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Human Metabolome Database Version 2.5

 

Showing metabocard for Guanosine monophosphate (HMDB01397)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-06 12:57:46
Accession Number HMDB01397
Secondary Accession Numbers Not Available
Common Name Guanosine monophosphate
Description Guanosine 5'-monophosphate. A guanine nucleotide containing one phosphate group esterified to the sugar moiety and found widely in nature.
Synonyms
  1. 5'-GMP
  2. E 626
  3. GMP
  4. Guanidine monophosphate
  5. Guanosine 5'-monophosphate
  6. Guanosine 5'-phosphate
  7. Guanosine 5'-phosphorate
  8. Guanosine 5'-phosphoric acid
  9. guanosine monophosphate
  10. guanosine-5'-monophosphate
  11. guanosine-5'-phosphate
  12. guanosine-phosphate
  13. guanylate
  14. guanylic acid
Chemical IUPAC Name [5-(2-amino-6-oxo-3H-purin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methoxyphosphonic acid
Chemical Formula C10H14N5O8P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide monophosphates
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
  • Second messenger
  • Component of Glutamate metabolism
  • Component of Purine metabolism
  • Component of Pyrimidine metabolism
Application
Source
  • Endogenous
Average Molecular Weight 363.221
Monoisotopic Molecular Weight 363.058014
Isomeric SMILES NC1=NC2=C(N=CN2[C@@H]2O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]2O)C(=O)N1
Canonical SMILES NC1=NC2=C(N=CN2C2OC(COP(O)(O)=O)C(O)C2O)C(=O)N1
KEGG Compound ID C00144 Link Image
BioCyc ID GMP Link Image
BiGG ID 34024 Link Image
Wikipedia Link GMP Link Image
NuGOwiki Link HMDB01397 Link Image
Metagene Link HMDB01397 Link Image
METLIN ID 6216 Link Image
PubChem Compound 6804 Link Image
PubChem Substance 830674 Link Image
ChEBI ID 17345 Link Image
CAS Registry Number 85-32-5
InChI Identifier InChI=1/C10H14N5O8P/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(23-9)1-22-24(19,20)21/h2-3,5-6,9,16-17H,1H2,(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1
Synthesis Reference Sato, Katsuaki; Matsui, Hiroshi; Ei, Hitoshi; Takinami, Koichi. Guanosine-5'-monophosphate. Jpn. Kokai Tokkyo Koho (1979), 3 pp.
Melting Point (Experimental) Not Available
Experimental Water Solubility 369 mg/mL [sodium salt, HMP experimental] Source: PhysProp
Predicted Water Solubility 13.0 mg/mL [MEYLAN,WM et al. (1996)]; 3.56 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.99 [Predicted by ALOGPS]; -3.3 [Predicted by PubChem via XLOGP]; -2.00 [MEYLAN,WM & HOWARD,PH (1995)] 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 1A97 Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • Extracellular
  • golgi apparatus
  • lysosome
  • mitochondria
  • nucleus
Biofluid Location
  • Blood
Tissue Location
Tissue References
Bladder
Epidermis
Heart
Intestine
Nerve Cells
Neuron
Platelet
Smooth Muscle
Concentrations (Normal)
Biofluid Blood
Value 0.0099 +/- 0.0024 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 0.0095 +/- 0.0021 uM
Age Adult:>18 yrs old
Sex Female
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.
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Glutamate Metabolism SMP00072 Link Image map00250 Link Image
Purine Metabolism SMP00050 Link Image map00230 Link Image
Transcription/Translation SMP00019 Link Image
General References
  1. Matata BM, Galinanes M: Effect of diabetes on nitric oxide metabolism during cardiac surgery. Diabetes. 2001 Nov;50(11):2603-10. [PubMed Link Image]
  2. Sales ME, Espanol AJ, Sterin-Borda L, Borda E, de Bracco MM: Protein kinase C regulates NO-cGMP pathway in muscarinic receptor activation by HIV+-IgA. Int J Mol Med. 1999 Jun;3(6):633-7. [PubMed Link Image]
  3. Scheen AJ: [Medication of the month. Vardenafil (Levitra)] Rev Med Liege. 2003 Sep;58(9):576-9. [PubMed Link Image]
  4. Boehning D, Moon C, Sharma S, Hurt KJ, Hester LD, Ronnett GV, Shugar D, Snyder SH: Carbon monoxide neurotransmission activated by CK2 phosphorylation of heme oxygenase-2. Neuron. 2003 Sep 25;40(1):129-37. [PubMed Link Image]
  5. Begonja AJ, Gambaryan S, Geiger J, Aktas B, Pozgajova M, Nieswandt B, Walter U: Platelet NAD(P)H-oxidase-generated ROS production regulates alphaIIbbeta3-integrin activation independent of the NO/cGMP pathway. Blood. 2005 Oct 15;106(8):2757-60. Epub 2005 Jun 23. [PubMed Link Image]
  6. Favory R, Lancel S, Tissier S, Mathieu D, Decoster B, Neviere R: Myocardial dysfunction and potential cardiac hypoxia in rats induced by carbon monoxide inhalation. Am J Respir Crit Care Med. 2006 Aug 1;174(3):320-5. Epub 2006 May 11. [PubMed Link Image]
  7. Yildiz O, Gul H, Ozgok Y, Onguru O, Kilciler M, Aydin A, Isimer A, Harmankaya AC: Increased vasoconstrictor reactivity and decreased endothelial function in high grade varicocele; functional and morphological study. Urol Res. 2003 Oct;31(5):323-8. Epub 2003 Jul 11. [PubMed Link Image]
  8. Seftel AD: Phosphodiesterase type 5 inhibitor differentiation based on selectivity, pharmacokinetic, and efficacy profiles. Clin Cardiol. 2004 Apr;27(4 Suppl 1):I14-19. [PubMed Link Image]
  9. Salomon P, Przewlocka-Kosmala M, Orda A: [Plasma levels of brain natriuretic peptide, cyclic 3'5'-guanosine monophosphate, endothelin 1, and noradrenaline in patients with chronic congestive heart failure] Pol Arch Med Wewn. 2003 Jan;109(1):43-8. [PubMed Link Image]
  10. Khush KK, De Marco T, Vakharia KT, Harmon C, Fineman JR, Chatterjee K, Michaels AD: Nesiritide acutely increases pulmonary and systemic levels of nitric oxide in patients with pulmonary hypertension. J Card Fail. 2006 Sep;12(7):507-13. [PubMed Link Image]
  11. Yoshimura N, Seki S, Chancellor MB, de Groat WC, Ueda T: Targeting afferent hyperexcitability for therapy of the painful bladder syndrome. Urology. 2002 May;59(5 Suppl 1):61-7. [PubMed Link Image]
  12. Ralph DJ: Normal erectile function. Clin Cornerstone. 2005;7(1):13-8. [PubMed Link Image]
  13. Rosen RC, McKenna KE: PDE-5 inhibition and sexual response: pharmacological mechanisms and clinical outcomes. Annu Rev Sex Res. 2002;13:36-88. [PubMed Link Image]
  14. Zhao L, Gray L, Leonardi-Bee J, Weaver CS, Heptinstall S, Bath PM: Effect of aspirin, clopidogrel and dipyridamole on soluble markers of vascular function in normal volunteers and patients with prior ischaemic stroke. Platelets. 2006 Mar;17(2):100-4. [PubMed Link Image]
  15. Zusman RM, Morales A, Glasser DB, Osterloh IH: Overall cardiovascular profile of sildenafil citrate. Am J Cardiol. 1999 Mar 4;83(5A):35C-44C. [PubMed Link Image]
  16. Hamed EA, Meki AR, Gaafar AA, Hamed SA: Role of some vasoactive mediators in patients with erectile dysfunction: their relationship with angiotensin-converting enzyme and growth hormone. Int J Impot Res. 2003 Dec;15(6):418-25. [PubMed Link Image]
  17. Ehsan A, Sommer F, Schmidt A, Klotz T, Koslowski J, Niggemann S, Jacobs G, Engelmann U, Addicks K, Bloch W: Nitric oxide pathways in human bladder carcinoma. The distribution of nitric oxide synthases, soluble guanylyl cyclase, cyclic guanosine monophosphate, and nitrotyrosine. Cancer. 2002 Dec 1;95(11):2293-301. [PubMed Link Image]
  18. Lepore JJ, Maroo A, Bigatello LM, Dec GW, Zapol WM, Bloch KD, Semigran MJ: Hemodynamic effects of sildenafil in patients with congestive heart failure and pulmonary hypertension: combined administration with inhaled nitric oxide. Chest. 2005 May;127(5):1647-53. [PubMed Link Image]
  19. Kekilli M, Beyazit Y, Purnak T, Dogan S, Atalar E: Acute myocardial infarction after sildenafil citrate ingestion. Ann Pharmacother. 2005 Jul-Aug;39(7-8):1362-4. Epub 2005 May 24. [PubMed Link Image]
  20. Ivanovic Z, Duchez P, Dazey B, Hermitte F, Lamrissi-Garcia I, Mazurier F, Praloran V, Reiffers J, Vezon G, Boiron JM: A clinical-scale expansion of mobilized CD 34+ hematopoietic stem and progenitor cells by use of a new serum-free medium. Transfusion. 2006 Jan;46(1):126-31. [PubMed Link Image]
  21. Wikipedia Link Image
Metabolic Enzymes
  1. Cytosolic 5'-nucleotidase 1B
  2. Cytosolic 5'-nucleotidase 1A
  3. 5'(3')-deoxyribonucleotidase, cytosolic type
  4. 5'(3')-deoxyribonucleotidase, mitochondrial
  5. Cytosolic purine 5'-nucleotidase
  6. Ectonucleoside triphosphate diphosphohydrolase 1
  7. Soluble calcium-activated nucleotidase 1
  8. Ectonucleoside triphosphate diphosphohydrolase 3
  9. Inosine triphosphate pyrophosphatase
  10. Adenine phosphoribosyltransferase
  11. Hypoxanthine-guanine phosphoribosyltransferase
  12. Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
  13. Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
  14. High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A
  15. Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
  16. cGMP-inhibited 3',5'-cyclic phosphodiesterase B
  17. Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'
  18. GMP synthase [glutamine-hydrolyzing]
  19. cGMP-inhibited 3',5'-cyclic phosphodiesterase A
  20. cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
  21. Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
  22. cAMP-specific 3',5'-cyclic phosphodiesterase 4B
  23. cAMP-specific 3',5'-cyclic phosphodiesterase 7B
  24. High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
  25. cGMP-dependent 3',5'-cyclic phosphodiesterase
  26. Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
  27. Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
  28. High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B
  29. cAMP-specific 3',5'-cyclic phosphodiesterase 4C
  30. Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
  31. cAMP-specific 3',5'-cyclic phosphodiesterase 4D
  32. Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
  33. Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
  34. cAMP-specific 3',5'-cyclic phosphodiesterase 4A
  35. cGMP-specific 3',5'-cyclic phosphodiesterase
  36. GMP reductase 2
  37. GMP reductase 1
  38. Guanylate kinase
  39. Atrial natriuretic peptide receptor 2
  40. Atrial natriuretic peptide receptor 1
  41. Heat-stable enterotoxin receptor
  42. Cyclic nucleotide-gated cation channel alpha-3
  43. Rap guanine nucleotide exchange factor 2
  44. Rho guanine nucleotide exchange factor 1
  45. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
  46. Ras-related C3 botulinum toxin substrate 1
  47. Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
  48. Proto-oncogene DBL
  49. Cell division control protein 42 homolog
  50. Ras-related C3 botulinum toxin substrate 2
  51. Vinexin
  52. GTPase HRas
  53. Rho-related GTP-binding protein RhoQ
  54. Guanine nucleotide-binding protein G(q) subunit alpha
  55. Guanine nucleotide-binding protein subunit alpha-11
  56. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-11
  57. Guanine nucleotide-binding protein G(t) subunit alpha-1
  58. Protein ALEX
  59. Rap guanine nucleotide exchange factor 3
  60. Lysophosphatidic acid receptor 2
  61. Rap guanine nucleotide exchange factor 4
  62. Cytosolic 5'-nucleotidase 3
  63. ENTPD4 protein
  64. Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A
  65. Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
  66. Guanine monphosphate synthetase, isoform CRA_b
  67. Ectonucleoside triphosphate diphosphohydrolase 8
  68. Synembryn-B
  69. Rap guanine nucleotide exchange factor 6
  70. Neuroepithelial cell-transforming gene 1 protein
  71. Cell cycle progression protein 1
  72. Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein
  73. Dedicator of cytokinesis protein 10
  74. Dedicator of cytokinesis protein 1
  75. Dedicator of cytokinesis protein 2
  76. Dedicator of cytokinesis protein 3
  77. Dedicator of cytokinesis protein 4
  78. Dedicator of cytokinesis protein 5
  79. Dedicator of cytokinesis protein 6
  80. Dedicator of cytokinesis protein 7
  81. Dedicator of cytokinesis protein 8
  82. GTPase-activating protein and VPS9 domain-containing protein 1
  83. Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
  84. Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2
  85. Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3
  86. Guanine nucleotide-binding protein subunit beta-4
  87. Guanine nucleotide-binding protein subunit beta-5
  88. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10
  89. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12
  90. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13
  91. Guanine nucleotide-binding protein G(T) subunit gamma-T1
  92. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3
  93. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-4
  94. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5
  95. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7
  96. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-8
  97. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-T2
  98. Guanine nucleotide-binding protein-like 1
  99. Probable E3 ubiquitin-protein ligase HERC1
  100. Eukaryotic translation initiation factor 5
  101. IQ motif and SEC7 domain-containing protein 1
  102. Guanine nucleotide exchange factor DBS
  103. Ras-related protein Rab-5A
  104. Ras-related protein Rab-5B
  105. Ran-binding protein 3
  106. Ral guanine nucleotide dissociation stimulator-like 2
  107. Ral guanine nucleotide dissociation stimulator-like 3
  108. Synembryn-A
  109. Ras and Rab interactor 1
  110. Ras and Rab interactor 2
  111. Ras and Rab interactor 3
  112. GTP-binding protein Rit1
  113. GTP-binding protein Rit2
  114. Rap guanine nucleotide exchange factor 5
  115. Ras-related GTP-binding protein A
  116. Ras-related GTP-binding protein B
  117. Ras-related GTP-binding protein C
  118. Ras-related GTP-binding protein D
  119. Secretion-regulating guanine nucleotide exchange factor
  120. T-lymphoma invasion and metastasis-inducing protein 2
  121. Protein XRP2
  122. Rho-related GTP-binding protein RhoU
  123. cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
  124. 3',5'-cyclic nucleotide phosphodiesterase 10A2
  125. Putative uncharacterized protein DKFZp761J1915 (Ectonucleoside triphosphate diphosphohydrolase 6 (Putative function), isoform CRA_a)
  126. Ectonucleoside triphosphate diphosphohydrolase 5
  127. cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
  128. Phosphodiesterase 7B (Phosphodiesterase 7B, isoform CRA_b)
  129. cDNA FLJ38065 fis, clone CTONG2015316, highly similar to cAMP-specific 3',5'-cyclic phosphodiesterase 4C (EC 3.1.4.17)
  130. cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
  131. Guanine nucleotide-binding protein G(i) subunit alpha-1
  132. Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas
  133. Guanine nucleotide exchange factor VAV2
  134. Rho-guanine nucleotide exchange factor
  135. Ras guanyl-releasing protein 3
  136. Protein RCC2
  137. Protein very KIND
  138. Guanine nucleotide binding protein (G protein), gamma transducing activity polypeptide 1
  139. Abl interactor 1
  140. GTP-binding protein SAR1b
  141. Ras-GEF domain-containing family member 1A
  142. G-protein-signaling modulator 1
  143. GTP-binding protein GEM
  144. Rap guanine nucleotide exchange factor-like 1
  145. Guanine nucleotide binding protein-like 1
  146. Rho guanine nucleotide exchange factor 6
  147. Guanine nucleotide binding protein (G protein), alpha 13, isoform CRA_a
  148. cDNA, FLJ92996, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta polypeptide 1 (GNB1), mRNA
  149. Guanine nucleotide-binding protein subunit alpha-14
  150. PH and SEC7 domain-containing protein 4
  151. Rho guanine nucleotide exchange factor 9
  152. Guanine nucleotide-binding protein G(k) subunit alpha
  153. Epithelial cell-transforming sequence 2 oncogene-like
  154. cDNA, FLJ95645, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta 5(GNB5), transcript variant 1, mRNA
  155. Pleckstrin homology domain-containing family G member 6
  156. Guanine nucleotide-binding protein G(i) subunit alpha-2
  157. cDNA FLJ78228, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta 5(GNB5), transcript variant 1, mRNA
  158. Guanine nucleotide binding protein (G protein), beta polypeptide 1
  159. Guanine nucleotide-binding protein G(t) subunit alpha-2
  160. Rho guanine nucleotide exchange factor 37
  161. PH and SEC7 domain-containing protein 3
  162. PH and SEC7 domain-containing protein 1
  163. Guanine nucleotide-binding protein G(o) subunit alpha
  164. Ras-GEF domain-containing family member 1B
  165. Rho guanine nucleotide exchange factor 18
  166. ALS2 C-terminal-like protein
  167. Switch-associated protein 70
  168. Ras-specific guanine nucleotide-releasing factor RalGPS2
  169. FERM, RhoGEF and pleckstrin domain-containing protein 2
  170. Ral guanine nucleotide dissociation stimulator-like 1
  171. Guanine nucleotide-binding protein subunit alpha-13
  172. Vav-like protein C9orf100
  173. Probable guanine nucleotide exchange factor MCF2L2
  174. Rho guanine nucleotide exchange factor 7
  175. Guanine nucleotide binding protein (G protein), alpha 14
  176. Guanine nucleotide binding protein-like 1
  177. Guanine nucleotide binding protein (G protein), alpha activating activity polypeptide, olfactory type, isoform CRA_b
  178. Guanine nucleotide-binding protein subunit alpha-12
  179. Ras-specific guanine nucleotide-releasing factor RalGPS1
  180. Rho guanine nucleotide exchange factor 11
  181. cDNA FLJ76843, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), alpha 15 (Gq class) (GNA15), mRNA
  182. Growth factor receptor-bound protein 2
  183. Guanine nucleotide binding protein (G protein), beta polypeptide 1
  184. Rho guanine nucleotide exchange factor 10-like protein
  185. Guanine nucleotide binding protein (G protein), q polypeptide
  186. Protein SOLO
  187. Prolactin regulatory element-binding protein
  188. Rho guanine nucleotide exchange factor 4
  189. Not Available
  190. Guanine nucleotide exchange factor for Rab-3A
  191. cDNA FLJ77654, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta polypeptide 4 (GNB4), mRNA
  192. Guanine nucleotide binding protein-like 1
  193. Engulfment and cell motility protein 1
  194. GRB2-related adapter protein
  195. Guanine nucleotide-binding protein G(z) subunit alpha
  196. Engulfment and cell motility protein 3
  197. Guanine nucleotide exchange factor GEFT
  198. Differentially expressed in FDCP 6 homolog
  199. Alpha-catulin
  200. Guanine nucleotide binding protein (G protein), beta polypeptide 1
  201. IQ motif and SEC7 domain-containing protein 3
  202. Engulfment and cell motility protein 2
  203. Rho guanine nucleotide exchange factor 17
  204. Ras-GEF domain-containing family member 1C
  205. Rho guanine nucleotide exchange factor 12
  206. Ephexin-1
  207. Guanine nucleotide binding protein-like 1
  208. Guanine nucleotide-binding protein G(olf) subunit alpha
  209. Guanine nucleotide-binding protein subunit alpha-15
  210. Rho guanine nucleotide exchange factor 3
Enzyme 1 [top]
Enzyme 1 ID 5232
Enzyme 1 Name Cytosolic 5'-nucleotidase 1B
Enzyme 1 Synonyms
  1. cN1B
  2. Autoimmune infertility-related protein
  3. Cytosolic 5'-nucleotidase IB
  4. cN-IB
Enzyme 1 Gene Name NT5C1B
Enzyme 1 Protein Sequence >Cytosolic 5'-nucleotidase 1B
MSQTSLKQKKNEPGMRSSKESLEAEKRKESDKTGVRLSNQMRRAVNPNHSLRCCPFQGHS
SCRRCLCAAEGTALGPCHTIRIYIHMCLLWEQGQQITMMRGSQESSLRKTDSRGYLVRSQ
WSRISRSPSTKAPSIDEPRSRNTSAKLPSSSTSSRTPSTSPSLHDSSPPPLSGQPSLQPP
ASPQLPRSLDSRPPTPPEPDPGSRRSTKMQENPEAWAQGIVREIRQTRDSQPLEYSRTSP
TEWKSSSQRRGIYPASTQLDRNSLSEQQQQQREDEDDYEAAYWASMRSFYEKNPSCSRPW
PPKPKNAITIALSSCALFNMVDGRKIYEQEGLEKYMEYQLTNENVILTPGPAFRFVKALQ
YVNARLRDLYPDEQDLFDIVLMTNNHAQVGVRLINSVNHYGLLIDRFCLTGGKDPIGYLK
AYLTNLYIAADSEKVQEAIQEGIASATMFDGAKDMAYCDTQLRVAFDGDAVLFSDESEHF
TKEHGLDKFFQYDTLCESKPLAQGPLKGFLEDLGRLQKKFYAKNERLLCPIRTYLVTARS
AASSGARVLKTLRRWGLEIDEALFLAGAPKSPILVKIRPHIFFDDHMFHIEGAQRLGSIA
AYGFNKKFSS
Enzyme 1 Number of Residues 610
Enzyme 1 Molecular Weight 68803.1
Enzyme 1 Theoretical pI 9.03
Enzyme 1 GO Classification
Function
  • 5'-nucleotidase activity
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleotidase activity
  • nucleotide binding
  • phosphatase activity
  • phosphoric ester hydrolase activity
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
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 1 General Function Involved in nucleotide binding
Enzyme 1 Specific Function Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Helps to regulate adenosine levels
Enzyme 1 Pathways
Enzyme 1 Reactions
  • a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate [RN:R07297]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 50593110 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q96P26 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name 5NT1B_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1833 bp
ATGAGTCAAACATCTCTCAAACAGAAAAAGAATGAGCCTGGAATGAGGTCCTCAAAAGAG
AGTCTAGAAGCAGAAAAAAGAAAGGAATCTGACAAAACAGGAGTTCGTCTGAGCAATCAG
ATGAGGCGTGCAGTCAATCCGAATCACTCGCTGAGATGTTGCCCCTTCCAGGGTCACTCG
TCGTGTAGACGCTGCCTTTGTGCAGCTGAGGGAACAGCCCTTGGCCCCTGCCACACAATA
CGTATTTATATTCACATGTGCCTGTTGTGGGAGCAGGGCCAGCAGATCACCATGATGAGG
GGATCACAAGAATCATCACTGCGGAAGACAGACTCTCGAGGGTACCTTGTGCGCAGTCAA
TGGTCTAGAATATCCCGGAGCCCATCCACCAAGGCTCCATCCATAGATGAGCCTAGAAGC
AGGAACACCAGTGCTAAGCTCCCCAGCAGCTCCACGAGCTCCCGGACTCCATCCACCTCC
CCAAGCCTGCATGACTCCTCACCGCCGCCGCTGTCCGGGCAGCCCTCGCTCCAGCCACCC
GCGTCGCCCCAGCTGCCCCGGTCGCTGGACTCGCGGCCTCCCACGCCCCCAGAGCCCGAT
CCTGGCTCCCGGCGCAGCACCAAAATGCAAGAGAATCCGGAGGCCTGGGCCCAAGGCATC
GTGCGGGAAATCCGCCAGACCCGGGACTCGCAGCCGCTGGAATATTCGCGCACGTCCCCC
ACCGAGTGGAAGTCCTCCAGCCAGCGCAGGGGGATCTACCCCGCCTCCACCCAGCTGGAC
CGCAACTCTCTGTCCGAGCAGCAGCAGCAGCAGCGGGAGGACGAGGACGACTACGAGGCT
GCCTACTGGGCATCCATGAGGTCGTTCTACGAGAAGAACCCGAGCTGCTCGCGCCCCTGG
CCGCCCAAACCCAAGAACGCCATCACCATTGCTCTCTCATCCTGCGCGCTCTTCAACATG
GTGGACGGCAGGAAAATCTACGAGCAAGAGGGTCTGGAAAAGTACATGGAGTATCAGCTC
ACCAATGAGAACGTCATCCTGACCCCGGGCCCGGCGTTCCGCTTCGTCAAGGCACTACAG
TATGTCAATGCTAGACTCCGTGATCTATATCCTGATGAACAGGACTTATTTGATATTGTA
CTGATGACTAATAACCATGCCCAAGTGGGAGTGCGGCTTATAAACAGCGTCAATCACTAC
GGCTTACTGATTGACCGCTTCTGTCTGACCGGGGGAAAAGACCCCATTGGCTATTTGAAG
GCATATCTTACCAACTTGTATATTGCTGCAGATTCTGAAAAAGTGCAAGAGGCAATACAA
GAAGGTATTGCCTCTGCGACAATGTTTGATGGAGCCAAAGACATGGCTTACTGTGACACT
CAGCTCCGTGTAGCCTTTGATGGGGATGCTGTCCTCTTCTCTGATGAGTCTGAACATTTT
ACCAAGGAGCATGGGCTCGACAAATTCTTCCAGTATGATACATTATGTGAAAGTAAGCCT
CTTGCTCAGGGTCCCCTAAAAGGCTTTCTGGAAGATTTAGGCAGACTGCAAAAGAAGTTC
TATGCCAAAAATGAACGGTTACTTTGTCCTATCAGGACCTACCTGGTTACAGCTAGGAGT
GCAGCCAGTTCAGGCGCCCGTGTGCTGAAGACCCTTCGACGCTGGGGTCTAGAGATAGAC
GAAGCTCTTTTCCTTGCTGGAGCCCCCAAAAGTCCCATCTTGGTGAAGATCCGGCCCCAC
ATCTTCTTTGATGACCACATGTTCCACATTGAAGGGGCACAGAGGTTAGGTTCCATCGCA
GCTTATGGCTTTAATAAAAAATTCAGTAGTTAG
Enzyme 1 GenBank Gene ID NM_001002006.2 Link Image
Enzyme 1 GeneCard ID NT5C1B Link Image
Enzyme 1 GenAtlas ID NT5C1B Link Image
Enzyme 1 HGNC ID HGNC:17818 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2p24.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 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]
  4. Sala-Newby GB, Newby AC: Cloning of a mouse cytosolic 5'-nucleotidase-I identifies a new gene related to human autoimmune infertility-related protein. Biochim Biophys Acta. 2001 Oct 31;1521(1-3):12-8. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5233
Enzyme 2 Name Cytosolic 5'-nucleotidase 1A
Enzyme 2 Synonyms
  1. cN1A
  2. Cytosolic 5'-nucleotidase IA
  3. cN-I
  4. cN-IA
Enzyme 2 Gene Name NT5C1A
Enzyme 2 Protein Sequence >Cytosolic 5'-nucleotidase 1A
MEPGQPREPQEPREPGPGAETAAAPVWEEAKIFYDNLAPKKKPKSPKPQNAVTIAVSSRA
LFRMDEEQQIYTEQGVEEYVRYQLEHENEPFSPGPAFPFVKALEAVNRRLRELYPDSEDV
FDIVLMTNNHAQVGVRLINSINHYDLFIERFCMTGGNSPICYLKAYHTNLYLSADAEKVR
EAIDEGIAAATIFSPSRDVVVSQSQLRVAFDGDAVLFSDESERIVKAHGLDRFFEHEKAH
ENKPLAQGPLKGFLEALGRLQKKFYSKGLRLECPIRTYLVTARSAASSGARALKTLRSWG
LETDEALFLAGAPKGPLLEKIRPHIFFDDQMFHVAGAQEMGTVAAHVPYGVAQTPRRTAP
AKQAPSAQ
Enzyme 2 Number of Residues 368
Enzyme 2 Molecular Weight 41020.1
Enzyme 2 Theoretical pI 6.52
Enzyme 2 GO Classification
Function
  • 5'-nucleotidase activity
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleotidase activity
  • nucleotide binding
  • phosphatase activity
  • phosphoric ester hydrolase activity
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
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 2 General Function Involved in nucleotide binding
Enzyme 2 Specific Function Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides and has a broad substrate specificity. Helps to regulate adenosine levels in heart during ischemia and hypoxia
Enzyme 2 Pathways
Enzyme 2 Reactions
  • a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate [RN:R07297]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 12659324 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9BXI3 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name 5NT1A_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1107 bp
ATGGAACCTGGGCAGCCCCGGGAGCCCCAGGAGCCCCGCGAGCCCGGGCCAGGAGCGGAG
ACCGCTGCGGCCCCGGTCTGGGAGGAAGCCAAGATTTTCTACGACAACCTCGCGCCCAAG
AAGAAACCCAAATCGCCCAAGCCTCAGAATGCAGTCACCATCGCTGTGTCCTCCCGAGCC
TTGTTTCGCATGGACGAGGAGCAGCAGATCTACACGGAGCAGGGCGTGGAGGAGTACGTG
CGCTACCAGCTGGAACATGAGAACGAACCCTTCAGTCCCGGGCCAGCCTTCCCTTTTGTG
AAGGCTCTGGAGGCCGTGAACAGGCGGCTGCGGGAGCTGTACCCTGATAGTGAGGACGTC
TTCGACATCGTCCTCATGACTAACAACCATGCTCAAGTGGGTGTCCGCCTCATCAACAGT
ATCAACCACTATGACCTGTTCATCGAGAGGTTCTGCATGACAGGTGGGAACAGCCCGATC
TGCTACCTCAAGGCCTATCACACCAACCTCTACTTGTCAGCCGATGCGGAAAAAGTGCGA
GAAGCCATTGATGAGGGGATCGCAGCTGCCACCATCTTCAGCCCCAGCAGGGATGTGGTT
GTGTCCCAGAGTCAGCTGCGCGTGGCCTTCGATGGGGACGCCGTGCTCTTCTCGGACGAG
TCGGAGCGCATCGTCAAGGCCCACGGGCTGGACCGATTCTTCGAGCATGAGAAGGCCCAC
GAGAACAAGCCTCTGGCTCAGGGCCCCTTAAAGGGCTTTCTGGAGGCACTGGGTAGGTTG
CAGAAGAAGTTCTACTCCAAAGGCCTGCGGCTGGAGTGCCCAATTCGTACCTACTTGGTG
ACAGCACGCAGTGCAGCCAGTTCCGGGGCCCGGGCTCTCAAGACCCTGCGCAGCTGGGGC
CTGGAGACAGATGAAGCCTTGTTCCTTGCTGGAGCGCCCAAGGGCCCTCTCCTTGAGAAG
ATCCGCCCACACATCTTCTTTGATGACCAGATGTTCCATGTGGCTGGGGCTCAGGAGATG
GGCACTGTGGCCGCCCATGTGCCTTATGGTGTGGCACAGACACCCCGGCGGACTGCACCT
GCAAAGCAGGCCCCATCTGCACAGTAG
Enzyme 2 GenBank Gene ID AF331801 Link Image
Enzyme 2 GeneCard ID NT5C1A Link Image
Enzyme 2 GenAtlas ID NT5C1A Link Image
Enzyme 2 HGNC ID HGNC:17819 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1p34.3-p33
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Hunsucker SA, Spychala J, Mitchell BS: Human cytosolic 5'-nucleotidase I: characterization and role in nucleoside analog resistance. J Biol Chem. 2001 Mar 30;276(13):10498-504. Epub 2000 Dec 22. [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 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5234
Enzyme 3 Name 5'(3')-deoxyribonucleotidase, cytosolic type
Enzyme 3 Synonyms
  1. Cytosolic 5',3'-pyrimidine nucleotidase
  2. Deoxy-5'-nucleotidase 1
  3. dNT-1
Enzyme 3 Gene Name NT5C
Enzyme 3 Protein Sequence >5'(3')-deoxyribonucleotidase, cytosolic type
MARSVRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRALRPDLADK
VASVYEAPGFFLDLEPIPGALDAVREMNDLPDTQVFICTSPLLKYHHCVGEKYRWVEQHL
GPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSWEHILFTCCHNRHLVLPPTRRRL
LSWSDNWREILDSKRGAAQRE
Enzyme 3 Number of Residues 201
Enzyme 3 Molecular Weight 23382.5
Enzyme 3 Theoretical pI 6.63
Enzyme 3 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphatase activity
  • phosphoric ester hydrolase activity
Process
Component
Enzyme 3 General Function Involved in metal ion binding
Enzyme 3 Specific Function Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 7524492 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q8TCD5 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name NT5C_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >606 bp
ATGGCGCGGAGCGTGCGCGTGCTGGTGGACATGGACGGCGTCCTGGCCGACTTCGAGGCC
GGCCTCCTGCGGGGCTTCCGCCGCCGCTTCCCTGAGGAGCCGCACGTGCCGCTGGAGCAA
CGCCGCGGCTTCCTGGCCCGCGAGCAGTACCGCGCCCTGCGGCCCGACCTGGCGGATAAA
GTGGCCAGTGTGTACGAAGCCCCGGGCTTTTTCCTGGACCTGGAGCCCATCCCGGGAGCC
TTGGACGCTGTGCGGGAGATGAACGACCTACCGGACACGCAGGTCTTCATCTGCACCAGC
CCCCTGCTGAAGTACCACCACTGTGTGGGTGAGAAGTACCGCTGGGTGGAGCAGCACCTG
GGGCCCCAGTTCGTAGAACGAATTATCCTGACAAGGGACAAGACGGTGGTCTTGGGGGAC
CTGCTCATTGATGACAAGGACACAGTTCGAGGCCAGGAGGAGACCCCAAGCTGGGAGCAC
ATCTTGTTCACCTGCTGCCACAATCGGCACCTGGTCCTGCCCCCGACAAGGAGACGGCTG
CTCTCCTGGAGTGACAACTGGAGGGAGATCTTAGATAGCAAGCGCGGAGCTGCGCAGCGG
GAATGA
Enzyme 3 GenBank Gene ID AF154829 Link Image
Enzyme 3 GeneCard ID NT5C Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 17q25.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Rampazzo C, Johansson M, Gallinaro L, Ferraro P, Hellman U, Karlsson A, Reichard P, Bianchi V: Mammalian 5'(3')-deoxyribonucleotidase, cDNA cloning, and overexpression of the enzyme in Escherichia coli and mammalian cells. J Biol Chem. 2000 Feb 25;275(8):5409-15. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. 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. Rampazzo C, Kost-Alimova M, Ruzzenente B, Dumanski JP, Bianchi V: Mouse cytosolic and mitochondrial deoxyribonucleotidases: cDNA cloning of the mitochondrial enzyme, gene structures, chromosomal mapping and comparison with the human orthologs. Gene. 2002 Jul 10;294(1-2):109-17. [PubMed Link Image]
  5. 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]
  6. 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]
  7. Wallden K, Rinaldo-Matthis A, Ruzzenente B, Rampazzo C, Bianchi V, Nordlund P: Crystal structures of human and murine deoxyribonucleotidases: insights into recognition of substrates and nucleotide analogues. Biochemistry. 2007 Dec 4;46(48):13809-18. Epub 2007 Nov 7. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5236
Enzyme 4 Name 5'(3')-deoxyribonucleotidase, mitochondrial
Enzyme 4 Synonyms
  1. 5',3'-nucleotidase, mitochondrial
  2. Deoxy-5'-nucleotidase 2
  3. dNT-2
Enzyme 4 Gene Name NT5M
Enzyme 4 Protein Sequence >5'(3')-deoxyribonucleotidase, mitochondrial
MIRLGGWCARRLCSAAVPAGRRGAAGGLGLAGGRALRVLVDMDGVLADFEGGFLRKFRAR
FPDQPFIALEDRRGFWVSEQYGRLRPGLSEKAISIWESKNFFFELEPLPGAVEAVKEMAS
LQNTDVFICTSPIKMFKYCPYEKYAWVEKYFGPDFLEQIVLTRDKTVVSADLLIDDRPDI
TGAEPTPSWEHVLFTACHNQHLQLQPPRRRLHSWADDWKAILDSKRPC
Enzyme 4 Number of Residues 228
Enzyme 4 Molecular Weight 25861.5
Enzyme 4 Theoretical pI 8.12
Enzyme 4 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphatase activity
  • phosphoric ester hydrolase activity
Process
Component
Enzyme 4 General Function Involved in phosphatase activity
Enzyme 4 Specific Function Dephosphorylates specifically the 5' and 2'(3')- phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID Q9NPB1 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name NT5M_HUMAN Link Image
Enzyme 4 PDB ID 1Q92 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >687 bp
ATGATCCGGCTGGGCGGCTGGTGTGCGCGGCGGCTCTGCAGCGCGGCGGTTCCCGCGGGG
CGGCGCGGGGCGGCGGGCGGGCTGGGCCTGGCGGGAGGCCGCGCCCTACGGGTGCTGGTG
GACATGGACGGCGTGCTGGCTGACTTCGAGGGCGGATTCCTCAGGAAGTTCCGCGCGCGC
TTTCCCGACCAGCCCTTCATCGCGCTGGAGGACCGGCGCGGCTTCTGGGTGTCGGAGCAG
TACGGCCGCCTGCGGCCAGGGCTGAGCGAGAAGGCCATCAGCATTTGGGAGTCAAAGAAT
TTCTTTTTTGAACTTGAGCCTCTGCCAGGGGCCGTGGAAGCTGTCAAGGAGATGGCCAGC
CTACAAAACACTGACGTCTTCATCTGCACAAGCCCCATCAAGATGTTCAAGTACTGTCCC
TATGAGAAGTATGCCTGGGTGGAGAAGTACTTTGGCCCTGACTTTCTGGAGCAGATTGTG
CTGACCAGAGACAAGACCGTGGTCTCTGCTGACCTTCTCATAGACGACCGGCCGGACATC
ACAGGGGCCGAGCCAACCCCCAGCTGGGAGCATGTCCTCTTCACCGCCTGCCACAACCAG
CACCTGCAGCTGCAGCCCCCCCGCCGCAGGCTGCACTCGTGGGCGGACGACTGGAAGGCC
ATTCTGGACAGCAAGCGGCCCTGCTGA
Enzyme 4 GenBank Gene ID AF210652 Link Image
Enzyme 4 GeneCard ID NT5M Link Image
Enzyme 4 GenAtlas ID NT5M Link Image
Enzyme 4 HGNC ID HGNC:15769 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 17p11.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Rampazzo C, Gallinaro L, Milanesi E, Frigimelica E, Reichard P, Bianchi V: A deoxyribonucleotidase in mitochondria: involvement in regulation of dNTP pools and possible link to genetic disease. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8239-44. [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. Rinaldo-Matthis A, Rampazzo C, Reichard P, Bianchi V, Nordlund P: Crystal structure of a human mitochondrial deoxyribonucleotidase. Nat Struct Biol. 2002 Oct;9(10):779-87. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5237
Enzyme 5 Name Cytosolic purine 5'-nucleotidase
Enzyme 5 Synonyms
  1. Cytosolic 5'-nucleotidase II
Enzyme 5 Gene Name NT5C2
Enzyme 5 Protein Sequence >Cytosolic purine 5'-nucleotidase
MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVY
KSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLV
CAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTS
CETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMK
EVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGT
VLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKS
KKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQ
RRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAA
HVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLA
PQEITHCHDEDDDEEEEEEEE
Enzyme 5 Number of Residues 561
Enzyme 5 Molecular Weight 64969.2
Enzyme 5 Theoretical pI 6.05
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Involved in 5'-nucleotidase activity
Enzyme 5 Specific Function May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides
Enzyme 5 Pathways
Enzyme 5 Reactions
  • a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate [RN:R07297]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID P49902 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name 5NTC_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1686 bp
ATGTCGACCTCCTGGAGTGATCGGTTACAGAATGCAGCAGATATGCCTGCTAACATGGAT
AAGCATGCCCTGAAAAAGTATCGTCGAGAAGCCTATCATCGGGTGTTTGTGAACCGAAGT
TTAGCAATGGAAAAGATAAAGTGTTTTGGTTTTGATATGGATTATACCCTTGCTGTGTAC
AAGTCCCCAGAGTATGAGTCCCTTGGTTTTGAGCTTACTGTGGAGAGATTAGTTTCTATT
GGCTATCCCCAGGAGTTGCTCAGCTTTGCTTATGATTCTACATTCCCTACCAGGGGACTT
GTCTTTGACACACTGTATGGAAATCTTTTGAAAGTCGATGCCTATGGAAACCTCTTGGTC
TGTGCACATGGATTTAACTTTATAAGGGGACCAGAAACTAGAGAACAGTATCCAAATAAA
TTTATCCAGCGAGATGATACTGAAAGATTTTACATTCTGAACACACTATTCAACCTACCA
GAGACCTACCTGTTGGCCTGCCTAGTAGATTTTTTTACTAATTGTCCCAGATATACCAGT
TGTGAAACAGGATTTAAAGATGGGGACCTCTTCATGTCCTACCGGAGTATGTTCCAGGAT
GTAAGAGATGCTGTTGACTGGGTTCATTACAAGGGCTCCCTTAAGGAAAAGACAGTTGAA
AATCTTGAGAAGTATGTAGTCAAAGATGGAAAACTGCCTTTGCTTCTGAGCCGGATGAAG
GAAGTAGGGAAAGTATTTCTTGCTACCAACAGTGACTATAAATATACAGATAAAATTATG
