubMed Link Image]
  9. Kinsella BT, Erdman RA, Maltese WA: Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA. J Biol Chem. 1991 May 25;266(15):9786-94. [PubMed Link Image]
  10. Nishihara H, Kobayashi S, Hashimoto Y, Ohba F, Mochizuki N, Kurata T, Nagashima K, Matsuda M: Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins. Biochim Biophys Acta. 1999 Nov 11;1452(2):179-87. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  12. Scheffzek K, Stephan I, Jensen ON, Illenberger D, Gierschik P: The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI. Nat Struct Biol. 2000 Feb;7(2):122-6. [PubMed Link Image]
  13. Ambruso DR, Knall C, Abell AN, Panepinto J, Kurkchubasche A, Thurman G, Gonzalez-Aller C, Hiester A, deBoer M, Harbeck RJ, Oyer R, Johnson GL, Roos D: Human neutrophil immunodeficiency syndrome is associated with an inhibitory Rac2 mutation. Proc Natl Acad Sci U S A. 2000 Apr 25;97(9):4654-9. [PubMed Link Image]
  14. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 85 Metabolite References Not Available
Enzyme 86 [top]
Enzyme 86 ID 7272
Enzyme 86 Name Elongation factor 1-alpha 1
Enzyme 86 Synonyms
  1. EF-1-alpha-1
  2. Elongation factor Tu
  3. EF-Tu
  4. Eukaryotic elongation factor 1 A-1
  5. eEF1A-1
  6. Leukocyte receptor cluster member 7
Enzyme 86 Gene Name EEF1A1
Enzyme 86 Protein Sequence >Elongation factor 1-alpha 1
MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVL
DKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGV
GEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKK
IGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTR
PTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALS
EALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPV
LDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPP
LGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK
Enzyme 86 Number of Residues 462
Enzyme 86 Molecular Weight 50140.6
Enzyme 86 Theoretical pI 9.50
Enzyme 86 GO Classification
Function
  • GTP binding
  • GTPase activity
  • RNA binding
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleic acid binding
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • translation elongation factor activity
  • translation factor activity, nucleic acid binding
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • translational elongation
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 86 General Function Involved in GTPase activity
Enzyme 86 Specific Function This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis
Enzyme 86 Pathways Not Available
Enzyme 86 Reactions Not Available
Enzyme 86 Pfam Domain Function
Enzyme 86 Signals
  • None
Enzyme 86 Transmembrane Regions
  • None
Enzyme 86 Essentiality Not Available
Enzyme 86 GenBank ID Protein 31098 Link Image
Enzyme 86 UniProtKB/Swiss-Prot ID P68104 Link Image
Enzyme 86 UniProtKB/Swiss-Prot Entry Name EF1A1_HUMAN Link Image
Enzyme 86 PDB ID Not Available
Enzyme 86 Cellular Location Not Available
Enzyme 86 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 86 GenBank Gene ID X03558 Link Image
Enzyme 86 GeneCard ID EEF1A1 Link Image
Enzyme 86 GenAtlas ID EEF1A1 Link Image
Enzyme 86 HGNC ID HGNC:3189 Link Image
Enzyme 86 Chromosome Location 6
Enzyme 86 Locus 6q14.1
Enzyme 86 SNPs SNPJam Report Link Image
Enzyme 86 General References
  1. Brands JH, Maassen JA, van Hemert FJ, Amons R, Moller W: The primary structure of the alpha subunit of human elongation factor 1. Structural aspects of guanine-nucleotide-binding sites. Eur J Biochem. 1986 Feb 17;155(1):167-71. [PubMed Link Image]
  2. Uetsuki T, Naito A, Nagata S, Kaziro Y: Isolation and characterization of the human chromosomal gene for polypeptide chain elongation factor-1 alpha. J Biol Chem. 1989 Apr 5;264(10):5791-8. [PubMed Link Image]
  3. Madsen HO, Poulsen K, Dahl O, Clark BF, Hjorth JP: Retropseudogenes constitute the major part of the human elongation factor 1 alpha gene family. Nucleic Acids Res. 1990 Mar 25;18(6):1513-6. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Rao TR, Slobin LI: Structure of the amino-terminal end of mammalian elongation factor Tu. Nucleic Acids Res. 1986 Mar 11;14(5):2409. [PubMed Link Image]
  6. Ann DK, Wu MM, Huang T, Carlson DM, Wu R: Retinol-regulated gene expression in human tracheobronchial epithelial cells. Enhanced expression of elongation factor EF-1 alpha. J Biol Chem. 1988 Mar 15;263(8):3546-9. [PubMed Link Image]
  7. Whiteheart SW, Shenbagamurthi P, Chen L, Cotter RJ, Hart GW: Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha. J Biol Chem. 1989 Aug 25;264(24):14334-41. [PubMed Link Image]
  8. Bohnsack MT, Regener K, Schwappach B, Saffrich R, Paraskeva E, Hartmann E, Gorlich D: Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm. EMBO J. 2002 Nov 15;21(22):6205-15. [PubMed Link Image]
  9. Calado A, Treichel N, Muller EC, Otto A, Kutay U: Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA. EMBO J. 2002 Nov 15;21(22):6216-24. [PubMed Link Image]
  10. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  11. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed Link Image]
  12. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  13. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  14. Guzzo CM, Yang DC: Lysyl-tRNA synthetase interacts with EF1alpha, aspartyl-tRNA synthetase and p38 in vitro. Biochem Biophys Res Commun. 2008 Jan 25;365(4):718-23. Epub 2007 Nov 20. [PubMed Link Image]
  15. Yang YF, Chou MY, Fan CY, Chen SF, Lyu PC, Liu CC, Tseng TL: The possible interaction of CDA14 and protein elongation factor 1alpha. Biochim Biophys Acta. 2008 Feb;1784(2):312-8. Epub 2007 Oct 17. [PubMed Link Image]
  16. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 86 Metabolite References Not Available
Enzyme 87 [top]
Enzyme 87 ID 7276
Enzyme 87 Name Elongation factor 1-alpha 2
Enzyme 87 Synonyms
  1. EF-1-alpha-2
  2. Eukaryotic elongation factor 1 A-2
  3. eEF1A-2
  4. Statin-S1
Enzyme 87 Gene Name EEF1A2
Enzyme 87 Protein Sequence >Elongation factor 1-alpha 2
MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVL
DKLKAERERGITIDISLWKFETTKYYITIIDAPGHRDFIKNMITGTSQADCAVLIVAAGV
GEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPAYSEKRYDEIVKEVSAYIKK
IGYNPATVPFVPISGWHGDNMLEPSPNMPWFKGWKVERKEGNASGVSLLEALDTILPPTR
PTDKPLRLPLQDVYKIGGIGTVPVGRVETGILRPGMVVTFAPVNITTEVKSVEMHHEALS
EALPGDNVGFNVKNVSVKDIRRGNVCGDSKSDPPQEAAQFTSQVIILNHPGQISAGYSPV
IDCHTAHIACKFAELKEKIDRRSGKKLEDNPKSLKSGDAAIVEMVPGKPMCVESFSQYPP
LGRFAVRDMRQTVAVGVIKNVEKKSGGAGKVTKSAQKAQKAGK
Enzyme 87 Number of Residues 463
Enzyme 87 Molecular Weight 50469.9
Enzyme 87 Theoretical pI 9.50
Enzyme 87 GO Classification
Function
  • GTP binding
  • GTPase activity
  • RNA binding
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleic acid binding
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • translation elongation factor activity
  • translation factor activity, nucleic acid binding
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • translational elongation
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 87 General Function Involved in GTPase activity
Enzyme 87 Specific Function This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis
Enzyme 87 Pathways Not Available
Enzyme 87 Reactions Not Available
Enzyme 87 Pfam Domain Function
Enzyme 87 Signals
  • None
Enzyme 87 Transmembrane Regions
  • None
Enzyme 87 Essentiality Not Available
Enzyme 87 GenBank ID Protein 38456 Link Image
Enzyme 87 UniProtKB/Swiss-Prot ID Q05639 Link Image
Enzyme 87 UniProtKB/Swiss-Prot Entry Name EF1A2_HUMAN Link Image
Enzyme 87 PDB ID Not Available
Enzyme 87 Cellular Location Not Available
Enzyme 87 Gene Sequence >1392 bp
ATGGGCAAGGAGAAGACCCACATCAACATCGTGGTCATCGGCCACGTGGACTCCGGAAAG
TCCACCACCACGGGCCACCTCATCTACAAATGCGGAGGTATTGACAAAAGGACCATTGAG
AAGTTCGAGAAGGAGGCGGCTGAGATGGGGAAGGGATCCTTCAAGTATGCCTGGGTGCTG
GACAAGCTGAAGGCGGAGCGTGAGCGCGGCATCACCATCGACATCTCCCTCTGGAAGTTC
GAGACCACCAAGTACTACATCACCATCATCGATGCCCCCGGCCACCGCGACTTCATCAAG
AACATGATCACGGGTACATCCCAGGCGGACTGCGCAGTGCTGATCGTGGCGGCGGGCGTG
GGCGAGTTCGAGGCGGGCATCTCCAAGAATGGGCAGACGCGGGAGCATGCCCTGCTGGCC
TACACGCTGGGTGTGAAGCAGCTCATCGTGGGCGTGAACAAAATGGACTCCACAGAGCCG
GCCTACAGCGAGAAGCGCTACGACGAGATCGTCAAGGAAGTCAGCGCCTACATCAAGAAG
ATCGGCTACAACCCGGCCACCGTGCCCTTTGTGCCCATCTCCGGCTGGCACGGCGACAAC
ATGCTGGAGCCCTCCCCCAACATGCCGTGGTTCAAGGGCTGGAAGGTGGAGCGTAAGGAG
GGCAACGCAAGCGGCGTGTCCCTGCTGGAGGCCCTGGACACCATCCTGCCCCCCACGCGC
CCCACGGACAAGCCCCTGCGCCTGCCGCTGCAGGACGTGTACAAGATTGGCGGCATTGGC
ACGGTGCCCGTGGGCCGGGTGGAGACCGGCATCCTGCGGCCGGGCATGGTGGTGACCTTT
GCGCCAGTGAACATCACCACTGAGGTGAAGTCAGTGGAGATGCACCACGAGGCTCTGAGC
GAAGCTCTGCCCGGCGACAACGTCGGCTTCAATGTGAAGAACGTGTCGGTGAAGGACATC
CGGCGGGGCAACGTGTGTGGGGACAGCAAGTCTGACCCGCCGCAGGAGGCTGCTCAGTTC
ACCTCCCAGGTCATCATCCTGAACCACCCGGGGCAGATTAGCGCCGGCTACTCCCCGGTC
ATCGACTGCCACACAGCCCACATCGCCTGCAAGTTTGCGGAGCTGAAGGAGAAGATTGAC
CGGCGCTCTGGCAAGAAGCTGGAGGACAACCCCAAGTCCCTGAAGTCTGGAGACGCGGCC
ATCGTGGAGATGGTGCCGGGAAAGCCCATGTGTGTGGAGAGCTTCTCCCAGTACCCGCCT
CTCGGCCGCTTCGCCGTGCGCGACATGAGGCAGACGGTGGCCGTAGGCGTCATCAAGAAC
GTGGAAAAGAAGAGCGGCGGCGCCGGCAAGGTCACCAAGTCGGCGCAGAAGGCGCAGAAG
GCGGGCAAGTGA
Enzyme 87 GenBank Gene ID X70940 Link Image
Enzyme 87 GeneCard ID EEF1A2 Link Image
Enzyme 87 GenAtlas ID EEF1A2 Link Image
Enzyme 87 HGNC ID HGNC:3192 Link Image
Enzyme 87 Chromosome Location 2
Enzyme 87 Locus 20q13.3
Enzyme 87 SNPs SNPJam Report Link Image
Enzyme 87 General References
  1. Knudsen SM, Frydenberg J, Clark BF, Leffers H: Tissue-dependent variation in the expression of elongation factor-1 alpha isoforms: isolation and characterisation of a cDNA encoding a novel variant of human elongation-factor 1 alpha. Eur J Biochem. 1993 Aug 1;215(3):549-54. [PubMed Link Image]
  2. Bischoff C, Kahns S, Lund A, Jorgensen HF, Praestegaard M, Clark BF, Leffers H: The human elongation factor 1 A-2 gene (EEF1A2): complete sequence and characterization of gene structure and promoter activity. Genomics. 2000 Aug 15;68(1):63-70. [PubMed Link Image]
  3. Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7. [PubMed Link Image]
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Lee S, Ann DK, Wang E: Cloning of human and mouse brain cDNAs coding for S1, the second member of the mammalian elongation factor-1 alpha gene family: analysis of a possible evolutionary pathway. Biochem Biophys Res Commun. 1994 Sep 30;203(3):1371-7. [PubMed Link Image]
  7. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  8. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  9. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  10. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  12. Dai S, Crawford F, Marrack P, Kappler JW: The structure of HLA-DR52c: comparison to other HLA-DRB3 alleles. Proc Natl Acad Sci U S A. 2008 Aug 19;105(33):11893-7. Epub 2008 Aug 12. [PubMed Link Image]
Enzyme 87 Metabolite References Not Available
Enzyme 88 [top]
Enzyme 88 ID 7342
Enzyme 88 Name Vinexin
Enzyme 88 Synonyms
  1. SH3-containing adapter molecule 1
  2. SCAM-1
  3. Sorbin and SH3 domain-containing protein 3
Enzyme 88 Gene Name SORBS3
Enzyme 88 Protein Sequence >Vinexin
MQGPPRSLRAGLSLDDFIPGHLQSHIGSSSRGTRVPVIRNGGSNTLNFQFHDPAPRTVCN
GGYTPRRDASQHPDPAWYQTWPGPGSKPSASTKIPASQHTQNWSATWTKDSKRRDKRWVK
YEGIGPVDESGMPIAPRSSVDRPRDWYRRMFQQIHRKMPDLQLDWTFEEPPRDPRHLGAQ
QRPAHRPGPATSSSGRSWDHSEELPRSTFNYRPGAFSTVLQPSNQVLRRREKVDNVWTEE
SWNQFLQELETGQRPKKPLVDDPGEKPSQPIEVLLERELAELSAELDKDLRAIETRLPSP
KSSPAPRRAPEQRPPAGPASAWSSSYPHAPYLGSARSLSPHKMADGGSPFLGRRDFVYPS
STRDPSASNGGGSPARREEKKRKAARLKFDFQAQSPKELTLQKGDIVYIHKEVDKNWLEG
EHHGRLGIFPANYVEVLPADEIPKPIKPPTYQVLEYGEAVAQYTFKGDLEVELSFRKGEH
ICLIRKVNENWYEGRITGTGRQGIFPASYVQVSREPRLRLCDDGPQLPTSPRLTAAARSA
RHPSSPSALRSPADPTDLGGQTSPRRTGFSFPTQEPRPQTQNLGTPGPALSHSRGPSHPL
DLGTSSPNTSQIHWTPYRAMYQYRPQNEDELELREGDRVDVMQQCDDGWFVGVSRRTQKF
GTFPGNYVAPV
Enzyme 88 Number of Residues 671
Enzyme 88 Molecular Weight 75328.4
Enzyme 88 Theoretical pI 9.87
Enzyme 88 GO Classification Not Available
Enzyme 88 General Function Involved in structural constituent of cytoskeleton
Enzyme 88 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 88 Pathways Not Available
Enzyme 88 Reactions Not Available
Enzyme 88 Pfam Domain Function
Enzyme 88 Signals
  • None
Enzyme 88 Transmembrane Regions
  • None
Enzyme 88 Essentiality Not Available
Enzyme 88 GenBank ID Protein 155030230 Link Image
Enzyme 88 UniProtKB/Swiss-Prot ID O60504 Link Image
Enzyme 88 UniProtKB/Swiss-Prot Entry Name VINEX_HUMAN Link Image
Enzyme 88 PDB ID Not Available
Enzyme 88 Cellular Location Not Available
Enzyme 88 Gene Sequence >2016 bp
ATGCAGGGCCCACCCCGCAGCCTCCGCGCTGGGCTCAGCCTGGACGACTTCATCCCTGGC
CACCTCCAGTCCCACATAGGGTCTTCCTCCCGGGGGACACGGGTGCCCGTGATCCGGAAT
GGTGGCTCCAACACCCTTAATTTCCAGTTCCACGACCCCGCGCCCAGGACTGTGTGCAAT
GGGGGCTACACACCAAGACGAGATGCTTCCCAGCACCCGGACCCTGCGTGGTATCAGACC
TGGCCAGGCCCTGGGAGCAAGCCCTCTGCAAGCACAAAGATCCCTGCCTCCCAGCACACC
CAGAACTGGTCAGCCACGTGGACCAAGGACAGCAAGCGTCGGGACAAGCGCTGGGTCAAG
TACGAGGGAATCGGGCCCGTGGACGAGAGCGGCATGCCCATTGCCCCCCGATCCAGCGTT
GACAGACCCAGAGACTGGTACCGGAGAATGTTCCAGCAGATTCACCGGAAAATGCCAGAC
TTGCAGCTGGACTGGACCTTCGAGGAGCCACCCAGAGACCCCAGGCATCTAGGAGCCCAG
CAAAGACCTGCCCACAGGCCCGGCCCGGCAACATCTTCCAGTGGAAGAAGCTGGGACCAC
TCTGAAGAGTTACCTAGAAGCACCTTCAACTACAGACCTGGAGCATTCTCCACTGTGCTG
CAGCCCTCAAATCAGGTGCTCAGACGCCGGGAAAAAGTAGACAATGTCTGGACGGAAGAG
TCCTGGAACCAGTTTCTGCAGGAACTAGAGACTGGGCAGAGGCCCAAGAAACCGCTGGTG
GACGACCCTGGTGAGAAGCCCTCCCAGCCCATTGAGGTGCTGCTGGAGAGAGAGCTGGCC
GAGCTGAGCGCCGAGCTGGACAAGGACCTGCGGGCAATTGAGACCCGACTGCCGTCCCCC
AAGAGCTCGCCGGCGCCCCGACGGGCCCCGGAGCAGCGGCCCCCGGCCGGCCCGGCCTCA
GCCTGGAGCTCCAGCTACCCACATGCACCTTACCTGGGTTCCGCCCGGTCCCTGAGTCCC
CACAAAATGGCTGATGGAGGAAGCCCCTTCCTAGGTCGGAGGGACTTTGTCTACCCTTCC
TCAACCCGAGACCCTAGTGCCTCTAACGGAGGGGGCAGCCCAGCCAGGAGGGAAGAGAAG
AAGAGAAAGGCCGCCAGGCTCAAGTTTGACTTCCAGGCGCAGTCCCCCAAGGAGCTGACT
CTGCAGAAGGGTGACATTGTCTACATCCACAAGGAGGTGGACAAGAACTGGCTGGAGGGA
GAGCACCACGGCCGCCTGGGCATCTTCCCTGCTAATTATGTGGAGGTGCTGCCCGCAGAT
GAGATCCCTAAGCCCATCAAGCCCCCGACCTACCAGGTGCTGGAGTATGGAGAGGCTGTG
GCCCAGTACACCTTCAAGGGGGACCTGGAGGTGGAGCTGTCCTTCCGCAAGGGAGAGCAC
ATCTGCCTGATCCGCAAGGTGAACGAGAACTGGTACGAGGGACGCATCACGGGCACGGGG
CGCCAAGGCATATTCCCTGCCAGCTACGTGCAGGTGTCTCGTGAACCCCGGCTCCGGCTC
TGTGACGACGGCCCCCAGCTCCCCACGTCTCCCCGCCTGACCGCTGCCGCCCGCTCAGCC
CGTCACCCCAGCTCCCCCTCAGCCCTGCGCAGCCCAGCTGACCCCATCGACTTGGGGGGA
CAGACCTCCCCCCGTCGCACTGGCTTCTCCTTCCCCACCCAGGAGCCTAGACCCCAGACC
CAGAATCTTGGCACCCCTGGTCCAGCTCTGTCCCACTCTCGAGGTCCCAGCCATCCCCTG
GACCTGGGGACCTCCTCTCCTAACACCTCTCAGATACACTGGACCCCGTACCGGGCGATG
TACCAGTACAGGCCCCAGAACGAAGACGAGCTGGAGCTGCGCGAGGGGGACAGGGTGGAT
GTCATGCAGCAGTGTGACGATGGCTGGTTTGTGGGTGTCTCCCGGAGGACCCAGAAATTC
GGAACGTTCCCTGGAAATTACGTTGCCCCGGTGTGA
Enzyme 88 GenBank Gene ID NM_005775.4 Link Image
Enzyme 88 GeneCard ID SORBS3 Link Image
Enzyme 88 GenAtlas ID SORBS3 Link Image
Enzyme 88 HGNC ID HGNC:30907 Link Image
Enzyme 88 Chromosome Location 8
Enzyme 88 Locus 8p21.3
Enzyme 88 SNPs SNPJam Report Link Image
Enzyme 88 General References
  1. Kioka N, Sakata S, Kawauchi T, Amachi T, Akiyama SK, Okazaki K, Yaen C, Yamada KM, Aota S: Vinexin: a novel vinculin-binding protein with multiple SH3 domains enhances actin cytoskeletal organization. J Cell Biol. 1999 Jan 11;144(1):59-69. [PubMed Link Image]
  2. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Akamatsu M, Aota S, Suwa A, Ueda K, Amachi T, Yamada KM, Akiyama SK, Kioka N: Vinexin forms a signaling complex with Sos and modulates epidermal growth factor-induced c-Jun N-terminal kinase/stress-activated protein kinase activities. J Biol Chem. 1999 Dec 10;274(50):35933-7. [PubMed Link Image]
  5. Townson SM, Dobrzycka KM, Lee AV, Air M, Deng W, Kang K, Jiang S, Kioka N, Michaelis K, Oesterreich S: SAFB2, a new scaffold attachment factor homolog and estrogen receptor corepressor. J Biol Chem. 2003 May 30;278(22):20059-68. Epub 2003 Mar 26. [PubMed Link Image]
  6. Martens N, Wery M, Wang P, Braet F, Gertler A, Hooghe R, Vandenhaute J, Hooghe-Peters EL: The suppressor of cytokine signaling (SOCS)-7 interacts with the actin cytoskeleton through vinexin. Exp Cell Res. 2004 Aug 1;298(1):239-48. [PubMed Link Image]
  7. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  8. Paternotte N, Zhang J, Vandenbroere I, Backers K, Blero D, Kioka N, Vanderwinden JM, Pirson I, Erneux C: SHIP2 interaction with the cytoskeletal protein Vinexin. FEBS J. 2005 Dec;272(23):6052-66. [PubMed Link Image]
  9. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  10. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  11. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  12. Ito H, Atsuzawa K, Sudo K, Di Stefano P, Iwamoto I, Morishita R, Takei S, Semba R, Defilippi P, Asano T, Usuda N, Nagata K: Characterization of a multidomain adaptor protein, p140Cap, as part of a pre-synaptic complex. J Neurochem. 2008 Oct;107(1):61-72. Epub 2008 Jul 24. [PubMed Link Image]
  13. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  14. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  15. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  16. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  17. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  18. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 88 Metabolite References Not Available
Enzyme 89 [top]
Enzyme 89 ID 7350
Enzyme 89 Name Ras-related protein Rab-1A
Enzyme 89 Synonyms
  1. YPT1-related protein
Enzyme 89 Gene Name RAB1A
Enzyme 89 Protein Sequence >Ras-related protein Rab-1A
MSSMNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTI
KLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESFNNVKQWLQEIDRYASENVNKL
LVGNKCDLTTKKVVDYTTAKEFADSLGIPFLETSAKNATNVEQSFMTMAAEIKKRMGPGA
TAGGAEKSNVKIQSTPVKQSGGGCC
Enzyme 89 Number of Residues 205
Enzyme 89 Molecular Weight 22677.6
Enzyme 89 Theoretical pI 6.00
Enzyme 89 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • biological regulation
  • establishment of localization
  • intracellular signal transduction
  • protein transport
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
  • transport
Component
Enzyme 89 General Function Involved in GTP binding
Enzyme 89 Specific Function Probably required for transit of protein from the ER through Golgi compartment. Binds GTP and GDP and possesses intrinsic GTPase activity
Enzyme 89 Pathways Not Available
Enzyme 89 Reactions Not Available
Enzyme 89 Pfam Domain Function
Enzyme 89 Signals
  • None
Enzyme 89 Transmembrane Regions
  • None
Enzyme 89 Essentiality Not Available
Enzyme 89 GenBank ID Protein 20379034 Link Image
Enzyme 89 UniProtKB/Swiss-Prot ID P62820 Link Image
Enzyme 89 UniProtKB/Swiss-Prot Entry Name RAB1A_HUMAN Link Image
Enzyme 89 PDB ID Not Available
Enzyme 89 Cellular Location Not Available
Enzyme 89 Gene Sequence >618 bp
ATGTCCAGCATGAATCCCGAATATGATTATTTATTCAAGTTACTTCTGATTGGCGACTCA
GGGGTTGGAAAGTCTTGCCTTCTTCTTAGGTTTGCAGATGATACATATACAGAAAGCTAC
ATCAGCACAATTGGTGTGGATTTCAAAATAAGAACTATAGAGTTAGACGGGAAAACAATC
AAGCTTCAAATATGGGACACAGCAGGCCAGGAAAGATTTCGAACAATCACCTCCAGTTAT
TACAGAGGAGCCCATGGCATCATAGTTGTGTATGATGTGACAGATCAGGAGTCCTTCAAT
AATGTTAAACAGTGGCTGCAGGAAATAGATCGTTATGCCAGTGAAAATGTCAACAAATTG
TTGGTAGGGAACAAATGTGATCTGACCACAAAGAAAGTAGTAGACTACACAACAGCGAAG
GAATTTGCTGATTCCCTTGGAATTCCGTTTTTGGAAACCAGTGCTAAGAATGCAACGAAT
GTAGAACAGTCTTTCATGACGATGGCAGCTGAGATTAAAAAGCGAATGGGTCCCGGAGCA
ACAGCTGGTGGTGCTGAGAAGTCCAATGTTAAAATTCAGAGCACTCCAGTCAAGCAGTCA
GGTGGAGGTTGCTGCTAA
Enzyme 89 GenBank Gene ID AF498929 Link Image
Enzyme 89 GeneCard ID RAB1A Link Image
Enzyme 89 GenAtlas ID RAB1A Link Image
Enzyme 89 HGNC ID HGNC:9758 Link Image
Enzyme 89 Chromosome Location 2
Enzyme 89 Locus 2p14
Enzyme 89 SNPs SNPJam Report Link Image
Enzyme 89 General References
  1. Zahraoui A, Touchot N, Chardin P, Tavitian A: The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion. J Biol Chem. 1989 Jul 25;264(21):12394-401. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Bailly E, McCaffrey M, Touchot N, Zahraoui A, Goud B, Bornens M: Phosphorylation of two small GTP-binding proteins of the Rab family by p34cdc2. Nature. 1991 Apr 25;350(6320):715-8. [PubMed Link Image]
  7. Farnsworth CC, Seabra MC, Ericsson LH, Gelb MH, Glomset JA: Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A. Proc Natl Acad Sci U S A. 1994 Dec 6;91(25):11963-7. [PubMed Link Image]
Enzyme 89 Metabolite References Not Available
Enzyme 90 [top]
Enzyme 90 ID 7383
Enzyme 90 Name GTPase HRas
Enzyme 90 Synonyms
  1. H-Ras-1
  2. Ha-Ras
  3. Transforming protein p21
  4. c-H-ras
  5. p21ras
  6. GTPase HRas, N-terminally processed
Enzyme 90 Gene Name HRAS
Enzyme 90 Protein Sequence >GTPase HRas
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG
QEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL
AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPG
CMSCKCVLS
Enzyme 90 Number of Residues 189
Enzyme 90 Molecular Weight 21298.0
Enzyme 90 Theoretical pI 4.94
Enzyme 90 GO Classification
Function
  • GTP binding
  • GTPase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
  • membrane
Enzyme 90 General Function Involved in GTP binding
Enzyme 90 Specific Function Ras proteins bind GDP/GTP and possess intrinsic GTPase activity
Enzyme 90 Pathways Not Available
Enzyme 90 Reactions Not Available
Enzyme 90 Pfam Domain Function
Enzyme 90 Signals
  • None
Enzyme 90 Transmembrane Regions
  • None
Enzyme 90 Essentiality Not Available
Enzyme 90 GenBank ID Protein 20147725 Link Image
Enzyme 90 UniProtKB/Swiss-Prot ID P01112 Link Image
Enzyme 90 UniProtKB/Swiss-Prot Entry Name RASH_HUMAN Link Image
Enzyme 90 PDB ID 4Q21 Link Image
Enzyme 90 PDB File Show
Enzyme 90 3D Structure
Enzyme 90 Cellular Location Not Available
Enzyme 90 Gene Sequence >570 bp
ATGACGGAATATAAGCTGGTGGTGGTGGGCGCCGGCGGTGTGGGCAAGAGTGCGCTGACC
ATCCAGCTGATCCAGAACCATTTTGTGGACGAATACGACCCCACTATAGAGGATTCCTAC
CGGAAGCAGGTGGTCATTGATGGGGAGACGTGCCTGTTGGACATCCTGGATACCGCCGGC
CAGGAGGAGTACAGCGCCATGCGGGACCAGTACATGCGCACCGGGGAGGGCTTCCTGTGT
GTGTTTGCCATCAACAACACCAAGTCTTTTGAGGACATCCACCAGTACAGGGAGCAGATC
AAACGGGTGAAGGACTCGGATGACGTGCCCATGGTGCTGGTGGGGAACAAGTGTGACCTG
GCTGCACGCACTGTGGAATCTCGGCAGGCTCAGGACCTCGCCCGAAGCTACGGCATCCCC
TACATCGAGACCTCGGCCAAGACCCGGCAGGGAGTGGAGGATGCCTTCTACACGTTGGTG
CGTGAGATCCGGCAGCACAAGCTGCGGAAGCTGAACCCTCCTGATGAGAGTGGCCCCGGC
TGCATGAGCTGCAAGTGTGTGCTCTCCTGA
Enzyme 90 GenBank Gene ID AF493916 Link Image
Enzyme 90 GeneCard ID HRAS Link Image
Enzyme 90 GenAtlas ID HRAS Link Image
Enzyme 90 HGNC ID HGNC:5173 Link Image
Enzyme 90 Chromosome Location 1
Enzyme 90 Locus 11p15.5
Enzyme 90 SNPs SNPJam Report Link Image
Enzyme 90 General References
  1. Capon DJ, Chen EY, Levinson AD, Seeburg PH, Goeddel DV: Complete nucleotide sequences of the T24 human bladder carcinoma oncogene and its normal homologue. Nature. 1983 Mar 3;302(5903):33-7. [PubMed Link Image]
  2. Reddy EP: Nucleotide sequence analysis of the T24 human bladder carcinoma oncogene. Science. 1983 Jun 3;220(4601):1061-3. [PubMed Link Image]
  3. Sekiya T, Fushimi M, Hori H, Hirohashi S, Nishimura S, Sugimura T: Molecular cloning and the total nucleotide sequence of the human c-Ha-ras-1 gene activated in a melanoma from a Japanese patient. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4771-5. [PubMed Link Image]
  4. Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Tabin CJ, Bradley SM, Bargmann CI, Weinberg RA, Papageorge AG, Scolnick EM, Dhar R, Lowy DR, Chang EH: Mechanism of activation of a human oncogene. Nature. 1982 Nov 11;300(5888):143-9. [PubMed Link Image]
  7. Honkawa H, Masahashi W, Hashimoto S, Hashimoto-Gotoh T: Identification of the principal promoter sequence of the c-H-ras transforming oncogene: deletion analysis of the 5'-flanking region by focus formation assay. Mol Cell Biol. 1987 Aug;7(8):2933-40. [PubMed Link Image]
  8. Low A, Sprinzl M, Faulhammer HG: Affinity labeling of c-H-ras p21 consensus elements with periodate-oxidized GDP and GTP. Eur J Biochem. 1993 Jul 15;215(2):473-9. [PubMed Link Image]
  9. Feig LA, Pan BT, Roberts TM, Cooper GM: Isolation of ras GTP-binding mutants using an in situ colony-binding assay. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4607-11. [PubMed Link Image]
  10. Lacal JC, Anderson PS, Aaronson SA: Deletion mutants of Harvey ras p21 protein reveal the absolute requirement of at least two distant regions for GTP-binding and transforming activities. EMBO J. 1986 Apr;5(4):679-87. [PubMed Link Image]
  11. Hancock JF, Magee AI, Childs JE, Marshall CJ: All ras proteins are polyisoprenylated but only some are palmitoylated. Cell. 1989 Jun 30;57(7):1167-77. [PubMed Link Image]
  12. Dudler T, Gelb MH: Palmitoylation of Ha-Ras facilitates membrane binding, activation of downstream effectors, and meiotic maturation in Xenopus oocytes. J Biol Chem. 1996 May 10;271(19):11541-7. [PubMed Link Image]
  13. Lander HM, Hajjar DP, Hempstead BL, Mirza UA, Chait BT, Campbell S, Quilliam LA: A molecular redox switch on p21(ras). Structural basis for the nitric oxide-p21(ras) interaction. J Biol Chem. 1997 Feb 14;272(7):4323-6. [PubMed Link Image]
  14. Song C, Hu CD, Masago M, Kariyai K, Yamawaki-Kataoka Y, Shibatohge M, Wu D, Satoh T, Kataoka T: Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras. J Biol Chem. 2001 Jan 26;276(4):2752-7. Epub 2000 Oct 5. [PubMed Link Image]
  15. Topham MK, Prescott SM: Diacylglycerol kinase zeta regulates Ras activation by a novel mechanism. J Cell Biol. 2001 Mar 19;152(6):1135-43. [PubMed Link Image]