ACTTACCTGTTTGACTTCCCACATGGCCCCAAGCCTGGGAGCTCCCATCGACCATGGCAG
TCCTACTTTGACTTGATCTTGGTGGATGCACGGAAACCACTCTTTTTTGGAGAAGGCACA
GTACTGCGTCAGGTGGATACTAAAACTGGCAAGCTGAAAATTGGTACCTACACAGGGCCC
CTACAGCATGGTATCGTCTACTCAGGAGGTTCTTCTGATACGATCTGTGACCTGTTGGGA
GCCAAGGGAAAAGACATTTTGTATATTGGAGATCACATTTTTGGGGACATTTTAAAATCA
AAGAAACGGCAAGGGTGGCGAACTTTTTTGGTGATTCCTGAACTCGCACAGGAGCTACAT
GTCTGGACTGACAAGAGTTCACTTTTCGAAGAACTTCAGAGCTTGGATATTTTCTTGGCT
GAACTCTACAAGCATCTTGACAGCAGTAGCAATGAGCGTCCAGACATCAGTTCCATCCAG
AGACGTATTAAGAAAGTAACTCATGACATGGACATGTGCTATGGGATGATGGGAAGCCTG
TTTCGCAGTGGCTCCCGGCAGACCCTTTTTGCCAGTCAAGTGATGCGTTATGCTGACCTC
TATGCAGCATCTTTCATCAACCTGCTGTATTACCCTTTCAGCTACCTCTTCAGGGCTGCC
CATGTCTTGATGCCTCATGAATCAACGGTGGAGCACACACACGTAGATATCAATGAGATG
GAGTCTCCTCTTGCCACCCGGAACCGCACATCAGTGGATTTCAAAGACACTGACTACAAG
CGGCACCAGCTGACACGGTCAATTAGTGAGATTAAACCTCCCAACCTCTTCCCACTGGCC
CCCCAGGAAATTACACACTGCCATGACGAAGATGATGATGAAGAGGAGGAGGAGGAGGAA
GAATAA
Enzyme 5 GenBank Gene ID D38524 Link Image
Enzyme 5 GeneCard ID NT5C2 Link Image
Enzyme 5 GenAtlas ID NT5C2 Link Image
Enzyme 5 HGNC ID HGNC:8022 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 10q24.32
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Oka J, Matsumoto A, Hosokawa Y, Inoue S: Molecular cloning of human cytosolic purine 5'-nucleotidase. Biochem Biophys Res Commun. 1994 Nov 30;205(1):917-22. [PubMed Link Image]
  2. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  3. 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. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  5. Wallden K, Stenmark P, Nyman T, Flodin S, Graslund S, Loppnau P, Bianchi V, Nordlund P: Crystal structure of human cytosolic 5'-nucleotidase II: insights into allosteric regulation and substrate recognition. J Biol Chem. 2007 Jun 15;282(24):17828-36. Epub 2007 Apr 3. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5313
Enzyme 6 Name Ectonucleoside triphosphate diphosphohydrolase 1
Enzyme 6 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 6 Gene Name ENTPD1
Enzyme 6 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 1
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
Enzyme 6 Number of Residues 510
Enzyme 6 Molecular Weight 57964.1
Enzyme 6 Theoretical pI 6.29
Enzyme 6 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 6 General Function Involved in hydrolase activity
Enzyme 6 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 6 Pathways
Enzyme 6 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 17-37 479-499
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 45580700 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P49961 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name ENTP1_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 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 6 GenBank Gene ID NM_001776.5 Link Image
Enzyme 6 GeneCard ID ENTPD1 Link Image
Enzyme 6 GenAtlas ID ENTPD1 Link Image
Enzyme 6 HGNC ID HGNC:3363 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 10q24
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5314
Enzyme 7 Name Soluble calcium-activated nucleotidase 1
Enzyme 7 Synonyms
  1. SCAN-1
  2. Apyrase homolog
  3. Putative MAPK-activating protein PM09
  4. Putative NF-kappa-B-activating protein 107
Enzyme 7 Gene Name CANT1
Enzyme 7 Protein Sequence >Soluble calcium-activated nucleotidase 1
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
Enzyme 7 Number of Residues 401
Enzyme 7 Molecular Weight 44839.2
Enzyme 7 Theoretical pI 5.98
Enzyme 7 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 7 General Function Involved in calcium ion binding
Enzyme 7 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 7 Pathways
Enzyme 7 Reactions
  • a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 45-62
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 229577440 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q8WVQ1 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name CANT1_HUMAN Link Image
Enzyme 7 PDB ID 1S1D Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 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 7 GenBank Gene ID NM_001159772.1 Link Image
Enzyme 7 GeneCard ID CANT1 Link Image
Enzyme 7 GenAtlas ID CANT1 Link Image
Enzyme 7 HGNC ID HGNC:19721 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 17q25.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5318
Enzyme 8 Name Ectonucleoside triphosphate diphosphohydrolase 3
Enzyme 8 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 8 Gene Name ENTPD3
Enzyme 8 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 3
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
Enzyme 8 Number of Residues 529
Enzyme 8 Molecular Weight 59104.8
Enzyme 8 Theoretical pI 6.40
Enzyme 8 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 8 General Function Involved in hydrolase activity
Enzyme 8 Specific Function Has a threefold preference for the hydrolysis of ATP over ADP
Enzyme 8 Pathways
Enzyme 8 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 23-43 486-506
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 13817037 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID O75355 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name ENTP3_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 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 8 GenBank Gene ID AF034840 Link Image
Enzyme 8 GeneCard ID ENTPD3 Link Image
Enzyme 8 GenAtlas ID ENTPD3 Link Image
Enzyme 8 HGNC ID HGNC:3365 Link Image
Enzyme 8 Chromosome Location 3
Enzyme 8 Locus 3p21.3
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5668
Enzyme 9 Name Inosine triphosphate pyrophosphatase
Enzyme 9 Synonyms
  1. ITPase
  2. Inosine triphosphatase
  3. Putative oncogene protein hlc14-06-p
Enzyme 9 Gene Name ITPA
Enzyme 9 Protein Sequence >Inosine triphosphate pyrophosphatase
MAASLVGKKIVFVTGNAKKLEEVVQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEA
VRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLKPEGLHQLLAGFEDKSAYALCTFAL
STGDPSQPVRLFRGRTSGRIVAPRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFR
ALLELQEYFGSLAA
Enzyme 9 Number of Residues 194
Enzyme 9 Molecular Weight 21445.5
Enzyme 9 Theoretical pI 5.34
Enzyme 9 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 9 General Function Involved in hydrolase activity
Enzyme 9 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 9 Pathways
Enzyme 9 Reactions
  • a nucleoside triphosphate + H2O = a nucleotide + diphosphate [RN:R01532]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 21104378 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q9BY32 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name ITPA_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >585 bp
ATGGCGGCCTCATTGGTGGGGAAGAAGATCGTGTTTGTAACGGGGAACGCCAAGAAGCTG
GAGGAGGTCGTTCAGATTCTAGGAGATAAGTTTCCATGCACTTTGGTGGCACAGAAAATT
GACCTGCCGGAGTACCAAGGGGAGCCGGATGAGATTTCCATACAGAAATGTCAGGAGGCA
GTTCGCCAGGTACAGGGGCCCGTGCTGGTTGAGGACACTTGTCTGTGCTTCAATGCCCTT
GGAGGGCTCCCCGGCCCCTACATAAAGTGGTTTCTGGAGAAGTTAAAGCCTGAAGGTCTC
CACCAGCTCCTGGCCGGGTTCGAGGACAAGTCAGCCTATGCGCTCTGCACGTTTGCACTC
AGCACCGGGGACCCAAGCCAGCCCGTGCGCCTGTTCAGGGGCCGGACCTCGGGCCGGATC
GTGGCACCCAGAGGCTGCCAGGACTTTGGCTGGGACCCCTGCTTTCAGCCTGATGGATAT
GAGCAGACGTACGCAGAGATGCCTAAGGCGGAGAAGAACGCTGTCTCCCATCGCTTCCGG
GCCCTGCTGGAGCTGCAGGAATACTTTGGCAGTTTGGCAGCTTGA
Enzyme 9 GenBank Gene ID AB062127 Link Image
Enzyme 9 GeneCard ID ITPA Link Image
Enzyme 9 GenAtlas ID ITPA Link Image
Enzyme 9 HGNC ID HGNC:6176 Link Image
Enzyme 9 Chromosome Location 2
Enzyme 9 Locus 20p
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 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 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5676
Enzyme 10 Name Adenine phosphoribosyltransferase
Enzyme 10 Synonyms
  1. APRT
Enzyme 10 Gene Name APRT
Enzyme 10 Protein Sequence >Adenine phosphoribosyltransferase
MADSELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKATHGGRIDY
IAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYSLEYGKAELEIQKDALEPG
QRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGREKLAPVPFFSLLQYE
Enzyme 10 Number of Residues 180
Enzyme 10 Molecular Weight 19607.5
Enzyme 10 Theoretical pI 5.82
Enzyme 10 GO Classification
Function
  • adenine phosphoribosyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • adenine salvage
  • cellular aromatic compound metabolic process
  • cellular metabolic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside metabolic process
  • purine base biosynthetic process
  • purine base metabolic process
  • purine base salvage
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 10 General Function Involved in adenine phosphoribosyltransferase activity
Enzyme 10 Specific Function Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis
Enzyme 10 Pathways
Enzyme 10 Reactions
  • AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate [RN:R00190]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 51476557 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P07741 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name APT_HUMAN Link Image
Enzyme 10 PDB ID 1ORE Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >543 bp
ATGGCCGACTCCGAGCTGCAGCTGGTTGAGCAGCGGATCCGCAGCTTCCCCGACTTCCCC
ACCCCAGGCGTGGTATTCAGGGACATCTCGCCCGTCCTGAAGGACCCCGCCTCCTTCCGC
GCCGCCATCGGCCTCCTGGCGCGACACCTGAAGGCGACCCACGGGGGCCGCATCGACTAC
ATCGCAGGCCTAGACTCCCGAGGCTTCCTCTTTGGCCCCTCCCTGGCCCAGGAGCTTGGA
CTGGGCTGCGTGCTCATCCGAAAGCGGGGGAAGCTGCCAGGCCCCACTCTGTGGGCCTCC
TATTCCCTGGAGTACGGGAAGGCTGAGCTGGAGATTCAGAAAGACGCCCTGGAGCCAGGA
CAGAGGGTGGTCGTCGTGGATGATCTGCTGGCCACTGGTGGAACCATGAACGCTGCCTGT
GAGCTGCTGGGCCGCCTGCAGGCTGAGGTCCTGGAGTGCGTGAGCCTGGTGGAGCTGACC
TCGCTTAAGGGCAGGGAGAAGCTGGCACCTGTACCCTTCTTCTCTCTCCTGCAGTATGAG
TGA
Enzyme 10 GenBank Gene ID CR749423 Link Image
Enzyme 10 GeneCard ID APRT Link Image
Enzyme 10 GenAtlas ID APRT Link Image
Enzyme 10 HGNC ID HGNC:626 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 16q24
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Hidaka Y, Tarle SA, O'Toole TE, Kelley WN, Palella TD: Nucleotide sequence of the human APRT gene. Nucleic Acids Res. 1987 Nov 11;15(21):9086. [PubMed Link Image]
  2. Broderick TP, Schaff DA, Bertino AM, Dush MK, Tischfield JA, Stambrook PJ: Comparative anatomy of the human APRT gene and enzyme: nucleotide sequence divergence and conservation of a nonrandom CpG dinucleotide arrangement. Proc Natl Acad Sci U S A. 1987 May;84(10):3349-53. [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. Wilson JM, O'Toole TE, Argos P, Shewach DS, Daddona PE, Kelley WN: Human adenine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme. J Biol Chem. 1986 Oct 15;261(29):13677-83. [PubMed Link Image]
  6. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  7. 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. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  9. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  10. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  11. Silva M, Silva CH, Iulek J, Thiemann OH: Three-dimensional structure of human adenine phosphoribosyltransferase and its relation to DHA-urolithiasis. Biochemistry. 2004 Jun 22;43(24):7663-71. [PubMed Link Image]
  12. Chen J, Sahota A, Laxdal T, Scrine M, Bowman S, Cui C, Stambrook PJ, Tischfield JA: Identification of a single missense mutation in the adenine phosphoribosyltransferase (APRT) gene from five Icelandic patients and a British patient. Am J Hum Genet. 1991 Dec;49(6):1306-11. [PubMed Link Image]
  13. Sahota A, Chen J, Boyadjiev SA, Gault MH, Tischfield JA: Missense mutation in the adenine phosphoribosyltransferase gene causing 2,8-dihydroxyadenine urolithiasis. Hum Mol Genet. 1994 May;3(5):817-8. [PubMed Link Image]
  14. Hidaka Y, Palella TD, O'Toole TE, Tarle SA, Kelley WN: Human adenine phosphoribosyltransferase. Identification of allelic mutations at the nucleotide level as a cause of complete deficiency of the enzyme. J Clin Invest. 1987 Nov;80(5):1409-15. [PubMed Link Image]
  15. Hidaka Y, Tarle SA, Fujimori S, Kamatani N, Kelley WN, Palella TD: Human adenine phosphoribosyltransferase deficiency. Demonstration of a single mutant allele common to the Japanese. J Clin Invest. 1988 Mar;81(3):945-50. [PubMed Link Image]
  16. Kamatani N, Hakoda M, Otsuka S, Yoshikawa H, Kashiwazaki S: Only three mutations account for almost all defective alleles causing adenine phosphoribosyltransferase deficiency in Japanese patients. J Clin Invest. 1992 Jul;90(1):130-5. [PubMed Link Image]
  17. Deng L, Yang M, Frund S, Wessel T, De Abreu RA, Tischfield JA, Sahota A: 2,8-Dihydroxyadenine urolithiasis in a patient with considerable residual adenine phosphoribosyltransferase activity in cell extracts but with mutations in both copies of APRT. Mol Genet Metab. 2001 Mar;72(3):260-4. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5715
Enzyme 11 Name Hypoxanthine-guanine phosphoribosyltransferase
Enzyme 11 Synonyms
  1. HGPRT
  2. HGPRTase
Enzyme 11 Gene Name HPRT1
Enzyme 11 Protein Sequence >Hypoxanthine-guanine phosphoribosyltransferase
MATRSPGVVISDDEPGYDLDLFCIPNHYAEDLERVFIPHGLIMDRTERLARDVMKEMGGH
HIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGD
DLSTLTGKNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLLVKRTPRSVGYKPDFVG
FEIPDKFVVGYALDYNEYFRDLNHVCVISETGKAKYKA
Enzyme 11 Number of Residues 218
Enzyme 11 Molecular Weight 24579.2
Enzyme 11 Theoretical pI 6.67
Enzyme 11 GO Classification
Function
  • catalytic activity
  • hypoxanthine phosphoribosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring pentosyl groups
Process
  • biosynthetic process
  • cellular biosynthetic process
  • cellular nitrogen compound metabolic process
  • heterocycle biosynthetic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside metabolic process
  • purine ribonucleoside salvage
  • purine salvage
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 11 General Function Involved in hypoxanthine phosphoribosyltransferase activity
Enzyme 11 Specific Function IMP + diphosphate = hypoxanthine + 5-phospho- alpha-D-ribose 1-diphosphate
Enzyme 11 Pathways
Enzyme 11 Reactions
  • IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate [RN:R01132]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 306885 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P00492 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name HPRT_HUMAN Link Image
Enzyme 11 PDB ID 1BZY Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >657 bp
ATGGCGACCCGCAGCCCTGGCGTCGTGATTAGTGATGATGAACCAGGTTATGACCTTGAT
TTATTTTGCATACCTAATCATTATGCTGAGGATTTGGAAAGGGTGTTTATTCCTCATGGA
CTAATTATGGACAGGACTGAACGTCTTGCTCGAGATGTGATGAAGGAGATGGGAGGCCAT
CACATTGTAGCCCTCTGTGTGCTCAAGGGGGGCTATAAATTCTTTGCTGACCTGCTGGAT
TACATCAAAGCACTGAATAGAAATAGTGATAGATCCATTCCTATGACTGTAGATTTTATC
AGACTGAAGAGCTATTGTAATGACCAGTCAACAGGGGACATAAAAGTAATTGGTGGAGAT
GATCTCTCAACTTTAACTGGAAAGAATGTCTTGATTGTGGAAGATATAATTGACACTGGC
AAAACAATGCAGACTTTGCTTTCCTTGGTCAGGCAGTATAATCCAAAGATGGTCAAGGTC
GCAAGCTTGCTGGTGAAAAGGACCCCACGAAGTGTTGGATATAAGCCAGACTTTGTTGGA
TTTGAAATTCCAGACAAGTTTGTTGTAGGATATGCCCTTGACTATAATGAATACTTCAGG
GATTTGAATCATGTTTGTGTCATTAGTGAAACTGGAAAAGCAAAATACAAAGCCTAA
Enzyme 11 GenBank Gene ID M31642 Link Image
Enzyme 11 GeneCard ID HPRT1 Link Image
Enzyme 11 GenAtlas ID HPRT1 Link Image
Enzyme 11 HGNC ID HGNC:5157 Link Image
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Jolly DJ, Okayama H, Berg P, Esty AC, Filpula D, Bohlen P, Johnson GG, Shively JE, Hunkapillar T, Friedmann T: Isolation and characterization of a full-length expressible cDNA for human hypoxanthine phosphoribosyl transferase. Proc Natl Acad Sci U S A. 1983 Jan;80(2):477-81. [PubMed Link Image]
  2. Edwards A, Voss H, Rice P, Civitello A, Stegemann J, Schwager C, Zimmermann J, Erfle H, Caskey CT, Ansorge W: Automated DNA sequencing of the human HPRT locus. Genomics. 1990 Apr;6(4):593-608. [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. 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. Wilson JM, Tarr GE, Mahoney WC, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme. J Biol Chem. 1982 Sep 25;257(18):10978-85. [PubMed Link Image]
  7. Patel PI, Framson PE, Caskey CT, Chinault AC: Fine structure of the human hypoxanthine phosphoribosyltransferase gene. Mol Cell Biol. 1986 Feb;6(2):393-403. [PubMed Link Image]
  8. Eads JC, Scapin G, Xu Y, Grubmeyer C, Sacchettini JC: The crystal structure of human hypoxanthine-guanine phosphoribosyltransferase with bound GMP. Cell. 1994 Jul 29;78(2):325-34. [PubMed Link Image]
  9. Shi W, Li CM, Tyler PC, Furneaux RH, Grubmeyer C, Schramm VL, Almo SC: The 2.0 A structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor. Nat Struct Biol. 1999 Jun;6(6):588-93. [PubMed Link Image]
  10. Balendiran GK, Molina JA, Xu Y, Torres-Martinez J, Stevens R, Focia PJ, Eakin AE, Sacchettini JC, Craig SP 3rd: Ternary complex structure of human HGPRTase, PRPP, Mg2+, and the inhibitor HPP reveals the involvement of the flexible loop in substrate binding. Protein Sci. 1999 May;8(5):1023-31. [PubMed Link Image]
  11. Sculley DG, Dawson PA, Emmerson BT, Gordon RB: A review of the molecular basis of hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency. Hum Genet. 1992 Nov;90(3):195-207. [PubMed Link Image]
  12. Wilson JM, Kobayashi R, Fox IH, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. J Biol Chem. 1983 May 25;258(10):6458-60. [PubMed Link Image]
  13. Wilson JM, Kelley WN: Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in a patient with the Lesch-Nyhan syndrome. J Clin Invest. 1983 May;71(5):1331-5. [PubMed Link Image]
  14. Wilson JM, Tarr GE, Kelley WN: Human hypoxanthine (guanine) phosphoribosyltransferase: an amino acid substitution in a mutant form of the enzyme isolated from a patient with gout. Proc Natl Acad Sci U S A. 1983 Feb;80(3):870-3. [PubMed Link Image]
  15. Wilson JM, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase. Structural alteration in a dysfunctional enzyme variant (HPRTMunich) isolated from a patient with gout. J Biol Chem. 1984 Jan 10;259(1):27-30. [PubMed Link Image]
  16. Cariello NF, Scott JK, Kat AG, Thilly WG, Keohavong P: Resolution of a missense mutant in human genomic DNA by denaturing gradient gel electrophoresis and direct sequencing using in vitro DNA amplification: HPRT Munich. Am J Hum Genet. 1988 May;42(5):726-34. [PubMed Link Image]
  17. Davidson BL, Pashmforoush M, Kelley WN, Palella TD: Genetic basis of hypoxanthine guanine phosphoribosyltransferase deficiency in a patient with the Lesch-Nyhan syndrome (HPRTFlint). Gene. 1988 Mar 31;63(2):331-6. [PubMed Link Image]
  18. Davidson BL, Palella TD, Kelley WN: Human hypoxanthine-guanine phosphoribosyltransferase: a single nucleotide substitution in cDNA clones isolated from a patient with Lesch-Nyhan syndrome (HPRTMidland). Gene. 1988 Aug 15;68(1):85-91. [PubMed Link Image]
  19. Fujimori S, Hidaka Y, Davidson BL, Palella TD, Kelley WN: Identification of a single nucleotide change in a mutant gene for hypoxanthine-guanine phosphoribosyltransferase (HPRT Ann Arbor). Hum Genet. 1988 May;79(1):39-43. [PubMed Link Image]
  20. Davidson BL, Chin SJ, Wilson JM, Kelley WN, Palella TD: Hypoxanthine-guanine phosphoribosyltransferase. Genetic evidence for identical mutations in two partially deficient subjects. J Clin Invest. 1988 Dec;82(6):2164-7. [PubMed Link Image]
  21. Keough DT, Gordon RB, de Jersey J, Emmerson BT: Biochemical basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in nine families. J Inherit Metab Dis. 1988;11(3):229-38. [PubMed Link Image]
  22. Igarashi T, Minami M, Nishida Y: Molecular analysis of hypoxanthine-guanine phosphoribosyltransferase mutations in five unrelated Japanese patients. Acta Paediatr Jpn. 1989 Jun;31(3):303-13. [PubMed Link Image]
  23. Davidson BL, Pashmforoush M, Kelley WN, Palella TD: Human hypoxanthine-guanine phosphoribosyltransferase deficiency. The molecular defect in a patient with gout (HPRTAshville). J Biol Chem. 1989 Jan 5;264(1):520-5. [PubMed Link Image]
  24. Fujimori S, Davidson BL, Kelley WN, Palella TD: Identification of a single nucleotide change in the hypoxanthine-guanine phosphoribosyltransferase gene (HPRTYale) responsible for Lesch-Nyhan syndrome. J Clin Invest. 1989 Jan;83(1):11-3. [PubMed Link Image]
  25. Davidson BL, Tarle SA, Palella TD, Kelley WN: Molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in ten subjects determined by direct sequencing of amplified transcripts. J Clin Invest. 1989 Jul;84(1):342-6. [PubMed Link Image]
  26. Gibbs RA, Nguyen PN, McBride LJ, Koepf SM, Caskey CT: Identification of mutations leading to the Lesch-Nyhan syndrome by automated direct DNA sequencing of in vitro amplified cDNA. Proc Natl Acad Sci U S A. 1989 Mar;86(6):1919-23. [PubMed Link Image]
  27. Gibbs RA, Nguyen PN, Edwards A, Civitello AB, Caskey CT: Multiplex DNA deletion detection and exon sequencing of the hypoxanthine phosphoribosyltransferase gene in Lesch-Nyhan families. Genomics. 1990 Jun;7(2):235-44. [PubMed Link Image]
  28. Skopek TR, Recio L, Simpson D, Dallaire L, Melancon SB, Ogier H, O'Neill JP, Falta MT, Nicklas JA, Albertini RJ: Molecular analyses of a Lesch-Nyhan syndrome mutation (hprtMontreal) by use of T-lymphocyte cultures. Hum Genet. 1990 Jun;85(1):111-6. [PubMed Link Image]
  29. Gordon RB, Sculley DG, Dawson PA, Beacham IR, Emmerson BT: Identification of a single nucleotide substitution in the coding sequence of in vitro amplified cDNA from a patient with partial HPRT deficiency (HPRTBRISBANE). J Inherit Metab Dis. 1990;13(5):692-700. [PubMed Link Image]
  30. Davidson BL, Tarle SA, Van Antwerp M, Gibbs DA, Watts RW, Kelley WN, Palella TD: Identification of 17 independent mutations responsible for human hypoxanthine-guanine phosphoribosyltransferase (HPRT) deficiency. Am J Hum Genet. 1991 May;48(5):951-8. [PubMed Link Image]
  31. Tarle SA, Davidson BL, Wu VC, Zidar FJ, Seegmiller JE, Kelley WN, Palella TD: Determination of the mutations responsible for the Lesch-Nyhan syndrome in 17 subjects. Genomics. 1991 Jun;10(2):499-501. [PubMed Link Image]
  32. Sculley DG, Dawson PA, Beacham IR, Emmerson BT, Gordon RB: Hypoxanthine-guanine phosphoribosyltransferase deficiency: analysis of HPRT mutations by direct sequencing and allele-specific amplification. Hum Genet. 1991 Oct;87(6):688-92. [PubMed Link Image]
  33. Yamada Y, Goto H, Ogasawara N: Identification of two independent Japanese mutant HPRT genes using the PCR technique. Adv Exp Med Biol. 1991;309B:121-4. [PubMed Link Image]
  34. Lightfoot T, Joshi R, Nuki G, Snyder FF: The point mutation of hypoxanthine-guanine phosphoribosyltransferase (HPRTEdinburgh) and detection by allele-specific polymerase chain reaction. Hum Genet. 1992 Mar;88(6):695-6. [PubMed Link Image]
  35. Sege-Peterson K, Chambers J, Page T, Jones OW, Nyhan WL: Characterization of mutations in phenotypic variants of hypoxanthine phosphoribosyltransferase deficiency. Hum Mol Genet. 1992 Sep;1(6):427-32. [PubMed Link Image]
  36. Burgemeister R, Rotzer E, Gutensohn W, Gehrke M, Schiel W: Identification of a new missense mutation in exon 2 of the human hypoxanthine phosphoribosyltransferase gene (HPRTIsar): a further example of clinical heterogeneity in HPRT deficiencies. Hum Mutat. 1995;5(4):341-4. [PubMed Link Image]
  37. Fujimori S, Sakuma R, Yamaoka N, Hakoda M, Yamanaka H, Kamatani N: An asymptomatic germline missense base substitution in the hypoxanthine phosphoribosyltransferase (HPRT) gene that reduces the amount of enzyme in humans. Hum Genet. 1997 Jan;99(1):8-10. [PubMed Link Image]
  38. Liu G, Aral B, Zabot MT, Kamoun P, Ceballos-Picot I: The molecular basis of hypoxanthine-guanine phosphoribosyltransferase deficiency in French families; report of two novel mutations. Hum Mutat. 1998;Suppl 1:S88-90. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5833
Enzyme 12 Name Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
Enzyme 12 Synonyms
  1. GMP-PDE gamma
Enzyme 12 Gene Name PDE6H
Enzyme 12 Protein Sequence >Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
MSDNTTLPAPASNQGPTTPRKGPPKFKQRQTRQFKSKPPKKGVKGFGDDIPGMEGLGTDI
TVICPWEAFSHLELHELAQFGII
Enzyme 12 Number of Residues 83
Enzyme 12 Molecular Weight 9074.4
Enzyme 12 Theoretical pI 9.98
Enzyme 12 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • GMP binding
  • binding
  • cGMP binding
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nucleoside binding
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • purine nucleoside binding
Process
  • multicellular organismal process
  • neurological system process
  • sensory perception
  • sensory perception of light stimulus
  • system process
  • visual perception
Component
Enzyme 12 General Function Involved in 3',5'-cyclic-nucleotide phosphodiesterase activity
Enzyme 12 Specific Function Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones
Enzyme 12 Pathways
Enzyme 12 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein Not Available
Enzyme 12 UniProtKB/Swiss-Prot ID Q13956 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name CNCG_HUMAN Link Image
Enzyme 12 PDB ID 1FQJ Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >252 bp
ATGAGTGACAACACTACTCTGCCTGCTCCAGCTTCAAACCAGGGTCCTACCACCCCACGC
AAAGGCCCTCCCAAGTTCAAGCAGAGGCAGACTCGCCAATTCAAGAGTAAACCTCCAAAG
AAAGGTGTGAAAGGATTTGGAGATGACATTCCAGGAATGGAGGGGCTAGGAACAGATATC
ACAGTGATTTGTCCATGGGAGGCATTCAGCCACCTGGAATTGCATGAGCTCGCTCAGTTT
GGGATTATCTGA
Enzyme 12 GenBank Gene ID D45399 Link Image
Enzyme 12 GeneCard ID PDE6H Link Image
Enzyme 12 GenAtlas ID PDE6H Link Image
Enzyme 12 HGNC ID HGNC:8790 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 12p13
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Shimizu-Matsumoto A, Itoh K, Inazawa J, Nishida K, Matsumoto Y, Kinoshita S, Matsubara K, Okubo K: Isolation and chromosomal localization of the human cone cGMP phosphodiesterase gamma cDNA (PDE6H). Genomics. 1996 Feb 15;32(1):121-4. [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. Piri N, Gao YQ, Danciger M, Mendoza E, Fishman GA, Farber DB: A substitution of G to C in the cone cGMP-phosphodiesterase gamma subunit gene found in a distinctive form of cone dystrophy. Ophthalmology. 2005 Jan;112(1):159-66. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5843
Enzyme 13 Name Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
Enzyme 13 Synonyms
  1. Cam-PDE 1A
  2. 61 kDa Cam-PDE
  3. hCam-1
Enzyme 13 Gene Name PDE1A
Enzyme 13 Protein Sequence >Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
MGSSATEIEELENTTFKYLTGEQTEKMWQRLKGILRCLVKQLERGDVNVVDLKKNIEYAA
SVLEAVYIDETRRLLDTEDELSDIQTDSVPSEVRDWLASTFTRKMGMTKKKPEEKPKFRS
IVHAVQAGIFVERMYRKTYHMVGLAYPAAVIVTLKDVDKWSFDVFALNEASGEHSLKFMI
YELFTRYDLINRFKIPVSCLITFAEALEVGYSKYKNPYHNLIHAADVTQTVHYIMLHTGI
MHWLTELEILAMVFAAAIHDYEHTGTTNNFHIQTRSDVAILYNDRSVLENHHVSAAYRLM
QEEEMNILINLSKDDWRDLRNLVIEMVLSTDMSGHFQQIKNIRNSLQQPEGIDRAKTMSL
ILHAADISHPAKSWKLHYRWTMALMEEFFLQGDKEAELGLPFSPLCDRKSTMVAQSQIGF
IDFIVEPTFSLLTDSTEKIVIPLIEEASKAETSSYVASSSTTIVGLHIADALRRSNTKGS
MSDGSYSPDYSLAAVDLKSFKNNLVDIIQQNKERWKELAAQEARTSSQKCEFIHQ
Enzyme 13 Number of Residues 535
Enzyme 13 Molecular Weight 61251.4
Enzyme 13 Theoretical pI 6.02
Enzyme 13 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 13 General Function Involved in catalytic activity
Enzyme 13 Specific Function Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a higher affinity for cGMP than for cAMP
Enzyme 13 Pathways
Enzyme 13 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 1151109 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P54750 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name PDE1A_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1608 bp
ATGGGGTCTAGTGCCACAGAGATTGAAGAATTGGAAAACACCACTTTTAAGTATCTTACA
GGAGAACAGACTGAAAAAATGTGGCAGCGCCTGAAAGGAATACTAAGATGCTTGGTGAAG
CAGCTGGAAAGAGGTGATGTTAACGTCGTCGACTTAAAGAAGAATATTGAATATGCGGCA
TCTGTGCTGGAAGCAGTTTATATCGATGAAACAAGAAGACTTCTGGATACTGAAGATGAG
CTCAGTGACATTCAGACTGACTCAGTCCCATCTGAAGTCCGGGACTGGTTGGCTTCTACC
TTTACACGGAAAATGGGGATGACAAAAAAGAAACCTGAGGAAAAACCAAAATTTCGGAGC
ATTGTGCATGCTGTTCAAGCTGGAATTTTTGTGGAAAGAATGTACCGAAAAACATATCAT
ATGGTTGGTTTGGCATATCCAGCAGCTGTCATCGTAACATTAAAGGATGTTGATAAATGG
TCTTTCGATGTATTTGCCCTAAATGAAGCAAGTGGAGAGCATAGTCTGAAGTTTATGATT
TATGAACTGTTTACCAGATATGATCTTATCAACCGTTTCAAGATTCCTGTTTCTTGCCTA
ATCACCTTTGCAGAAGCTTTAGAAGTTGGTTACAGCAAGTACAAAAATCCATATCACAAT
TTGATTCATGCAGCTGATGTCACTCAAACTGTGCATTACATAATGCTTCATACAGGTATC
ATGCACTGGCTCACTGAACTGGAAATTTTAGCAATGGTCTTTGCTGCTGCCATTCATGAT
TATGAGCATACAGGGACAACAAACAACTTTCACATTCAGACAAGGTCAGATGTTGCCATT
TTGTATAATGATCGCTCTGTCCTTGAGAATCACCACGTGAGTGCAGCTTATCGACTTATG
CAAGAAGAAGAAATGAATATCTTGATAAATTTATCCAAAGATGACTGGAGGGATCTTCGG
AACCTAGTGATTGAAATGGTTTTATCTACAGACATGTCAGGTCACTTCCAGCAAATTAAA
AATATAAGAAACAGTTTGCAGCAGCCTGAAGGGATTGACAGAGCCAAAACCATGTCCCTG
ATTCTCCACGCAGCAGACATCAGCCACCCAGCCAAATCCTGGAAGCTGCATTATCGGTGG
ACCATGGCCCTAATGGAGGAGTTTTTCCTGCAGGGAGATAAAGAAGCTGAATTAGGGCTT
CCATTTTCCCCACTTTGTGATCGGAAGTCAACCATGGTGGCCCAGTCACAAATAGGTTTC
ATCGATTTCATAGTAGAGCCAACATTTTCTCTTCTGACAGACTCAACAGAGAAAATTGTT
ATTCCTCTTATAGAGGAAGCCTCAAAAGCCGAAACTTCTTCCTATGTGGCAAGCAGCTCA
ACCACCATTGTGGGGTTACACATTGCTGATGCACTAAGACGATCAAATACAAAAGGCTCC
ATGAGTGATGGGTCCTATTCCCCAGACTACTCCCTTGCAGCAGTGGACCTGAAGAGTTTC
AAGAACAACCTGGTGGACATCATTCAGCAGAACAAAGAGAGGTGGAAAGAGTTAGCTGCA
CAAGAAGCAAGAACCAGTTCACAGAAGTGTGAGTTTATTCATCAGTAA
Enzyme 13 GenBank Gene ID U40370 Link Image
Enzyme 13 GeneCard ID PDE1A Link Image
Enzyme 13 GenAtlas ID PDE1A Link Image
Enzyme 13 HGNC ID HGNC:8774 Link Image
Enzyme 13 Chromosome Location 2
Enzyme 13 Locus 2q32.1
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Loughney K, Martins TJ, Harris EA, Sadhu K, Hicks JB, Sonnenburg WK, Beavo JA, Ferguson K: Isolation and characterization of cDNAs corresponding to two human calcium, calmodulin-regulated, 3',5'-cyclic nucleotide phosphodiesterases. J Biol Chem. 1996 Jan 12;271(2):796-806. [PubMed Link Image]
  2. Michibata H, Yanaka N, Kanoh Y, Okumura K, Omori K: Human Ca2+/calmodulin-dependent phosphodiesterase PDE1A: novel splice variants, their specific expression, genomic organization, and chromosomal localization. Biochim Biophys Acta. 2001 Jan 26;1517(2):278-87. [PubMed Link Image]
  3. Fidock M, Miller M, Lanfear J: Isolation and differential tissue distribution of two human cDNAs encoding PDE1 splice variants. Cell Signal. 2002 Jan;14(1):53-60. [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]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5847
Enzyme 14 Name High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name PDE8A
Enzyme 14 Protein Sequence >High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A
MGCAPSIHISERLVAEDAPSPAAPPLSSGGPRLPQGQKTAALPRTRGAGLLESELRDGSG
KKVAVADVQFGPMRFHQDQLQVLLVFTKEDNQCNGFCRACEKAGFKCTVTKEAQAVLACF
LDKHHDIIIIDHRNPRQLDAEALCRSIRSSKLSENTVIVGVVRRVDREELSVMPFISAGF
TRRYVENPNIMACYNELLQLEFGEVRSQLKLRACNSVFTALENSEDAIEITSEDRFIQYA
NPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGDNI
QQNVKIIPVIGQGGKIRHYVSIIRVCNGNNKAEKISECVQSDTHTDNQTGKHKDRRKGSL
DVKAVASRATEVSSQRRHSSMARIHSMTIEAPITKVINIINAAQESSPMPVTEALDRVLE
ILRTTELYSPQFGAKDDDPHANDLVGGLMSDGLRRLSGNEYVLSTKNTQMVSSNIITPIS
LDDVPPRIARAMENEEYWDFDIFELEAATHNRPLIYLGLKMFARFGICEFLHCSESTLRS
WLQIIEANYHSSNPYHNSTHSADVLHATAYFLSKERIKETLDPIDEVAALIAATIHDVDH
PGRTNSFLCNAGSELAILYNDTAVLESHHAALAFQLTTGDDKCNIFKNMERNDYRTLRQG
IIDMVLATEMTKHFEHVNKFVNSINKPLATLEENGETDKNQEVINTMLRTPENRTLIKRM
LIKCADVSNPCRPLQYCIEWAARISEEYFSQTDEEKQQGLPVVMPVFDRNTCSIPKSQIS
FIDYFITDMFDAWDAFVDLPDLMQHLDNNFKYWKGLDEMKLRNLRPPPE
Enzyme 14 Number of Residues 829
Enzyme 14 Molecular Weight 93303.1
Enzyme 14 Theoretical pI 6.03
Enzyme 14 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • molecular transducer activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • signal transducer activity
  • two-component response regulator activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
  • signal transduction
  • signal transmission
  • signaling process
  • two-component signal transduction system (phosphorelay)
Component
Enzyme 14 General Function Involved in catalytic activity
Enzyme 14 Specific Function Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development
Enzyme 14 Pathways
Enzyme 14 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein Not Available
Enzyme 14 UniProtKB/Swiss-Prot ID O60658 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name PDE8A_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >2490 bp
ATGGGCTGTGCCCCGAGCATCCACATTTCCGAGCGCCTGGTGGCCGAGGACGCGCCTAGC
CCCGCGGCACCGCCGCTGTCGTCCGGCGGGCCGCGCCTCCCGCAGGGCCAGAAGACGGCC
GCCTTGCCCCGGACCCGCGGCGCCGGCCTCTTGGAGTCGGAGCTTCGCGACGGCAGCGGC
AAGAAGGTAGCAGTAGCTGATGTGCAGTTTGGCCCCATGAGATTTCATCAAGATCAACTT
CAGGTACTTTTAGTGTTTACCAAAGAAGATAACCAATGTAATGGATTCTGCAGGGCATGT
GAAAAAGCAGGGTTTAAGTGTACAGTTACCAAGGAGGCTCAGGCTGTCCTTGCCTGTTTC
CTGGACAAACATCATGACATTATCATCATAGACCACAGAAATCCTCGACAGCTGGATGCA
GAGGCACTGTGCAGGTCTATCAGATCATCAAAACTCTCAGAAAACACAGTTATTGTTGGT
GTAGTACGCAGGGTGGATAGAGAAGAGTTGTCCGTAATGCCTTTCATTTCTGCTGGATTT
ACAAGGAGGTATGTAGAAAACCCCAACATCATGGCCTGCTACAATGAACTGCTCCAGCTG
GAGTTTGGAGAGGTGCGATCACAACTGAAACTCAGGGCTTGTAACTCAGTATTCACTGCA
TTAGAAAACAGTGAAGATGCAATTGAAATTACAAGCGAAGACCGTTTTATACAGTATGCA
AATCCTGCATTTGAAACAACAATGGGCTATCAGTCAGGTGAATTAATAGGGAAGGAGTTA
GGAGAAGTGCCTATAAATGAAAAAAAGGCTGACTTGCTCGATACTATAAATTCATGCATC
AGGATAGGCAAGGAGTGGCAAGGAATTTACTATGCAAAAAAGAAAAACGGAGATAATATA
CAACAAAATGTGAAGATAATACCTGTCATTGGACAGGGAGGAAAAATTAGACACTATGTG
TCCATTATCAGAGTGTGCAATGGCAACAATAAGGCTGAGAAAATATCCGAATGTGTTCAG
TCTGACACTCATACAGATAATCAGACAGGCAAACATAAAGACAGGAGAAAAGGCTCACTA
GACGTCAAAGCTGTTGCCTCCCGTGCAACTGAAGTTTCCAGCCAGAGACGACACTCTTCC
ATGGCCCGGATACATTCCATGACAATTGAGGCGCCCATCACCAAGGTAATCAATATTATC
AATGCTGCCCAGGAAAGTAGTCCCATGCCTGTGACAGAAGCCCTAGACCGTGTGCTGGAA
ATTCTAAGAACCACTGAGTTATATTCACCACAGTTTGGTGCTAAAGATGATGATCCCCAT
GCCAATGACCTTGTTGGGGGCTTAATGTCTGATGGTTTGCGAAGACTATCAGGGAATGAA
TATGTTCTTTCAACAAAAAACACTCAAATGGTTTCAAGCAATATAATCACTCCCATCTCC
CTTGATGATGTCCCACCACGGATAGCTCGGGCCATGGAAAATGAGGAATACTGGGACTTT
GATATTTTTGAACTGGAGGCTGCCACCCACAATAGGCCTTTGATTTATCTTGGTCTCAAA
ATGTTTGCTCGCTTTGGAATCTGTGAATTCTTACACTGCTCCGAGTCAACGCTAAGATCA
TGGTTACAAATTATCGAAGCCAATTATCATTCCTCCAATCCCTACCACAATTCTACACAT
TCTGCTGATGTGCTTCATGCCACTGCCTATTTTCTCTCCAAGGAGAGGATAAAGGAAACT
TTAGATCCAATTGATGAGGTCGCTGCACTCATCGCAGCCACCATTCATGATGTGGATCAC
CCTGGGAGAACCAACTCCTTCCTGTGTAATGCTGGAAGTGAGCTGGCCATTTTGTACAAT
GACACTGCTGTGCTGGAGAGCCACCATGCGGCCTTGGCCTTCCAGCTGACCACTGGAGAT
GATAAATGCAATATATTTAAAAACATGGAGAGGAATGATTATCGGACACTGCGCCAGGGG
ATTATCGACATGGTCTTAGCCACAGAAATGACAAAGCACTTTGAGCATGTCAACAAATTT
GTCAACAGCATCAACAAACCCTTGGCAACACTAGAAGAAAATGGGGAAACTGATAAAAAC
CAGGAAGTGATAAACACTATGCTTAGGACTCCAGAGAACCGGACCCTAATCAAACGAATG
CTGATTAAATGTGCTGATGTGTCCAATCCCTGCCGACCCCTGCAGTACTGCATCGAGTGG
GCTGCACGCATTTCGGAAGAATATTTTTCTCAGACTGATGAAGAGAAGCAGCAGGGCTTA
CCTGTGGTGATGCCAGTGTTTGACAGAAATACCTGCAGCATCCCCAAATCCCAAATCTCT
TTCATTGATTACTTCATCACAGACATGTTTGATGCTTGGGATGCCTTTGTAGACCTGCCT
GATTTAATGCAGCATCTTGACAACAACTTTAAATACTGGAAAGGACTGGACGAAATGAAG
CTGCGGAACCTCCGACCACCTCCTGAATAG
Enzyme 14 GenBank Gene ID AF388183 Link Image
Enzyme 14 GeneCard ID PDE8A Link Image
Enzyme 14 GenAtlas ID PDE8A Link Image
Enzyme 14 HGNC ID HGNC:8793 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 15q25.3
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Wang P, Wu P, Egan RW, Billah MM: Human phosphodiesterase 8A splice variants: cloning, gene organization, and tissue distribution. Gene. 2001 Dec 12;280(1-2):183-94. [PubMed Link Image]
  2. Glavas NA, Ostenson C, Schaefer JB, Vasta V, Beavo JA: T cell activation up-regulates cyclic nucleotide phosphodiesterases 8A1 and 7A3. Proc Natl Acad Sci U S A. 2001 May 22;98(11):6319-24. [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. Fisher DA, Smith JF, Pillar JS, St Denis SH, Cheng JB: Isolation and characterization of PDE8A, a novel human cAMP-specific phosphodiesterase. Biochem Biophys Res Commun. 1998 May 29;246(3):570-7. [PubMed Link Image]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Wang H, Yan Z, Yang S, Cai J, Robinson H, Ke H: Kinetic and structural studies of phosphodiesterase-8A and implication on the inhibitor selectivity. Biochemistry. 2008 Dec 2;47(48):12760-8. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5848
Enzyme 15 Name Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
Enzyme 15 Synonyms
  1. Cam-PDE 1B
  2. 63 kDa Cam-PDE
Enzyme 15 Gene Name PDE1B
Enzyme 15 Protein Sequence >Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
MELSPRSPPEMLEESDCPSPLELKSAPSKKMWIKLRSLLRYMVKQLENGEINIEELKKNL
EYTASLLEAVYIDETRQILDTEDELQELRSDAVPSEVRDWLASTFTQQARAKGRRAEEKP
KFRSIVHAVQAGIFVERMFRRTYTSVGPTYSTAVLNCLKNLDLWCFDVFSLNQAADDHAL
RTIVFELLTRHNLISRFKIPTVFLMSFLDALETGYGKYKNPYHNQIHAADVTQTVHCFLL
RTGMVHCLSEIELLAIIFAAAIHDYEHTGTTNSFHIQTKSECAIVYNDRSVLENHHISSV
FRLMQDDEMNIFINLTKDEFVELRALVIEMVLATDMSCHFQQVKTMKTALQQLERIDKPK
ALSLLLHAADISHPTKQWLVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQS
QIGFIDFIVEPTFSVLTDVAEKSVQPLADEDSKSKNQPSFQWRQPSLDVEVGDPNPDVVS
FRSTWVKRIQENKQKWKERAASGITNQMSIDELSPCEEEAPPSPAEDEHNQNGNLD
Enzyme 15 Number of Residues 536
Enzyme 15 Molecular Weight 61379.2
Enzyme 15 Theoretical pI 5.22
Enzyme 15 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 15 General Function Involved in catalytic activity
Enzyme 15 Specific Function Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a preference for cGMP as a substrate
Enzyme 15 Pathways
Enzyme 15 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
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 Q01064 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name PDE1B_HUMAN Link Image
Enzyme 15 PDB ID 1TAZ Link Image
Enzyme 15 PDB File Show
Enzyme 15 3D Structure
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1611 bp
ATGGAGCTGTCCCCCCGCAGTCCTCCGGAGATGCTGGAGGAGTCGGATTGCCCGTCACCC
CTGGAGCTGAAGTCAGCCCCCAGCAAGAAGATGTGGATTAAGCTTCGGTCTCTGCTGCGC
TACATGGTGAAGCAGTTGGAGAATGGGGAGATAAACATTGAGGAGCTGAAGAAAAATCTG
GAGTACACAGCTTCTCTGCTGGAAGCCGTCTACATAGATGAGACACGGCAAATCTTGGAC
ACGGAGGACGAGCTGCAGGAGCTGCGGTCAGATGCCGTGCCTTCGGAGGTGCGGGACTGG
CTGGCCTCCACCTTCACCCAGCAGGCCCGGGCCAAAGGCCGCCGAGCAGAGGAGAAGCCC
AAGTTCCGAAGCATTGTGCACGCTGTGCAGGCTGGGATCTTCGTGGAACGGATGTTCCGG
AGAACATACACCTCTGTGGGCCCCACTTACTCTACTGCGGTTCTCAACTGTCTCAAGAAC
CTGGATCTCTGGTGCTTTGATGTCTTTTCCTTGAACCAGGCAGCAGATGACCATGCCCTG
AGGACCATTGTTTTTGAGTTGCTGACTCGGCATAACCTCATCAGCCGCTTCAAGATTCCC
ACTGTGTTTTTGATGAGTTTCCTGGATGCCTTGGAGACAGGCTATGGGAAGTACAAGAAT
CCTTACCACAACCAGATCCACGCAGCCGATGTTACCCAGACAGTCCATTGCTTCTTGCTC
CGCACAGGGATGGTGCACTGCCTGTCGGAGATTGAGCTCCTGGCCATCATCTTTGCTGCA
GCTATCCATGATTATGAGCACACGGGCACTACCAACAGCTTCCACATCCAGACCAAGTCA
GAATGTGCCATCGTGTACAATGATCGTTCAGTGCTGGAGAATCACCACATCAGCTCTGTT
TTCCGATTGATGCAGGATGATGAGATGAACATTTTCATCAACCTCACCAAGGATGAGTTT
GTAGAACTCCGAGCCCTGGTCATTGAGATGGTGTTGGCCACAGACATGTCCTGCCATTTC
CAGCAAGTGAAGACCATGAAGACAGCCTTGCAACAGCTGGAGAGGATTGACAAGCCCAAG
GCCCTGTCTCTACTGCTCCATGCTGCTGACATCAGCCACCCAACCAAGCAGTGGTTGGTC
CACAGCCGTTGGACCAAGGCCCTCATGGAGGAATTCTTCCGTCAGGGTGACAAGGAGGCA
GAGTTGGGCCTGCCCTTTTCTCCACTCTGTGACCGCACTTCCACTCTAGTGGCACAGTCT
CAGATAGGGTTCATCGACTTCATTGTGGAGCCCACATTCTCTGTGCTGACTGACGTGGCA
GAGAAGAGTGTTCAGCCCCTGGCGGATGAGGACTCCAAGTCTAAAAACCAGCCCAGCTTT
CAGTGGCGCCAGCCCTCTCTGGATGTGGAAGTGGGAGACCCCAACCCTGATGTGGTCAGC
TTTCGTTCCACCTGGGTCAAGCGCATTCAGGAGAACAAGCAGAAATGGAAGGAACGGGCA
GCAAGTGGCATCACCAACCAGATGTCCATTGACGAGCTGTCCCCCTGTGAAGAAGAGGCC
CCCCCATCCCCTGCCGAAGATGAACACAACCAGAATGGGAATCTGGATTAG
Enzyme 15 GenBank Gene ID U56976 Link Image
Enzyme 15 GeneCard ID PDE1B Link Image
Enzyme 15 GenAtlas ID PDE1B Link Image
Enzyme 15 HGNC ID HGNC:8775 Link Image
Enzyme 15 Chromosome Location 1
Enzyme 15 Locus 12q13
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Jiang X, Li J, Paskind M, Epstein PM: Inhibition of calmodulin-dependent phosphodiesterase induces apoptosis in human leukemic cells. Proc Natl Acad Sci U S A. 1996 Oct 1;93(20):11236-41. [PubMed Link Image]
  2. Yu J, Wolda SL, Frazier AL, Florio VA, Martins TJ, Snyder PB, Harris EA, McCaw KN, Farrell CA, Steiner B, Bentley JK, Beavo JA, Ferguson K, Gelinas R: Identification and characterisation of a human calmodulin-stimulated phosphodiesterase PDE1B1. Cell Signal. 1997 Nov;9(7):519-29. [PubMed Link Image]
  3. Fidock M, Miller M, Lanfear J: Isolation and differential tissue distribution of two human cDNAs encoding PDE1 splice variants. Cell Signal. 2002 Jan;14(1):53-60. [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. Repaske DR, Swinnen JV, Jin SL, Van Wyk JJ, Conti M: A polymerase chain reaction strategy to identify and clone cyclic nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA encoding the 63-kDa calmodulin-dependent phosphodiesterase. J Biol Chem. 1992 Sep 15;267(26):18683-8. [PubMed Link Image]
  7. Zhang KY, Card GL, Suzuki Y, Artis DR, Fong D, Gillette S, Hsieh D, Neiman J, West BL, Zhang C, Milburn MV, Kim SH, Schlessinger J, Bollag G: A glutamine switch mechanism for nucleotide selectivity by phosphodiesterases. Mol Cell. 2004 Jul 23;15(2):279-86. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5850
Enzyme 16 Name cGMP-inhibited 3',5'-cyclic phosphodiesterase B
Enzyme 16 Synonyms
  1. CGIPDE1
  2. CGIP1
  3. Cyclic GMP-inhibited phosphodiesterase B
  4. CGI-PDE B
Enzyme 16 Gene Name PDE3B
Enzyme 16 Protein Sequence >cGMP-inhibited 3',5'-cyclic phosphodiesterase B
MRRDERDAKAMRSLQPPDGAGSPPESLRNGYVKSCVSPLRQDPPRGFFFHLCRFCNVELR
PPPASPQQPRRCSPFCRARLSLGALAAFVLALLLGAEPESWAAGAAWLRTLLSVCSHSLS
PLFSIACAFFFLTCFLTRTKRGPGPGRSCGSWWLLALPACCYLGDFLVWQWWSWPWGDGD
AGSAAPHTPPEAAAGRLLLVLSCVGLLLTLAHPLRLRHCVLVLLLASFVWWVSFTSLGSL
PSALRPLLSGLVGGAGCLLALGLDHFFQIREAPLHPRLSSAAEEKVPVIRPRRRSSCVSL
GETAASYYGSCKIFRRPSLPCISREQMILWDWDLKQWYKPHYQNSGGGNGVDLSVLNEAR
NMVSDLLTDPSLPPQVISSLRSISSLMGAFSGSCRPKINPLTPFPGFYPCSEIEDPAEKG
DRKLNKGLNRNSLPTPQLRRSSGTSGLLPVEQSSRWDRNNGKRPHQEFGISSQGCYLNGP
FNSNLLTIPKQRSSSVSLTHHVGLRRAGVLSSLSPVNSSNHGPVSTGSLTNRSPIEFPDT
ADFLNKPSVILQRSLGNAPNTPDFYQQLRNSDSNLCNSCGHQMLKYVSTSESDGTDCCSG
KSGEEENIFSKESFKLMETQQEEETEKKDSRKLFQEGDKWLTEEAQSEQQTNIEQEVSLD
LILVEEYDSLIEKMSNWNFPIFELVEKMGEKSGRILSQVMYTLFQDTGLLEIFKIPTQQF
MNYFRALENGYRDIPYHNRIHATDVLHAVWYLTTRPVPGLQQIHNGCGTGNETDSDGRIN
HGRIAYISSKSCSNPDESYGCLSSNIPALELMALYVAAAMHDYDHPGRTNAFLVATNAPQ
AVLYNDRSVLENHHAASAWNLYLSRPEYNFLLHLDHVEFKRFRFLVIEAILATDLKKHFD
FLAEFNAKANDVNSNGIEWSNENDRLLVCQVCIKLADINGPAKVRDLHLKWTEGIVNEFY
EQGDEEANLGLPISPFMDRSSPQLAKLQESFITHIVGPLCNSYDAAGLLPGQWLEAEEDN
DTESGDDEDGEELDTEDEEMENNLNPKPPRRKSRRRIFCQLMHHLTENHKIWKEIVEEEE
KCKADGNKLQVENSSLPQADEIQVIEEADEEE
Enzyme 16 Number of Residues 1112
Enzyme 16 Molecular Weight 124332.1
Enzyme 16 Theoretical pI 5.75
Enzyme 16 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 16 General Function Involved in catalytic activity
Enzyme 16 Specific Function Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. May play a role in fat metabolism
Enzyme 16 Pathways
Enzyme 16 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • 88-108 117-137 152-172 192-212 220-240 247-267
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 1246755 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q13370 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name PDE3B_HUMAN Link Image
Enzyme 16 PDB ID 1SOJ Link Image
Enzyme 16 PDB File Show
Enzyme 16 3D Structure
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >3339 bp
ATGAGGAGGGACGAGCGAGACGCCAAAGCCATGCGGTCCCTGCAGCCGCCGGATGGGGCC
GGCTCGCCCCCCGAGAGTCTGAGGAACGGCTACGTGAAGAGCTGCGTGAGCCCCTTGCGG
CAGGACCCTCCGCGCGGCTTCTTCTTCCACCTCTGCCGCTTCTGCAACGTGGAGCTGCGG
CCGCCGCCGGCCTCTCCCCAGCAGCCGCGGCGCTGCTCCCCCTTCTGCCGGGCGCGCCTC
TCGCTGGGCGCCCTGGCTGTCTTTGTCCTCGCCCTGCTGCTGGGCGCGGAACCCGAGAGC
TGGGCTGCCGGGGCCGCCTGGCTGCGGACGCTGCTGAGCGTGTGTTCGCACAGCTTGAGC
CCCCTCTTCAGCATCGCCTGTGCCTTCTTCTTCCTCACCTGCTTCCTCACCCGGACCAAG
CGGGGACCCGGCCCGGGCCGGAGCTGCGGCTCCTGGTGGCTGCTGGCGCTGCCCGCCTGC
TGTTACCTGGGGGACTTCTTGGTGTGGCAGTGGTGGTCTTGGCCTTGGGGGGATGGCGAC
GCAGGGTCCGCGGCCCCGCACACGCCCCCGGAGGCGGCAGCGGGCAGGTTGCTGCTGGTG
CTGAGCTGCGTAGGGCTGCTGCTGACGCTCGCGCACCCGCTGCGGCTCCGGCACTGCGTT
CTGGTGCTGCTCCTGGCCAGCTTCGTCTGGTGGGTCTCCTTCACCAGCCTCGGGTCGCTG
CCCTCCGCCCTCAGGCCGCTGCTCTCCGGCCTGGTGGGGGGCGCTGGCTGCCTGCTGGCC
CTGGGGTTGGATCACTTCTTTCAAATCAGGGAAGCGCCTCTTCATCCTCGACTGTCCAGT
GCCGCCGAAGAAAAAGTGCCTGTGATCCGACCCCGGAGGAGGTCCAGCTGCGTGTCGTTA
GGAGAAACTGCAGCCAGTTACTATGGCAGTTGCAAAATATTCAGGAGACCGTCGTTGCCT
TGTATTTCCAGAGAACAGATGATTCTTTGGGATTGGGACTTAAAACAATGGTATAAGCCT
CATTATCAAAATTCTGGAGGTGGAAATGGAGTTGATCTTTCAGTGCTAAATGAGGCTCGC
AATATGGTGTCAGATCTTCTGACTGATCCAAGCCTTCCACCACAAGTCATTTCCTCTCTA
CGGAGTATTAGTAGCTTAATGGGTGCTTTCTCAGGTTCCTGTAGGCCAAAGATTAATCCT
CTCACACCATTTCCTGGATTTTACCCCTGTTCTGAAATAGAGGACCCAGCTGAGAAAGGG
GATAGAAAACTTAACAAGGGACTAAATAGGAATAGTTTGCCAACTCCACAGCTGAGGAGA
AGCTCAGGAACTTCAGGATTGCTACCTGTTGAACAGTCTTCAAGGTGGGATCGTAATAAT
GGCAAAAGGCCTCACCAAGAATTTGGCATTTCAAGTCAAGGATGCTATCTAAATGGGCCT
TTTAATTCAAATCTACTGACTATCCCGAAGCAAAGGTCATCTTCTGTATCACTGACTCAC
CATGTAGGTCTCAGAAGAGCTGGTGTTTTGTCCAGTCTGAGTCCTGTGAATTCTTCCAAC
CATGGACCAGTGTCTACTGGCTCTCTAACTAATCGATCACCCATAGAATTTCCTGATACT
GCTGATTTTCTTAATAAGCCAAGCGTTATCTTGCAGAGATCTCTGGGCAATGCACCTAAT
ACTCCAGATTTTTATCAGCAACTTAGAAATTCTGATAGCAATCTGTGTAACAGCTGTGGA
CATCAAATGCTGAAATATGTTTCAACATCTGAATCAGATGGTACAGATTGCTGCAGTGGA
AAATCAGGTGAAGAAGAAAACATTTTCTCGAAAGAATCATTCAAACTTATGGAAACTCAA
CAAGAAGAGGAAACAGAGAAGAAAGACAGCAGAAAATTATTTCAGGAAGGTGATAAGTGG
CTAACAGAAGAGGCACAGAGTGAACAGCAAACAAATATTGAACAGGAAGTATCACTGGAC
CTGATTTTAGTAGAAGAGTATGACTCATTAATAGAAAAGATGAGCAACTGGAATTTTCCA
ATTTTTGAACTTGTAGAAAAGATGGGAGAGAAATCAGGAAGGATTCTCAGTCAGGTTATG
TATACCTTATTTCAAGACACTGGTTTATTGGAAATATTTAAAATTCCCACTCAACAATTT
ATGAACTATTTTCGTGCATTAGAAAATGGCTATCGAGACATTCCTTATCACAATCGTATA
CATGCCACAGATGTGCTACATGCAGTTTGGTATCTGACAACGCGGCCAGTTCCTGGCTTA
CAGCAGATCCACAATGGTTGTGGAACAGGAAATGAAACAGATTCTGATGGTAGAATTAAC
CATGGGCGAATTGCTTATATTTCTTCGAAGAGCTGCTCTAATCCTGATGAGAGTTATGGC
TGCCTGTCTTCAAACATTCCTGCATTAGAATTGATGGCTCTATACGTGGCAGCTGCCATG
CATGATTATGATCACCCAGGGAGGACAAATGCATTTCTAGTGGCTACAAATGCCCCTCAG
GCAGTTTTATACAATGACAGATCTGTTCTGGAAAATCATCATGCTGCGTCAGCTTGGAAT
CTATATCTTTCTCGCCCAGAATACAACTTCCTTCTTCATCTTGATCATGTGGAATTCAAG
CGCTTTCGTTTTTTAGTCATTGAAGCAATCCTTGCTACGGATCTTAAAAAGCATTTTGAT
TTTCTCGCAGAATTCAATGCCAAGGCAAATGATGTAAATAGTAATGGCATAGAATGGAGT
AATGAAAATGATCGCCTCTTGGTATGCCAGGTGTGCATCAAACTGGCAGATATAAATGGC
CCAGCAAAAGTTCGAGACTTGCATTTGAAATGGACAGAAGGCATTGTCAATGAATTTTAT
GAGCAGGGAGATGAAGAAGCAAATCTTGGTCTGCCCATCAGTCCATTCATGGATCGTTCT
TCTCCTCAACTAGCAAAACTCCAAGAATCTTTTATCACCCACATAGTGGGTCCCCTGTGT
AACTCCTATGATGCTGCTGGTTTGCTACCAGGTCAGTGGTTAGAAGCAGAAGAGGATAAT
GATACTGAAAGTGGTGATGATGAAGACGGTGAAGAATTAGATACAGAAGATGAAGAAATG
GAAAACAATCTAAATCCAAAACCACCAAGAAGGAAAAGCAGACGGCGAATATTTTGTCAG
CTAATGCACCACCTCACTGAAAACCACAAGATATGGAAGGAAATCGTAGAGGAAGAAGAA
AAATGTAAAGCTGATGGGAATAAACTGCAGGTGGAGAATTCCTCCTTACCTCAAGCAGAT
GAGATTCAGGTAATTGAAGAGGCAGATGAAGAGGAATAG
Enzyme 16 GenBank Gene ID X95520 Link Image
Enzyme 16 GeneCard ID PDE3B Link Image
Enzyme 16 GenAtlas ID PDE3B Link Image
Enzyme 16 HGNC ID HGNC:8779 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 11p15.1
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Miki T, Taira M, Hockman S, Shimada F, Lieman J, Napolitano M, Ward D, Taira M, Makino H, Manganiello VC: Characterization of the cDNA and gene encoding human PDE3B, the cGIP1 isoform of the human cyclic GMP-inhibited cyclic nucleotide phosphodiesterase family. Genomics. 1996 Sep 15;36(3):476-85. [PubMed Link Image]
  2. Murata T, Taira M, Manganiello VC: Differential expression of cGMP-inhibited cyclic nucleotide phosphodiesterases in human hepatoma cell lines. FEBS Lett. 1996 Jul 15;390(1):29-33. [PubMed Link Image]
  3. Lobbert RW, Winterpacht A, Seipel B, Zabel BU: Molecular cloning and chromosomal assignment of the human homologue of the rat cGMP-inhibited phosphodiesterase 1 (PDE3A)--a gene involved in fat metabolism located at 11p 15.1. Genomics. 1996 Oct 15;37(2):211-8. [PubMed Link Image]
  4. Liu H, Tang JR, Choi YH, Napolitano M, Hockman S, Taira M, Degerman E, Manganiello VC: Importance of cAMP-response element-binding protein in regulation of expression of the murine cyclic nucleotide phosphodiesterase 3B (Pde3b) gene in differentiating 3T3-L1 preadipocytes. J Biol Chem. 2006 Jul 28;281(30):21096-113. Epub 2006 May 15. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  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. Scapin G, Patel SB, Chung C, Varnerin JP, Edmondson SD, Mastracchio A, Parmee ER, Singh SB, Becker JW, Van der Ploeg LH, Tota MR: Crystal structure of human phosphodiesterase 3B: atomic basis for substrate and inhibitor specificity. Biochemistry. 2004 May 25;43(20):6091-100. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5854
Enzyme 17 Name Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'
Enzyme 17 Synonyms
  1. cGMP phosphodiesterase 6C
Enzyme 17 Gene Name PDE6C
Enzyme 17 Protein Sequence >Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'
MGEINQVAVEKYLEENPQFAKEYFDRKLRVEVLGEIFKNSQVPVQSSMSFSELTQVEESA
LCLELLWTVQEEGGTPEQGVHRALQRLAHLLQADRCSMFLCRSRNGIPEVASRLLDVTPT
SKFEDNLVGPDKEVVFPLDIGIVGWAAHTKKTHNVPDVKKNSHFSDFMDKQTGYVTKNLL
ATPIVVGKEVLAVIMAVNKVNASEFSKQDEEVFSKYLNFVSIILRLHHTSYMYNIESRRS
QILMWSANKVFEELTDVERQFHKALYTVRSYLNCERYSIGLLDMTKEKEFYDEWPIKLGE
VEPYKGPKTPDGREVNFYKIIDYILHGKEEIKVIPTPPADHWTLISGLPTYVAENGFICN
MMNAPADEYFTFQKGPVDETGWVIKNVLSLPIVNKKEDIVGVATFYNRKDGKPFDEHDEY
ITETLTQFLGWSLLNTDTYDKMNKLENRKDIAQEMLMNQTKATPEEIKSILKFQEKLNVD
VIDDCEEKQLVAILKEDLPDPRSAELYEFRFSDFPLTEHGLIKCGIRLFFEINVVEKFKV
PVEVLTRWMYTVRKGYRAVTYHNWRHGFNVGQTMFTLLMTGRLKKYYTDLEAFAMLAAAF
CHDIDHRGTNNLYQMKSTSPLARLHGSSILERHHLEYSKTLLQDESLNIFQNLNKRQFET
VIHLFEVAIIATDLALYFKKRTMFQKIVDACEQMQTEEEAIKYVTVDPTKKEIIMAMMMT
ACDLSAITKPWEVQSQVALMVANEFWEQGDLERTVLQQQPIPMMDRNKRDELPKLQVGFI
DFVCTFVYKEFSRFHKEITPMLSGLQNNRVEWKSLADEYDAKMKVIEEEAKKQEGGAEKA
AEDSGGGDDKKSKTCLML
Enzyme 17 Number of Residues 858
Enzyme 17 Molecular Weight 99146.1
Enzyme 17 Theoretical pI 5.45
Enzyme 17 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 17 General Function Involved in catalytic activity
Enzyme 17 Specific Function Guanosine 3',5'-cyclic phosphate + H(2)O = guanosine 5'-phosphate
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions
  • guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate [RN:R01234]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 55661526 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID P51160 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name PDE6C_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >2577 bp
ATGGGTGAGATCAACCAAGTTGCCGTGGAGAAATACCTGGAGGAGAACCCTCAGTTTGCC
AAGGAGTACTTTGACAGGAAGTTGCGGGTGGAGGTGCTGGGAGAAATCTTCAAGAACAGC
CAGGTGCCAGTCCAGTCCAGCATGTCCTTCTCTGAGCTGACCCAGGTGGAGGAGTCAGCC
CTGTGCTTGGAGCTGCTGTGGACCGTGCAGGAGGAGGGGGGCACCCCAGAGCAGGGGGTT
CACAGGGCCCTGCAGAGGCTGGCCCACCTGCTCCAGGCTGACCGCTGCAGCATGTTCCTG
TGCCGGTCCCGGAACGGCATACCTGAGGTGGCCTCTAGGTTGCTGGATGTCACCCCCACC
TCCAAGTTTGAGGACAACCTGGTGGGCCCTGACAAAGAAGTTGTGTTTCCATTGGACATT
GGGATAGTGGGTTGGGCTGCTCACACGAAGAAAACTCATAATGTCCCAGATGTGAAAAAG
AACAGCCATTTTTCTGACTTCATGGACAAGCAAACTGGGTATGTCACTAAGAACCTGCTG
GCAACCCCGATCGTGGTGGGCAAGGAGGTTCTTGCTGTGATCATGGCAGTTAACAAAGTA
AATGCATCTGAATTTTCCAAACAGGATGAAGAGGTCTTTTCCAAATACCTCAACTTTGTG
TCTATCATCCTAAGGCTTCATCACACCAGCTACATGTACAATATTGAATCCCGAAGAAGC
CAGATCCTTATGTGGTCAGCCAATAAAGTATTTGAAGAACTCACAGATGTTGAGCGACAG
TTTCACAAAGCGCTCTACACGGTTAGATCATATCTGAACTGTGAACGATACTCCATTGGA
CTGCTGGACATGACCAAGGAGAAGGAATTCTACGATGAATGGCCAATCAAGCTTGGAGAA
GTAGAGCCTTATAAAGGTCCAAAGACACCTGATGGCAGGGAAGTCAACTTTTATAAAATC
ATTGATTACATTTTACATGGAAAAGAAGAGATCAAAGTGATTCCGACGCCTCCTGCAGAC
CACTGGACACTCATTAGTGGGTTGCCAACATATGTTGCTGAAAATGGATTTATCTGTAAC
ATGATGAATGCCCCTGCGGATGAATACTTCACATTTCAGAAAGGACCTGTAGACGAAACT
GGTTGGGTCATTAAGAATGTTTTGTCCCTGCCTATTGTCAACAAGAAAGAAGATATTGTG
GGAGTGGCTACATTTTACAACAGGAAGGATGGAAAACCTTTCGATGAGCATGATGAATAC
ATTACCGAGACTCTCACACAATTTCTTGGATGGTCTCTTTTAAATACTGACACCTACGAT
AAGATGAATAAGCTAGAAAACAGAAAGGACATTGCTCAGGAAATGCTCATGAACCAAACC
AAAGCCACTCCTGAAGAAATTAAGTCCATTTTGAAATTTCAAGAGAAGTTAAATGTTGAT
GTAATTGACGACTGTGAAGAAAAACAACTTGTTGCAATTTTGAAAGAGGACTTGCCAGAC
CCACGCTCAGCAGAACTGTACGAATTCCGCTTCAGTGACTTCCCCCTTACAGAGCACGGA
TTGATTAAATGTGGAATACGACTGTTTTTTGAAATAAATGTGGTGGAGAAATTCAAAGTA
CCTGTAGAGGTTCTTACCAGATGGATGTACACTGTGAGGAAAGGGTACCGAGCTGTCACT
TACCACAATTGGCGGCATGGGTTCAACGTGGGGCAGACCATGTTTACTTTGCTGATGACA
GGAAGATTAAAGAAGTACTACACAGATCTCGAAGCCTTTGCCATGCTTGCTGCTGCTTTC
TGCCATGATATTGACCACAGAGGCACCAATAATTTGTACCAGATGAAATCCACGTCTCCA
TTAGCAAGACTTCATGGTTCTTCTATTTTGGAGAGGCACCACCTGGAGTACAGTAAGACT
CTGTTGCAGGATGAGAGTTTAAACATCTTCCAGAACCTAAATAAGCGGCAGTTTGAAACA
GTTATTCATTTGTTCGAGGTCGCAATAATAGCAACTGACCTGGCTTTATATTTCAAGAAG
AGGACCATGTTTCAAAAAATTGTTGATGCCTGTGAACAAATGCAAACGGAAGAAGAAGCC
ATCAAATATGTAACTGTTGATCCAACCAAGAAAGAGATTATCATGGCAATGATGATGACG
GCATGTGACTTGTCTGCTATTACCAAGCCCTGGGAGGTGCAAAGTCAGGTAGCACTTATG
GTTGCAAATGAATTTTGGGAACAAGGAGATCTGGAGAGAACAGTGTTGCAGCAACAACCC
ATTCCTATGATGGACAGAAACAAAAGAGATGAATTACCTAAACTTCAAGTTGGATTTATT
GATTTTGTTTGTACTTTTGTATATAAGGAGTTCTCACGGTTTCACAAAGAAATCACACCT
ATGCTGAGTGGTCTTCAGAATAACAGAGTAGAATGGAAATCACTAGCTGATGAGTATGAT
GCAAAGATGAAGGTCATTGAAGAGGAGGCAAAAAAGCAAGAAGGAGGAGCCGAAAAAGCT
GCTGAAGATTCAGGAGGTGGTGATGACAAAAAGTCCAAAACATGTTTAATGTTGTAA
Enzyme 17 GenBank Gene ID AL157396 Link Image
Enzyme 17 GeneCard ID PDE6C Link Image
Enzyme 17 GenAtlas ID PDE6C Link Image
Enzyme 17 HGNC ID HGNC:8787 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 10q24
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Viczian AS, Piriev NI, Farber DB: Isolation and characterization of a cDNA encoding the alpha' subunit of human cone cGMP-phosphodiesterase. Gene. 1995 Dec 12;166(2):205-11. [PubMed Link Image]
  2. Piriev NI, Viczian AS, Ye J, Kerner B, Korenberg JR, Farber DB: Gene structure and amino acid sequence of the human cone photoreceptor cGMP-phosphodiesterase alpha' subunit (PDEA2) and its chromosomal localization to 10q24. Genomics. 1995 Aug 10;28(3):429-35. [PubMed Link Image]
  3. Feshchenko EA, Andreeva SG, Suslova VA, Smirnova EV, Zagranichny VE, Lipkin VM: Human cone-specific cGMP phosphodiesterase alpha' subunit: complete cDNA sequence and gene arrangement. FEBS Lett. 1996 Feb 26;381(1-2):149-52. [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. Gao YQ, Danciger M, Longmuir R, Piriev NI, Zhao DY, Heckenlively JR, Fishman GA, Weleber RG, Jacobson SG, Stone EM, Farber DB: Screening of the gene encoding the alpha'-subunit of cone cGMP-PDE in patients with retinal degenerations. Invest Ophthalmol Vis Sci. 1999 Jul;40(8):1818-22. [PubMed Link Image]
  6. Thiadens AA, den Hollander AI, Roosing S, Nabuurs SB, Zekveld-Vroon RC, Collin RW, De Baere E, Koenekoop RK, van Schooneveld MJ, Strom TM, van Lith-Verhoeven JJ, Lotery AJ, van Moll-Ramirez N, Leroy BP, van den Born LI, Hoyng CB, Cremers FP, Klaver CC: Homozygosity mapping reveals PDE6C mutations in patients with early-onset cone photoreceptor disorders. Am J Hum Genet. 2009 Aug;85(2):240-7. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5864
Enzyme 18 Name GMP synthase [glutamine-hydrolyzing]
Enzyme 18 Synonyms
  1. GMP synthetase
  2. Glutamine amidotransferase
Enzyme 18 Gene Name GMPS
Enzyme 18 Protein Sequence >GMP synthase [glutamine-hydrolyzing]
MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETP
AFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHK
KSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANE
SKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVL
VLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAA
HSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPE
EVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVR
ILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPH
TLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDW
ESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILR
ESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVE
VVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE
Enzyme 18 Number of Residues 693
Enzyme 18 Molecular Weight 76714.8
Enzyme 18 Theoretical pI 6.86
Enzyme 18 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 18 General Function Involved in catalytic activity
Enzyme 18 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 18 Pathways
Enzyme 18 Reactions
  • ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate [RN:R01231]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein Not Available
Enzyme 18 UniProtKB/Swiss-Prot ID P49915 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name GUAA_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 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 18 GenBank Gene ID U10860 Link Image
Enzyme 18 GeneCard ID GMPS Link Image
Enzyme 18 GenAtlas ID GMPS Link Image
Enzyme 18 HGNC ID HGNC:4378 Link Image
Enzyme 18 Chromosome Location 3
Enzyme 18 Locus 3q24
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 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 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5872
Enzyme 19 Name cGMP-inhibited 3',5'-cyclic phosphodiesterase A
Enzyme 19 Synonyms
  1. Cyclic GMP-inhibited phosphodiesterase A
  2. CGI-PDE A
Enzyme 19 Gene Name PDE3A
Enzyme 19 Protein Sequence >cGMP-inhibited 3',5'-cyclic phosphodiesterase A
MAVPGDAARVRDKPVHSGVSQAPTAGRDCHHRADPASPRDSGCRGCWGDLVLQPLRSSRK
LSSALCAGSLSFLLALLVRLVRGEVGCDLEQCKEAAAAEEEEAAPGAEGGVFPGPRGGAP
GGGARLSPWLQPSALLFSLLCAFFWMGLYLLRAGVRLPLAVALLAACCGGEALVQIGLGV
GEDHLLSLPAAGVVLSCLAAATWLVLRLRLGVLMIALTSAVRTVSLISLERFKVAWRPYL
AYLAGVLGILLARYVEQILPQSAEAAPREHLGSQLIAGTKEDIPVFKRRRRSSSVVSAEM
SGCSSKSHRRTSLPCIPREQLMGHSEWDHKRGPRGSQSSGTSITVDIAVMGEAHGLITDL
LADPSLPPNVCTSLRAVSNLLSTQLTFQAIHKPRVNPVTSLSENYTCSDSEESSEKDKLA
IPKRLRRSLPPGLLRRVSSTWTTTTSATGLPTLEPAPVRRDRSTSIKLQEAPSSSPDSWN
NPVMMTLTKSRSFTSSYAISAANHVKAKKQSRPGALAKISPLSSPCSSPLQGTPASSLVS
KISAVQFPESADTTAKQSLGSHRALTYTQSAPDLSPQILTPPVICSSCGRPYSQGNPADE
PLERSGVATRTPSRTDDTAQVTSDYETNNNSDSSDIVQNEDETECLREPLRKASACSTYA
PETMMFLDKPILAPEPLVMDNLDSIMEQLNTWNFPIFDLVENIGRKCGRILSQVSYRLFE
DMGLFEAFKIPIREFMNYFHALEIGYRDIPYHNRIHATDVLHAVWYLTTQPIPGLSTVIN
DHGSTSDSDSDSGFTHGHMGYVFSKTYNVTDDKYGCLSGNIPALELMALYVAAAMHDYDH
PGRTNAFLVATSAPQAVLYNDRSVLENHHAAAAWNLFMSRPEYNFLINLDHVEFKHFRFL
VIEAILATDLKKHFDFVAKFNGKVNDDVGIDWTNENDRLLVCQMCIKLADINGPAKCKEL
HLQWTDGIVNEFYEQGDEEASLGLPISPFMDRSAPQLANLQESFISHIVGPLCNSYDSAG
LMPGKWVEDSDESGDTDDPEEEEEEAPAPNEEETCENNESPKKKTFKRRKIYCQITQHLL
QNHKMWKKVIEEEQRLAGIENQSLDQTPQSHSSEQIQAIKEEEEEKGKPRGEEIPTQKPD
Q
Enzyme 19 Number of Residues 1141
Enzyme 19 Molecular Weight 124978.1
Enzyme 19 Theoretical pI 5.87
Enzyme 19 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 19 General Function Involved in catalytic activity
Enzyme 19 Specific Function Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes
Enzyme 19 Pathways
Enzyme 19 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • 61-81 130-150 160-180 185-205 210-230 232-252
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 38201493 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q14432 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name PDE3A_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >3426 bp
ATGGCAGTGCCCGGCGACGCTGCACGAGTCAGGGACAAGCCCGTCCACAGTGGGGTGAGT
CAAGCCCCCACGGCGGGCCGGGACTGCCACCATCGTGCGGACCCCGCATCGCCGCGGGAC
TCGGGCTGCCGTGGCTGCTGGGGAGACCTGGTGCTGCAGCCGCTCCGGAGCTCTCGGAAA
CTTTCCTCCGCGCTGTGCGCGGGCTCCCTATCCTTTCTGCTGGCGCTGCTGGTGAGGCTG
GTCCGCGGGGAGGTCGGCTGTGACCTGGAGCAGTGTAAGGAGGCGGCGGCGGCGGAGGAG
GAGGAAGCAGCCCCGGGAGCAGAAGGGGGCGTCTTCCCGGGGCCTCGGGGAGGTGCTCCC
GGGGGCGGTGCGCGGCTCAGCCCCTGGCTGCAGCCCTCGGCGCTGCTCTTCAGTCTCCTG
TGTGCCTTCTTCTGGATGGGCTTGTACCTCCTGCGCGCCGGGGTGCGCCTGCCTCTGGCT
GTCGCGCTGCTGGCCGCCTGCTGCGGGGGGGAAGCGCTCGTCCAGATTGGGCTGGGCGTC
GGGGAGGATCACTTACTCTCACTCCCCGCTGCGGGGGTGGTGCTCAGCTGCTTGGCCGCC
GCGACATGGCTGGTGCTGAGGCTGAGGCTGGGCGTCCTCATGATCGCCTTGACTAGCGCG
GTCAGGACCGTGTCCCTCATTTCCTTAGAGAGGTTCAAGGTCGCCTGGAGACCTTACCTG
GCGTACCTGGCCGGCGTGCTGGGGATCCTCTTGGCCAGGTACGTGGAACAAATCTTGCCG
CAGTCCGCGGAGGCGGCTCCAAGGGAGCATTTGGGGTCCCAGCTGATTGCTGGGACCAAG
GAAGATATCCCGGTGTTTAAGAGGAGGAGGCGGTCCAGCTCCGTCGTGTCCGCCGAGATG
TCCGGCTGCAGCAGCAAGTCCCATCGGAGGACCTCCCTGCCCTGTATACCGAGGGAACAG
CTCATGGGGCATTCAGAATGGGACCACAAACGAGGGCCAAGAGGATCACAGTCTTCAGGA
ACCAGTATTACTGTGGACATCGCCGTCATGGGCGAAGCCCACGGCCTCATTACCGACCTC
CTGGCAGACCCTTCTCTTCCACCAAACGTGTGCACATCCTTGAGAGCCGTGAGCAACTTG
CTCAGCACACAGCTCACCTTCCAGGCCATTCACAAGCCCAGAGTGAATCCCGTTACTTCG
CTCAGTGAAAACTATACCTGTTCTGACTCTGAAGAGAGCTCTGAAAAAGACAAGCTTGCT
ATTCCAAAGCGCCTGAGAAGGAGTTTGCCTCCTGGCTTGTTGAGACGAGTTTCTTCCACT
TGGACCACCACCACCTCGGCCACAGGTCTACCCACCTTGGAGCCTGCACCAGTACGGAGA
GACCGCAGCACCAGCATCAAACTGCAGGAAGCACCTTCATCCAGTCCTGATTCTTGGAAT
AATCCAGTGATGATGACCCTCACCAAAAGCAGATCCTTTACTTCATCCTATGCTATTTCT
GCAGCTAACCATGTAAAGGCTAAAAAGCAAAGTCGACCAGGTGCCCTCGCTAAAATTTCA
CCTCTTTCATCGCCCTGCTCCTCACCTCTCCAAGGGACTCCTGCCAGCAGCCTGGTCAGC
AAAATTTCTGCAGTGCAGTTTCCAGAATCTGCTGACACAACTGCCAAACAAAGCCTAGGT
TCTCACAGGGCCTTAACTTACACTCAGAGTGCCCCAGACCTATCCCCTCAAATCCTGACT
CCACCTGTTATATGTAGCAGCTGTGGCAGACCATATTCCCAAGGGAATCCTGCTGATGAG
CCCCTGGAGAGAAGTGGGGTAGCCACTCGGACACCAAGTCGAACAGATGACACTGCTCAA
GTTACCTCTGATTATGAAACCAATAACAACAGTGACAGCAGTGACATTGTACAGAATGAA
GATGAAACAGAGTGCCTGAGAGAGCCTCTGAGGAAAGCATCGGCTTGCAGCACCTATGCT
CCTGAGACCATGATGTTTCTGGACAAACCAATTCTTGCTCCCGAACCTCTTGTCATGGAT
AACCTGGACTCAATTATGGAGCAGCTAAATACTTGGAATTTTCCAATTTTTGATTTAGTG
GAAAATATAGGAAGAAAATGTGGCCGTATTCTTAGTCAGGTATCTTACAGACTTTTTGAA
GACATGGGCCTCTTTGAAGCTTTTAAAATTCCAATTAGGGAATTTATGAATTATTTTCAT
GCTTTGGAGATTGGATATAGGGATATTCCTTATCATAACAGAATCCATGCCACTGATGTT
TTACATGCTGTTTGGTATCTTACTACACAGCCTATTCCAGGCCTCTCAACTGTGATTAAT
GATCATGGTTCAACCAGTGATTCAGATTCTGACAGTGGATTTACACATGGACATATGGGA
TATGTATTCTCAAAAACGTATAATGTGACAGATGATAAATACGGATGTCTGTCTGGGAAT
ATCCCTGCCTTGGAGTTGATGGCGCTGTATGTGGCTGCAGCCATGCACGATTATGATCAT
CCAGGAAGGACTAATGCTTTCCTGGTTGCAACTAGTGCTCCTCAGGCGGTGCTATATAAC
GATCGTTCAGTTTTGGAGAATCATCACGCAGCTGCTGCATGGAATCTTTTCATGTCCCGG
CCAGAGTATAACTTCTTAATTAACCTTGACCATGTGGAATTTAAGCATTTCCGTTTCCTT
GTCATTGAAGCAATTTTGGCCACTGACCTGAAGAAACACTTTGACTTCGTAGCCAAATTT
AATGGCAAGGTAAATGATGATGTTGGAATAGATTGGACCAATGAAAATGATCGTCTACTG
GTTTGTCAAATGTGTATAAAGTTGGCTGATATCAATGGTCCAGCTAAATGTAAAGAACTC
CATCTTCAGTGGACAGATGGTATTGTCAATGAATTTTATGAACAGGGTGATGAAGAGGCC
AGCCTTGGATTACCCATAAGCCCCTTCATGGATCGTTCTGCTCCTCAGCTGGCCAACCTT
CAGGAATCCTTCATCTCTCACATTGTGGGGCCTCTGTGCAACTCCTATGATTCAGCAGGA
CTAATGCCTGGAAAATGGGTGGAAGACAGCGATGAGTCAGGAGATACTGATGACCCAGAA
GAAGAGGAGGAAGAAGCACCAGCACCAAATGAAGAGGAAACCTGTGAAAATAATGAATCT
CCAAAAAAGAAGACTTTCAAAAGGAGAAAAATCTACTGCCAAATAACTCAGCACCTCTTA
CAGAACCACAAGATGTGGAAGAAAGTCATTGAAGAGGAGCAACGGTTGGCAGGCATAGAA
AATCAATCCCTGGACCAGACCCCTCAGTCGCACTCTTCAGAACAGATCCAGGCTATCAAG
GAAGAAGAAGAAGAGAAAGGGAAACCAAGAGGCGAGGAGATACCAACCCAAAAGCCAGAC
CAGTGA
Enzyme 19 GenBank Gene ID M91667 Link Image
Enzyme 19 GeneCard ID PDE3A Link Image
Enzyme 19 GenAtlas ID PDE3A Link Image
Enzyme 19 HGNC ID HGNC:8778 Link Image
Enzyme 19 Chromosome Location 1
Enzyme 19 Locus 12p12
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Meacci E, Taira M, Moos M Jr, Smith CJ, Movsesian MA, Degerman E, Belfrage P, Manganiello V: Molecular cloning and expression of human myocardial cGMP-inhibited cAMP phosphodiesterase. Proc Natl Acad Sci U S A. 1992 May 1;89(9):3721-5. [PubMed Link Image]
  2. Cheung PP, Xu H, McLaughlin MM, Ghazaleh FA, Livi GP, Colman RW: Human platelet cGI-PDE: expression in yeast and localization of the catalytic domain by deletion mutagenesis. Blood. 1996 Aug 15;88(4):1321-9. [PubMed Link Image]
  3. Kuthe A, Eckel H, Stief CG, Uckert S, Forssmann WG, Jonas U, Magert HJ: Molecular biological characterization of phosphodiesterase 3A from human corpus cavernosum. Chem Biol Interact. 1999 May 14;119-120:593-8. [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. Degerman E, Moos M Jr, Rascon A, Vasta V, Meacci E, Smith CJ, Lindgren S, Andersson KE, Belfrage P, Manganiello V: Single-step affinity purification, partial structure and properties of human platelet cGMP inhibited cAMP phosphodiesterase. Biochim Biophys Acta. 1994 Apr 13;1205(2):189-98. [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. 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. 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]
  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]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5876
Enzyme 20 Name cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
Enzyme 20 Synonyms Not Available
Enzyme 20 Gene Name PDE10A
Enzyme 20 Protein Sequence >cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
MRIEERKSQHLTGLTDEKVKAYLSLHPQVLDEFVSESVSAETVEKWLKRKNNKSEDESAP
KEVSRYQDTNMQGVVYELNSYIEQRLDTGGDNQLLLYELSSIIKIATKADGFALYFLGEC
NNSLCIFTPPGIKEGKPRLIPAGPITQGTTVSAYVAKSRKTLLVEDILGDERFPRGTGLE
SGTRIQSVLCLPIVTAIGDLIGILELYRHWGKEAFCLSHQEVATANLAWASVAIHQVQVC
RGLAKQTELNDFLLDVSKTYFDNIVAIDSLLEHIMIYAKNLVNADRCALFQVDHKNKELY
SDLFDIGEEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDAYADPRFNREVDLYT
GYTTRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHR
IRHSECIYRVTMEKLSYHSICTSEEWQGLMQFTLPVRLCKEIELFHFDIGPFENMWPGIF
VYMVHRSCGTSCFELEKLCRFIMSVKKNYRRVPYHNWKHAVTVAHCMYAILQNNHTLFTD
LERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYSTSTMEQHHFSQTVSILQLEGHNI
FSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSLNLNNQSHRDRVIGLMM
TACDLCSVTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKDEVPQGQLGFY
NAVAIPCYTTLTQILPPTEPLLKACRDNLSQWEKVIRGEETATWISSPSVAQKAAASED
Enzyme 20 Number of Residues 779
Enzyme 20 Molecular Weight 88411.7
Enzyme 20 Theoretical pI 6.57
Enzyme 20 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 20 General Function Involved in catalytic activity
Enzyme 20 Specific Function Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate
Enzyme 20 Pathways
Enzyme 20 Reactions
  • guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate [RN:R01234]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein Not Available
Enzyme 20 UniProtKB/Swiss-Prot ID Q9Y233 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name PDE10_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >2340 bp
ATGAGGATAGAAGAGAGGAAATCCCAACATTTAACAGGTTTGACAGATGAAAAAGTGAAG
GCATATCTTTCTCTTCACCCCCAGGTATTAGATGAATTTGTATCTGAAAGTGTTAGTGCA
GAGACAGTAGAGAAATGGCTGAAGAGGAAGAACAACAAATCAGAAGATGAATCAGCTCCT
AAGGAAGTCAGCAGGTACCAAGATACGAATATGCAGGGAGTTGTATATGAACTAAACAGC
TATATAGAACAACGGTTGGACACAGGAGGAGACAACCAGCTACTCCTCTATGAACTGAGC
AGCATCATTAAAATAGCCACAAAAGCCGATGGATTTGCACTGTATTTCCTTGGAGAGTGC
AATAATAGCCTGTGTATATTCACGCCACCTGGGATAAAGGAAGGAAAACCCCGCCTCATC
CCTGCTGGGCCCATCACTCAGGGCACCACCGTCTCTGCTTATGTGGCCAAGTCCAGGAAA
ACACTGCTAGTAGAAGACATCCTTGGAGATGAACGATTTCCAAGAGGTACTGGACTGGAA
TCAGGGACTCGTATCCAGTCTGTTCTTTGCTTACCAATTGTCACTGCAATTGGTGACTTG
ATTGGTATTCTCGAGCTGTATCGGCACTGGGGCAAAGAAGCCTTCTGTCTTAGTCACCAG
GAGGTTGCAACAGCAAATCTTGCCTGGGCTTCAGTAGCAATACATCAGGTGCAGGTATGC
AGAGGCCTTGCCAAACAGACAGAATTGAATGACTTCCTACTCGACGTATCAAAAACATAT
TTTGATAACATAGTTGCAATAGATTCTCTACTTGAACACATAATGATATATGCAAAAAAC
CTGGTGAATGCCGATCGTTGTGCGCTTTTCCAGGTGGACCATAAGAACAAGGAGTTATAT
TCAGACCTTTTTGATATTGGAGAGGAAAAGGAAGGAAAACCTGTCTTCAAGAAGACCAAA
GAGATAAGATTTTCAATTGAGAAAGGAATTGCTGGCCAAGTAGCAAGAACAGGGGAAGTC
CTGAACATTCCAGATGCCTATGCAGACCCACGCTTTAACAGAGAAGTAGACTTGTACACA
GGCTACACCACGCGGAACATCCTGTGCATGCCCATCGTCAGCCGAGGCAGCGTGATAGGT
GTGGTGCAGATGGTCAACAAAATCAGTGGCAGTGCCTTCTCTAAAACAGATGAAAACAAC
TTCAAAATGTTTGCCGTCTTTTGTGCTTTAGCCTTACACTGTGCTAATATGTATCATAGA
ATTCGCCACTCAGAGTGCATTTACCGGGTAACGATGGAAAAGCTGTCCTACCATAGCATT
TGTACTTCAGAAGAGTGGCAAGGTCTCATGCAATTCACCCTTCCCGTGCGTCTCTGCAAA
GAAATTGAATTATTCCACTTTGACATTGGTCCTTTTGAAAACATGTGGCCTGGAATTTTT
GTCTACATGGTTCATCGGTCCTGTGGGACATCCTGCTTTGAGCTTGAAAAGTTGTGTCGT
TTTATTATGTCTGTGAAGAAGAACTATCGGCGGGTTCCTTATCACAACTGGAAGCATGCG
GTCACTGTAGCACACTGCATGTATGCCATACTTCAGAACAATCACACGCTTTTCACAGAC
CTTGAGCGCAAAGGACTGCTGATTGCGTGTCTGTGTCATGACCTGGACCACAGGGGCTTC
AGTAACAGCTACCTGCAGAAGTTCGACCACCCTCTGGCCGCTCTCTACTCCACTTCCACC
ATGGAGCAGCACCACTTCTCCCAGACTGTGTCCATCCTTCAGTTGGAAGGGCACAATATC
TTCTCCACTCTGAGCTCCAGTGAATATGAGCAGGTGCTTGAGATCATCCGCAAAGCCATC
ATTGCCACAGACCTTGCTTTATACTTTGGAAACAGGAAGCAGTTGGAAGAGATGTACCAG
ACCGGATCACTAAACCTTAATAATCAATCACATAGAGACCGTGTAATTGGTTTGATGATG
ACTGCCTGTGACCTTTGTTCTGTGACAAAACTGTGGCCCGTTACAAAATTGACGGCAAAT
GATATATATGCAGAATTCTGGGCTGAGGGTGATGAAATGAAGAAATTGGGAATACAGCCT
ATTCCTATGATGGACAGAGACAAGAAGGATGAAGTCCCCCAAGGCCAGCTTGGGTTCTAC
AATGCCGTGGCCATTCCCTGCTATACAACCCTTACCCAGATCCTCCCTCCCACGGAGCCT
CTTCTGAAAGCATGCAGGGATAATCTCAGTCAGTGGGAGAAGGTGATTCGAGGGGAGGAG
ACTGCAACCTGGATTTCATCCCCATCCGTGGCTCAGAAGGCAGCTGCATCTGAAGATTGA
Enzyme 20 GenBank Gene ID AB020593 Link Image
Enzyme 20 GeneCard ID PDE10A Link Image
Enzyme 20 GenAtlas ID PDE10A Link Image
Enzyme 20 HGNC ID HGNC:8772 Link Image
Enzyme 20 Chromosome Location 6
Enzyme 20 Locus 6q26
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Fujishige K, Kotera J, Michibata H, Yuasa K, Takebayashi S, Okumura K, Omori K: Cloning and characterization of a novel human phosphodiesterase that hydrolyzes both cAMP and cGMP (PDE10A). J Biol Chem. 1999 Jun 25;274(26):18438-45. [PubMed Link Image]