  16. Swarthout JT, Lobo S, Farh L, Croke MR, Greentree WK, Deschenes RJ, Linder ME: DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H- and N-Ras. J Biol Chem. 2005 Sep 2;280(35):31141-8. Epub 2005 Jul 6. [PubMed Link Image]
  17. Rocks O, Peyker A, Kahms M, Verveer PJ, Koerner C, Lumbierres M, Kuhlmann J, Waldmann H, Wittinghofer A, Bastiaens PI: An acylation cycle regulates localization and activity of palmitoylated Ras isoforms. Science. 2005 Mar 18;307(5716):1746-52. Epub 2005 Feb 10. [PubMed Link Image]
  18. Pan F, Sun L, Kardian DB, Whartenby KA, Pardoll DM, Liu JO: Feedback inhibition of calcineurin and Ras by a dual inhibitory protein Carabin. Nature. 2007 Jan 25;445(7126):433-6. Epub 2007 Jan 17. [PubMed Link Image]
  19. de Vos AM, Tong L, Milburn MV, Matias PM, Jancarik J, Noguchi S, Nishimura S, Miura K, Ohtsuka E, Kim SH: Three-dimensional structure of an oncogene protein: catalytic domain of human c-H-ras p21. Science. 1988 Feb 19;239(4842):888-93. [PubMed Link Image]
  20. Pai EF, Kabsch W, Krengel U, Holmes KC, John J, Wittinghofer A: Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. Nature. 1989 Sep 21;341(6239):209-14. [PubMed Link Image]
  21. Pai EF, Krengel U, Petsko GA, Goody RS, Kabsch W, Wittinghofer A: Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 1990 Aug;9(8):2351-9. [PubMed Link Image]
  22. Tong LA, de Vos AM, Milburn MV, Kim SH: Crystal structures at 2.2 A resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP. J Mol Biol. 1991 Feb 5;217(3):503-16. [PubMed Link Image]
  23. Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED: Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy. Biochemistry. 1994 Mar 29;33(12):3515-31. [PubMed Link Image]
  24. Scheffzek K, Ahmadian MR, Kabsch W, Wiesmuller L, Lautwein A, Schmitz F, Wittinghofer A: The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science. 1997 Jul 18;277(5324):333-8. [PubMed Link Image]
  25. Scheidig AJ, Burmester C, Goody RS: The pre-hydrolysis state of p21(ras) in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins. Structure. 1999 Nov 15;7(11):1311-24. [PubMed Link Image]
  26. Hall BE, Bar-Sagi D, Nassar N: The structural basis for the transition from Ras-GTP to Ras-GDP. Proc Natl Acad Sci U S A. 2002 Sep 17;99(19):12138-42. Epub 2002 Sep 4. [PubMed Link Image]
  27. Williams JG, Pappu K, Campbell SL: Structural and biochemical studies of p21Ras S-nitrosylation and nitric oxide-mediated guanine nucleotide exchange. Proc Natl Acad Sci U S A. 2003 May 27;100(11):6376-81. Epub 2003 May 9. [PubMed Link Image]
  28. Buhrman G, Wink G, Mattos C: Transformation efficiency of RasQ61 mutants linked to structural features of the switch regions in the presence of Raf. Structure. 2007 Dec;15(12):1618-29. [PubMed Link Image]
  29. Stieglitz B, Bee C, Schwarz D, Yildiz O, Moshnikova A, Khokhlatchev A, Herrmann C: Novel type of Ras effector interaction established between tumour suppressor NORE1A and Ras switch II. EMBO J. 2008 Jul 23;27(14):1995-2005. Epub 2008 Jul 3. [PubMed Link Image]
  30. Sakai E, Rikimaru K, Ueda M, Matsumoto Y, Ishii N, Enomoto S, Yamamoto H, Tsuchida N: The p53 tumor-suppressor gene and ras oncogene mutations in oral squamous-cell carcinoma. Int J Cancer. 1992 Dec 2;52(6):867-72. [PubMed Link Image]
  31. Nikiforova MN, Lynch RA, Biddinger PW, Alexander EK, Dorn GW 2nd, Tallini G, Kroll TG, Nikiforov YE: RAS point mutations and PAX8-PPAR gamma rearrangement in thyroid tumors: evidence for distinct molecular pathways in thyroid follicular carcinoma. J Clin Endocrinol Metab. 2003 May;88(5):2318-26. [PubMed Link Image]
  32. Aoki Y, Niihori T, Kawame H, Kurosawa K, Ohashi H, Tanaka Y, Filocamo M, Kato K, Suzuki Y, Kure S, Matsubara Y: Germline mutations in HRAS proto-oncogene cause Costello syndrome. Nat Genet. 2005 Oct;37(10):1038-40. Epub 2005 Sep 18. [PubMed Link Image]
  33. Gripp KW, Lin AE, Stabley DL, Nicholson L, Scott CI Jr, Doyle D, Aoki Y, Matsubara Y, Zackai EH, Lapunzina P, Gonzalez-Meneses A, Holbrook J, Agresta CA, Gonzalez IL, Sol-Church K: HRAS mutation analysis in Costello syndrome: genotype and phenotype correlation. Am J Med Genet A. 2006 Jan 1;140(1):1-7. [PubMed Link Image]
  34. Kerr B, Delrue MA, Sigaudy S, Perveen R, Marche M, Burgelin I, Stef M, Tang B, Eden OB, O'Sullivan J, De Sandre-Giovannoli A, Reardon W, Brewer C, Bennett C, Quarell O, M'Cann E, Donnai D, Stewart F, Hennekam R, Cave H, Verloes A, Philip N, Lacombe D, Levy N, Arveiler B, Black G: Genotype-phenotype correlation in Costello syndrome: HRAS mutation analysis in 43 cases. J Med Genet. 2006 May;43(5):401-5. Epub 2006 Jan 27. [PubMed Link Image]
  35. Zampino G, Pantaleoni F, Carta C, Cobellis G, Vasta I, Neri C, Pogna EA, De Feo E, Delogu A, Sarkozy A, Atzeri F, Selicorni A, Rauen KA, Cytrynbaum CS, Weksberg R, Dallapiccola B, Ballabio A, Gelb BD, Neri G, Tartaglia M: Diversity, parental germline origin, and phenotypic spectrum of de novo HRAS missense changes in Costello syndrome. Hum Mutat. 2007 Mar;28(3):265-72. [PubMed Link Image]
  36. van der Burgt I, Kupsky W, Stassou S, Nadroo A, Barroso C, Diem A, Kratz CP, Dvorsky R, Ahmadian MR, Zenker M: Myopathy caused by HRAS germline mutations: implications for disturbed myogenic differentiation in the presence of constitutive HRas activation. J Med Genet. 2007 Jul;44(7):459-62. Epub 2007 Apr 5. [PubMed Link Image]
  37. Gripp KW, Innes AM, Axelrad ME, Gillan TL, Parboosingh JS, Davies C, Leonard NJ, Lapointe M, Doyle D, Catalano S, Nicholson L, Stabley DL, Sol-Church K: Costello syndrome associated with novel germline HRAS mutations: an attenuated phenotype? Am J Med Genet A. 2008 Mar 15;146A(6):683-90. [PubMed Link Image]
Enzyme 90 Metabolite References Not Available
Enzyme 91 [top]
Enzyme 91 ID 7384
Enzyme 91 Name Transforming protein RhoA
Enzyme 91 Synonyms
  1. Rho cDNA clone 12
  2. h12
Enzyme 91 Gene Name RHOA
Enzyme 91 Protein Sequence >Transforming protein RhoA
MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDT
AGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKD
LRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQ
ARRGKKKSGCLVL
Enzyme 91 Number of Residues 193
Enzyme 91 Molecular Weight 21767.9
Enzyme 91 Theoretical pI 5.89
Enzyme 91 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 91 General Function Involved in GTP binding
Enzyme 91 Specific Function Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP
Enzyme 91 Pathways Not Available
Enzyme 91 Reactions Not Available
Enzyme 91 Pfam Domain Function
Enzyme 91 Signals
  • None
Enzyme 91 Transmembrane Regions
  • None
Enzyme 91 Essentiality Not Available
Enzyme 91 GenBank ID Protein 36030 Link Image
Enzyme 91 UniProtKB/Swiss-Prot ID P61586 Link Image
Enzyme 91 UniProtKB/Swiss-Prot Entry Name RHOA_HUMAN Link Image
Enzyme 91 PDB ID 1X86 Link Image
Enzyme 91 PDB File Show
Enzyme 91 3D Structure
Enzyme 91 Cellular Location Not Available
Enzyme 91 Gene Sequence >582 bp
ATGGCTGCCATCCGGAAGAAACTGGTGATTGTTGGTGATGGAGCCTGTGGAAAGACATGC
TTGCTCATAGTCTTCAGCAAGGACCAGTTCCCAGAGGTGTATGTGCCCACAGTGTTTGAG
AACTATGTGGCAGATATCGAGGTGGATGGAAAGCAGGTAGAGTTGGCTTTGTGGGACACA
GCTGGGCAGGAAGATTATGATCGCCTGAGGCCCCTCTCCTACCCAGATACCGATGTTATA
CTGATGTGTTTTTCCATCGACAGCCCTGATAGTTTAGAAAACATCCCAGAAAAGTGGACC
CCAGAAGTCAAGCATTTCTGTCCCAACGTGCCCATCATCCTGGTTGGGAATAAGAAGGAT
CTTCGGAATGATGAGCACACAAGGCGGGAGCTAGCCAAGATGAAGCAGGAGCCGGTGAAA
CCTGAAGAAGGCAGAGATATGGCAAACAGGATTGGCGCTTTTGGGTACATGGAGTGTTCA
GCAAAGACCAAAGATGGAGTGAGAGAGGTTTTTGAAATGGCTACGAGAGCTGCTCTGCAA
GCTAGACGTGGGAAGAAAAAATCTGGTTGCCTTGTCTTGTGA
Enzyme 91 GenBank Gene ID X05026 Link Image
Enzyme 91 GeneCard ID RHOA Link Image
Enzyme 91 GenAtlas ID RHOA Link Image
Enzyme 91 HGNC ID HGNC:667 Link Image
Enzyme 91 Chromosome Location 3
Enzyme 91 Locus 3p21.3
Enzyme 91 SNPs SNPJam Report Link Image
Enzyme 91 General References
  1. Yeramian P, Chardin P, Madaule P, Tavitian A: Nucleotide sequence of human rho cDNA clone 12. Nucleic Acids Res. 1987 Feb 25;15(4):1869. [PubMed Link Image]
  2. Fagan KP, Oliveira L, Pittler SJ: Sequence of rho small GTP-binding protein cDNAs from human retina and identification of novel 5' end cloning artifacts. Exp Eye Res. 1994 Aug;59(2):235-7. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Moscow JA, He R, Gudas JM, Cowan KH: Utilization of multiple polyadenylation signals in the human RHOA protooncogene. Gene. 1994 Jul 8;144(2):229-36. [PubMed Link Image]
  6. Nemoto Y, Namba T, Teru-uchi T, Ushikubi F, Morii N, Narumiya S: A rho gene product in human blood platelets. I. Identification of the platelet substrate for botulinum C3 ADP-ribosyltransferase as rhoA protein. J Biol Chem. 1992 Oct 15;267(29):20916-20. [PubMed Link Image]
  7. Moscow JA, Morrow CS, He R, Mullenbach GT, Cowan KH: Structure and function of the 5'-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1). J Biol Chem. 1992 Mar 25;267(9):5949-58. [PubMed Link Image]
  8. Ishizaki T, Maekawa M, Fujisawa K, Okawa K, Iwamatsu A, Fujita A, Watanabe N, Saito Y, Kakizuka A, Morii N, Narumiya S: The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase. EMBO J. 1996 Apr 15;15(8):1885-93. [PubMed Link Image]
  9. Matsui T, Amano M, Yamamoto T, Chihara K, Nakafuku M, Ito M, Nakano T, Okawa K, Iwamatsu A, Kaibuchi K: Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho. EMBO J. 1996 May 1;15(9):2208-16. [PubMed Link Image]
  10. Ren Y, Li R, Zheng Y, Busch H: Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases. J Biol Chem. 1998 Dec 25;273(52):34954-60. [PubMed Link Image]
  11. Houssa B, de Widt J, Kranenburg O, Moolenaar WH, van Blitterswijk WJ: Diacylglycerol kinase theta binds to and is negatively regulated by active RhoA. J Biol Chem. 1999 Mar 12;274(11):6820-2. [PubMed Link Image]
  12. Pastey MK, Crowe JE Jr, Graham BS: RhoA interacts with the fusion glycoprotein of respiratory syncytial virus and facilitates virus-induced syncytium formation. J Virol. 1999 Sep;73(9):7262-70. [PubMed Link Image]
  13. Reynaud C, Fabre S, Jalinot P: The PDZ protein TIP-1 interacts with the Rho effector rhotekin and is involved in Rho signaling to the serum response element. J Biol Chem. 2000 Oct 27;275(43):33962-8. [PubMed Link Image]
  14. Klussmann E, Edemir B, Pepperle B, Tamma G, Henn V, Klauschenz E, Hundsrucker C, Maric K, Rosenthal W: Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling. FEBS Lett. 2001 Nov 2;507(3):264-8. [PubMed Link Image]
  15. Arthur WT, Ellerbroek SM, Der CJ, Burridge K, Wennerberg K: XPLN, a guanine nucleotide exchange factor for RhoA and RhoB, but not RhoC. J Biol Chem. 2002 Nov 8;277(45):42964-72. Epub 2002 Sep 6. [PubMed Link Image]
  16. Shao F, Merritt PM, Bao Z, Innes RW, Dixon JE: A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis. Cell. 2002 May 31;109(5):575-88. [PubMed Link Image]
  17. Wing MR, Snyder JT, Sondek J, Harden TK: Direct activation of phospholipase C-epsilon by Rho. J Biol Chem. 2003 Oct 17;278(42):41253-8. Epub 2003 Aug 4. [PubMed Link Image]
  18. Shao F, Vacratsis PO, Bao Z, Bowers KE, Fierke CA, Dixon JE: Biochemical characterization of the Yersinia YopT protease: cleavage site and recognition elements in Rho GTPases. Proc Natl Acad Sci U S A. 2003 Feb 4;100(3):904-9. Epub 2003 Jan 21. [PubMed Link Image]
  19. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  20. Worby CA, Mattoo S, Kruger RP, Corbeil LB, Koller A, Mendez JC, Zekarias B, Lazar C, Dixon JE: The fic domain: regulation of cell signaling by adenylylation. Mol Cell. 2009 Apr 10;34(1):93-103. [PubMed Link Image]
  21. Chen Y, Yang Z, Meng M, Zhao Y, Dong N, Yan H, Liu L, Ding M, Peng HB, Shao F: Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement. Mol Cell. 2009 Sep 24;35(6):841-55. [PubMed Link Image]
  22. Yarbrough ML, Li Y, Kinch LN, Grishin NV, Ball HL, Orth K: AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science. 2009 Jan 9;323(5911):269-72. Epub 2008 Nov 27. [PubMed Link Image]
  23. Wei Y, Zhang Y, Derewenda U, Liu X, Minor W, Nakamoto RK, Somlyo AV, Somlyo AP, Derewenda ZS: Crystal structure of RhoA-GDP and its functional implications. Nat Struct Biol. 1997 Sep;4(9):699-703. [PubMed Link Image]
  24. Ihara K, Muraguchi S, Kato M, Shimizu T, Shirakawa M, Kuroda S, Kaibuchi K, Hakoshima T: Crystal structure of human RhoA in a dominantly active form complexed with a GTP analogue. J Biol Chem. 1998 Apr 17;273(16):9656-66. [PubMed Link Image]
  25. Maesaki R, Shimizu T, Ihara K, Kuroda S, Kaibuchi K, Hakoshima T: Biochemical and crystallographic characterization of a Rho effector domain of the protein serine/threonine kinase N in a complex with RhoA. J Struct Biol. 1999 Jun 15;126(2):166-70. [PubMed Link Image]
  26. Shimizu T, Ihara K, Maesaki R, Kuroda S, Kaibuchi K, Hakoshima T: An open conformation of switch I revealed by the crystal structure of a Mg2+-free form of RHOA complexed with GDP. Implications for the GDP/GTP exchange mechanism. J Biol Chem. 2000 Jun 16;275(24):18311-7. [PubMed Link Image]
  27. Graham DL, Lowe PN, Grime GW, Marsh M, Rittinger K, Smerdon SJ, Gamblin SJ, Eccleston JF: MgF(3)(-) as a transition state analog of phosphoryl transfer. Chem Biol. 2002 Mar;9(3):375-81. [PubMed Link Image]
  28. Snyder JT, Worthylake DK, Rossman KL, Betts L, Pruitt WM, Siderovski DP, Der CJ, Sondek J: Structural basis for the selective activation of Rho GTPases by Dbl exchange factors. Nat Struct Biol. 2002 Jun;9(6):468-75. [PubMed Link Image]
  29. Longenecker K, Read P, Lin SK, Somlyo AP, Nakamoto RK, Derewenda ZS: Structure of a constitutively activated RhoA mutant (Q63L) at 1.55 A resolution. Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):876-80. Epub 2003 Apr 25. [PubMed Link Image]
Enzyme 91 Metabolite References Not Available
Enzyme 92 [top]
Enzyme 92 ID 7386
Enzyme 92 Name GTP cyclohydrolase 1 feedback regulatory protein
Enzyme 92 Synonyms
  1. GFRP
  2. GTP cyclohydrolase I feedback regulatory protein
  3. p35
Enzyme 92 Gene Name GCHFR
Enzyme 92 Protein Sequence >GTP cyclohydrolase 1 feedback regulatory protein
MPYLLISTQIRMEVGPTMVGDEQSDPELMQHLGASKRRALGNNFYEYYVDDPPRIVLDKL
ERRGFRVLSMTGVGQTLVWCLHKE
Enzyme 92 Number of Residues 84
Enzyme 92 Molecular Weight 9698.2
Enzyme 92 Theoretical pI 6.51
Enzyme 92 GO Classification
Function
  • binding
  • protein binding
Process
  • biological regulation
  • negative regulation of biosynthetic process
  • regulation of biological process
  • regulation of biosynthetic process
  • regulation of metabolic process
Component
Enzyme 92 General Function Involved in protein binding
Enzyme 92 Specific Function Mediates tetrahydrobiopterin inhibition of GTP cyclohydrolase 1. This inhibition is reversed by L-phenylalanine
Enzyme 92 Pathways Not Available
Enzyme 92 Reactions Not Available
Enzyme 92 Pfam Domain Function
Enzyme 92 Signals
  • None
Enzyme 92 Transmembrane Regions
  • None
Enzyme 92 Essentiality Not Available
Enzyme 92 GenBank ID Protein 189053191 Link Image
Enzyme 92 UniProtKB/Swiss-Prot ID P30047 Link Image
Enzyme 92 UniProtKB/Swiss-Prot Entry Name GFRP_HUMAN Link Image
Enzyme 92 PDB ID 1IS8 Link Image
Enzyme 92 PDB File Show
Enzyme 92 3D Structure
Enzyme 92 Cellular Location Not Available
Enzyme 92 Gene Sequence >255 bp
ATGCCCTACCTGCTCATCAGCACCCAGATCCGCATGGAGGTGGGCCCCACTATGGTGGGC
GATGAACAGTCGGATCCAGAGCTGATGCAGCATCTGGGGGCTTCAAAGAGAAGAGCCTTG
GGAAACAACTTTTATGAATACTACGTCGATGACCCTCCCCGCATAGTCCTGGACAAGCTG
GAACGCAGGGGCTTCCGTGTGCTGAGCATGACGGGGGTGGGCCAGACGCTGGTGTGGTGT
CTGCACAAGGAGTGA
Enzyme 92 GenBank Gene ID AK311872 Link Image
Enzyme 92 GeneCard ID GCHFR Link Image
Enzyme 92 GenAtlas ID GCHFR Link Image
Enzyme 92 HGNC ID HGNC:4194 Link Image
Enzyme 92 Chromosome Location 1
Enzyme 92 Locus 15q15
Enzyme 92 SNPs SNPJam Report Link Image
Enzyme 92 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed Link Image]
  4. Chavan B, Gillbro JM, Rokos H, Schallreuter KU: GTP cyclohydrolase feedback regulatory protein controls cofactor 6-tetrahydrobiopterin synthesis in the cytosol and in the nucleus of epidermal keratinocytes and melanocytes. J Invest Dermatol. 2006 Nov;126(11):2481-9. Epub 2006 Jun 15. [PubMed Link Image]
  5. Swick L, Kapatos G: A yeast 2-hybrid analysis of human GTP cyclohydrolase I protein interactions. J Neurochem. 2006 Jun;97(5):1447-55. [PubMed Link Image]
Enzyme 92 Metabolite References Not Available
Enzyme 93 [top]
Enzyme 93 ID 7388
Enzyme 93 Name ADP-ribosylation factor 1
Enzyme 93 Synonyms Not Available
Enzyme 93 Gene Name ARF1
Enzyme 93 Protein Sequence >ADP-ribosylation factor 1
MGNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKN
ISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAV
LLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQ
K
Enzyme 93 Number of Residues 181
Enzyme 93 Molecular Weight 20696.6
Enzyme 93 Theoretical pI 6.80
Enzyme 93 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 93 General Function Involved in GTP binding
Enzyme 93 Specific Function GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP- ribosyltransferase. Involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles
Enzyme 93 Pathways Not Available
Enzyme 93 Reactions Not Available
Enzyme 93 Pfam Domain Function
Enzyme 93 Signals
  • None
Enzyme 93 Transmembrane Regions
  • None
Enzyme 93 Essentiality Not Available
Enzyme 93 GenBank ID Protein Not Available
Enzyme 93 UniProtKB/Swiss-Prot ID P84077 Link Image
Enzyme 93 UniProtKB/Swiss-Prot Entry Name ARF1_HUMAN Link Image
Enzyme 93 PDB ID 1R8Q Link Image
Enzyme 93 PDB File Show
Enzyme 93 3D Structure
Enzyme 93 Cellular Location Not Available
Enzyme 93 Gene Sequence >546 bp
ATGGGGAACATCTTCGCCAACCTCTTCAAGGGCCTTTTTGGCAAAAAAGAAATGCGCATC
CTCATGGTGGGCCTGGATGCTGCAGGGAAGACCACGATCCTCTACAAGCTTAAGCTGGGT
GAGATCGTGACCACCATTCCCACCATAGGCTTCAACGTGGAAACCGTGGAGTACAAGAAC
ATCAGCTTCACTGTGTGGGACGTGGGTGGCCAGGACAAGATCCGGCCCCTGTGGCGCCAC
TACTTCCAGAACACACAAGGCCTGATCTTCGTGGTGGACAGCAATGACAGAGAGCGTGTG
AACGAGGCCCGTGAGGAGCTCATGAGGATGCTGGCCGAGGACGAGCTCCGGGATGCTGTC
CTCCTGGTGTTCGCCAACAAGCAGGACCTCCCCAACGCCATGAATGCGGCCGAGATCACA
GACAAGCTGGGGCTGCACTCACTACGCCACAGGAACTGGTACATTCAGGCCACCTGCGCC
ACCAGCGGCGACGGGCTCTATGAAGGACTGGACTGGCTGTCCAATCAGCTCCGGAACCAG
AAGTGA
Enzyme 93 GenBank Gene ID M36340 Link Image
Enzyme 93 GeneCard ID ARF1 Link Image
Enzyme 93 GenAtlas ID ARF1 Link Image
Enzyme 93 HGNC ID HGNC:652 Link Image
Enzyme 93 Chromosome Location 1
Enzyme 93 Locus 1q42
Enzyme 93 SNPs SNPJam Report Link Image
Enzyme 93 General References
  1. Bobak DA, Nightingale MS, Murtagh JJ, Price SR, Moss J, Vaughan M: Molecular cloning, characterization, and expression of human ADP-ribosylation factors: two guanine nucleotide-dependent activators of cholera toxin. Proc Natl Acad Sci U S A. 1989 Aug;86(16):6101-5. [PubMed Link Image]
  2. Kahn RA, Kern FG, Clark J, Gelmann EP, Rulka C: Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins. J Biol Chem. 1991 Feb 5;266(4):2606-14. [PubMed Link Image]
  3. Lee CM, Haun RS, Tsai SC, Moss J, Vaughan M: Characterization of the human gene encoding ADP-ribosylation factor 1, a guanine nucleotide-binding activator of cholera toxin. J Biol Chem. 1992 May 5;267(13):9028-34. [PubMed Link Image]
  4. Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Rosa JL, Casaroli-Marano RP, Buckler AJ, Vilaro S, Barbacid M: p619, a giant protein related to the chromosome condensation regulator RCC1, stimulates guanine nucleotide exchange on ARF1 and Rab proteins. EMBO J. 1996 Aug 15;15(16):4262-73. [PubMed Link Image]
  8. Andreev J, Simon JP, Sabatini DD, Kam J, Plowman G, Randazzo PA, Schlessinger J: Identification of a new Pyk2 target protein with Arf-GAP activity. Mol Cell Biol. 1999 Mar;19(3):2338-50. [PubMed Link Image]
  9. Menetrey J, Perderiset M, Cicolari J, Dubois T, Elkhatib N, El Khadali F, Franco M, Chavrier P, Houdusse A: Structural basis for ARF1-mediated recruitment of ARHGAP21 to Golgi membranes. EMBO J. 2007 Apr 4;26(7):1953-62. Epub 2007 Mar 8. [PubMed Link Image]
  10. Haynes LP, Sherwood MW, Dolman NJ, Burgoyne RD: Specificity, promiscuity and localization of ARF protein interactions with NCS-1 and phosphatidylinositol-4 kinase-III beta. Traffic. 2007 Aug;8(8):1080-92. Epub 2007 Jun 6. [PubMed Link Image]
  11. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  12. Amor JC, Harrison DH, Kahn RA, Ringe D: Structure of the human ADP-ribosylation factor 1 complexed with GDP. Nature. 1994 Dec 15;372(6507):704-8. [PubMed Link Image]
  13. Goldberg J: Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis. Cell. 1999 Mar 19;96(6):893-902. [PubMed Link Image]
Enzyme 93 Metabolite References Not Available
Enzyme 94 [top]
Enzyme 94 ID 7390
Enzyme 94 Name Ras-related protein Rap-1A
Enzyme 94 Synonyms
  1. C21KG
  2. G-22K
  3. GTP-binding protein smg p21A
  4. Ras-related protein Krev-1
Enzyme 94 Gene Name RAP1A
Enzyme 94 Protein Sequence >Ras-related protein Rap-1A
MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQQCMLEILDTAG
TEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDL
EDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYDLVRQINRKTPVEKKKPKKKS
CLLL
Enzyme 94 Number of Residues 184
Enzyme 94 Molecular Weight 20987.1
Enzyme 94 Theoretical pI 6.55
Enzyme 94 GO Classification
Function
  • GTP binding
  • GTPase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
  • membrane
Enzyme 94 General Function Involved in GTP binding
Enzyme 94 Specific Function Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner
Enzyme 94 Pathways Not Available
Enzyme 94 Reactions Not Available
Enzyme 94 Pfam Domain Function
Enzyme 94 Signals
  • None
Enzyme 94 Transmembrane Regions
  • None
Enzyme 94 Essentiality Not Available
Enzyme 94 GenBank ID Protein 20147717 Link Image
Enzyme 94 UniProtKB/Swiss-Prot ID P62834 Link Image
Enzyme 94 UniProtKB/Swiss-Prot Entry Name RAP1A_HUMAN Link Image
Enzyme 94 PDB ID 1C1Y Link Image
Enzyme 94 PDB File Show
Enzyme 94 3D Structure
Enzyme 94 Cellular Location Not Available
Enzyme 94 Gene Sequence >555 bp
ATGCGTGAGTACAAGCTAGTGGTCCTTGGTTCAGGAGGCGTTGGGAAGTCTGCTCTGACA
GTTCAGTTTGTTCAGGGAATTTTTGTTGAAAAATATGACCCAACGATAGAAGATTCCTAC
AGAAAGCAAGTTGAAGTCGATTGCCAACAGTGTATGCTCGAAATCCTGGATACTGCAGGG
ACAGAGCAATTTACAGCAATGAGGGATTTGTATATGAAGAACGGCCAAGGTTTTGCACTA
GTATATTCTATTACAGCTCAGTCCACGTTTAACGACTTACAGGACCTGAGGGAACAGATT
TTACGGGTTAAGGACACGGAAGATGTTCCAATGATTTTGGTTGGCAATAAATGTGACCTG
GAAGATGAGCGAGTAGTTGGCAAAGAGCAGGGCCAGAATTTAGCAAGACAGTGGTGTAAC
TGTGCCTTTTTAGAATCTTCTGCAAAGTCAAAGATCAATGTTAATGAGATATTTTATGAC
CTGGTCAGACAGATAAATAGGAAAACACCAGTGGAAAAGAAGAAGCCTAAAAAGAAATCA
TGTCTGCTGCTCTAG
Enzyme 94 GenBank Gene ID AF493912 Link Image
Enzyme 94 GeneCard ID RAP1A Link Image
Enzyme 94 GenAtlas ID RAP1A Link Image
Enzyme 94 HGNC ID HGNC:9855 Link Image
Enzyme 94 Chromosome Location 1
Enzyme 94 Locus 1p13.3
Enzyme 94 SNPs SNPJam Report Link Image
Enzyme 94 General References
  1. Pizon V, Chardin P, Lerosey I, Olofsson B, Tavitian A: Human cDNAs rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related to ras in the 'effector' region. Oncogene. 1988 Aug;3(2):201-4. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Nagata K, Itoh H, Katada T, Takenaka K, Ui M, Kaziro Y, Nozawa Y: Purification, identification, and characterization of two GTP-binding proteins with molecular weights of 25,000 and 21,000 in human platelet cytosol. One is the rap1/smg21/Krev-1 protein and the other is a novel GTP-binding protein. J Biol Chem. 1989 Oct 15;264(29):17000-5. [PubMed Link Image]
  5. Bokoch GM, Parkos CA, Mumby SM: Purification and characterization of the 22,000-dalton GTP-binding protein substrate for ADP-ribosylation by botulinum toxin, G22K. J Biol Chem. 1988 Nov 15;263(32):16744-9. [PubMed Link Image]
  6. Ohmori T, Kikuchi A, Yamamoto K, Kawata M, Kondo J, Takai Y: Identification of a platelet Mr 22,000 GTP-binding protein as the novel smg-21 gene product having the same putative effector domain as the ras gene products. Biochem Biophys Res Commun. 1988 Dec 15;157(2):670-6. [PubMed Link Image]
  7. Buss JE, Quilliam LA, Kato K, Casey PJ, Solski PA, Wong G, Clark R, McCormick F, Bokoch GM, Der CJ: The COOH-terminal domain of the Rap1A (Krev-1) protein is isoprenylated and supports transformation by an H-Ras:Rap1A chimeric protein. Mol Cell Biol. 1991 Mar;11(3):1523-30. [PubMed Link Image]
  8. 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]
  9. Song C, Satoh T, Edamatsu H, Wu D, Tadano M, Gao X, Kataoka T: Differential roles of Ras and Rap1 in growth factor-dependent activation of phospholipase C epsilon. Oncogene. 2002 Nov 21;21(53):8105-13. [PubMed Link Image]
  10. Smolen GA, Schott BJ, Stewart RA, Diederichs S, Muir B, Provencher HL, Look AT, Sgroi DC, Peterson RT, Haber DA: A Rap GTPase interactor, RADIL, mediates migration of neural crest precursors. Genes Dev. 2007 Sep 1;21(17):2131-6. Epub 2007 Aug 17. [PubMed Link Image]
  11. Yang H, Sasaki T, Minoshima S, Shimizu N: Identification of three novel proteins (SGSM1, 2, 3) which modulate small G protein (RAP and RAB)-mediated signaling pathway. Genomics. 2007 Aug;90(2):249-60. Epub 2007 May 23. [PubMed Link Image]
  12. Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A: The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature. 1995 Jun 15;375(6532):554-60. [PubMed Link Image]
  13. Nassar N, Horn G, Herrmann C, Block C, Janknecht R, Wittinghofer A: Ras/Rap effector specificity determined by charge reversal. Nat Struct Biol. 1996 Aug;3(8):723-9. [PubMed Link Image]
Enzyme 94 Metabolite References Not Available