  2. Loughney K, Snyder PB, Uher L, Rosman GJ, Ferguson K, Florio VA: Isolation and characterization of PDE10A, a novel human 3', 5'-cyclic nucleotide phosphodiesterase. Gene. 1999 Jun 24;234(1):109-17. [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. Fujishige K, Kotera J, Yuasa K, Omori K: The human phosphodiesterase PDE10A gene genomic organization and evolutionary relatedness with other PDEs containing GAF domains. Eur J Biochem. 2000 Oct;267(19):5943-51. [PubMed Link Image]
  6. Gross-Langenhoff M, Hofbauer K, Weber J, Schultz A, Schultz JE: cAMP is a ligand for the tandem GAF domain of human phosphodiesterase 10 and cGMP for the tandem GAF domain of phosphodiesterase 11. J Biol Chem. 2006 Feb 3;281(5):2841-6. Epub 2005 Dec 5. [PubMed Link Image]
  7. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  8. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  9. Wang H, Liu Y, Hou J, Zheng M, Robinson H, Ke H: Structural insight into substrate specificity of phosphodiesterase 10. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5782-7. Epub 2007 Mar 26. [PubMed Link Image]
  10. Handa N, Mizohata E, Kishishita S, Toyama M, Morita S, Uchikubo-Kamo T, Akasaka R, Omori K, Kotera J, Terada T, Shirouzu M, Yokoyama S: Crystal structure of the GAF-B domain from human phosphodiesterase 10A complexed with its ligand, cAMP. J Biol Chem. 2008 Jul 11;283(28):19657-64. Epub 2008 May 13. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5877
Enzyme 21 Name Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
Enzyme 21 Synonyms
  1. Cam-PDE 1C
  2. hCam-3
Enzyme 21 Gene Name PDE1C
Enzyme 21 Protein Sequence >Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
MESPTKEIEEFESNSLKYLQPEQIEKIWLRLRGLRKYKKTSQRLRSLVKQLERGEASVVD
LKKNLEYAATVLESVYIDETRRLLDTEDELSDIQSDAVPSEVRDWLASTFTRQMGMMLRR
SDEKPRFKSIVHAVQAGIFVERMYRRTSNMVGLSYPPAVIEALKDVDKWSFDVFSLNEAS
GDHALKFIFYELLTRYDLISRFKIPISALVSFVEALEVGYSKHKNPYHNLMHAADVTQTV
HYLLYKTGVANWLTELEIFAIIFSAAIHDYEHTGTTNNFHIQTRSDPAILYNDRSVLENH
HLSAAYRLLQDDEEMNILINLSKDDWREFRTLVIEMVMATDMSCHFQQIKAMKTALQQPE
AIEKPKALSLMLHTADISHPAKAWDLHHRWTMSLLEEFFRQGDREAELGLPFSPLCDRKS
TMVAQSQVGFIDFIVEPTFTVLTDMTEKIVSPLIDETSQTGGTGQRRSSLNSISSSDAKR
SGVKTSGSEGSAPINNSVISVDYKSFKATWTEVVHINRERWRAKVPKEEKAKKEAEEKAR
LAAEEQQKEMEAKSQAEEGASGKAEKKTSGETKNQVNGTRANKSDNPRGKNSKAEKSSGE
QQQNGDFKDGKNKTDKKDHSNIGNDSKKTDGTKQRSHGSPAPSTSSTCRLTLPVIKPPLR
HFKRPAYASSSYAPSVSKKTDEHPARYKMLDQRIKMKKIQNISHNWNRK
Enzyme 21 Number of Residues 709
Enzyme 21 Molecular Weight 80759.7
Enzyme 21 Theoretical pI 9.31
Enzyme 21 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 21 General Function Involved in catalytic activity
Enzyme 21 Specific Function Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a high affinity for both cAMP and cGMP
Enzyme 21 Pathways
Enzyme 21 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 193786355 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q14123 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name PDE1C_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >2130 bp
ATGGAGTCGCCAACCAAGGAGATTGAAGAATTTGAGAGCAACTCTCTGAAATACCTGCAA
CCGGAACAGATCGAGAAAATCTGGCTTCGGCTCCGCGGGCTGAGGAAATATAAGAAAACG
TCCCAGAGATTACGGTCTTTGGTCAAACAATTAGAGAGAGGGGAAGCTTCAGTGGTAGAT
CTTAAGAAGAATTTGGAATATGCAGCCACAGTGCTTGAATCTGTGTATATTGATGAAACA
AGGAGACTCCTGGATACAGAGGATGAGCTCAGTGACATTCAGTCAGATGCTGTGCCTTCT
GAGGTCCGAGACTGGCTGGCCTCCACCTTCACGCGGCAGATGGGGATGATGCTCAGGAGG
AGCGACGAGAAGCCCCGGTTCAAGAGCATCGTTCACGCAGTGCAGGCTGGGATATTTGTG
GAGAGAATGTATAGACGGACATCAAACATGGTTGGACTGAGCTATCCACCAGCTGTTATT
GAGGCATTAAAGGATGTGGACAAGTGGTCCTTTGACGTCTTTTCCCTCAATGAGGCCAGT
GGGGATCATGCACTGAAATTTATTTTCTATGAACTACTCACACGTTATGATCTGATCAGC
CGTTTCAAGATCCCCATTTCTGCACTTGTCTCATTTGTGGAGGCCCTGGAAGTGGGATAC
AGCAAGCACAAAAATCCTTACCATAACTTAATGCACGCTGCCGATGTTACACAGACAGTG
CATTACCTCCTCTATAAGACAGGAGTGGCGAACTGGCTGACGGAGCTGGAGATCTTTGCT
ATAATCTTCTCAGCTGCCATCCATGACTACGAGCATACCGGAACCACCAACAATTTCCAC
ATTCAGACTCGGTCTGATCCAGCTATTCTGTATAATGACAGATCTGTACTGGAGAATCAC
CATTTAAGTGCAGCTTATCGCCTTCTGCAAGATGACGAGGAAATGAATATTTTGATTAAC
CTCTCAAAGGATGACTGGAGGGAGTTTCGAACCTTGGTAATTGAAATGGTGATGGCCACA
GATATGTCTTGTCACTTCCAACAAATCAAAGCAATGAAGACTGCTCTGCAGCAGCCAGAA
GCCATTGAAAAGCCAAAAGCCTTATCCCTTATGCTGCATACAGCAGATATTAGCCATCCA
GCAAAAGCATGGGACCTCCATCATCGCTGGACAATGTCACTCCTGGAGGAGTTCTTCAGA
CAGGGTGACAGAGAAGCAGAGCTGGGGCTGCCTTTTTCTCCTCTGTGTGACCGAAAGTCC
ACTATGGTTGCTCAGTCACAAGTAGGTTTCATTGATTTCATCGTGGAACCCACCTTCACT
GTGCTTACGGACATGACCGAGAAGATTGTGAGTCCATTAATCGATGAAACCTCTCAAACT
GGTGGGACAGGACAGAGGCGTTCGAGTTTGAATAGCATCAGCTCGTCAGATGCCAAGCGA
TCAGGTGTCAAGACCTCTGGTTCAGAGGGAAGTGCCCCGATCAACAATTCTGTCATCTCC
GTTGACTATAAGAGCTTTAAAGCTACTTGGACGGAAGTGGTGCACATCAATCGGGAGAGA
TGGAGGGCCAAGGTACCCAAAGAGGAGAAGGCCAAGAAGGAAGCAGAGGAAAAGGCTCGC
CTGGCCGCAGAGGAGCAGCAAAAGGAAATGGAAGCCAAAAGCCAGGCTGAAGAAGGCGCA
TCCGGCAAAGCTGAGAAAAAGACGTCTGGAGAAACTAAGAATCAAGTCAATGGAACACGG
GCAAACAAAAGTGACAACCCTCGTGGGAAAAATTCCAAAGCCGAGAAGTCATCAGGAGAA
CAGCAACAGAATGGTGACTTCAAAGATGGTAAAAATAAGACAGACAAGAAGGATCACTCT
AACATCGGAAATGATTCAAAGAAAACAGATGGCACAAAACAGCGTTCTCACGGCTCACCA
GCCCCAAGCACCAGCTCCACGTGTCGCCTTACGTTGCCAGTCATCAAGCCTCCTTTGCGT
CATTTTAAACGCCCTGCTTACGCATCTAGCTCCTATGCACCTTCAGTCTCAAAGAAAACT
GATGAGCATCCTGCAAGGTACAAGATGCTGGATCAGAGGATCAAAATGAAAAAGATTCAG
AACATCTCACATAACTGGAACAGAAAATAG
Enzyme 21 GenBank Gene ID AK056170 Link Image
Enzyme 21 GeneCard ID PDE1C Link Image
Enzyme 21 GenAtlas ID PDE1C Link Image
Enzyme 21 HGNC ID HGNC:8776 Link Image
Enzyme 21 Chromosome Location 7
Enzyme 21 Locus 7p14.3
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Loughney K, Martins TJ, Harris EA, Sadhu K, Hicks JB, Sonnenburg WK, Beavo JA, Ferguson K: Isolation and characterization of cDNAs corresponding to two human calcium, calmodulin-regulated, 3',5'-cyclic nucleotide phosphodiesterases. J Biol Chem. 1996 Jan 12;271(2):796-806. [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. 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 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5881
Enzyme 22 Name cAMP-specific 3',5'-cyclic phosphodiesterase 4B
Enzyme 22 Synonyms
  1. DPDE4
  2. PDE32
Enzyme 22 Gene Name PDE4B
Enzyme 22 Protein Sequence >cAMP-specific 3',5'-cyclic phosphodiesterase 4B
MKKSRSVMTVMADDNVKDYFECSLSKSYSSSSNTLGIDLWRGRRCCSGNLQLPPLSQRQS
ERARTPEGDGISRPTTLPLTTLPSIAITTVSQECFDVENGPSPGRSPLDPQASSSAGLVL
HATFPGHSQRRESFLYRSDSDYDLSPKAMSRNSSLPSEQHGDDLIVTPFAQVLASLRSVR
NNFTILTNLHGTSNKRSPAASQPPVSRVNPQEESYQKLAMETLEELDWCLDQLETIQTYR
SVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEYISNTFLDKQNDVEIPSPTQKDREKKK
KQQLMTQISGVKKLMHSSSLNNTSISRFGVNTENEDHLAKELEDLNKWGLNIFNVAGYSH
NRPLTCIMYAIFQERDLLKTFRISSDTFITYMMTLEDHYHSDVAYHNSLHAADVAQSTHV
LLSTPALDAVFTDLEILAAIFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHL
AVGFKLLQEEHCDIFMNLTKKQRQTLRKMVIDMVLATDMSKHMSLLADLKTMVETKKVTS
SGVLLLDNYTDRIQVLRNMVHCADLSNPTKSLELYRQWTDRIMEEFFQQGDKERERGMEI
SPMCDKHTASVEKSQVGFIDYIVHPLWETWADLVQPDAQDILDTLEDNRNWYQSMIPQSP
SPPLDEQNRDCQGLMEKFQFELTLDEEDSEGPEKEGEGHSYFSSTKTLCVIDPENRDSLG
ETDIDIATEDKSPVDT
Enzyme 22 Number of Residues 736
Enzyme 22 Molecular Weight 83342.7
Enzyme 22 Theoretical pI 4.89
Enzyme 22 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 22 General Function Involved in catalytic activity
Enzyme 22 Specific Function Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in mediating central nervous system effects of therapeutic agents ranging from antidepressants to antiasthmatic and anti-inflammatory agents
Enzyme 22 Pathways
Enzyme 22 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein Not Available
Enzyme 22 UniProtKB/Swiss-Prot ID Q07343 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name PDE4B_HUMAN Link Image
Enzyme 22 PDB ID 1TB5 Link Image
Enzyme 22 PDB File Show
Enzyme 22 3D Structure
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >2211 bp
ATGAAGAAAAGCAGGAGTGTGATGACGGTGATGGCTGATGATAATGTTAAAGATTATTTT
GAATGTAGCTTGAGTAAATCCTACAGTTCTTCCAGTAACACACTTGGGATCGACCTCTGG
AGAGGGAGAAGGTGTTGCTCAGGAAACTTACAGTTACCACCACTGTCTCAAAGACAGAGT
GAAAGGGCAAGGACTCCTGAGGGAGATGGTATTTCCAGGCCGACCACACTGCCTTTGACA
ACGCTTCCAAGCATTGCTATTACAACTGTAAGCCAGGAGTGCTTTGATGTGGAAAATGGC
CCTTCCCCAGGTCGGAGTCCACTGGATCCCCAGGCCAGCTCTTCCGCTGGGCTGGTACTT
CACGCCACCTTTCCTGGGCACAGCCAGCGCAGAGAGTCATTTCTCTACAGATCAGACAGC
GACTATGACTTGTCACCAAAGGCGATGTCGAGAAACTCTTCTCTTCCAAGCGAGCAACAC
GGCGATGACTTGATTGTAACTCCTTTTGCCCAGGTCCTTGCCAGCTTGCGAAGTGTGAGA
AACAACTTCACTATACTGACAAACCTTCATGGTACATCTAACAAGAGGTCCCCAGCTGCT
AGTCAGCCTCCTGTCTCCAGAGTCAACCCACAAGAAGAATCTTATCAAAAATTAGCAATG
GAAACGCTGGAGGAATTAGACTGGTGTTTAGACCAGCTAGAGACCATACAGACCTACCGG
TCTGTCAGTGAGATGGCTTCTAACAAGTTCAAAAGAATGCTGAACCGGGAGCTGACACAC
CTCTCAGAGATGAGCCGATCAGGGAACCAGGTGTCTGAATACATTTCAAATACTTTCTTA
GACAAGCAGAATGATGTGGAGATCCCATCTCCTACCCAGAAAGACAGGGAGAAAAAGAAA
AAGCAGCAGCTCATGACCCAGATAAGTGGAGTGAAGAAATTAATGCATAGTTCAAGCCTA
AACAATACAAGCATCTCACGCTTTGGAGTCAACACTGAAAATGAAGATCACCTGGCCAAG
GAGCTGGAAGACCTGAACAAATGGGGTCTTAACATCTTTAATGTGGCTGGATATTCTCAC
AATAGACCCCTAACATGCATCATGTATGCTATATTCCAGGAAAGAGACCTCCTAAAGACA
TTCAGAATCTCATCTGACACATTTATAACCTACATGATGACTTTAGAAGACCATTACCAT
TCTGACGTGGCATATCACAACAGCCTGCACGCTGCTGATGTAGCCCAGTCGACCCATGTT
CTCCTTTCTACACCAGCATTAGACGCTGTCTTCACAGATTTGGAGATCCTGGCTGCCATT
TTTGCAGCTGCCATCCATGACGTTGATCATCCTGGAGTCTCCAATCAGTTTCTCATCAAC
ACAAATTCAGAACTTGCTTTGATGTATAATGATGAATCTGTGTTGGAAAATCATCACCTT
GCTGTGGGTTTCAAACTGCTGCAAGAAGAACACTGTGACATCTTCATGAATCTCACCAAG
AAGCAGCGTCAGACACTCAGGAAGATGGTTATTGACATGGTGTTAGCAACTGATATGTCT
AAACATATGAGCCTGCTGGCAGACCTGAAGACAATGGTAGAAACGAAGAAAGTTACAAGT
TCAGGCGTTCTTCTCCTAGACAACTATACCGATCGCATTCAGGTCCTTCGCAACATGGTA
CACTGTGCAGACCTGAGCAACCCCACCAAGTCCTTGGAATTGTATCGGCAATGGACAGAC
CGCATCATGGAGGAATTTTTCCAGCAGGGAGACAAAGAGCGGGAGAGGGGAATGGAAATT
AGCCCAATGTGTGATAAACACACAGCTTCTGTGGAAAAATCCCAGGTTGGTTTCATCGAC
TACATTGTCCATCCATTGTGGGAGACATGGGCAGATTTGGTACAGCCTGATGCTCAGGAC
ATTCTCGATACCTTAGAAGATAACAGGAACTGGTATCAGAGCATGATACCTCAAAGTCCC
TCACCACCACTGGACGAGCAGAACAGGGACTGCCAGGGTCTGATGGAGAAGTTTCAGTTT
GAACTGACTCTCGATGAGGAAGATTCTGAAGGACCTGAGAAGGAGGGAGAGGGACACAGC
TATTTCAGCAGCACAAAGACGCTTTGTGTGATTGATCCAGAAAACAGAGATTCCCTGGGA
GAGACTGACATAGACATTGCAACAGAAGACAAGTCCCCCGTGGATACATAA
Enzyme 22 GenBank Gene ID L20966 Link Image
Enzyme 22 GeneCard ID PDE4B Link Image
Enzyme 22 GenAtlas ID PDE4B Link Image
Enzyme 22 HGNC ID HGNC:8781 Link Image
Enzyme 22 Chromosome Location 1
Enzyme 22 Locus 1p31
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed Link Image]
  2. Huston E, Lumb S, Russell A, Catterall C, Ross AH, Steele MR, Bolger GB, Perry MJ, Owens RJ, Houslay MD: Molecular cloning and transient expression in COS7 cells of a novel human PDE4B cAMP-specific phosphodiesterase, HSPDE4B3. Biochem J. 1997 Dec 1;328 ( Pt 2):549-58. [PubMed Link Image]
  3. McLaughlin MM, Cieslinski LB, Burman M, Torphy TJ, Livi GP: A low-Km, rolipram-sensitive, cAMP-specific phosphodiesterase from human brain. Cloning and expression of cDNA, biochemical characterization of recombinant protein, and tissue distribution of mRNA. J Biol Chem. 1993 Mar 25;268(9):6470-6. [PubMed Link Image]
  4. Xu RX, Hassell AM, Vanderwall D, Lambert MH, Holmes WD, Luther MA, Rocque WJ, Milburn MV, Zhao Y, Ke H, Nolte RT: Atomic structure of PDE4: insights into phosphodiesterase mechanism and specificity. Science. 2000 Jun 9;288(5472):1822-5. [PubMed Link Image]
  5. Xu RX, Rocque WJ, Lambert MH, Vanderwall DE, Luther MA, Nolte RT: Crystal structures of the catalytic domain of phosphodiesterase 4B complexed with AMP, 8-Br-AMP, and rolipram. J Mol Biol. 2004 Mar 19;337(2):355-65. [PubMed Link Image]
  6. Zhang KY, Card GL, Suzuki Y, Artis DR, Fong D, Gillette S, Hsieh D, Neiman J, West BL, Zhang C, Milburn MV, Kim SH, Schlessinger J, Bollag G: A glutamine switch mechanism for nucleotide selectivity by phosphodiesterases. Mol Cell. 2004 Jul 23;15(2):279-86. [PubMed Link Image]
  7. Card GL, England BP, Suzuki Y, Fong D, Powell B, Lee B, Luu C, Tabrizizad M, Gillette S, Ibrahim PN, Artis DR, Bollag G, Milburn MV, Kim SH, Schlessinger J, Zhang KY: Structural basis for the activity of drugs that inhibit phosphodiesterases. Structure. 2004 Dec;12(12):2233-47. [PubMed Link Image]
  8. Card GL, Blasdel L, England BP, Zhang C, Suzuki Y, Gillette S, Fong D, Ibrahim PN, Artis DR, Bollag G, Milburn MV, Kim SH, Schlessinger J, Zhang KY: A family of phosphodiesterase inhibitors discovered by cocrystallography and scaffold-based drug design. Nat Biotechnol. 2005 Feb;23(2):201-7. Epub 2005 Jan 30. [PubMed Link Image]
  9. Wang H, Peng MS, Chen Y, Geng J, Robinson H, Houslay MD, Cai J, Ke H: Structures of the four subfamilies of phosphodiesterase-4 provide insight into the selectivity of their inhibitors. Biochem J. 2007 Dec 1;408(2):193-201. [PubMed Link Image]
  10. Hamblin JN, Angell TD, Ballantine SP, Cook CM, Cooper AW, Dawson J, Delves CJ, Jones PS, Lindvall M, Lucas FS, Mitchell CJ, Neu MY, Ranshaw LE, Solanke YE, Somers DO, Wiseman JO: Pyrazolopyridines as a novel structural class of potent and selective PDE4 inhibitors. Bioorg Med Chem Lett. 2008 Jul 15;18(14):4237-41. Epub 2008 May 17. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5884
Enzyme 23 Name cAMP-specific 3',5'-cyclic phosphodiesterase 7B
Enzyme 23 Synonyms Not Available
Enzyme 23 Gene Name PDE7B
Enzyme 23 Protein Sequence >cAMP-specific 3',5'-cyclic phosphodiesterase 7B
MSCLMVERCGEILFENPDQNAKCVCMLGDIRLRGQTGVRAERRGSYPFIDFRLLNSTTYS
GEIGTKKKVKRLLSFQRYFHASRLLRGIIPQAPLHLLDEDYLGQARHMLSKVGMWDFDIF
LFDRLTNGNSLVTLLCHLFNTHGLIHHFKLDMVTLHRFLVMVQEDYHSQNPYHNAVHAAD
VTQAMHCYLKEPKLASFLTPLDIMLGLLAAAAHDVDHPGVNQPFLIKTNHHLANLYQNMS
VLENHHWRSTIGMLRESRLLAHLPKEMTQDIEQQLGSLILATDINRQNEFLTRLKAHLHN
KDLRLEDAQDRHFMLQIALKCADICNPCRIWEMSKQWSERVCEEFYRQGELEQKFELEIS
PLCNQQKDSIPSIQIGFMSYIVEPLFREWAHFTGNSTLSENMLGHLAHNKAQWKSLLPRQ
HRSRGSSGSGPDHDHAGQGTESEEQEGDSP
Enzyme 23 Number of Residues 450
Enzyme 23 Molecular Weight 51834.9
Enzyme 23 Theoretical pI 7.03
Enzyme 23 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 23 General Function Involved in catalytic activity
Enzyme 23 Specific Function Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in the control of cAMP-mediated neural activity and cAMP metabolism in the brain
Enzyme 23 Pathways
Enzyme 23 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 8439497 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q9NP56 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name PDE7B_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1353 bp
ATGTCTTGTTTAATGGTTGAGAGGTGTGGCGAAATCTTGTTTGAGAACCCCGATCAGAAT
GCCAAATGTGTTTGCATGCTGGGAGATATACGACTAAGGGGTCAGACGGGGGTTCGTGCT
GAACGCCGTGGCTCCTACCCATTCATTGACTTCCGCCTACTTAACAGTACAACATACTCA
GGGGAGATTGGCACCAAGAAAAAGGTGAAAAGACTATTAAGCTTTCAAAGATACTTCCAT
GCATCAAGGCTGCTTCGTGGAATTATACCACAAGCCCCTCTGCACCTGCTGGATGAAGAC
TACCTTGGACAAGCAAGGCATATGCTCTCCAAAGTGGGAATGTGGGATTTTGACATTTTC
TTGTTTGATCGCTTGACAAATGGAAACAGCCTGGTAACACTGTTGTGCCACCTCTTCAAT
ACCCATGGACTCATTCACCATTTCAAGTTAGATATGGTGACCTTACACCGATTTTTAGTC
ATGGTTCAAGAAGATTACCACAGCCAAAACCCGTATCACAATGCTGTTCACGCAGCCGAC
GTCACCCAGGCCATGCACTGCTACCTGAAAGAGCCAAAGCTTGCCAGCTTCCTCACGCCT
CTGGACATCATGCTTGGACTGCTGGCTGCAGCAGCACACGATGTGGACCACCCAGGGGTG
AACCAGCCATTTTTGATAAAAACTAACCACCATCTTGCAAACCTATATCAGAATATGTCT
GTGCTGGAGAATCATCACTGGCGATCTACAATTGGCATGCTTCGAGAATCAAGGCTTCTT
GCTCATTTGCCAAAGGAAATGACACAGGATATTGAACAGCAGCTGGGCTCCTTGATCTTG
GCAACAGACATCAACAGGCAGAATGAATTTTTGACCAGATTGAAAGCTCACCTCCACAAT
AAAGACTTAAGACTGGAGGATGCACAGGACAGGCACTTTATGCTTCAGATCGCCTTGAAG
TGTGCTGACATTTGCAATCCTTGTAGAATCTGGGAGATGAGCAAGCAGTGGAGTGAAAGG
GTCTGTGAAGAATTCTACAGGCAAGGTGAACTTGAACAGAAATTTGAACTGGAAATCAGT
CCTCTTTGTAATCAACAGAAAGATTCCATCCCTAGTATACAAATTGGTTTCATGAGCTAC
ATCGTGGAGCCGCTCTTCCGGGAATGGGCCCATTTCACGGGTAACAGCACCCTGTCGGAG
AACATGCTGGGCCACCTCGCACACAACAAGGCCCAGTGGAAGAGCCTGTTGCCCAGGCAG
CACAGAAGCAGGGGCAGCAGTGGCAGCGGGCCTGACCACGACCACGCAGGCCAAGGGACT
GAGAGCGAGGAGCAGGAAGGCGACAGCCCCTAG
Enzyme 23 GenBank Gene ID AB038040 Link Image
Enzyme 23 GeneCard ID PDE7B Link Image
Enzyme 23 GenAtlas ID PDE7B Link Image
Enzyme 23 HGNC ID HGNC:8792 Link Image
Enzyme 23 Chromosome Location 6
Enzyme 23 Locus 6q23-q24
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Sasaki T, Kotera J, Yuasa K, Omori K: Identification of human PDE7B, a cAMP-specific phosphodiesterase. Biochem Biophys Res Commun. 2000 May 19;271(3):575-83. [PubMed Link Image]
  2. Gardner C, Robas N, Cawkill D, Fidock M: Cloning and characterization of the human and mouse PDE7B, a novel cAMP-specific cyclic nucleotide phosphodiesterase. Biochem Biophys Res Commun. 2000 May 27;272(1):186-92. [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. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  6. 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 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 5888
Enzyme 24 Name High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
Enzyme 24 Synonyms Not Available
Enzyme 24 Gene Name PDE9A
Enzyme 24 Protein Sequence >High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAM
VSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRRE
GAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFSRAFKINELKAEVANH
LAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDV
PTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLF
CVHDNYRNNPFHNFRHCFCVAQMMYSMVWLCSLQEKFSQTDILILMTAAICHDLDHPGYN
NTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNIFSNIPPDGFKQIRQGMITLI
LATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCL
LEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIML
QPLWESRDRYEELKRIDDAMKELQKKTDSLTSGATEKSRERSRDVKNSEGDCA
Enzyme 24 Number of Residues 593
Enzyme 24 Molecular Weight 68491.9
Enzyme 24 Theoretical pI 6.10
Enzyme 24 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 24 General Function Involved in catalytic activity
Enzyme 24 Specific Function Hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions
  • guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate [RN:R01234]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein Not Available
Enzyme 24 UniProtKB/Swiss-Prot ID O76083 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name PDE9A_HUMAN Link Image
Enzyme 24 PDB ID 1TBM Link Image
Enzyme 24 PDB File Show
Enzyme 24 3D Structure
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >1782 bp
ATGGGATCCGGCTCCTCCAGCTACCGGCCCAAGGCCATCTACCTGGACATCGATGGACGC
ATTCAGAAGGTAATCTTCAGCAAGTACTGCAACTCCAGCGACATCATGGACCTGTTCTGC
ATCGCCACCGGCCTGCCTCGGAACACGACCATCTCCCTGCTGACCACCGACGACGCCATG
GTCTCCATCGACCCCACCATGCCCGCGAATTCAGAACGCACTCCGTACAAAGTGAGACCT
GTGGCCATCAAGCAACTCTCCGCTGGTGTCGAGGACAAGAGAACCACAAGCCGTGGCCAG
TCTGCTGAGAGACCACTGAGGGACAGACGGGTTGTGGGCCTGGAGCAGCCCCGGAGGGAA
GGAGCATTTGAAAGTGGACAGGTAGAGCCCAGGCCCAGAGAGCCCCAGGGCTGCTACCAG
GAAGGCCAGCGCATCCCTCCAGAGAGAGAAGAATTAATCCAGAGCGTGCTGGCGCAGGTT
GCAGAGCAGTTCTCAAGAGCATTCAAAATCAATGAACTGAAAGCTGAAGTTGCAAATCAC
TTGGCTGTCCTAGAGAAACGCGTGGAATTGGAAGGACTAAAAGTGGTGGAGATTGAGAAA
TGCAAGAGTGACATTAAGAAGATGAGGGAGGAGCTGGCGGCCAGAAGCAGCAGGACCAAC
TGCCCCTGTAAGTACAGTTTTTTGGATAACCACAAGAAGTTGACTCCTCGACGCGATGTT
CCCACTTACCCCAAGTACCTGCTCTCTCCAGAGACCATCGAGGCCCTGCGGAAGCCGACC
TTTGACGTCTGGCTTTGGGAGCCCAATGAGATGCTGAGCTGCCTGGAGCACATGTACCAC
GACCTCGGGCTGGTCAGGGACTTCAGCATCAACCCTGTCACCCTCAGGAGGTGGCTGTTC
TGTGTCCACGACAACTACAGAAACAACCCCTTCCACAACTTCCGGCACTGCTTCTGCGTG
GCCCAGATGATGTACAGCATGGTCTGGCTCTGCAGTCTCCAGGAGAAGTTCTCACAAACG
GATATCCTGATCCTAATGACAGCGGCCATCTGCCACGATCTGGACCATCCCGGCTACAAC
AACACGTACCAGATCAATGCCCGCACAGAGCTGGCGGTCCGCTACAATGACATCTCACCG
CTGGAGAACCACCACTGCGCCGTGGCCTTCCAGATCCTCGCCGAGCCTGAGTGCAACATC
TTCTCCAACATCCCACCTGATGGGTTCAAGCAGATCCGACAGGGAATGATCACATTAATC
TTGGCCACTGACATGGCAAGACATGCAGAAATTATGGATTCTTTCAAAGAGAAAATGGAG
AATTTTGACTACAGCAACGAGGAGCACATGACCCTGCTGAAGATGATTTTGATAAAATGC
TGTGATATCTCTAACGAGGTCCGTCCAATGGAAGTCGCAGAGCCTTGGGTGGACTGTTTA
TTAGAGGAATATTTTATGCAGAGCGACCGTGAGAAGTCAGAAGGCCTTCCTGTGGCACCG
TTCATGGACCGAGACAAAGTGACCAAGGCCACAGCCCAGATTGGGTTCATCAAGTTTGTC
CTGATCCCAATGTTTGAAACAGTGACCAAGCTCTTCCCCATGGTTGAGGAGATCATGCTG
CAGCCACTTTGGGAATCCCGAGATCGCTACGAGGAGCTGAAGCGGATAGATGACGCCATG
AAAGAGTTACAGAAGAAGACTGACAGCTTGACGTCTGGGGCCACCGAGAAGTCCAGAGAG
AGAAGCAGAGATGTGAAAAACAGTGAAGGAGACTGTGCCTGA
Enzyme 24 GenBank Gene ID AF048837 Link Image
Enzyme 24 GeneCard ID PDE9A Link Image
Enzyme 24 GenAtlas ID PDE9A Link Image
Enzyme 24 HGNC ID HGNC:8795 Link Image
Enzyme 24 Chromosome Location 2
Enzyme 24 Locus 21q22.3
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Fisher DA, Smith JF, Pillar JS, St Denis SH, Cheng JB: Isolation and characterization of PDE9A, a novel human cGMP-specific phosphodiesterase. J Biol Chem. 1998 Jun 19;273(25):15559-64. [PubMed Link Image]
  2. Guipponi M, Scott HS, Kudoh J, Kawasaki K, Shibuya K, Shintani A, Asakawa S, Chen H, Lalioti MD, Rossier C, Minoshima S, Shimizu N, Antonarakis SE: Identification and characterization of a novel cyclic nucleotide phosphodiesterase gene (PDE9A) that maps to 21q22.3: alternative splicing of mRNA transcripts, genomic structure and sequence. Hum Genet. 1998 Oct;103(4):386-92. [PubMed Link Image]
  3. Rentero C, Monfort A, Puigdomenech P: Identification and distribution of different mRNA variants produced by differential splicing in the human phosphodiesterase 9A gene. Biochem Biophys Res Commun. 2003 Feb 14;301(3):686-92. [PubMed Link Image]
  4. Wang P, Wu P, Egan RW, Billah MM: Identification and characterization of a new human type 9 cGMP-specific phosphodiesterase splice variant (PDE9A5). Differential tissue distribution and subcellular localization of PDE9A variants. Gene. 2003 Sep 18;314:15-27. [PubMed Link Image]
  5. Rentero C, Puigdomenech P: Specific use of start codons and cellular localization of splice variants of human phosphodiesterase 9A gene. BMC Mol Biol. 2006 Nov 8;7:39. [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. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed Link Image]
  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. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed Link Image]
  10. Huai Q, Wang H, Zhang W, Colman RW, Robinson H, Ke H: Crystal structure of phosphodiesterase 9 shows orientation variation of inhibitor 3-isobutyl-1-methylxanthine binding. Proc Natl Acad Sci U S A. 2004 Jun 29;101(26):9624-9. Epub 2004 Jun 21. [PubMed Link Image]
  11. Liu S, Mansour MN, Dillman KS, Perez JR, Danley DE, Aeed PA, Simons SP, Lemotte PK, Menniti FS: Structural basis for the catalytic mechanism of human phosphodiesterase 9. Proc Natl Acad Sci U S A. 2008 Sep 9;105(36):13309-14. Epub 2008 Aug 29. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 5889
Enzyme 25 Name cGMP-dependent 3',5'-cyclic phosphodiesterase
Enzyme 25 Synonyms
  1. Cyclic GMP-stimulated phosphodiesterase
  2. CGS-PDE
  3. cGSPDE
Enzyme 25 Gene Name PDE2A
Enzyme 25 Protein Sequence >cGMP-dependent 3',5'-cyclic phosphodiesterase
MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPPPQPCADSLQDALLSLGSVIDI
SGLQRAVKEALSAVLPRVETVYTYLLDGESQLVCEDPPHELPQEGKVREAIISQKRLGCN
GLGFSDLPGKPLARLVAPLAPDTQVLVMPLADKEAGAVAAVILVHCGQLSDNEEWSLQAV
EKHTLVALRRVQVLQQRGPREAPRAVQNPPEGTAEDQKGGAAYTDRDRKILQLCGELYDL
DASSLQLKVLQYLQQETRASRCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPLTGCLGQVV
EDKKSIQLKDLTSEDVQQLQSMLGCELQAMLCVPVISRATDQVVALACAFNKLEGDLFTD
EDEHVIQHCFHYTSTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITE
ARNLSNAEICSVFLLDQNELVAKVFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPD
AYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELVNKINGPWFSKFDEDLATAF
SIYCGISIAHSLLYKKVNEAQYRSHLANEMMMYHMKVSDDEYTKLLHDGIQPVAAIDSNF
ASFTYTPRSLPEDDTSMAILSMLQDMNFINNYKIDCPTLARFCLMVKKGYRDPPYHNWMH
AFSVSHFCYLLYKNLELTNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYS
SEGSVMERHHFAQAIAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDL
QKMAEVGYDRNNKQHHRLLLCLLMTSCDLSDQTKGWKTTRKIAELIYKEFFSQGDLEKAM
GNRPMEMMDREKAYIPELQISFMEHIAMPIYKLLQDLFPKAAELYERVASNREHWTKVSH
KFTIRGLPSNNSLDFLDEEYEVPDLDGTRAPINGCCSLDAE
Enzyme 25 Number of Residues 941
Enzyme 25 Molecular Weight 105715.8
Enzyme 25 Theoretical pI 5.08
Enzyme 25 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 25 General Function Involved in catalytic activity
Enzyme 25 Specific Function Cyclic nucleotide phosphodiesterase with a dual- specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes
Enzyme 25 Pathways
Enzyme 25 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 2108052 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID O00408 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name PDE2A_HUMAN Link Image
Enzyme 25 PDB ID 1MC0 Link Image
Enzyme 25 PDB File Show
Enzyme 25 3D Structure
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >2826 bp
ATGGGGCAGGCATGCGGCCACTCCATCCTCTGCAGGAGCCAGCAGTACCCGGCAGCGCGA
CCGGCTGAGCCGCGGGGCCAGCAGGTCTTCCTCAAGCCGGACGAGCCGCCGCCGCCGCCG
CAGCCATGCGCCGACAGCCTGCAGGACGCCTTGCTGAGTCTGGGCTCTGTCATCGACATT
TCAGGCCTGCAACGTGCTGTCAAGGAGGCCCTGTCAGCTGTGCTCCCCCGAGTGGAAACT
GTCTACACCTACCTACTGGATGGTGAGTCCCAGCTGGTGTGTGAGGACCCCCCACATGAG
CTGCCCCAGGAGGGGAAAGTCCGGGAGGCTATCATCTCCCAGAAGCGGCTGGGCTGCAAT
GGGCTGGGCTTCTCAGACCTGCCAGGGAAGCCCTTGGCCAGGCTGGTGGCTCCACTGGCT
CCTGATACCCAAGTGCTGGTCATGCCGCTAGCGGACAAGGAGGCTGGGGCCGTGGCAGCT
GTCATCTTGGTGCACTGTGGCCAGCTGAGTGATAATGAGGAATGGAGCCTGCAGGCGGTG
GAGAAGCATACCCTGGTCGCCCTGCGGAGGGTGCAGGTCCTGCAGCAGCGCGGGCCCAGG
GAGGCTCCCCGAGCCGTCCAGAACCCCCCGGAGGGGACGGCGGAAGACCAGAAGGGCGGG
GCGGCGTACACCGACCGCGACCGCAAGATCCTCCAACTGTGCGGGGAACTCTACGACCTG
GATGCCTCTTCCCTGCAGCTCAAAGTGCTCCAATACCTGCAGCAGGAGACCCGGGCATCC
CGCTGCTGCCTCCTGCTGGTGTCGGAGGACAATCTCCAGCTTTCTTGCAAGGTCATCGGA
GACAAAGTGCTCGGGGAAGAGGTCAGCTTTCCCTTGACAGGATGCCTGGGCCAGGTGGTG
GAAGACAAGAAGTCCATCCAGCTGAAGGACCTCACCTCCGAGGATGTACAACAGCTGCAG
AGCATGTTGGGCTGTGAGCTGCAGGCCATGCTCTGTGTCCCTGTCATCAGCCGGGCCACT
GACCAGGTGGTGGCCTTGGCCTGCGCCTTCAACAAGCTAGAAGGAGACTTGTTCACCGAC
GAGGACGAGCATGTGATCCAGCACTGCTTCCACTACACCAGCACCGTGCTCACCAGCACC
CTGGCCTTCCAGAAGGAACAGAAACTCAAGTGTGAGTGCCAGGCTCTTCTCCAAGTGGCA
AAGAACCTCTTCACCCACCTGGATGACGTCTCTGTCCTGCTCCAGGAGATCATCACGGAG
GCCAGAAACCTCAGCAACGCAGAGATCTGCTCTGTGTTCCTGCTGGATCAGAATGAGCTG
GTGGCCAAGGTGTTCGACGGGGGCGTGGTGGATGATGAGAGCTATGAGATCCGCATCCCG
GCCGATCAGGGCATCGCGGGACACGTGGCGACCACGGGCCAGATCCTGAACATCCCTGAC
GCATATGCCCATCCGCTTTTCTACCGCGGCGTGGACGACAGCACCGGCTTCCGCACGCGC
AACATCCTCTGCTTCCCCATCAAGAACGAGAACCAGGAGGTCATCGGTGTGGCCGAGCTG
GTGAACAAGATCAATGGGCCATGGTTCAGCAAGTTCGACGAGGACCTGGCGACGGCCTTC
TCCATCTACTGCGGCATCAGCATCGCCCATTCTCTCCTATACAAAAAAGTGAATGAGGCT
CAGTATCGCAGCCACCTGGCCAATGAGATGATGATGTACCACATGAAGGTCTCCGACGAT
GAGTATACCAAACTTCTCCATGATGGGATCCAGCCTGTGGCTGCCATTGACTCCAATTTT
GCAAGTTTCACCTATACCCCTCGTTCCCTGCCCGAGGATGACACGTCCATGGCCATCCTG
AGCATGCTGCAGGACATGAATTTCATCAACAACTACAAAATTGACTGCCCGACCCTGGCC
CGGTTCTGTTTGATGGTGAAGAAGGGCTACCGGGATCCCCCCTACCACAACTGGATGCAC
GCCTTTTCTGTCTCCCACTTCTGCTACCTGCTCTACAAGAACCTGGAGCTCACCAACTAC
CTCGAGGACATCGAGATCTTTGCCTTGTTTATTTCCTGCATGTGTCATGACCTGGACCAC
AGAGGCACAAACAACTCTTTCCAGGTGGCCTCGAAATCTGTGCTGGCTGCGCTCTACAGC
TCTGAGGGCTCCGTCATGGAGAGGCACCACTTTGCTCAGGCCATCGCCATCCTCAACACC
CACGGCTGCAACATCTTTGATCATTTCTCCCGGAAGGACTATCAGCGCATGCTGGATCTG
ATGCGGGACATCATCTTGGCCACAGACCTGGCCCACCATCTCCGCATCTTCAAGGACCTC
CAGAAGATGGCTGAGGTGGGCTACGACCGAAACAACAAGCAGCACCACAGACTTCTCCTC
TGCCTCCTCATGACCTCCTGTGACCTCTCTGACCAGACCAAGGGCTGGAAGACTACGAGA
AAGATCGCGGAGCTGATCTACAAAGAATTCTTCTCCCAGGGAGACCTGGAGAAGGCCATG
GGCAACAGGCCGATGGAGATGATGGACCGGGAGAAGGCCTATATCCCTGAGCTGCAAATC
AGCTTCATGGAGCACATTGCAATGCCCATCTACAAGCTGTTGCAGGACCTGTTCCCCAAA
GCGGCAGAGCTGTACGAGCGCGTGGCCTCCAACCGTGAGCACTGGACCAAGGTGTCCCAC
AAGTTCACCATCCGCGGCCTCCCAAGTAACAACTCGCTGGACTTCCTGGATGAGGAGTAC
GAGGTGCCTGATCTGGATGGCACTAGGGCCCCCATCAATGGCTGCTGCAGCCTTGATGCT
GAGTGA
Enzyme 25 GenBank Gene ID U67733 Link Image
Enzyme 25 GeneCard ID PDE2A Link Image
Enzyme 25 GenAtlas ID PDE2A Link Image
Enzyme 25 HGNC ID HGNC:8777 Link Image
Enzyme 25 Chromosome Location 1
Enzyme 25 Locus 11q13.4
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Rosman GJ, Martins TJ, Sonnenburg WK, Beavo JA, Ferguson K, Loughney K: Isolation and characterization of human cDNAs encoding a cGMP-stimulated 3',5'-cyclic nucleotide phosphodiesterase. Gene. 1997 May 20;191(1):89-95. [PubMed Link Image]
  2. 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]
  3. Iffland A, Kohls D, Low S, Luan J, Zhang Y, Kothe M, Cao Q, Kamath AV, Ding YH, Ellenberger T: Structural determinants for inhibitor specificity and selectivity in PDE2A using the wheat germ in vitro translation system. Biochemistry. 2005 Jun 14;44(23):8312-25. [PubMed Link Image]
  4. Pandit J, Forman MD, Fennell KF, Dillman KS, Menniti FS: Mechanism for the allosteric regulation of phosphodiesterase 2A deduced from the X-ray structure of a near full-length construct. Proc Natl Acad Sci U S A. 2009 Oct 27;106(43):18225-30. Epub 2009 Oct 14. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 5893
Enzyme 26 Name Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
Enzyme 26 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 26 Gene Name NUDT2
Enzyme 26 Protein Sequence >Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
MALRACGLIIFRRCLIPKVDNNAIEFLLLQASDGIHHWTPPKGHVEPGEDDLETALRETQ
EEAGIEAGQLTIIEGFKRELNYVARNKPKTVIYWLAEVKDYDVEIRLSHEHQAYRWLGLE
EACQLAQFKEMKAALQEGHQFLCSIEA
Enzyme 26 Number of Residues 147
Enzyme 26 Molecular Weight 16829.1
Enzyme 26 Theoretical pI 5.06
Enzyme 26 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 26 General Function Involved in hydrolase activity
Enzyme 26 Specific Function Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis
Enzyme 26 Pathways
Enzyme 26 Reactions
  • P1,P4-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP [RN:R01232]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 55958893 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P50583 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name AP4A_HUMAN Link Image
Enzyme 26 PDB ID 1XSC Link Image
Enzyme 26 PDB File Show
Enzyme 26 3D Structure
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >444 bp
ATGGCCTTGAGAGCATGTGGCTTGATCATCTTCCGAAGATGCCTCATTCCCAAAGTGGAC
AACAATGCAATTGAGTTTTTACTGCTGCAGGCATCAGATGGCATTCATCACTGGACTCCT
CCCAAAGGCCATGTGGAACCAGGAGAGGATGACTTGGAAACAGCCCTGAGGGAGACCCAA
GAGGAAGCAGGCATAGAAGCAGGCCAGCTGACCATTATTGAGGGGTTCAAAAGGGAACTC
AATTATGTGGCCAGGAACAAGCCTAAAACAGTCATTTACTGGCTGGCGGAGGTGAAGGAC
TATGACGTGGAGATCCGCCTCTCCCATGAGCACCAAGCCTACCGCTGGCTGGGGCTGGAG
GAGGCCTGCCAGTTGGCTCAGTTCAAGGAGATGAAGGCAGCGCTCCAAGAAGGACACCAG
TTTCTTTGCTCCATAGAGGCCTGA
Enzyme 26 GenBank Gene ID AL356494 Link Image
Enzyme 26 GeneCard ID NUDT2 Link Image
Enzyme 26 GenAtlas ID NUDT2 Link Image
Enzyme 26 HGNC ID HGNC:8049 Link Image
Enzyme 26 Chromosome Location 9
Enzyme 26 Locus 9p13
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 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 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 5896
Enzyme 27 Name Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
Enzyme 27 Synonyms
  1. GMP-PDE alpha
  2. PDE V-B1
Enzyme 27 Gene Name PDE6A
Enzyme 27 Protein Sequence >Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
MGEVTAEEVEKFLDSNIGFAKQYYNLHYRAKLISDLLGAKEAAVDFSNYHSPSSMEESEI
IFDLLRDFQENLQTEKCIFNVMKKLCFLLQADRMSLFMYRTRNGIAELATRLFNVHKDAV
LEDCLVMPDQEIVFPLDMGIVGHVAHSKKIANVPNTEEDEHFCDFVDILTEYKTKNILAS
PIMNGKDVVAIIMAVNKVDGSHFTKRDEEILLKYLNFANLIMKVYHLSYLHNCETRRGQI
LLWSGSKVFEELTDIERQFHKALYTVRAFLNCDRYSVGLLDMTKQKEFFDVWPVLMGEVP
PYSGPRTPDGREINFYKVIDYILHGKEDIKVIPNPPPDHWALVSGLPAYVAQNGLICNIM
NAPAEDFFAFQKEPLDESGWMIKNVLSMPIVNKKEEIVGVATFYNRKDGKPFDEMDETLM
ESLTQFLGWSVLNPDTYESMNKLENRKDIFQDIVKYHVKCDNEEIQKILKTREVYGKEPW
ECEEEELAEILQAELPDADKYEINKFHFSDLPLTELELVKCGIQMYYELKVVDKFHIPQE
ALVRFMYSLSKGYRKITYHNWRHGFNVGQTMFSLLVTGKLKRYFTDLEALAMVTAAFCHD
IDHRGTNNLYQMKSQNPLAKLHGSSILERHHLEFGKTLLRDESLNIFQNLNRRQHEHAIH
MMDIAIIATDLALYFKKRTMFQKIVDQSKTYESEQEWTQYMMLEQTRKEIVMAMMMTACD
LSAITKPWEVQSQVALLVAAEFWEQGDLERTVLQQNPIPMMDRNKADELPKLQVGFIDFV
CTFVYKEFSRFHEEITPMLDGITNNRKEWKALADEYDAKMKVQEEKKQKQQSAKSAAAGN
QPGGNPSPGGATTSKSCCIQ
Enzyme 27 Number of Residues 860
Enzyme 27 Molecular Weight 99546.6
Enzyme 27 Theoretical pI 5.48
Enzyme 27 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 27 General Function Involved in catalytic activity
Enzyme 27 Specific Function This protein participates in processes of transmission and amplification of the visual signal
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions
  • guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate [RN:R01234]
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 112180437 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID P16499 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name PDE6A_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >2583 bp
ATGGGCGAGGTGACAGCAGAGGAGGTGGAGAAGTTCCTGGACTCGAATATTGGCTTTGCC
AAACAGTACTACAACCTCCACTACCGGGCCAAGCTCATCTCCGACCTCCTTGGGGCCAAG
GAGGCTGCCGTGGACTTCAGCAACTACCACTCCCCGAGCAGCATGGAGGAGAGCGAAATC
ATCTTTGATCTCCTGCGGGACTTTCAGGAGAATTTACAGACAGAGAAATGCATCTTCAAT
GTCATGAAGAAGCTGTGCTTCCTCCTGCAGGCAGACCGCATGAGCCTGTTCATGTACCGG
ACCCGCAATGGCATCGCAGAGCTGGCCACCAGGCTTTTCAATGTCCACAAGGATGCTGTC
CTCGAGGACTGCCTGGTGATGCCCGACCAAGAGATCGTCTTCCCTTTGGACATGGGCATC
GTGGGCCATGTCGCACACTCTAAGAAGATTGCTAACGTCCCCAACACAGAGGAGGATGAG
CATTTCTGTGACTTTGTGGACATCCTCACAGAGTACAAGACCAAGAACATCTTGGCTTCC
CCCATAATGAATGGGAAGGATGTGGTGGCCATAATCATGGCTGTGAATAAAGTGGATGGA
TCCCACTTCACCAAGAGAGATGAAGAGATTCTTCTCAAGTACCTCAATTTTGCAAATCTA
ATCATGAAGGTGTACCACCTGAGTTACCTGCACAACTGTGAAACTCGACGTGGCCAGATA
CTGCTGTGGTCTGGGAGCAAAGTCTTTGAAGAACTTACGGACATCGAACGACAGTTCCAC
AAAGCCCTGTACACAGTCCGTGCTTTCCTCAACTGTGACAGATACTCTGTGGGTCTCTTA
GACATGACCAAGCAGAAGGAATTTTTTGATGTGTGGCCGGTTCTGATGGGTGAAGTTCCA
CCTTACTCTGGTCCCAGGACTCCGGATGGAAGAGAAATTAACTTTTACAAGGTCATTGAC
TACATCCTGCATGGCAAAGAGGACATCAAAGTCATCCCGAATCCACCTCCTGACCATTGG
GCTTTAGTAAGCGGTCTCCCAGCTTATGTTGCCCAGAATGGCCTGATTTGCAACATCATG
AATGCGCCTGCGGAGGACTTTTTTGCATTTCAGAAAGAACCTCTGGATGAGTCTGGATGG
ATGATTAAAAATGTGCTTTCAATGCCGATTGTGAACAAGAAGGAAGAAATTGTTGGAGTG
GCCACATTTTACAATCGTAAAGATGGGAAGCCCTTTGATGAAATGGATGAGACGCTCATG
GAGTCTTTGACTCAATTTCTGGGCTGGTCTGTCTTAAATCCTGACACCTATGAGTCAATG
AATAAACTTGAAAATAGGAAGGATATTTTCCAGGACATAGTAAAATATCATGTGAAGTGT
GACAATGAAGAAATTCAGAAAATCTTGAAAACCAGAGAGGTGTATGGGAAGGAGCCATGG
GAGTGTGAGGAAGAGGAGCTGGCTGAGATCCTGCAAGCGGAGCTGCCAGATGCAGATAAA
TACGAAATTAATAAATTTCACTTCAGTGACTTACCCCTAACAGAACTGGAGCTGGTAAAA
TGTGGAATACAGATGTATTATGAGCTCAAAGTGGTGGATAAATTTCACATTCCACAAGAG
GCCCTGGTGCGGTTCATGTACTCCCTGAGTAAGGGCTACCGCAAGATCACCTACCACAAC
TGGCGGCACGGCTTCAACGTGGGGCAGACCATGTTCTCCCTGCTGGTGACGGGAAAGCTG
AAGCGCTACTTCACGGACCTAGAGGCCTTGGCCATGGTCACTGCTGCTTTCTGCCATGAC
ATTGACCACAGAGGCACCAATAACCTCTACCAGATGAAATCCCAGAACCCACTGGCCAAG
CTCCATGGGTCCTCTATCTTGGAAAGACACCACTTGGAGTTTGGCAAAACACTGCTCAGA
GACGAGAGCCTGAATATCTTTCAAAACCTCAATCGTCGACAGCATGAGCATGCCATCCAC
ATGATGGACATTGCAATCATTGCCACAGACCTCGCCCTGTATTTCAAGAAGAGGACGATG
TTCCAAAAGATCGTGGATCAGTCTAAGACATATGAGAGTGAACAGGAGTGGACACAGTAC
ATGATGCTGGAGCAGACACGGAAGGAAATCGTTATGGCCATGATGATGACCGCCTGTGAT
CTCTCAGCCATCACCAAACCCTGGGAGGTGCAGAGCCAGGTAGCTCTGCTGGTGGCTGCT
GAATTCTGGGAACAAGGTGACCTGGAGCGCACGGTGCTGCAACAGAATCCCATTCCCATG
ATGGACAGAAACAAAGCAGATGAACTCCCTAAGCTTCAAGTCGGCTTCATTGACTTTGTT
TGCACCTTCGTCTACAAGGAATTCTCCCGTTTCCACGAGGAGATCACCCCAATGTTGGAC
GGGATCACCAACAATCGCAAGGAGTGGAAGGCGCTTGCTGATGAGTACGATGCCAAGATG
AAGGTGCAGGAGGAGAAGAAGCAGAAACAGCAGTCGGCCAAGTCAGCAGCCGCAGGAAAT
CAGCCGGGGGGAAACCCCAGCCCAGGGGGTGCAACTACATCCAAGTCCTGCTGCATCCAG
TAA
Enzyme 27 GenBank Gene ID BC035909 Link Image
Enzyme 27 GeneCard ID PDE6A Link Image
Enzyme 27 GenAtlas ID PDE6A Link Image
Enzyme 27 HGNC ID HGNC:8785 Link Image
Enzyme 27 Chromosome Location 5
Enzyme 27 Locus 5q31.2-q34
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Pittler SJ, Baehr W, Wasmuth JJ, McConnell DG, Champagne MS, vanTuinen P, Ledbetter D, Davis RL: Molecular characterization of human and bovine rod photoreceptor cGMP phosphodiesterase alpha-subunit and chromosomal localization of the human gene. Genomics. 1990 Feb;6(2):272-83. [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. Huang SH, Pittler SJ, Huang X, Oliveira L, Berson EL, Dryja TP: Autosomal recessive retinitis pigmentosa caused by mutations in the alpha subunit of rod cGMP phosphodiesterase. Nat Genet. 1995 Dec;11(4):468-71. [PubMed Link Image]
  4. Dryja TP, Rucinski DE, Chen SH, Berson EL: Frequency of mutations in the gene encoding the alpha subunit of rod cGMP-phosphodiesterase in autosomal recessive retinitis pigmentosa. Invest Ophthalmol Vis Sci. 1999 Jul;40(8):1859-65. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 5902
Enzyme 28 Name High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B
Enzyme 28 Synonyms
  1. HsPDE8B
  2. Cell proliferation-inducing gene 22 protein
Enzyme 28 Gene Name PDE8B
Enzyme 28 Protein Sequence >High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B
MGCAPSIHVSQSGVIYCRDSDESSSPRQTTSVSQGPAAPLPGLFVQTDAADAIPPSRASG
PPSVARVRRARTELGSGSSAGSAAPAATTSRGRRRHCCSSAEAETQTCYTSVKQVSSAEV
RIGPMRLTQDPIQVLLIFAKEDSQSDGFWWACDRAGYRCNIARTPESALECFLDKHHEII
VIDHRQTQNFDAEAVCRSIRATNPSEHTVILAVVSRVSDDHEEASVLPLLHAGFNRRFME
NSSIIACYNELIQIEHGEVRSQFKLRACNSVFTALDHCHEAIEITSDDHVIQYVNPAFER
MMGYHKGELLGKELADLPKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVK
ITPVIGQGGKIRHFVSLKKLCCTTDNNKQIHKIHRDSGDNSQTEPHSFRYKNRRKESIDV
KSISSRGSDAPSLQNRRYPSMARIHSMTIEAPITKVINIINAAQENSPVTVAEALDRVLE
ILRTTELYSPQLGTKDEDPHTSDLVGGLMTDGLRRLSGNEYVFTKNVHQSHSHLAMPITI
NDVPPCISQLLDNEESWDFNIFELEAITHKRPLVYLGLKVFSRFGVCEFLNCSETTLRAW
FQVIEANYHSSNAYHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHP
GRTNSFLCNAGSELAVLYNDTAVLESHHTALAFQLTVKDTKCNIFKNIDRNHYRTLRQAI
IDMVLATEMTKHFEHVNKFVNSINKPMAAEIEGSDCECNPAGKNFPENQILIKRMMIKCA
DVANPCRPLDLCIEWAGRISEEYFAQTDEEKRQGLPVVMPVFDRNTCSIPKSQISFIDYF
ITDMFDAWDAFAHLPALMQHLADNYKHWKTLDDLKCKSLRLPSDS
Enzyme 28 Number of Residues 885
Enzyme 28 Molecular Weight 98977.9
Enzyme 28 Theoretical pI 6.81
Enzyme 28 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • molecular transducer activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • signal transducer activity
  • two-component response regulator activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
  • signal transduction
  • signal transmission
  • signaling process
  • two-component signal transduction system (phosphorelay)
Component
Enzyme 28 General Function Involved in catalytic activity
Enzyme 28 Specific Function Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in specific signaling in the thyroid gland
Enzyme 28 Pathways
Enzyme 28 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 27372873 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID O95263 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name PDE8B_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >2658 bp
ATGGGCTGCGCCCCCAGCATCCATGTCTCGCAGAGCGGCGTGATCTACTGCCGGGACTCG
GACGAGTCCAGCTCGCCCCGCCAGACCACCAGCGTGTCGCAGGGCCCGGCGGCACCCCTG
CCCGGCCTCTTCGTCCAGACCGACGCCGCCGACGCCATCCCCCCGAGCCGCGCGTCGGGA
CCCCCCAGCGTAGCCCGCGTCCGCAGGGCCCGCACCGAGCTGGGCAGCGGTAGCAGCGCG
GGTTCCGCAGCCCCCGCCGCGACCACCAGCAGGGGCCGGAGGCGCCACTGCTGCAGCAGC
GCCGAGGCCGAGACTCAGACCTGCTACACCAGCGTGAAGCAGGTGTCTTCTGCGGAGGTG
CGCATCGGGCCCATGAGACTGACGCAGGACCCTATTCAGGTTTTGCTGATCTTTGCAAAG
GAAGATAGTCAGAGCGATGGCTTCTGGTGGGCCTGCGACAGAGCTGGTTATAGATGCAAT
ATTGCTCGGACTCCAGAGTCAGCCCTTGAATGCTTTCTTGATAAGCATCATGAAATTATT
GTAATTGATCATAGACAAACTCAGAACTTCGATGCAGAAGCAGTGTGCAGGTCGATCCGG
GCCACAAATCCCTCCGAGCACACGGTGATCCTCGCAGTGGTTTCGCGAGTATCGGATGAC
CATGAAGAGGCGTCAGTCCTTCCTCTTCTCCACGCAGGCTTCAACAGGAGATTTATGGAG
AATAGCAGCATAATTGCTTGCTATAATGAACTGATTCAAATAGAACATGGGGAAGTTCGC
TCCCAGTTCAAATTACGGGCCTGTAATTCAGTGTTTACAGCATTAGATCACTGTCATGAA
GCCATAGAAATAACAAGCGATGACCACGTGATTCAGTATGTCAACCCAGCCTTCGAAAGG
ATGATGGGCTACCACAAAGGTGAGCTCCTGGGAAAAGAACTCGCTGATCTGCCCAAAAGC
GATAAGAACCGGGCAGACCTTCTCGACACCATCAATACATGCATCAAGAAGGGAAAGGAG
TGGCAGGGGGTTTACTATGCCAGACGGAAATCCGGGGACAGCATCCAACAGCACGTGAAG
ATCACCCCAGTGATTGGCCAAGGAGGGAAAATTAGGCATTTTGTCTCGCTCAAGAAACTG
TGTTGTACCACTGACAATAATAAGCAGATTCACAAGATTCATCGTGATTCAGGAGACAAT
TCTCAGACAGAGCCTCATTCATTCAGATATAAGAACAGGAGGAAAGAGTCCATTGACGTG
AAATCGATATCATCTCGAGGCAGTGATGCACCAAGCCTGCAGAATCGTCGCTATCCGTCC
ATGGCGAGGATCCACTCCATGACCATCGAGGCTCCCATCACAAAGGTTATAAATATAATC
AATGCAGCCCAAGAAAACAGCCCAGTCACAGTAGCGGAAGCCTTGGACAGAGTTCTAGAG
ATTTTACGGACCACAGAACTGTACTCCCCTCAGCTGGGTACCAAAGATGAAGATCCCCAC
ACCAGTGATCTTGTTGGAGGCCTGATGACTGACGGCTTGAGAAGACTGTCAGGAAACGAG
TATGTGTTTACTAAGAATGTGCACCAGAGTCACAGTCACCTTGCAATGCCAATAACCATC
AATGATGTTCCCCCTTGTATCTCTCAATTACTTGATAATGAGGAGAGTTGGGACTTCAAC
ATCTTTGAATTGGAAGCCATTACGCATAAAAGGCCATTGGTTTATCTGGGCTTAAAGGTC
TTCTCTCGGTTTGGAGTATGTGAGTTTTTAAACTGTTCTGAAACCACTCTTCGGGCCTGG
TTCCAAGTGATCGAAGCCAACTACCACTCTTCCAATGCCTACCACAACTCCACCCATGCT
GCCGACGTCCTGCACGCCACCGCTTTCTTTCTTGGAAAGGAAAGAGTAAAGGGAAGCCTC
GATCAGTTGGATGAGGTGGCAGCCCTCATTGCTGCCACAGTCCATGACGTGGATCACCCG
GGAAGGACCAACTCTTTCCTCTGCAATGCAGGCAGTGAGCTTGCTGTGCTCTACAATGAC
ACTGCTGTTCTGGAGAGTCACCACACCGCCCTGGCCTTCCAGCTCACGGTCAAGGACACC
AAATGCAACATTTTCAAGAATATTGACAGGAACCATTATCGAACGCTGCGCCAGGCTATT
ATTGACATGGTTTTGGCAACAGAGATGACAAAACACTTTGAACATGTGAATAAGTTTGTG
AACAGCATCAACAAGCCAATGGCAGCTGAGATTGAAGGCAGCGACTGTGAATGCAACCCT
GCTGGGAAGAACTTCCCTGAAAACCAAATCCTGATCAAACGCATGATGATTAAGTGTGCT
GACGTGGCCAACCCATGCCGCCCCTTGGACCTGTGCATTGAATGGGCTGGGAGGATCTCT
GAGGAGTATTTTGCACAGACTGATGAAGAGAAGAGACAGGGACTACCTGTGGTGATGCCA
GTGTTTGACCGGAATACCTGTAGCATCCCCAAGTCTCAGATCTCTTTCATTGACTACTTC
ATAACAGACATGTTTGATGCTTGGGATGCCTTTGCACATCTGCCAGCCCTGATGCAACAT
TTGGCTGACAACTACAAACACTGGAAGACACTAGATGACCTAAAGTGCAAAAGTTTGAGG
CTTCCATCTGACAGCTAA
Enzyme 28 GenBank Gene ID AB085824 Link Image
Enzyme 28 GeneCard ID PDE8B Link Image
Enzyme 28 GenAtlas ID PDE8B Link Image
Enzyme 28 HGNC ID HGNC:8794 Link Image
Enzyme 28 Chromosome Location 5
Enzyme 28 Locus 5q13.3
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Hayashi M, Shimada Y, Nishimura Y, Hama T, Tanaka T: Genomic organization, chromosomal localization, and alternative splicing of the human phosphodiesterase 8B gene. Biochem Biophys Res Commun. 2002 Oct 11;297(5):1253-8. [PubMed Link Image]
  2. Gamanuma M, Yuasa K, Sasaki T, Sakurai N, Kotera J, Omori K: Comparison of enzymatic characterization and gene organization of cyclic nucleotide phosphodiesterase 8 family in humans. Cell Signal. 2003 Jun;15(6):565-74. [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. Hayashi M, Matsushima K, Ohashi H, Tsunoda H, Murase S, Kawarada Y, Tanaka T: Molecular cloning and characterization of human PDE8B, a novel thyroid-specific isozyme of 3',5'-cyclic nucleotide phosphodiesterase. Biochem Biophys Res Commun. 1998 Sep 29;250(3):751-6. [PubMed Link Image]
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 5903
Enzyme 29 Name cAMP-specific 3',5'-cyclic phosphodiesterase 4C
Enzyme 29 Synonyms
  1. DPDE1
  2. PDE21
Enzyme 29 Gene Name PDE4C
Enzyme 29 Protein Sequence >cAMP-specific 3',5'-cyclic phosphodiesterase 4C
MENLGVGEGAEACSRLSRSRGRHSMTRAPKHLWRQPRRPIRIQQRFYSDPDKSAGCRERD
LSPRPELRKSRLSWPVSSCRRFDLENGLSCGRRALDPQSSPGLGRIMQAPVPHSQRRESF
LYRSDSDYELSPKAMSRNSSVASDLHGEDMIVTPFAQVLASLRTVRSNVAALARQQCLGA
AKQGPVGNPSSSNQLPPAEDTGQKLALETLDELDWCLDQLETLQTRHSVGEMASNKFKRI
LNRELTHLSETSRSGNQVSEYISRTFLDQQTEVELPKVTAEEAPQPMSRISGLHGLCHSA
SLSSATVPRFGVQTDQEEQLAKELEDTNKWGLDVFKVAELSGNRPLTAIIFSIFQERDLL
KTFQIPADTLATYLLMLEGHYHANVAYHNSLHAADVAQSTHVLLATPALEAVFTDLEILA
ALFASAIHDVDHPGVSNQFLINTNSELALMYNDASVLENHHLAVGFKLLQAENCDIFQNL
SAKQRLSLRRMVIDMVLATDMSKHMNLLADLKTMVETKKVTSLGVLLLDNYSDRIQVLQN
LVHCADLSNPTKPLPLYRQWTDRIMAEFFQQGDRERESGLDISPMCDKHTASVEKSQVGF
IDYIAHPLWETWADLVHPDAQDLLDTLEDNREWYQSKIPRSPSDLTNPERDGPDRFQFEL
TLEEAEEEDEEEEEEGEETALAKEALELPDTELLSPEAGPDPGDLPLDNQRT
Enzyme 29 Number of Residues 712
Enzyme 29 Molecular Weight 79900.8
Enzyme 29 Theoretical pI 4.84
Enzyme 29 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 29 General Function Involved in catalytic activity
Enzyme 29 Specific Function Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes
Enzyme 29 Pathways
Enzyme 29 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 115529445 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q08493 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name PDE4C_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >2139 bp
ATGGAGAACCTGGGGGTCGGCGAAGGGGCAGAGGCTTGCAGCAGGTTGAGTCGCTCTCGC
GGCCGCCACAGCATGACCAGAGCCCCGAAGCACCTGTGGCGGCAACCCCGGCGCCCCATC
CGCATCCAACAGCGCTTCTATTCGGATCCGGACAAGTCCGCGGGCTGCCGCGAGAGGGAC
CTGAGCCCGCGGCCGGAGCTCAGGAAGTCGCGGCTCTCCTGGCCCGTTTCCTCCTGCAGG
CGCTTTGACCTGGAAAATGGGCTCTCGTGTGGGAGGAGGGCCCTGGACCCTCAGTCCAGC
CCTGGCCTGGGCCGGATTATGCAGGCTCCAGTCCCGCACAGCCAGCGGCGCGAGTCCTTC
CTGTACCGCTCAGATAGCGACTATGAACTCTCGCCCAAGGCCATGTCTCGGAACTCCTCT
GTGGCCAGCGACCTACATGGAGAGGACATGATTGTGACGCCCTTTGCCCAGGTCCTGGCC
AGTCTGCGGACCGTTCGGAGCAACGTGGCGGCCCTTGCCCGCCAGCAATGCCTAGGAGCA
GCCAAGCAGGGACCCGTCGGAAACCCTTCATCCAGCAATCAGCTCCCTCCTGCAGAGGAC
ACGGGGCAGAAGCTGGCATTGGAGACGCTAGACGAGCTGGACTGGTGCCTGGATCAGTTG
GAGACGCTGCAGACCCGGCACTCGGTGGGGGAGATGGCCTCCAACAAGTTCAAGCGGATC
CTGAACCGGGAGTTGACCCACCTGTCCGAAACCAGCCGCTCCGGGAACCAGGTGTCCGAG
TACATCTCCCGGACCTTCCTGGACCAGCAGACCGAGGTGGAGCTGCCCAAGGTGACCGCT
GAGGAGGCCCCACAGCCCATGTCCCGGATCAGTGGCCTACATGGGCTCTGCCACAGTGCC
AGCCTCTCCTCAGCCACTGTCCCACGCTTTGGGGTCCAGACTGACCAGGAGGAGCAACTG
GCCAAGGAGCTAGAAGACACCAACAAGTGGGGACTTGATGTGTTCAAGGTGGCGGAGCTA
AGTGGGAACCGGCCCCTCACAGCTATCATATTCAGCATTTTTCAGGAGCGGGACCTGCTG
AAGACATTCCAGATCCCAGCAGACACACTGGCCACCTACCTGCTGATGCTGGAAGGTCAC
TACCACGCCAATGTGGCCTACCACAACAGCCTACATGCCGCCGACGTGGCCCAGTCCACG
CATGTGCTGCTGGCTACGCCCGCCCTCGAGGCTGTGTTCACAGACTTGGAAATCCTGGCT
GCCCTCTTTGCAAGCGCCATCCACGACGTGGACCATCCTGGGGTCTCCAACCAGTTTCTG
ATTAACACCAACTCAGAGCTGGCGCTTATGTACAACGACGCCTCGGTGCTGGAGAACCAT
CACCTGGCTGTGGGCTTCAAGCTGCTGCAGGCAGAGAACTGCGATATCTTCCAGAACCTC
AGCGCCAAGCAGCGACTGAGTCTGCGCAGGATGGTCATTGACATGGTGCTGGCCACAGAC
ATGTCCAAACACATGAACCTCCTGGCCGACCTCAAGACCATGGTGGAGACCAAGAAGGTG
ACAAGCCTCGGTGTCCTCCTCCTGGACAACTATTCCGACCGAATCCAGGTCTTGCAGAAC
CTGGTGCACTGTGCTGATCTGAGCAACCCCACCAAGCCGCTGCCCCTGTACCGCCAGTGG
ACGGACCGCATCATGGCCGAGTTCTTCCAGCAGGGAGACCGCGAGCGTGAGTCGGGCCTG
GACATCAGTCCCATGTGTGACAAGCATACGGCCTCAGTGGAGAAGTCCCAGGTGGGTTTC
ATTGACTACATTGCTCACCCACTGTGGGAGACTTGGGCTGACCTGGTCCACCCAGATGCA
CAGGACCTGCTGGACACGCTGGAGGACAATCGAGAGTGGTACCAGAGCAAGATCCCCCGA
AGTCCCTCAGACCTCACCAACCCCGAGCGGGACGGGCCTGACAGATTCCAGTTTGAACTG
ACTCTGGAGGAGGCAGAGGAAGAGGATGAGGAGGAAGAAGAGGAGGGGGAAGAGACAGCT
TTAGCCAAAGAGGCCTTGGAGTTGCCTGACACTGAACTCCTGTCCCCTGAAGCCGGCCCA
GACCCTGGGGACTTACCCCTCGACAACCAGAGGACTTAG
Enzyme 29 GenBank Gene ID NM_000923.3 Link Image
Enzyme 29 GeneCard ID PDE4C Link Image
Enzyme 29 GenAtlas ID PDE4C Link Image
Enzyme 29 HGNC ID HGNC:8782 Link Image
Enzyme 29 Chromosome Location 1
Enzyme 29 Locus 19p13.11
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Engels P, Sullivan M, Muller T, Lubbert H: Molecular cloning and functional expression in yeast of a human cAMP-specific phosphodiesterase subtype (PDE IV-C). FEBS Lett. 1995 Jan 30;358(3):305-10. [PubMed Link Image]
  2. Sullivan M, Olsen AS, Houslay MD: Genomic organisation of the human cyclic AMP-specific phosphodiesterase PDE4C gene and its chromosomal localisation to 19p13.1, between RAB3A and JUND. Cell Signal. 1999 Oct;11(10):735-42. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  5. Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [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. 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]
  8. Wang H, Peng MS, Chen Y, Geng J, Robinson H, Houslay MD, Cai J, Ke H: Structures of the four subfamilies of phosphodiesterase-4 provide insight into the selectivity of their inhibitors. Biochem J. 2007 Dec 1;408(2):193-201. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 5906
Enzyme 30 Name Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
Enzyme 30 Synonyms
  1. GMP-PDE beta
Enzyme 30 Gene Name PDE6B
Enzyme 30 Protein Sequence >Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
MSLSEEQARSFLDQNPDFARQYFGKKLSPENVAAACEDGCPPDCDSLRDLCQVEESTALL
ELVQDMQESINMERVVFKVLRRLCTLLQADRCSLFMYRQRNGVAELATRLFSVQPDSVLE
DCLVPPDSEIVFPLDIGVVGHVAQTKKMVNVEDVAECPHFSSFADELTDYKTKNMLATPI
MNGKDVVAVIMAVNKLNGPFFTSEDEDVFLKYLNFATLYLKIYHLSYLHNCETRRGQVLL
WSANKVFEELTDIERQFHKAFYTVRAYLNCERYSVGLLDMTKEKEFFDVWSVLMGESQPY
SGPRTPDGREIVFYKVIDYVLHGKEEIKVIPTPSADHWALASGLPSYVAESGFICNIMNA
SADEMFKFQEGALDDSGWLIKNVLSMPIVNKKEEIVGVATFYNRKDGKPFDEQDEVLMES
LTQFLGWSVMNTDTYDKMNKLENRKDIAQDMVLYHVKCDRDEIQLILPTRARLGKEPADC
DEDELGEILKEELPGPTTFDIYEFHFSDLECTELDLVKCGIQMYYELGVVRKFQIPQEVL
VRFLFSISKGYRRITYHNWRHGFNVAQTMFTLLMTGKLKSYYTDLEAFAMVTAGLCHDID
HRGTNNLYQMKSQNPLAKLHGSSILERHHLEFGKFLLSEETLNIYQNLNRRQHEHVIHLM
DIAIIATDLALYFKKRAMFQKIVDESKNYQDKKSWVEYLSLETTRKEIVMAMMMTACDLS
AITKPWEVQSKVALLVAAEFWEQGDLERTVLDQQPIPMMDRNKAAELPKLQVGFIDFVCT
FVYKEFSRFHEEILPMFDRLQNNRKEWKALADEYEAKVKALEEKEEEERVAAKKVGTEIC
NGGPAPKSSTCCIL
Enzyme 30 Number of Residues 854
Enzyme 30 Molecular Weight 98334.9
Enzyme 30 Theoretical pI 4.88
Enzyme 30 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 30 General Function Involved in catalytic activity
Enzyme 30 Specific Function This protein participates in processes of transmission and amplification of the visual signal. Necessary for the formation of a functional phosphodiesterase holoenzyme
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions
  • guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate [RN:R01234]
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 105990537 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID P35913 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name PDE6B_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >2565 bp
ATGAGCCTCAGTGAGGAGCAGGCCCGGAGCTTTCTGGACCAGAACCCCGATTTTGCCCGC
CAGTACTTTGGGAAGAAACTGAGCCCTGAGAATGTGGCCGCGGCCTGCGAGGACGGGTGC
CCGCCGGACTGCGACAGCCTCCGGGACCTCTGCCAGGTGGAGGAGAGCACGGCGCTGCTG
GAGCTGGTGCAGGATATGCAGGAGAGCATCAACATGGAGCGCGTGGTCTTCAAGGTCCTG
CGGCGCCTCTGCACCCTCCTGCAGGCCGACCGCTGCAGCCTCTTCATGTACCGCCAGCGC
AACGGCGTGGCCGAGCTGGCCACCAGGCTTTTCAGCGTGCAGCCGGACAGCGTCCTGGAG
GACTGCCTGGTGCCCCCCGACTCCGAGATCGTCTTCCCACTGGACATCGGGGTCGTGGGC
CACGTGGCTCAGACCAAAAAGATGGTGAACGTCGAGGACGTGGCCGAGTGCCCTCACTTC
AGCTCATTTGCTGACGAGCTCACTGACTACAAGACAAAGAATATGCTGGCCACACCCATC
ATGAATGGCAAAGACGTCGTGGCGGTGATCATGGCAGTGAACAAGCTCAACGGCCCATTC
TTCACCAGCGAAGACGAAGATGTGTTCTTGAAGTACCTGAATTTTGCCACGTTGTACCTG
AAGATCTATCACCTGAGCTACCTCCACAACTGCGAGACGCGCCGCGGCCAGGTGCTGCTG
TGGTCGGCCAACAAGGTGTTTGAGGAGCTGACGGACATCGAGAGGCAGTTCCACAAGGCC
TTCTACACGGTGCGGGCCTACCTCAACTGCGAGCGGTACTCCGTGGGCCTCCTGGACATG
ACCAAGGAGAAGGAATTTTTTGACGTGTGGTCTGTGCTGATGGGAGAGTCCCAGCCGTAC
TCGGGCCCACGCACGCCTGATGGCCGGGAAATTGTCTTCTACAAAGTGATCGACTACATC
CTCCACGGCAAGGAGGAGATCAAGGTCATTCCCACACCCTCAGCCGATCACTGGGCCCTG
GCCAGCGGCCTTCCAAGCTACGTGGCAGAAAGCGGCTTTATTTGTAACATCATGAATGCT
TCCGCTGACGAAATGTTCAAATTTCAGGAAGGGGCCCTGGACGACTCCGGGTGGCTCATC
AAGAATGTGCTGTCCATGCCCATCGTCAACAAGAAGGAGGAGATTGTGGGAGTCGCCACA
TTTTACAACAGGAAAGACGGGAAGCCCTTTGACGAACAGGACGAGGTTCTCATGGAGTCC
CTGACACAGTTCCTGGGCTGGTCAGTGATGAACACCGACACCTACGACAAGATGAACAAG
CTGGAGAACCGCAAGGACATCGCACAGGACATGGTCCTTTACCACGTGAAGTGCGACAGG
GACGAGATCCAGCTCATCCTGCCAACCAGAGCGCGCCTGGGGAAGGAGCCTGCTGACTGC
GATGAGGACGAGCTGGGCGAAATCCTGAAGGAGGAGCTGCCAGGGCCCACCACATTTGAC
ATCTACGAATTCCACTTCTCTGACCTGGAGTGCACCGAACTGGACCTGGTCAAATGTGGC
ATCCAGATGTACTACGAGCTGGGCGTGGTCCGAAAGTTCCAGATCCCCCAGGAGGTCCTG
GTGCGGTTCCTGTTCTCCATCAGCAAAGGGTACCGGAGAATCACCTACCACAACTGGCGC
CACGGCTTCAACGTGGCCCAGACGATGTTCACGCTGCTCATGACCGGCAAACTGAAGAGC
TACTACACGGACCTGGAGGCCTTCGCCATGGTGACAGCCGGCCTGTGCCATGACATCGAC
CACCGCGGCACCAACAACCTGTACCAGATGAAGTCCCAGAACCCCTTGGCTAAGCTCCAC
GGCTCCTCGATTTTGGAGCGGCACCACCTGGAGTTTGGGAAGTTCCTGCTCTCGGAGGAG
ACCCTGAACATCTACCAGAACCTGAACCGGCGGCAGCACGAGCACGTGATCCACCTGATG
GACATCGCCATCATCGCCACGGACCTGGCCCTGTACTTCAAGAAGAGAGCGATGTTTCAG
AAGATCGTGGATGAGTCCAAGAACTACCAGGACAAGAAGAGCTGGGTGGAGTACCTGTCC
CTGGAGACGACCCGGAAGGAGATCGTCATGGCCATGATGATGACAGCCTGCGACCTGTCT
GCCATCACCAAGCCCTGGGAAGTCCAGAGCAAGGTCGCACTTCTCGTGGCTGCTGAGTTC
TGGGAGCAAGGTGACTTGGAAAGGACAGTCTTGGATCAGCAGCCCATTCCTATGATGGAC
CGGAACAAGGCGGCCGAGCTCCCCAAGCTGCAAGTGGGCTTCATCGACTTCGTGTGCACA
TTCGTGTACAAGGAGTTCTCTCGTTTCCACGAAGAGATCCTGCCCATGTTCGACCGACTG
CAGAACAATAGGAAAGAGTGGAAGGCGCTGGCTGATGAGTATGAGGCCAAAGTGAAGGCT
CTGGAGGAGAAGGAGGAGGAGGAGAGGGTGGCAGCCAAGAAAGTAGGCACAGAAATTTGC
AATGGCGGCCCAGCACCCAAGTCTTCAACCTGCTGTATCCTGTGA
Enzyme 30 GenBank Gene ID NM_000283.3 Link Image
Enzyme 30 GeneCard ID PDE6B Link Image
Enzyme 30 GenAtlas ID PDE6B Link Image
Enzyme 30 HGNC ID HGNC:8786 Link Image
Enzyme 30 Chromosome Location 4
Enzyme 30 Locus 4p16.3
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Weber B, Riess O, Hutchinson G, Collins C, Lin BY, Kowbel D, Andrew S, Schappert K, Hayden MR: Genomic organization and complete sequence of the human gene encoding the beta-subunit of the cGMP phosphodiesterase and its localisation to 4p 16.3. Nucleic Acids Res. 1991 Nov 25;19(22):6263-8. [PubMed Link Image]
  2. Khramtsov NV, Feshchenko EA, Suslova VA, Terpugov BE, Rakitina TV, Atabekova NV, Shmukler BE, Lipkin VM: [Structural studies of cDNA and the gene for the beta-subunit of cGMP phosphodiesterase from human retina] Bioorg Khim. 1992 Dec;18(12):1551-4. [PubMed Link Image]
  3. Collins C, Hutchinson G, Kowbel D, Riess O, Weber B, Hayden MR: The human beta-subunit of rod photoreceptor cGMP phosphodiesterase: complete retinal cDNA sequence and evidence for expression in brain. Genomics. 1992 Jul;13(3):698-704. [PubMed Link Image]
  4. Khramtsov NV, Feshchenko EA, Suslova VA, Shmukler BE, Terpugov BE, Rakitina TV, Atabekova NV, Lipkin VM: The human rod photoreceptor cGMP phosphodiesterase beta-subunit. Structural studies of its cDNA and gene. FEBS Lett. 1993 Aug 2;327(3):275-8. [PubMed Link Image]
  5. 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]
  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. Gal A, Orth U, Baehr W, Schwinger E, Rosenberg T: Heterozygous missense mutation in the rod cGMP phosphodiesterase beta-subunit gene in autosomal dominant stationary night blindness. Nat Genet. 1994 May;7(1):64-8. [PubMed Link Image]
  8. Gal A, Orth U, Baehr W, Schwinger E, Rosenberg T: Heterozygous missense mutation in the rod cGMP phosphodiesterase beta-subunit gene in autosomal dominant stationary night blindness. Nat Genet. 1994 Aug;7(4):551. [PubMed Link Image]
  9. Suslova VA, Suslov ON, Kim EE, Lipkin VM: [Organization of the gene for the beta-subunit of human photoreceptor cyclic GMP phosphodiesterase] Bioorg Khim. 1996 Apr;22(4):256-63. [PubMed Link Image]
  10. McLaughlin ME, Sandberg MA, Berson EL, Dryja TP: Recessive mutations in the gene encoding the beta-subunit of rod phosphodiesterase in patients with retinitis pigmentosa. Nat Genet. 1993 Jun;4(2):130-4. [PubMed Link Image]
  11. Danciger M, Blaney J, Gao YQ, Zhao DY, Heckenlively JR, Jacobson SG, Farber DB: Mutations in the PDE6B gene in autosomal recessive retinitis pigmentosa. Genomics. 1995 Nov 1;30(1):1-7. [PubMed Link Image]
  12. Gao YQ, Danciger M, Zhao DY, Blaney J, Piriev NI, Shih J, Jacobson SG, Heckenlively JH, Farber DB: Screening of the PDE6B gene in patients with autosomal dominant retinitis pigmentosa. Exp Eye Res. 1996 Feb;62(2):149-54. [PubMed Link Image]
  13. Valverde D, Solans T, Grinberg D, Balcells S, Vilageliu L, Bayes M, Chivelet P, Besmond C, Goossens M, Gonzalez-Duarte R, Baiget M: A novel mutation in exon 17 of the beta-subunit of rod phosphodiesterase in two RP sisters of a consanguineous family. Hum Genet. 1996 Jan;97(1):35-8. [PubMed Link Image]
  14. Valverde D, Baiget M, Seminago R, del Rio E, Garcia-Sandoval B, del Rio T, Bayes M, Balcells S, Martinez A, Grinberg D, Ayuso C: Identification of a novel R552O mutation in exon 13 of the beta-subunit of rod phosphodiesterase gene in a Spanish family with autosomal recessive retinitis pigmentosa. Hum Mutat. 1996;8(4):393-4. [PubMed Link Image]
  15. Saga M, Mashima Y, Akeo K, Kudoh J, Oguchi Y, Shimizu N: A novel homozygous Ile535Asn mutation in the rod cGMP phosphodiesterase beta-subunit gene in two brothers of a Japanese family with autosomal recessive retinitis pigmentosa. Curr Eye Res. 1998 Mar;17(3):332-5. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 5908
Enzyme 31 Name cAMP-specific 3',5'-cyclic phosphodiesterase 4D
Enzyme 31 Synonyms
  1. DPDE3
  2. PDE43
Enzyme 31 Gene Name PDE4D
Enzyme 31 Protein Sequence >cAMP-specific 3',5'-cyclic phosphodiesterase 4D
MEAEGSSAPARAGSGEGSDSAGGATLKAPKHLWRHEQHHQYPLRQPQFRLLHPHHHLPPP
PPPSPQPQPQCPLQPPPPPPLPPPPPPPGAARGRYASSGATGRVRHRGYSDTERYLYCRA
MDRTSYAVETGHRPGLKKSRMSWPSSFQGLRRFDVDNGTSAGRSPLDPMTSPGSGLILQA
NFVHSQRRESFLYRSDSDYDLSPKSMSRNSSIASDIHGDDLIVTPFAQVLASLRTVRNNF
AALTNLQDRAPSKRSPMCNQPSINKATITEEAYQKLASETLEELDWCLDQLETLQTRHSV
SEMASNKFKRMLNRELTHLSEMSRSGNQVSEFISNTFLDKQHEVEIPSPTQKEKEKKKRP
MSQISGVKKLMHSSSLTNSSIPRFGVKTEQEDVLAKELEDVNKWGLHVFRIAELSGNRPL
TVIMHTIFQERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVVQSTHVLLST
PALEAVFTDLEILAAIFASAIHDVDHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGF
KLLQEENCDIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVETKKVTSSGVL
LLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQWTDRIMEEFFRQGDRERERGMEISPMC
DKHNASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIPQSPSPAP
DDPEEGRQGQTEKFQFELTLEEDGESDTEKDSGSQVEEDTSCSDSKTLCTQDSESTEIPL
DEQVEEEAVGEEEESQPEACVIDDRSPDT
Enzyme 31 Number of Residues 809
Enzyme 31 Molecular Weight 91114.1
Enzyme 31 Theoretical pI 5.25
Enzyme 31 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 31 General Function Involved in catalytic activity
Enzyme 31 Specific Function Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes
Enzyme 31 Pathways
Enzyme 31 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 157277988 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q08499 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name PDE4D_HUMAN Link Image
Enzyme 31 PDB ID 1PTW Link Image
Enzyme 31 PDB File Show
Enzyme 31 3D Structure
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >2430 bp
ATGGAGGCAGAGGGCAGCAGCGCGCCGGCCCGGGCGGGCAGCGGAGAGGGCAGCGACAGC
GCCGGCGGGGCCACGCTCAAAGCCCCCAAGCATCTCTGGAGGCACGAGCAGCACCACCAG
TACCCGCTCCGGCAGCCCCAGTTCCGCCTCCTGCATCCCCATCACCACCTGCCCCCGCCG
CCGCCACCCTCGCCCCAGCCCCAGCCCCAGTGTCCGCTACAGCCGCCGCCGCCGCCCCCC
CTGCCGCCGCCCCCGCCGCCGCCCGGGGCTGCCCGCGGCCGCTACGCCTCGAGCGGGGCC
ACCGGCCGCGTCCGGCATCGCGGCTACTCGGACACCGAGCGCTACCTGTACTGTCGCGCC
ATGGACCGCACCTCCTACGCGGTGGAGACCGGCCACCGGCCCGGCCTGAAGAAATCCAGG
ATGTCCTGGCCCTCCTCGTTCCAGGGACTCAGGCGTTTTGATGTGGACAATGGCACATCT
GCGGGACGGAGTCCCTTGGATCCCATGACCAGCCCAGGATCCGGGCTAATTCTCCAAGCA
AATTTTGTCCACAGTCAACGACGGGAGTCCTTCCTGTATCGATCCGACAGCGATTATGAC
CTCTCTCCAAAGTCTATGTCCCGGAACTCCTCCATTGCCAGTGATATACACGGAGATGAC
TTGATTGTGACTCCATTTGCTCAGGTCTTGGCCAGTCTGCGAACTGTACGAAACAACTTT
GCTGCATTAACTAATTTGCAAGATCGAGCACCTAGCAAAAGATCACCCATGTGCAACCAA
CCATCCATCAACAAAGCCACCATAACAGAGGAGGCCTACCAGAAACTGGCCAGCGAGACC
CTGGAGGAGCTGGACTGGTGTCTGGACCAGCTAGAGACCCTACAGACCAGGCACTCCGTC
AGTGAGATGGCCTCCAACAAGTTTAAAAGGATGCTTAATCGGGAGCTCACCCATCTCTCT
GAAATGAGTCGGTCTGGAAATCAAGTGTCAGAGTTTATATCAAACACATTCTTAGATAAG
CAACATGAAGTGGAAATTCCTTCTCCAACTCAGAAGGAAAAGGAGAAAAAGAAAAGACCA
ATGTCTCAGATCAGTGGAGTCAAGAAATTGATGCACAGCTCTAGTCTGACTAATTCAAGT
ATCCCAAGGTTTGGAGTTAAAACTGAACAAGAAGATGTCCTTGCCAAGGAACTAGAAGAT
GTGAACAAATGGGGTCTTCATGTTTTCAGAATAGCAGAGTTGTCTGGTAACCGGCCCTTG
ACTGTTATCATGCACACCATTTTTCAGGAACGGGATTTATTAAAAACATTTAAAATTCCA
GTAGATACTTTAATTACATATCTTATGACTCTCGAAGACCATTACCATGCTGATGTGGCC
TATCACAACAATATCCATGCTGCAGATGTTGTCCAGTCTACTCATGTGCTATTATCTACA
CCTGCTTTGGAGGCTGTGTTTACAGATTTGGAGATTCTTGCAGCAATTTTTGCCAGTGCA
ATACATGATGTAGATCATCCTGGTGTGTCCAATCAATTTCTGATCAATACAAACTCTGAA
CTTGCCTTGATGTACAATGATTCCTCAGTCTTAGAGAACCATCATTTGGCTGTGGGCTTT
AAATTGCTTCAGGAAGAAAACTGTGACATTTTCCAGAATTTGACCAAAAAACAAAGACAA
TCTTTAAGGAAAATGGTCATTGACATCGTACTTGCAACAGATATGTCAAAACACATGAAT
CTACTGGCTGATTTGAAGACTATGGTTGAAACTAAGAAAGTGACAAGCTCTGGAGTTCTT
CTTCTTGATAATTATTCCGATAGGATTCAGGTTCTTCAGAATATGGTGCACTGTGCAGAT
CTGAGCAACCCAACAAAGCCTCTCCAGCTGTACCGCCAGTGGACGGACCGGATAATGGAG
GAGTTCTTCCGCCAAGGAGACCGAGAGAGGGAACGTGGCATGGAGATAAGCCCCATGTGT
GACAAGCACAATGCTTCCGTGGAAAAATCACAGGTGGGCTTCATAGACTATATTGTTCAT
CCCCTCTGGGAGACATGGGCAGACCTCGTCCACCCTGACGCCCAGGATATTTTGGACACT
TTGGAGGACAATCGTGAATGGTACCAGAGCACAATCCCTCAGAGCCCCTCTCCTGCACCT
GATGACCCAGAGGAGGGCCGGCAGGGTCAAACTGAGAAATTCCAGTTTGAACTAACTTTA
GAGGAAGATGGTGAGTCAGACACGGAAAAGGACAGTGGCAGTCAAGTGGAAGAAGACACT
AGCTGCAGTGACTCCAAGACTCTTTGTACTCAAGACTCAGAGTCTACTGAAATTCCCCTT
GATGAACAGGTTGAAGAGGAGGCAGTAGGGGAAGAAGAGGAAAGCCAGCCTGAAGCCTGT
GTCATAGATGATCGTTCTCCTGACACGTAA
Enzyme 31 GenBank Gene ID NM_001104631.1 Link Image
Enzyme 31 GeneCard ID PDE4D Link Image
Enzyme 31 GenAtlas ID PDE4D Link Image
Enzyme 31 HGNC ID HGNC:8783 Link Image
Enzyme 31 Chromosome Location 5
Enzyme 31 Locus 5q12
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed Link Image]
  2. Nemoz G, Zhang R, Sette C, Conti M: Identification of cyclic AMP-phosphodiesterase variants from the PDE4D gene expressed in human peripheral mononuclear cells. FEBS Lett. 1996 Apr 8;384(1):97-102. [PubMed Link Image]
  3. Baecker PA, Obernolte R, Bach C, Yee C, Shelton ER: Isolation of a cDNA encoding a human rolipram-sensitive cyclic AMP phosphodiesterase (PDE IVD). Gene. 1994 Jan 28;138(1-2):253-6. [PubMed Link Image]
  4. Bolger GB, Erdogan S, Jones RE, Loughney K, Scotland G, Hoffmann R, Wilkinson I, Farrell C, Houslay MD: Characterization of five different proteins produced by alternatively spliced mRNAs from the human cAMP-specific phosphodiesterase PDE4D gene. Biochem J. 1997 Dec 1;328 ( Pt 2):539-48. [PubMed Link Image]
  5. Miro X, Casacuberta JM, Gutierrez-Lopez MD, de Landazuri MO, Puigdomenech P: Phosphodiesterases 4D and 7A splice variants in the response of HUVEC cells to TNF-alpha(1). Biochem Biophys Res Commun. 2000 Aug 2;274(2):415-21. [PubMed Link Image]
  6. Wang D, Deng C, Bugaj-Gaweda B, Kwan M, Gunwaldsen C, Leonard C, Xin X, Hu Y, Unterbeck A, De Vivo M: Cloning and characterization of novel PDE4D isoforms PDE4D6 and PDE4D7. Cell Signal. 2003 Sep;15(9):883-91. [PubMed Link Image]
  7. Gretarsdottir S, Thorleifsson G, Reynisdottir ST, Manolescu A, Jonsdottir S, Jonsdottir T, Gudmundsdottir T, Bjarnadottir SM, Einarsson OB, Gudjonsdottir HM, Hawkins M, Gudmundsson G, Gudmundsdottir H, Andrason H, Gudmundsdottir AS, Sigurdardottir M, Chou TT, Nahmias J, Goss S, Sveinbjornsdottir S, Valdimarsson EM, Jakobsson F, Agnarsson U, Gudnason V, Thorgeirsson G, Fingerle J, Gurney M, Gudbjartsson D, Frigge ML, Kong A, Stefansson K, Gulcher JR: The gene encoding phosphodiesterase 4D confers risk of ischemic stroke. Nat Genet. 2003 Oct;35(2):131-8. Epub 2003 Sep 21. [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. Bolger GB, McCahill A, Yarwood SJ, Steele MR, Warwicker J, Houslay MD: Delineation of RAID1, the RACK1 interaction domain located within the unique N-terminal region of the cAMP-specific phosphodiesterase, PDE4D5. BMC Biochem. 2002 Aug 23;3:24. [PubMed Link Image]
  10. Bolger GB, McCahill A, Huston E, Cheung YF, McSorley T, Baillie GS, Houslay MD: The unique amino-terminal region of the PDE4D5 cAMP phosphodiesterase isoform confers preferential interaction with beta-arrestins. J Biol Chem. 2003 Dec 5;278(49):49230-8. Epub 2003 Sep 18. [PubMed Link Image]
  11. Richter W, Conti M: The oligomerization state determines regulatory properties and inhibitor sensitivity of type 4 cAMP-specific phosphodiesterases. J Biol Chem. 2004 Jul 16;279(29):30338-48. Epub 2004 May 6. [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. Rosand J, Bayley N, Rost N, de Bakker PI: Many hypotheses but no replication for the association between PDE4D and stroke. Nat Genet. 2006 Oct;38(10):1091-2; author reply 1092-3. [PubMed Link Image]
  15. 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]
  16. 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]
  17. 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]
  18. 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]
  19. Lee ME, Markowitz J, Lee JO, Lee H: Crystal structure of phosphodiesterase 4D and inhibitor complex(1). FEBS Lett. 2002 Oct 23;530(1-3):53-8. [PubMed Link Image]
  20. Huai Q, Colicelli J, Ke H: The crystal structure of AMP-bound PDE4 suggests a mechanism for phosphodiesterase catalysis. Biochemistry. 2003 Nov 18;42(45):13220-6. [PubMed Link Image]
  21. Huai Q, Wang H, Sun Y, Kim HY, Liu Y, Ke H: Three-dimensional structures of PDE4D in complex with roliprams and implication on inhibitor selectivity. Structure. 2003 Jul;11(7):865-73. [PubMed Link Image]
  22. Huai Q, Liu Y, Francis SH, Corbin JD, Ke H: Crystal structures of phosphodiesterases 4 and 5 in complex with inhibitor 3-isobutyl-1-methylxanthine suggest a conformation determinant of inhibitor selectivity. J Biol Chem. 2004 Mar 26;279(13):13095-101. Epub 2003 Dec 10. [PubMed Link Image]
  23. Xu RX, Rocque WJ, Lambert MH, Vanderwall DE, Luther MA, Nolte RT: Crystal structures of the catalytic domain of phosphodiesterase 4B complexed with AMP, 8-Br-AMP, and rolipram. J Mol Biol. 2004 Mar 19;337(2):355-65. [PubMed Link Image]
  24. Zhang KY, Card GL, Suzuki Y, Artis DR, Fong D, Gillette S, Hsieh D, Neiman J, West BL, Zhang C, Milburn MV, Kim SH, Schlessinger J, Bollag G: A glutamine switch mechanism for nucleotide selectivity by phosphodiesterases. Mol Cell. 2004 Jul 23;15(2):279-86. [PubMed Link Image]
  25. Card GL, England BP, Suzuki Y, Fong D, Powell B, Lee B, Luu C, Tabrizizad M, Gillette S, Ibrahim PN, Artis DR, Bollag G, Milburn MV, Kim SH, Schlessinger J, Zhang KY: Structural basis for the activity of drugs that inhibit phosphodiesterases. Structure. 2004 Dec;12(12):2233-47. [PubMed Link Image]
  26. Card GL, Blasdel L, England BP, Zhang C, Suzuki Y, Gillette S, Fong D, Ibrahim PN, Artis DR, Bollag G, Milburn MV, Kim SH, Schlessinger J, Zhang KY: A family of phosphodiesterase inhibitors discovered by cocrystallography and scaffold-based drug design. Nat Biotechnol. 2005 Feb;23(2):201-7. Epub 2005 Jan 30. [PubMed Link Image]
  27. Huai Q, Sun Y, Wang H, Macdonald D, Aspiotis R, Robinson H, Huang Z, Ke H: Enantiomer discrimination illustrated by the high resolution crystal structures of type 4 phosphodiesterase. J Med Chem. 2006 Mar 23;49(6):1867-73. [PubMed Link Image]
  28. Wang H, Peng MS, Chen Y, Geng J, Robinson H, Houslay MD, Cai J, Ke H: Structures of the four subfamilies of phosphodiesterase-4 provide insight into the selectivity of their inhibitors. Biochem J. 2007 Dec 1;408(2):193-201. [PubMed Link Image]
  29. Smith KJ, Baillie GS, Hyde EI, Li X, Houslay TM, McCahill A, Dunlop AJ, Bolger GB, Klussmann E, Adams DR, Houslay MD: 1H NMR structural and functional characterisation of a cAMP-specific phosphodiesterase-4D5 (PDE4D5) N-terminal region peptide that disrupts PDE4D5 interaction with the signalling scaffold proteins, beta-arrestin and RACK1. Cell Signal. 2007 Dec;19(12):2612-24. Epub 2007 Sep 1. [PubMed Link Image]
  30. Wang H, Robinson H, Ke H: The molecular basis for different recognition of substrates by phosphodiesterase families 4 and 10. J Mol Biol. 2007 Aug 10;371(2):302-7. Epub 2007 May 26. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 5909
Enzyme 32 Name Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
Enzyme 32 Synonyms
  1. GMP-PDE gamma
Enzyme 32 Gene Name PDE6G
Enzyme 32 Protein Sequence >Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
MNLEPPKAEFRSATRVAGGPVTPRKGPPKFKQRQTRQFKSKPPKKGVQGFGDDIPGMEGL
GTDITVICPWEAFNHLELHELAQYGII
Enzyme 32 Number of Residues 87
Enzyme 32 Molecular Weight 9643.1
Enzyme 32 Theoretical pI 10.16
Enzyme 32 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • GMP binding
  • binding
  • cGMP binding
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nucleoside binding
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • purine nucleoside binding
Process
  • multicellular organismal process
  • neurological system process
  • sensory perception
  • sensory perception of light stimulus
  • system process
  • visual perception
Component
Enzyme 32 General Function Involved in 3',5'-cyclic-nucleotide phosphodiesterase activity
Enzyme 32 Specific Function Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones
Enzyme 32 Pathways
Enzyme 32 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein Not Available
Enzyme 32 UniProtKB/Swiss-Prot ID P18545 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name CNRG_HUMAN Link Image
Enzyme 32 PDB ID 1FQJ Link Image
Enzyme 32 PDB File Show
Enzyme 32 3D Structure
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >264 bp
ATGAACCTGGAACCGCCCAAGGCTGAGTTCCGGTCAGCCACCAGGGTGGCCGGGGGACCT
GTCACCCCCAGGAAAGGGCCCCCTAAATTTAAGCAGCGACAGACCAGGCAGTTCAAGAGC
AAGCCCCCAAAGAAAGGCGTTCAAGGGTTTGGGGACGACATCCCTGGAATGGAAGGCCTG
GGAACAGACATCACAGTCATCTGCCCTTGGGAGGCCTTCAACCACCTGGAGCTGCACGAG
CTGGCCCAATATGGCATCATCTAG
Enzyme 32 GenBank Gene ID M36476 Link Image
Enzyme 32 GeneCard ID PDE6G Link Image
Enzyme 32 GenAtlas ID PDE6G Link Image
Enzyme 32 HGNC ID HGNC:8789 Link Image
Enzyme 32 Chromosome Location 1
Enzyme 32 Locus 17q25
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Tuteja N, Danciger M, Klisak I, Tuteja R, Inana G, Mohandas T, Sparkes RS, Farber DB: Isolation and characterization of cDNA encoding the gamma-subunit of cGMP phosphodiesterase in human retina. Gene. 1990 Apr 16;88(2):227-32. [PubMed Link Image]