Enzyme 95 [top]
Enzyme 95 ID 7391
Enzyme 95 Name Rho-related GTP-binding protein RhoQ
Enzyme 95 Synonyms
  1. Ras-like protein TC10
  2. Ras-like protein family member 7A
Enzyme 95 Gene Name RHOQ
Enzyme 95 Protein Sequence >Rho-related GTP-binding protein RhoQ
MAHGPGALMLKCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVSVTVGGKQYLLG
LYDTAGQEDYDRLRPLSYPMTDVFLICFSVVNPASFQNVKEEWVPELKEYAPNVPFLLIG
TQIDLRDDPKTLARLNDMKEKPICVEQGQKLAKEIGACCYVECSALTQKGLKTVFDEAII
AILTPKKHTVKKRIGSRCINCCLIT
Enzyme 95 Number of Residues 205
Enzyme 95 Molecular Weight 22659.3
Enzyme 95 Theoretical pI 6.25
Enzyme 95 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 95 General Function Involved in GTP binding
Enzyme 95 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 95 Pathways Not Available
Enzyme 95 Reactions Not Available
Enzyme 95 Pfam Domain Function
Enzyme 95 Signals
  • None
Enzyme 95 Transmembrane Regions
  • None
Enzyme 95 Essentiality Not Available
Enzyme 95 GenBank ID Protein 62822285 Link Image
Enzyme 95 UniProtKB/Swiss-Prot ID P17081 Link Image
Enzyme 95 UniProtKB/Swiss-Prot Entry Name RHOQ_HUMAN Link Image
Enzyme 95 PDB ID Not Available
Enzyme 95 Cellular Location Not Available
Enzyme 95 Gene Sequence >618 bp
ATGGCTCACGGGCCCGGCGCGCTGATGCTCAAGTGCGTGGTGGTCGGCGACGGGGCGGTG
GGCAAGACGTGCCTACTCATGAGCTATGCCAACGACGCCTTCCCGGAGGAGTACGTGCCC
ACCGTCTTCGACCACTACGCAGTCAGCGTCACCGTGGGGGGCAAGCAGTACCTCCTAGGA
CTCTATGACACGGCCGGACAGGAAGACTATGACCGTCTGAGGCCTTTATCTTACCCAATG
ACCGATGTCTTCCTTATATGCTTCTCGGTGGTAAATCCAGCCTCATTTCAAAATGTGAAA
GAGGAGTGGGTACCGGAACTTAAGGAATACGCACCAAATGTACCCTTTTTATTAATAGGA
ACTCAGATTGATCTCCGAGATGACCCCAAAACTTTAGCAAGACTGAATGATATGAAAGAA
AAACCTATATGTGTGGAACAAGGACAGAAACTAGCAAAAGAGATAGGAGCATGCTGCTAT
GTGGAATGTTCAGCTTTAACCCAGAAGGGATTGAAGACTGTTTTTGATGAGGCTATCATA
GCCATTTTAACTCCAAAGAAACACACTGTAAAAAAAAGAATAGGATCAAGATGTATAAAC
TGTTGTTTAATTACGTGA
Enzyme 95 GenBank Gene ID AC018682 Link Image
Enzyme 95 GeneCard ID RHOQ Link Image
Enzyme 95 GenAtlas ID RHOQ Link Image
Enzyme 95 HGNC ID HGNC:17736 Link Image
Enzyme 95 Chromosome Location 2
Enzyme 95 Locus 2p21
Enzyme 95 SNPs SNPJam Report Link Image
Enzyme 95 General References
  1. Drivas GT, Shih A, Coutavas E, Rush MG, D'Eustachio P: Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line. Mol Cell Biol. 1990 Apr;10(4):1793-8. [PubMed Link Image]
  2. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Joberty G, Perlungher RR, Macara IG: The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins. Mol Cell Biol. 1999 Oct;19(10):6585-97. [PubMed Link Image]
  5. Joberty G, Petersen C, Gao L, Macara IG: The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42. Nat Cell Biol. 2000 Aug;2(8):531-9. [PubMed Link Image]
  6. Neudauer CL, Joberty G, Macara IG: PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10. Biochem Biophys Res Commun. 2001 Jan 19;280(2):541-7. [PubMed Link Image]
  7. Cheng J, Wang H, Guggino WB: Regulation of cystic fibrosis transmembrane regulator trafficking and protein expression by a Rho family small GTPase TC10. J Biol Chem. 2005 Feb 4;280(5):3731-9. Epub 2004 Nov 15. [PubMed Link Image]
Enzyme 95 Metabolite References Not Available
Enzyme 96 [top]
Enzyme 96 ID 7394
Enzyme 96 Name Breakpoint cluster region protein
Enzyme 96 Synonyms
  1. Renal carcinoma antigen NY-REN-26
Enzyme 96 Gene Name BCR
Enzyme 96 Protein Sequence >Breakpoint cluster region protein
MVDPVGFAEAWKAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQ
TLLAKEKKSYDRQRWGFRRAAQAPDGASEPRASASRPQPAPADGADPPPAEEPEARPDGE
GSPGKARPGTARRPGAAASGERDDRGPPASVAALRSNFERIRKGHGQPGADAEKPFYVNV
EFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQHGAGSSVGDASRPPYRGRSSESSC
GVDGDYEDAELNPRFLKDNLIDANGGSRPPWPPLEYQPYQSIYVGGMMEGEGKGPLLRSQ
STSEQEKRLTWPRRSYSPRSFEDCGGGYTPDCSSNENLTSSEEDFSSGQSSRVSPSPTTY
RMFRDKSRSPSQNSQQSFDSSSPPTPQCHKRHRHCPVVVSEATIVGVRKTGQIWPNDGEG
AFHGDADGSFGTPPGYGCAADRAEEQRRHQDGLPYIDDSPSSSPHLSSKGRGSRDALVSG
ALESTKASELDLEKGLEMRKWVLSGILASEETYLSHLEALLLPMKPLKAAATTSQPVLTS
QQIETIFFKVPELYEIHKEFYDGLFPRVQQWSHQQRVGDLFQKLASQLGVYRAFVDNYGV
AMEMAEKCCQANAQFAEISENLRARSNKDAKDPTTKNSLETLLYKPVDRVTRSTLVLHDL
LKHTPASHPDHPLLQDALRISQNFLSSINEEITPRRQSMTVKKGEHRQLLKDSFMVELVE
GARKLRHVFLFTDLLLCTKLKKQSGGKTQQYDCKWYIPLTDLSFQMVDELEAVPNIPLVP
DEELDALKIKISQIKNDIQREKRANKGSKATERLKKKLSEQESLLLLMSPSMAFRVHSRN
GKSYTFLISSDYERAEWRENIREQQKKCFRSFSLTSVELQMLTNSCVKLQTVHSIPLTIN
KEDDESPGLYGFLNVIVHSATGFKQSSNLYCTLEVDSFGYFVNKAKTRVYRDTAEPNWNE
EFEIELEGSQTLRILCYEKCYNKTKIPKEDGESTDRLMGKGQVQLDPQALQDRDWQRTVI
AMNGIEVKLSVKFNSREFSLKRMPSRKQTGVFGVKIAVVTKRERSKVPYIVRQCVEEIER
RGMEEVGIYRVSGVATDIQALKAAFDVNNKDVSVMMSEMDVNAIAGTLKLYFRELPEPLF
TDEFYPNFAEGIALSDPVAKESCMLNLLLSLPEANLLTFLFLLDHLKRVAEKEAVNKMSL
HNLATVFGPTLLRPSEKESKLPANPSQPITMTDSWSLEVMSQVQVLLYFLQLEAIPAPDS
KRQSILFSTEV
Enzyme 96 Number of Residues 1271
Enzyme 96 Molecular Weight 142818.1
Enzyme 96 Theoretical pI 7.03
Enzyme 96 GO Classification
Function
  • GTPase activator activity
  • GTPase regulator activity
  • Ras guanyl-nucleotide exchange factor activity
  • Rho guanyl-nucleotide exchange factor activity
  • catalytic activity
  • enzyme activator activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • kinase activity
  • nucleoside-triphosphatase regulator activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • small GTPase regulator activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biological regulation
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • regulation of Ras protein signal transduction
  • regulation of Rho protein signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • signaling
  • signaling pathway
Component
  • cell part
  • intracellular
Enzyme 96 General Function Involved in protein serine/threonine kinase activity
Enzyme 96 Specific Function GTPase-activating protein for RAC1 and CDC42. Promotes the exchange of RAC or CDC42-bound GDP by GTP, thereby activating them. Displays serine/threonine kinase activity
Enzyme 96 Pathways Not Available
Enzyme 96 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 96 Pfam Domain Function
Enzyme 96 Signals
  • None
Enzyme 96 Transmembrane Regions
  • None
Enzyme 96 Essentiality Not Available
Enzyme 96 GenBank ID Protein 82546843 Link Image
Enzyme 96 UniProtKB/Swiss-Prot ID P11274 Link Image
Enzyme 96 UniProtKB/Swiss-Prot Entry Name BCR_HUMAN Link Image
Enzyme 96 PDB ID 1K1F Link Image
Enzyme 96 PDB File Show
Enzyme 96 3D Structure
Enzyme 96 Cellular Location Not Available
Enzyme 96 Gene Sequence >3816 bp
ATGGTGGACCCGGTGGGCTTCGCGGAGGCGTGGAAGGCGCAGTTCCCGGACTCAGAGCCC
CCGCGCATGGAGCTGCGCTCAGTGGGCGACATCGAGCAGGAGCTGGAGCGCTGCAAGGCC
TCCATTCGGCGCCTGGAGCAGGAGGTGAACCAGGAGCGCTTCCGCATGATCTACCTGCAG
ACGTTGCTGGCCAAGGAAAAGAAGAGCTATGACCGGCAGCGATGGGGCTTCCGGCGCGCG
GCGCAGGCCCCCGACGGCGCCTCCGAGCCCCGAGCGTCCGCGTCGCGCCCGCAGCCAGCG
CCCGCCGACGGAGCCGACCCGCCGCCCGCCGAGGAGCCCGAGGCCCGGCCCGACGGCGAG
GGTTCTCCGGGTAAGGCCAGGCCCGGGACCGCCCGCAGGCCCGGGGCAGCCGCGTCGGGG
GAACGGGACGACCGGGGACCCCCCGCCAGCGTGGCGGCGCTCAGGTCCAACTTCGAGCGG
ATCCGCAAGGGCCATGGCCAGCCCGGGGCGGACGCCGAGAAGCCCTTCTACGTGAACGTC
GAGTTTCACCACGAGCGCGGCCTGGTGAAGGTCAACGACAAAGAGGTGTCGGACCGCATC
AGCTCCCTGGGCAGCCAGGCCATGCAGATGGAGCGCAAAAAGTCCCAGCACGGCGCGGGC
TCGAGCGTGGGGGATGCATCCAGGCCCCCTTACCGGGGACGCTCCTCGGAGAGCAGCTGC
GGCGTCGACGGCGACTACGAGGACGCCGAGTTGAACCCCCGCTTCCTGAAGGACAACCTG
ATCGACGCCAATGGCGGTAGCAGGCCCCCTTGGCCGCCCCTGGAGTACCAGCCCTACCAG
AGCATCTACGTCGGGGGCATGATGGAAGGGGAGGGCAAGGGCCCGCTCCTGCGCAGCCAG
AGCACCTCTGAGCAGGAGAAGCGCCTTACCTGGCCCCGCAGGTCCTACTCCCCCCGGAGT
TTTGAGGATTGCGGAGGCGGCTATACCCCGGACTGCAGCTCCAATGAGAACCTCACCTCC
AGCGAGGAGGACTTCTCCTCTGGCCAGTCCAGCCGCGTGTCCCCAAGCCCCACCACCTAC
CGCATGTTCCGGGACAAAAGCCGCTCTCCCTCGCAGAACTCGCAACAGTCCTTCGACAGC
AGCAGTCCCCCCACGCCGCAGTGCCATAAGCGGCACCGGCACTGCCCGGTTGTCGTGTCC
GAGGCCACCATCGTGGGCGTCCGCAAGACCGGGCAGATCTGGCCCAACGATGGCGAGGGC
GCCTTCCATGGAGACGCAGATGGCTCGTTCGGAACACCACCTGGATACGGCTGCGCTGCA
GACCGGGCAGAGGAGCAGCGCCGGCACCAAGATGGGCTGCCCTACATTGATGACTCGCCC
TCCTCATCGCCCCACCTCAGCAGCAAGGGCAGGGGCAGCCGGGATGCGCTGGTCTCGGGA
GCCCTGGAGTCCACTAAAGCGAGTGAGCTGGACTTGGAAAAGGGCTTGGAGATGAGAAAA
TGGGTCCTGTCGGGAATCCTGGCTAGCGAGGAGACTTACCTGAGCCACCTGGAGGCACTG
CTGCTGCCCATGAAGCCTTTGAAAGCCGCTGCCACCACCTCTCAGCCGGTGCTGACGAGT
CAGCAGATCGAGACCATCTTCTTCAAAGTGCCTGAGCTCTACGAGATCCACAAGGAGTTC
TATGATGGGCTCTTCCCCCGCGTGCAGCAGTGGAGCCACCAGCAGCGGGTGGGCGACCTC
TTCCAGAAGCTGGCCAGCCAGCTGGGTGTGTACCGGGCCTTCGTGGACAACTACGGAGTT
GCCATGGAAATGGCTGAGAAGTGCTGTCAGGCCAATGCTCAGTTTGCAGAAATCTCCGAG
AACCTGAGAGCCAGAAGCAACAAAGATGCCAAGGATCCAACGACCAAGAACTCTCTGGAA
ACTCTGCTCTACAAGCCTGTGGACCGTGTGACGAGGAGCACGCTGGTCCTCCATGACTTG
CTGAAGCACACTCCTGCCAGCCACCCTGACCACCCCTTGCTGCAGGACGCCCTCCGCATC
TCACAGAACTTCCTGTCCAGCATCAATGAGGAGATCACACCCCGACGGCAGTCCATGACG
GTGAAGAAGGGAGAGCACCGGCAGCTGCTGAAGGACAGCTTCATGGTGGAGCTGGTGGAG
GGGGCCCGCAAGCTGCGCCACGTCTTCCTGTTCACCGACCTGCTTCTCTGCACCAAGCTC
AAGAAGCAGAGCGGAGGCAAAACGCAGCAGTATGACTGCAAATGGTACATTCCGCTCACG
GATCTCAGCTTCCAGATGGTGGATGAACTGGAGGCAGTGCCCAACATCCCCCTGGTGCCC
GATGAGGAGCTGGACGCTTTGAAGATCAAGATCTCCCAGATCAAGAATGACATCCAGAGA
GAGAAGAGGGCGAACAAGGGCAGCAAGGCTACGGAGAGGCTGAAGAAGAAGCTGTCGGAG
CAGGAGTCACTGCTGCTGCTTATGTCTCCCAGCATGGCCTTCAGGGTGCACAGCCGCAAC
GGCAAGAGTTACACGTTCCTGATCTCCTCTGACTATGAGCGTGCAGAGTGGAGGGAGAAC
ATCCGGGAGCAGCAGAAGAAGTGTTTCAGAAGCTTCTCCCTGACATCCGTGGAGCTGCAG
ATGCTGACCAACTCGTGTGTGAAACTCCAGACTGTCCACAGCATTCCGCTGACCATCAAT
AAGGAAGATGATGAGTCTCCGGGGCTCTATGGGTTTCTGAATGTCATCGTCCACTCAGCC
ACTGGATTTAAGCAGAGTTCAAATCTGTACTGCACCCTGGAGGTGGATTCCTTTGGGTAT
TTTGTGAATAAAGCAAAGACGCGCGTCTACAGGGACACAGCTGAGCCAAACTGGAACGAG
GAATTTGAGATAGAGCTGGAGGGCTCCCAGACCCTGAGGATACTGTGCTATGAAAAGTGT
TACAACAAGACGAAGATCCCCAAGGAGGACGGCGAGAGCACGGACAGACTCATGGGGAAG
GGCCAGGTCCAGCTGGACCCGCAGGCCCTGCAGGACAGAGACTGGCAGCGCACCGTCATC
GCCATGAATGGGATCGAAGTAAAGCTCTCGGTCAAGTTCAACAGCAGGGAGTTCAGCTTG
AAGAGGATGCCGTCCCGAAAACAGACAGGGGTCTTCGGAGTCAAGATTGCTGTGGTCACC
AAGAGAGAGAGGTCCAAGGTGCCCTACATCGTGCGCCAGTGCGTGGAGGAGATCGAGCGC
CGAGGCATGGAGGAGGTGGGCATCTACCGCGTGTCCGGTGTGGCCACGGACATCCAGGCA
CTGAAGGCAGCCTTCGACGTCAATAACAAGGACGTGTCGGTGATGATGAGCGAGATGGAC
GTGAACGCCATCGCAGGCACGCTGAAGCTGTACTTCCGTGAGCTGCCCGAGCCCCTCTTC
ACTGACGAGTTCTACCCCAACTTCGCAGAGGGCATCGCTCTTTCAGACCCGGTTGCAAAG
GAGAGCTGCATGCTCAACCTGCTGCTGTCCCTGCCGGAGGCCAACCTGCTCACCTTCCTT
TTCCTTCTGGACCACCTGAAAAGGGTGGCAGAGAAGGAGGCAGTCAATAAGATGTCCCTG
CACAACCTCGCCACGGTCTTTGGCCCCACGCTGCTCCGGCCCTCCGAGAAGGAGAGCAAG
CTCCCTGCCAACCCCAGCCAGCCTATCACCATGACTGACAGCTGGTCCTTGGAGGTCATG
TCCCAGGTCCAGGTGCTGCTGTACTTCCTGCAGCTGGAGGCCATCCCTGCCCCGGACAGC
AAGAGACAGAGCATCCTGTTCTCCACCGAAGTCTAA
Enzyme 96 GenBank Gene ID NM_004327.3 Link Image
Enzyme 96 GeneCard ID BCR Link Image
Enzyme 96 GenAtlas ID BCR Link Image
Enzyme 96 HGNC ID HGNC:1014 Link Image
Enzyme 96 Chromosome Location 2
Enzyme 96 Locus 22q11|22q11.23
Enzyme 96 SNPs SNPJam Report Link Image
Enzyme 96 General References
  1. Lifshitz B, Fainstein E, Marcelle C, Shtivelman E, Amson R, Gale RP, Canaani E: bcr genes and transcripts. Oncogene. 1988 Feb;2(2):113-7. [PubMed Link Image]
  2. Chissoe SL, Bodenteich A, Wang YF, Wang YP, Burian D, Clifton SW, Crabtree J, Freeman A, Iyer K, Jian L, et al.: Sequence and analysis of the human ABL gene, the BCR gene, and regions involved in the Philadelphia chromosomal translocation. Genomics. 1995 May 1;27(1):67-82. [PubMed Link Image]
  3. Hariharan IK, Adams JM: cDNA sequence for human bcr, the gene that translocates to the abl oncogene in chronic myeloid leukaemia. EMBO J. 1987 Jan;6(1):115-9. [PubMed Link Image]
  4. Mes-Masson AM, McLaughlin J, Daley GQ, Paskind M, Witte ON: Overlapping cDNA clones define the complete coding region for the P210c-abl gene product associated with chronic myelogenous leukemia cells containing the Philadelphia chromosome. Proc Natl Acad Sci U S A. 1986 Dec;83(24):9768-72. [PubMed Link Image]
  5. Heisterkamp N, Stam K, Groffen J, de Klein A, Grosveld G: Structural organization of the bcr gene and its role in the Ph' translocation. Nature. 1985 Jun 27-Jul 3;315(6022):758-61. [PubMed Link Image]
  6. Zhu QS, Heisterkamp N, Groffen J: Unique organization of the human BCR gene promoter. Nucleic Acids Res. 1990 Dec 11;18(23):7119-25. [PubMed Link Image]
  7. Fainstein E, Marcelle C, Rosner A, Canaani E, Gale RP, Dreazen O, Smith SD, Croce CM: A new fused transcript in Philadelphia chromosome positive acute lymphocytic leukaemia. Nature. 1987 Nov 26-Dec 2;330(6146):386-8. [PubMed Link Image]
  8. Romero P, Beran M, Shtalrid M, Andersson B, Talpaz M, Blick M: Alternative 5' end of the bcr-abl transcript in chronic myelogenous leukemia. Oncogene. 1989 Jan;4(1):93-8. [PubMed Link Image]
  9. Selleri L, von Lindern M, Hermans A, Meijer D, Torelli G, Grosveld G: Chronic myeloid leukemia may be associated with several bcr-abl transcripts including the acute lymphoid leukemia-type 7 kb transcript. Blood. 1990 Mar 1;75(5):1146-53. [PubMed Link Image]
  10. Shah NP, Witte ON, Denny CT: Characterization of the BCR promoter in Philadelphia chromosome-positive and -negative cell lines. Mol Cell Biol. 1991 Apr;11(4):1854-60. [PubMed Link Image]
  11. Diekmann D, Brill S, Garrett MD, Totty N, Hsuan J, Monfries C, Hall C, Lim L, Hall A: Bcr encodes a GTPase-activating protein for p21rac. Nature. 1991 May 30;351(6325):400-2. [PubMed Link Image]
  12. Pendergast AM, Muller AJ, Havlik MH, Maru Y, Witte ON: BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner. Cell. 1991 Jul 12;66(1):161-71. [PubMed Link Image]
  13. Maru Y, Witte ON: The BCR gene encodes a novel serine/threonine kinase activity within a single exon. Cell. 1991 Nov 1;67(3):459-68. [PubMed Link Image]
  14. Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed Link Image]
  15. Salomon AR, Ficarro SB, Brill LM, Brinker A, Phung QT, Ericson C, Sauer K, Brock A, Horn DM, Schultz PG, Peters EC: Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry. Proc Natl Acad Sci U S A. 2003 Jan 21;100(2):443-8. Epub 2003 Jan 9. [PubMed Link Image]
  16. Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC: Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. Anal Chem. 2004 May 15;76(10):2763-72. [PubMed Link Image]
  17. Malmberg EK, Andersson CX, Gentzsch M, Chen JH, Mengos A, Cui L, Hansson GC, Riordan JR: Bcr (breakpoint cluster region) protein binds to PDZ-domains of scaffold protein PDZK1 and vesicle coat protein Mint3. J Cell Sci. 2004 Nov 1;117(Pt 23):5535-41. Epub 2004 Oct 19. [PubMed Link Image]
  18. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  19. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  20. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  21. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  22. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  23. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  24. Zhao X, Ghaffari S, Lodish H, Malashkevich VN, Kim PS: Structure of the Bcr-Abl oncoprotein oligomerization domain. Nat Struct Biol. 2002 Feb;9(2):117-20. [PubMed Link Image]
  25. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 96 Metabolite References Not Available
Enzyme 97 [top]
Enzyme 97 ID 7474
Enzyme 97 Name Molybdenum cofactor biosynthesis protein 1 A
Enzyme 97 Synonyms
  1. MOCS1A
Enzyme 97 Gene Name MOCS1
Enzyme 97 Protein Sequence >Molybdenum cofactor biosynthesis protein 1 A
MAARPLSRMLRRLLRSSARSCSSGAPVTQPCPGESARAASEEVSRRRQFLREHAAPFSAF
LTDSFGRQHSYLRISLTEKCNLRCQYCMPEEGVPLTPKANLLTTEEILTLARLFVKEGID
KIRLTGGEPLIRPDVVDIVAQLQRLEGLRTIGVTTNGINLARLLPQLQKAGLSAINISLD
TLVPAKFEFIVRRKGFHKVMEGIHKAIELGYNPVKVNCVVMRGLNEDELLDFAALTEGLP
LDVRFIEYMPFDGNKWNFKKMVSYKEMLDTVRQQWPELEKVPEEESSTAKAFKIPGFQGQ
ISFITSMSEHFCGTCNRLRITADGNLKVCLFGNSEVSLRDHLRAGASEQELLRIIGAAVG
RKKRQHAGMFSISQMKNRPMILIGG
Enzyme 97 Number of Residues 385
Enzyme 97 Molecular Weight 43089
Enzyme 97 Theoretical pI 9.78
Enzyme 97 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • transition metal ion binding
Process
  • Mo-molybdopterin cofactor biosynthesis
  • cellular metabolism
  • coenzyme biosynthesis
  • coenzyme metabolism
  • cofactor metabolism
  • metabolism
  • physiological process
Component
  • molybdopterin synthase complex
  • protein complex
  • unlocalized protein complex
Enzyme 97 General Function Coenzyme transport and metabolism
Enzyme 97 Specific Function Involved in the biosynthesis of molybdopterin precursor Z from guanosine
Enzyme 97 Pathways Not Available
Enzyme 97 Reactions Not Available
Enzyme 97 Pfam Domain Function
Enzyme 97 Signals
  • None
Enzyme 97 Transmembrane Regions
  • None
Enzyme 97 Essentiality Not Available
Enzyme 97 GenBank ID Protein 2645879 Link Image
Enzyme 97 UniProtKB/Swiss-Prot ID O14940 Link Image
Enzyme 97 UniProtKB/Swiss-Prot Entry Name MOS1A_HUMAN Link Image
Enzyme 97 PDB ID Not Available
Enzyme 97 Cellular Location Not Available
Enzyme 97 Gene Sequence >1158 bp
ATGGCGGCGCGGCCACTGTCCCGGATGCTGCGGCGGCTTCTGAGGTCCAGCGCCCGGAGC
TGCAGCTCAGGGGCTCCGGTGACCCAGCCCTGCCCCGGGGAGTCCGCGCGAGCTGCCTCG
GAGGAGGTGTCCAGGCGGAGGCAGTTCCTGCGGGAGCATGCGGCCCCCTTCTCCGCCTTC
CTCACAGACAGCTTCGGCCGGCAGCACAGCTACCTGCGGATCTCCCTCACAGAGAAGTGC
AACCTCAGATGTCAGTACTGCATGCCCGAGGAGGGGGTCCCGCTGACCCCCAAAGCCAAC
CTGCTGACCACAGAGGAGATCCTGACCCTCGCCCGGCTCTTTGTGAAGGAAGGCATCGAC
AAGATCCGGCTCACAGGTGGAGAGCCGCTTATCCGGCCGGACGTGGTGGACATTGTGGCC
CAGCTCCAGCGGCTGGAAGGGCTGAGAACCATAGGTGTTACCACCAATGGCATCAACCTG
GCCCGGCTACTGCCCCAGCTTCAGAAGGCTGGTCTCAGTGCCATCAACATCAGCCTGGAC
ACCCTGGTGCCTGCCAAGTTTGAGTTCATTGTCCGCAGGAAAGGCTTCCACAAGGTCATG
GAGGGCATCCACAAGGCCATCGAGCTGGGCTACAACCCTGTGAAGGTGAACTGTGTGGTG
ATGCGAGGCCTTAACGAGGATGAACTCCTGGACTTTGCGGCCTTGACTGAGGGCCACCCC
CTGGATGTGCGCTTCATAGAGTATATGCCCTTTGATGGCAACAAGTGGAACTTCAAGAAG
ATGGTCAGCTATAAGGAGATGCTAGACACTGTCCGGCAGCAGTGGCCAGAGCTGGAGAAG
GTGCCAGAGGAGGAATCCAGCACAGCCAAGGCCTTTAAAATCCCTGGCTTCCAAGGCCAG
ATCAGCTTCATCACATCCATGTCTGAGCATTTCTGTGGGACCTGCAACCGCCTGCGAATC
ACAGCTGATGGGAACCTCAAGGTCTGCCTCTTTGGAAACTCTGAGGTATCCCTGCGGGAT
CACCTGCGAGCTGGGGCCTCTGAGCAGGAGCTGCTGAGAATCATTGGGGCTGCTGTGGGC
AGGAAGAAGCGGCAGCATGCAGGCATGTTCAGTATTTCCCAGATGAAGAACCGGCCCATG
ATCCTCATCGGTGGGTGA
Enzyme 97 GenBank Gene ID AF034374 Link Image
Enzyme 97 GeneCard ID MOCS1 Link Image
Enzyme 97 GenAtlas ID MOCS1 Link Image
Enzyme 97 HGNC ID HGNC:7190 Link Image
Enzyme 97 Chromosome Location 6
Enzyme 97 Locus 6p21.3
Enzyme 97 SNPs SNPJam Report Link Image
Enzyme 97 General References
  1. Reiss J, Cohen N, Dorche C, Mandel H, Mendel RR, Stallmeyer B, Zabot MT, Dierks T: Mutations in a polycistronic nuclear gene associated with molybdenum cofactor deficiency. Nat Genet. 1998 Sep;20(1):51-3. [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. Gross-Hardt S, Reiss J: The bicistronic MOCS1 gene has alternative start codons on two mutually exclusive exons. Mol Genet Metab. 2002 Aug;76(4):340-3. [PubMed Link Image]
  4. Hanzelmann P, Schwarz G, Mendel RR: Functionality of alternative splice forms of the first enzymes involved in human molybdenum cofactor biosynthesis. J Biol Chem. 2002 May 24;277(21):18303-12. Epub 2002 Mar 12. [PubMed Link Image]
  5. Reiss J, Christensen E, Kurlemann G, Zabot MT, Dorche C: Genomic structure and mutational spectrum of the bicistronic MOCS1 gene defective in molybdenum cofactor deficiency type A. Hum Genet. 1998 Dec;103(6):639-44. [PubMed Link Image]
Enzyme 97 Metabolite References Not Available
Enzyme 98 [top]
Enzyme 98 ID 7480
Enzyme 98 Name Guanine nucleotide-binding protein G(q) subunit alpha
Enzyme 98 Synonyms
  1. Guanine nucleotide-binding protein alpha-q
Enzyme 98 Gene Name GNAQ
Enzyme 98 Protein Sequence >Guanine nucleotide-binding protein G(q) subunit alpha
MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMR
IIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEK
VSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPAYLPTQQDVL
RVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLV
ESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQR
DAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
Enzyme 98 Number of Residues 359
Enzyme 98 Molecular Weight 42141.7
Enzyme 98 Theoretical pI 5.37
Enzyme 98 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • molecular transducer activity
  • nucleotide binding
  • purine nucleotide binding
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • biological regulation
  • cell surface receptor linked signaling pathway
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • post-translational protein modification
  • protein amino acid ADP-ribosylation
  • protein modification process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 98 General Function Involved in signal transducer activity
Enzyme 98 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems
Enzyme 98 Pathways Not Available
Enzyme 98 Reactions Not Available
Enzyme 98 Pfam Domain Function
Enzyme 98 Signals
  • None
Enzyme 98 Transmembrane Regions
  • None
Enzyme 98 Essentiality Not Available
Enzyme 98 GenBank ID Protein 1181671 Link Image
Enzyme 98 UniProtKB/Swiss-Prot ID P50148 Link Image
Enzyme 98 UniProtKB/Swiss-Prot Entry Name GNAQ_HUMAN Link Image
Enzyme 98 PDB ID Not Available
Enzyme 98 Cellular Location Not Available
Enzyme 98 Gene Sequence >1080 bp
ATGACTCTGGAGTCCATCATGGCGTGCTGCCTGAGCGAGGAGGCCAAGGAAGCCCGGCGG
ATCAACGACGAGATCGAGCGGCACGTCCGCAGGGACAAGCGGGACGCCCGCCGGGAGCTC
AAGCTGCTGCTGCTCGGGACAGGAGAGAGTGGCAAGAGTACGTTTATCAAGCAGATGAGA
ATCATCCATGGGTCAGGATACTCTGATGAAGATAAAAGGGGCTTCACCAAGCTGGTGTAT
CAGAACATCTTCACGGCCATGCAGGCCATGATCAGAGCCATGGACACACTCAAGATCCCA
TACAAGTATGAGCACAATAAGGCTCATGCACAATTAGTTCGAGAAGTTGATGTGGAGAAG
GTGTCTGCTTTTGAGAATCCATATGTAGATGCAATAAAGAGTTTATGGAATGATCCTGGA
ATCCAGGAATGCTATGATAGACGACGAGAATATCAATTATCTGACTCTACCAAATACTAT
CTTAATGACTTGGACCGCGTAGCTGACCCTGCCTACCTGCCTACGCAACAAGATGTGCTT
AGAGTTCGAGTCCCCACCACAGGGATCATCGAATACCCCTTTGACTTACAAAGTGTCATT
TTCAGAATGGTCGATGTAGGGGGCCAAAGGTCAGAGAGAAGAAAATGGATACACTGCTTT
GAAAATGTCACCTCTATCATGTTTCTAGTAGCGCTTAGTGAATATGATCAAGTTCTCGTG
GAGTCAGACAATGAGAACCGAATGGAGGAAAGCAAGGCTCTCTTTAGAACAATTATCACA
TACCCCTGGTTCCAGAACTCCTCGGTTATTCTGTTCTTAAACAAGAAAGATCTTCTAGAG
GAGAAAATCATGTATTCCCATCTAGTCGACTACTTCCCAGAATATGATGGACCCCAGAGA
GATGCCCAGGCAGCCCGAGAATTCATTCTGAAGATGTTCGTGGACCTGAACCCAGACAGT
GACAAAATTATCTACTCCCACTTCACGTGCGCCACAGACACCGAGAATATCCGCTTTGTC
TTTGCTGCCGTCAAGGACACCATCCTCCAGTTGAACCTGAAGGAGTACAATCTGGTCTAA
Enzyme 98 GenBank Gene ID U40038 Link Image
Enzyme 98 GeneCard ID GNAQ Link Image
Enzyme 98 GenAtlas ID GNAQ Link Image
Enzyme 98 HGNC ID HGNC:4390 Link Image
Enzyme 98 Chromosome Location 9
Enzyme 98 Locus 9q21
Enzyme 98 SNPs SNPJam Report Link Image
Enzyme 98 General References
  1. Dong Q, Shenker A, Way J, Haddad BR, Lin K, Hughes MR, McBride OW, Spiegel AM, Battey J: Molecular cloning of human G alpha q cDNA and chromosomal localization of the G alpha q gene (GNAQ) and a processed pseudogene. Genomics. 1995 Dec 10;30(3):470-75. [PubMed Link Image]
  2. Chen B, Leverette RD, Schwinn DA, Kwatra MM: Human G(alpha q): cDNA and tissue distribution. Biochim Biophys Acta. 1996 Jun 11;1281(2):125-8. [PubMed Link Image]
  3. Johnson GJ, Leis LA, Dunlop PC: Specificity of G alpha q and G alpha 11 gene expression in platelets and erythrocytes. Expressions of cellular differentiation and species differences. Biochem J. 1996 Sep 15;318 ( Pt 3):1023-31. [PubMed Link Image]
  4. Gabbeta J, Dhanasekaran N, Rao AK: G alpha q cDNA sequence from human platelets. Thromb Res. 1998 Jul 1;91(1):29-32. [PubMed Link Image]
  5. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Lesch KP, Manji HK: Signal-transducing G proteins and antidepressant drugs: evidence for modulation of alpha subunit gene expression in rat brain. Biol Psychiatry. 1992 Oct 1;32(7):549-79. [PubMed Link Image]
  8. Thomas CP, Dunn MJ, Mattera R: Ca2+ signalling in K562 human erythroleukaemia cells: effect of dimethyl sulphoxide and role of G-proteins in thrombin- and thromboxane A2-activated pathways. Biochem J. 1995 Nov 15;312 ( Pt 1):151-8. [PubMed Link Image]
  9. Rochdi MD, Watier V, La Madeleine C, Nakata H, Kozasa T, Parent JL: Regulation of GTP-binding protein alpha q (Galpha q) signaling by the ezrin-radixin-moesin-binding phosphoprotein-50 (EBP50). J Biol Chem. 2002 Oct 25;277(43):40751-9. Epub 2002 Aug 21. [PubMed Link Image]
  10. Yeh JC, Otte LA, Frangos JA: Regulation of G protein-coupled receptor activities by the platelet-endothelial cell adhesion molecule, PECAM-1. Biochemistry. 2008 Aug 26;47(34):9029-39. Epub 2008 Aug 2. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 98 Metabolite References Not Available
Enzyme 99 [top]
Enzyme 99 ID 7482
Enzyme 99 Name Guanine nucleotide-binding protein subunit alpha-11
Enzyme 99 Synonyms
  1. G alpha-11
  2. G-protein subunit alpha-11
  3. Guanine nucleotide-binding protein G(y) subunit alpha
Enzyme 99 Gene Name GNA11
Enzyme 99 Protein Sequence >Guanine nucleotide-binding protein subunit alpha-11
MTLESMMACCLSDEVKESKRINAEIEKQLRRDKRDARRELKLLLLGTGESGKSTFIKQMR
IIHGAGYSEEDKRGFTKLVYQNIFTAMQAMIRAMETLKILYKYEQNKANALLIREVDVEK
VTTFEHQYVSAIKTLWEDPGIQECYDRRREYQLSDSAKYYLTDVDRIATLGYLPTQQDVL
RVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLV
ESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEDKILYSHLVDYFPEFDGPQR
DAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
Enzyme 99 Number of Residues 359
Enzyme 99 Molecular Weight 42122.9
Enzyme 99 Theoretical pI 5.38
Enzyme 99 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • molecular transducer activity
  • nucleotide binding
  • purine nucleotide binding
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • biological regulation
  • cell surface receptor linked signaling pathway
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • post-translational protein modification