  2. Piriev NI, Purishko VA, Khramtsov NV, Lipkin VM: [The organization of the gamma-subunit gene of human photoreceptor cyclic GMP phosphodiesterase] Dokl Akad Nauk SSSR. 1990;315(1):229-31. [PubMed Link Image]
  3. Hahn LB, Berson EL, Dryja TP: Evaluation of the gene encoding the gamma subunit of rod phosphodiesterase in retinitis pigmentosa. Invest Ophthalmol Vis Sci. 1994 Mar;35(3):1077-82. [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]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 5913
Enzyme 33 Name Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
Enzyme 33 Synonyms
  1. GMP-PDE delta
  2. Protein p17
Enzyme 33 Gene Name PDE6D
Enzyme 33 Protein Sequence >Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
MSAKDERAREILRGFKLNWMNLRDAETGKILWQGTEDLSVPGVEHEARVPKKILKCKAVS
RELNFSSTEQMEKFRLEQKVYFKGQCLEEWFFEFGFVIPNSTNTWQSLIEAAPESQMMPA
SVLTGNVIIETKFFDDDLLVSTSRVRLFYV
Enzyme 33 Number of Residues 150
Enzyme 33 Molecular Weight 17419.9
Enzyme 33 Theoretical pI 5.35
Enzyme 33 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • binding
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • protein binding
Process
  • multicellular organismal process
  • neurological system process
  • sensory perception
  • sensory perception of light stimulus
  • system process
  • visual perception
Component
Enzyme 33 General Function Involved in 3',5'-cyclic-nucleotide phosphodiesterase activity
Enzyme 33 Specific Function Not Available
Enzyme 33 Pathways
Enzyme 33 Reactions Not Available
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 2655094 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID O43924 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name PDE6D_HUMAN Link Image
Enzyme 33 PDB ID 1KSG Link Image
Enzyme 33 PDB File Show
Enzyme 33 3D Structure
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >453 bp
ATGTCAGCCAAGGACGAGCGGGCCAGGGAGATCCTGAGGGGCTTCAAACTAAATTGGATG
AACCTTCGGGATGCTGAGACAGGGAAGATACTCTGGCAAGGAACAGAAGACCTGTCTGTC
CCTGGTGTGGAGCATGAAGCCCGTGTTCCCAAGAAAATCCTCAAGTGCAAGGCAGTGTCT
CGAGAACTTAATTTTTCTTCGACAGAACAAATGGAAAAATTCCGCCTGGAACAAAAAGTT
TACTTCAAAGGGCAATGCCTAGAAGAATGGTTCTTCGAGTTTGGCTTTGTGATCCCTAAC
TCCACAAATACCTGGCAGTCCTTGATAGAGGCAGCACCCGAGTCCCAGATGATGCCAGCA
AGCGTCTTAACTGGGAACGTTATCATAGAAACAAAGTTTTTTGACGACGATCTTCTTGTA
AGCACATCCAGAGTGAGACTTTTCTATGTTTGA
Enzyme 33 GenBank Gene ID AF022912 Link Image
Enzyme 33 GeneCard ID PDE6D Link Image
Enzyme 33 GenAtlas ID PDE6D Link Image
Enzyme 33 HGNC ID HGNC:8788 Link Image
Enzyme 33 Chromosome Location 2
Enzyme 33 Locus 2q35-q36
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Li N, Florio SK, Pettenati MJ, Rao PN, Beavo JA, Baehr W: Characterization of human and mouse rod cGMP phosphodiesterase delta subunit (PDE6D) and chromosomal localization of the human gene. Genomics. 1998 Apr 1;49(1):76-82. [PubMed Link Image]
  2. Ershova G, Derre J, Chetelin S, Nancy V, Berger R, Kaplan J, Munnich A, de Gunzburg J: cDNA sequence, genomic organization and mapping of PDE6D, the human gene encoding the delta subunit of the cGMP phosphodiesterase of retinal rod cells to chromosome 2q36. Cytogenet Cell Genet. 1997;79(1-2):139-41. [PubMed Link Image]
  3. Lorenz B, Migliaccio C, Lichtner P, Meyer C, Strom TM, D'Urso M, Becker J, Ciccodicola A, Meitinger T: Cloning and gene structure of the rod cGMP phosphodiesterase delta subunit gene (PDED) in man and mouse. Eur J Hum Genet. 1998 May-Jun;6(3):283-90. [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. Linari M, Hanzal-Bayer M, Becker J: The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE delta, interacts with the Arf-like protein Arl3 in a GTP specific manner. FEBS Lett. 1999 Sep 10;458(1):55-9. [PubMed Link Image]
  6. Hanzal-Bayer M, Renault L, Roversi P, Wittinghofer A, Hillig RC: The complex of Arl2-GTP and PDE delta: from structure to function. EMBO J. 2002 May 1;21(9):2095-106. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 5922
Enzyme 34 Name cAMP-specific 3',5'-cyclic phosphodiesterase 4A
Enzyme 34 Synonyms
  1. DPDE2
  2. PDE46
Enzyme 34 Gene Name PDE4A
Enzyme 34 Protein Sequence >cAMP-specific 3',5'-cyclic phosphodiesterase 4A
MEPPTVPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPIRIQQRGYSDSAERAERERQ
PHRPIERADAMDTSDRPGLRTTRMSWPSSFHGTGTGSGGAGGGSSRRFEAENGPTPSPGR
SPLDSQASPGLVLHAGAATSQRRESFLYRSDSDYDMSPKTMSRNSSVTSEAHAEDLIVTP
FAQVLASLRSVRSNFSLLTNVPVPSNKRSPLGGPTPVCKATLSEETCQQLARETLEELDW
CLEQLETMQTYRSVSEMASHKFKRMLNRELTHLSEMSRSGNQVSEYISTTFLDKQNEVEI
PSPTMKEREKQQAPRPRPSQPPPPPVPHLQPMSQITGLKKLMHSNSLNNSNIPRFGVKTD
QEELLAQELENLNKWGLNIFCVSDYAGGRSLTCIMYMIFQERDLLKKFRIPVDTMVTYML
TLEDHYHADVAYHNSLHAADVLQSTHVLLATPALDAVFTDLEILAALFAAAIHDVDHPGV
SNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEDNCDIFQNLSKRQRQSLRKMVIDM
VLATDMSKHMTLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLRNMVHCADLSNPTKPLE
LYRQWTDRIMAEFFQQGDRERERGMEISPMCDKHTASVEKSQVGFIDYIVHPLWETWADL
VHPDAQEILDTLEDNRDWYYSAIRQSPSPPPEEESRGPGHPPLPDKFQFELTLEEEEEEE
ISMAQIPCTAQEALTAQGLSGVEEALDATIAWEASPAQESLEVMAQEASLEAELEAVYLT
QQAQSTGSAPVAPDEFSSREEFVVAVSHSSPSALALQSPLLPAWRTLSVSEHAPGLPGLP
STAAEVEAQREHQAAKRACSACAGTFGEDTSALPAPGGGGSGGDPT
Enzyme 34 Number of Residues 886
Enzyme 34 Molecular Weight 98142.2
Enzyme 34 Theoretical pI 4.87
Enzyme 34 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 34 General Function Involved in 3',5'-cyclic-nucleotide phosphodiesterase activity
Enzyme 34 Specific Function Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes
Enzyme 34 Pathways
Enzyme 34 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259]
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein Not Available
Enzyme 34 UniProtKB/Swiss-Prot ID P27815 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name PDE4A_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >2661 bp
ATGGAACCCCCGACCGTCCCCTCGGAAAGGAGCCTGTCTCTGTCACTGCCCGGGCCCCGG
GAGGGCCAGGCCACCCTGAAGCCTCCCCCGCAGCACCTGTGGCGGCAGCCTCGGACCCCC
ATCCGTATCCAGCAGCGCGGCTACTCCGACAGCGCGGAGCGCGCCGAGCGGGAGCGGCAG
CCGCACCGGCCCATAGAGCGCGCCGATGCCATGGACACCAGCGACCGGCCCGGCCTGCGC
ACGACCCGCATGTCCTGGCCCTCGTCCTTCCATGGCACTGGCACCGGCAGCGGCGGCGCG
GGCGGAGGCAGCAGCAGGCGCTTCGAGGCAGAGAATGGGCCGACACCATCTCCTGGCCGC
AGCCCCCTGGACTCGCAGGCGAGCCCAGGACTCGTGCTGCACGCCGGGGCGGCCACCAGC
CAGCGCCGGGAGTCCTTCCTGTACCGCTCAGACAGCGACTATGACATGTCACCCAAGACC
ATGTCCCGGAACTCATCGGTCACCAGCGAGGCGCACGCTGAAGACCTCATCGTAACACCA
TTTGCTCAGGTGCTGGCCAGCCTCCGGAGCGTCCGTAGCAACTTCTCACTCCTGACCAAT
GTGCCCGTTCCCAGTAACAAGCGGTCCCCGCTGGGCGGCCCCACCCCTGTCTGCAAGGCC
ACGCTGTCAGAAGAAACGTGTCAGCAGTTGGCCCGGGAGACTCTGGAGGAGCTGGACTGG
TGTCTGGAGCAGCTGGAGACCATGCAGACCTATCGCTCTGTCAGCGAGATGGCCTCGCAC
AAGTTCAAAAGGATGTTGAACCGTGAGCTCACACACCTGTCAGAAATGAGCAGGTCCGGA
AACCAGGTCTCAGAGTACATTTCCACAACATTCCTGGACAAACAGAATGAAGTGGAGATC
CCATCACCCACGATGAAGGAACGAGAAAAACAGCAAGCGCCGCGACCAAGACCCTCCCAG
CCGCCCCCGCCCCCTGTACCACACTTACAGCCCATGTCCCAAATCACAGGGTTGAAAAAG
TTGATGCATAGTAACAGCCTGAACAACTCTAACATTCCCCGATTTGGGGTGAAGACCGAT
CAAGAAGAGCTCCTGGCCCAAGAACTGGAGAACCTGAACAAGTGGGGCCTGAACATCTTT
TGCGTGTCGGATTACGCTGGAGGCCGCTCACTCACCTGCATCATGTACATGATATTCCAG
GAGCGGGACCTGCTGAAGAAATTCCGCATCCCGGTGGACACGATGGTGACATACATGCTG
ACGCTGGAGGATCACTACCACGCTGACGTGGCCTACCATAACAGCCTGCACGCAGCTGAC
GTGCTGCAGTCCACCCACGTACTGCTGGCCACGCCTGCACTAGATGCAGTGTTCACGGAC
CTGGAGATTCTCGCCGCCCTCTTCGCGGCTGCCATCCACGATGTGGATCACCCTGGGGTC
TCCAACCAGTTCCTCATCAACACCAATTCGGAGCTGGCGCTCATGTACAACGATGAGTCG
GTGCTCGAGAATCACCACCTGGCCGTGGGCTTCAAGCTGCTGCAGGAGGACAACTGCGAC
ATCTTCCAGAACCTCAGCAAGCGCCAGCGGCAGAGCCTACGCAAGATGGTCATCGACATG
GTGCTGGCCACGGACATGTCCAAGCACATGACCCTCCTGGCTGACCTGAAGACCATGGTG
GAGACCAAGAAAGTGACCAGCTCAGGGGTCCTCCTGCTAGATAACTACTCCGACCGCATC
CAGGTCCTCCGGAACATGGTGCACTGTGCCGACCTCAGCAACCCCACCAAGCCGCTGGAG
CTGTACCGCCAGTGGACAGACCGCATCATGGCCGAGTTCTTCCAGCAGGGTGACCGAGAG
CGCGAGCGTGGCATGGAAATCAGCCCCATGTGTGACAAGCACACTGCCTCCGTGGAGAAG
TCTCAGGTGGGTTTTATTGACTACATTGTGCACCCATTGTGGGAGACCTGGGCGGACCTT
GTCCACCCAGATGCCCAGGAGATCTTGGACACTTTGGAGGACAACCGGGACTGGTACTAC
AGCGCCATCCGGCAGAGCCCATCTCCGCCACCCGAGGAGGAGTCAAGGGGGCCAGGCCAC
CCACCCCTGCCTGACAAGTTCCAGTTTGAGCTGACGCTGGAGGAGGAAGAGGAGGAAGAA
ATATCAATGGCCCAGATACCGTGCACAGCCCAAGAGGCATTGACTGCGCAGGGATTGTCA
GGAGTCGAGGAAGCTCTGGATGCAACCATAGCCTGGGAGGCATCCCCGGCCCAGGAGTCG
TTGGAAGTTATGGCACAGGAAGCATCCCTGGAGGCCGAGCTGGAGGCAGTGTATTTGACA
CAGCAGGCACAGTCCACAGGCAGTGCACCTGTGGCTCCGGATGAGTTCTCGTCCCGGGAG
GAATTCGTGGTTGCTGTAAGCCACAGCAGCCCCTCTGCCCTGGCTCTTCAAAGCCCCCTT
CTCCCTGCTTGGAGGACCCTGTCTGTTTCAGAGCATGCCCCGGGCCTCCCGGGCCTCCCC
TCCACGGCGGCCGAGGTGGAGGCCCAACGAGAGCACCAGGCTGCCAAGAGGGCTTGCAGT
GCCTGCGCAGGGACATTTGGGGAGGACACATCCGCACTCCCAGCTCCTGGTGGCGGGGGG
TCAGGTGGAGACCCTACCTGA
Enzyme 34 GenBank Gene ID L20965 Link Image
Enzyme 34 GeneCard ID PDE4A Link Image
Enzyme 34 GenAtlas ID PDE4A Link Image
Enzyme 34 HGNC ID HGNC:8780 Link Image
Enzyme 34 Chromosome Location 1
Enzyme 34 Locus 19p13.2
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Bolger G, Michaeli T, Martins T, St John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K: A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol. 1993 Oct;13(10):6558-71. [PubMed Link Image]
  2. Sullivan M, Egerton M, Shakur Y, Marquardsen A, Houslay MD: Molecular cloning and expression, in both COS-1 cells and S. cerevisiae, of a human cytosolic type-IVA, cyclic AMP specific phosphodiesterase (hPDE-IVA-h6.1). Cell Signal. 1994 Sep;6(7):793-812. [PubMed Link Image]
  3. Horton YM, Sullivan M, Houslay MD: Molecular cloning of a novel splice variant of human type IVA (PDE-IVA) cyclic AMP phosphodiesterase and localization of the gene to the p13.2-q12 region of human chromosome 19 [corrected] Biochem J. 1995 Jun 1;308 ( Pt 2):683-91. [PubMed Link Image]
  4. Sullivan M, Rena G, Begg F, Gordon L, Olsen AS, Houslay MD: Identification and characterization of the human homologue of the short PDE4A cAMP-specific phosphodiesterase RD1 (PDE4A1) by analysis of the human HSPDE4A gene locus located at chromosome 19p13.2. Biochem J. 1998 Aug 1;333 ( Pt 3):693-703. [PubMed Link Image]
  5. Rena G, Begg F, Ross A, MacKenzie C, McPhee I, Campbell L, Huston E, Sullivan M, Houslay MD: Molecular cloning, genomic positioning, promoter identification, and characterization of the novel cyclic amp-specific phosphodiesterase PDE4A10. Mol Pharmacol. 2001 May;59(5):996-1011. [PubMed Link Image]
  6. Wallace DA, Johnston LA, Huston E, MacMaster D, Houslay TM, Cheung YF, Campbell L, Millen JE, Smith RA, Gall I, Knowles RG, Sullivan M, Houslay MD: Identification and characterization of PDE4A11, a novel, widely expressed long isoform encoded by the human PDE4A cAMP phosphodiesterase gene. Mol Pharmacol. 2005 Jun;67(6):1920-34. Epub 2005 Feb 28. [PubMed Link Image]
  7. Mackenzie KF, Topping EC, Bugaj-Gaweda B, Deng C, Cheung YF, Olsen AE, Stockard CR, High Mitchell L, Baillie GS, Grizzle WE, De Vivo M, Houslay MD, Wang D, Bolger GB: Human PDE4A8, a novel brain-expressed PDE4 cAMP-specific phosphodiesterase that has undergone rapid evolutionary change. Biochem J. 2008 Apr 15;411(2):361-9. [PubMed Link Image]
  8. 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]
  9. 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]
  10. Livi GP, Kmetz P, McHale MM, Cieslinski LB, Sathe GM, Taylor DP, Davis RL, Torphy TJ, Balcarek JM: Cloning and expression of cDNA for a human low-Km, rolipram-sensitive cyclic AMP phosphodiesterase. Mol Cell Biol. 1990 Jun;10(6):2678-86. [PubMed Link Image]
  11. Lario PI, Bobechko B, Bateman K, Kelly J, Vrielink A, Huang Z: Purification and characterization of the human PDE4A catalytic domain (PDE4A330-723) expressed in Sf9 cells. Arch Biochem Biophys. 2001 Oct 1;394(1):54-60. [PubMed Link Image]
  12. 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]
  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. Wang H, Peng MS, Chen Y, Geng J, Robinson H, Houslay MD, Cai J, Ke H: Structures of the four subfamilies of phosphodiesterase-4 provide insight into the selectivity of their inhibitors. Biochem J. 2007 Dec 1;408(2):193-201. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 5927
Enzyme 35 Name cGMP-specific 3',5'-cyclic phosphodiesterase
Enzyme 35 Synonyms
  1. cGMP-binding cGMP-specific phosphodiesterase
  2. CGB-PDE
Enzyme 35 Gene Name PDE5A
Enzyme 35 Protein Sequence >cGMP-specific 3',5'-cyclic phosphodiesterase
MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKATREMVNAWFAE
RVHTIPVCKEGIRGHTESCSCPLQQSPRADNSVPGTPTRKISASEFDRPLRPIVVKDSEG
TVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLI
SADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCIRLEWNKGIVGHVAALGEPL
NIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDE
KDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIIS
FMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKSSDTLTREHDANKINYMYAQYVKNTME
PLNIPDVSKDKRFPWTTENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGK
VKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETREL
QSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWIL
SVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGV
NNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAI
LATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAE
LVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCF
PLLDGCRKNRQKWQALAEQQEKMLINGESGQAKRN
Enzyme 35 Number of Residues 875
Enzyme 35 Molecular Weight 100012.2
Enzyme 35 Theoretical pI 6.00
Enzyme 35 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 35 General Function Involved in catalytic activity
Enzyme 35 Specific Function Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'- GMP
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions
  • guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate [RN:R01234]
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein Not Available
Enzyme 35 UniProtKB/Swiss-Prot ID O76074 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name PDE5A_HUMAN Link Image
Enzyme 35 PDB ID 1T9R Link Image
Enzyme 35 PDB File Show
Enzyme 35 3D Structure
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >2628 bp
ATGGAGCGGGCCGGCCCCAGCTTCGGGCAGCAGCGACAGCAGCAGCAGCCCCAGCAGCAG
AAGCAGCAGCAGAGGGATCAGGACTCGGTCGAAGCATGGCTGGACGATCACTGGGACTTT
ACCTTCTCATACTTTGTTAGAAAAGCCACCAGAGAAATGGTCAATGCATGGTTTGCTGAG
AGAGTTCACACCATCCCTGTGTGCAAGGAAGGTATCAGAGGCCACACCGAATCTTGCTCT
TGTCCCTTGCAGCAGAGTCCTCGTGCAGATAACAGTGTCCCTGGAACACCAACCAGGAAA
ATCTCTGCCTCTGAATTTGACCGGCCTCTTAGACCCATTGTTGTCAAGGATTCTGAGGGA
ACTGTGAGCTTCCTCTCTGACTCAGAAAAGAAGGAACAGATGCCTCTAACCCCTCCAAGG
TTTGATCATGATGAAGGGGACCAGTGCTCAAGACTCTTGGAATTAGTGAAGGATATTTCT
AGTCATTTGGATGTCACAGCCTTATGTCACAAAATTTTCTTGCATATCCATGGACTGATA
TCTGCTGACCGCTATTCCCTGTTCCTTGTCTGTGAAGACAGCTCCAATGACAAGTTTCTT
ATCAGCCGCCTCTTTGATGTTGCTGAAGGTTCAACACTGGAAGAAGTTTCAAATAACTGT
ATCCGCTTAGAATGGAACAAAGGCATTGTGGGACATGTGGCAGCGCTTGGTGAGCCCTTG
AACATCAAAGATGCATATGAGGATCCTCGGTTCAATGCAGAAGTTGACCAAATTACAGGC
TACAAGACACAAAGCATTCTTTGTATGCCAATTAAGAATCATAGGGAAGAGGTTGTTGGT
GTAGCCCAGGCCATCAACAAGAAATCAGGAAACGGTGGGACATTTACTGAAAAAGATGAA
AAGGACTTTGCTGCTTATTTGGCATTTTGTGGTATTGTTCTTCATAATGCTCAGCTCTAT
GAGACTTCACTGCTGGAGAACAAGAGAAATCAGGTGCTGCTTGACCTTGCTAGTTTAATT
TTTGAAGAACAACAATCATTAGAAGTAATTTTGAAGAAAATAGCTGCCACTATTATCTCT
TTCATGCAAGTGCAGAAATGCACCATTTTCATAGTGGATGAAGATTGCTCCGATTCTTTT
TCTAGTGTGTTTCACATGGAGTGTGAGGAATTAGAAAAATCATCTGATACATTAACAAGG
GAACATGATGCAAACAAAATCAATTACATGTATGCTCAGTATGTCAAAAATACTATGGAA
CCACTTAATATCCCAGATGTCAGTAAGGATAAAAGATTTCCCTGGACAACTGAAAATACA
GGAAATGTAAACCAGCAGTGCATTAGAAGTTTGCTTTGTACACCTATAAAAAATGGAAAG
AAGAATAAAGTTATAGGGGTTTGCCAACTTGTTAATAAGATGGAGGAGAATACTGGCAAG
GTTAAGCCTTTCAACCGAAATGACGAACAGTTTCTGGAAGCTTTTGTCATCTTTTGTGGC
TTGGGGATCCAGAACACGCAGATGTATGAAGCAGTGGAGAGAGCCATGGCCAAGCAAATG
GTCACATTGGAGGTTCTGTCGTATCATGCTTCAGCAGCAGAGGAAGAAACAAGAGAGCTA
CAGTCGTTAGCGGCTGCTGTGGTGCCATCTGCCCAGACCCTTAAAATTACTGACTTTAGC
TTCAGTGACTTTGAGCTGTCTGATCTGGAAACAGCACTGTGTACAATTCGGATGTTTACT
GACCTCAACCTTGTGCAGAACTTCCAGATGAAACATGAGGTTCTTTGCAGATGGATTTTA
AGTGTTAAGAAGAATTATCGGAAGAATGTTGCCTATCATAATTGGAGACATGCCTTTAAT
ACAGCTCAGTGCATGTTTGCTGCTCTAAAAGCAGGCAAAATTCAGAACAAGCTGACTGAC
CTGGAGATACTTGCATTGCTGATTGCTGCACTAAGCCACGATTTGGATCACCGTGGTGTG
AATAACTCTTACATACAGCGAAGTGAACATCCACTTGCCCAGCTTTACTGCCATTCAATC
ATGGAACACCATCATTTTGACCAGTGCCTGATGATTCTTAATAGTCCAGGCAATCAGATT
CTCAGTGGCCTCTCCATTGAAGAATATAAGACCACGTTGAAAATAATCAAGCAAGCTATT
TTAGCTACAGACCTAGCACTGTACATTAAGAGGCGAGGAGAATTTTTTGAACTTATAAGA
AAAAATCAATTCAATTTGGAAGATCCTCATCAAAAGGAGTTGTTTTTGGCAATGCTGATG
ACAGCTTGTGATCTTTCTGCAATTACAAAACCCTGGCCTATTCAACAACGGATAGCAGAA
CTTGTAGCAACTGAATTTTTTGATCAAGGAGACAGAGAGAGAAAAGAACTCAACATAGAA
CCCACTGATCTAATGAACAGGGAGAAGAAAAACAAAATCCCAAGTATGCAAGTTGGGTTC
ATAGATGCCATCTGCTTGCAACTGTATGAGGCCCTGACCCACGTGTCAGAGGACTGTTTC
CCTTTGCTAGATGGCTGCAGAAAGAACAGGCAGAAATGGCAGGCCCTTGCAGAACAGCAG
GAGAAGATGCTGATTAATGGGGAAAGCGGCCAGGCCAAGCGGAACTGA
Enzyme 35 GenBank Gene ID AF043731 Link Image
Enzyme 35 GeneCard ID PDE5A Link Image
Enzyme 35 GenAtlas ID PDE5A Link Image
Enzyme 35 HGNC ID HGNC:8784 Link Image
Enzyme 35 Chromosome Location 4
Enzyme 35 Locus 4q27
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Loughney K, Hill TR, Florio VA, Uher L, Rosman GJ, Wolda SL, Jones BA, Howard ML, McAllister-Lucas LM, Sonnenburg WK, Francis SH, Corbin JD, Beavo JA, Ferguson K: Isolation and characterization of cDNAs encoding PDE5A, a human cGMP-binding, cGMP-specific 3',5'-cyclic nucleotide phosphodiesterase. Gene. 1998 Aug 17;216(1):139-47. [PubMed Link Image]
  2. Yanaka N, Kotera J, Ohtsuka A, Akatsuka H, Imai Y, Michibata H, Fujishige K, Kawai E, Takebayashi S, Okumura K, Omori K: Expression, structure and chromosomal localization of the human cGMP-binding cGMP-specific phosphodiesterase PDE5A gene. Eur J Biochem. 1998 Jul 15;255(2):391-9. [PubMed Link Image]
  3. Stacey P, Rulten S, Dapling A, Phillips SC: Molecular cloning and expression of human cGMP-binding cGMP-specific phosphodiesterase (PDE5). Biochem Biophys Res Commun. 1998 Jun 18;247(2):249-54. [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. Zhou L, Thompson WJ, Potter DE: Multiple cyclic nucleotide phosphodiesterases in human trabecular meshwork cells. Invest Ophthalmol Vis Sci. 1999 Jul;40(8):1745-52. [PubMed Link Image]
  7. Sung BJ, Hwang KY, Jeon YH, Lee JI, Heo YS, Kim JH, Moon J, Yoon JM, Hyun YL, Kim E, Eum SJ, Park SY, Lee JO, Lee TG, Ro S, Cho JM: Structure of the catalytic domain of human phosphodiesterase 5 with bound drug molecules. Nature. 2003 Sep 4;425(6953):98-102. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 5951
Enzyme 36 Name GMP reductase 2
Enzyme 36 Synonyms
  1. Guanosine 5'-monophosphate oxidoreductase 2
  2. Guanosine monophosphate reductase 2
Enzyme 36 Gene Name GMPR2
Enzyme 36 Protein Sequence >GMP reductase 2
MPHIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQTYSGVPIIAANMDTVGT
FEMAKVLCKFSLFTAVHKHYSLVQWQEFAGQNPDCLEHLAASSGTGSSDFEQLEQILEAI
PQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTGEMVEELILSGADIIKVGI
GPGSVCTTRKKTGVGYPQLSAVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVM
LGGMLAGHSESGGELIERDGKKYKLFYGMSSEMAMKKYAGGVAEYRASEGKTVEVPFKGD
VEHTIRDILGGIRSTCTYVGAAKLKELSRRTTFIRVTQQVNPIFSEAC
Enzyme 36 Number of Residues 348
Enzyme 36 Molecular Weight 37874.1
Enzyme 36 Theoretical pI 7.25
Enzyme 36 GO Classification
Function
  • GMP reductase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on NADH or NADPH, nitrogenous group as acceptor
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
  • oxidation reduction
Component
Enzyme 36 General Function Involved in catalytic activity
Enzyme 36 Specific Function Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. Plays a role in modulating cellular differentiation
Enzyme 36 Pathways
Enzyme 36 Reactions
  • inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH + H+ [RN:R01134]
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein Not Available
Enzyme 36 UniProtKB/Swiss-Prot ID Q9P2T1 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name GMPR2_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >1047 bp
ATGCCTCATATTGACAACGATGTGAAACTGGACTTCAAGGATGTCCTTTTGAGGCCCAAA
CGCAGTACCCTTAAGTCTCGAAGTGAGGTGGATCTCACAAGATCCTTTTCATTTCGGAAC
TCAAAGCAGACATACTCTGGGGTTCCCATCATTGCTGCCAATATGGATACTGTGGGCACC
TTTGAGATGGCCAAGGTTCTCTGTAAGTTCTCTCTCTTCACTGCTGTCCATAAGCACTAT
AGCCTCGTTCAGTGGCAAGAGTTTGCTGGCCAGAATCCTGACTGTCTTGAGCATCTGGCT
GCCAGCTCAGGCACAGGCTCTTCTGACTTTGAGCAGCTGGAACAGATCCTGGAAGCTATT
CCCCAGGTGAAGTATATATGCCTGGATGTGGCAAATGGCTACTCTGAACACTTTGTTGAA
TTTGTAAAAGATGTACGGAAGCGCTTCCCCCAGCACACCATCATGGCAGGGAATGTGGTA
ACAGGAGAGATGGTAGAAGAGCTCATCCTTTCTGGGGCTGACATCATCAAAGTGGGAATT
GGGCCAGGCTCTGTGTGTACTACTCGGAAGAAAACTGGAGTGGGGTATCCACAGCTCAGC
GCAGTGATGGAGTGTGCAGATGCTGCTCATGGCCTCAAAGGCCACATCATTTCAGATGGA
GGTTGCAGCTGTCCTGGGGATGTGGCCAAGGCTTTTGGGGCAGGAGCTGACTTCGTGATG
CTGGGTGGCATGCTGGCTGGGCACAGTGAGTCAGGTGGTGAGCTCATCGAGAGGGATGGC
AAGAAGTACAAGCTCTTCTATGGAATGAGTTCTGAAATGGCCATGAAGAAGTATGCTGGG
GGCGTGGCTGAGTACAGAGCCTCAGAGGGAAAGACAGTGGAAGTTCCTTTTAAAGGAGAT
GTGGAACATACCATCCGAGACATCCTAGGAGGGATCCGCTCTACGTGTACCTATGTGGGA
GCAGCTAAGCTCAAAGAGTTGAGCAGGAGAACTACCTTCATCCGAGTCACCCAGCAGGTG
AATCCAATCTTCAGTGAGGCGTGCTAG
Enzyme 36 GenBank Gene ID AF419346 Link Image
Enzyme 36 GeneCard ID GMPR2 Link Image
Enzyme 36 GenAtlas ID GMPR2 Link Image
Enzyme 36 HGNC ID HGNC:4377 Link Image
Enzyme 36 Chromosome Location 1
Enzyme 36 Locus 14q12
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Deng Y, Wang Z, Ying K, Gu S, Ji C, Huang Y, Gu X, Wang Y, Xu Y, Li Y, Xie Y, Mao Y: NADPH-dependent GMP reductase isoenzyme of human (GMPR2). Expression, purification, and kinetic properties. Int J Biochem Cell Biol. 2002 Sep;34(9):1035-50. [PubMed Link Image]
  2. Zhang J, Zhang W, Zou D, Chen G, Wan T, Zhang M, Cao X: Cloning and functional characterization of GMPR2, a novel human guanosine monophosphate reductase, which promotes the monocytic differentiation of HL-60 leukemia cells. J Cancer Res Clin Oncol. 2003 Feb;129(2):76-83. Epub 2003 Mar 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. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 5958
Enzyme 37 Name GMP reductase 1
Enzyme 37 Synonyms
  1. Guanosine 5'-monophosphate oxidoreductase 1
  2. Guanosine monophosphate reductase 1
Enzyme 37 Gene Name GMPR
Enzyme 37 Protein Sequence >GMP reductase 1
MPRIDADLKLDFKDVLLRPKRSSLKSRAEVDLERTFTFRNSKQTYSGIPIIVANMDTVGT
FEMAAVMSQHSMFTAIHKHYSLDDWKLFATNHPECLQNVAVSSGSGQNDLEKMTSILEAV
PQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGADIIKVGV
GPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVM
LGGMFSGHTECAGEVFERNGRKLKLFYGMSSDTAMNKHAGGVAEYRASEGKTVEVPYKGD
VENTILDILGGLRSTCTYVGAAKLKELSRRATFIRVTQQHNTVFS
Enzyme 37 Number of Residues 345
Enzyme 37 Molecular Weight 37418.6
Enzyme 37 Theoretical pI 7.08
Enzyme 37 GO Classification
Function
  • GMP reductase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on NADH or NADPH
  • oxidoreductase activity, acting on NADH or NADPH, nitrogenous group as acceptor
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
  • oxidation reduction
Component
Enzyme 37 General Function Involved in catalytic activity
Enzyme 37 Specific Function Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides
Enzyme 37 Pathways
Enzyme 37 Reactions
  • inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH + H+ [RN:R01134]
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • None
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 56001065 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID P36959 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name GMPR1_HUMAN Link Image
Enzyme 37 PDB ID 2BLE Link Image
Enzyme 37 PDB File Show
Enzyme 37 3D Structure
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >1038 bp
ATGCCCCGCATAGATGCGGACCTCAAGCTCGACTTCAAGGATGTCCTGCTCCGACCTAAG
CGGAGCAGCCTCAAGAGCCGAGCCGAGGTGGATCTTGAACGCACCTTCACGTTTCGAAAT
TCAAAGCAGACCTACTCAGGGATTCCCATCATCGTGGCCAACATGGACACTGTGGGCACG
TTTGAGATGGCAGCCGTGATGTCACAGCACTCCATGTTTACAGCAATTCATAAGCATTAC
TCCCTGGATGACTGGAAGCTCTTTGCCACAAATCACCCAGAATGCCTGCAGAATGTAGCC
GTGAGTTCAGGCAGTGGGCAGAATGATCTGGAAAAGATGACCAGCATCCTGGAAGCTGTG
CCACAGGTTAAGTTTATTTGCCTGGATGTGGCCAATGGGTATTCAGAACATTTTGTGGAA
TTCGTGAAACTTGTCCGTGCCAAATTTCCTGAACACACCATTATGGCAGGGAACGTGGTG
ACAGGAGAAATGGTAGAAGAGCTTATTCTTTCCGGAGCAGATATCATCAAAGTGGGAGTT
GGACCAGGTTCTGTGTGCACCACCCGCACCAAGACGGGAGTGGGGTACCCCCAGCTGAGT
GCCGTCATTGAGTGTGCCGACTCTGCCCATGGCCTGAAGGGCCACATCATCTCTGATGGA
GGCTGTACGTGTCCAGGGGATGTCGCCAAAGCCTTTGGAGCTGGAGCAGATTTTGTCATG
CTGGGAGGAATGTTTTCGGGTCATACGGAGTGTGCTGGAGAAGTGTTTGAGAGGAACGGA
CGGAAGCTCAAGCTCTTCTACGGGATGAGCTCTGACACCGCCATGAACAAGCACGCAGGA
GGAGTTGCTGAGTACAGAGCCTCTGAGGGTAAGACTGTGGAAGTTCCTTACAAAGGAGAT
GTGGAAAACACTATCCTGGATATTCTCGGGGGACTGAGGTCCACGTGCACCTACGTGGGG
GCCGCCAAACTCAAGGAGCTCAGCAGGAGGGCAACATTCATCCGGGTGACCCAGCAGCAC
AACACCGTGTTCAGCTAA
Enzyme 37 GenBank Gene ID AL009031 Link Image
Enzyme 37 GeneCard ID GMPR Link Image
Enzyme 37 GenAtlas ID GMPR Link Image
Enzyme 37 HGNC ID HGNC:4376 Link Image
Enzyme 37 Chromosome Location 6
Enzyme 37 Locus 6p23
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Kanno H, Huang IY, Kan YW, Yoshida A: Two structural genes on different chromosomes are required for encoding the major subunit of human red cell glucose-6-phosphate dehydrogenase. Cell. 1989 Aug 11;58(3):595-606. [PubMed Link Image]
  2. Kondoh T, Kanno H, Chang L, Yoshida A: Genomic structure and expression of human guanosine monophosphate reductase. Hum Genet. 1991 Dec;88(2):219-24. [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. Henikoff S, Smith JM: The human mRNA that provides the N-terminus of chimeric G6PD encodes GMP reductase. Cell. 1989 Sep 22;58(6):1021-2. [PubMed Link Image]
  6. Yoshida A, Kan YW: Origin of "fused" glucose-6-phosphate dehydrogenase. Cell. 1990 Jul 13;62(1):11-2. [PubMed Link Image]
  7. Kondoh T, Kanno H, Chang LF, Yoshida A: Identification of common variant alleles of the human guanosine monophosphate reductase gene. Hum Genet. 1991 Dec;88(2):225-7. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 6218
Enzyme 38 Name Guanylate kinase
Enzyme 38 Synonyms
  1. GMP kinase
Enzyme 38 Gene Name GUK1
Enzyme 38 Protein Sequence >Guanylate kinase
MSGPRPVVLSGPSGAGKSTLLKRLLQEHSGIFGFSVSHTTRNPRPGEENGKDYYFVTREV
MQRDIAAGDFIEHAEFSGNLYGTSKVAVQAVQAMNRICVLDVDLQGVRNIKATDLRPIYI
SVQPPSLHVLEQRLRQRNTETEESLVKRLAAAQADMESSKEPGLFDVVIINDSLDQAYAE
LKEALSEEIKKAQRTGA
Enzyme 38 Number of Residues 197
Enzyme 38 Molecular Weight 21725.4
Enzyme 38 Theoretical pI 6.53
Enzyme 38 GO Classification
Function
  • catalytic activity
  • guanylate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleotide metabolic process
Component
Enzyme 38 General Function Involved in guanylate kinase activity
Enzyme 38 Specific Function Essential for recycling GMP and indirectly, cGMP
Enzyme 38 Pathways
Enzyme 38 Reactions
  • ATP + GMP = ADP + GDP [RN:R00332]
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 1196436 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID Q16774 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name KGUA_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >594 bp
ATGTCGGGCCCCAGGCCTGTGGTGCTGAGCGGGCCTTCGGGAGCTGGGAAGAGCACCCTG
CTGAAGAGGCTGCTCCAGGAGCACAGCGGCATCTTTGGCTTCAGCGTGTCCCATACCACG
AGGAACCCGAGGCCCGGCGAGGAGAACGGCAAAGATTACTACTTTGTAACCAGGGAGGTG
ATGCAGCGTGACATAGCAGCCGGCGACTTCATCGAGCATGCCGAGTTCTCGGGGAACCTG
TATGGCACGAGCAAGGTGGCGGTGCAGGCCGTGCAGGCCATGAACCGCATCTGTGTGCTG
GACGTGGACCTGCAGGGTGTGCGGAACATCAAGGCCACCGATCTGCGGCCCATCTACATC
TCTGTGCAGCCGCCTTCACTGCACGTGCTGGAGCAGCGGCTGCGGCAGCGCAACACTGAA
ACCGAGGAGAGCCTGGTGAAGCGGCTGGCTGCTGCCCAGGCCGACATGGAGAGCAGCAAG
GAGCCCGGCCTGTTTGATGTGGTCATCATTAACGACAGCCTGGACCAGGCCTACGCAGAG
CTGAAGGAGGCGCTCTCTGAGGAAATCAAGAAAGCTCAAAGGACCGGCGCCTGA
Enzyme 38 GenBank Gene ID L76200 Link Image
Enzyme 38 GeneCard ID GUK1 Link Image
Enzyme 38 GenAtlas ID GUK1 Link Image
Enzyme 38 HGNC ID HGNC:4693 Link Image
Enzyme 38 Chromosome Location 1
Enzyme 38 Locus 1q32-q41
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Fitzgibbon J, Katsanis N, Wells D, Delhanty J, Vallins W, Hunt DM: Human guanylate kinase (GUK1): cDNA sequence, expression and chromosomal localisation. FEBS Lett. 1996 May 6;385(3):185-8. [PubMed Link Image]
  2. Brady WA, Kokoris MS, Fitzgibbon M, Black ME: Cloning, characterization, and modeling of mouse and human guanylate kinases. J Biol Chem. 1996 Jul 12;271(28):16734-40. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 6352
Enzyme 39 Name Atrial natriuretic peptide receptor 2
Enzyme 39 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 39 Gene Name NPR2
Enzyme 39 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 39 Number of Residues 1047
Enzyme 39 Molecular Weight 117021.0
Enzyme 39 Theoretical pI 6.86
Enzyme 39 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 39 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 39 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 39 Pathways
Enzyme 39 Reactions
  • GTP = 3',5'-cyclic GMP + diphosphate [RN:R00434]
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • 1-22
Enzyme 39 Transmembrane Regions
  • 459-478
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 5139790 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID P20594 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name ANPRB_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 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 39 GenBank Gene ID AB005647 Link Image
Enzyme 39 GeneCard ID NPR2 Link Image
Enzyme 39 GenAtlas ID NPR2 Link Image
Enzyme 39 HGNC ID HGNC:7944 Link Image
Enzyme 39 Chromosome Location 9
Enzyme 39 Locus 9p21-p12
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 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 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 6358
Enzyme 40 Name Atrial natriuretic peptide receptor 1
Enzyme 40 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 40 Gene Name NPR1
Enzyme 40 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 40 Number of Residues 1061
Enzyme 40 Molecular Weight 118918.1
Enzyme 40 Theoretical pI 6.61
Enzyme 40 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 40 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 40 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 40 Pathways
Enzyme 40 Reactions
  • GTP = 3',5'-cyclic GMP + diphosphate [RN:R00434]
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • 1-32
Enzyme 40 Transmembrane Regions
  • 474-494
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 3297986 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID P16066 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name ANPRA_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 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 40 GenBank Gene ID AB010491 Link Image
Enzyme 40 GeneCard ID NPR1 Link Image
Enzyme 40 GenAtlas ID NPR1 Link Image
Enzyme 40 HGNC ID HGNC:7943 Link Image
Enzyme 40 Chromosome Location 1
Enzyme 40 Locus 1q21-q22
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 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 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 6359
Enzyme 41 Name Heat-stable enterotoxin receptor
Enzyme 41 Synonyms
  1. STA receptor
  2. hSTAR
  3. Guanylyl cyclase C
  4. GC-C
  5. Intestinal guanylate cyclase
Enzyme 41 Gene Name GUCY2C
Enzyme 41 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 41 Number of Residues 1073
Enzyme 41 Molecular Weight 123367.7
Enzyme 41 Theoretical pI 7.18
Enzyme 41 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 41 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 41 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 41 Pathways
Enzyme 41 Reactions
  • GTP = 3',5'-cyclic GMP + diphosphate [RN:R00434]
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • 1-23
Enzyme 41 Transmembrane Regions
  • 431-454
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 222080083 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID P25092 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name GUC2C_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 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 41 GenBank Gene ID NM_004963.3 Link Image
Enzyme 41 GeneCard ID GUCY2C Link Image
Enzyme 41 GenAtlas ID GUCY2C Link Image
Enzyme 41 HGNC ID HGNC:4688 Link Image
Enzyme 41 Chromosome Location 1
Enzyme 41 Locus 12p12
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 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 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 6413
Enzyme 42 Name Cyclic nucleotide-gated cation channel alpha-3
Enzyme 42 Synonyms
  1. Cone photoreceptor cGMP-gated channel subunit alpha
  2. Cyclic nucleotide-gated channel alpha-3
  3. CNG channel alpha-3
  4. CNG-3
  5. CNG3
Enzyme 42 Gene Name CNGA3
Enzyme 42 Protein Sequence >Cyclic nucleotide-gated cation channel alpha-3
MAKINTQYSHPSRTHLKVKTSDRDLNRAENGLSRAHSSSEETSSVLQPGIAMETRGLADS
GQGSFTGQGIARLSRLIFLLRRWAARHVHHQDQGPDSFPDRFRGAELKEVSSQESNAQAN
VGSQEPADRGRSAWPLAKCNTNTSNNTEEEKKTKKKDAIVVDPSSNLYYRWLTAIALPVF
YNWYLLICRACFDELQSEYLMLWLVLDYSADVLYVLDVLVRARTGFLEQGLMVSDTNRLW
QHYKTTTQFKLDVLSLVPTDLAYLKVGTNYPEVRFNRLLKFSRLFEFFDRTETRTNYPNM
FRIGNLVLYILIIIHWNACIYFAISKFIGFGTDSWVYPNISIPEHGRLSRKYIYSLYWST
LTLTTIGETPPPVKDEEYLFVVVDFLVGVLIFATIVGNVGSMISNMNASRAEFQAKIDSI
KQYMQFRKVTKDLETRVIRWFDYLWANKKTVDEKEVLKSLPDKLKAEIAINVHLDTLKKV
RIFQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGKEMYIINEGKLAVVADDGVTQFVV
LSDGSYFGEISILNIKGSKSGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPEAKKALEE
KGRQILMKDNLIDEELARAGADPKDLEEKVEQLGSSLDTLQTRFARLLAEYNATQMKMKQ
RLSQLESQVKGGGDKPLADGEVPGDATKTEDKQQ
Enzyme 42 Number of Residues 694
Enzyme 42 Molecular Weight 78837.4
Enzyme 42 Theoretical pI 7.80
Enzyme 42 GO Classification
Function
  • ion channel activity
  • ion transmembrane transporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • membrane
Enzyme 42 General Function Involved in ion channel activity
Enzyme 42 Specific Function Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cyclic GMP which leads to an opening of the cation channel and thereby causing a depolarization of cone photoreceptors. Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficacy of the channel when coexpressed with CNGB3. Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones
Enzyme 42 Pathways Not Available
Enzyme 42 Reactions Not Available
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • 171-192 305-325 378-397