  • protein amino acid ADP-ribosylation
  • protein modification process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 99 General Function Involved in signal transducer activity
Enzyme 99 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C
Enzyme 99 Pathways Not Available
Enzyme 99 Reactions Not Available
Enzyme 99 Pfam Domain Function
Enzyme 99 Signals
  • None
Enzyme 99 Transmembrane Regions
  • None
Enzyme 99 Essentiality Not Available
Enzyme 99 GenBank ID Protein 3289982 Link Image
Enzyme 99 UniProtKB/Swiss-Prot ID P29992 Link Image
Enzyme 99 UniProtKB/Swiss-Prot Entry Name GNA11_HUMAN Link Image
Enzyme 99 PDB ID Not Available
Enzyme 99 Cellular Location Not Available
Enzyme 99 Gene Sequence >1080 bp
ATGACTCTGGAGTCCATGATGGCGTGTTGCCTGAGCGATGAGGTGAAGGAGTCCAAGCGG
ATCAACGCCGAGATCGAGAAGCAGCTGCGGCGGGACAAGCGCGACGCCCGGCGCGAGCTC
AAGCTGCTGCTGCTCGGCACGGGCGAGAGCGGGAAGAGCACGTTCATCAAGCAGATGCGC
ATCATCCACGGCGCCGGCTACTCGGAGGAGGACAAGCGCGGCTTCACCAAGCTCGTCTAC
CAGAACATCTTCACCGCCATGCAGGCCATGATCCGGGCCATGGAGACGCTCAAGATCCTC
TACAAGTACGAGCAGAACAAGGCCAATGCGCTCCTGATCCGGGAGGTGGACGTGGAGAAG
GTGACCACCTTCGAGCATCAGTACGTCAGTGCCATCAAGACCCTGTGGGAGGACCCGGGC
ATCCAGGAATGCTACGACCGCAGGCGCGAGTACCAGCTCTCCGACTCTGCCAAGTACTAC
CTGACCGACGTTGACCGCATCGCCACCTTGGGCTACCTGCCCACCCAGCAGGACGTGCTG
CGGGTCCGCGTGCCCACCACCGGCATCATCGAGTACCCTTTCGACCTGGAGAACATCATC
TTCCGGATGGTGGATGTGGGGGGCCAGCGGTCGGAGCGGAGGAAGTGGATCCACTGCTTT
GAGAACGTGACATCCATCATGTTTCTCGTCGCCCTCAGCGAATACGACCAAGTCCTGGTG
GAGTCGGACAACGAGAACCGGATGGAGGAGAGCAAAGCCCTGTTCCGGACCATCATCACC
TACCCCTGGTTCCAGAACTCCTCCGTCATCCTCTTCCTCAACAAGAAGGACCTGCTGGAG
GACAAGATCCTGTACTCGCACCTGGTGGACTACTTCCCCGAGTTCGATGGTCCCCAGCGG
GACGCCCAGGCGGCGCGGGAGTTCATCCTGAAGATGTTCGTGGACCTGAACCCCGACAGC
GACAAGATCATCTACTCACACTTCACGTGTGCCACCGACACGGAGAACATCCGCTTCGTG
TTCGCGGCCGTGAAGGACACCATCCTGCAGCTCAACCTCAAGGAGTACAACCTGGTCTGA
Enzyme 99 GenBank Gene ID AC005262 Link Image
Enzyme 99 GeneCard ID GNA11 Link Image
Enzyme 99 GenAtlas ID GNA11 Link Image
Enzyme 99 HGNC ID HGNC:4379 Link Image
Enzyme 99 Chromosome Location 1
Enzyme 99 Locus 19p13.3
Enzyme 99 SNPs SNPJam Report Link Image
Enzyme 99 General References
  1. Jiang M, Pandey S, Tran VT, Fong HK: Guanine nucleotide-binding regulatory proteins in retinal pigment epithelial cells. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3907-11. [PubMed Link Image]
  2. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Thomas CP, Dunn MJ, Mattera R: Ca2+ signalling in K562 human erythroleukaemia cells: effect of dimethyl sulphoxide and role of G-proteins in thrombin- and thromboxane A2-activated pathways. Biochem J. 1995 Nov 15;312 ( Pt 1):151-8. [PubMed Link Image]
Enzyme 99 Metabolite References Not Available
Enzyme 100 [top]
Enzyme 100 ID 7684
Enzyme 100 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-11
Enzyme 100 Synonyms Not Available
Enzyme 100 Gene Name GNG11
Enzyme 100 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-11
MPALHIEDLPEKEKLKMEVEQLRKEVKLQRQQVSKCSEEIKNYIEERSGEDPLVKGIPED
KNPFKEKGSCVIS
Enzyme 100 Number of Residues 73
Enzyme 100 Molecular Weight 8480.7
Enzyme 100 Theoretical pI 5.23
Enzyme 100 GO Classification
Function
  • molecular transducer activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • extrinsic to membrane
  • extrinsic to plasma membrane
  • heterotrimeric G-protein complex
  • membrane part
Enzyme 100 General Function Involved in signal transducer activity
Enzyme 100 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Enzyme 100 Pathways Not Available
Enzyme 100 Reactions Not Available
Enzyme 100 Pfam Domain Function
Enzyme 100 Signals
  • None
Enzyme 100 Transmembrane Regions
  • None
Enzyme 100 Essentiality Not Available
Enzyme 100 GenBank ID Protein 41393495 Link Image
Enzyme 100 UniProtKB/Swiss-Prot ID P61952 Link Image
Enzyme 100 UniProtKB/Swiss-Prot Entry Name GBG11_HUMAN Link Image
Enzyme 100 PDB ID Not Available
Enzyme 100 Cellular Location Not Available
Enzyme 100 Gene Sequence >222 bp
ATGCCTGCCCTTCACATCGAAGATTTGCCAGAGAAGGAAAAACTGAAAATGGAAGTTGAG
CAGCTTCGCAAAGAAGTGAAGTTGCAGAGACAACAAGTGTCTAAATGTTCTGAAGAAATA
AAGAACTATATTGAAGAACGTTCTGGAGAGGATCCTCTAGTAAAGGGAATTCCAGAAGAC
AAGAACCCCTTTAAAGAAAAAGGCAGCTGTGTTATTTCATAA
Enzyme 100 GenBank Gene ID AC002076 Link Image
Enzyme 100 GeneCard ID GNG11 Link Image
Enzyme 100 GenAtlas ID GNG11 Link Image
Enzyme 100 HGNC ID HGNC:4403 Link Image
Enzyme 100 Chromosome Location 7
Enzyme 100 Locus 7q21
Enzyme 100 SNPs SNPJam Report Link Image
Enzyme 100 General References
  1. Ray K, Kunsch C, Bonner LM, Robishaw JD: Isolation of cDNA clones encoding eight different human G protein gamma subunits, including three novel forms designated the gamma 4, gamma 10, and gamma 11 subunits. J Biol Chem. 1995 Sep 15;270(37):21765-71. [PubMed Link Image]
  2. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 100 Metabolite References Not Available
Enzyme 101 [top]
Enzyme 101 ID 7703
Enzyme 101 Name Tubulin beta-3 chain
Enzyme 101 Synonyms
  1. Tubulin beta-4 chain
  2. Tubulin beta-III
Enzyme 101 Gene Name TUBB3
Enzyme 101 Protein Sequence >Tubulin beta-3 chain
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPSGNYVGDSDLQLERISVYYNEASSHKYV
PRAILVDLEPGTMDSVRSGAFGHLFRPDNFIFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKVREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKLATPTYGDLNHLVSATMSGVTTSL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTARGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVATVFRGRMSMKEVDEQMLAIQSKNSSYFVEWIPNNVKVAVCDIPPRG
LKMSSTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATAEEEGEMYEDDEEESEAQGPK
Enzyme 101 Number of Residues 450
Enzyme 101 Molecular Weight 50432.4
Enzyme 101 Theoretical pI 4.57
Enzyme 101 GO Classification
Function
  • GTP binding
  • GTPase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
  • structural molecule activity
Process
  • cellular component assembly
  • cellular component organization
  • cellular component organization or biogenesis
  • cellular process
  • cellular protein complex assembly
  • macromolecular complex assembly
  • microtubule-based movement
  • microtubule-based process
  • protein complex assembly
  • protein polymerization
Component
  • macromolecular complex
  • microtubule
  • protein complex
Enzyme 101 General Function Involved in structural molecule activity
Enzyme 101 Specific Function Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain. TUBB3 plays a critical role in proper axon guidance and mantainance
Enzyme 101 Pathways Not Available
Enzyme 101 Reactions Not Available
Enzyme 101 Pfam Domain Function
Enzyme 101 Signals
  • None
Enzyme 101 Transmembrane Regions
  • None
Enzyme 101 Essentiality Not Available
Enzyme 101 GenBank ID Protein 16755780 Link Image
Enzyme 101 UniProtKB/Swiss-Prot ID Q13509 Link Image
Enzyme 101 UniProtKB/Swiss-Prot Entry Name TBB3_HUMAN Link Image
Enzyme 101 PDB ID 1SA1 Link Image
Enzyme 101 PDB File Show
Enzyme 101 3D Structure
Enzyme 101 Cellular Location Not Available
Enzyme 101 Gene Sequence >1353 bp
ATGCGGGAGATCGTGCACATCCAGGCCGGCCAGTGCGGCAACCAGATCGGGGCCAAGTTC
TGGGAAGTCATCAGTGATGAGCATGGCATCGACCCCAGCGGCAACTACGTGGGCGACTCG
GACTTGCAGCTGGAGCGGATCAGCGTCTACTACAACGAGGCCTCTTCTCACAAGTACGTG
CCTCGAGCCATTCTGGTGGACCTGGAACCCGGAACCATGGACAGTGTCCGCTCAGGGGCC
TTTGGACATCTCTTCAGGCCTGACAATTTCATCTTTGGTCAGAGTGGGGCCGGCAACAAC
TGGGCCAAGGGTCACTACACGGAGGGGGCGGAGCTGGTGGATTCGGTCCTGGATGTGGTG
CGGAAGGAGTGTGAAAACTGCGACTGCCTGCAGGGCTTCCAGCTGACCCACTCGCTGGGG
GGCGGCACGGGCTCCGGCATGGGCACGTTGCTCATCAGCAAGGTGCGTGAGGAGTATCCC
GACCGCATCATGAACACCTTCAGCGTCGTGCCCTCACCCAAGGTGTCAGACACGGTGGTG
GAGCCCTACAACGCCACGCTGTCCATCCACCAGCTGGTGGAGAACACGGATGAGACCTAC
TGCATCGACAACGAGGCGCTCTACGACATCTGCTTCCGCACCCTCAAGCTGGCCACGCCC
ACCTACGGGGACCTCAACCACCTGGTATCGGCCACCATGAGCGGAGTCACCACCTCCTTG
CGCTTCCCGGGCCAGCTCAACGCTGACCTGCGCAAGCTGGCCGTCAACATGGTGCCCTTC
CCGCGCCTGCACTTCTTCATGCCCGGCTTCGCCCCCCTCACAGCCCGGGGCAGCCAGCAG
TACCGGGCCCTGACCGTGCCCGAGCTCACCCAGCAGATGTTCGATGCCAAGAACATGATG
GCCGCCTGCGACCCGCGCCACGGCCGCTACCTGACGGTGGCCACCGTGTTCCGGGGCCGC
ATGTCCATGAAGGAGGTGGACGAGCAGATGCTGGCCATCCAGAGCAAGAACAGCAGCTAC
TTCGTGGAGTGGATCCCCAACAACGTGAAGGTGGCCGTGTGTGACATCCCGCCCCGCGGC
CTCAAGATGTCCTCCACCTTCATCGGGAACAGCACGGCCATCCAGGAGCTGTTCAAGCGC
ATCTCCGAGCAGTTCACGGCCATGTTCCGGCGCAAGGCCTTCCTGCACTGGTACACGGGC
GAGGGCATGGACGAGATGGAGTTCACCGAGGCCGAGAGCAACATGAACGACCTGGTGTCC
GAGTACCAGCAGTACCAGGACGCCACGGCCGAGGAAGAGGGCGAGATGTACGAAGACGAC
GAGGAGGAGTCGGAGGCCCAGGGCCCCAAGTGA
Enzyme 101 GenBank Gene ID AF427491 Link Image
Enzyme 101 GeneCard ID TUBB3 Link Image
Enzyme 101 GenAtlas ID TUBB3 Link Image
Enzyme 101 HGNC ID HGNC:20772 Link Image
Enzyme 101 Chromosome Location 1
Enzyme 101 Locus 16q24.3
Enzyme 101 SNPs SNPJam Report Link Image
Enzyme 101 General References
  1. Ranganathan S, Dexter DW, Benetatos CA, Hudes GR: Cloning and sequencing of human betaIII-tubulin cDNA: induction of betaIII isotype in human prostate carcinoma cells by acute exposure to antimicrotubule agents. Biochim Biophys Acta. 1998 Jan 21;1395(2):237-45. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Katsetos CD, Legido A, Perentes E, Mork SJ: Class III beta-tubulin isotype: a key cytoskeletal protein at the crossroads of developmental neurobiology and tumor neuropathology. J Child Neurol. 2003 Dec;18(12):851-66; discussion 867. [PubMed Link Image]
  4. Rogowski K, Juge F, van Dijk J, Wloga D, Strub JM, Levilliers N, Thomas D, Bre MH, Van Dorsselaer A, Gaertig J, Janke C: Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation. Cell. 2009 Jun 12;137(6):1076-87. [PubMed Link Image]
  5. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  6. Tischfield MA, Baris HN, Wu C, Rudolph G, Van Maldergem L, He W, Chan WM, Andrews C, Demer JL, Robertson RL, Mackey DA, Ruddle JB, Bird TD, Gottlob I, Pieh C, Traboulsi EI, Pomeroy SL, Hunter DG, Soul JS, Newlin A, Sabol LJ, Doherty EJ, de Uzcategui CE, de Uzcategui N, Collins ML, Sener EC, Wabbels B, Hellebrand H, Meitinger T, de Berardinis T, Magli A, Schiavi C, Pastore-Trossello M, Koc F, Wong AM, Levin AV, Geraghty MT, Descartes M, Flaherty M, Jamieson RV, Moller HU, Meuthen I, Callen DF, Kerwin J, Lindsay S, Meindl A, Gupta ML Jr, Pellman D, Engle EC: Human TUBB3 mutations perturb microtubule dynamics, kinesin interactions, and axon guidance. Cell. 2010 Jan 8;140(1):74-87. [PubMed Link Image]
Enzyme 101 Metabolite References Not Available
Enzyme 102 [top]
Enzyme 102 ID 7761
Enzyme 102 Name Eukaryotic translation initiation factor 2 subunit 1
Enzyme 102 Synonyms
  1. Eukaryotic translation initiation factor 2 subunit alpha
  2. eIF-2-alpha
  3. eIF-2A
  4. eIF-2alpha
Enzyme 102 Gene Name EIF2S1
Enzyme 102 Protein Sequence >Eukaryotic translation initiation factor 2 subunit 1
MPGLSCRFYQHKFPEVEDVVMVNVRSIAEMGAYVSLLEYNNIEGMILLSELSRRRIRSIN
KLIRIGRNECVVVIRVDKEKGYIDLSKRRVSPEEAIKCEDKFTKSKTVYSILRHVAEVLE
YTKDEQLESLFQRTAWVFDDKYKRPGYGAYDAFKHAVSDPSILDSLDLNEDEREVLINNI
NRRLTPQAVKIRADIEVACYGYEGIDAVKEALRAGLNCSTENMPIKINLIAPPRYVMTTT
TLERTEGLSVLSQAMAVIKEKIEEKRGVFNVQMEPKVVTDTDETELARQMERLERENAEV
DGDDDAEEMEAKAED
Enzyme 102 Number of Residues 315
Enzyme 102 Molecular Weight 36111.8
Enzyme 102 Theoretical pI 4.73
Enzyme 102 GO Classification
Function
  • RNA binding
  • binding
  • nucleic acid binding
  • translation factor activity, nucleic acid binding
  • translation initiation factor activity
Process
  • biosynthetic process
  • cellular macromolecule biosynthetic process
  • macromolecule biosynthetic process
  • metabolic process
  • translation
Component
  • eukaryotic translation initiation factor 2 complex
  • macromolecular complex
  • protein complex
Enzyme 102 General Function Translation, ribosomal structure and biogenesis
Enzyme 102 Specific Function Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B
Enzyme 102 Pathways Not Available
Enzyme 102 Reactions Not Available
Enzyme 102 Pfam Domain Function
Enzyme 102 Signals
  • None
Enzyme 102 Transmembrane Regions
  • None
Enzyme 102 Essentiality Not Available
Enzyme 102 GenBank ID Protein 12803385 Link Image
Enzyme 102 UniProtKB/Swiss-Prot ID P05198 Link Image
Enzyme 102 UniProtKB/Swiss-Prot Entry Name IF2A_HUMAN Link Image
Enzyme 102 PDB ID 1Q8K Link Image
Enzyme 102 PDB File Show
Enzyme 102 3D Structure
Enzyme 102 Cellular Location Not Available
Enzyme 102 Gene Sequence >948 bp
ATGCCGGGTCTAAGTTGTAGATTTTATCAACACAAATTTCCTGAGGTGGAAGATGTAGTG
ATGGTGAATGTCAGATCCATTGCTGAAATGGGGGCTTATGTCAGCTTGCTGGAATACAAC
AACATTGAAGGCATGATTCTTCTTAGTGAATTATCCAGAAGGCGTATCCGTTCTATCAAC
AAACTCATCCGAATTGGCAGGAATGAGTGTGTGGTTGTCATTAGGGTGGACAAAGAAAAA
GGATATATTGATTTGTCAAAAAGAAGAGTTTCTCCAGAGGAAGCAATCAAATGTGAAGAC
AAATTCACAAAATCCAAAACTGTTTATAGCATTCTTCGTCATGTTGCTGAGGTGTTAGAA
TACACCAAGGATGAGCAGCTGGAAAGCCTATTCCAGAGGACTGCCTGGGTCTTTGATGAC
AAGTACAAGAGACCTGGATATGGTGCCTATGATGCATTTAAGCATGCAGTCTCAGACCCA
TCTATTTTGGATAGTTTAGATTTGAATGAAGATGAACGGGAAGTACTCATTAATAATATT
AATAGGCGCTTGACCCCACAGGCTGTCAAAATTCGAGCAGATATTGAAGTGGCTTGTTAT
GGTTATGAAGGCATTGATGCTGTAAAAGAAGCCCTAAGAGCAGGTTTGAATTGTTCTACA
GAAAACATGCCCATTAAGATTAATCTAATAGCTCCTCCTCGGTATGTAATGACTACGACA
ACCCTGGAGAGAACAGAAGGCCTTTCTGTCCTCAGTCAAGCTATGGCTGTTATCAAAGAG
AAGATTGAGGAAAAGAGGGGTGTGTTCAATGTTCAAATGGAGCCCAAAGTGGTCACAGAT
ACAGATGAGACTGAACTTGCGAGGCAGATGGAGAGGCTTGAAAGAGAAAATGCCGAAGTG
GATGGAGATGATGATGCAGAAGAAATGGAAGCCAAAGCTGAAGATTAA
Enzyme 102 GenBank Gene ID BC002513 Link Image
Enzyme 102 GeneCard ID EIF2S1 Link Image
Enzyme 102 GenAtlas ID Not Available
Enzyme 102 HGNC ID Not Available
Enzyme 102 Chromosome Location 1
Enzyme 102 Locus 14q23.3
Enzyme 102 SNPs SNPJam Report Link Image
Enzyme 102 General References
  1. Ernst H, Duncan RF, Hershey JW: Cloning and sequencing of complementary DNAs encoding the alpha-subunit of translational initiation factor eIF-2. Characterization of the protein and its messenger RNA. J Biol Chem. 1987 Jan 25;262(3):1206-12. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Langland JO, Jacobs BL: Inhibition of PKR by vaccinia virus: role of the N- and C-terminal domains of E3L. Virology. 2004 Jul 1;324(2):419-29. [PubMed Link Image]
  4. Montero H, Rojas M, Arias CF, Lopez S: Rotavirus infection induces the phosphorylation of eIF2alpha but prevents the formation of stress granules. J Virol. 2008 Feb;82(3):1496-504. Epub 2007 Nov 21. [PubMed Link Image]
  5. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  7. Nonato MC, Widom J, Clardy J: Crystal structure of the N-terminal segment of human eukaryotic translation initiation factor 2alpha. J Biol Chem. 2002 May 10;277(19):17057-61. Epub 2002 Feb 21. [PubMed Link Image]
  8. Ito T, Marintchev A, Wagner G: Solution structure of human initiation factor eIF2alpha reveals homology to the elongation factor eEF1B. Structure. 2004 Sep;12(9):1693-704. [PubMed Link Image]
Enzyme 102 Metabolite References Not Available
Enzyme 103 [top]
Enzyme 103 ID 7832
Enzyme 103 Name RalA-binding protein 1
Enzyme 103 Synonyms
  1. RalBP1
  2. 76 kDa Ral-interacting protein
  3. Dinitrophenyl S-glutathione ATPase
  4. DNP-SG ATPase
  5. Ral-interacting protein 1
Enzyme 103 Gene Name RALBP1
Enzyme 103 Protein Sequence >RalA-binding protein 1
MTECFLPPTSSPSEHRRVEHGSGLTRTPSSEEISPTKFPGLYRTGEPSPPHDILHEPPDV
VSDDEKDHGKKKGKFKKKEKRTEGYAAFQEDSSGDEAESPSKMKRSKGIHVFKKPSFSKK
KEKDFKIKEKPKEEKHKEEKHKEEKHKEKKSKDLTAADVVKQWKEKKKKKKPIQEPEVPQ
IDVPNLKPIFGIPLADAVERTMMYDGIRLPAVFRECIDYVEKYGMKCEGIYRVSGIKSKV
DELKAAYDREESTNLEDYEPNTVASLLKQYLRDLPENLLTKELMPRFEEACGRTTETEKV
QEFQRLLKELPECNYLLISWLIVHMDHVIAKELETKMNIQNISIVLSPTVQISNRVLYVF
FTHVQELFGNVVLKQVMKPLRWSNMATMPTLPETQAGIKEEIRRQEFLLNCLHRDLQGGI
KDLSKEERLWEVQRILTALKRKLREAKRQECETKIAQEIASLSKEDVSKEEMNENEEVIN
ILLAQENEILTEQEELLAMEQFLRRQIASEKEEIERLRAEIAEIQSRQQHGRSETEEYSS
ESESESEDEEELQIILEDLQRQNEELEIKNNHLNQAIHEEREAIIELRVQLRLLQMQRAK
AEQQAQEDEEPEWRGGAVQPPRDGVLEPKAAKEQPKAGKEPAKPSPSRDRKETSI
Enzyme 103 Number of Residues 655
Enzyme 103 Molecular Weight 76062.9
Enzyme 103 Theoretical pI 5.68
Enzyme 103 GO Classification
Function
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
  • cell part
  • intracellular
Enzyme 103 General Function Involved in signal transduction
Enzyme 103 Specific Function Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin
Enzyme 103 Pathways Not Available
Enzyme 103 Reactions Not Available
Enzyme 103 Pfam Domain Function
Enzyme 103 Signals
  • None
Enzyme 103 Transmembrane Regions
  • None
Enzyme 103 Essentiality Not Available
Enzyme 103 GenBank ID Protein 15341887 Link Image
Enzyme 103 UniProtKB/Swiss-Prot ID Q15311 Link Image
Enzyme 103 UniProtKB/Swiss-Prot Entry Name RBP1_HUMAN Link Image
Enzyme 103 PDB ID Not Available
Enzyme 103 Cellular Location Not Available
Enzyme 103 Gene Sequence >1968 bp
ATGACTGAGTGCTTCCTGCCCCCCACCAGCAGCCCCAGTGAACACCGCAGGGTGGAGCAT
GGCAGCGGGCTTACCCGGACCCCCAGCTCTGAAGAGATCAGCCCTACTAAGTTTCCTGGA
TTGTACCGCACTGGCGAGCCCTCACCTCCCCATGACATCCTCCATGAGCCTCCTGATGTA
GTGTCTGATGATGAGAAAGATCATGGGAAGAAAAAAGGGAAATTTAAGAAAAAGGAAAAG
AGGACTGAAGGCTATGCAGCCTTTCAGGAAGATAGCTCTGGAGATGAGGCAGAAAGTCCT
TCTAAAATGAAGAGGTCCAAGGGAATCCATGTTTTCAAGAAGCCCAGCTTTTCTAAAAAG
AAGGAAAAGGATTTTAAAATAAAAGAGAAACCCAAAGAAGAAAAGCATAAAGAAGAAAAG
CACAAAGAAGAAAAACATAAAGAGAAGAAGTCAAAAGACTTGACAGCAGCTGATGTTGTT
AAACAGTGGAAGGAAAAGAAGAAAAAGAAAAAGCCAATTCAGGAGCCAGAGGTGCCTCAG
ATTGATGTTCCAAATCTCAAACCCATTTTTGGAATTCCTTTGGCTGATGCAGTAGAGAGG
ACCATGATGTATGATGGCATTCGGCTGCCAGCCGTTTTCCGTGAATGTATAGATTACGTA
GAGAAGTATGGCATGAAGTGTGAAGGCATCTACAGAGTATCAGGAATTAAATCAAAGGTG
GATGAGCTAAAAGCAGCCTATGACCGGGAGGAGTCTACAAACTTGGAAGACTATGAGCCT
AACACTGTAGCCAGTTTGCTGAAGCAGTATTTGCGAGACCTTCCAGAGAATTTGCTTACC
AAAGAGCTTATGCCCAGATTTGAAGAGGCTTGTGGGAGGACCACGGAGACTGAGAAAGTG
CAGGAATTCCAGCGTTTACTCAAAGAACTGCCAGAATGTAACTATCTTCTGATTTCTTGG
CTCATTGTGCACATGGACCATGTCATTGCAAAGGAACTGGAAACAAAAATGAATATACAG
AACATTTCTATAGTGCTCAGCCCAACTGTGCAGATCAGCAATCGAGTCCTGTATGTGTTT
TTCACACATGTGCAAGAACTCTTTGGAAATGTGGTACTAAAGCAAGTGATGAAACCTCTG
CGATGGTCTAACATGGCCACGATGCCCACGCTGCCAGAGACCCAGGCGGGCATCAAGGAG
GAGATCAGGAGACAGGAGTTTCTTTTGAATTGTTTACATCGAGATCTGCAGGGTGGGATA
AAGGATTTGTCTAAAGAAGAAAGATTATGGGAAGTACAAAGAATTTTGACAGCCCTCAAA
AGAAAACTGAGAGAAGCTAAAAGACAGGAGTGTGAAACCAAGATTGCACAAGAGATAGCC
AGTCTTTCAAAAGAGGATGTTTCCAAAGAAGAGATGAATGAAAATGAAGAAGTTATAAAT
ATTCTCCTTGCTCAGGAGAATGAGATCCTGACTGAACAGGAGGAGCTCCTGGCCATGGAG
CAGTTTCTGCGCCGGCAGATTGCCTCAGAAAAAGAAGAGATTGAACGCCTCAGAGCTGAG
ATTGCTGAAATTCAGAGTCGCCAGCAGCACGGCCGAAGTGAGACTGAGGAGTACTCCTCC
GAGAGCGAGAGCGAGAGTGAGGATGAGGAGGAGCTGCAGATCATTCTGGAAGACTTACAG
AGACAGAACGAAGAGCTGGAAATAAAGAACAATCATTTGAATCAAGCAATTCATGAGGAG
CGCGAGGCCATCATCGAGCTGCGCGTGCAGCTGCGGCTGCTCCAGATGCAGCGAGCCAAG
GCCGAGCAGCAGGCGCAGGAGGACGAGGAGCCTGAGTGGCGCGGGGGTGCCGTCCAGCCG
CCCAGAGACGGCGTCCTTGAGCCAAAAGCAGCTAAAGAGCAGCCAAAGGCAGGCAAGGAG
CCGGCAAAGCCATCGCCCAGCAGGGATAGGAAGGAGACGTCCATCTGA
Enzyme 103 GenBank Gene ID BC013126 Link Image
Enzyme 103 GeneCard ID RALBP1 Link Image
Enzyme 103 GenAtlas ID RALBP1 Link Image
Enzyme 103 HGNC ID HGNC:9841 Link Image
Enzyme 103 Chromosome Location 1
Enzyme 103 Locus 18p11.3
Enzyme 103 SNPs SNPJam Report Link Image
Enzyme 103 General References
  1. 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]
  2. Awasthi S, Cheng J, Singhal SS, Saini MK, Pandya U, Pikula S, Bandorowicz-Pikula J, Singh SV, Zimniak P, Awasthi YC: Novel function of human RLIP76: ATP-dependent transport of glutathione conjugates and doxorubicin. Biochemistry. 2000 Aug 8;39(31):9327-34. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ikeda M, Ishida O, Hinoi T, Kishida S, Kikuchi A: Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral. J Biol Chem. 1998 Jan 9;273(2):814-21. [PubMed Link Image]
  5. Rosse C, L'Hoste S, Offner N, Picard A, Camonis J: RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis. J Biol Chem. 2003 Aug 15;278(33):30597-604. Epub 2003 May 29. [PubMed Link Image]
  6. Sharma R, Singhal SS, Cheng J, Yang Y, Sharma A, Zimniak P, Awasthi S, Awasthi YC: RLIP76 is the major ATP-dependent transporter of glutathione-conjugates and doxorubicin in human erythrocytes. Arch Biochem Biophys. 2001 Jul 15;391(2):171-9. [PubMed Link Image]
  7. Zhang H, Zhang R, Luo Y, D'Alessio A, Pober JS, Min W: AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-induced ASK1-JNK activation. J Biol Chem. 2004 Oct 22;279(43):44955-65. Epub 2004 Aug 13. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  9. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  10. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  11. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  12. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  13. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  14. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 103 Metabolite References Not Available
Enzyme 104 [top]
Enzyme 104 ID 7906
Enzyme 104 Name Guanine nucleotide-binding protein G(t) subunit alpha-1
Enzyme 104 Synonyms
  1. Transducin alpha-1 chain
Enzyme 104 Gene Name GNAT1
Enzyme 104 Protein Sequence >Guanine nucleotide-binding protein G(t) subunit alpha-1
MGAGASAEEKHSRELEKKLKEDAEKDARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLE
ECLEFIAIIYGNTLQSILAIVRAMTTLNIQYGDSARQDDARKLMHMADTIEEGTMPKEMS
DIIQRLWKDSGIQACFERASEYQLNDSAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGI
IETQFSFKDLNFRMFDVGGQRSERKKWIHCFEGVTCIIFIAALSAYDMVLVEDDEVNRMH
ESLHLFNSICNHRYFATTSIVLFLNKKDVFFEKIKKAHLSICFPDYDGPNTYEDAGNYIK
VQFLELNMRRDVKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF
Enzyme 104 Number of Residues 350
Enzyme 104 Molecular Weight 40040.4
Enzyme 104 Theoretical pI 5.32
Enzyme 104 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • molecular transducer activity
  • nucleotide binding
  • purine nucleotide binding
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • biological regulation
  • cell surface receptor linked signaling pathway
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 104 General Function Involved in signal transducer activity
Enzyme 104 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase
Enzyme 104 Pathways Not Available
Enzyme 104 Reactions Not Available
Enzyme 104 Pfam Domain Function
Enzyme 104 Signals
  • None
Enzyme 104 Transmembrane Regions
  • None
Enzyme 104 Essentiality Not Available
Enzyme 104 GenBank ID Protein 31865 Link Image
Enzyme 104 UniProtKB/Swiss-Prot ID P11488 Link Image
Enzyme 104 UniProtKB/Swiss-Prot Entry Name GNAT1_HUMAN Link Image
Enzyme 104 PDB ID 1TND Link Image
Enzyme 104 PDB File Show
Enzyme 104 3D Structure
Enzyme 104 Cellular Location Not Available
Enzyme 104 Gene Sequence >1053 bp
ATGGGGGCTGGGGCCAGTGCTGAGGAGAAGCACTCCAGGGAGCTGGAAAAGAAGCTGAAA
GAGGACGCTGAGAAGGATGCTCGAACCGTGAAGCTGCTGCTTCTGGGTGCCGGTGAGTCC
GGGAAGAGCACCATCGTCAAGCAGATGAAGATTATCCACCAGGACGGGTACTCGCTGGAA
GAGTGCCTCGAGTTTATCGCCATCATCTACGGCAACACGTTGCAGTCCATCCTGGCCATC
GTACGCGCCATGACCACACTCAACATCCAGTACGGAGACTCTGCACGCCAGGACGACGCC
CGGAAGCTGATGCACATGGCAGACACTATCGAGGAGGGCACGATGCCCAAGGAGATGTCG
GACATCATCCAGCGGCTGTGGAAGGACTCCGGTATCCAGGCCTGTTTTGAGCGCGCCTCG
GAGTACCAGCTCAACGACTCGGCGGGCTACTACCTCTCCGACCTGGAGCGCCTGGTAACC
CCGGGCTACGTGCCCACCGAGCAGGACGTGCTGCGCTCGCGAGTCAAGACCACTGGCATC
ATCGAGACGCAGTTCTCCTTCAAGGATCTCAACTTCCGGATGTTCGATGTGGGCGGGCAG
CGCTCGGAGCCGAAGAAGTGGATCCACTGCTTCGAGGGCGTGACCTGCATCATCTTCATC
GCGGCGCTGACCGCGTACGACATGGTGCTAGTGGAGGACGACGAAGTGAACCGCATGCAC
GAGAGCCTGCACCTGTTCAACAGCATCTGCAACCACCGCTACTTCGCCACGACGTCCATC
GTGCTCTTCCTTAACAAGAAGGACGTCTTCTTCGAGAAGGTCAAGAAGGCGCACCTCAGC
ATCTGTTTCCCGGACTACGATGGACCCAACACCTACGAGGACGCCGGCAACTACATCAAG
GTGCAGTTCCTCGAGCTCAACATGCGGCGCGACGTGAAGGAGATCTATTCCCACATGACG
TGCGCCACCGACACGCAGAACGTCAAATTCTGCTTCGACGCTGTCACCGACATCATCATC
AAGGAGAACCTCAAAGACTGTGGCCTCTTCTGA
Enzyme 104 GenBank Gene ID X15088 Link Image
Enzyme 104 GeneCard ID GNAT1 Link Image
Enzyme 104 GenAtlas ID GNAT1 Link Image
Enzyme 104 HGNC ID HGNC:4393 Link Image
Enzyme 104 Chromosome Location 3
Enzyme 104 Locus 3p21
Enzyme 104 SNPs SNPJam Report Link Image
Enzyme 104 General References
  1. Fong SL: Characterization of the human rod transducin alpha-subunit gene. Nucleic Acids Res. 1992 Jun 11;20(11):2865-70. [PubMed Link Image]
  2. Lerea CL, Bunt-Milam AH, Hurley JB: Alpha transducin is present in blue-, green-, and red-sensitive cone photoreceptors in the human retina. Neuron. 1989 Sep;3(3):367-76. [PubMed Link Image]
  3. Van Dop C, Medynski DC, Apone LM: Nucleotide sequence for a cDNA encoding the alpha subunit of retinal transducin (GNAT1) isolated from the human eye. Nucleic Acids Res. 1989 Jun 26;17(12):4887. [PubMed Link Image]
  4. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Bell MW, Desai N, Guo XX, Ghalayini AJ: Tyrosine phosphorylation of the alpha subunit of transducin and its association with Src in photoreceptor rod outer segments. J Neurochem. 2000 Nov;75(5):2006-19. [PubMed Link Image]
  7. Dryja TP, Hahn LB, Reboul T, Arnaud B: Missense mutation in the gene encoding the alpha subunit of rod transducin in the Nougaret form of congenital stationary night blindness. Nat Genet. 1996 Jul;13(3):358-60. [PubMed Link Image]
Enzyme 104 Metabolite References Not Available
Enzyme 105 [top]
Enzyme 105 ID 7920
Enzyme 105 Name Early endosome antigen 1
Enzyme 105 Synonyms
  1. Endosome-associated protein p162
  2. Zinc finger FYVE domain-containing protein 2
Enzyme 105 Gene Name EEA1
Enzyme 105 Protein Sequence >Early endosome antigen 1
MLRRILQRTPGRVGSQGSDLDSSATPINTVDVNNESSSEGFICPQCMKSLGSADELFKHY
EAVHDAGNDSGHGGESNLALKRDDVTLLRQEVQDLQASLKEEKWYSEELKKELEKYQGLQ
QQEAKPDGLVTDSSAELQSLEQQLEEAQTENFNIKQMKDLFEQKAAQLATEIADIKSKYD
EERSLREAAEQKVTRLTEELNKEATVIQDLKTELLQRPGIEDVAVLKKELVQVQTLMDNM
TLERERESEKLKDECKKLQSQYASSEATISQLRSELAKGPQEVAVYVQELQKLKSSVNEL
TQKNQTLTENLLKKEQDYTKLEEKHNEESVSKKNIQATLHQKDLDCQQLQSRLSASETSL
HRIHVELSEKGEATQKLKEELSEVETKYQHLKAEFKQLQQQREEKEQHGLQLQSEINQLH
SKLLETERQLGEAHGRLKEQRQLSSEKLMDKEQQVADLQLKLSRLEEQLKEKVTNSTELQ
HQLDKTKQQHQEQQALQQSTTAKLREAQNDLEQVLRQIGDKDQKIQNLEALLQKSKENIS
LLEKEREDLYAKIQAGEGETAVLNQLQEKNHTLQEQVTQLTEKLKNQSESHKQAQENLHD
QVQEQKAHLRAAQDRVLSLETSVNELNSQLNESKEKVSQLDIQIKAKTELLLSAEAAKTA
QRADLQNHLDTAQNALQDKQQELNKITTQLDQVTAKLQDKQEHCSQLESHLKEYKEKYLS
LEQKTEELEGQIKKLEADSLEVKASKEQALQDLQQQRQLNTDLELRATELSKQLEMEKEI
VSSTRLDLQKKSEALESIKQKLTKQEEEKKILKQDFETLSQETKIQHEELNNRIQTTVTE
LQKVKMEKEALMTELSTVKDKLSKVSDSLKNSKSEFEKENQKGKAAILDLEKTCKELKHQ
LQVQMENTLKEQKELKKSLEKEKEASHQLKLELNSMQEQLIQAQNTLKQNEKEEQQLQGN
INELKQSSEQKKKQIEALQGELKIAVLQKTELENKLQQQLTQAAQELAAEKEKISVLQNN
YEKSQETFKQLQSDFYGRESELLATRQDLKSVEEKLSLAQEDLISNRNQIGNQNKLIQEL
KTAKATLEQDSAKKEQQLQERCKALQDIQKEKSLKEKELVNEKSKLAEIEEIKCRQEKEI
TKLNEELKSHKLESIKEITNLKDAKQLLIQQKLELQGKADSLKAAVEQEKRNQQILKDQV
KKEEEELKKEFIEKEAKLHSEIKEKEVGMKKHEENEAKLTMQITALNENLGTVKKEWQSS
QRRVSELEKQTDDLRGEIAVLEATVQNNQDERRALLERCLKGEGEIEKLQTKVLELQRKL
DNTTAAVQELGRENQSLQIKHTQALNRKWAEDNEVQNCMACGKGFSVTVRRHHCRQCGNI
FCAECSAKNALTPSSKKPVRVCDACFNDLQG
Enzyme 105 Number of Residues 1411
Enzyme 105 Molecular Weight 162464.9
Enzyme 105 Theoretical pI 5.41
Enzyme 105 GO Classification
Function
  • binding
  • cation binding
  • ion binding
  • metal ion binding
  • transition metal ion binding
  • zinc ion binding
Process
Component
  • cell part
  • intracellular
Enzyme 105 General Function Involved in zinc ion binding
Enzyme 105 Specific Function Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in endosomal trafficking
Enzyme 105 Pathways Not Available
Enzyme 105 Reactions Not Available
Enzyme 105 Pfam Domain Function
Enzyme 105 Signals
  • None
Enzyme 105 Transmembrane Regions
  • None
Enzyme 105 Essentiality Not Available
Enzyme 105 GenBank ID Protein 1016368 Link Image
Enzyme 105 UniProtKB/Swiss-Prot ID Q15075 Link Image
Enzyme 105 UniProtKB/Swiss-Prot Entry Name EEA1_HUMAN Link Image
Enzyme 105 PDB ID 1JOC Link Image
Enzyme 105 PDB File Show
Enzyme 105 3D Structure
Enzyme 105 Cellular Location Not Available
Enzyme 105 Gene Sequence >4233 bp
ATGTTAAGGAGGATTTTACAGAGGACTCCTGGGAGAGTTGGCTCTCAAGGTTCTGATTTA
GATTCATCAGCAACTCCTATAAACACAGTGGACGTCAATAATGAAAGCTCTTCAGAAGGT
TTCATATGTCCCCAGTGTATGAAATCTCTTGGATCTGCTGATGAACTTTTCAAACATTAT
GAAGCTGTTCATGATGCTGGTAATGACTCAGGTCATGGAGGAGAGTCTAATCTTGCTTTG
AAGCGAGATGATGTAACACTGCTCAGACAAGAGGTCCAAGACCTACAGGCTTCACTTAAG
GAAGAAAAATGGTACTCGGAAGAATTAAAGAAGGAATTAGAAAAATATCAAGGGCTGCAG
CAGCAAGAGGCCAAACCTGATGGGTTGGTGACTGATTCATCAGCAGAACTACAGTCTTTG
GAACAGCAATTAGAAGAAGCCCAAACAGAAAATTTTAATATTAAGCAAATGAAAGACTTA
TTTGAACAGAAAGCAGCCCAACTTGCTACTGAAATTGCAGATATAAAGTCAAAGTATGAT
GAAGAAAGGAGTCTTCGAGAAGCTGCTGAACAAAAAGTGACACGTCTGACAGAAGAATTA
AACAAAGAGGCAACTGTAATTCAAGATCTGAAGACGGAACTGCTTCAGAGACCTGGTATA
GAAGATGTTGCCGTGCTAAAGAAAGAACTGGTCCAAGTTCAAACACTAATGGATAACATG
ACCTTGGAACGTGAGCGAGAATCTGAAAAACTCAAAGATGAATCGAAAAAATTCGAGTCA
CAATATGCTAGCTCAGAGGCCACAATAAGCCAGCTAAGGAGTGAACTGTCCAAAGGCCCC
CAGGAAGTTCGTGTATATGTACAGGAACTACAAAAACTGAAAAGTTCAGTTAATGAATTA
ACACAAAAAAATCAGACCTTGACAGAAAACTTGCTGAAAAAAGAACAAGACTATACTAAG
TTAGAGGAGAAACATAATGAAGAATCTGTGAGTAAAAAGAATATTCAGGCAACCCTTCAT
CAAAAAGACCTAGATTGTCAACAGCTTCAGTCAAGATTGTCTGCATCTGAAACCTCACTG
CATAGAATACATGTAGAACTAAGTGAAAAAGGAGAAGCTACTCAAAAGCTCAAAGAAGAA
TTATCTGAGGTAGAGACCAAGTACCAGCATCTAAAGGCGGAGTTTAAGCAGCTACAACAA
CAGAGAGAAGAAAAGGAGCAGCATGGGTTACAACTCCAAAGTGAAATTAATCAATTACAT
AGCAAACTTCTGGAGACAGAGCGCCAACTAGGGGAAGCTCATGGTAGGCTGAAGGAACAG
AGACAGCTTTCAAGTGAAAAGTTGATGGATAAAGAACAACAAGTGGCTGATTTACAACTC
AAACTTTCTCGGTTAGAAGAGCAGTTGAAGGAAAAAGTTACAAATTCTACAGAATTGCAG
CATCAATTAGATAAAACAAAGCAACAGCATCAAGAACAACAGGCTCTTCAGCAAAGCACC
ACGGCAAAACTTCGAGAAGCTCAGAATGATTTGGAACAAGTTCTACGTCAAATTGGCGAA
AAGGACCAAAAGATCCAGAACCTTGAAGCTTTATTACAGAAGAGTAAAGAAAATATTTCA
TTACTAGAAAAAGAAAGAGAAGATCTTTATGCAAAAATTCAGGCTGGTGAAGGAGAGACT
GCTGTTCTTAACCAGTTACAAGAAAAAAACCATACACTACAGGACGAAGTAACTCAACTA
ACAGAGAACGTGAAGAATCAGTCAGAAAGTCATAAACAAGCCCAGGAGAATTTGCATGAC
CAGGTACAAGAGCAGAAGGCACATCTTAGAGCTGCACAAGACCGTGTCCTTTCCCTAGAA
ACTAGTGTCAATGAATTAAATAGTCAATTAAATGAAAGCAAGGAGAAGGTCTCCCAGCTT
GACATACAGATTAAAGCCAAAACCGAACTATTACTATCAGCAGAAGCAGCAAAAACTGCT
CAAAGAGCTGATCTTCAGAATCATTTGGACACAGCTCAAAATGCATTACAAGATAAACAC
CAGGAGTTAAATAAGATTACTACTCAGTTGGATCAGGTCACTGCAAAGTTACAAGACAAG
CAAGAACATTGCAGTCAGCTGGAAAGTCATCTTAAAGAATATAAAGAGAAATACCTCTCT
TTAGAACAGAAAACCGAAGAGCTAGAAGGTCAAATTAAGAAACTAGAAGCTGATAGTCTT
GAAGTTAAAGCAAGCAAGGAGCAGGCTTTGCAAGATCTACAACAGCAAAGACAGCTGAAC
ACAGATTTAGAGCTCAGAGCCACAGAATTGAGTAAACAACTTGAAATGGAGAAGGAAATA
GTATCCAGTACAAGATTGGATCTACAGAAAAAATCTGAAGCCCTTGAAAGTATCAAGCAA
AAGCTTACCAAGCAAGAGGAAGAAAAACAAATCCTGAAACAAGATTTTGAAACTTTAAGT
CAAGAAACAAAGATTCAGCATGAGGAATTGAATAACAGAATTCAAACAACAGTAACAGAA
CTACAAAAAGTGAAAATGGAGAAAGAAGCTTTAATGACAGAGCTTTCTACAGTAAAGGAC
AAACTATCAAAAGTTTCTGATTCTTTGAAAAACTCTAAAAGTGAATTTGAAAAGGAGAAT
CAGAAAGGAAAAGCCGCTATATTAGACTTGGAAAAAACTTGCAAAGAATTAAAGCATCAA
CTTCAAGTGCAGATGGAAAACACACTTAAGGAACAGAAGGAACTGAAAAAGTCACTTGAA
AAAGAGAAGGAGGCTTCTCATCAGTTGAAATTGGAACTCAATTCAATGCAGGAACAACTT
ATACAGGCCCAGAATACTTTAAAACAAAATGAAAAAGAAGAGCAACAACTTCAGGGGAAC
ATAAATGAGCTAAAGCAATCAAGTGAACAGAAGAAAAAACAAATTGAAGCACTCCAAGGA
GAGCTTAAAATTGCTGTTTTACAGAAGACAGAGCTTGAGAATAAACTACAGCAGCAGTTA
ACACAGGCAGCCCAGGAACTTGCAGCAGAGAAAGAGAAAATATCAGTATTACAAAACAAC
TATGAAAAAAGTCAGGAAACTTTCAAACAGCTTCAATCTGATTTCTATGGGAGGGAATCT
GAACTTCTAGCCACCAGGCAAGATCTTAAGTCTGTAGAAGAGAAGCTTTCTCTAGCACAG
GAGGACTTGATTTCAAACAGAAATCAAATTGGAAATCAAAATAAATTGATTCAAGAACTG
AAGACTGCCAAGGCTACATTGGAGCAGGATTCAGCAAAGAAAGAACAGCAATTGCAGGAG
CGATGTAAAGCACTACAAGACATTCAGAAAGAAAAGTCACTGAAAGAAAAAGAACTGGTA
AATGAGAAGTCTAAATTGGCAGAGATAGAAGAAATTAAATGTAGACAAGAAAAAGAAATC
ACTAAACTAAACGAAGAACTCAAGTCCCACAAACTAGAAAGCATAAAGGAGATAACAAAT
CTTAAAGATGCTAAACAGCTTCTAATTCAGCAGAAATTAGAACTTCAAGGAAAAGCGGAC
TCCCTGAAGGCAGCTGTTGAACAGGAGAAGAGAAATCAGCAGATACTAAAAGACCAGGTG
AAAAAGGAAGAAGAGGAGCTGAAGAAAGAATTTATTGAGAAAGAAGCTAAGTTGCATTCC
GAAATAAAAGAAAAGGAAGTAGGAATGAAGAAGCATGAAGAAAATGAGGCTAAACTTACC
ATGCAGATTACAGCATTAAATGAAAACTTAGGCACTGTGAAGAAGGAGTGGCAATCTAGT
CAACGGAGAGTTAGTGAGCTTGAGAAACAAACGGATGACTTACGGGGTGAAATTGCAGTA
TTAGAAGCAACGGTTCAGAATAATCAAGATGAAAGGAGAGCACTACTGGAAAGATGTCTT
AAAGGAGAAGGTGAAATAGAAAAGCTTCAAACCAAAGTATTAGAATTGCAAAGAAAGCTG
GATAATACAACTGCAGTGCAGGAGCTGGGCAGAGAAAACCAATCACTTCAGATCAAACAT
ACACAAGCGTTGAATAGAAAGTGGGCCGAAGACAATGAAGTACAAAACTGTATGGCCTGT
GGGAAAGGCTTTTCAGTAACAGTGAGACGGCATCACTGCCGACAGTGTGGAAATATCTTC
TGTGCTGAATGTTCAGCCAAAAATGCCTTAACTCCTTCCTCCAAGAAGCCTGTTCGTGTC
TGTGATGCATGTTTCAATGACTTGCAAGGATAA
Enzyme 105 GenBank Gene ID L40157 Link Image
Enzyme 105 GeneCard ID EEA1 Link Image
Enzyme 105 GenAtlas ID EEA1 Link Image
Enzyme 105 HGNC ID HGNC:3185 Link Image
Enzyme 105 Chromosome Location 1
Enzyme 105 Locus 12q22
Enzyme 105 SNPs SNPJam Report Link Image
Enzyme 105 General References
  1. Mu FT, Callaghan JM, Steele-Mortimer O, Stenmark H, Parton RG, Campbell PL, McCluskey J, Yeo JP, Tock EP, Toh BH: EEA1, an early endosome-associated protein. EEA1 is a conserved alpha-helical peripheral membrane protein flanked by cysteine "fingers" and contains a calmodulin-binding IQ motif. J Biol Chem. 1995 Jun 2;270(22):13503-11. [PubMed Link Image]
  2. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  3. Simonsen A, Lippe R, Christoforidis S, Gaullier JM, Brech A, Callaghan J, Toh BH, Murphy C, Zerial M, Stenmark H: EEA1 links PI(3)K function to Rab5 regulation of endosome fusion. Nature. 1998 Jul 30;394(6692):494-8. [PubMed Link Image]
  4. Callaghan J, Nixon S, Bucci C, Toh BH, Stenmark H: Direct interaction of EEA1 with Rab5b. Eur J Biochem. 1999 Oct 1;265(1):361-6. [PubMed Link Image]
  5. Simonsen A, Gaullier JM, D'Arrigo A, Stenmark H: The Rab5 effector EEA1 interacts directly with syntaxin-6. J Biol Chem. 1999 Oct 8;274(41):28857-60. [PubMed Link Image]
  6. Kutateladze TG, Ogburn KD, Watson WT, de Beer T, Emr SD, Burd CG, Overduin M: Phosphatidylinositol 3-phosphate recognition by the FYVE domain. Mol Cell. 1999 Jun;3(6):805-11. [PubMed Link Image]
  7. Gaullier JM, Ronning E, Gillooly DJ, Stenmark H: Interaction of the EEA1 FYVE finger with phosphatidylinositol 3-phosphate and early endosomes. Role of conserved residues. J Biol Chem. 2000 Aug 11;275(32):24595-600. [PubMed Link Image]
  8. Kauppi M, Simonsen A, Bremnes B, Vieira A, Callaghan J, Stenmark H, Olkkonen VM: The small GTPase Rab22 interacts with EEA1 and controls endosomal membrane trafficking. J Cell Sci. 2002 Mar 1;115(Pt 5):899-911. [PubMed Link Image]
  9. Merithew E, Stone C, Eathiraj S, Lambright DG: Determinants of Rab5 interaction with the N terminus of early endosome antigen 1. J Biol Chem. 2003 Mar 7;278(10):8494-500. Epub 2002 Dec 19. [PubMed Link Image]
  10. Dumas JJ, Merithew E, Sudharshan E, Rajamani D, Hayes S, Lawe D, Corvera S, Lambright DG: Multivalent endosome targeting by homodimeric EEA1. Mol Cell. 2001 Nov;8(5):947-58. [PubMed Link Image]
  11. Kutateladze T, Overduin M: Structural mechanism of endosome docking by the FYVE domain. Science. 2001 Mar 2;291(5509):1793-6. [PubMed Link Image]
Enzyme 105 Metabolite References Not Available
Enzyme 106 [top]
Enzyme 106 ID 7998
Enzyme 106 Name Target of rapamycin complex 2 subunit MAPKAP1
Enzyme 106 Synonyms
  1. TORC2 subunit MAPKAP1
  2. Mitogen-activated protein kinase 2-associated protein 1
  3. Stress-activated map kinase-interacting protein 1
  4. SAPK-interacting protein 1
  5. mSIN1
Enzyme 106 Gene Name MAPKAP1
Enzyme 106 Protein Sequence >Target of rapamycin complex 2 subunit MAPKAP1
MAFLDNPTIILAHIRQSHVTSDDTGMCEMVLIDHDVDLEKIHPPSMPGDSGSEIQGSNGE
TQGYVYAQSVDITSSWDFGIRRRSNTAQRLERLRKERQNQIKCKNIQWKERNSKQSAQEL
KSLFEKKSLKEKPPISGKQSILSVRLEQCPLQLNNPFNEYSKFDGKGHVGTTATKKIDVY
LPLHSSQDRLLPMTVVTMASARVQDLIGLICWQYTSEGREPKLNDNVSAYCLHIAEDDGE
VDTDFPPLDSNEPIHKFGFSTLALVEKYSSPGLTSKESLFVRINAAHGFSLIQVDNTKVT
MKEILLKAVKRRKGSQKVSGPQYRLEKQSEPNVAVDLDSTLESQSAWEFCLVRENSSRAD
GVFEEDSQIDIATVQDMLSSHHYKSFKVSMIHRLRFTTDVQLGISGDKVEIDPVTNQKAS
TKFWIKQKPISIDSDLLCACDLAEEKSPSHAIFKLTYLSNHDYKHLYFESDAATVNEIVL
KVNYILESRASTARADYFAQKQRKLNRRTSFSFQKEKKSGQQ
Enzyme 106 Number of Residues 522
Enzyme 106 Molecular Weight 59122.3
Enzyme 106 Theoretical pI 7.61
Enzyme 106 GO Classification Not Available
Enzyme 106 General Function Involved in Ras GTPase binding
Enzyme 106 Specific Function Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient- insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Within mTORC2, MAPKAP1 is required for complex formation and mTORC2 kinase activity. MAPKAP1 inhibits MAP3K2 by preventing its dimerization and autophosphorylation. Inhibits HRAS and KRAS signaling. Enhances osmotic stress-induced phosphorylation of ATF2 and ATF2-mediated transcription
Enzyme 106 Pathways Not Available
Enzyme 106 Reactions Not Available
Enzyme 106 Pfam Domain Function
Enzyme 106 Signals
  • None
Enzyme 106 Transmembrane Regions
  • None
Enzyme 106 Essentiality Not Available
Enzyme 106 GenBank ID Protein Not Available
Enzyme 106 UniProtKB/Swiss-Prot ID Q9BPZ7 Link Image
Enzyme 106 UniProtKB/Swiss-Prot Entry Name SIN1_HUMAN Link Image
Enzyme 106 PDB ID Not Available
Enzyme 106 Cellular Location Not Available
Enzyme 106 Gene Sequence >1569 bp
ATGGCCTTCTTGGACAATCCAACTATCATTCTAGCTCATATTCGACAGTCACATGTGACC
AGTGATGACACGGGAATGTGTGAGATGGTTCTCATTGATCATGATGTTGACCTAGAGAAG
ATTCATCCTCCTTCAATGCCTGGAGACAGTGGGTCAGAAATTCAGGGAAGCAATGGTGAG
ACTCAGGGCTATGTATATGCCCAGTCAGTCGATATTACCTCAAGTTGGGACTTTGGTATT
AGAAGACGCTCAAACACAGCTCAAAGATTAGAACGACTCCGAAAAGAGAGACAAAACCAG
ATCAAATGCAAAAATATTCAGTGGAAAGAAAGAAATTCTAAGCAATCAGCCCAGGAGTTA
AAGTCACTGTTTGAAAAAAAATCTCTCAAAGAGAAGCCTCCAATTTCTGGGAAGCAGTCG
ATATTATCTGTACGCCTAGAACAGTGCCCTCTGCAGCTGAATAACCCTTTTAACGAGTAT
TCCAAATTTGATGGCAAGGGTCATGTAGGTACAACAGCAACCAAGAAGATCGATGTCTAC
CTCCCTCTGCACTCGAGCCAGGACAGACTGCTGCCAATGACCGTGGTGACAATGGCCAGC
GCCAGGGTGCAGGACCTGATCGGGCTCATCTGCTGGCAGTATACAAGCGAAGGACGGGAG
CCGAAGCTCAATGACAATGTCAGTGCCTACTGCCTGCATATTGCTGAGGATGATGGGGAG
GTGGACACCGATTTCCCCCCGCTGGATTCCAATGAGCCCATTCATAAGTTTGGCTTCAGT
ACTTTGGCCCTGGTTGAAAAGTACTCATCTCCTGGTCTGACATCCAAAGAGTCACTCTTT
GTTCGAATAAATGCTGCTCATGGATTCTCCCTTATTCAGGTGGACAACACAAAGGTTACC
ATGAAGGAAATCTTACTGAAGGCAGTGAAGCGAAGAAAAGGATCCCAGAAAGTTTCAGGC
CCTCAGTACCGCCTGGAGAAGCAGAGCGAGCCCAATGTCGCCGTTGACCTGGACAGCACT
TTGGAGAGCCAGAGCGCATGGGAGTTCTGCCTGGTCCGCGAGAACAGTTCAAGGGCAGAC
GGGGTTTTTGAGGAGGATTCGCAAATTGACATAGCCACAGTACAGGATATGCTTAGCAGC
CACCATTACAAGTCATTCAAAGTCAGCATGATCCACAGACTGCGATTCACAACCGACGTA
CAGCTAGGTATCTCTGGAGACAAAGTAGAGATAGACCCTGTTACGAATCAGAAAGCCAGC
ACTAAGTTTTGGATTAAGCAGAAACCCATCTCAATCGATTCCGACCTGCTCTGTGCCTGT
GACCTTGCTGAAGAGAAAAGCCCCAGTCACGCAATATTTAAACTCACGTATCTAAGCAAT
CACGACTATAAACACCTCTACTTTGAATCGGACGCTGCTACCGTCAATGAAATTGTGCTC
AAGGTTAACTACATCCTGGAATCGCGAGCTAGCACTGCCCGGGCTGACTACTTTGCTCAA
AAACAAAGAAAACTGAACAGACGTACGAGCTTCAGCTTCCAGAAGGAGAAGAAATCCGGG
CAGCAGTGA
Enzyme 106 GenBank Gene ID AY524429 Link Image
Enzyme 106 GeneCard ID MAPKAP1 Link Image
Enzyme 106 GenAtlas ID MAPKAP1 Link Image
Enzyme 106 HGNC ID HGNC:18752 Link Image
Enzyme 106 Chromosome Location 9
Enzyme 106 Locus 9q33.3
Enzyme 106 SNPs SNPJam Report Link Image
Enzyme 106 General References
  1. Schroder W, Cloonan N, Bushell G, Sculley T: Alternative polyadenylation and splicing of mRNAs transcribed from the human Sin1 gene. Gene. 2004 Sep 15;339:17-23. [PubMed Link Image]
  2. Cheng J, Zhang D, Kim K, Zhao Y, Zhao Y, Su B: Mip1, an MEKK2-interacting protein, controls MEKK2 dimerization and activation. Mol Cell Biol. 2005 Jul;25(14):5955-64. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Colicelli J, Nicolette C, Birchmeier C, Rodgers L, Riggs M, Wigler M: Expression of three mammalian cDNAs that interfere with RAS function in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2913-7. [PubMed Link Image]
  8. Jacinto E, Facchinetti V, Liu D, Soto N, Wei S, Jung SY, Huang Q, Qin J, Su B: SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity. Cell. 2006 Oct 6;127(1):125-37. Epub 2006 Sep 7. [PubMed Link Image]
  9. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  10. Frias MA, Thoreen CC, Jaffe JD, Schroder W, Sculley T, Carr SA, Sabatini DM: mSin1 is necessary for Akt/PKB phosphorylation, and its isoforms define three distinct mTORC2s. Curr Biol. 2006 Sep 19;16(18):1865-70. Epub 2006 Aug 17. [PubMed Link Image]
  11. Makino C, Sano Y, Shinagawa T, Millar JB, Ishii S: Sin1 binds to both ATF-2 and p38 and enhances ATF-2-dependent transcription in an SAPK signaling pathway. Genes Cells. 2006 Nov;11(11):1239-51. [PubMed Link Image]
  12. Yang Q, Inoki K, Ikenoue T, Guan KL: Identification of Sin1 as an essential TORC2 component required for complex formation and kinase activity. Genes Dev. 2006 Oct 15;20(20):2820-32. [PubMed Link Image]
  13. Schroder WA, Buck M, Cloonan N, Hancock JF, Suhrbier A, Sculley T, Bushell G: Human Sin1 contains Ras-binding and pleckstrin homology domains and suppresses Ras signalling. Cell Signal. 2007 Jun;19(6):1279-89. Epub 2007 Jan 20. [PubMed Link Image]
  14. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  15. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  16. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
Enzyme 106 Metabolite References Not Available
Enzyme 107 [top]
Enzyme 107 ID 8075
Enzyme 107 Name Uridine-cytidine kinase 2
Enzyme 107 Synonyms
  1. UCK 2
  2. Cytidine monophosphokinase 2
  3. Testis-specific protein TSA903
  4. Uridine monophosphokinase 2
Enzyme 107 Gene Name UCK2
Enzyme 107 Protein Sequence >Uridine-cytidine kinase 2
MAGDSEQTLQNHQQPNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQNEVDYRQKQVVILS
QDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELILKTLKEITEGKTVQIPVYDFVSHSRK
EETVTVYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ
ILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNGGPSKRQTNG
CLNGYTPSRKRQASESSSRPH
Enzyme 107 Number of Residues 261
Enzyme 107 Molecular Weight 29298.9
Enzyme 107 Theoretical pI 6.68
Enzyme 107 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolic process
Component
Enzyme 107 General Function Involved in ATP binding
Enzyme 107 Specific Function Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and N(4)-anisoylcytidine
Enzyme 107 Pathways
Enzyme 107 Reactions
  • ATP + uridine = ADP + UMP [RN:R00964]
Enzyme 107 Pfam Domain Function
Enzyme 107 Signals
  • None
Enzyme 107 Transmembrane Regions
  • None
Enzyme 107 Essentiality Not Available
Enzyme 107 GenBank ID Protein 18699734 Link Image
Enzyme 107 UniProtKB/Swiss-Prot ID Q9BZX2 Link Image
Enzyme 107 UniProtKB/Swiss-Prot Entry Name UCK2_HUMAN Link Image
Enzyme 107 PDB ID 1XRJ Link Image
Enzyme 107 PDB File Show
Enzyme 107 3D Structure
Enzyme 107 Cellular Location Not Available
Enzyme 107 Gene Sequence >786 bp
ATGGCCGGGGACAGCGAGCAGACCCTGCAGAACCACCAGCAGCCCAACGGCGGCGAGCCC
TTCCTTATAGGCGTCAGCGGGGGAACAGCTAGCGGCAAGTCTTCCGTGTGTGCTAAGATC
GTGCAGCTCCTGGGGCAGAATGAGGTGGACTATCGCCAGAAGCAGGTGGTCATCCTGAGC
CAGGATAGCTTCTACCGTGTCCTTACCTCGGAGCAGAAGGCCAAAGCCCTGAAGGGCCAG
TTCAACTTTGACCACCCGGATGCCTTTGACAATGAACTCATTCTCAAAACACTCAAAGAA
ATCACTGAAGGGAAAACAGTCCAGATCCCCGTGTATGACTTTGTCTCCCATTCCCGGAAG
GAGGAGACAGTTACTGTCTATCCCGCAGACGTGGTGCTCTTTGAAGGGATCCTGGCCTTC
TACTCCCAGGAGGTACGAGACCTGTTCCAGATGAAGCTTTTTGTGGATACAGATGCGGAC
ACCCGGCTCTCACGCAGAGTATTAAGGGACATCAGCGAGAGAGGCAGGGATCTTGAGCAG
ATTTTATCTCAGTACATTACGTTCGTCAAGCCTGCCTTTGAGGAATTCTGCTTGCCAACA
AAGAAGTATGCTGATGTGATCATCCCTAGAGGTGCAGATAATCTGGTGGCCATCAACCTC
ATCGTGCAGCACATCCAGGACATCCTGAATGGAGGGCCCTCCAAACGGCAGACCAATGGC
TGTCTCAACGGCTACACCCCTTCACGCAAGAGGCAGGCATCGGAGTCCAGCAGCAGGCCG
CATTGA
Enzyme 107 GenBank Gene ID NM_012474.3 Link Image
Enzyme 107 GeneCard ID UCK2 Link Image
Enzyme 107 GenAtlas ID UCK2 Link Image
Enzyme 107 HGNC ID HGNC:12562 Link Image
Enzyme 107 Chromosome Location 1
Enzyme 107 Locus 1q23
Enzyme 107 SNPs SNPJam Report Link Image
Enzyme 107 General References
  1. Ozaki K, Kuroki T, Hayashi S, Nakamura Y: Isolation of three testis-specific genes (TSA303, TSA806, TSA903) by a differential mRNA display method. Genomics. 1996 Sep 1;36(2):316-9. [PubMed Link Image]
  2. Van Rompay AR, Norda A, Linden K, Johansson M, Karlsson A: Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases. Mol Pharmacol. 2001 May;59(5):1181-6. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Koizumi K, Shimamoto Y, Azuma A, Wataya Y, Matsuda A, Sasaki T, Fukushima M: Cloning and expression of uridine/cytidine kinase cDNA from human fibrosarcoma cells. Int J Mol Med. 2001 Sep;8(3):273-8. [PubMed Link Image]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  8. Suzuki NN, Koizumi K, Fukushima M, Matsuda A, Inagaki F: Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase. Structure. 2004 May;12(5):751-64. [PubMed Link Image]
  9. Appleby TC, Larson G, Cheney IW, Walker H, Wu JZ, Zhong W, Hong Z, Yao N: Structure of human uridine-cytidine kinase 2 determined by SIRAS using a rotating-anode X-ray generator and a single samarium derivative. Acta Crystallogr D Biol Crystallogr. 2005 Mar;61(Pt 3):278-84. Epub 2005 Feb 24. [PubMed Link Image]
Enzyme 107 Metabolite References Not Available
Enzyme 108 [top]
Enzyme 108 ID 8236
Enzyme 108 Name Protein ALEX
Enzyme 108 Synonyms
  1. Alternative gene product encoded by XL-exon
Enzyme 108 Gene Name GNAS
Enzyme 108 Protein Sequence >Protein ALEX
MMARPVDPQRSPDPTFRSSTRHSGKLEPMEATAHLLRKQCPSRLNSPAWEASGLHWSSLD
SPVGSMQALRPSAQHSWSPEPSVVPDQAWEDTALHQKKLCPLSLTSLPREAAVNFSYRSQ
TLLQEAQVLQGSPELLPRSPKPSGLQRLAPEEATALPLRRLCHLSLMEKDLGTTAHPRGF
PELSHKSTAAASSRQSRPRVRSASLPPRTRLPSGSQAPSAAHPKRLSDLLLTSRAAAPGW
RSPDPRSRLAAPPLGSTTLPSTWTAPQSRLTARPSRSPEPQIRESEQRDPQLRRKQQRWK
EPLMPRREEKYPLRGTDPLPPGQPQRIPLPGQPLQPQPILTPGQPQKIPTPGQHQPILTP
GHSQPIPTPGQPLPPQPIPTPGRPLTPQPIPTPGRPLTPQPIQMPGRPLRLPPPLRLLRP
GQPMSPQLRQTQGLPLPQPLLPPGQPKSAGRPLQPLPPGPDARSISDPPAPRSRLPIRLL
RGLLARLPGGASPRAAAAAACTTMKGWPAATMTPAETSPTMGPPDASAGFSIGEIAAAES
PSATYSATFSCKPSGAASVDLRVPSPKPRALSRSRRYPWRRSADRCAKKPWRSGPRSAQR
RNAVSSSTNNSRTKRWATCVRTACCF
Enzyme 108 Number of Residues 626
Enzyme 108 Molecular Weight 67947.1
Enzyme 108 Theoretical pI 12.07
Enzyme 108 GO Classification Not Available
Enzyme 108 General Function Not Available
Enzyme 108 Specific Function May inhibit the adenylyl cyclase-stimulating activity of guanine nucleotide-binding protein G(s) subunit alpha which is produced from the same locus in a different open reading frame
Enzyme 108 Pathways Not Available
Enzyme 108 Reactions Not Available
Enzyme 108 Pfam Domain Function Not Available
Enzyme 108 Signals
  • None
Enzyme 108 Transmembrane Regions
  • None
Enzyme 108 Essentiality Not Available
Enzyme 108 GenBank ID Protein 117938768 Link Image
Enzyme 108 UniProtKB/Swiss-Prot ID P84996 Link Image
Enzyme 108 UniProtKB/Swiss-Prot Entry Name ALEX_HUMAN Link Image
Enzyme 108 PDB ID Not Available
Enzyme 108 Cellular Location Not Available
Enzyme 108 Gene Sequence >1881 bp
ATGATGGCGAGGCCTGTGGACCCCCAGAGGTCTCCAGACCCAACTTTCAGGTCCTCAACC
CGGCATTCAGGGAAGCTGGAGCCCATGGAAGCTACAGCCCACCTCCTGAGGAAGCAATGC
CCTTCGAGGCTGAACAGCCCAGCTTGGGAGGCTTCTGGCCTACACTGGAGCAGCCTGGAT
TCCCCAGTGGGGTCCATGCAGGCCTTGAGGCCTTCGGCCCAGCACTCATGGAGCCCGGAG
CCTTCAGTGGTGCCAGACCAGGCCTGGGAGGATACAGCCCTCCACCAGAAGAAGCTATGC
CCTTTGAGTTTGACCAGCCTGCCCAGAGAGGCTGCAGTCAACTTCTCTTACAGGTCCCAG
ACCTTGCTCCAGGAGGCCCAGGTGCTGCAGGGGTCCCCGGAGCTCCTCCCGAGGAGCCCC
AAGCCCTCAGGCCTGCAAAGGCTGGCTCCAGAGGAGGCTACAGCCCTCCCCCTGAGGAGA
CTATGCCATTTGAGCTTGATGGAGAAGGATTTGGGGACGACAGCCCACCCCCGGGGCTTT
CCCGAGTTATCGCACAAGTCGACGGCAGCAGCCAGTTCGCGGCAGTCGCGGCCTCGAGTG
CGGTCCGCCTCACTCCCGCCGCGAACGCGCCTCCCCTCTGGGTCCCAGGCGCCATCGGCA
GCCCATCCCAAGAGGCTGTCAGACCTCCTTCTAACTTCACGGGCAGCAGCCCCTGGATGG
AGATCTCCGGACCCCCGTTCGAGATTGGCAGCGCCCCCGCTGGGGTCGACGACACTCCCG
TCAACATGGACAGCCCCCCAATCGCGCTTGACGGCCCGCCCATCAAGGTCTCCGGAGCCC
CAGATAAGAGAGAGCGAGCAGAGAGACCCCCAGTTGAGGAGGAAGCAGCAGAGATGGAAG
GAGCCGCTGATGCCGCGGAGGGAGGAAAAGTACCCTCTCCGGGGTACGGATCCCCTGCCG
CCGGGGCAGCCTCAGCGGATACCGCTGCCAGGGCAGCCCCTGCAGCCCCAGCCGATCCTG
ACTCCGGGGCAACCCCAGAAGATCCCGACTCCGGGACAGCACCAGCCGATCCTGACTCCG
GGGCATTCGCAGCCGATCCCGACTCCGGGGCAGCCCCTGCCGCCCCAGCCGATCCCGACT
CCGGGGCGGCCCCTGACGCCCCAGCCGATCCCGACTCCGGGGCGGCCCCTGACGCCCCAG
CCGATCCAGATGCCGGGGCGGCCCCTGAGGCTCCCGCCGCCCCTGCGGCTGCTGAGACCC
GGGCAGCCCATGTCGCCCCAGCTGCGCCAGACGCAGGGGCTCCCACTGCCCCAGCCGCTT
CTGCCACCCGGGCAGCCCAAGTCCGCCGGGCGGCCTCTGCAGCCCCTGCCTCCGGGGCCA
GACGCAAGATCCATCTCAGACCCCCCAGCCCCGAGATCCAGGCTGCCGATCCGCCTACTC
CGCGGCCTACTCGCGCGTCTGCCTGGCGGGGCAAGTCCGAGAGCAGCCGCGGCCGCCGCG
TGTACTACGATGAAGGGGTGGCCAGCAGCGACGATGACTCCAGCGGAGACGAGTCCGACG
ATGGGACCTCCGGATGCCTCCGCTGGTTTCAGCATCGGCGAAATCGCCGCCGCCGAAAGC
CCCAGCGCAACTTACTCCGCAACTTTCTCGTGCAAGCCTTCGGGGGCTGCTTCGGTCGAT
CTGAGAGTCCCCAGCCCAAAGCCTCGCGCTCTCTCAAGGTCAAGAAGGTACCCCTGGCGG
AGAAGCGCAGACAGATGCGCAAAGAAGCCCTGGAGAAGCGGGCCCAGAAGCGCGCAGAGA
AGAAACGCAGTAAGCTCATCGACAAACAACTCCAGGACGAAAAGATGGGCTACATGTGTA
CGCACCGCCTGCTGCTTCTAG
Enzyme 108 GenBank Gene ID NM_001077490.1 Link Image
Enzyme 108 GeneCard ID GNAS Link Image
Enzyme 108 GenAtlas ID GNAS Link Image
Enzyme 108 HGNC ID HGNC:4392 Link Image
Enzyme 108 Chromosome Location 2
Enzyme 108 Locus 20q13.3
Enzyme 108 SNPs SNPJam Report Link Image
Enzyme 108 General References
  1. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  2. Freson K, Jaeken J, Van Helvoirt M, de Zegher F, Wittevrongel C, Thys C, Hoylaerts MF, Vermylen J, Van Geet C: Functional polymorphisms in the paternally expressed XLalphas and its cofactor ALEX decrease their mutual interaction and enhance receptor-mediated cAMP formation. Hum Mol Genet. 2003 May 15;12(10):1121-30. [PubMed Link Image]
  3. Abramowitz J, Grenet D, Birnbaumer M, Torres HN, Birnbaumer L: XLalphas, the extra-long form of the alpha-subunit of the Gs G protein, is significantly longer than suspected, and so is its companion Alex. Proc Natl Acad Sci U S A. 2004 Jun 1;101(22):8366-71. Epub 2004 May 17. [PubMed Link Image]
  4. Liu J, Litman D, Rosenberg MJ, Yu S, Biesecker LG, Weinstein LS: A GNAS1 imprinting defect in pseudohypoparathyroidism type IB. J Clin Invest. 2000 Nov;106(9):1167-74. [PubMed Link Image]
  5. Bastepe M, Lane AH, Juppner H: Paternal uniparental isodisomy of chromosome 20q--and the resulting changes in GNAS1 methylation--as a plausible cause of pseudohypoparathyroidism. Am J Hum Genet. 2001 May;68(5):1283-9. Epub 2001 Apr 9. [PubMed Link Image]
  6. Wu WI, Schwindinger WF, Aparicio LF, Levine MA: Selective resistance to parathyroid hormone caused by a novel uncoupling mutation in the carboxyl terminus of G alpha(s). A cause of pseudohypoparathyroidism type Ib. J Biol Chem. 2001 Jan 5;276(1):165-71. [PubMed Link Image]
  7. Jan de Beur S, Ding C, Germain-Lee E, Cho J, Maret A, Levine MA: Discordance between genetic and epigenetic defects in pseudohypoparathyroidism type 1b revealed by inconsistent loss of maternal imprinting at GNAS1. Am J Hum Genet. 2003 Aug;73(2):314-22. Epub 2003 Jul 11. [PubMed Link Image]
  8. Fragoso MC, Domenice S, Latronico AC, Martin RM, Pereira MA, Zerbini MC, Lucon AM, Mendonca BB: Cushing's syndrome secondary to adrenocorticotropin-independent macronodular adrenocortical hyperplasia due to activating mutations of GNAS1 gene. J Clin Endocrinol Metab. 2003 May;88(5):2147-51. [PubMed Link Image]
  9. Bastepe M, Frohlich LF, Hendy GN, Indridason OS, Josse RG, Koshiyama H, Korkko J, Nakamoto JM, Rosenbloom AL, Slyper AH, Sugimoto T, Tsatsoulis A, Crawford JD, Juppner H: Autosomal dominant pseudohypoparathyroidism type Ib is associated with a heterozygous microdeletion that likely disrupts a putative imprinting control element of GNAS. J Clin Invest. 2003 Oct;112(8):1255-63. [PubMed Link Image]