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 62988794 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID Q16281 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name CNGA3_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >2085 bp
ATGGCCAAGATCAACACCCAATACTCCCACCCCTCCAGGACCCACCTCAAGGTAAAGACC
TCAGACCGAGATCTCAATCGCGCTGAAAATGGCCTCAGCAGAGCCCACTCGTCAAGTGAG
GAGACATCGTCAGTGCTGCAGCCGGGGATCGCCATGGAGACCAGAGGACTGGCTGACTCC
GGGCAGGGCTCCTTCACCGGCCAGGGGATCGCCAGGCTGTCGCGCCTCATCTTCTTGCTG
CGCAGGTGGGCTGCCAGGCATGTGCACCACCAGGACCAGGGACCGGACTCTTTTCCTGAT
CGTTTCCGTGGAGCCGAGCTTAAGGAGGTGTCCAGCCAAGAAAGCAATGCCCAGGCAAAT
GTGGGCAGCCAGGAGCCAGCAGACAGAGGGAGAAGCGCCTGGCCCCTGGCCAAATGCAAC
ACTAACACCAGCAACAACACGGAGGAGGAGAAGAAGACGAAAAAGAAGGATGCGATCGTG
GTGGACCCGTCCAGCAACCTGTACTACCGCTGGCTGACCGCCATCGCCCTGCCTGTCTTC
TATAACTGGTATCTGCTTATTTGCAGGGCCTGTTTCGATGAGCTGCAGTCCGAGTACCTG
ATGCTGTGGCTGGTCCTGGACTACTCGGCAGATGTCCTGTATGTCTTGGATGTGCTTGTA
CGAGCTCGGACAGGTTTTCTCGAGCAAGGCTTAATGGTCAGTGATACCAACAGGCTGTGG
CAGCATTACAAGACGACCACGCAGTTCAAGCTGGATGTGTTGTCCCTGGTCCCCACCGAC
CTGGCTTACTTAAAGGTGGGCACAAACTACCCAGAAGTGAGGTTCAACCGCCTACTGAAG
TTTTCCCGGCTCTTTGAATTCTTTGACCGCACAGAGACAAGGACCAACTACCCCAATATG
TTCAGGATTGGGAACTTGGTCTTGTACATTCTCATCATCATCCACTGGAATGCCTGCATC
TACTTTGCCATTTCCAAGTTCATTGGTTTTGGGACAGACTCCTGGGTCTACCCAAACATC
TCAATCCCAGAGCATGGGCGCCTCTCCAGGAAGTACATTTACAGTCTCTACTGGTCCACC
TTGACCCTTACCACCATTGGTGAGACCCCACCCCCCGTGAAAGATGAGGAGTATCTCTTT
GTGGTCGTAGACTTCTTGGTGGGTGTTCTGATTTTTGCCACCATTGTGGGCAATGTGGGC
TCCATGATCTCGAATATGAATGCCTCACGGGCAGAGTTCCAGGCCAAGATTGATTCCATC
AAGCAGTACATGCAGTTCCGCAAGGTCACCAAGGACTTGGAGACGCGGGTTATCCGGTGG
TTTGACTACCTGTGGGCCAACAAGAAGACGGTGGATGAGAAGGAGGTGCTCAAGAGCCTC
CCAGACAAGCTGAAGGCTGAGATCGCCATCAACGTGCACCTGGACACGCTGAAGAAGGTT
CGCATCTTCCAGGACTGTGAGGCAGGGCTGCTGGTGGAGCTGGTGCTGAAGCTGCGACCC
ACTGTGTTCAGCCCTGGGGATTATATCTGCAAGAAGGGAGATATTGGGAAGGAGATGTAC
ATCATCAACGAGGGCAAGCTGGCCGTGGTGGCTGATGATGGGGTCACCCAGTTCGTGGTC
CTCAGCGATGGCAGCTACTTCGGGGAGATCAGCATTCTGAACATCAAGGGGAGCAAGTCG
GGGAACCGCAGGACGGCCAACATCCGCAGCATTGGCTACTCAGACCTGTTCTGCCTCTCA
AAGGACGATCTCATGGAGGCCCTCACCGAGTACCCCGAAGCCAAGAAGGCCCTGGAGGAG
AAAGGACGGCAGATCCTGATGAAAGACAACCTGATCGATGAGGAGCTGGCCAGGGCGGGC
GCGGACCCCAAGGACCTTGAGGAGAAAGTGGAGCAGCTGGGGTCCTCCCTGGACACCCTG
CAGACCAGGTTTGCACGCCTCCTGGCTGAGTACAACGCCACCCAGATGAAGATGAAGCAG
CGTCTCAGCCAACTGGAAAGCCAGGTGAAGGGTGGTGGGGACAAGCCCCTGGCTGATGGG
GAAGTTCCCGGGGATGCTACAAAAACAGAGGACAAACAACAGTGA
Enzyme 42 GenBank Gene ID AC092675 Link Image
Enzyme 42 GeneCard ID CNGA3 Link Image
Enzyme 42 GenAtlas ID CNGA3 Link Image
Enzyme 42 HGNC ID HGNC:2150 Link Image
Enzyme 42 Chromosome Location 2
Enzyme 42 Locus 2q11.2
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Wissinger B, Muller F, Weyand I, Schuffenhauer S, Thanos S, Kaupp UB, Zrenner E: Cloning, chromosomal localization and functional expression of the gene encoding the alpha-subunit of the cGMP-gated channel in human cone photoreceptors. Eur J Neurosci. 1997 Dec;9(12):2512-21. [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]
  4. Distler M, Biel M, Flockerzi V, Hofmann F: Expression of cyclic nucleotide-gated cation channels in non-sensory tissues and cells. Neuropharmacology. 1994 Nov;33(11):1275-82. [PubMed Link Image]
  5. Sundin OH, Yang JM, Li Y, Zhu D, Hurd JN, Mitchell TN, Silva ED, Maumenee IH: Genetic basis of total colourblindness among the Pingelapese islanders. Nat Genet. 2000 Jul;25(3):289-93. [PubMed Link Image]
  6. Peng C, Rich ED, Varnum MD: Subunit configuration of heteromeric cone cyclic nucleotide-gated channels. Neuron. 2004 May 13;42(3):401-10. [PubMed Link Image]
  7. Kohl S, Marx T, Giddings I, Jagle H, Jacobson SG, Apfelstedt-Sylla E, Zrenner E, Sharpe LT, Wissinger B: Total colourblindness is caused by mutations in the gene encoding the alpha-subunit of the cone photoreceptor cGMP-gated cation channel. Nat Genet. 1998 Jul;19(3):257-9. [PubMed Link Image]
  8. Wissinger B, Gamer D, Jagle H, Giorda R, Marx T, Mayer S, Tippmann S, Broghammer M, Jurklies B, Rosenberg T, Jacobson SG, Sener EC, Tatlipinar S, Hoyng CB, Castellan C, Bitoun P, Andreasson S, Rudolph G, Kellner U, Lorenz B, Wolff G, Verellen-Dumoulin C, Schwartz M, Cremers FP, Apfelstedt-Sylla E, Zrenner E, Salati R, Sharpe LT, Kohl S: CNGA3 mutations in hereditary cone photoreceptor disorders. Am J Hum Genet. 2001 Oct;69(4):722-37. Epub 2001 Aug 30. [PubMed Link Image]
  9. Johnson S, Michaelides M, Aligianis IA, Ainsworth JR, Mollon JD, Maher ER, Moore AT, Hunt DM: Achromatopsia caused by novel mutations in both CNGA3 and CNGB3. J Med Genet. 2004 Feb;41(2):e20. [PubMed Link Image]
  10. Liu C, Varnum MD: Functional consequences of progressive cone dystrophy-associated mutations in the human cone photoreceptor cyclic nucleotide-gated channel CNGA3 subunit. Am J Physiol Cell Physiol. 2005 Jul;289(1):C187-98. Epub 2005 Mar 2. [PubMed Link Image]
  11. Nishiguchi KM, Sandberg MA, Gorji N, Berson EL, Dryja TP: Cone cGMP-gated channel mutations and clinical findings in patients with achromatopsia, macular degeneration, and other hereditary cone diseases. Hum Mutat. 2005 Mar;25(3):248-58. [PubMed Link Image]
  12. Reuter P, Koeppen K, Ladewig T, Kohl S, Baumann B, Wissinger B: Mutations in CNGA3 impair trafficking or function of cone cyclic nucleotide-gated channels, resulting in achromatopsia. Hum Mutat. 2008 Oct;29(10):1228-36. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 6417
Enzyme 43 Name Rap guanine nucleotide exchange factor 2
Enzyme 43 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 43 Gene Name RAPGEF2
Enzyme 43 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 43 Number of Residues 1499
Enzyme 43 Molecular Weight 167415.5
Enzyme 43 Theoretical pI 6.64
Enzyme 43 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 43 General Function Involved in protein binding
Enzyme 43 Specific Function Guanine nucleotide exchange factor (GEF) for Rap1A, Rap1B and Rap2B GTPases. Does not interact with cAMP or cGMP
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions Not Available
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 7657261 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID Q9Y4G8 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name RPGF2_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 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 43 GenBank Gene ID NM_014247.2 Link Image
Enzyme 43 GeneCard ID RAPGEF2 Link Image
Enzyme 43 GenAtlas ID RAPGEF2 Link Image
Enzyme 43 HGNC ID HGNC:16854 Link Image
Enzyme 43 Chromosome Location 4
Enzyme 43 Locus 4q32.1
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 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 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 7002
Enzyme 44 Name Rho guanine nucleotide exchange factor 1
Enzyme 44 Synonyms
  1. 115 kDa guanine nucleotide exchange factor
  2. p115-RhoGEF
  3. p115RhoGEF
  4. Sub1.5
Enzyme 44 Gene Name ARHGEF1
Enzyme 44 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 44 Number of Residues 912
Enzyme 44 Molecular Weight 102434.3
Enzyme 44 Theoretical pI 5.37
Enzyme 44 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 44 General Function Involved in GTPase activator activity
Enzyme 44 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 44 Pathways Not Available
Enzyme 44 Reactions Not Available
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 15011972 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID Q92888 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name ARHG1_HUMAN Link Image
Enzyme 44 PDB ID 1SHZ Link Image
Enzyme 44 PDB File Show
Enzyme 44 3D Structure
Enzyme 44 Cellular Location Not Available
Enzyme 44 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 44 GenBank Gene ID NM_004706.3 Link Image
Enzyme 44 GeneCard ID ARHGEF1 Link Image
Enzyme 44 GenAtlas ID Not Available
Enzyme 44 HGNC ID Not Available
Enzyme 44 Chromosome Location 1
Enzyme 44 Locus 19q13.13
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 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 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 7120
Enzyme 45 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
Enzyme 45 Synonyms
  1. G gamma-I
Enzyme 45 Gene Name GNG2
Enzyme 45 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFCAIL
Enzyme 45 Number of Residues 71
Enzyme 45 Molecular Weight 7850.0
Enzyme 45 Theoretical pI 8.22
Enzyme 45 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 45 General Function Involved in signal transducer activity
Enzyme 45 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 45 Pathways Not Available
Enzyme 45 Reactions Not Available
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 20147633 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID P59768 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name GBG2_HUMAN Link Image
Enzyme 45 PDB ID 1GP2 Link Image
Enzyme 45 PDB File Show
Enzyme 45 3D Structure
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >216 bp
ATGGCCAGCAACAACACCGCCAGCATAGCACAAGCCAGGAAGCTGGTAGAGCAGCTTAAG
ATGGAAGCCAATATCGACAGGATAAAGGTGTCCAAGGCAGCTGCAGATTTGATGGCCTAC
TGTGAAGCACATGCCAAGGAAGACCCCCTCCTGACCCCTGTTCCGGCTTCAGAAAACCCG
TTTAGGGAGAAGAAGTTTTTCTGTGCCATCCTTTAA
Enzyme 45 GenBank Gene ID AF493870 Link Image
Enzyme 45 GeneCard ID GNG2 Link Image
Enzyme 45 GenAtlas ID GNG2 Link Image
Enzyme 45 HGNC ID HGNC:4404 Link Image
Enzyme 45 Chromosome Location 1
Enzyme 45 Locus 14q21
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 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 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 7131
Enzyme 46 Name Ras-related C3 botulinum toxin substrate 1
Enzyme 46 Synonyms
  1. Cell migration-inducing gene 5 protein
  2. Ras-like protein TC25
  3. p21-Rac1
Enzyme 46 Gene Name RAC1
Enzyme 46 Protein Sequence >Ras-related C3 botulinum toxin substrate 1
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAG
QEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLR
DDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPP
PVKKRKRKCLLL
Enzyme 46 Number of Residues 192
Enzyme 46 Molecular Weight 21449.9
Enzyme 46 Theoretical pI 8.65
Enzyme 46 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 46 General Function Involved in GTP binding
Enzyme 46 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 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein Not Available
Enzyme 46 UniProtKB/Swiss-Prot ID P63000 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name RAC1_HUMAN Link Image
Enzyme 46 PDB ID 1I4L Link Image
Enzyme 46 PDB File Show
Enzyme 46 3D Structure
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >579 bp
ATGCAGGCCATCAAGTGTGTGGTGGTGGGAGACGGAGCTGTAGGTAAAACTTGCCTACTG
ATCAGTTACACAACCAATGCATTTCCTGGAGAATATATCCCTACTGTCTTTGACAATTAT
TCTGCCAATGTTATGGTAGATGGAAAACCGGTGAATCTGGGCTTATGGGATACAGCTGGA
CAAGAAGATTATGACAGATTACGCCCCCTATCCTATCCGCAAACAGATGTGTTCTTAATT
TGCTTTTCCCTTGTGAGTCCTGCATCATTTGAAAATGTCCGTGCAAAGTGGTATCCTGAG
GTGCGGCACCACTGTCCCAACACTCCCATCATCCTAGTGGGAACTAAACTTGATCTTAGG
GATGATAAAGACACGATCGAGAAACTGAAGGAGAAGAAGCTGACTCCCATCACCTATCCG
CAGGGTCTAGCCATGGCTAAGGAGATTGGTGCTGTAAAATACCTGGAGTGCTCGGCGCTC
ACACAGCGAGGCCTCAAGACAGTGTTTGACGAAGCGATCCGAGCAGTCCTCTGCCCGCCT
CCCGTGAAGAAGAGGAAGAGAAAATGCCTGCTGTTGTAA
Enzyme 46 GenBank Gene ID M29870 Link Image
Enzyme 46 GeneCard ID RAC1 Link Image
Enzyme 46 GenAtlas ID RAC1 Link Image
Enzyme 46 HGNC ID HGNC:9801 Link Image
Enzyme 46 Chromosome Location 7
Enzyme 46 Locus 7p22
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 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 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 7134
Enzyme 47 Name Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Enzyme 47 Synonyms
  1. Adenylate cyclase-stimulating G alpha protein
Enzyme 47 Gene Name GNAS
Enzyme 47 Protein Sequence >Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQM
RILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELA
NPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLD
KIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFND
VTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEK
VLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCY
PHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL
Enzyme 47 Number of Residues 394
Enzyme 47 Molecular Weight 45664.2
Enzyme 47 Theoretical pI 5.56
Enzyme 47 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 47 General Function Involved in signal transducer activity
Enzyme 47 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 47 Pathways Not Available
Enzyme 47 Reactions Not Available
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 31915 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID P63092 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name GNAS2_HUMAN Link Image
Enzyme 47 PDB ID 1U0H Link Image
Enzyme 47 PDB File Show
Enzyme 47 3D Structure
Enzyme 47 Cellular Location Not Available
Enzyme 47 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 47 GenBank Gene ID X04408 Link Image
Enzyme 47 GeneCard ID GNAS Link Image
Enzyme 47 GenAtlas ID GNAS Link Image
Enzyme 47 HGNC ID HGNC:4392 Link Image
Enzyme 47 Chromosome Location 2
Enzyme 47 Locus 20q13.3
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 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 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 7136
Enzyme 48 Name Proto-oncogene DBL
Enzyme 48 Synonyms
  1. Proto-oncogene MCF-2
  2. MCF2-transforming protein
  3. DBL-transforming protein
Enzyme 48 Gene Name MCF2
Enzyme 48 Protein Sequence >Proto-oncogene DBL
MAEANPRRGKMRFRRNAASFPGNLHLVLVLRPTSFLQRTFTDIGFWFSQEDFMLKLPVVM
LSSVSDLLTYIDDKQLTPELGGTLQYCHSEWIIFRNAIENFALTVKEMAQMLQSFGTELA
ETELPDDIPSIEEILAIRAERYHLLKNDITAVTKEGKILLTNLEVPDTEGAVSSRLECHR
QISGDWQTINKLLTQVHDMETAFDGFWEKHQLKMEQYLQLWKFEQDFQQLVTEVEFLLNQ
QAELADVTGTIAQVKQKIKKLENLDENSQELLSKAQFVILHGHKLAANHHYALDLICQRC
NELRYLSDILVNEIKAKRIQLSRTFKMHKLLQQARQCCDEGECLLANQEIDKFQSKEDAQ
KALQDIENFLEMALPFINYEPETLQYEFDVILSPELKVQMKTIQLKLENIRSIFENQQAG
FRNLADKHVRPIQFVVPTPENLVTSGTPFFSSKQGKKTWRQNQSNLKIEVVPDCQEKRSS
GPSSSLDNGNSLDVLKNHVLNELIQTERVYVRELYTVLLGYRAEMDNPEMFDLMPPLLRN
KKDILFGNMAEIYEFHNDIFLSSLENCAHAPERVGPCFLERKDDFQMYAKYCQNKPRSET
IWRKYSECAFFQECQRKLKHRLRLDSYLLKPVQRITKYQLLLKELLKYSKDCEGSALLKK
ALDAMLDLLKSVNDSMHQIAINGYIGNLNELGKMIMQGGFSVWIGHKKGATKMKDLARFK
PMQRHLFLYEKAIVFCKRRVESGEGSDRYPSYSFKHCWKMDEVGITEYVKGDNRKFEIWY
GEKEEVYIVQASNVDVKMTWLKEIRNILLKQQELLTVKKRKQQDQLTERDKFQISLQQND
EKQQGAFISTEETELEHTSTVVEVCEAIASVQAEANTVWTEASQSAEISEEPAEWSSNYF
YPTYDENEEENRPLMRPVSEMALLY
Enzyme 48 Number of Residues 925
Enzyme 48 Molecular Weight 107672.4
Enzyme 48 Theoretical pI 5.87
Enzyme 48 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 48 General Function Involved in protein binding
Enzyme 48 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 48 Pathways Not Available
Enzyme 48 Reactions Not Available
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 153791325 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID P10911 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name MCF2_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 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 48 GenBank Gene ID NM_005369.4 Link Image
Enzyme 48 GeneCard ID MCF2 Link Image
Enzyme 48 GenAtlas ID Not Available
Enzyme 48 HGNC ID Not Available
Enzyme 48 Chromosome Location Not Available
Enzyme 48 Locus Not Available
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 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 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 7137
Enzyme 49 Name Cell division control protein 42 homolog
Enzyme 49 Synonyms
  1. G25K GTP-binding protein
Enzyme 49 Gene Name CDC42
Enzyme 49 Protein Sequence >Cell division control protein 42 homolog
MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAG
QEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLR
DDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQRGLKNVFDEAILAALEPP
ETQPKRKCCIF
Enzyme 49 Number of Residues 191
Enzyme 49 Molecular Weight 21310.4
Enzyme 49 Theoretical pI 5.83
Enzyme 49 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 49 General Function Involved in GTP binding
Enzyme 49 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 49 Pathways Not Available
Enzyme 49 Reactions Not Available
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • None
Enzyme 49 Transmembrane Regions
  • None
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 182857 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID P60953 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name CDC42_HUMAN Link Image
Enzyme 49 PDB ID 1GRN Link Image
Enzyme 49 PDB File Show
Enzyme 49 3D Structure
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >576 bp
ATGCAGACAATTAAGTGTGTTGTTGTGGGCGATGGTGCTGTTGGTAAAACATGTCTCCTG
ATATCCTACACAACAAACAAATTTCCATCGGAATATGTACCGACTGTTTTTGACAACTAT
GCAGTCACAGTTATGATTGGTGGAGAACCATATACTCTTGGACTTTTTGATACTGCAGGG
CAAGAGGATTATGACAGATTACGACCGCTGAGTTATCCACAAACAGATGTATTTCTAGTC
TGTTTTTCAGTGGTCTCTCCATCTTCATTTGAAAACGTGAAAGAAAAGTGGGTGCCTGAG
ATAACTCACCACTGTCCAAAGACTCCTTTCTTGCTTGTTGGGACTCAAATTGATCTCAGA
GATGACCCCTCTACTATTGAGAAACTTGCCAAGAACAAACAGAAGCCTATCACTCCAGAG
ACTGCTGAAAAGCTGGCCCGTGACCTGAAGGCTGTCAAGTATGTGGAGTGTTCTGCACTT
ACACAGAGAGGTCTGAAGAATGTGTTTGATGAGGCTATCCTAGCTGCCCTCGAGCCTCCG
GAAACTCAACCCAAAAGGAAGTGCTGTATATTCTAA
Enzyme 49 GenBank Gene ID M35543 Link Image
Enzyme 49 GeneCard ID CDC42 Link Image
Enzyme 49 GenAtlas ID CDC42 Link Image
Enzyme 49 HGNC ID HGNC:1736 Link Image
Enzyme 49 Chromosome Location 1
Enzyme 49 Locus 1p36.1
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 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 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 7141
Enzyme 50 Name Ras-related C3 botulinum toxin substrate 2
Enzyme 50 Synonyms
  1. GX
  2. Small G protein
  3. p21-Rac2
Enzyme 50 Gene Name RAC2
Enzyme 50 Protein Sequence >Ras-related C3 botulinum toxin substrate 2
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDSKPVNLGLWDTAG
QEDYDRLRPLSYPQTDVFLICFSLVSPASYENVRAKWFPEVRHHCPSTPIILVGTKLDLR
DDKDTIEKLKEKKLAPITYPQGLALAKEIDSVKYLECSALTQRGLKTVFDEAIRAVLCPQ
PTRQQKRACSLL
Enzyme 50 Number of Residues 192
Enzyme 50 Molecular Weight 21428.6
Enzyme 50 Theoretical pI 7.70
Enzyme 50 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 50 General Function Involved in GTP binding
Enzyme 50 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 50 Pathways Not Available
Enzyme 50 Reactions Not Available
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • None
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein Not Available
Enzyme 50 UniProtKB/Swiss-Prot ID P15153 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name RAC2_HUMAN Link Image
Enzyme 50 PDB ID 1DS6 Link Image
Enzyme 50 PDB File Show
Enzyme 50 3D Structure
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence >579 bp
ATGCAGGCCATCAAGTGTGTGGTGGTGGGAGATGGGGCCGTGGGCAAGACCTGCCTTCTC
ATCAGCTACACCACCAACGCCTTTCCCGGAGAGTACATCCCCACCGTGTTTGACAACTAT
TCAGCCAATGTGATGGTGGACAGCAAGCCAGTGAACCTGGGGCTGTGGGACACTGCTGGG
CAGGAGGACTACGACCGTCTCCGGCCGCTCTCCTATCCACAGACGGACGTCTTCCTCATC
TGCTTCTCCCTCGTCAGCCCAGCCTCTTATGAGAACGTCCGCGCCAAGTGGTTCCCAGAA
GTGCGGCACCACTGCCCCAGCACACCCATCATCCTGGTGGGCACCAAGCTGGACCTGCGG
GACGACAAGGACACCATCGAGAAACTGAAGGAGAAGAAGCTGGCTCCCATCACCTACCCG
CAGGGCCTGGCACTGGCCAAGGAGATTGACTCGGTGAAATACCTGGAGTGCTCAGCCCTC
ACCCAGAGAGGCCTGAAAACCGTGTTCGACGAGGCCATCCGGGCCGTGCTGTGCCCTCAG
CCCACGCGGCAGCAGAAGCGCGCCTGCAGCCTCCTCTAG
Enzyme 50 GenBank Gene ID M29871 Link Image
Enzyme 50 GeneCard ID RAC2 Link Image
Enzyme 50 GenAtlas ID RAC2 Link Image
Enzyme 50 HGNC ID HGNC:9802 Link Image
Enzyme 50 Chromosome Location 2
Enzyme 50 Locus 22q13.1
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 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 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 7342
Enzyme 51 Name Vinexin
Enzyme 51 Synonyms
  1. SH3-containing adapter molecule 1
  2. SCAM-1
  3. Sorbin and SH3 domain-containing protein 3
Enzyme 51 Gene Name SORBS3
Enzyme 51 Protein Sequence >Vinexin
MQGPPRSLRAGLSLDDFIPGHLQSHIGSSSRGTRVPVIRNGGSNTLNFQFHDPAPRTVCN
GGYTPRRDASQHPDPAWYQTWPGPGSKPSASTKIPASQHTQNWSATWTKDSKRRDKRWVK
YEGIGPVDESGMPIAPRSSVDRPRDWYRRMFQQIHRKMPDLQLDWTFEEPPRDPRHLGAQ
QRPAHRPGPATSSSGRSWDHSEELPRSTFNYRPGAFSTVLQPSNQVLRRREKVDNVWTEE
SWNQFLQELETGQRPKKPLVDDPGEKPSQPIEVLLERELAELSAELDKDLRAIETRLPSP
KSSPAPRRAPEQRPPAGPASAWSSSYPHAPYLGSARSLSPHKMADGGSPFLGRRDFVYPS
STRDPSASNGGGSPARREEKKRKAARLKFDFQAQSPKELTLQKGDIVYIHKEVDKNWLEG
EHHGRLGIFPANYVEVLPADEIPKPIKPPTYQVLEYGEAVAQYTFKGDLEVELSFRKGEH
ICLIRKVNENWYEGRITGTGRQGIFPASYVQVSREPRLRLCDDGPQLPTSPRLTAAARSA
RHPSSPSALRSPADPTDLGGQTSPRRTGFSFPTQEPRPQTQNLGTPGPALSHSRGPSHPL
DLGTSSPNTSQIHWTPYRAMYQYRPQNEDELELREGDRVDVMQQCDDGWFVGVSRRTQKF
GTFPGNYVAPV
Enzyme 51 Number of Residues 671
Enzyme 51 Molecular Weight 75328.4
Enzyme 51 Theoretical pI 9.87
Enzyme 51 GO Classification Not Available
Enzyme 51 General Function Involved in structural constituent of cytoskeleton
Enzyme 51 Specific Function Vinexin alpha isoform promotes up-regulation of actin stress fiber formation. Vinexin beta isoform plays a role in cell spreading and enhances the activation of JNK/SAPK in response to EGF stimulation by using its third SH3 domain
Enzyme 51 Pathways Not Available
Enzyme 51 Reactions Not Available
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • None
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 155030230 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID O60504 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name VINEX_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence >2016 bp
ATGCAGGGCCCACCCCGCAGCCTCCGCGCTGGGCTCAGCCTGGACGACTTCATCCCTGGC
CACCTCCAGTCCCACATAGGGTCTTCCTCCCGGGGGACACGGGTGCCCGTGATCCGGAAT
GGTGGCTCCAACACCCTTAATTTCCAGTTCCACGACCCCGCGCCCAGGACTGTGTGCAAT
GGGGGCTACACACCAAGACGAGATGCTTCCCAGCACCCGGACCCTGCGTGGTATCAGACC
TGGCCAGGCCCTGGGAGCAAGCCCTCTGCAAGCACAAAGATCCCTGCCTCCCAGCACACC
CAGAACTGGTCAGCCACGTGGACCAAGGACAGCAAGCGTCGGGACAAGCGCTGGGTCAAG
TACGAGGGAATCGGGCCCGTGGACGAGAGCGGCATGCCCATTGCCCCCCGATCCAGCGTT
GACAGACCCAGAGACTGGTACCGGAGAATGTTCCAGCAGATTCACCGGAAAATGCCAGAC
TTGCAGCTGGACTGGACCTTCGAGGAGCCACCCAGAGACCCCAGGCATCTAGGAGCCCAG
CAAAGACCTGCCCACAGGCCCGGCCCGGCAACATCTTCCAGTGGAAGAAGCTGGGACCAC
TCTGAAGAGTTACCTAGAAGCACCTTCAACTACAGACCTGGAGCATTCTCCACTGTGCTG
CAGCCCTCAAATCAGGTGCTCAGACGCCGGGAAAAAGTAGACAATGTCTGGACGGAAGAG
TCCTGGAACCAGTTTCTGCAGGAACTAGAGACTGGGCAGAGGCCCAAGAAACCGCTGGTG
GACGACCCTGGTGAGAAGCCCTCCCAGCCCATTGAGGTGCTGCTGGAGAGAGAGCTGGCC
GAGCTGAGCGCCGAGCTGGACAAGGACCTGCGGGCAATTGAGACCCGACTGCCGTCCCCC
AAGAGCTCGCCGGCGCCCCGACGGGCCCCGGAGCAGCGGCCCCCGGCCGGCCCGGCCTCA
GCCTGGAGCTCCAGCTACCCACATGCACCTTACCTGGGTTCCGCCCGGTCCCTGAGTCCC
CACAAAATGGCTGATGGAGGAAGCCCCTTCCTAGGTCGGAGGGACTTTGTCTACCCTTCC
TCAACCCGAGACCCTAGTGCCTCTAACGGAGGGGGCAGCCCAGCCAGGAGGGAAGAGAAG
AAGAGAAAGGCCGCCAGGCTCAAGTTTGACTTCCAGGCGCAGTCCCCCAAGGAGCTGACT
CTGCAGAAGGGTGACATTGTCTACATCCACAAGGAGGTGGACAAGAACTGGCTGGAGGGA
GAGCACCACGGCCGCCTGGGCATCTTCCCTGCTAATTATGTGGAGGTGCTGCCCGCAGAT
GAGATCCCTAAGCCCATCAAGCCCCCGACCTACCAGGTGCTGGAGTATGGAGAGGCTGTG
GCCCAGTACACCTTCAAGGGGGACCTGGAGGTGGAGCTGTCCTTCCGCAAGGGAGAGCAC
ATCTGCCTGATCCGCAAGGTGAACGAGAACTGGTACGAGGGACGCATCACGGGCACGGGG
CGCCAAGGCATATTCCCTGCCAGCTACGTGCAGGTGTCTCGTGAACCCCGGCTCCGGCTC
TGTGACGACGGCCCCCAGCTCCCCACGTCTCCCCGCCTGACCGCTGCCGCCCGCTCAGCC
CGTCACCCCAGCTCCCCCTCAGCCCTGCGCAGCCCAGCTGACCCCATCGACTTGGGGGGA
CAGACCTCCCCCCGTCGCACTGGCTTCTCCTTCCCCACCCAGGAGCCTAGACCCCAGACC
CAGAATCTTGGCACCCCTGGTCCAGCTCTGTCCCACTCTCGAGGTCCCAGCCATCCCCTG
GACCTGGGGACCTCCTCTCCTAACACCTCTCAGATACACTGGACCCCGTACCGGGCGATG
TACCAGTACAGGCCCCAGAACGAAGACGAGCTGGAGCTGCGCGAGGGGGACAGGGTGGAT
GTCATGCAGCAGTGTGACGATGGCTGGTTTGTGGGTGTCTCCCGGAGGACCCAGAAATTC
GGAACGTTCCCTGGAAATTACGTTGCCCCGGTGTGA
Enzyme 51 GenBank Gene ID NM_005775.4 Link Image
Enzyme 51 GeneCard ID SORBS3 Link Image
Enzyme 51 GenAtlas ID SORBS3 Link Image
Enzyme 51 HGNC ID HGNC:30907 Link Image
Enzyme 51 Chromosome Location 8
Enzyme 51 Locus 8p21.3
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 General References
  1. Kioka N, Sakata S, Kawauchi T, Amachi T, Akiyama SK, Okazaki K, Yaen C, Yamada KM, Aota S: Vinexin: a novel vinculin-binding protein with multiple SH3 domains enhances actin cytoskeletal organization. J Cell Biol. 1999 Jan 11;144(1):59-69. [PubMed Link Image]
  2. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Akamatsu M, Aota S, Suwa A, Ueda K, Amachi T, Yamada KM, Akiyama SK, Kioka N: Vinexin forms a signaling complex with Sos and modulates epidermal growth factor-induced c-Jun N-terminal kinase/stress-activated protein kinase activities. J Biol Chem. 1999 Dec 10;274(50):35933-7. [PubMed Link Image]
  5. Townson SM, Dobrzycka KM, Lee AV, Air M, Deng W, Kang K, Jiang S, Kioka N, Michaelis K, Oesterreich S: SAFB2, a new scaffold attachment factor homolog and estrogen receptor corepressor. J Biol Chem. 2003 May 30;278(22):20059-68. Epub 2003 Mar 26. [PubMed Link Image]
  6. Martens N, Wery M, Wang P, Braet F, Gertler A, Hooghe R, Vandenhaute J, Hooghe-Peters EL: The suppressor of cytokine signaling (SOCS)-7 interacts with the actin cytoskeleton through vinexin. Exp Cell Res. 2004 Aug 1;298(1):239-48. [PubMed Link Image]
  7. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  8. Paternotte N, Zhang J, Vandenbroere I, Backers K, Blero D, Kioka N, Vanderwinden JM, Pirson I, Erneux C: SHIP2 interaction with the cytoskeletal protein Vinexin. FEBS J. 2005 Dec;272(23):6052-66. [PubMed Link Image]
  9. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  10. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  11. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  12. Ito H, Atsuzawa K, Sudo K, Di Stefano P, Iwamoto I, Morishita R, Takei S, Semba R, Defilippi P, Asano T, Usuda N, Nagata K: Characterization of a multidomain adaptor protein, p140Cap, as part of a pre-synaptic complex. J Neurochem. 2008 Oct;107(1):61-72. Epub 2008 Jul 24. [PubMed Link Image]
  13. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  14. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  15. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  16. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  17. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  18. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 7383
Enzyme 52 Name GTPase HRas
Enzyme 52 Synonyms
  1. H-Ras-1
  2. Ha-Ras
  3. Transforming protein p21
  4. c-H-ras
  5. p21ras
  6. GTPase HRas, N-terminally processed
Enzyme 52 Gene Name HRAS
Enzyme 52 Protein Sequence >GTPase HRas
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG
QEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL
AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPG
CMSCKCVLS
Enzyme 52 Number of Residues 189
Enzyme 52 Molecular Weight 21298.0
Enzyme 52 Theoretical pI 4.94
Enzyme 52 GO Classification
Function
  • GTP binding
  • GTPase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • nucleoside-triphosphatase activity
  • nucleotide binding
  • purine nucleotide binding
  • pyrophosphatase activity
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
  • membrane
Enzyme 52 General Function Involved in GTP binding
Enzyme 52 Specific Function Ras proteins bind GDP/GTP and possess intrinsic GTPase activity
Enzyme 52 Pathways Not Available
Enzyme 52 Reactions Not Available
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • None
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein 20147725 Link Image
Enzyme 52 UniProtKB/Swiss-Prot ID P01112 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name RASH_HUMAN Link Image
Enzyme 52 PDB ID 4Q21 Link Image
Enzyme 52 PDB File Show
Enzyme 52 3D Structure
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence >570 bp
ATGACGGAATATAAGCTGGTGGTGGTGGGCGCCGGCGGTGTGGGCAAGAGTGCGCTGACC
ATCCAGCTGATCCAGAACCATTTTGTGGACGAATACGACCCCACTATAGAGGATTCCTAC
CGGAAGCAGGTGGTCATTGATGGGGAGACGTGCCTGTTGGACATCCTGGATACCGCCGGC
CAGGAGGAGTACAGCGCCATGCGGGACCAGTACATGCGCACCGGGGAGGGCTTCCTGTGT
GTGTTTGCCATCAACAACACCAAGTCTTTTGAGGACATCCACCAGTACAGGGAGCAGATC
AAACGGGTGAAGGACTCGGATGACGTGCCCATGGTGCTGGTGGGGAACAAGTGTGACCTG
GCTGCACGCACTGTGGAATCTCGGCAGGCTCAGGACCTCGCCCGAAGCTACGGCATCCCC
TACATCGAGACCTCGGCCAAGACCCGGCAGGGAGTGGAGGATGCCTTCTACACGTTGGTG
CGTGAGATCCGGCAGCACAAGCTGCGGAAGCTGAACCCTCCTGATGAGAGTGGCCCCGGC
TGCATGAGCTGCAAGTGTGTGCTCTCCTGA
Enzyme 52 GenBank Gene ID AF493916 Link Image
Enzyme 52 GeneCard ID HRAS Link Image
Enzyme 52 GenAtlas ID HRAS Link Image
Enzyme 52 HGNC ID HGNC:5173 Link Image
Enzyme 52 Chromosome Location 1
Enzyme 52 Locus 11p15.5
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 General References
  1. Capon DJ, Chen EY, Levinson AD, Seeburg PH, Goeddel DV: Complete nucleotide sequences of the T24 human bladder carcinoma oncogene and its normal homologue. Nature. 1983 Mar 3;302(5903):33-7. [PubMed Link Image]
  2. Reddy EP: Nucleotide sequence analysis of the T24 human bladder carcinoma oncogene. Science. 1983 Jun 3;220(4601):1061-3. [PubMed Link Image]
  3. Sekiya T, Fushimi M, Hori H, Hirohashi S, Nishimura S, Sugimura T: Molecular cloning and the total nucleotide sequence of the human c-Ha-ras-1 gene activated in a melanoma from a Japanese patient. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4771-5. [PubMed Link Image]
  4. Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Tabin CJ, Bradley SM, Bargmann CI, Weinberg RA, Papageorge AG, Scolnick EM, Dhar R, Lowy DR, Chang EH: Mechanism of activation of a human oncogene. Nature. 1982 Nov 11;300(5888):143-9. [PubMed Link Image]
  7. Honkawa H, Masahashi W, Hashimoto S, Hashimoto-Gotoh T: Identification of the principal promoter sequence of the c-H-ras transforming oncogene: deletion analysis of the 5'-flanking region by focus formation assay. Mol Cell Biol. 1987 Aug;7(8):2933-40. [PubMed Link Image]
  8. Low A, Sprinzl M, Faulhammer HG: Affinity labeling of c-H-ras p21 consensus elements with periodate-oxidized GDP and GTP. Eur J Biochem. 1993 Jul 15;215(2):473-9. [PubMed Link Image]
  9. Feig LA, Pan BT, Roberts TM, Cooper GM: Isolation of ras GTP-binding mutants using an in situ colony-binding assay. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4607-11. [PubMed Link Image]
  10. Lacal JC, Anderson PS, Aaronson SA: Deletion mutants of Harvey ras p21 protein reveal the absolute requirement of at least two distant regions for GTP-binding and transforming activities. EMBO J. 1986 Apr;5(4):679-87. [PubMed Link Image]
  11. Hancock JF, Magee AI, Childs JE, Marshall CJ: All ras proteins are polyisoprenylated but only some are palmitoylated. Cell. 1989 Jun 30;57(7):1167-77. [PubMed Link Image]
  12. Dudler T, Gelb MH: Palmitoylation of Ha-Ras facilitates membrane binding, activation of downstream effectors, and meiotic maturation in Xenopus oocytes. J Biol Chem. 1996 May 10;271(19):11541-7. [PubMed Link Image]
  13. Lander HM, Hajjar DP, Hempstead BL, Mirza UA, Chait BT, Campbell S, Quilliam LA: A molecular redox switch on p21(ras). Structural basis for the nitric oxide-p21(ras) interaction. J Biol Chem. 1997 Feb 14;272(7):4323-6. [PubMed Link Image]
  14. Song C, Hu CD, Masago M, Kariyai K, Yamawaki-Kataoka Y, Shibatohge M, Wu D, Satoh T, Kataoka T: Regulation of a novel human phospholipase C, PLCepsilon, through membrane targeting by Ras. J Biol Chem. 2001 Jan 26;276(4):2752-7. Epub 2000 Oct 5. [PubMed Link Image]
  15. Topham MK, Prescott SM: Diacylglycerol kinase zeta regulates Ras activation by a novel mechanism. J Cell Biol. 2001 Mar 19;152(6):1135-43. [PubMed Link Image]
  16. Swarthout JT, Lobo S, Farh L, Croke MR, Greentree WK, Deschenes RJ, Linder ME: DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H- and N-Ras. J Biol Chem. 2005 Sep 2;280(35):31141-8. Epub 2005 Jul 6. [PubMed Link Image]
  17. Rocks O, Peyker A, Kahms M, Verveer PJ, Koerner C, Lumbierres M, Kuhlmann J, Waldmann H, Wittinghofer A, Bastiaens PI: An acylation cycle regulates localization and activity of palmitoylated Ras isoforms. Science. 2005 Mar 18;307(5716):1746-52. Epub 2005 Feb 10. [PubMed Link Image]
  18. Pan F, Sun L, Kardian DB, Whartenby KA, Pardoll DM, Liu JO: Feedback inhibition of calcineurin and Ras by a dual inhibitory protein Carabin. Nature. 2007 Jan 25;445(7126):433-6. Epub 2007 Jan 17. [PubMed Link Image]
  19. de Vos AM, Tong L, Milburn MV, Matias PM, Jancarik J, Noguchi S, Nishimura S, Miura K, Ohtsuka E, Kim SH: Three-dimensional structure of an oncogene protein: catalytic domain of human c-H-ras p21. Science. 1988 Feb 19;239(4842):888-93. [PubMed Link Image]
  20. Pai EF, Kabsch W, Krengel U, Holmes KC, John J, Wittinghofer A: Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. Nature. 1989 Sep 21;341(6239):209-14. [PubMed Link Image]
  21. Pai EF, Krengel U, Petsko GA, Goody RS, Kabsch W, Wittinghofer A: Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 1990 Aug;9(8):2351-9. [PubMed Link Image]
  22. Tong LA, de Vos AM, Milburn MV, Kim SH: Crystal structures at 2.2 A resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP. J Mol Biol. 1991 Feb 5;217(3):503-16. [PubMed Link Image]
  23. Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED: Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy. Biochemistry. 1994 Mar 29;33(12):3515-31. [PubMed Link Image]
  24. Scheffzek K, Ahmadian MR, Kabsch W, Wiesmuller L, Lautwein A, Schmitz F, Wittinghofer A: The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science. 1997 Jul 18;277(5324):333-8. [PubMed Link Image]
  25. Scheidig AJ, Burmester C, Goody RS: The pre-hydrolysis state of p21(ras) in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins. Structure. 1999 Nov 15;7(11):1311-24. [PubMed Link Image]
  26. Hall BE, Bar-Sagi D, Nassar N: The structural basis for the transition from Ras-GTP to Ras-GDP. Proc Natl Acad Sci U S A. 2002 Sep 17;99(19):12138-42. Epub 2002 Sep 4. [PubMed Link Image]
  27. Williams JG, Pappu K, Campbell SL: Structural and biochemical studies of p21Ras S-nitrosylation and nitric oxide-mediated guanine nucleotide exchange. Proc Natl Acad Sci U S A. 2003 May 27;100(11):6376-81. Epub 2003 May 9. [PubMed Link Image]
  28. Buhrman G, Wink G, Mattos C: Transformation efficiency of RasQ61 mutants linked to structural features of the switch regions in the presence of Raf. Structure. 2007 Dec;15(12):1618-29. [PubMed Link Image]
  29. Stieglitz B, Bee C, Schwarz D, Yildiz O, Moshnikova A, Khokhlatchev A, Herrmann C: Novel type of Ras effector interaction established between tumour suppressor NORE1A and Ras switch II. EMBO J. 2008 Jul 23;27(14):1995-2005. Epub 2008 Jul 3. [PubMed Link Image]