  10. Linglart A, Gensure RC, Olney RC, Juppner H, Bastepe M: A novel STX16 deletion in autosomal dominant pseudohypoparathyroidism type Ib redefines the boundaries of a cis-acting imprinting control element of GNAS. Am J Hum Genet. 2005 May;76(5):804-14. Epub 2005 Mar 30. [PubMed Link Image]
  11. Bastepe M, Frohlich LF, Linglart A, Abu-Zahra HS, Tojo K, Ward LM, Juppner H: Deletion of the NESP55 differentially methylated region causes loss of maternal GNAS imprints and pseudohypoparathyroidism type Ib. Nat Genet. 2005 Jan;37(1):25-7. Epub 2004 Dec 12. [PubMed Link Image]
  12. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 108 Metabolite References Not Available
Enzyme 109 [top]
Enzyme 109 ID 8268
Enzyme 109 Name Rap guanine nucleotide exchange factor 3
Enzyme 109 Synonyms
  1. Exchange factor directly activated by cAMP 1
  2. Exchange protein directly activated by cAMP 1
  3. EPAC 1
  4. Rap1 guanine-nucleotide-exchange factor directly activated by cAMP
  5. cAMP-regulated guanine nucleotide exchange factor I
  6. cAMP-GEFI
Enzyme 109 Gene Name RAPGEF3
Enzyme 109 Protein Sequence >Rap guanine nucleotide exchange factor 3
MKVGWPGESCWQVGLAVEDSPALGAPRVGALPDVVPEGTLLNMVLRRMHRPRSCSYQLLL
EHQRPSCIQGLRWTPLTNSEESLDFSESLEQASTERVLRAGRQLHRHLLATCPNLIRDRK
YHLRLYRQCCSGRELVDGILALGLGVHSRSQVVGICQVLLDEGALCHVKHDWAFQDRDAQ
FYRFPGPEPEPVGTHEMEEELAEAVALLSQRGPDALLTVALRKPPGQRTDEELDLIFEEL
LHIKAVAHLSNSVKRELAAVLLFEPHSKAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKGL
VTTLHEGDDFGQLALVNDAPRAATIILREDNCHFLRVDKQDFNRIIKDVEAKTMRLEEHG
KVVLVLERASQGAGPSRPPTPGRNRYTVMSGTPEKILELLLEAMGPDSSAHDPTETFLSD
FLLTHRVFMPSAQLCAALLHHFHVEPAGGSEQERSTYVCNKRQQILRLVSQWVALYGSML
HTDPVATSFLQKLSDLVGRDTRLSNLLREQWPERRRCHRLENGCGNASPQMKARNLPVWL
PNQDEPLPGSSCAIQVGDKVPYDICRPDHSVLTLQLPVTASVREVMAALAQEDGWTKGQV
LVKVNSAGDAIGLQPDARGVATSLGLNERLFVVNPQEVHELIPHPDQLGPTVGSAEGLDL
VSAKDLAGQLTDHDWSLFNSIHQVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVAT
ELCLCPVPGPRAQLLRKFIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKV
RKLYSALERLLDPSWNHRVYRLALAKLSPPVIPFMPLLLKDMTFIHEGNHTLVENLINFE
KMRMMARAARMLHHCRSHNPVPLSPLRSRVSHLHEDSQVARISTCSEQSLSTRSPASTWA
YVQQLKVIDNQRELSRLSRELEP
Enzyme 109 Number of Residues 923
Enzyme 109 Molecular Weight 103651.0
Enzyme 109 Theoretical pI 7.49
Enzyme 109 GO Classification
Function
  • GTPase regulator activity
  • cAMP-dependent protein kinase regulator activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • kinase regulator activity
  • nucleoside-triphosphatase regulator activity
  • protein kinase regulator activity
Process
  • biological regulation
  • intracellular signal transduction
  • intracellular signaling pathway
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular metabolic process
  • regulation of cellular process
  • regulation of cellular protein metabolic process
  • regulation of metabolic process
  • regulation of protein amino acid phosphorylation
  • regulation of protein modification process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • signaling
  • signaling pathway
  • small GTPase mediated signal transduction
Component
  • cAMP-dependent protein kinase complex
  • cell part
  • intracellular
  • macromolecular complex
  • protein complex
Enzyme 109 General Function Involved in cAMP-dependent protein kinase regulator activity
Enzyme 109 Specific Function Guanine nucleotide exchange factor (GEF) for RAP1A and RAP2A small GTPases that is activated by binding cAMP
Enzyme 109 Pathways Not Available
Enzyme 109 Reactions Not Available
Enzyme 109 Pfam Domain Function
Enzyme 109 Signals
  • None
Enzyme 109 Transmembrane Regions
  • None
Enzyme 109 Essentiality Not Available
Enzyme 109 GenBank ID Protein 148747859 Link Image
Enzyme 109 UniProtKB/Swiss-Prot ID O95398 Link Image
Enzyme 109 UniProtKB/Swiss-Prot Entry Name RPGF3_HUMAN Link Image
Enzyme 109 PDB ID Not Available
Enzyme 109 Cellular Location Not Available
Enzyme 109 Gene Sequence >2772 bp
ATGAAGGTGGGCTGGCCAGGTGAGAGCTGCTGGCAGGTGGGCCTGGCTGTGGAGGATAGC
CCAGCTCTGGGAGCACCGCGGGTGGGAGCCCTCCCTGACGTGGTGCCGGAGGGGACACTA
CTCAACATGGTGTTGAGAAGGATGCACCGGCCCCGAAGCTGCTCCTACCAGCTGCTGCTG
GAGCACCAGCGTCCGAGCTGCATCCAGGGGCTGCGCTGGACACCACTCACCAACAGCGAG
GAGTCCCTGGATTTCAGCGAGAGCCTGGAGCAGGCCTCCACAGAGCGGGTGCTCAGGGCT
GGGAGGCAGCTGCATCGGCATCTGCTGGCCACCTGCCCAAACCTCATCCGAGACCGGAAG
TACCACCTTAGGCTCTATCGGCAGTGCTGCTCTGGCCGGGAGCTGGTGGATGGGATCTTG
GCCCTGGGACTTGGGGTCCATTCCCGGAGCCAAGTTGTGGGAATCTGCCAGGTGCTGCTG
GATGAAGGTGCCCTCTGCCATGTGAAACACGACTGGGCCTTCCAGGACCGAGATGCCCAA
TTCTACCGGTTCCCCGGGCCCGAGCCCGAGCCCGTGGGAACTCATGAGATGGAGGAGGAG
TTGGCCGAAGCTGTGGCCCTGCTCTCCCAGCGGGGGCCTGACGCCCTGCTCACTGTGGCA
CTTCGAAAGCCCCCAGGTCAGCGCACGGATGAAGAGCTGGACCTCATCTTTGAGGAGCTG
CTGCACATCAAGGCTGTGGCCCACCTCTCCAACTCGGTGAAGCGAGAATTAGCGGCTGTT
CTGCTCTTTGAACCACACAGCAAGGCAGGGACCGTGTTGTTCAGCCAGGGGGACAAGGGC
ACTTCGTGGTACATTATCTGGAAGGGATCTGTCAACGTGGTGACCCATGGCAAGGGGCTG
GTGACCACCCTGCATGAGGGAGATGATTTTGGACAGCTGGCTCTGGTGAATGATGCACCC
CGGGCAGCCACCATCATCCTGCGAGAAGACAACTGTCATTTCCTGCGTGTGGACAAGCAG
GACTTCAACCGTATCATCAAGGATGTGGAGGCAAAGACCATGCGGCTGGAAGAACATGGC
AAAGTGGTGCTGGTGCTGGAGAGAGCCTCTCAGGGCGCCGGCCCTTCCCGACCCCCAACC
CCAGGCAGGAACCGGTATACAGTGATGTCTGGCACCCCAGAGAAGATCCTAGAGCTTCTG
TTGGAGGCCATGGGACCAGATTCCAGTGCTCATGACCCAACAGAGACATTCCTCAGCGAC
TTCCTCCTGACCCACAGGGTCTTCATGCCCAGCGCCCAACTCTGCGCTGCCCTTCTGCAC
CACTTCCATGTGGAGCCTGCGGGTGGCAGCGAGCAGGAGCGCAGCACCTACGTCTGCAAC
AAGAGGCAGCAGATCTTGCGGCTGGTCAGCCAGTGGGTGGCCCTGTATGGCTCCATGCTC
CACACTGACCCTGTGGCCACCAGCTTCCTCCAGAAACTCTCAGACCTGGTGGGCAGGGAC
ACCCGACTCAGCAACCTGCTGAGGGAGCAGTGGCCAGAGAGGCGGCGATGCCACAGGTTG
GAGAATGGCTGTGGGAATGCATCTCCTCAGATGAAGGCCCGGAACTTGCCTGTTTGGCTC
CCCAACCAGGACGAGCCCCTTCCTGGCAGCAGCTGTGCCATCCAAGTTGGGGATAAAGTC
CCCTATGACATCTGCCGGCCAGACCACTCAGTGTTGACCCTGCAGCTGCCTGTGACAGCC
TCCGTGAGAGAGGTGATGGCAGCGTTGGCCCAGGAGGATGGCTGGACCAAGGGGCAGGTG
CTGGTGAAGGTCAATTCTGCAGGTGATGCCATTGGCCTGCAGCCAGATGCCCGTGGTGTG
GCCACATCTCTGGGGCTCAATGAGCGTCTCTTTGTTGTCAACCCACAGGAAGTGCATGAG
CTGATCCCACACCCTGACCAGCTGGGGCCCACTGTGGGCTCTGCTGAGGGGCTGGACCTG
GTGAGTGCCAAGGACCTGGCAGGCCAGCTGACGGACCACGACTGGAGCCTCTTCAACAGT
ATCCACCAGGTGGAGCTGATCCACTATGTGCTGGGCCCCCAGCATCTGCGGGATGTCACC
ACCGCCAACCTGGAGCGCTTCATGCGCCGCTTCAATGAGCTGCAGTACTGGGTGGCCACC
GAGCTGTGTCTCTGCCCCGTGCCCGGCCCCCGGGCCCAGCTGCTCAGGAAGTTCATTAAG
CTGGCGGCCCACCTCAAGGAGCAGAAGAATCTCAATTCCTTCTTTGCCGTCATGTTTGGC
CTCAGCAACTCGGCCATCAGCCGCCTAGCCCACACCTGGGAGCGGCTGCCTCACAAAGTC
CGGAAGCTGTACTCCGCCCTCGAGAGGCTGCTGGATCCCTCATGGAACCACCGGGTATAC
CGACTGGCCCTCGCCAAGCTCTCCCCTCCTGTCATCCCCTTCATGCCCCTTCTTCTCAAA
GACATGACCTTCATTCATGAGGGAAACCACACACTAGTGGAGAATCTCATCAACTTTGAG
AAGATGAGAATGATGGCCAGAGCCGCGCGGATGCTGCACCACTGCCGAAGCCACAACCCT
GTGCCTCTCTCACCACTCAGAAGCCGAGTTTCCCACCTCCACGAGGACAGCCAGGTGGCG
AGGATTTCCACATGCTCGGAGCAGTCCCTGAGCACCCGGAGTCCAGCCAGCACCTGGGCT
TATGTCCAGCAGCTGAAGGTCATTGACAACCAGCGGGAACTCTCCCGCCTCTCCCGAGAG
CTGGAGCCATGA
Enzyme 109 GenBank Gene ID NM_001098531.2 Link Image
Enzyme 109 GeneCard ID RAPGEF3 Link Image
Enzyme 109 GenAtlas ID RAPGEF3 Link Image
Enzyme 109 HGNC ID HGNC:16629 Link Image
Enzyme 109 Chromosome Location 1
Enzyme 109 Locus 12q13.1
Enzyme 109 SNPs SNPJam Report Link Image
Enzyme 109 General References
  1. Kawasaki H, Springett GM, Mochizuki N, Toki S, Nakaya M, Matsuda M, Housman DE, Graybiel AM: A family of cAMP-binding proteins that directly activate Rap1. Science. 1998 Dec 18;282(5397):2275-9. [PubMed Link Image]
  2. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. de Rooij J, Zwartkruis FJ, Verheijen MH, Cool RH, Nijman SM, Wittinghofer A, Bos JL: Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP. Nature. 1998 Dec 3;396(6710):474-7. [PubMed Link Image]
  5. de Rooij J, Rehmann H, van Triest M, Cool RH, Wittinghofer A, Bos JL: Mechanism of regulation of the Epac family of cAMP-dependent RapGEFs. J Biol Chem. 2000 Jul 7;275(27):20829-36. [PubMed Link Image]
  6. Rehmann H, Prakash B, Wolf E, Rueppel A, de Rooij J, Bos JL, Wittinghofer A: Structure and regulation of the cAMP-binding domains of Epac2. Nat Struct Biol. 2003 Jan;10(1):26-32. [PubMed Link Image]
Enzyme 109 Metabolite References Not Available
Enzyme 110 [top]
Enzyme 110 ID 8354
Enzyme 110 Name Lysophosphatidic acid receptor 2
Enzyme 110 Synonyms
  1. LPA receptor 2
  2. LPA-2
  3. Lysophosphatidic acid receptor Edg-4
Enzyme 110 Gene Name LPAR2
Enzyme 110 Protein Sequence >Lysophosphatidic acid receptor 2
MVIMGQCYYNETIGFFYNNSGKELSSHWRPKDVVVVALGLTVSVLVLLTNLLVIAAIASN
RRFHQPIYYLLGNLAAADLFAGVAYLFLMFHTGPRTARLSLEGWFLRQGLLDTSLTASVA
TLLAIAVERHRSVMAVQLHSRLPRGRVVMLIVGVWVAALGLGLLPAHSWHCLCALDRCSR
MAPLLSRSYLAVWALSSLLVFLLMVAVYTRIFFYVRRRVQRMAEHVSCHPRYRETTLSLV
KTVVIILGAFVVCWTPGQVVLLLDGLGCESCNVLAVEKYFLLLAEANSLVNAAVYSCRDA
EMRRTFRRLLCCACLRQSTRESVHYTSSAQGGASTRIMLPENGHPLMDSTL
Enzyme 110 Number of Residues 351
Enzyme 110 Molecular Weight 39083.8
Enzyme 110 Theoretical pI 9.42
Enzyme 110 GO Classification
Function
  • G-protein coupled receptor activity
  • bioactive lipid receptor activity
  • lysosphingolipid and lysophosphatidic acid receptor activity
  • molecular transducer activity
  • receptor activity
  • signal transducer activity
  • transmembrane receptor activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 110 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 110 Specific Function Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. Seems to be coupled to the G(i)/G(o), G(12)/G(13), and G(q) families of heteromeric G proteins. Plays a key role in phospholipase C-beta (PLC-beta) signaling pathway. Stimulates phospholipase C (PLC) activity in a manner that is independent of RALA activation
Enzyme 110 Pathways Not Available
Enzyme 110 Reactions Not Available
Enzyme 110 Pfam Domain Function
Enzyme 110 Signals
  • None
Enzyme 110 Transmembrane Regions
  • 34-54 70-90 104-126 147-167 189-209 243-263 280-297
Enzyme 110 Essentiality Not Available
Enzyme 110 GenBank ID Protein 2213635 Link Image
Enzyme 110 UniProtKB/Swiss-Prot ID Q9HBW0 Link Image
Enzyme 110 UniProtKB/Swiss-Prot Entry Name LPAR2_HUMAN Link Image
Enzyme 110 PDB ID Not Available
Enzyme 110 Cellular Location Not Available
Enzyme 110 Gene Sequence >1056 bp
ATGGTCATCATGGGCCAGTGCTACTACAACGAGACCATCGGCTTCTTCTATAACAACAGT
GGCAAAGAGCTCAGCTCCCACTGGCGGCCCAAGGATGTGGTCGTGGTGGCACTGGGGCTG
ACCGTCAGCGTGCTGGTGCTGCTGACCAATCTGCTGGTCATAGCAGCCATCGCCTCCAAC
CGCCGCTTCCACCAGCCCATCTACTACCTGCTCGGCAATCTGGCCGCGGCTGACCTCTTC
GCGGGCGTGGCCTACCTCTTCCTCATGTTCCACACTGGTCCCCGCACAGCCCGACTTTCA
CTTGAGGGCTGGTTCCTGCGGCAGGGCTTGCTGGACACAAGCCTCACTGCGTCGGTGGCC
ACACTGCTGGCCATCGCCGTGGAGCGGCACCGCAGTGTGATGGCCGTGCAGCTGCACAGC
CGCCTGCCCCGTGGCCGCGTGGTCATGCTCATTGTGGGCGTGTGGGTGGCTGCCCTGGGC
CTGGGGCTGCTGCCTGCCCACTCCTGGCACTGCCTCTGTGCCCTGGACCGCTGCTCACGC
ATGGCACCCCTGCTCAGCCGCTCCTATTTGGCCGTCTGGGCTCTGTCGAGCCTGCTTGTC
TTCCTGCTCATGGTGGCTGTGTACACCCGCATTTTCTTCTACGTGCGGCGGCGAGTGCAG
CGCATGGCAGAGCATGTCAGCTGCCACCCCCGCTACCGAGAGACCACGCTCAGCCTGGTC
AAGACTGTTGTCATCATCCTGGGGGCGTTCGTGGTCTGCTGGACACCAGGCCAGGTGGTA
CTGCTCCTGGATGGTTTAGGCTGTGAGTCCTGCAATGTCCTGGCTGTAGAAAAGTACTTC
CTACTGTTGGCCGAGGCCAACTCACTGGTCAATGCTGCTGTGTACTCTTGCCGAGATGCT
GAGATGCGCCGCACCTTCCGCCGCCTTCTCTGCTGCGCGTGCCTCCGCCAGTCCACCCGC
GAGTCTGTCCACTATACATCCTCTGCCCAGGGAGGTGCCAGCACTCGCATCATGCTTCCC
GAGAACGGCCACCCACTGATGGACTCCACCCTTTAG
Enzyme 110 GenBank Gene ID AC002306 Link Image
Enzyme 110 GeneCard ID LPAR2 Link Image
Enzyme 110 GenAtlas ID LPAR2 Link Image
Enzyme 110 HGNC ID HGNC:3168 Link Image
Enzyme 110 Chromosome Location 1
Enzyme 110 Locus 19p12
Enzyme 110 SNPs SNPJam Report Link Image
Enzyme 110 General References
  1. An S, Bleu T, Hallmark OG, Goetzl EJ: Characterization of a novel subtype of human G protein-coupled receptor for lysophosphatidic acid. J Biol Chem. 1998 Apr 3;273(14):7906-10. [PubMed Link Image]
  2. Bandoh K, Aoki J, Taira A, Tsujimoto M, Arai H, Inoue K: Lysophosphatidic acid (LPA) receptors of the EDG family are differentially activated by LPA species. Structure-activity relationship of cloned LPA receptors. FEBS Lett. 2000 Jul 28;478(1-2):159-65. [PubMed Link Image]
  3. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Contos JJ, Ishii I, Chun J: Lysophosphatidic acid receptors. Mol Pharmacol. 2000 Dec;58(6):1188-96. [PubMed Link Image]
  6. Contos JJ, Chun J: Genomic characterization of the lysophosphatidic acid receptor gene, lp(A2)/Edg4, and identification of a frameshift mutation in a previously characterized cDNA. Genomics. 2000 Mar 1;64(2):155-69. [PubMed Link Image]
  7. Oh YS, Jo NW, Choi JW, Kim HS, Seo SW, Kang KO, Hwang JI, Heo K, Kim SH, Kim YH, Kim IH, Kim JH, Banno Y, Ryu SH, Suh PG: NHERF2 specifically interacts with LPA2 receptor and defines the specificity and efficiency of receptor-mediated phospholipase C-beta3 activation. Mol Cell Biol. 2004 Jun;24(11):5069-79. [PubMed Link Image]
  8. Zhang H, Wang D, Sun H, Hall RA, Yun CC: MAGI-3 regulates LPA-induced activation of Erk and RhoA. Cell Signal. 2007 Feb;19(2):261-8. Epub 2006 Aug 9. [PubMed Link Image]
  9. Aziziyeh AI, Li TT, Pape C, Pampillo M, Chidiac P, Possmayer F, Babwah AV, Bhattacharya M: Dual regulation of lysophosphatidic acid (LPA1) receptor signalling by Ral and GRK. Cell Signal. 2009 Jul;21(7):1207-17. Epub 2009 Mar 21. [PubMed Link Image]
Enzyme 110 Metabolite References Not Available
Enzyme 111 [top]
Enzyme 111 ID 8364
Enzyme 111 Name Rho-related GTP-binding protein Rho6
Enzyme 111 Synonyms
  1. Rho family GTPase 1
  2. Rnd1
Enzyme 111 Gene Name RND1
Enzyme 111 Protein Sequence >Rho-related GTP-binding protein Rho6
MKERRAPQPVVARCKLVLVGDVQCGKTAMLQVLAKDCYPETYVPTVFENYTACLETEEQR
VELSLWDTSGSPYYDNVRPLCYSDSDAVLLCFDISRPETVDSALKKWRTEILDYCPSTRV
LLIGCKTDLRTDLSTLMELSHQKQAPISYEQGCAIAKQLGAEIYLEGSAFTSEKSIHSIF
RTASMLCLNKPSPLPQKSPVRSLSKRLLHLPSRSELISSTFKKEKAKSCSIM
Enzyme 111 Number of Residues 232
Enzyme 111 Molecular Weight 26055.8
Enzyme 111 Theoretical pI 8.03
Enzyme 111 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 111 General Function Involved in GTP binding
Enzyme 111 Specific Function Lacks intrinsic GTPase activity. Has a low affinity for GDP, and constitutively binds GTP. Controls rearrangements of the actin cytoskeleton. Induces the Rac-dependent neuritic process formation in part by disruption of the cortical actin filaments. Causes the formation of many neuritic processes from the cell body with disruption of the cortical actin filaments
Enzyme 111 Pathways Not Available
Enzyme 111 Reactions Not Available
Enzyme 111 Pfam Domain Function
Enzyme 111 Signals
  • None
Enzyme 111 Transmembrane Regions
  • None
Enzyme 111 Essentiality Not Available
Enzyme 111 GenBank ID Protein 1546902 Link Image
Enzyme 111 UniProtKB/Swiss-Prot ID Q92730 Link Image
Enzyme 111 UniProtKB/Swiss-Prot Entry Name RND1_HUMAN Link Image
Enzyme 111 PDB ID Not Available
Enzyme 111 Cellular Location Not Available
Enzyme 111 Gene Sequence >699 bp
ATGAAGGAGAGACGGGCCCCCCAGCCAGTCGTGGCCAGATGTAAGCTCGTTCTGGTCGGG
GACGTGCAGTGTGGGAAGACCGCGATGTTGCAAGTGTTAGCGAAGGATTGCTATCCAGAG
ACCTATGTGCCCACCGTGTTCGAAAATTACACAGCCTGTTTGGAGACAGAGGAACAGAGG
GTGGAGCTTAGTCTCTGGGATACCTCAGGATCTCCCTACTACGATAATGTCCGTCCACTC
TGCTACAGCGACTCGGATGCAGTATTACTATGTTTTGACATCAGCCGTCCAGAGACAGTG
GACAGCGCACTGAAGAAGTGGAGGACAGAAATCCTAGATTATTGTCCCAGCACCCGCGTT
TTGCTCATTGGCTGCAAGACAGACCTGCGAACAGACCTGAGTACTCTGATGGAGCTGTCC
CACCAGAAGCAGGCGCCCATCTCCTATGAGCAGGGTTGTGCAATAGCAAAGCAGCTGGGT
GCAGAAATCTACCTGGAAGGCTCAGCTTTCACCTCAGAAAAGAGCATCCACAGCATCTTT
CGGACGGCATCCATGCTGTGTCTGAACAAGCCTAGCCCACTGCCCCAGAAGAGCCCTGTC
CGAAGCCTCTCCAAACGACTGCTCCACCTCCCCAGTCGCTCTGAACTCATCTCTTCTACC
TTCAAGAAGGAAAAGGCCAAAAGCTGTTCCATTATGTGA
Enzyme 111 GenBank Gene ID Y07923 Link Image
Enzyme 111 GeneCard ID RND1 Link Image
Enzyme 111 GenAtlas ID RND1 Link Image
Enzyme 111 HGNC ID HGNC:18314 Link Image
Enzyme 111 Chromosome Location 1
Enzyme 111 Locus 12q12
Enzyme 111 SNPs SNPJam Report Link Image
Enzyme 111 General References
  1. Nobes CD, Lauritzen I, Mattei MG, Paris S, Hall A, Chardin P: A new member of the Rho family, Rnd1, promotes disassembly of actin filament structures and loss of cell adhesion. J Cell Biol. 1998 Apr 6;141(1):187-97. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Aoki J, Katoh H, Mori K, Negishi M: Rnd1, a novel rho family GTPase, induces the formation of neuritic processes in PC12 cells. Biochem Biophys Res Commun. 2000 Nov 30;278(3):604-8. [PubMed Link Image]
  5. Vayssiere B, Zalcman G, Mahe Y, Mirey G, Ligensa T, Weidner KM, Chardin P, Camonis J: Interaction of the Grb7 adapter protein with Rnd1, a new member of the Rho family. FEBS Lett. 2000 Feb 4;467(1):91-6. [PubMed Link Image]
  6. Katoh H, Harada A, Mori K, Negishi M: Socius is a novel Rnd GTPase-interacting protein involved in disassembly of actin stress fibers. Mol Cell Biol. 2002 May;22(9):2952-64. [PubMed Link Image]
  7. Oinuma I, Katoh H, Harada A, Negishi M: Direct interaction of Rnd1 with Plexin-B1 regulates PDZ-RhoGEF-mediated Rho activation by Plexin-B1 and induces cell contraction in COS-7 cells. J Biol Chem. 2003 Jul 11;278(28):25671-7. Epub 2003 May 1. [PubMed Link Image]
Enzyme 111 Metabolite References Not Available
Enzyme 112 [top]
Enzyme 112 ID 8421
Enzyme 112 Name Selenocysteine-specific elongation factor
Enzyme 112 Synonyms
  1. Elongation factor sec
  2. Eukaryotic elongation factor, selenocysteine-tRNA-specific
Enzyme 112 Gene Name EEFSEC
Enzyme 112 Protein Sequence >Selenocysteine-specific elongation factor
MAGRRVNVNVGVLGHIDSGKTALARALSTTASTAAFDKQPQSRERGITLDLGFSCFSVPL
PARLRSSLPEFQAAPEAEPEPGEPLLQVTLVDCPGHASLIRTIIGGAQIIDLMMLVIDVT
KGMQTQSAECLVIGQIACQKLVVVLNKIDLLPEGKRQAAIDKMTKKMQKTLENTKFRGAP
IIPVAAKPGGPEAPETEAPQGIPELIELLTSQISIPTRDPSGPFLMSVDHCFSIKGQGTV
MTGTILSGSISLGDSVEIPALKVVKKVKSMQMFHMPITSAMQGDRLGICVTQFDPKLLER
GLVCAPESLHTVHAALISVEKIPYFRGPLQTKAKFHITVGHETVMGRLMFFSPAPDNFDQ
EPILDSFNFSQEYLFQEQYLSKDLTPAVTDNDEADKKAGQATEGHCPRQQWALVEFEKPV
TCPRLCLVIGSRLDADIHTNTCRLAFHGILLHGLEDRNYADSFLPRLKVYKLKHKHGLVE
RAMDDYSVIGRSLFKKETNIQLFVGLKVHLSTGELGIIDSAFGQSGKFKIHIPGGLSPES
KKILTPALKKRARAGRGEATRQEESAERSEPSQHVVLSLTFKRYVFDTHKRMVQSP
Enzyme 112 Number of Residues 596
Enzyme 112 Molecular Weight 65304.1
Enzyme 112 Theoretical pI 8.48
Enzyme 112 GO Classification
Function
  • GTP binding
  • GTPase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
Process
Component
Enzyme 112 General Function Involved in GTPase activity
Enzyme 112 Specific Function Translation factor necessary for the incorporation of selenocysteine into proteins. It probably replaces EF-Tu for the insertion of selenocysteine directed by the UGA codon. SelB binds GTP and GDP
Enzyme 112 Pathways Not Available
Enzyme 112 Reactions Not Available
Enzyme 112 Pfam Domain Function
Enzyme 112 Signals
  • None
Enzyme 112 Transmembrane Regions
  • None
Enzyme 112 Essentiality Not Available
Enzyme 112 GenBank ID Protein 54607086 Link Image
Enzyme 112 UniProtKB/Swiss-Prot ID P57772 Link Image
Enzyme 112 UniProtKB/Swiss-Prot Entry Name SELB_HUMAN Link Image
Enzyme 112 PDB ID Not Available
Enzyme 112 Cellular Location Not Available
Enzyme 112 Gene Sequence >1791 bp
ATGGCAGGGCGGCGGGTGAACGTGAACGTGGGCGTGCTGGGCCACATCGACAGCGGCAAG
ACGGCGCTGGCGCGGGCGCTAAGCACCACAGCCTCCACCGCCGCCTTTGACAAGCAGCCG
CAGAGCCGCGAGCGCGGCATCACGCTCGATCTGGGCTTCTCGTGCTTCTCGGTGCCGCTG
CCCGCGCGCCTGCGGTCGTCTTTGCCCGAGTTCCAGGCAGCGCCCGAGGCCGAGCCCGAG
CCCGGCGAGCCACTGCTTCAGGTCACGCTGGTCGACTGCCCCGGGCACGCCTCCCTCATC
CGGACCATCATCGGCGGGGCCCAGATCATTGATCTGATGATGCTGGTCATCGATGTGACC
AAGGGGATGCAGACCCAGTCAGCGGAATGCCTTGTGATCGGCCAGATTGCCTGCCAGAAG
CTGGTCGTGGTGCTGAACAAAATAGACCTCTTACCTGAAGGAAAGAGACAGGCAGCAATT
GATAAAATGACCAAGAAAATGCAGAAGACCCTAGAGAACACCAAGTTCCGAGGTGCACCG
ATTATACCCGTGGCGGCCAAGCCGGGGGGACCAGAGGCCCCCGAAACTGAAGCTCCACAG
GGCATTCCAGAGCTCATTGAGCTCCTGACGTCCCAGATTTCCATCCCAACGAGAGACCCC
TCGGGACCGTTCCTCATGTCTGTGGACCACTGTTTCTCCATCAAAGGCCAAGGCACTGTG
ATGACAGGGACCATCCTTTCAGGCTCCATCAGCCTCGGTGACAGTGTGGAGATCCCTGCC
CTCAAGGTGGTGAAGAAGGTGAAGTCCATGCAGATGTTCCACATGCCCATCACTTCAGCC
ATGCAAGGAGACCGGCTGGGCATCTGCGTCACCCAGTTTGACCCTAAGCTGCTGGAGCGC
GGGTTGGTGTGTGCCCCCGAGTCCCTGCACACTGTCCATGCGGCCCTCATCTCTGTGGAA
AAGATACCGTATTTCCGGGGGCCCCTGCAAACCAAGGCCAAGTTCCACATTACAGTGGGC
CATGAAACAGTCATGGGCCGGTTGATGTTCTTCAGTCCTGCTCCAGATAACTTTGACCAG
GAGCCTATACTGGACTCTTTCAACTTCTCTCAAGAATACCTTTTCCAGGAGCAGTACCTG
TCCAAGGATTTGACACCAGCAGTGACAGACAATGATGAGGCCGACAAGAAGGCCGGCCAG
GCCACAGAGGGCCATTGTCCTCGGCAGCAGTGGGCCCTGGTGGAGTTTGAGAAGCCCGTC
ACCTGCCCTCGGCTGTGCCTGGTGATTGGCTCCAGGCTAGATGCGGACATTCACACCAAC
ACGTGCCGGCTAGCCTTCCATGGCATCCTGCTCCACGGGCTAGAGGACAGGAACTACGCC
GACAGCTTCCTGCCCAGGCTGAAGGTGTACAAGCTGAAGCACAAGCATGGCCTTGTGGAG
CGGGCGATGGATGACTACAGTGTGATCGGCCGCTCCCTGTTCAAAAAGGAAACCAACATC
CAGCTCTTCGTGGGGCTCAAGGTGCACTTGTCCACTGGGGAACTGGGCATCATCGACAGT
GCCTTCGGCCAGAGCGGCAAGTTCAAGATCCACATCCCAGGTGGCCTCAGCCCCGAGTCC
AAGAAGATCCTGACACCCGCCCTCAAGAAGCGGGCCCGGGCTGGCCGTGGGGAGGCCACC
AGGCAGGAGGAGAGCGCCGAGCGGAGCGAGCCCTCACAGCATGTGGTGCTCAGCCTGACT
TTCAAGCGTTATGTCTTCGACACCCACAAGCGCATGGTTCAGTCTCCCTGA
Enzyme 112 GenBank Gene ID NM_021937.3 Link Image
Enzyme 112 GeneCard ID EEFSEC Link Image
Enzyme 112 GenAtlas ID EEFSEC Link Image
Enzyme 112 HGNC ID HGNC:24614 Link Image
Enzyme 112 Chromosome Location 3
Enzyme 112 Locus 3q21.3
Enzyme 112 SNPs SNPJam Report Link Image
Enzyme 112 General References
  1. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  2. Fagegaltier D, Hubert N, Yamada K, Mizutani T, Carbon P, Krol A: Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation. EMBO J. 2000 Sep 1;19(17):4796-805. [PubMed Link Image]
Enzyme 112 Metabolite References Not Available
Enzyme 113 [top]
Enzyme 113 ID 8453
Enzyme 113 Name Rap guanine nucleotide exchange factor 4
Enzyme 113 Synonyms
  1. Exchange factor directly activated by cAMP 2
  2. Exchange protein directly activated by cAMP 2
  3. EPAC 2
  4. cAMP-regulated guanine nucleotide exchange factor II
  5. cAMP-GEFII
Enzyme 113 Gene Name RAPGEF4
Enzyme 113 Protein Sequence >Rap guanine nucleotide exchange factor 4
MVAAHAAHSSSSAEWIACLDKRPLERSSEDVDIIFTRLKEVKAFEKFHPNLLHQICLCGY
YENLEKGITLFRQGDIGTNWYAVLAGSLDVKVSETSSHQDAVTICTLGIGTAFGESILDN
TPRHATIVTRESSELLRIEQKDFKALWEKYRQYMAGLLAPPYGVMETGSNNDRIPDKENT
PLIEPHVPLRPANTITKVPSEKILRAGKILRNAILSRAPHMIRDRKYHLKTYRQCCVGTE
LVDWMMQQTPCVHSRTQAVGMWQVLLEDGVLNHVDQEHHFQDKYLFYRFLDDEHEDAPLP
TEEEKKECDEELQDTMLLLSQMGPDAHMRMILRKPPGQRTVDDLEIIYEELLHIKALSHL
STTVKRELAGVLIFESHAKGGTVLFNQGEEGTSWYIILKGSVNVVIYGKGVVCTLHEGDD
FGKLALVNDAPRAASIVLREDNCHFLRVDKEDFNRILRDVEANTVRLKEHDQDVLVLEKV
PAGNRASNQGNSQPQQKYTVMSGTPEKILEHFLETIRLEATLNEATDSVLNDFIMMHCVF
MPNTQLCPALVAHYHAQPSQGTEQEKMDYALNNKRRVIRLVLQWAAMYGDLLQEDDVSMA
FLEEFYVSVSDDARMIAALKEQLPELEKIVKQISEDAKAPQKKHKVLLQQFNTGDERAQK
RQPIRGSDEVLFKVYCMDHTYTTIRVPVATSVKEVISAVADKLGSGEGLIIVKMSSGGEK
VVLKPNDVSVFTTLTINGRLFACPREQFDSLTPLPEQEGPTVGTVGTFELMSSKDLAYQM
TIYDWELFNCVHELELIYHTFGRHNFKKTTANLDLFLRRFNEIQFWVVTEICLCSQLSKR
VQLLKKFIKIAAHCKEYKNLNSFFAIVMGLSNVAVSRLALTWEKLPSKFKKFYAEFESLM
DPSRNHRAYRLTVAKLEPPLIPFMPLLIKDMTFTHEGNKTFIDNLVNFEKMRMIANTART
VRYYRSQPFNPDAAQANKNHQDVRSYVRQLNVIDNQRTLSQMSHRLEPRRP
Enzyme 113 Number of Residues 1011
Enzyme 113 Molecular Weight 115520.7
Enzyme 113 Theoretical pI 6.83
Enzyme 113 GO Classification
Function
  • GTPase regulator activity
  • cAMP-dependent protein kinase regulator activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • kinase regulator activity
  • nucleoside-triphosphatase regulator activity
  • protein kinase regulator activity
Process
  • biological regulation
  • intracellular signal transduction
  • intracellular signaling pathway
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular metabolic process
  • regulation of cellular process
  • regulation of cellular protein metabolic process
  • regulation of metabolic process
  • regulation of protein amino acid phosphorylation
  • regulation of protein modification process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • signaling
  • signaling pathway
  • small GTPase mediated signal transduction
Component
  • cAMP-dependent protein kinase complex
  • cell part
  • intracellular
  • macromolecular complex
  • protein complex
Enzyme 113 General Function Involved in cAMP-dependent protein kinase regulator activity
Enzyme 113 Specific Function Guanine nucleotide exchange factor (GEF) for RAP1A, RAP1B and RAP2A small GTPases that is activated by binding cAMP. Seems not to activate RAB3A. Involved in cAMP-dependent, PKA- independent exocytosis through interaction with RIMS2
Enzyme 113 Pathways Not Available
Enzyme 113 Reactions Not Available
Enzyme 113 Pfam Domain Function
Enzyme 113 Signals
  • None
Enzyme 113 Transmembrane Regions
  • None
Enzyme 113 Essentiality Not Available
Enzyme 113 GenBank ID Protein 17061825 Link Image
Enzyme 113 UniProtKB/Swiss-Prot ID Q8WZA2 Link Image
Enzyme 113 UniProtKB/Swiss-Prot Entry Name RPGF4_HUMAN Link Image
Enzyme 113 PDB ID Not Available
Enzyme 113 Cellular Location Not Available
Enzyme 113 Gene Sequence >3036 bp
ATGGTCGCTGCGCACGCTGCCCATTCTTCCTCCTCTGCCGAGTGGATCGCCTGCCTGGAT
AAAAGACCACTGGAGCGATCCAGCGAAGATGTGGATATAATCTTCACTCGACTGAAAGAA
GTTAAAGCTTTTGAGAAATTTCACCCAAATCTCCTTCATCAGATTTGCTTATGTGGTTAT
TATGAGAATCTGGAAAAGGGAATAACATTATTTCGCCAGGGTGATATTGGAACAAACTGG
TATGCTGTCCTGGCAGGGTCTTTGGATGTTAAAGTATCTGAGACCAGCAGTCACCAGGAT
GCTGTGACCATCTGTACCCTGGGAATTGGGACGGCCTTTGGAGAGTCCATTCTGGACAAC
ACACCCCGCCATGCAACCATCGTTACCAGGGAGAGCAGTGAATTGCTCCGCATCGAGCAG
AAGGACTTCAAGGCACTATGGGAGAAATATCGACAGTATATGGCAGGACTTCTGGCTCCT
CCTTATGGTGTTATGGAAACGGGCTCTAACAATGACAGGATTCCTGACAAGGAGAACACA
CCTCTCATTGAACCTCACGTTCCTCTTCGTCCTGCTAACACCATTACCAAGGTCCCTTCA
GAGAAGATCCTCAGAGCTGGAAAAATTTTACGAAATGCCATTCTCTCTCGAGCACCTCAC
ATGATAAGAGATAGAAAATACCACCTAAAGACATACAGACAATGCTGTGTGGGAACTGAA
CTGGTGGACTGGATGATGCAGCAGACACCATGTGTTCACTCCCGGACTCAAGCTGTTGGC
ATGTGGCAAGTCCTGTTAGAAGATGGTGTTCTCAACCACGTGGACCAGGAGCACCATTTC
CAAGACAAATATTTATTCTATCGATTTCTGGATGATGAGCACGAGGATGCCCCTTTGCCT
ACTGAGGAGGAGAAGAAGGAGTGTGATGAGGAGCTCCAGGACACCATGCTGCTGCTGTCA
CAGATGGGCCCCGACGCCCACATGAGGATGATCCTTCGCAAACCACCTGGCCAGAGGACT
GTGGATGACCTAGAGATTATCTATGAGGAGCTTCTTCATATTAAAGCCTTATCCCATCTT
TCTACCACAGTGAAACGAGAGTTAGCAGGTGTTCTCATTTTTGAGTCTCACGCCAAAGGA
GGGACTGTGTTGTTTAACCAGGGGGAAGAAGGTACCTCCTGGTACATTATTCTAAAAGGA
TCAGTGAATGTAGTCATTTACGGCAAGGGTGTGGTCTGCACCCTGCATGAAGGAGATGAC
TTCGGCAAGTTAGCACTAGTGAATGATGCCCCACGAGCTGCCTCTATCGTCTTACGAGAA
GATAACTGCCATTTCTTAAGAGTAGACAAGGAGGATTTCAACCGGATCCTAAGGGACGTG
GAGGCGAATACAGTCAGACTTAAAGAACATGACCAAGATGTCTTGGTGCTGGAGAAGGTC
CCAGCAGGGAACAGAGCTTCTAATCAAGGAAACTCACAGCCTCAGCAAAAGTATACTGTG
ATGTCAGGAACACCTGAAAAAATTTTAGAGCATTTTCTAGAAACAATACGCCTTGAGGCA
ACTTTAAATGAAGCAACAGATTCTGTTTTAAATGACTTTATTATGATGCACTGTGTTTTT
ATGCCAAATACCCAGCTTTGCCCGGCACTGGTGGCCCACTACCACGCACAGCCTTCACAA
GGTACAGAACAGGAGAAAATGGATTATGCCCTCAACAATAAGAGGCGAGTCATCCGCCTG
GTTCTACAGTGGGCTGCCATGTATGGAGACCTCCTGCAAGAGGATGACGTGTCTATGGCC
TTCCTGGAGGAGTTTTATGTATCTGTATCAGATGATGCCCGGATGATTGCTGCCCTCAAG
GAGCAACTGCCAGAGTTGGAGAAGATTGTCAAGCAAATCTCAGAAGATGCAAAGGCACCA
CAAAAGAAGCACAAGGTTCTTTTGCAACAGTTCAATACGGGCGATGAGAGAGCCCAGAAG
CGCCAGCCTATCCGCGGCTCTGATGAAGTTCTGTTTAAGGTCTATTGCATGGACCACACC
TACACAACCATTCGGGTGCCAGTGGCCACTTCGGTGAAGGAAGTCATCAGTGCAGTTGCC
GACAAGCTGGGCTCCGGGGAGGGCCTGATCATAGTCAAGATGAGTTCCGGAGGAGAAAAG
GTGGTGCTCAAACCTAATGATGTTTCAGTATTTACGACGCTCACCATTAATGGACGCCTG
TTTGCTTGCCCGCGAGAGCAATTCGATTCACTGACTCCCTTACCAGAACAGGAAGGCCCA
ACTGTTGGAACAGTGGGAACTTTTGAACTGATGAGCTCCAAAGATTTAGCATACCAGATG
ACAATTTATGATTGGGAACTCTTCAACTGCGTGCATGAGCTGGAGCTAATCTATCACACA
TTTGGAAGGCATAATTTTAAAAAGACCACAGCAAACTTGGATTTGTTCCTGAGGAGATTT
AATGAAATTCAGTTTTGGGTCGTCACTGAGATCTGCCTTTGTTCTCAGCTCAGCAAGCGT
GTTCAGCTATTAAAAAAATTTATTAAGATAGCAGCCCACTGTAAGGAGTATAAAAATCTG
AATTCCTTTTTTGCCATCGTCATGGGACTAAGTAACGTTGCTGTGAGCCGCTTGGCACTA
ACGTGGGAGAAACTGCCAAGCAAGTTCAAGAAGTTCTATGCGGAGTTTGAAAGTTTAATG
GACCCTTCAAGGAACCACAGGGCCTACAGGCTGACAGTAGCTAAGCTGGAACCTCCTCTC
ATCCCCTTCATGCCTTTGCTCATTAAAGATATGACATTTACTCATGAGGGGAACAAGACG
TTCATTGACAATCTAGTAAACTTTGAAAAAATGCGCATGATTGCAAATACGGCCAGAACA
GTGAGATACTACAGGAGCCAACCCTTCAATCCTGATGCAGCTCAAGCTAATAAGAACCAT
CAGGATGTCCGGAGTTATGTACGGCAATTAAATGTGATTGACAACCAGAGAACTTTATCA
CAGATGTCACACAGATTAGAGCCTCGTCGACCATAG
Enzyme 113 GenBank Gene ID AB027471 Link Image
Enzyme 113 GeneCard ID RAPGEF4 Link Image
Enzyme 113 GenAtlas ID RAPGEF4 Link Image
Enzyme 113 HGNC ID HGNC:16626 Link Image
Enzyme 113 Chromosome Location 2
Enzyme 113 Locus 2q31-q32
Enzyme 113 SNPs SNPJam Report Link Image
Enzyme 113 General References
  1. Kawasaki H, Springett GM, Mochizuki N, Toki S, Nakaya M, Matsuda M, Housman DE, Graybiel AM: A family of cAMP-binding proteins that directly activate Rap1. Science. 1998 Dec 18;282(5397):2275-9. [PubMed Link Image]
  2. Ueno H, Shibasaki T, Iwanaga T, Takahashi K, Yokoyama Y, Liu LM, Yokoi N, Ozaki N, Matsukura S, Yano H, Seino S: Characterization of the gene EPAC2: structure, chromosomal localization, tissue expression, and identification of the liver-specific isoform. Genomics. 2001 Nov;78(1-2):91-8. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. de Rooij J, Rehmann H, van Triest M, Cool RH, Wittinghofer A, Bos JL: Mechanism of regulation of the Epac family of cAMP-dependent RapGEFs. J Biol Chem. 2000 Jul 7;275(27):20829-36. [PubMed Link Image]
Enzyme 113 Metabolite References Not Available
Enzyme 114 [top]
Enzyme 114 ID 8457
Enzyme 114 Name Elongation factor 2
Enzyme 114 Synonyms
  1. EF-2
Enzyme 114 Gene Name EEF2
Enzyme 114 Protein Sequence >Elongation factor 2
MVNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTR
KDEQERCITIKSTAISLFYELSENDLNFIKQSKDGAGFLINLIDSPGHVDFSSEVTAALR
VTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQR
IVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKG
EGQLGPAERAKKVEDMMKKLWGDRYFDPANGKFSKSATSPEGKKLPRTFCQLILDPIFKV
FDAIMNFKKEETAKLIEKLDIKLDSEDKDKEGKPLLKAVMRRWLPAGDALLQMITIHLPS
PVTAQKYRCELLYEGPPDDEAAMGIKSCDPKGPLMMYISKMVPTSDKGRFYAFGRVFSGL
VSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLV
KTGTITTFEHAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEE
SGEHIIAGAGELHLEICLKDLEEDHACIPIKKSDPVVSYRETVSEESNVLCLSKSPNKHN
RLYMKARPFPDGLAEDIDKGEVSARQELKQRARYLAEKYEWDVAEARKIWCFGPDGTGPN
ILTDITKGVQYLNEIKDSVVAGFQWATKEGALCEENMRGVRFDVHDVTLHADAIHRGGGQ
IIPTARRCLYASVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVAGTP
MFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDNSSRPSQVVAETRK
RKGLKEGIPALDNFLDKL
Enzyme 114 Number of Residues 858
Enzyme 114 Molecular Weight 95337.4
Enzyme 114 Theoretical pI 6.82
Enzyme 114 GO Classification
Function
  • GTP binding
  • GTPase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
Process
Component
Enzyme 114 General Function Involved in GTPase activity
Enzyme 114 Specific Function This protein promotes the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site of the ribosome
Enzyme 114 Pathways Not Available
Enzyme 114 Reactions Not Available
Enzyme 114 Pfam Domain Function
Enzyme 114 Signals
  • None
Enzyme 114 Transmembrane Regions
  • None
Enzyme 114 Essentiality Not Available
Enzyme 114 GenBank ID Protein 60685056 Link Image
Enzyme 114 UniProtKB/Swiss-Prot ID P13639 Link Image
Enzyme 114 UniProtKB/Swiss-Prot Entry Name EF2_HUMAN Link Image
Enzyme 114 PDB ID Not Available
Enzyme 114 Cellular Location Not Available
Enzyme 114 Gene Sequence >2577 bp
ATGGTGAACTTCACGGTAGACCAGATCCGCGCCATCATGGACAAGAAGGCCAACATCCGC
AACATGTCTGTCATCGCCCACGTGGACCATGGCAAGTCCACGCTGACAGACTCCCTGGTG
TGCAAGGCGGGCATCATCGCCTCGGCCCGGGCCGGGGAGACACGCTTCACTGATACCCGG
AAGGACGAGCAGGAGCGTTGCATCACCATCAAGTCAACTGCCATCTCCCTCTTCTACGAG
CTCTCGGAGAATGACTTGAACTTCATCAAGCAGAGCAAGGACGGTGCCGGCTTCCTCATC
AACCTCATTGACTCCCCCGGGCATGTCGACTTCTCCTCGGAGGTGACTGCTGCCCTCCGA
GTCACCGATGGCGCATTGGTGGTGGTGGACTGCGTGTCAGGCGTGTGCGTGCAGACGGAG
ACAGTGCTGCGGCAGGCCATTGCCGAGCGCATCAAGCCTGTGCTGATGATGAACAAGATG
GACCGCGCCCTGCTGGAGCTGCAGCTGGAGCCCGAGGAGCTCTACCAGACTTTCCAGCGC
ATCGTGGAGAACGTGAACGTCATCATCTCCACCTACGGCGAGGGCGAGAGCGGCCCCATG
GGCAACATCATGATCGATCCTGTCCTCGGTACCGTGGGCTTTGGGTCTGGCCTCCACGGG
TGGGCCTTCACCCTGAAGCAGTTTGCCGAGATGTATGTGGCCAAGTTCGCCGCCAAGGGG
GAGGGCCAGTTGGGGCCTGCCGAGCGGGCCAAGAAAGTAGAGGACATGATGAAGAAGCTG
TGGGGTGACAGGTACTTTGACCCAGCCAACGGCAAGTTCAGCAAGTCAGCCACCAGCCCC
GAAGGGAAGAAGCTGCCACGCACCTTCTGCCAGCTGATCCTGGACCCCATCTTCAAGGTG
TTTGATGCGATCATGAATTTCAAGAAAGAGGAGACAGCAAAACTGATAGAGAAACTGGAC
ATCAAACTGGACAGCGAGGACAAGGACAAAGAAGGCAAACCCCTGCTGAAGGCTGTGATG
CGCCGCTGGCTGCCTGCCGGAGACGCCTTGTTGCAGATGATCACCATCCACCTGCCCTCC
CCTGTGACGGCCCAGAAGTACCGCTGCGAGCTCCTGTACGAGGGGCCCCCGGACGACGAG
GCTGCCATGGGCATTAAAAGCTGTGACCCCAAAGGCCCTCTTATGATGTATATTTCCAAA
ATGGTGCCAACCTCCGACAAAGGTCGGTTCTACGCCTTTGGACGAGTCTTCTCGGGGCTG
GTCTCCACTGGCCTGAAGGTCAGGATCATGGGGCCCAACTATACCCCTGGGAAGAAGGAG
GACCTCTACCTGAAGCCAATCCAGAGAACAATCTTGATGATGGGCCGCTACGTGGAGCCC
ATCGAGGATGTGCCTTGTGGGAACATTGTGGGCCTCGTGGGCGTGGACCAGTTCCTGGTG
AAGACGGGCACCATCACCACCTTCGAGCACGCGCACAACATGCGGGTGATGAAGTTCAGC
GTCAGCCCTGTTGTCAGAGTGGCCGTGGAGGCCAAGAACCCGGCTGACCTGCCCAAGCTG
GTGGAGGGGCTGAAGCGGCTGGCCAAGTCCGACCCCATGGTGCAGTGCATCATCGAGGAG
TCGGGAGAGCATATCATCGCGGGCGCCGGCGAGCTGCACCTGGAGATCTGCCTGAAGGAC
CTGGAGGAGGACCACGCCTGCATCCCCATCAAGAAATCTGACCCGGTCGTCTCGTACCGC
GAGACGGTCAGTGAAGAGTCGAACGTGCTCTGCCTCTCCAAGTCCCCCAACAAGCACAAC
CGGCTGTACATGAAGGCGCGGCCCTTCCCCGACGGCCTGGCCGAGGACATCGATAAAGGC
GAGGTGTCCGCCCGTCAGGAGCTCAAGCAGCGGGCGCGCTACCTGGCCGAGAAGTACGAG
TGGGACGTGGCTGAGGCCCGCAAGATCTGGTGCTTTGGGCCCGACGGCACCGGCCCCAAC
ATCCTCACCGACATCACCAAGGGTGTGCAGTACCTCAACGAGATCAAGGACAGTGTGGTG
GCCGGCTTCCAGTGGGCCACCAAGGAGGGCGCACTGTGTGAGGAGAACATGCGGGGTGTG
CGCTTCGACGTCCACGACGTCACCCTGCACGCCGATGCCATCCACCGCGGAGGGGGCCAG
ATCATCCCCACAGCACGGCGCTGCCTCTATGCCAGTGTGCTGACCGCCCAGCCACGCCTC
ATGGAGCCCATCTACCTTGTGGAGATCCAGTGTCCAGAGCAGGTGGTCGGTGGCATCTAC
GGGGTTTTGAACAGGAAGCGGGGCCACGTGTTCGAGGAGTCCCAGGTGGCCGGCACCCCC
ATGTTTGTGGTCAAGGCCTATCTGCCCGTCAACGAGTCCTTTGGCTTCACCGCTGACCTG
AGGTCCAACACGGGCGGCCAGGCGTTCCCCCAGTGTGTGTTTGACCACTGGCAGATCCTG
CCCGGAGACCCCTTCGACAACAGCAGCCGCCCCAGCCAGGTGGTGGCGGAGACCCGCAAG
CGCAAGGGCCTGAAAGAAGGCATCCCTGCCCTGGACAACTTCCTGGACAAATTGTAG
Enzyme 114 GenBank Gene ID AY942181 Link Image
Enzyme 114 GeneCard ID EEF2 Link Image
Enzyme 114 GenAtlas ID EEF2 Link Image
Enzyme 114 HGNC ID HGNC:3214 Link Image
Enzyme 114 Chromosome Location 1
Enzyme 114 Locus 19pter-q12
Enzyme 114 SNPs SNPJam Report Link Image
Enzyme 114 General References
  1. Rapp G, Klaudiny J, Hagendorff G, Luck MR, Scheit KH: Complete sequence of the coding region of human elongation factor 2 (EF-2) by enzymatic amplification of cDNA from human ovarian granulosa cells. Biol Chem Hoppe Seyler. 1989 Oct;370(10):1071-5. [PubMed Link Image]
  2. Hanes J, Freudenstein J, Rapp G, Scheit KH: Construction of a plasmid containing the complete coding region of human elongation factor 2. Biol Chem Hoppe Seyler. 1992 Apr;373(4):201-4. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Rapp G, Mucha J, Einspanier R, Luck M, Scheit KH: Cloning and sequence analysis of a cDNA from human ovarian granulosa cells encoding the C-terminal part of human elongation factor 2. Biol Chem Hoppe Seyler. 1988 Apr;369(4):247-50. [PubMed Link Image]
  5. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  6. Kim JE, Tannenbaum SR, White FM: Global phosphoproteome of HT-29 human colon adenocarcinoma cells. J Proteome Res. 2005 Jul-Aug;4(4):1339-46. [PubMed Link Image]
  7. Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J: Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC. Proteomics. 2005 Sep;5(14):3589-99. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  9. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  10. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  11. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  12. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  13. Yamashita A, Izumi N, Kashima I, Ohnishi T, Saari B, Katsuhata Y, Muramatsu R, Morita T, Iwamatsu A, Hachiya T, Kurata R, Hirano H, Anderson P, Ohno S: SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate remodeling of the mRNA surveillance complex during nonsense-mediated mRNA decay. Genes Dev. 2009 May 1;23(9):1091-105. [PubMed Link Image]
  14. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 114 Metabolite References Not Available
Enzyme 115 [top]
Enzyme 115 ID 8557
Enzyme 115 Name Succinate-CoA ligase, ADP-forming, beta subunit
Enzyme 115 Synonyms Not Available
Enzyme 115 Gene Name SUCLA2
Enzyme 115 Protein Sequence >Succinate-CoA ligase, ADP-forming, beta subunit
MAASMFYGRLVAVATLRNHRPRTAQRAAAQVLGSSGLFNNHGLQVQQQQQRNLSLHEYMS
MELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVK
IVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGP
VLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENM
VKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDER
DKDAAKANLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEA
FKLITSDKKVLAILVNIFGGIMRCDVIAQGIVMAVKDLEIKIPVVVRLQGTRVDDAKALI
ADSGLKILACDDLDEAARMVVKLSEIVTLAKQAHVDVKFQLPI
Enzyme 115 Number of Residues 463
Enzyme 115 Molecular Weight 50318
Enzyme 115 Theoretical pI 7.50
Enzyme 115 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
Enzyme 115 General Function Energy production and conversion
Enzyme 115 Specific Function Not Available
Enzyme 115 Pathways Not Available
Enzyme 115 Reactions Not Available
Enzyme 115 Pfam Domain Function
Enzyme 115 Signals Not Available
Enzyme 115 Transmembrane Regions Not Available
Enzyme 115 Essentiality Not Available
Enzyme 115 GenBank ID Protein 55957259 Link Image
Enzyme 115 UniProtKB/Swiss-Prot ID Q5T9Q4 Link Image
Enzyme 115 UniProtKB/Swiss-Prot Entry Name Q5T9Q4_HUMAN Link Image
Enzyme 115 PDB ID Not Available
Enzyme 115 Cellular Location Not Available
Enzyme 115 Gene Sequence >1326 bp
ATGGCGGCCTCCATGTTCTACGGCAGGCTAGTGGCCGTGGCCACCCTTCGGAACCACCGG
CCTCGGACGGCCCAGCAACAGCAAAGGAATCTCTCACTACATGAATACATGAGTATGGAA
TTATTGCAAGAAGCTGGTGTCTCCGTTCCCAAAGGATATGTGGCAAAGTCACCAGATGAA
GCTTATGCAATTGCCAAAAAATTAGGTTCAAAAGATGTCGTGATAAAGGCACAGGTTTTA
GCTGGTGGTAGAGGAAAAGGAACATTTGAAAGTGGCCTCAAAGGAGGAGTGAAGATAGTT
TTCTCTCCAGAAGAAGCAAAAGCTGTTTCTTCACAAATGATTGGGAAAAAATTGTTTACC
AAGCAAACGGGAGAAAAGGGCAGAATATGCAATCAAGTATTGGTCTGTGAGCGAAAATAT
CCCAGGAGAGAATACTACTTTGCAATAACAATGGAAAGGTCATTTCAAGGTCCTGTATTA
ATAGGAAGTTCACATGGTGGTGTCAACATTGAAGATGTTGCTGCTGAGTCTCCTGAAGCA
ATAATTAAAGAACCTATTGATATTGAAGAAGGCATCAAAAAGGAACAAGCTCTCCAGCTT
GCACAGAAGATGGGATTTCCACCTAATATTGTGGAATCAGCAGCAGAAAACATGGTCAAG
CTTTACAGCCTTTTTCTGAAATACGATGCAACCATGATAGAAATAAATCCAATGGTGGAA
GATTCAGATGGAGCTGTATTGTGTATGGATGCAAAGATCAATTTTGACTCTAATTCAGCC
TATCGCCAAAAGAAAATCTTTGATCTACAGGACTGGACCCAGGAAGATGAAAGGGACAAA
GATGCTGCTAAGGCAAATCTCAACTACATTGGCCTCGATGGAAATATAGGCTGCCTAGTA
AATGGTGCTGGTTTGGCTATGGCCACAATGGATATAATAAAACTTCATGGAGGGACTCCA
GCCAACTTCCTTGATGTTGGTGGTGGTGCTACAGTCCATCAAGTAACAGAAGCATTTAAG
CTTATCACTTCAGATAAAAAGGTACTGGCTATTCTGGTCAACATTTTTGGAGGAATCATG
CGCTGTGATGTTATTGCACAGGGTATAGTCATGGCAGTAAAAGACTTGGAAATTAAAATA
CCTGTTGTGGTACGGTTACAAGGTACACGAGTCGATGATGCTAAGGCACTGATAGCGGAC
AGTGGACTTAAAATACTTGCTTGTGATGACTTGGATGAAGCTGCTAGAATGGTTGTAAAG
CTCTCTGAAATAGTGACCTTAGCGAAGCAAGCACATGTGGATGTGAAATTTCAGTTGCCA
ATATGA
Enzyme 115 GenBank Gene ID AL157369 Link Image
Enzyme 115 GeneCard ID SUCLA2 Link Image
Enzyme 115 GenAtlas ID SUCLA2 Link Image
Enzyme 115 HGNC ID HGNC:11448 Link Image
Enzyme 115 Chromosome Location 13
Enzyme 115 Locus 13q12.2-q13.3
Enzyme 115 SNPs SNPJam Report Link Image
Enzyme 115 General References Not Available
Enzyme 115 Metabolite References Not Available
Enzyme 116 [top]
Enzyme 116 ID 9324
Enzyme 116 Name Mannose-1-phosphate guanyltransferase beta
Enzyme 116 Synonyms
  1. GDP-mannose pyrophosphorylase B
  2. GTP-mannose-1-phosphate guanylyltransferase beta
Enzyme 116 Gene Name GMPPB
Enzyme 116 Protein Sequence >Mannose-1-phosphate guanyltransferase beta
MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQVL
EKEMKAQEQRLGIRISMSHEEEPLGTAGPLALARDLLSETADPFFVLNSDVICDFPFQAM
VQFHRHHGQEGSILVTKVEEPSKYGVVVCEADTGRIHRFVEKPQVFVSNKINAGMYILSP
AVLQRIQLQPTSIEKEVFPIMAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFLQSLRQKQ
PERLCSGPGIVGNVLVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVLRDARIRSH
SWLESCIVGWRCRVGQWVRMENVTVLGEDVIVNDELYLNGASVLPHKSIGESVPEPRIIM
Enzyme 116 Number of Residues 360
Enzyme 116 Molecular Weight 39834.1
Enzyme 116 Theoretical pI 6.59
Enzyme 116 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • metabolic process
Component
Enzyme 116 General Function Involved in transferase activity
Enzyme 116 Specific Function GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose
Enzyme 116 Pathways
Enzyme 116 Reactions
  • GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose [RN:R00885]
Enzyme 116 Pfam Domain Function
Enzyme 116 Signals
  • None
Enzyme 116 Transmembrane Regions
  • None
Enzyme 116 Essentiality Not Available
Enzyme 116 GenBank ID Protein 5052351 Link Image
Enzyme 116 UniProtKB/Swiss-Prot ID Q9Y5P6 Link Image
Enzyme 116 UniProtKB/Swiss-Prot Entry Name GMPPB_HUMAN Link Image
Enzyme 116 PDB ID Not Available
Enzyme 116 Cellular Location Not Available
Enzyme 116 Gene Sequence >1083 bp
ATGAAGGCACTGATCTTAGTGGGGGGCTATGGGACGCGGCTACGGCCGCTGACGCTGAGC
ACCCCGAAGCCACTGGTGGACTTCTGCAATAAGCCCATCTTGCTGCACCAAGTGGAGGCG
CTAGCCGCGGCAGGCGTGGACCACGTGATCCTGGCCGTGAGCTACATGTCGCAGGTGCTG
GAGAAGGAAATGAAGGCACAGGAGCAGAGGCTGGGAATCCGAATCTCCATGTCCCATGAA
GAGGAGCCTTTGGGGACAGCTGGGCCCCTGGCGCTGGCCCGTGACCTACTCTCTGAGACT
GCAGACCCTTTCTTCGTCCTCAACAGTGACGTGATCTGCGATTTCCCCTTCCAAGCCATG
GTGCAGTTCCACCGGCACCATGGCCAGGAGGGCTCCATCCTGGTGACCAAGGTGGAGGAA
CCCTCCAAGTACGGTGTGGTGGTGTGTGAGGCTGACACAGGCCGCATTCACCGGTTCGTG
GAGAAGCCACAGGTGTTTGTGTCCAATAAGATCAACGCAGGCATGTACATCCTGAGCCCT
GCAGTGCTGCGGCGCATCCAGCTGCAGCCTACGTCCATTGAGAAGGAGGTCTTCCCCATT
ATGGCCAAGGAGGGGCAGCTATATGCCATGGAGTTACAGGGCTTCTGGATGGACATTGGG
CAGCCCAAGGACTTCCTCACTGGCATGTGCCTCTTCCTGCAGTCACTGAGGCAGAAGCAG
CCTGAGCGGCTGTGCTCAGGCCCTGGCATTGTGGGCAACGTGCTGGTGGACCCAAGTGCC
CGCATCGGCCAGAACTGCAGCATTGGCCCCAATGTGAGCCTGGGACCTGGCGTGGTGGTC
GAAGATGGTGTGTGTATCCGGCGGTGCACGGTGCTGCGGGATGCCCGGATCCGTTCCCAT
TCCTGGCTTGAGTCCTGCATTGTGGGCTGGCGCTGCCGCGTGGGTCAGTGGGTACGCATG
GAGAACGTGACAGTGCTGGGTGAGGACGTCATAGTTAATGATGAGCTCTACCTCAACGGA
GCCAGCGTGCTGCCCCACAAGTCTATTGGCGAGTCAGTGCCAGAGCCTCGTATCATCATG
TGA
Enzyme 116 GenBank Gene ID AF135421 Link Image
Enzyme 116 GeneCard ID GMPPB Link Image
Enzyme 116 GenAtlas ID GMPPB Link Image
Enzyme 116 HGNC ID HGNC:22932 Link Image
Enzyme 116 Chromosome Location 3
Enzyme 116 Locus 3p21.31
Enzyme 116 SNPs SNPJam Report Link Image
Enzyme 116 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 116 Metabolite References Not Available
Enzyme 117 [top]
Enzyme 117 ID 9325
Enzyme 117 Name Mannose-1-phosphate guanyltransferase alpha
Enzyme 117 Synonyms
  1. GDP-mannose pyrophosphorylase A
  2. GTP-mannose-1-phosphate guanylyltransferase alpha
Enzyme 117 Gene Name GMPPA
Enzyme 117 Protein Sequence >Mannose-1-phosphate guanyltransferase alpha
MLKAVILIGGPQKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGFYQ
PDEPLTQFLEAAQQEFNLPVRYLQEFAPLGTGGGLYHFRDQILAGSPEAFFVLNADVCSD
FPLSAMLEAHRRQRHPFLLLGTTANRTQSLNYGCIVENPQTHEVLHYVEKPSTFISDIIN
CGIYLFSPEALKPLRDVFQRNQQDGQLEDSPGLWPGAGTIRLEQDVFSALAGQGQIYVHL
TDGIWSQIKSAGSALYASRLYLSRYQDTHPERLAKHTPGGPWIRGNVYIHPTAKVAPSAV
LGPNVSIGKGVTVGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARVEGTPSDP
NPNDPRARMDSESLFKDGKLLPAITILGCRVRIPAEVLILNSIVLPHKELSRSFTNQIIL
Enzyme 117 Number of Residues 420
Enzyme 117 Molecular Weight 46290.8
Enzyme 117 Theoretical pI 7.23
Enzyme 117 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biosynthetic process
  • metabolic process
Component
Enzyme 117 General Function Involved in transferase activity
Enzyme 117 Specific Function GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose
Enzyme 117 Pathways Not Available
Enzyme 117 Reactions
  • GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose [RN:R00885]
Enzyme 117 Pfam Domain Function
Enzyme 117 Signals
  • None
Enzyme 117 Transmembrane Regions
  • None
Enzyme 117 Essentiality Not Available
Enzyme 117 GenBank ID Protein 62822505 Link Image
Enzyme 117 UniProtKB/Swiss-Prot ID Q96IJ6 Link Image
Enzyme 117 UniProtKB/Swiss-Prot Entry Name GMPPA_HUMAN Link Image
Enzyme 117 PDB ID Not Available
Enzyme 117 Cellular Location Not Available
Enzyme 117 Gene Sequence >1263 bp
ATGCTCAAAGCGGTGATCCTGATTGGAGGCCCTCAAAAGGGAACTCGCTTCAGACCTTTG
TCTTTTGAGGTGCCCAAACCATTGTTTCCTGTGGCAGGGGTCCCTATGATCCAACACCAT
ATTGAAGCCTGTGCCCAGGTCCCTGGAATGCAGGAGATTCTGCTCATTGGCTTCTACCAA
CCTGATGAGCCCCTCACCCAGTTCCTAGAAGCCGCCCAGCAGGAGTTTAACCTTCCAGTC
AGGTACCTGCAGGAATTTGCCCCCCTAGGCACAGGGGGTGGTCTTTACCATTTTCGAGAC
CAGATCCTGGCTGGGAGCCCCGAGGCATTCTTCGTGCTCAATGCTGATGTCTGCTCCGAC
TTCCCCTTGAGTGCTATGTTGGAAGCCCACCGACGCCAGCGTCACCCTTTCTTACTCCTT
GGCACTACGGCTAACAGGACGCAATCCCTCAACTACGGCTGCATCGTTGAGAATCCACAG
ACACACGAGGTATTGCACTATGTGGAGAAACCCAGCACATTTATCAGTGACATCATCAAC
TGCGGCATCTACCTCTTTTCTCCTGAAGCCTTGAAGCCTCTTCGGGATGTCTTCCAGCGT
AATCAGCAGGATGGGCAATTGGAGGACTCACCAGGCTTGTGGCCAGGGGCAGGTACCATC
CGCCTAGAGCAGGATGTGTTTTCAGCCCTGGCAGGGCAGGGCCAGATATACGTGCATCTC
ACTGATGGTATCTGGAGTCAGATCAAGTCCGCAGGTTCAGCCCTCTACGCCTCCCGCCTC
TACCTGAGCCGATACCAGGACACTCACCCAGAACGGCTGGCCAAGCACACCCCAGGGGGC
CCATGGATCCGAGGGAATGTGTACATCCACCCGACCGCCAAGGTGGCCCCCTCGGCTGTG
CTGGGCCCCAACGTCTCCATCGGGAAGGGGGTGACCGTGGGTGAGGGTGTGCGGCTCCGG
GAGAGCATCGTCCTCCATGGAGCCACTTTGCAGGAGCACACGTGTGTTCTGCATAGCATC
GTGGGCTGGGGGAGCACCGTGGGACGCTGGGCCCGCGTGGAGGGTACCCCCAGTGACCCT
AACCCCAACGATCCCCGAGCCCGCATGGACAGTGAGAGCCTCTTCAAGGACGGGAAGCTG
CTGCCTGCTATCACCATCCTGGGCTGCCGAGTCCGGATCCCTGCCGAGGTGCTCATCCTG
AACTCGATTGTTCTGCCACACAAGGAGCTGAGCCGAAGCTTCACCAACCAGATCATCCTC
TGA
Enzyme 117 GenBank Gene ID AC053503 Link Image
Enzyme 117 GeneCard ID GMPPA Link Image
Enzyme 117 GenAtlas ID GMPPA Link Image
Enzyme 117 HGNC ID HGNC:22923 Link Image
Enzyme 117 Chromosome Location 2
Enzyme 117 Locus 2q35
Enzyme 117 SNPs SNPJam Report Link Image
Enzyme 117 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 117 Metabolite References Not Available
Enzyme 118 [top]
Enzyme 118 ID 9777
Enzyme 118 Name Acyl-coenzyme A synthetase ACSM1, mitochondrial
Enzyme 118 Synonyms
  1. Acyl-CoA synthetase medium-chain family member 1
  2. Butyrate--CoA ligase 1
  3. Butyryl-coenzyme A synthetase 1
  4. Lipoate-activating enzyme
  5. Middle-chain acyl-CoA synthetase 1
Enzyme 118 Gene Name ACSM1
Enzyme 118 Protein Sequence >Acyl-coenzyme A synthetase ACSM1, mitochondrial
MQWLMRFRTLWGIHKSFHNIHPAPSQLRCRSLSEFGAPRWNDYEVPEEFNFASYVLDYWA
QKEKEGKRGPNPAFWWVNGQGDEVKWSFREMGDLTRRVANVFTQTCGLQQGDHLALMLPR
VPEWWLVAVGCMRTGIIFIPATILLKAKDILYRLQLSKAKGIVTIDALASEVDSIASQCP
SLKTKLLVSDHSREGWLDFRSLVKSASPEHTCVKSKTLDPMVIFFTSGTTGFPKMAKHSH
GLALQPSFPGSRKLRSLKTSDVSWCLSDSGWIVATIWTLVEPWTAGCTVFIHHLPQFDTK
VIIQTLLKYPINHFWGVSSIYRMILQQDFTSIRFPALEHCYTGGEVVLPKDQEEWKRRTG
LLLYENYGQSETGLICATYWGMKIKPGFMGKATPPYDVQVIDDKGSILPPNTEGNIGIRI
KPVRPVSLFMCYEGDPEKTAKVECGDFYNTGDRGKMDEEGYICFLGRSDDIINASGYRIG
PAEVESALVEHPAVAESAVVGSPDPIRGEVVKAFIVLTPQFLSHDKDQLTKELQQHVKSV
TAPYKYPRKVEFVSELPKTITGKIERKELRKKETGQM
Enzyme 118 Number of Residues 577
Enzyme 118 Molecular Weight 65272.7
Enzyme 118 Theoretical pI 8.40
Enzyme 118 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
Enzyme 118 General Function Involved in catalytic activity
Enzyme 118 Specific Function Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4- unsaturated acids (in vitro). Functions as GTP-dependent lipoate- activating enzyme that generates the substrate for lipoyltransferase
Enzyme 118 Pathways
Enzyme 118 Reactions
  • ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA [RN:R00389]
Enzyme 118 Pfam Domain Function
Enzyme 118 Signals
  • None
Enzyme 118 Transmembrane Regions
  • None
Enzyme 118 Essentiality Not Available
Enzyme 118 GenBank ID Protein 15487302 Link Image
Enzyme 118 UniProtKB/Swiss-Prot ID Q08AH1 Link Image
Enzyme 118 UniProtKB/Swiss-Prot Entry Name ACSM1_HUMAN Link Image
Enzyme 118 PDB ID Not Available
Enzyme 118 Cellular Location Not Available
Enzyme 118 Gene Sequence >1734 bp
ATGCAGTGGCTAATGAGGTTCCGGACCCTCTGGGGCATCCACAAATCCTTCCACAACATC
CACCCTGCCCCTTCACAGCTGCGCTGCCGGTCTTTATCAGAATTTGGAGCCCCAAGATGG
AATGACTATGAAGTACCGGAGGAATTTAACTTTGCAAGTTATGTACTGGACTACTGGGCT
CAAAAGGAGAAGGAGGGCAAGAGAGGTCCAAATCCAGCTTTTTGGTGGGTGAATGGCCAA
GGGGATGAAGTAAAGTGGAGCTTCAGAGAGATGGGAGACCTAACCCGCCGTGTAGCCAAC
GTCTTCACACAGACCTGTGGCCTACAACAGGGAGACCATCTGGCCTTGATGCTGCCTCGA
GTTCCTGAGTGGTGGCTGGTGGCTGTGGGCTGCATGCGAACAGGGATCATCTTCATTCCT
GCGACCATCCTGTTGAAGGCCAAAGACATTCTCTATCGACTACAGTTGTCTAAAGCCAAG
GGCATTGTGACCATAGATGCCCTTGCCTCAGAGGTGGACTCCATAGCTTCTCAGTGCCCC
TCTCTGAAAACCAAGCTCCTGGTGTCTGATCACAGCCGTGAAGGGTGGCTGGACTTCCGA
TCGCTGGTTAAATCAGCATCCCCAGAACACACCTGTGTTAAGTCAAAGACCTTGGACCCA
ATGGTCATCTTCTTCACCAGTGGGACCACAGGCTTCCCCAAGATGGCAAAACACTCCCAT
GGGTTGGCCTTACAACCCTCCTTCCCAGGAAGTAGGAAATTACGGAGCCTGAAGACATCT
GATGTCTCCTGGTGCCTGTCGGACTCAGGATGGATTGTGGCTACCATTTGGACCCTGGTA
GAACCATGGACAGCGGGTTGTACAGTCTTTATCCACCATCTGCCACAGTTTGACACCAAG
GTCATCATACAGACATTGTTGAAATACCCCATTAACCACTTTTGGGGGGTATCATCTATA
TATCGAATGATTCTGCAGCAGGATTTCACCAGCATCAGGTTCCCTGCCCTGGAGCACTGC
TATACTGGCGGGGAGGTCGTGTTGCCCAAGGATCAGGAGGAGTGGAAAAGACGGACGGGC
CTTCTGCTCTACGAGAACTATGGGCAGTCGGAAACGGGACTAATTTGTGCCACCTACTGG
GGAATGAAGATCAAGCCGGGTTTCATGGGGAAGGCCACTCCACCCTATGACGTCCAGGTC
ATTGATGACAAGGGCAGCATCCTGCCACCTAACACAGAAGGAAACATTGGCATCAGAATC
AAACCTGTCAGGCCTGTGAGCCTCTTCATGTGCTATGAGGGTGACCCAGAGAAGACAGCT
AAAGTGGAATGTGGGGACTTCTACAACACTGGGGACAGAGGAAAGATGGATGAAGAGGGC
TACATTTGTTTCCTGGGGAGGAGTGATGACATCATTAATGCCTCTGGGTATCGCATCGGG
CCTGCAGAGGTTGAAAGCGCTTTGGTGGAGCACCCAGCGGTGGCGGAGTCAGCCGTGGTG
GGCAGCCCAGACCCGATTCGAGGGGAGGTGGTGAAGGCCTTTATTGTCCTGACCCCACAG
TTCCTGTCCCATGACAAGGATCAGCTGACCAAGGAACTGCAGCAGCATGTCAAGTCAGTG
ACAGCCCCATACAAGTACCCAAGGAACGTGGAGTTTGTCTCAGAGCTGCCAAAAACCATC
ACTGGCAAGATTGAACGGAAGGAACTTCGGAAAAAGGAGACTGGTCAGATGTAA
Enzyme 118 GenBank Gene ID AB059429 Link Image
Enzyme 118 GeneCard ID ACSM1 Link Image
Enzyme 118 GenAtlas ID ACSM1 Link Image
Enzyme 118 HGNC ID HGNC:18049 Link Image
Enzyme 118 Chromosome Location 1
Enzyme 118 Locus 16p12.3
Enzyme 118 SNPs SNPJam Report Link Image
Enzyme 118 General References
  1. Fujino T, Takei YA, Sone H, Ioka RX, Kamataki A, Magoori K, Takahashi S, Sakai J, Yamamoto TT: Molecular identification and characterization of two medium-chain acyl-CoA synthetases, MACS1 and the Sa gene product. J Biol Chem. 2001 Sep 21;276(38):35961-6. Epub 2001 Jul 24. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 118 Metabolite References Not Available
Enzyme 119 [top]
Enzyme 119 ID 10049
Enzyme 119 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1
Enzyme 119 Synonyms
  1. Pancreas-enriched phospholipase C
  2. Phosphoinositide phospholipase C-epsilon-1
  3. Phospholipase C-epsilon-1
  4. PLC-epsilon-1
Enzyme 119 Gene Name PLCE1
Enzyme 119 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1
MTSEEMTASVLIPVTQRKVVSAQSAADESSEKVSDINISKAHTVRRSGETSHTISQLNKL
KEEPSGSNLPKILSIAREKIVSDENSNEKCWEKIMPDSAKNLNINCNNILRNHQHGLPQR
QFYEMYNSVAEEDLCLETGIPSPLERKVFPGIQLELDRPSMGISPLGNQSVIIETGRAHP
DSRRAVFHFHYEVDRRMSDTFCTLSENLILDDCGNCVPLPGGEEKQKKNYVAYTCKLMEL
AKNCDNKNEQLQCDHCDTLNDKYFCFEGSCEKVDMVYSGDSFCRKDFTDSQAAKTFLSHF
EDFPDNCDDVEEDAFKSKKERSTLLVRRFCKNDREVKKSVYTGTRAIVRTLPSGHIGLTA
WSYIDQKRNGPLLPCGRVMEPPSTVEIRQDGSQRLSEAQWYPIYNAVRREETENTVGSLL
HFLTKLPASETAHGRISVGPCLKQCVRDTVCEYRATLQRTSISQYITGSLLEATTSLGAR
SGLLSTFGGSTGRMMLKERQPGPSVANSNALPSSSAGISKELIDLQPLIQFPEEVASILM
EQEQTIYRRVLPVDYLCFLTRDLGTPECQSSLPCLKASISASILTTQNGEHNALEDLVMR
FNEVSSWVTWLILTAGSMEEKREVFSYLVHVAKCCWNMGNYNAVMEFLAGLRSRKVLKMW
QFMDQSDIETMRSLKDAMAQHESSCEYRKVVTRALHIPGCKVVPFCGVFLKELCEVLDGA
SGLMKLCPRYNSQEETLEFVADYSGQDNFLQRVGQNGLKNSEKESTVNSIFQVIRSCNRS
LETDEEDSPSEGNSSRKSSLKDKSRWQFIIGDLLDSDNDIFEQSKEYDSHGSEDSQKAFD
HGTELIPWYVLSIQADVHQFLLQGATVIHYDQDTHLSARCFLQLQPDNSTLTWVKPTTAS
PASSKAKLGVLNNTAEPGKFPLLGNAGLSSLTEGVLDLFAVKAVYMGHPGIDIHTVCVQN
KLGSMFLSETGVTLLYGLQTTDNRLLHFVAPKHTAKMLFSGLLELTRAVRKMRKFPDQRQ
QWLRKQYVSLYQEDGRYEGPTLAHAVELFGGRRWSARNPSPGTSAKNAEKPNMQRNNTLG
ISTTKKKKKILMRGESGEVTDDEMATRKAKMHKECRSRSGSDPQDINEQEESEVNAIANP
PNPLPSRRAHSLTTAGSPNLAAGTSSPIRPVSSPVLSSSNKSPSSAWSSSSWHGRIKGGM
KGFQSFMVSDSNMSFVEFVELFKSFSVRSRKDLKDLFDVYAVPCNRSGSESAPLYTNLTI
DENTSDLQPDLDLLTRNVSDLGLFIKSKQQLSDNQRQISDAIAAASIVTNGTGIESTSLG
IFGVGILQLNDFLVNCQGEHCTYDEILSIIQKFEPSISMCHQGLMSFEGFARFLMDKENF
ASKNDESQENIKELQLPLSYYYIESSHNTYLTGHQLKGESSVELYSQVLLQGCRSVELDC
WDGDDGMPIIYHGHTLTTKIPFKEVVEAIDRSAFINSDLPIIISIENHCSLPQQRKMAEI
FKTVFGEKLVTKFLFETDFSDDPMLPSPDQLRKKVLLKNKKLKAHQTPVDILKQKAHQLA
SMQVQAYNGGNANPRPANNEEEEDEEDEYDYDYESLSDDNILEDRPENKSCNDKLQFEYN
EEIPKRIKKADNSACNKGKVYDMELGEEFYLDQNKKESRQIAPELSDLVIYCQAVKFPGL
STLNASGSSRGKERKSRKSIFGNNPGRMSPGETASFNKTSGKSSCEGIRQTWEESSSPLN
PTTSLSAIIRTPKCYHISSLNENAAKRLCRRYSQKLTQHTACQLLRTYPAATRIDSSNPN
PLMFWLHGIQLVALNYQTDDLPLHLNAAMFEANGGCGYVLKPPVLWDKNCPMYQKFSPLE
RDLDSMDPAVYSLTIVSGQNVCPSNSMGSPCIEVDVLGMPLDSCHFRTKPIHRNTLNPMW
NEQFLFHVHFEDLVFLRFAVVENNSSAVTAQRIIPLKALKRGYRHLQLRNLHNEVLEISS
LFINSRRMEENSSGNTMSASSMFNTEERKCLQTHRVTVHGVPGPEPFTVFTINGGTKAKQ
LLQQILTNEQDIKPVTTDYFLMEEKYFISKEKNECRKQPFQRAIGPEEEIMQILSSWFPE
EGYMGRIVLKTQQENLEEKNIVQDDKEVILSSEEESFFVQVHDVSPEQPRTVIKAPRVST
AQDVIQQTLCKAKYSYSILSNPNPSDYVLLEEVVKDTTNKKTTTPKSSQRVLLDQECVFQ
AQSKWKGAGKFILKLKEQVQASREDKKKGISFASELKKLTKSTKQPRGLTSPSQLLTSES
IQTKEEKPVGGLSSSDTMDYRQ
Enzyme 119 Number of Residues 2302
Enzyme 119 Molecular Weight 258712.3
Enzyme 119 Theoretical pI 6.44
Enzyme 119 GO Classification
Function
  • GTPase regulator activity
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • nucleoside-triphosphatase regulator activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signal transduction
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 119 General Function Involved in calcium ion binding
Enzyme 119 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. PLCE1 is a bifunctional enzyme which also regulates small GTPases of the Ras superfamily through its Ras guanine- exchange factor (RasGEF) activity. As an effector of heterotrimeric and small G-protein, it may play a role in cell survival, cell growth, actin organization and T-cell activation
Enzyme 119 Pathways
Enzyme 119 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 119 Pfam Domain Function
Enzyme 119 Signals
  • None
Enzyme 119 Transmembrane Regions
  • None
Enzyme 119 Essentiality Not Available
Enzyme 119 GenBank ID Protein 117168250 Link Image
Enzyme 119 UniProtKB/Swiss-Prot ID Q9P212 Link Image
Enzyme 119 UniProtKB/Swiss-Prot Entry Name PLCE1_HUMAN Link Image
Enzyme 119 PDB ID Not Available
Enzyme 119 Cellular Location Not Available
Enzyme 119 Gene Sequence >6909 bp
ATGACTTCTGAAGAAATGACAGCTTCTGTTCTCATACCTGTGACTCAGAGAAAAGTGGTT
TCTGCCCAGTCGGCTGCAGATGAAAGTAGTGAAAAGGTCTCAGACATCAATATTTCAAAA
GCACATACTGTCAGACGAAGTGGGGAGACTTCTCATACCATCTCACAACTGAACAAACTT
AAAGAAGAACCTTCTGGAAGCAACTTGCCAAAGATTCTCTCAATAGCGAGGGAGAAAATA
GTGAGTGATGAGAACAGTAATGAAAAATGTTGGGAGAAAATCATGCCAGATTCTGCGAAA
AACCTTAACATTAACTGCAACAACATATTGAGAAACCATCAGCATGGCCTTCCTCAGAGA
CAATTTTATGAAATGTACAACTCTGTTGCTGAGGAAGACTTGTGTTTAGAAACTGGAATT
CCTTCTCCACTGGAAAGAAAGGTGTTCCCTGGAATTCAACTGGAACTAGACAGACCTTCC
ATGGGCATTAGTCCTTTAGGAAATCAGTCAGTGATCATAGAGACAGGCAGAGCACACCCT
GACAGCAGAAGGGCAGTATTTCATTTTCATTATGAAGTTGACAGAAGAATGTCAGACACT
TTCTGTACCCTATCAGAAAACTTAATTTTAGACGATTGTGGAAATTGTGTACCACTACCT
GGGGGTGAGGAGAAGCAAAAGAAAAACTATGTGGCATATACCTGTAAACTGATGGAATTG
GCCAAAAATTGTGATAATAAGAATGAGCAGCTGCAGTGTGATCATTGTGACACCTTGAAT
GATAAATACTTTTGCTTTGAAGGCTCTTGTGAGAAGGTTGACATGGTATATTCAGGTGAT
AGCTTTTGTAGGAAAGACTTTACTGACAGTCAAGCTGCCAAGACCTTTTTGAGCCATTTT
GAGGACTTCCCTGATAATTGTGATGATGTAGAAGAAGACGCTTTTAAAAGCAAAAAGGAG
CGATCCACTTTGTTAGTCAGGAGATTCTGTAAAAATGACAGAGAAGTTAAGAAATCTGTG
TATACTGGAACAAGAGCAATTGTGAGAACTCTGCCTTCTGGCCACATTGGGCTGACTGCA
TGGAGTTACATAGATCAGAAGAGAAATGGTCCCTTACTGCCTTGTGGGAGAGTAATGGAA
CCCCCGTCAACAGTGGAGATAAGGCAAGATGGGAGCCAACGTCTGTCAGAAGCCCAGTGG
TATCCTATCTACAATGCAGTGAGAAGAGAAGAAACAGAAAATACAGTTGGATCTCTACTC
CATTTCCTCACCAAGCTCCCAGCCTCCGAGACAGCCCATGGAAGGATAAGCGTTGGTCCA
TGCTTAAAGCAATGTGTCCGAGACACTGTATGTGAGTATCGCGCCACCCTCCAAAGGACT
TCAATATCGCAGTACATCACCGGTTCTCTCCTAGAAGCAACCACGTCTTTGGGAGCAAGA
AGTGGCCTTCTCAGTACTTTTGGAGGATCCACTGGACGAATGATGCTGAAAGAACGCCAG
CCAGGCCCCTCTGTGGCCAATTCCAATGCCCTCCCTTCAAGTTCAGCTGGGATCAGCAAG
GAGCTGATCGATCTGCAGCCTCTCATCCAGTTCCCAGAGGAAGTCGCCAGCATCCTGATG
GAGCAAGAGCAGACTATTTACCGCAGGGTCTTGCCAGTCGACTACCTTTGCTTCTTAACA
CGGGACTTGGGCACTCCTGAATGCCAGAGCTCCTTGCCCTGCCTCAAAGCATCCATCTCA
GCGTCGATTCTTACCACTCAGAATGGAGAGCACAATGCCCTTGAAGATCTGGTGATGAGG
TTTAATGAGGTGAGCTCCTGGGTGACATGGCTGATCCTCACGGCAGGCTCCATGGAGGAG
AAGCGAGAAGTCTTTTCATATTTGGTGCATGTGGCCAAATGCTGCTGGAACATGGGCAAC
TACAACGCTGTCATGGAGTTCTTGGCTGGCCTCAGGTCAAGAAAAGTTTTAAAAATGTGG
CAGTTCATGGACCAGTCTGATATTGAGACCATGAGGAGCCTGAAGGATGCTATGGCCCAG
CATGAGTCCTCTTGTGAGTACAGAAAGGTGGTGACACGTGCCCTGCACATCCCTGGCTGT
AAGGTGGTTCCATTCTGTGGGGTGTTTCTGAAGGAGCTCTGTGAAGTGCTTGACGGCGCC
TCCGGTCTCATGAAGCTTTGCCCGCGGTACAATTCCCAAGAAGAAACTTTAGAGTTTGTA
GCAGATTACAGTGGACAAGATAATTTCTTACAACGAGTGGGACAAAATGGCTTAAAGAAT
TCGGAGAAGGAGTCCACTGTCAACAGCATCTTTCAGGTCATCCGGAGCTGCAATCGAAGT
CTGGAGACAGACGAGGAGGACAGCCCCAGTGAAGGAAACAGCTCCAGGAAAAGCTCCTTG
AAGGATAAAAGCCGATGGCAGTTTATAATTGGAGATTTGTTGGATTCAGACAATGACATC
TTTGAGCAATCCAAAGAATACGACTCTCATGGTTCAGAGGACTCACAGAAGGCCTTCGAC
CATGGGACGGAGCTCATCCCTTGGTACGTGCTGTCCATCCAAGCCGATGTGCACCAGTTC
CTGCTGCAGGGGGCCACGGTCATCCACTACGACCAGGACACACACCTCTCTGCCCGCTGC
TTCCTCCAGCTTCAGCCCGACAATAGCACCTTGACCTGGGTAAAGCCCACAACTGCCTCC
CCAGCCAGCAGTAAAGCAAAACTTGGTGTACTTAATAACACAGCTGAGCCTGGAAAATTC
CCACTACTGGGTAATGCTGGATTAAGTAGCCTGACGGAAGGGGTCTTGGATCTTTTTGCA
GTGAAGGCTGTATACATGGGCCACCCTGGCATTGATATACACACTGTGTGTGTTCAGAAC
AAACTGGGTAGCATGTTCCTGTCAGAGACTGGTGTGACATTGCTCTATGGGCTTCAGACC
ACAGACAACAGATTATTGCACTTCGTGGCACCAAAGCACACAGCTAAAATGCTCTTCAGC
GGATTATTGGAACTCACTAGAGCTGTGAGAAAGATGAGGAAATTCCCTGACCAAAGACAG
CAGTGGCTGCGGAAACAGTACGTCAGCCTTTATCAGGAGGATGGACGGTATGAAGGCCCA
ACTTTGGCTCACGCTGTGGAGTTGTTTGGTGGCAGACGGTGGAGTGCTCGAAACCCCAGC
CCCGGAACATCAGCAAAGAATGCTGAGAAGCCCAATATGCAGAGAAACAATACCCTGGGC
ATAAGCACTACCAAGAAAAAGAAGAAAATCCTCATGAGGGGTGAGAGTGGAGAGGTAACT
GACGATGAGATGGCAACCCGAAAGGCCAAGATGCACAAAGAGTGTCGAAGCCGGAGTGGT
TCTGATCCTCAAGACATTAATGAACAAGAAGAATCAGAGGTGAATGCCATCGCTAACCCT
CCAAACCCCCTCCCTTCCAGAAGAGCCCACTCTTTGACCACAGCTGGGTCCCCCAACTTG
GCTGCCGGGACGTCATCTCCCATCAGGCCAGTGTCCTCCCCTGTGCTGTCTTCTTCAAAC
AAGAGCCCATCCAGTGCTTGGAGCAGTAGTAGCTGGCACGGGCGGATCAAAGGCGGCATG
AAGGGATTTCAGAGCTTCATGGTTTCAGATAGCAACATGAGTTTTGTTGAATTTGTTGAG
CTGTTCAAATCATTCAGTGTCAGGAGCCGCAAGGACCTGAAGGATCTGTTTGATGTCTAT
GCAGTGCCCTGCAACCGATCTGGCTCCGAGTCAGCCCCACTCTACACCAACCTGACAATT
GATGAAAACACCAGCGATCTTCAGCCTGACCTAGATCTGTTGACCAGAAATGTCTCGGAT
TTGGGGTTGTTCATTAAGAGTAAACAGCAGCTATCGGACAACCAGAGGCAGATATCTGAT
GCCATTGCTGCTGCAAGCATTGTGACAAATGGCACTGGGATTGAGAGCACATCTCTGGGC
ATTTTTGGGGTGGGCATACTTCAGCTCAACGATTTCCTCGTGAATTGCCAAGGAGAACAC
TGCACTTATGATGAAATCCTCAGCATCATCCAGAAGTTCGAGCCTAGCATCAGTATGTGT
CATCAGGGACTAATGTCATTTGAAGGGTTTGCCAGGTTTCTGATGGATAAAGAAAATTTT
GCCTCAAAAAATGATGAGTCACAGGAGAACATTAAAGAACTGCAGCTACCCCTCTCATAC
TATTACATCGAATCTTCGCACAATACCTACCTCACGGGCCATCAGCTCAAAGGAGAATCC
TCGGTAGAACTCTACAGCCAGGTCCTTTTGCAAGGCTGTCGAAGTGTAGAATTGGACTGC
TGGGACGGAGACGATGGGATGCCCATCATTTATCATGGACATACGCTGACAACCAAGATC
CCCTTCAAGGAAGTGGTTGAAGCCATTGATCGCAGTGCCTTCATCAACTCTGACCTGCCA
ATCATCATATCGATTGAGAACCACTGTTCATTGCCTCAGCAACGAAAAATGGCAGAAATT
TTCAAGACTGTGTTTGGAGAAAAGCTGGTGACTAAATTCTTATTTGAGACTGATTTCTCA
GATGATCCAATGCTTCCTTCACCTGACCAACTCAGAAAGAAAGTTCTTCTTAAAAACAAG
AAGCTAAAAGCCCATCAGACGCCAGTGGATATCTTAAAGCAAAAGGCTCATCAGTTAGCA
TCTATGCAAGTGCAGGCTTATAATGGTGGGAATGCCAACCCCCGACCTGCCAATAATGAG
GAAGAGGAAGATGAGGAGGACGAATATGATTATGACTATGAATCCCTTTCTGATGACAAC
ATTCTGGAAGACAGACCTGAAAATAAATCATGTAATGACAAGCTTCAGTTTGAATATAAT
GAAGAAATCCCAAAGAGGATAAAGAAAGCAGATAACTCTGCTTGCAACAAAGGAAAGGTT
TATGATATGGAACTGGGAGAAGAATTTTATCTTGATCAGAATAAAAAGGAAAGCAGACAG
ATTGCACCAGAGCTTTCTGACCTTGTAATCTATTGTCAAGCAGTAAAATTTCCAGGACTG
TCAACTCTAAATGCATCTGGCTCTAGCAGAGGAAAAGAAAGGAAAAGCAGGAAGTCCATT
TTTGGCAACAATCCGGGCAGAATGAGCCCAGGGGAGACAGCATCATTTAACAAAACATCT
GGAAAAAGTTCCTGTGAAGGCATTCGACAGACCTGGGAGGAATCTTCTTCCCCTCTCAAC
CCAACCACGTCCCTCAGTGCTATCATTAGAACTCCCAAATGTTATCATATCTCGTCGCTG
AATGAAAATGCCGCCAAACGTCTGTGTCGCAGGTATTCTCAGAAACTGACCCAGCACACC
GCCTGTCAGCTGCTGAGAACTTACCCTGCTGCCACCCGCATCGACTCTTCCAACCCGAAC
CCCCTCATGTTCTGGCTCCATGGGATACAGCTTGTGGCACTCAACTACCAGACTGATGAT
CTCCCTTTACATTTAAATGCTGCAATGTTTGAGGCAAATGGTGGTTGTGGTTATGTATTG
AAACCTCCAGTTCTGTGGGACAAGAACTGCCCCATGTATCAGAAGTTTTCTCCACTAGAA
AGAGATCTGGACAGCATGGATCCTGCAGTCTATTCTTTAACTATTGTCTCTGGTCAGAAT
GTGTGCCCCAGTAATAGCATGGGAAGCCCGTGCATTGAAGTCGACGTCCTGGGCATGCCT
CTGGACAGCTGCCATTTCCGCACAAAGCCCATCCATCGAAACACCCTGAACCCCATGTGG
AACGAGCAGTTTCTGTTCCACGTTCACTTCGAAGATCTTGTATTTCTTCGTTTTGCAGTT
GTGGAAAACAATAGTTCAGCGGTAACTGCTCAGAGAATCATTCCACTGAAAGCTTTAAAA
CGAGGATATCGACATCTTCAGCTGCGAAACCTTCACAATGAAGTCTTGGAGATTTCTAGT
TTATTCATTAACAGCAGAAGGATGGAAGAAAATTCCTCTGGCAATACCATGTCAGCCTCT
TCGATGTTTAATACAGAAGAAAGAAAATGTTTGCAGACTCACAGAGTCACGGTGCATGGG
GTCCCAGGGCCAGAGCCCTTTACCGTTTTCACTATTAATGGAGGCACCAAGGCAAAGCAG
CTTCTGCAGCAAATTCTGACAAATGAACAAGACATCAAACCTGTTACCACAGACTATTTT
TTGATGGAAGAAAAATATTTTATATCTAAAGAAAAGAATGAATGTAGGAAACAACCATTC
CAGAGAGCCATTGGTCCAGAAGAGGAGATCATGCAAATTTTAAGCAGCTGGTTTCCAGAA
GAGGGATACATGGGCAGGATTGTCTTAAAAACCCAGCAGGAAAACCTAGAAGAGAAAAAC
ATTGTTCAAGATGACAAAGAGGTGATCTTGAGCTCAGAGGAGGAGAGTTTCTTTGTCCAA
GTGCATGATGTTTCTCCAGAGCAACCTCGAACAGTCATCAAAGCACCCCGCGTCAGCACT
GCACAGGATGTCATTCAGCAGACCTTATGCAAAGCCAAATATTCCTACAGCATCCTGAGC
AACCCCAATCCAAGCGACTATGTGCTTTTGGAAGAGGTGGTGAAAGACACTACCAACAAG
AAGACTACCACACCAAAGTCCTCTCAGCGGGTCCTTCTGGATCAGGAGTGTGTGTTTCAA
GCCCAAAGCAAGTGGAAAGGTGCAGGAAAATTCATCCTTAAGCTAAAGGAGCAGGTGCAG
GCATCTCGAGAAGATAAAAAGAAAGGCATTTCTTTCGCAAGTGAACTCAAGAAGCTCACC
AAGTCAACTAAACAGCCCCGAGGACTTACATCACCTTCTCAGCTCTTGACCTCAGAAAGT
ATCCAAACCAAGGAGGAGAAACCTGTGGGTGGCTTGTCCTCCAGTGACACAATGGATTAC
CGACAGTGA
Enzyme 119 GenBank Gene ID NM_016341.3 Link Image
Enzyme 119 GeneCard ID PLCE1 Link Image
Enzyme 119 GenAtlas ID PLCE1 Link Image
Enzyme 119 HGNC ID HGNC:17175 Link Image
Enzyme 119 Chromosome Location 1
Enzyme 119 Locus 10q23
Enzyme 119 SNPs SNPJam Report Link Image
Enzyme 119 General References
  1. 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]
  2. Lopez I, Mak EC, Ding J, Hamm HE, Lomasney JW: A novel bifunctional phospholipase c that is regulated by Galpha 12 and stimulates the Ras/mitogen-activated protein kinase pathway. J Biol Chem. 2001 Jan 26;276(4):2758-65. Epub 2000 Oct 5. [PubMed Link Image]
  3. Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Apr 28;7(2):143-50. [PubMed Link Image]
  4. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  7. Jin TG, Satoh T, Liao Y, Song C, Gao X, Kariya K, Hu CD, Kataoka T: Role of the CDC25 homology domain of phospholipase Cepsilon in amplification of Rap1-dependent signaling. J Biol Chem. 2001 Aug 10;276(32):30301-7. Epub 2001 Jun 6. [PubMed Link Image]
  8. Schmidt M, Evellin S, Weernink PA, von Dorp F, Rehmann H, Lomasney JW, Jakobs KH: A new phospholipase-C-calcium signalling pathway mediated by cyclic AMP and a Rap GTPase. Nat Cell Biol. 2001 Nov;3(11):1020-4. [PubMed Link Image]
  9. Evellin S, Nolte J, Tysack K, vom Dorp F, Thiel M, Weernink PA, Jakobs KH, Webb EJ, Lomasney JW, Schmidt M: Stimulation of phospholipase C-epsilon by the M3 muscarinic acetylcholine receptor mediated by cyclic AMP and the GTPase Rap2B. J Biol Chem. 2002 May 10;277(19):16805-13. Epub 2002 Mar 4. [PubMed Link Image]
  10. Song C, Satoh T, Edamatsu H, Wu D, Tadano M, Gao X, Kataoka T: Differential roles of Ras and Rap1 in growth factor-dependent activation of phospholipase C epsilon. Oncogene. 2002 Nov 21;21(53):8105-13. [PubMed Link Image]
  11. Czyzyk J, Brogdon JL, Badou A, Henegariu O, Preston Hurlburt P, Flavell R, Bottomly K: Activation of CD4 T cells by Raf-independent effectors of Ras. Proc Natl Acad Sci U S A. 2003 May 13;100(10):6003-8. Epub 2003 Apr 29. [PubMed Link Image]
  12. vom Dorp F, Sari AY, Sanders H, Keiper M, Oude Weernink PA, Jakobs KH, Schmidt M: Inhibition of phospholipase C-epsilon by Gi-coupled receptors. Cell Signal. 2004 Aug;16(8):921-8. [PubMed Link Image]
  13. Wang H, Oestreich EA, Maekawa N, Bullard TA, Vikstrom KL, Dirksen RT, Kelley GG, Blaxall BC, Smrcka AV: Phospholipase C epsilon modulates beta-adrenergic receptor-dependent cardiac contraction and inhibits cardiac hypertrophy. Circ Res. 2005 Dec 9;97(12):1305-13. Epub 2005 Nov 17. [PubMed Link Image]
  14. Sorli SC, Bunney TD, Sugden PH, Paterson HF, Katan M: Signaling properties and expression in normal and tumor tissues of two phospholipase C epsilon splice variants. Oncogene. 2005 Jan 6;24(1):90-100. [PubMed Link Image]
  15. Ada-Nguema AS, Xenias H, Hofman JM, Wiggins CH, Sheetz MP, Keely PJ: The small GTPase R-Ras regulates organization of actin and drives membrane protrusions through the activity of PLCepsilon. J Cell Sci. 2006 Apr 1;119(Pt 7):1307-19. Epub 2006 Mar 14. [PubMed Link Image]
  16. Bunney TD, Harris R, Gandarillas NL, Josephs MB, Roe SM, Sorli SC, Paterson HF, Rodrigues-Lima F, Esposito D, Ponting CP, Gierschik P, Pearl LH, Driscoll PC, Katan M: Structural and mechanistic insights into ras association domains of phospholipase C epsilon. Mol Cell. 2006 Feb 17;21(4):495-507. [PubMed Link Image]
  17. Hinkes B, Wiggins RC, Gbadegesin R, Vlangos CN, Seelow D, Nurnberg G, Garg P, Verma R, Chaib H, Hoskins BE, Ashraf S, Becker C, Hennies HC, Goyal M, Wharram BL, Schachter AD, Mudumana S, Drummond I, Kerjaschki D, Waldherr R, Dietrich A, Ozaltin F, Bakkaloglu A, Cleper R, Basel-Vanagaite L, Pohl M, Griebel M, Tsygin AN, Soylu A, Muller D, Sorli CS, Bunney TD, Katan M, Liu J, Attanasio M, O'toole JF, Hasselbacher K, Mucha B, Otto EA, Airik R, Kispert A, Kelley GG, Smrcka AV, Gudermann T, Holzman LB, Nurnberg P, Hildebrandt F: Positional cloning uncovers mutations in PLCE1 responsible for a nephrotic syndrome variant that may be reversible. Nat Genet. 2006 Dec;38(12):1397-405. Epub 2006 Nov 5. [PubMed Link Image]
Enzyme 119 Metabolite References Not Available
Enzyme 120 [top]
Enzyme 120 ID 12965
Enzyme 120 Name Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
Enzyme 120 Synonyms
  1. P-Rex1
  2. PtdIns(3,4,5)-dependent Rac exchanger 1
Enzyme 120 Gene Name PREX1
Enzyme 120 Protein Sequence >Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
MEAPSGSEPGGDGAGDCAHPDPRAPGAAAPSSGPGPCAAARESERQLRLRLCVLNEILGT
ERDYVGTLRFLQSAFLHRIRQNVADSVEKGLTEENVKVLFSNIEDILEVHKDFLAALEYC
LHPEPQSQHELGNVFLKFKDKFCVYEEYCSNHEKALRLLVELNKIPTVRAFLLSCMLLGG
RKTTDIPLEGYLLSPIQRICKYPLLLKELAKRTPGKHPDHPAVQSALQAMKTVCSNINET
KRQMEKLEALEQLQSHIEGWEGSNLTDICTQLLLQGTLLKISAGNIQERAFFLFDNLLVY
CKRKSRVTGSKKSTKRTKSINGSLYIFRGRINTEVMEVENVEDGTADYHSNGYTVTNGWK
IHNTAKNKWFVCMAKTAEEKQKWLDAIIREREQRESLKLGMERDAYVMIAEKGEKLYHMM
MNKKVNLIKDRRRKLSTVPKCFLGNEFVAWLLEIGEISKTEEGVNLGQALLENGIIHHVS
DKHQFKNEQVMYRFRYDDGTYKARSELEDIMSKGVRLYCRLHSLYTPVIKDRDYHLKTYK
SVLPGSKLVDWLLAQGDCQTREEAVALGVGLCNNGFMHHVLEKSEFRDESQYFRFHADEE
MEGTSSKNKQLRNDFKLVENILAKRLLILPQEEDYGFDIEEKNKAVVVKSVQRGSLAEVA
GLQVGRKIYSINEDLVFLRPFSEVESILNQSFCSRRPLRLLVATKAKEIIKIPDQPDTLC
FQIRGAAPPYVYAVGRGSEAMAAGLCAGQCILKVNGSNVMNDGAPEVLEHFQAFRSRREE
ALGLYQWIYHTHEDAQEARASQEASTEDPSGEQAQEEDQADSAFPLLSLGPRLSLCEDSP
MVTLTVDNVHLEHGVVYEYVSTAGVRCHVLEKIVEPRGCFGLTAKILEAFAANDSVFVEN
CRRLMALSSAIVTMPHFEFRNICDTKLESIGQRIACYQEFAAQLKSRVSPPFKQAPLEPH
PLCGLDFCPTNCHINLMEVSYPKTTPSVGRSFSIRFGRKPSLIGLDPEQGHLNPMSYTQH
CITTMAAPSWKCLPAAEGDPQGQGLHDGSFGPASGTLGQEDRGLSFLLKQEDREIQDAYL
QLFTKLDVALKEMKQYVTQINRLLSTITEPTSGGSCDASLAEEASSLPLVSEESEMDRSD
HGGIKKVCFKVAEEDQEDSGHDTMSYRDSYSECNSNRDSVLSYTSVRSNSSYLGSDEMGS
GDELPCDMRIPSDKQDKLHGCLEHLFNQVDSINALLKGPVMSRAFEETKHFPMNHSLQEF
KQKEECTIRGRSLIQISIQEDPWNLPNSIKTLVDNIQRYVEDGKNQLLLALLKCTDTELQ
LRRDAIFCQALVAAVCTFSKQLLAALGYRYNNNGEYEESSRDASRKWLEQVAATGVLLHC
QSLLSPATVKEERTMLEDIWVTLSELDNVTFSFKQLDENYVANTNVFYHIEGSRQALKVI
FYLDSYHFSKLPSRLEGGASLRLHTALFTKVLENVEGLPSPGSQAAEDLQQDINAQSLEK
VQQYYRKLRAFYLERSNLPTDASTTAVKIDQLIRPINALDELCRLMKSFVHPKPGAAGSV
GAGLIPISSELCYRLGACQMVMCGTGMQRSTLSVSLEQAAILARSHGLLPKCIMQATDIM
RKQGPRVEILAKNLRVKDQMPQGAPRLYRLCQPPVDGDL
Enzyme 120 Number of Residues 1659
Enzyme 120 Molecular Weight 186201.7
Enzyme 120 Theoretical pI 6.40
Enzyme 120 GO Classification
Function
  • GTPase regulator activity
  • Ras guanyl-nucleotide exchange factor activity
  • Rho guanyl-nucleotide exchange factor activity
  • binding
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • protein binding
  • small GTPase regulator activity
Process
  • biological regulation
  • intracellular signaling pathway
  • regulation of Ras protein signal transduction
  • regulation of Rho protein signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signaling
  • signaling pathway
Component
  • cell part
  • intracellular
Enzyme 120 General Function Involved in intracellular signaling pathway
Enzyme 120 Specific Function Functions as a RAC guanine nucleotide exchange factor (GEF), which activates the Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol-3,4,5-triphosphate and the beta gamma subunits of heterotrimeric G protein. May function downstream of heterotrimeric G proteins in neutrophils
Enzyme 120 Pathways Not Available
Enzyme 120 Reactions Not Available
Enzyme 120 Pfam Domain Function
Enzyme 120 Signals
  • None
Enzyme 120 Transmembrane Regions
  • None
Enzyme 120 Essentiality Not Available
Enzyme 120 GenBank ID Protein 34452732 Link Image
Enzyme 120 UniProtKB/Swiss-Prot ID Q8TCU6 Link Image
Enzyme 120 UniProtKB/Swiss-Prot Entry Name PREX1_HUMAN Link Image
Enzyme 120 PDB ID Not Available
Enzyme 120 Cellular Location Not Available
Enzyme 120 Gene Sequence >4980 bp
ATGGAGGCGCCCAGCGGCAGCGAGCCCGGCGGCGACGGGGCCGGGGACTGCGCCCACCCG
GACCCCCGGGCCCCTGGCGCCGCGGCGCCCAGCTCCGGCCCCGGCCCGTGCGCGGCCGCC
CGGGAGTCCGAGCGCCAGCTGCGCCTCCGCCTCTGCGTCCTCAACGAGATCTTGGGCACC
GAGAGGGACTACGTGGGCACCTTGCGCTTCTTGCAGTCGGCATTCCTGCATCGCATCCGG
CAGAACGTGGCCGACTCAGTGGAGAAGGGCCTCACGGAGGAGAATGTCAAGGTCCTGTTC
TCGAACATCGAAGACATCCTGGAAGTTCATAAGGATTTCTTGGCCGCCTTGGAGTATTGT
TTACACCCGGAGCCGCAGTCTCAGCATGAACTTGGGAATGTTTTCTTAAAATTCAAGGAC
AAGTTCTGCGTGTACGAGGAGTATTGCAGCAACCATGAGAAAGCCCTGAGGCTGCTGGTG
GAGCTGAACAAGATCCCTACCGTGCGCGCCTTCCTTTTGAGCTGCATGCTTCTGGGAGGC
CGGAAGACCACGGACATCCCTTTGGAAGGCTACCTGTTGTCTCCGATCCAGAGGATCTGC
AAGTACCCGCTCCTCCTTAAGGAGCTGGCCAAGAGGACTCCCGGCAAGCACCCAGACCAC
CCCGCGGTCCAGAGTGCCCTGCAGGCCATGAAGACCGTTTGCTCCAACATCAATGAGACC
AAGCGGCAGATGGAGAAGCTGGAAGCCCTGGAGCAGCTGCAGTCCCACATCGAAGGCTGG
GAGGGTTCCAACCTCACAGACATCTGCACTCAGCTCCTCCTGCAAGGGACTTTGTTAAAG
ATCTCTGCGGGCAACATCCAGGAAAGGGCCTTCTTCCTCTTCGACAACCTTCTCGTCTAC
TGCAAGCGGAAATCCAGGGTCACCGGGAGCAAGAAGTCCACCAAGAGGACCAAATCCATC
AACGGCTCCCTCTACATCTTCAGGGGTCGAATCAACACTGAAGTCATGGAGGTGGAGAAT
GTGGAAGATGGGACAGCGGATTACCATAGCAACGGCTATACCGTCACCAACGGCTGGAAG
ATCCACAACACGGCCAAGAATAAGTGGTTTGTCTGCATGGCCAAGACGGCAGAGGAGAAG
CAGAAGTGGCTGGATGCCATCATCCGCGAGCGGGAGCAGCGCGAGAGCCTGAAGCTGGGC
ATGGAGCGTGATGCCTACGTCATGATTGCGGAGAAGGGGGAGAAGCTGTACCACATGATG
ATGAACAAGAAGGTGAACCTCATCAAGGACCGCCGGAGAAAGCTGAGCACTGTCCCCAAG
TGCTTTCTTGGCAATGAGTTCGTTGCCTGGCTCCTAGAAATTGGTGAAATCAGCAAGACG
GAAGAAGGAGTCAACTTGGGCCAAGCCCTGTTGGAGAATGGCATCATCCACCATGTTTCC
GACAAGCACCAGTTCAAGAATGAGCAGGTGATGTATCGCTTCCGCTACGACGATGGCACC
TACAAGGCCCGAAGTGAGCTGGAGGACATCATGTCCAAGGGTGTGAGGCTTTACTGCCGT
CTTCACAGCCTCTACACCCCGGTGATCAAAGACCGTGATTACCACCTGAAGACCTACAAG
TCAGTGCTTCCCGGGAGCAAGCTGGTGGACTGGCTGCTGGCTCAGGGAGACTGCCAGACT
CGGGAGGAGGCAGTGGCGCTCGGCGTGGGTCTGTGCAACAATGGCTTCATGCACCACGTG
CTGGAGAAGAGCGAGTTCAGGGATGAGTCCCAGTACTTCCGCTTTCATGCTGACGAGGAG
ATGGAGGGGACCAGCAGCAAGAACAAACAGCTTCGCAACGACTTCAAGCTGGTGGAGAAC
ATTCTGGCCAAGCGCCTGCTGATCCTGCCCCAGGAGGAGGACTATGGCTTTGACATCGAG
GAGAAGAACAAGGCTGTGGTGGTGAAGTCCGTCCAGAGGGGCTCGCTGGCTGAGGTGGCT
GGCCTGCAGGTGGGGAGGAAGATCTACTCCATCAATGAGGACCTGGTGTTCCTGCGGCCG
TTTTCAGAGGTGGAGTCCATCCTCAACCAGTCCTTCTGCTCCCGCCGCCCTCTGCGCCTC
CTGGTGGCCACGAAGGCCAAAGAGATCATCAAAATCCCCGACCAGCCGGACACACTGTGC
TTCCAGATTCGTGGAGCTGCCCCACCGTACGTCTATGCTGTGGGGAGAGGCTCTGAGGCC
ATGGCTGCAGGGCTCTGTGCTGGTCAGTGCATTCTGAAGGTCAATGGCAGCAACGTGATG
AACGATGGTGCCCCTGAGGTCCTGGAGCACTTCCAGGCATTCCGGAGTCGGCGCGAAGAG
GCCCTGGGCCTGTACCAGTGGATCTACCACACCCATGAGGATGCCCAGGAAGCACGAGCC
AGTCAGGAGGCCTCCACTGAGGACCCCAGTGGCGAGCAGGCCCAGGAGGAAGACCAGGCT
GATTCAGCCTTCCCACTGCTGTCCCTGGGTCCCCGGCTGAGCCTGTGTGAGGACAGCCCC
ATGGTCACCCTGACTGTGGACAACGTGCACCTGGAACACGGCGTGGTGTATGAGTATGTG
AGCACGGCAGGCGTCAGGTGCCATGTGCTGGAGAAGATCGTGGAGCCCCGCGGCTGCTTC
GGCCTCACCGCCAAGATCCTCGAGGCCTTTGCTGCCAATGACAGCGTCTTCGTGGAGAAC
TGCAGGCGGCTCATGGCCCTGAGCAGCGCCATCGTGACCATGCCCCACTTTGAGTTCCGC
AACATCTGTGACACCAAGCTGGAGAGCATTGGCCAGAGGATTGCCTGCTACCAGGAGTTT
GCAGCCCAACTGAAGAGCAGGGTCAGCCCACCCTTCAAACAAGCCCCCCTGGAGCCCCAC
CCGCTGTGTGGCCTGGACTTCTGCCCCACCAATTGCCACATCAACCTCATGGAAGTGTCC
TACCCCAAGACCACCCCCTCAGTGGGCAGGTCCTTCAGCATCCGCTTTGGACGCAAACCC
TCCCTCATCGGCCTTGACCCGGAGCAAGGCCACCTGAACCCCATGTCGTACACCCAGCAC
TGCATCACCACCATGGCTGCTCCCTCCTGGAAGTGCTTGCCTGCTGCAGAGGGTGATCCC
CAAGGCCAGGGTCTCCATGATGGCAGCTTCGGGCCAGCCAGTGGGACCCTTGGTCAGGAA
GACCGGGGCCTCAGCTTCCTACTCAAGCAGGAGGACCGTGAGATCCAGGATGCCTACCTG
CAGCTCTTCACCAAGCTGGATGTGGCCCTGAAGGAGATGAAGCAATATGTCACCCAGATC
AACAGGCTGCTGTCCACCATCACAGAGCCCACCTCGGGTGGGTCCTGCGACGCATCCTTG
GCTGAGGAGGCCTCCTCCCTGCCCCTGGTCAGTGAAGAGAGCGAGATGGACAGGAGTGAC
CATGGGGGCATCAAGAAGGTGTGCTTCAAGGTGGCCGAGGAGGACCAGGAGGACTCAGGC
CACGACACCATGAGTTATCGCGACTCCTACAGCGAGTGTAACAGCAATCGAGACTCGGTC
CTGTCCTACACCAGCGTGAGAAGTAACAGCTCCTACTTGGGCAGCGACGAGATGGGGTCT
GGAGATGAGCTGCCCTGTGACATGCGGATCCCATCTGACAAGCAGGACAAGCTTCATGGC
TGCCTGGAGCACCTCTTTAACCAGGTGGACTCCATCAATGCTCTCCTCAAGGGGCCAGTC
ATGAGCCGGGCTTTCGAAGAGACCAAGCATTTCCCTATGAACCACAGCTTACAAGAGTTT
AAACAGAAAGAAGAGTGTACAATCCGTGGCCGGAGCCTGATCCAGATTAGCATCCAGGAG
GACCCCTGGAACCTCCCCAACTCCATCAAGACCCTGGTGGACAACATTCAGAGATATGTG
GAAGATGGGAAGAACCAGCTGCTCCTGGCCTTGCTGAAGTGCACAGACACGGAGCTGCAG
CTGCGCAGAGACGCGATCTTCTGCCAGGCCCTGGTGGCCGCCGTGTGCACCTTCTCCGAG
CAGCTGCTGGCGGCCCTGGGCTACCGCTACAACAACAATGGCGAGTACGAGGAGAGCAGC
CGCGACGCCAGCCGCAAGTGGCTGGAGCAGGTGGCGGCCACGGGCGTCCTGCTGCACTGC
CAGTCCCTGCTCTCGCCAGCCACAGTGAAGGAGGAACGGACCATGCTGGAGGACATCTGG
GTGACGCTGTCAGAGCTGGACAATGTCACCTTCTCCTTTAAGCAGCTGGACGAGAACTAT
GTGGCCAACACCAACGTCTTCTACCACATTGAGGGCAGCCGGCAGGCGCTGAAGGTCATC
TTCTACCTCGACAGCTACCACTTCTCCAAGCTGCCCTCCCGCCTGGAGGGTGGGGCCAGC
CTGAGGCTGCACACAGCGCTGTTCACGAAAGTGCTGGAGAACGTGGAGGGGCTGCCTTCT
CCAGGCAGCCAGGCCGCGGAGGATTTGCAGCAGGACATCAACGCGCAGTCCCTGGAGAAA
GTTCAGCAGTATTACCGCAAACTCAGGGCATTTTACCTGGAGCGGTCTAACCTGCCCACG
GATGCCAGCACCACGGCGGTAAAGATAGACCAGCTGATCCGCCCCATCAATGCCCTGGAT
GAGCTCTGCCGCCTCATGAAGTCCTTTGTCCACCCAAAGCCTGGTGCTGCTGGGAGTGTG
GGCGCCGGCCTCATCCCCATCTCCTCGGAGCTCTGCTACCGCCTGGGGGCCTGCCAGATG
GTCATGTGTGGCACAGGCATGCAGAGGAGCACCCTGAGCGTGTCCCTGGAGCAGGCGGCC
ATCTTGGCACGGAGCCACGGGTTGCTGCCCAAGTGCATCATGCAGGCCACGGACATCATG
CGGAAGCAGGGCCCAAGGGTGGAGATTCTGGCCAAAAACCTGCGAGTCAAGGACCAGATG
CCCCAGGGTGCTCCGCGCCTCTACCGCCTCTGCCAGCCGCCGGTGGATGGGGACCTCTGA
Enzyme 120 GenBank Gene ID NM_020820.3 Link Image
Enzyme 120 GeneCard ID PREX1 Link Image
Enzyme 120 GenAtlas ID PREX1 Link Image
Enzyme 120 HGNC ID HGNC:32594 Link Image
Enzyme 120 Chromosome Location 2
Enzyme 120 Locus 20q13.13
Enzyme 120 SNPs SNPJam Report Link Image
Enzyme 120 General References
  1. Welch HC, Coadwell WJ, Ellson CD, Ferguson GJ, Andrews SR, Erdjument-Bromage H, Tempst P, Hawkins PT, Stephens LR: P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-nucleotide exchange factor for Rac. Cell. 2002 Mar 22;108(6):809-21. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  4. Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Feb 28;7(1):65-73. [PubMed Link Image]
  5. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
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Enzyme 120 Metabolite References Not Available
Enzyme 121 [top]
Enzyme 121 ID 13091
Enzyme 121 Name Adenylate cyclase 1
Enzyme 121 Synonyms
  1. Brain
Enzyme 121 Gene Name ADCY1
Enzyme 121 Protein Sequence >Adenylate cyclase 1
MAGAPRGGGGGGGGAGEPGGAERAAGTSRRRGLRACDEEFACPELEALFRGYTLRLEQAA
TLKALAVLSLLAGALALAELLGAPGPAPGLAKGSHPVHCVLFLALLVVTNVRSLQVPQLQ
QVGQLALLFSLTFALLCCPFALGGPARGSAGAAGGPATAEQGVWQLLLVTFVSYALLPVR
SLLAIGFGLVVAASHLLVTATLVPAKRPRLWRTLGANALLFVGVNMYGVFVRILTERSQR
KAFLQARSCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDFLKPPERIFHKIYIQRHD
NVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGL
TQPKTDHAHCCVEMGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWS
NDVTLANVMEAAGLPGKVHITKTTLACLNGDYEVEPGYGHERNSFLKTHNIETFFIVPSH
RRKIFPGLILSDIKPAKRMKFKTVCYLLVQLMHCRKMFKAEIPFSNVMTCEDDDKRRALR
TASEKLRNRSSFSTNVVYTTPGTRVNRYISRLLEARQTELEMADLNFFTLKYKHVEREQK
YHQLQDEYFTSAVVLTLILAALFGLVYLLIFPQSVVVLLLLVFCICFLVACVLYLHITRV
QCFPGCLTIQIRTVLCIFIVVLIYSVAQGCVVGCLPWAWSSKPNSSLVVLSSGGQRTALP
TLPCESTHHALLCCLVGTLPLAIFFRVSSLPKMILLSGLTTSYILVLELSGYTRTGGGAV
SGRSYEPIVAILLFSCALALHARQVDIRLRLDYLWAAQAEEEREDMEKVKLDNRRILFNL
LPAHVAQHFLMSNPRNMDLYYQSYSQVGVMFASIPNFNDFYIELDGNNMGVECLRLLNEI
IADFDELMEKDFYKDIEKIKTIGSTYMAAVGLAPTSGTKAKKSISSHLSTLADFAIEMFD
VLDEINYQSYNDFVLRVGINVGPVVAGVIGARRPQYDIWGNTVNVASRMDSTGVQGRIQV
TEEVHRLLRRCPYHFVCRGKVSVKGKGEMLTYFLEGRTDGNGSQIRSLGLDRKMCPFGRA
GLQGRRPPVCPMPGVSVRAGLPPHSPGQYLPSAAAGKEA
Enzyme 121 Number of Residues 1119
Enzyme 121 Molecular Weight 123442
Enzyme 121 Theoretical pI 8.49
Enzyme 121 GO Classification
Function
  • catalytic activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cell communication
  • cellular metabolism
  • cellular process
  • cyclic nucleotide biosynthesis
  • intracellular signaling cascade
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide biosynthesis
  • nucleotide