  30. Sakai E, Rikimaru K, Ueda M, Matsumoto Y, Ishii N, Enomoto S, Yamamoto H, Tsuchida N: The p53 tumor-suppressor gene and ras oncogene mutations in oral squamous-cell carcinoma. Int J Cancer. 1992 Dec 2;52(6):867-72. [PubMed Link Image]
  31. Nikiforova MN, Lynch RA, Biddinger PW, Alexander EK, Dorn GW 2nd, Tallini G, Kroll TG, Nikiforov YE: RAS point mutations and PAX8-PPAR gamma rearrangement in thyroid tumors: evidence for distinct molecular pathways in thyroid follicular carcinoma. J Clin Endocrinol Metab. 2003 May;88(5):2318-26. [PubMed Link Image]
  32. Aoki Y, Niihori T, Kawame H, Kurosawa K, Ohashi H, Tanaka Y, Filocamo M, Kato K, Suzuki Y, Kure S, Matsubara Y: Germline mutations in HRAS proto-oncogene cause Costello syndrome. Nat Genet. 2005 Oct;37(10):1038-40. Epub 2005 Sep 18. [PubMed Link Image]
  33. Gripp KW, Lin AE, Stabley DL, Nicholson L, Scott CI Jr, Doyle D, Aoki Y, Matsubara Y, Zackai EH, Lapunzina P, Gonzalez-Meneses A, Holbrook J, Agresta CA, Gonzalez IL, Sol-Church K: HRAS mutation analysis in Costello syndrome: genotype and phenotype correlation. Am J Med Genet A. 2006 Jan 1;140(1):1-7. [PubMed Link Image]
  34. Kerr B, Delrue MA, Sigaudy S, Perveen R, Marche M, Burgelin I, Stef M, Tang B, Eden OB, O'Sullivan J, De Sandre-Giovannoli A, Reardon W, Brewer C, Bennett C, Quarell O, M'Cann E, Donnai D, Stewart F, Hennekam R, Cave H, Verloes A, Philip N, Lacombe D, Levy N, Arveiler B, Black G: Genotype-phenotype correlation in Costello syndrome: HRAS mutation analysis in 43 cases. J Med Genet. 2006 May;43(5):401-5. Epub 2006 Jan 27. [PubMed Link Image]
  35. Zampino G, Pantaleoni F, Carta C, Cobellis G, Vasta I, Neri C, Pogna EA, De Feo E, Delogu A, Sarkozy A, Atzeri F, Selicorni A, Rauen KA, Cytrynbaum CS, Weksberg R, Dallapiccola B, Ballabio A, Gelb BD, Neri G, Tartaglia M: Diversity, parental germline origin, and phenotypic spectrum of de novo HRAS missense changes in Costello syndrome. Hum Mutat. 2007 Mar;28(3):265-72. [PubMed Link Image]
  36. van der Burgt I, Kupsky W, Stassou S, Nadroo A, Barroso C, Diem A, Kratz CP, Dvorsky R, Ahmadian MR, Zenker M: Myopathy caused by HRAS germline mutations: implications for disturbed myogenic differentiation in the presence of constitutive HRas activation. J Med Genet. 2007 Jul;44(7):459-62. Epub 2007 Apr 5. [PubMed Link Image]
  37. Gripp KW, Innes AM, Axelrad ME, Gillan TL, Parboosingh JS, Davies C, Leonard NJ, Lapointe M, Doyle D, Catalano S, Nicholson L, Stabley DL, Sol-Church K: Costello syndrome associated with novel germline HRAS mutations: an attenuated phenotype? Am J Med Genet A. 2008 Mar 15;146A(6):683-90. [PubMed Link Image]
Enzyme 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 7391
Enzyme 53 Name Rho-related GTP-binding protein RhoQ
Enzyme 53 Synonyms
  1. Ras-like protein TC10
  2. Ras-like protein family member 7A
Enzyme 53 Gene Name RHOQ
Enzyme 53 Protein Sequence >Rho-related GTP-binding protein RhoQ
MAHGPGALMLKCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVSVTVGGKQYLLG
LYDTAGQEDYDRLRPLSYPMTDVFLICFSVVNPASFQNVKEEWVPELKEYAPNVPFLLIG
TQIDLRDDPKTLARLNDMKEKPICVEQGQKLAKEIGACCYVECSALTQKGLKTVFDEAII
AILTPKKHTVKKRIGSRCINCCLIT
Enzyme 53 Number of Residues 205
Enzyme 53 Molecular Weight 22659.3
Enzyme 53 Theoretical pI 6.25
Enzyme 53 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 53 General Function Involved in GTP binding
Enzyme 53 Specific Function Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. May play a role in CFTR trafficking to the plasma membrane. Causes the formation of thin, actin-rich surface projections called filopodia
Enzyme 53 Pathways Not Available
Enzyme 53 Reactions Not Available
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • None
Enzyme 53 Transmembrane Regions
  • None
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein 62822285 Link Image
Enzyme 53 UniProtKB/Swiss-Prot ID P17081 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name RHOQ_HUMAN Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence >618 bp
ATGGCTCACGGGCCCGGCGCGCTGATGCTCAAGTGCGTGGTGGTCGGCGACGGGGCGGTG
GGCAAGACGTGCCTACTCATGAGCTATGCCAACGACGCCTTCCCGGAGGAGTACGTGCCC
ACCGTCTTCGACCACTACGCAGTCAGCGTCACCGTGGGGGGCAAGCAGTACCTCCTAGGA
CTCTATGACACGGCCGGACAGGAAGACTATGACCGTCTGAGGCCTTTATCTTACCCAATG
ACCGATGTCTTCCTTATATGCTTCTCGGTGGTAAATCCAGCCTCATTTCAAAATGTGAAA
GAGGAGTGGGTACCGGAACTTAAGGAATACGCACCAAATGTACCCTTTTTATTAATAGGA
ACTCAGATTGATCTCCGAGATGACCCCAAAACTTTAGCAAGACTGAATGATATGAAAGAA
AAACCTATATGTGTGGAACAAGGACAGAAACTAGCAAAAGAGATAGGAGCATGCTGCTAT
GTGGAATGTTCAGCTTTAACCCAGAAGGGATTGAAGACTGTTTTTGATGAGGCTATCATA
GCCATTTTAACTCCAAAGAAACACACTGTAAAAAAAAGAATAGGATCAAGATGTATAAAC
TGTTGTTTAATTACGTGA
Enzyme 53 GenBank Gene ID AC018682 Link Image
Enzyme 53 GeneCard ID RHOQ Link Image
Enzyme 53 GenAtlas ID RHOQ Link Image
Enzyme 53 HGNC ID HGNC:17736 Link Image
Enzyme 53 Chromosome Location 2
Enzyme 53 Locus 2p21
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 General References
  1. Drivas GT, Shih A, Coutavas E, Rush MG, D'Eustachio P: Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line. Mol Cell Biol. 1990 Apr;10(4):1793-8. [PubMed Link Image]
  2. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Joberty G, Perlungher RR, Macara IG: The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins. Mol Cell Biol. 1999 Oct;19(10):6585-97. [PubMed Link Image]
  5. Joberty G, Petersen C, Gao L, Macara IG: The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42. Nat Cell Biol. 2000 Aug;2(8):531-9. [PubMed Link Image]
  6. Neudauer CL, Joberty G, Macara IG: PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10. Biochem Biophys Res Commun. 2001 Jan 19;280(2):541-7. [PubMed Link Image]
  7. Cheng J, Wang H, Guggino WB: Regulation of cystic fibrosis transmembrane regulator trafficking and protein expression by a Rho family small GTPase TC10. J Biol Chem. 2005 Feb 4;280(5):3731-9. Epub 2004 Nov 15. [PubMed Link Image]
Enzyme 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 7480
Enzyme 54 Name Guanine nucleotide-binding protein G(q) subunit alpha
Enzyme 54 Synonyms
  1. Guanine nucleotide-binding protein alpha-q
Enzyme 54 Gene Name GNAQ
Enzyme 54 Protein Sequence >Guanine nucleotide-binding protein G(q) subunit alpha
MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMR
IIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEK
VSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPAYLPTQQDVL
RVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLV
ESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQR
DAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
Enzyme 54 Number of Residues 359
Enzyme 54 Molecular Weight 42141.7
Enzyme 54 Theoretical pI 5.37
Enzyme 54 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • molecular transducer activity
  • nucleotide binding
  • purine nucleotide binding
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • biological regulation
  • cell surface receptor linked signaling pathway
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • post-translational protein modification
  • protein amino acid ADP-ribosylation
  • protein modification process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 54 General Function Involved in signal transducer activity
Enzyme 54 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems
Enzyme 54 Pathways Not Available
Enzyme 54 Reactions Not Available
Enzyme 54 Pfam Domain Function
Enzyme 54 Signals
  • None
Enzyme 54 Transmembrane Regions
  • None
Enzyme 54 Essentiality Not Available
Enzyme 54 GenBank ID Protein 1181671 Link Image
Enzyme 54 UniProtKB/Swiss-Prot ID P50148 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name GNAQ_HUMAN Link Image
Enzyme 54 PDB ID Not Available
Enzyme 54 Cellular Location Not Available
Enzyme 54 Gene Sequence >1080 bp
ATGACTCTGGAGTCCATCATGGCGTGCTGCCTGAGCGAGGAGGCCAAGGAAGCCCGGCGG
ATCAACGACGAGATCGAGCGGCACGTCCGCAGGGACAAGCGGGACGCCCGCCGGGAGCTC
AAGCTGCTGCTGCTCGGGACAGGAGAGAGTGGCAAGAGTACGTTTATCAAGCAGATGAGA
ATCATCCATGGGTCAGGATACTCTGATGAAGATAAAAGGGGCTTCACCAAGCTGGTGTAT
CAGAACATCTTCACGGCCATGCAGGCCATGATCAGAGCCATGGACACACTCAAGATCCCA
TACAAGTATGAGCACAATAAGGCTCATGCACAATTAGTTCGAGAAGTTGATGTGGAGAAG
GTGTCTGCTTTTGAGAATCCATATGTAGATGCAATAAAGAGTTTATGGAATGATCCTGGA
ATCCAGGAATGCTATGATAGACGACGAGAATATCAATTATCTGACTCTACCAAATACTAT
CTTAATGACTTGGACCGCGTAGCTGACCCTGCCTACCTGCCTACGCAACAAGATGTGCTT
AGAGTTCGAGTCCCCACCACAGGGATCATCGAATACCCCTTTGACTTACAAAGTGTCATT
TTCAGAATGGTCGATGTAGGGGGCCAAAGGTCAGAGAGAAGAAAATGGATACACTGCTTT
GAAAATGTCACCTCTATCATGTTTCTAGTAGCGCTTAGTGAATATGATCAAGTTCTCGTG
GAGTCAGACAATGAGAACCGAATGGAGGAAAGCAAGGCTCTCTTTAGAACAATTATCACA
TACCCCTGGTTCCAGAACTCCTCGGTTATTCTGTTCTTAAACAAGAAAGATCTTCTAGAG
GAGAAAATCATGTATTCCCATCTAGTCGACTACTTCCCAGAATATGATGGACCCCAGAGA
GATGCCCAGGCAGCCCGAGAATTCATTCTGAAGATGTTCGTGGACCTGAACCCAGACAGT
GACAAAATTATCTACTCCCACTTCACGTGCGCCACAGACACCGAGAATATCCGCTTTGTC
TTTGCTGCCGTCAAGGACACCATCCTCCAGTTGAACCTGAAGGAGTACAATCTGGTCTAA
Enzyme 54 GenBank Gene ID U40038 Link Image
Enzyme 54 GeneCard ID GNAQ Link Image
Enzyme 54 GenAtlas ID GNAQ Link Image
Enzyme 54 HGNC ID HGNC:4390 Link Image
Enzyme 54 Chromosome Location 9
Enzyme 54 Locus 9q21
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 General References
  1. Dong Q, Shenker A, Way J, Haddad BR, Lin K, Hughes MR, McBride OW, Spiegel AM, Battey J: Molecular cloning of human G alpha q cDNA and chromosomal localization of the G alpha q gene (GNAQ) and a processed pseudogene. Genomics. 1995 Dec 10;30(3):470-75. [PubMed Link Image]
  2. Chen B, Leverette RD, Schwinn DA, Kwatra MM: Human G(alpha q): cDNA and tissue distribution. Biochim Biophys Acta. 1996 Jun 11;1281(2):125-8. [PubMed Link Image]
  3. Johnson GJ, Leis LA, Dunlop PC: Specificity of G alpha q and G alpha 11 gene expression in platelets and erythrocytes. Expressions of cellular differentiation and species differences. Biochem J. 1996 Sep 15;318 ( Pt 3):1023-31. [PubMed Link Image]
  4. Gabbeta J, Dhanasekaran N, Rao AK: G alpha q cDNA sequence from human platelets. Thromb Res. 1998 Jul 1;91(1):29-32. [PubMed Link Image]
  5. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Lesch KP, Manji HK: Signal-transducing G proteins and antidepressant drugs: evidence for modulation of alpha subunit gene expression in rat brain. Biol Psychiatry. 1992 Oct 1;32(7):549-79. [PubMed Link Image]
  8. Thomas CP, Dunn MJ, Mattera R: Ca2+ signalling in K562 human erythroleukaemia cells: effect of dimethyl sulphoxide and role of G-proteins in thrombin- and thromboxane A2-activated pathways. Biochem J. 1995 Nov 15;312 ( Pt 1):151-8. [PubMed Link Image]
  9. Rochdi MD, Watier V, La Madeleine C, Nakata H, Kozasa T, Parent JL: Regulation of GTP-binding protein alpha q (Galpha q) signaling by the ezrin-radixin-moesin-binding phosphoprotein-50 (EBP50). J Biol Chem. 2002 Oct 25;277(43):40751-9. Epub 2002 Aug 21. [PubMed Link Image]
  10. Yeh JC, Otte LA, Frangos JA: Regulation of G protein-coupled receptor activities by the platelet-endothelial cell adhesion molecule, PECAM-1. Biochemistry. 2008 Aug 26;47(34):9029-39. Epub 2008 Aug 2. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 7482
Enzyme 55 Name Guanine nucleotide-binding protein subunit alpha-11
Enzyme 55 Synonyms
  1. G alpha-11
  2. G-protein subunit alpha-11
  3. Guanine nucleotide-binding protein G(y) subunit alpha
Enzyme 55 Gene Name GNA11
Enzyme 55 Protein Sequence >Guanine nucleotide-binding protein subunit alpha-11
MTLESMMACCLSDEVKESKRINAEIEKQLRRDKRDARRELKLLLLGTGESGKSTFIKQMR
IIHGAGYSEEDKRGFTKLVYQNIFTAMQAMIRAMETLKILYKYEQNKANALLIREVDVEK
VTTFEHQYVSAIKTLWEDPGIQECYDRRREYQLSDSAKYYLTDVDRIATLGYLPTQQDVL
RVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLV
ESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEDKILYSHLVDYFPEFDGPQR
DAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
Enzyme 55 Number of Residues 359
Enzyme 55 Molecular Weight 42122.9
Enzyme 55 Theoretical pI 5.38
Enzyme 55 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • molecular transducer activity
  • nucleotide binding
  • purine nucleotide binding
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • biological regulation
  • cell surface receptor linked signaling pathway
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • post-translational protein modification
  • protein amino acid ADP-ribosylation
  • protein modification process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
Enzyme 55 General Function Involved in signal transducer activity
Enzyme 55 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C
Enzyme 55 Pathways Not Available
Enzyme 55 Reactions Not Available
Enzyme 55 Pfam Domain Function
Enzyme 55 Signals
  • None
Enzyme 55 Transmembrane Regions
  • None
Enzyme 55 Essentiality Not Available
Enzyme 55 GenBank ID Protein 3289982 Link Image
Enzyme 55 UniProtKB/Swiss-Prot ID P29992 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name GNA11_HUMAN Link Image
Enzyme 55 PDB ID Not Available
Enzyme 55 Cellular Location Not Available
Enzyme 55 Gene Sequence >1080 bp
ATGACTCTGGAGTCCATGATGGCGTGTTGCCTGAGCGATGAGGTGAAGGAGTCCAAGCGG
ATCAACGCCGAGATCGAGAAGCAGCTGCGGCGGGACAAGCGCGACGCCCGGCGCGAGCTC
AAGCTGCTGCTGCTCGGCACGGGCGAGAGCGGGAAGAGCACGTTCATCAAGCAGATGCGC
ATCATCCACGGCGCCGGCTACTCGGAGGAGGACAAGCGCGGCTTCACCAAGCTCGTCTAC
CAGAACATCTTCACCGCCATGCAGGCCATGATCCGGGCCATGGAGACGCTCAAGATCCTC
TACAAGTACGAGCAGAACAAGGCCAATGCGCTCCTGATCCGGGAGGTGGACGTGGAGAAG
GTGACCACCTTCGAGCATCAGTACGTCAGTGCCATCAAGACCCTGTGGGAGGACCCGGGC
ATCCAGGAATGCTACGACCGCAGGCGCGAGTACCAGCTCTCCGACTCTGCCAAGTACTAC
CTGACCGACGTTGACCGCATCGCCACCTTGGGCTACCTGCCCACCCAGCAGGACGTGCTG
CGGGTCCGCGTGCCCACCACCGGCATCATCGAGTACCCTTTCGACCTGGAGAACATCATC
TTCCGGATGGTGGATGTGGGGGGCCAGCGGTCGGAGCGGAGGAAGTGGATCCACTGCTTT
GAGAACGTGACATCCATCATGTTTCTCGTCGCCCTCAGCGAATACGACCAAGTCCTGGTG
GAGTCGGACAACGAGAACCGGATGGAGGAGAGCAAAGCCCTGTTCCGGACCATCATCACC
TACCCCTGGTTCCAGAACTCCTCCGTCATCCTCTTCCTCAACAAGAAGGACCTGCTGGAG
GACAAGATCCTGTACTCGCACCTGGTGGACTACTTCCCCGAGTTCGATGGTCCCCAGCGG
GACGCCCAGGCGGCGCGGGAGTTCATCCTGAAGATGTTCGTGGACCTGAACCCCGACAGC
GACAAGATCATCTACTCACACTTCACGTGTGCCACCGACACGGAGAACATCCGCTTCGTG
TTCGCGGCCGTGAAGGACACCATCCTGCAGCTCAACCTCAAGGAGTACAACCTGGTCTGA
Enzyme 55 GenBank Gene ID AC005262 Link Image
Enzyme 55 GeneCard ID GNA11 Link Image
Enzyme 55 GenAtlas ID GNA11 Link Image
Enzyme 55 HGNC ID HGNC:4379 Link Image
Enzyme 55 Chromosome Location 1
Enzyme 55 Locus 19p13.3
Enzyme 55 SNPs SNPJam Report Link Image
Enzyme 55 General References
  1. Jiang M, Pandey S, Tran VT, Fong HK: Guanine nucleotide-binding regulatory proteins in retinal pigment epithelial cells. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3907-11. [PubMed Link Image]
  2. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Thomas CP, Dunn MJ, Mattera R: Ca2+ signalling in K562 human erythroleukaemia cells: effect of dimethyl sulphoxide and role of G-proteins in thrombin- and thromboxane A2-activated pathways. Biochem J. 1995 Nov 15;312 ( Pt 1):151-8. [PubMed Link Image]
Enzyme 55 Metabolite References Not Available
Enzyme 56 [top]
Enzyme 56 ID 7684
Enzyme 56 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-11
Enzyme 56 Synonyms Not Available
Enzyme 56 Gene Name GNG11
Enzyme 56 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-11
MPALHIEDLPEKEKLKMEVEQLRKEVKLQRQQVSKCSEEIKNYIEERSGEDPLVKGIPED
KNPFKEKGSCVIS
Enzyme 56 Number of Residues 73
Enzyme 56 Molecular Weight 8480.7
Enzyme 56 Theoretical pI 5.23
Enzyme 56 GO Classification
Function
  • molecular transducer activity
  • signal transducer activity
Process
  • G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • signaling
  • signaling pathway
Component
  • cell part
  • extrinsic to membrane
  • extrinsic to plasma membrane
  • heterotrimeric G-protein complex
  • membrane part
Enzyme 56 General Function Involved in signal transducer activity
Enzyme 56 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Enzyme 56 Pathways Not Available
Enzyme 56 Reactions Not Available
Enzyme 56 Pfam Domain Function
Enzyme 56 Signals
  • None
Enzyme 56 Transmembrane Regions
  • None
Enzyme 56 Essentiality Not Available
Enzyme 56 GenBank ID Protein 41393495 Link Image
Enzyme 56 UniProtKB/Swiss-Prot ID P61952 Link Image
Enzyme 56 UniProtKB/Swiss-Prot Entry Name GBG11_HUMAN Link Image
Enzyme 56 PDB ID Not Available
Enzyme 56 Cellular Location Not Available
Enzyme 56 Gene Sequence >222 bp
ATGCCTGCCCTTCACATCGAAGATTTGCCAGAGAAGGAAAAACTGAAAATGGAAGTTGAG
CAGCTTCGCAAAGAAGTGAAGTTGCAGAGACAACAAGTGTCTAAATGTTCTGAAGAAATA
AAGAACTATATTGAAGAACGTTCTGGAGAGGATCCTCTAGTAAAGGGAATTCCAGAAGAC
AAGAACCCCTTTAAAGAAAAAGGCAGCTGTGTTATTTCATAA
Enzyme 56 GenBank Gene ID AC002076 Link Image
Enzyme 56 GeneCard ID GNG11 Link Image
Enzyme 56 GenAtlas ID GNG11 Link Image
Enzyme 56 HGNC ID HGNC:4403 Link Image
Enzyme 56 Chromosome Location 7
Enzyme 56 Locus 7q21
Enzyme 56 SNPs SNPJam Report Link Image
Enzyme 56 General References
  1. Ray K, Kunsch C, Bonner LM, Robishaw JD: Isolation of cDNA clones encoding eight different human G protein gamma subunits, including three novel forms designated the gamma 4, gamma 10, and gamma 11 subunits. J Biol Chem. 1995 Sep 15;270(37):21765-71. [PubMed Link Image]
  2. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 56 Metabolite References Not Available
Enzyme 57 [top]
Enzyme 57 ID 7906
Enzyme 57 Name Guanine nucleotide-binding protein G(t) subunit alpha-1
Enzyme 57 Synonyms
  1. Transducin alpha-1 chain
Enzyme 57 Gene Name GNAT1
Enzyme 57 Protein Sequence >Guanine nucleotide-binding protein G(t) subunit alpha-1
MGAGASAEEKHSRELEKKLKEDAEKDARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLE
ECLEFIAIIYGNTLQSILAIVRAMTTLNIQYGDSARQDDARKLMHMADTIEEGTMPKEMS
DIIQRLWKDSGIQACFERASEYQLNDSAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGI
IETQFSFKDLNFRMFDVGGQRSERKKWIHCFEGVTCIIFIAALSAYDMVLVEDDEVNRMH
ESLHLFNSICNHRYFATTSIVLFLNKKDVFFEKIKKAHLSICFPDYDGPNTYEDAGNYIK
VQFLELNMRRDVKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF
Enzyme 57 Number of Residues 350
Enzyme 57 Molecular Weight 40040.4
Enzyme 57 Theoretical pI 5.32
Enzyme 57 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 57 General Function Involved in signal transducer activity
Enzyme 57 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 57 Pathways Not Available
Enzyme 57 Reactions Not Available
Enzyme 57 Pfam Domain Function
Enzyme 57 Signals
  • None
Enzyme 57 Transmembrane Regions
  • None
Enzyme 57 Essentiality Not Available
Enzyme 57 GenBank ID Protein 31865 Link Image
Enzyme 57 UniProtKB/Swiss-Prot ID P11488 Link Image
Enzyme 57 UniProtKB/Swiss-Prot Entry Name GNAT1_HUMAN Link Image
Enzyme 57 PDB ID 1TND Link Image
Enzyme 57 PDB File Show
Enzyme 57 3D Structure
Enzyme 57 Cellular Location Not Available
Enzyme 57 Gene Sequence >1053 bp
ATGGGGGCTGGGGCCAGTGCTGAGGAGAAGCACTCCAGGGAGCTGGAAAAGAAGCTGAAA
GAGGACGCTGAGAAGGATGCTCGAACCGTGAAGCTGCTGCTTCTGGGTGCCGGTGAGTCC
GGGAAGAGCACCATCGTCAAGCAGATGAAGATTATCCACCAGGACGGGTACTCGCTGGAA
GAGTGCCTCGAGTTTATCGCCATCATCTACGGCAACACGTTGCAGTCCATCCTGGCCATC
GTACGCGCCATGACCACACTCAACATCCAGTACGGAGACTCTGCACGCCAGGACGACGCC
CGGAAGCTGATGCACATGGCAGACACTATCGAGGAGGGCACGATGCCCAAGGAGATGTCG
GACATCATCCAGCGGCTGTGGAAGGACTCCGGTATCCAGGCCTGTTTTGAGCGCGCCTCG
GAGTACCAGCTCAACGACTCGGCGGGCTACTACCTCTCCGACCTGGAGCGCCTGGTAACC
CCGGGCTACGTGCCCACCGAGCAGGACGTGCTGCGCTCGCGAGTCAAGACCACTGGCATC
ATCGAGACGCAGTTCTCCTTCAAGGATCTCAACTTCCGGATGTTCGATGTGGGCGGGCAG
CGCTCGGAGCCGAAGAAGTGGATCCACTGCTTCGAGGGCGTGACCTGCATCATCTTCATC
GCGGCGCTGACCGCGTACGACATGGTGCTAGTGGAGGACGACGAAGTGAACCGCATGCAC
GAGAGCCTGCACCTGTTCAACAGCATCTGCAACCACCGCTACTTCGCCACGACGTCCATC
GTGCTCTTCCTTAACAAGAAGGACGTCTTCTTCGAGAAGGTCAAGAAGGCGCACCTCAGC
ATCTGTTTCCCGGACTACGATGGACCCAACACCTACGAGGACGCCGGCAACTACATCAAG
GTGCAGTTCCTCGAGCTCAACATGCGGCGCGACGTGAAGGAGATCTATTCCCACATGACG
TGCGCCACCGACACGCAGAACGTCAAATTCTGCTTCGACGCTGTCACCGACATCATCATC
AAGGAGAACCTCAAAGACTGTGGCCTCTTCTGA
Enzyme 57 GenBank Gene ID X15088 Link Image
Enzyme 57 GeneCard ID GNAT1 Link Image
Enzyme 57 GenAtlas ID GNAT1 Link Image
Enzyme 57 HGNC ID HGNC:4393 Link Image
Enzyme 57 Chromosome Location 3
Enzyme 57 Locus 3p21
Enzyme 57 SNPs SNPJam Report Link Image
Enzyme 57 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 57 Metabolite References Not Available
Enzyme 58 [top]
Enzyme 58 ID 8236
Enzyme 58 Name Protein ALEX
Enzyme 58 Synonyms
  1. Alternative gene product encoded by XL-exon
Enzyme 58 Gene Name GNAS
Enzyme 58 Protein Sequence >Protein ALEX
MMARPVDPQRSPDPTFRSSTRHSGKLEPMEATAHLLRKQCPSRLNSPAWEASGLHWSSLD
SPVGSMQALRPSAQHSWSPEPSVVPDQAWEDTALHQKKLCPLSLTSLPREAAVNFSYRSQ
TLLQEAQVLQGSPELLPRSPKPSGLQRLAPEEATALPLRRLCHLSLMEKDLGTTAHPRGF
PELSHKSTAAASSRQSRPRVRSASLPPRTRLPSGSQAPSAAHPKRLSDLLLTSRAAAPGW
RSPDPRSRLAAPPLGSTTLPSTWTAPQSRLTARPSRSPEPQIRESEQRDPQLRRKQQRWK
EPLMPRREEKYPLRGTDPLPPGQPQRIPLPGQPLQPQPILTPGQPQKIPTPGQHQPILTP
GHSQPIPTPGQPLPPQPIPTPGRPLTPQPIPTPGRPLTPQPIQMPGRPLRLPPPLRLLRP
GQPMSPQLRQTQGLPLPQPLLPPGQPKSAGRPLQPLPPGPDARSISDPPAPRSRLPIRLL
RGLLARLPGGASPRAAAAAACTTMKGWPAATMTPAETSPTMGPPDASAGFSIGEIAAAES
PSATYSATFSCKPSGAASVDLRVPSPKPRALSRSRRYPWRRSADRCAKKPWRSGPRSAQR
RNAVSSSTNNSRTKRWATCVRTACCF
Enzyme 58 Number of Residues 626
Enzyme 58 Molecular Weight 67947.1
Enzyme 58 Theoretical pI 12.07
Enzyme 58 GO Classification Not Available
Enzyme 58 General Function Not Available
Enzyme 58 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 58 Pathways Not Available
Enzyme 58 Reactions Not Available
Enzyme 58 Pfam Domain Function Not Available
Enzyme 58 Signals
  • None
Enzyme 58 Transmembrane Regions
  • None
Enzyme 58 Essentiality Not Available
Enzyme 58 GenBank ID Protein 117938768 Link Image
Enzyme 58 UniProtKB/Swiss-Prot ID P84996 Link Image
Enzyme 58 UniProtKB/Swiss-Prot Entry Name ALEX_HUMAN Link Image
Enzyme 58 PDB ID Not Available
Enzyme 58 Cellular Location Not Available
Enzyme 58 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 58 GenBank Gene ID NM_001077490.1 Link Image
Enzyme 58 GeneCard ID GNAS Link Image
Enzyme 58 GenAtlas ID GNAS Link Image
Enzyme 58 HGNC ID HGNC:4392 Link Image
Enzyme 58 Chromosome Location 2
Enzyme 58 Locus 20q13.3
Enzyme 58 SNPs SNPJam Report Link Image
Enzyme 58 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 58 Metabolite References Not Available
Enzyme 59 [top]
Enzyme 59 ID 8268
Enzyme 59 Name Rap guanine nucleotide exchange factor 3
Enzyme 59 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 59 Gene Name RAPGEF3
Enzyme 59 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 59 Number of Residues 923
Enzyme 59 Molecular Weight 103651.0
Enzyme 59 Theoretical pI 7.49
Enzyme 59 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 59 General Function Involved in cAMP-dependent protein kinase regulator activity
Enzyme 59 Specific Function Guanine nucleotide exchange factor (GEF) for RAP1A and RAP2A small GTPases that is activated by binding cAMP
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 148747859 Link Image
Enzyme 59 UniProtKB/Swiss-Prot ID O95398 Link Image
Enzyme 59 UniProtKB/Swiss-Prot Entry Name RPGF3_HUMAN Link Image
Enzyme 59 PDB ID Not Available
Enzyme 59 Cellular Location Not Available
Enzyme 59 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 59 GenBank Gene ID NM_001098531.2 Link Image
Enzyme 59 GeneCard ID RAPGEF3 Link Image
Enzyme 59 GenAtlas ID RAPGEF3 Link Image
Enzyme 59 HGNC ID HGNC:16629 Link Image
Enzyme 59 Chromosome Location 1
Enzyme 59 Locus 12q13.1
Enzyme 59 SNPs SNPJam Report Link Image
Enzyme 59 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 59 Metabolite References Not Available
Enzyme 60 [top]
Enzyme 60 ID 8354
Enzyme 60 Name Lysophosphatidic acid receptor 2
Enzyme 60 Synonyms
  1. LPA receptor 2
  2. LPA-2
  3. Lysophosphatidic acid receptor Edg-4
Enzyme 60 Gene Name LPAR2
Enzyme 60 Protein Sequence >Lysophosphatidic acid receptor 2
MVIMGQCYYNETIGFFYNNSGKELSSHWRPKDVVVVALGLTVSVLVLLTNLLVIAAIASN
RRFHQPIYYLLGNLAAADLFAGVAYLFLMFHTGPRTARLSLEGWFLRQGLLDTSLTASVA
TLLAIAVERHRSVMAVQLHSRLPRGRVVMLIVGVWVAALGLGLLPAHSWHCLCALDRCSR
MAPLLSRSYLAVWALSSLLVFLLMVAVYTRIFFYVRRRVQRMAEHVSCHPRYRETTLSLV
KTVVIILGAFVVCWTPGQVVLLLDGLGCESCNVLAVEKYFLLLAEANSLVNAAVYSCRDA
EMRRTFRRLLCCACLRQSTRESVHYTSSAQGGASTRIMLPENGHPLMDSTL
Enzyme 60 Number of Residues 351
Enzyme 60 Molecular Weight 39083.8
Enzyme 60 Theoretical pI 9.42
Enzyme 60 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 60 General Function Involved in G-protein coupled receptor protein signaling pathway
Enzyme 60 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 60 Pathways Not Available
Enzyme 60 Reactions Not Available
Enzyme 60 Pfam Domain Function
Enzyme 60 Signals
  • None
Enzyme 60 Transmembrane Regions
  • 34-54 70-90 104-126 147-167 189-209 243-263 280-297
Enzyme 60 Essentiality Not Available
Enzyme 60 GenBank ID Protein 2213635 Link Image
Enzyme 60 UniProtKB/Swiss-Prot ID Q9HBW0 Link Image
Enzyme 60 UniProtKB/Swiss-Prot Entry Name LPAR2_HUMAN Link Image
Enzyme 60 PDB ID Not Available
Enzyme 60 Cellular Location Not Available
Enzyme 60 Gene Sequence >1056 bp
ATGGTCATCATGGGCCAGTGCTACTACAACGAGACCATCGGCTTCTTCTATAACAACAGT
GGCAAAGAGCTCAGCTCCCACTGGCGGCCCAAGGATGTGGTCGTGGTGGCACTGGGGCTG
ACCGTCAGCGTGCTGGTGCTGCTGACCAATCTGCTGGTCATAGCAGCCATCGCCTCCAAC
CGCCGCTTCCACCAGCCCATCTACTACCTGCTCGGCAATCTGGCCGCGGCTGACCTCTTC
GCGGGCGTGGCCTACCTCTTCCTCATGTTCCACACTGGTCCCCGCACAGCCCGACTTTCA
CTTGAGGGCTGGTTCCTGCGGCAGGGCTTGCTGGACACAAGCCTCACTGCGTCGGTGGCC
ACACTGCTGGCCATCGCCGTGGAGCGGCACCGCAGTGTGATGGCCGTGCAGCTGCACAGC
CGCCTGCCCCGTGGCCGCGTGGTCATGCTCATTGTGGGCGTGTGGGTGGCTGCCCTGGGC
CTGGGGCTGCTGCCTGCCCACTCCTGGCACTGCCTCTGTGCCCTGGACCGCTGCTCACGC
ATGGCACCCCTGCTCAGCCGCTCCTATTTGGCCGTCTGGGCTCTGTCGAGCCTGCTTGTC
TTCCTGCTCATGGTGGCTGTGTACACCCGCATTTTCTTCTACGTGCGGCGGCGAGTGCAG
CGCATGGCAGAGCATGTCAGCTGCCACCCCCGCTACCGAGAGACCACGCTCAGCCTGGTC
AAGACTGTTGTCATCATCCTGGGGGCGTTCGTGGTCTGCTGGACACCAGGCCAGGTGGTA
CTGCTCCTGGATGGTTTAGGCTGTGAGTCCTGCAATGTCCTGGCTGTAGAAAAGTACTTC
CTACTGTTGGCCGAGGCCAACTCACTGGTCAATGCTGCTGTGTACTCTTGCCGAGATGCT
GAGATGCGCCGCACCTTCCGCCGCCTTCTCTGCTGCGCGTGCCTCCGCCAGTCCACCCGC
GAGTCTGTCCACTATACATCCTCTGCCCAGGGAGGTGCCAGCACTCGCATCATGCTTCCC
GAGAACGGCCACCCACTGATGGACTCCACCCTTTAG
Enzyme 60 GenBank Gene ID AC002306 Link Image
Enzyme 60 GeneCard ID LPAR2 Link Image
Enzyme 60 GenAtlas ID LPAR2 Link Image
Enzyme 60 HGNC ID HGNC:3168 Link Image
Enzyme 60 Chromosome Location 1
Enzyme 60 Locus 19p12
Enzyme 60 SNPs SNPJam Report Link Image
Enzyme 60 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 60 Metabolite References Not Available
Enzyme 61 [top]
Enzyme 61 ID 8453
Enzyme 61 Name Rap guanine nucleotide exchange factor 4
Enzyme 61 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 61 Gene Name RAPGEF4
Enzyme 61 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 61 Number of Residues 1011
Enzyme 61 Molecular Weight 115520.7
Enzyme 61 Theoretical pI 6.83
Enzyme 61 GO Classification
Function
  • GTPase regulator activity
  • cAMP-dependent protein kinase regulator activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • kinase regulator activity
  • nucleoside-triphosphatase regulator activity
  • protein kinase regulator activity
Process
  • biological regulation
  • intracellular signal transduction
  • intracellular signaling pathway
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular metabolic process
  • regulation of cellular process
  • regulation of cellular protein metabolic process
  • regulation of metabolic process
  • regulation of protein amino acid phosphorylation
  • regulation of protein modification process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • signaling
  • signaling pathway
  • small GTPase mediated signal transduction
Component
  • cAMP-dependent protein kinase complex
  • cell part
  • intracellular
  • macromolecular complex
  • protein complex
Enzyme 61 General Function Involved in cAMP-dependent protein kinase regulator activity
Enzyme 61 Specific Function Guanine nucleotide exchange factor (GEF) for RAP1A, 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 61 Pathways Not Available
Enzyme 61 Reactions Not Available
Enzyme 61 Pfam Domain Function
Enzyme 61 Signals
  • None
Enzyme 61 Transmembrane Regions
  • None
Enzyme 61 Essentiality Not Available
Enzyme 61 GenBank ID Protein 17061825 Link Image
Enzyme 61 UniProtKB/Swiss-Prot ID Q8WZA2 Link Image
Enzyme 61 UniProtKB/Swiss-Prot Entry Name RPGF4_HUMAN Link Image
Enzyme 61 PDB ID Not Available
Enzyme 61 Cellular Location Not Available
Enzyme 61 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 61 GenBank Gene ID AB027471 Link Image
Enzyme 61 GeneCard ID RAPGEF4 Link Image
Enzyme 61 GenAtlas ID RAPGEF4 Link Image
Enzyme 61 HGNC ID HGNC:16626 Link Image
Enzyme 61 Chromosome Location 2
Enzyme 61 Locus 2q31-q32
Enzyme 61 SNPs SNPJam Report Link Image
Enzyme 61 General References
  1. Kawasaki H, Springett GM, Mochizuki N, Toki S, Nakaya M, Matsuda M, Housman DE, Graybiel AM: A family of cAMP-binding proteins that directly activate Rap1. Science. 1998 Dec 18;282(5397):2275-9. [PubMed Link Image]
  2. 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 61 Metabolite References Not Available
Enzyme 62 [top]
Enzyme 62 ID 8749
Enzyme 62 Name Cytosolic 5'-nucleotidase 3
Enzyme 62 Synonyms
  1. Cytosolic 5'-nucleotidase III
  2. cN-III
  3. Pyrimidine 5'-nucleotidase 1
  4. P5'N-1
  5. P5N-1
  6. PN-I
  7. Uridine 5'-monophosphate hydrolase 1
  8. p36
Enzyme 62 Gene Name NT5C3
Enzyme 62 Protein Sequence >Cytosolic 5'-nucleotidase 3
MRAPSMDRAAVARVGAVASASVCALVAGVVLAQYIFTLKRKTGRKTKIIEMMPEFQKSSV
RIKNPTRVEEIICGLIKGGAAKLQIITDFDMTLSRFSYKGKRCPTCHNIIDNCKLVTDEC
RKKLLQLKEKYYAIEVDPVLTVEEKYPYMVEWYTKSHGLLVQQALPKAKLKEIVAESDVM
LKEGYENFFDKLQQHSIPVFIFSAGIGDVLEEVIRQAGVYHPNVKVVSNFMDFDETGVLK
GFKGELIHVFNKHDGALRNTEYFNQLKDNSNIILLGDSQGDLRMADGVANVEHILKIGYL
NDRVDELLEKYMDSYDIVLVQDESLEVANSILQKIL
Enzyme 62 Number of Residues 336
Enzyme 62 Molecular Weight 37947.8
Enzyme 62 Theoretical pI 7.15
Enzyme 62 GO Classification
Function
  • 5'-nucleotidase activity
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleotidase activity
  • phosphatase activity
  • phosphoric ester hydrolase activity
Process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 62 General Function Involved in magnesium ion binding
Enzyme 62 Specific Function Can act both as nucleotidase and as phosphotransferase
Enzyme 62 Pathways
Enzyme 62 Reactions
  • a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate [RN:R07297]
Enzyme 62 Pfam Domain Function Not Available
Enzyme 62 Signals
  • None
Enzyme 62 Transmembrane Regions
  • None
Enzyme 62 Essentiality Not Available
Enzyme 62 GenBank ID Protein 70608082 Link Image
Enzyme 62 UniProtKB/Swiss-Prot ID Q9H0P0 Link Image
Enzyme 62 UniProtKB/Swiss-Prot Entry Name 5NT3_HUMAN Link Image
Enzyme 62 PDB ID Not Available
Enzyme 62 Cellular Location Not Available
Enzyme 62 Gene Sequence >1011 bp
ATGAGGGCCCCGTCCATGGACCGCGCGGCCGTGGCGAGGGTGGGCGCGGTAGCGAGCGCC
AGCGTGTGCGCCCTGGTGGCGGGGGTGGTGCTGGCTCAGTACATATTCACCTTGAAGAGG
AAGACGGGGCGGAAGACCAAGATCATCGAGATGATGCCAGAATTCCAGAAAAGTTCAGTT
CGAATCAAGAACCCTACAAGAGTAGAAGAAATTATCTGTGGTCTTATCAAAGGAGGAGCT
GCCAAACTTCAGATAATAACGGACTTTGATATGACACTCAGTAGATTTTCATATAAAGGG
AAAAGATGCCCAACATGTCATAATATCATTGACAACTGTAAGCTGGTTACAGATGAATGT
AGAAAAAAGTTATTGCAACTAAAGGAAAAATATTACGCTATTGAAGTTGATCCTGTTCTT
ACTGTAGAAGAGAAGTACCCTTATATGGTGGAATGGTATACTAAATCACATGGTTTGCTT
GTTCAGCAAGCTTTACCAAAAGCTAAACTTAAAGAAATTGTGGCAGAATCTGACGTTATG
CTCAAAGAAGGATATGAGAATTTCTTTGATAAGCTCCAACAACATAGCATCCCCGTGTTC
ATATTTTCGGCTGGAATCGGCGATGTACTAGAGGAAGTTATTCGTCAAGCTGGTGTTTAT
CATCCCAATGTCAAAGTTGTGTCCAATTTTATGGATTTTGATGAAACTGGGGTGCTCAAA
GGATTTAAAGGAGAACTAATTCATGTATTTAACAAACATGATGGTGCCTTGAGGAATACA
GAATATTTCAATCAACTAAAAGACAATAGTAACATAATTCTTCTGGGAGACTCCCAAGGA
GACTTAAGAATGGCAGATGGAGTGGCCAATGTTGAGCACATTCTGAAAATTGGATATCTA
AATGATAGAGTGGATGAGCTTTTAGAAAAGTACATGGACTCTTATGATATTGTTTTAGTA
CAAGATGAATCATTAGAAGTAGCCAACTCTATTTTACAGAAGATTCTATAA
Enzyme 62 GenBank Gene ID NM_001002010.1 Link Image
Enzyme 62 GeneCard ID NT5C3 Link Image
Enzyme 62 GenAtlas ID NT5C3 Link Image
Enzyme 62 HGNC ID HGNC:17820 Link Image
Enzyme 62 Chromosome Location 7
Enzyme 62 Locus 7p14.3
Enzyme 62 SNPs SNPJam Report Link Image
Enzyme 62 General References
  1. Amici A, Emanuelli M, Raffaelli N, Ruggieri S, Saccucci F, Magni G: Human erythrocyte pyrimidine 5-nucleotidase, PN-I, is identical to p36, a protein associated to lupus inclusion formation in response to alpha-interferon. Blood. 2000 Aug 15;96(4):1596-8. [PubMed Link Image]
  2. Marinaki AM, Escuredo E, Duley JA, Simmonds HA, Amici A, Naponelli V, Magni G, Seip M, Ben-Bassat I, Harley EH, Thein SL, Rees DC: Genetic basis of hemolytic anemia caused by pyrimidine 5' nucleotidase deficiency. Blood. 2001 Jun 1;97(11):3327-32. [PubMed Link Image]
  3. Kanno H, Takizawa T, Miwa S, Fujii H: Molecular basis of Japanese variants of pyrimidine 5'-nucleotidase deficiency. Br J Haematol. 2004 Jul;126(2):265-71. [PubMed Link Image]
  4. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  5. 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. 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]
  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. 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]
  9. Rich SA, Bose M, Tempst P, Rudofsky UH: Purification, microsequencing, and immunolocalization of p36, a new interferon-alpha-induced protein that is associated with human lupus inclusions. J Biol Chem. 1996 Jan 12;271(2):1118-26. [PubMed Link Image]
  10. Amici A, Ciccioli K, Naponelli V, Raffaelli N, Magni G: Evidence for essential catalytic determinants for human erythrocyte pyrimidine 5'-nucleotidase. Cell Mol Life Sci. 2005 Jul;62(14):1613-20. [PubMed Link Image]
  11. Wallden K, Stenmark P, Nyman T, Flodin S, Graslund S, Loppnau P, Bianchi V, Nordlund P: Crystal structure of human cytosolic 5'-nucleotidase II: insights into allosteric regulation and substrate recognition. J Biol Chem. 2007 Jun 15;282(24):17828-36. Epub 2007 Apr 3. [PubMed Link Image]
  12. Bianchi P, Fermo E, Alfinito F, Vercellati C, Baserga M, Ferraro F, Guzzo I, Rotoli B, Zanella A: Molecular characterization of six unrelated Italian patients affected by pyrimidine 5'-nucleotidase deficiency. Br J Haematol. 2003 Sep;122(5):847-51. [PubMed Link Image]
Enzyme 62 Metabolite References Not Available
Enzyme 63 [top]
Enzyme 63 ID 8772
Enzyme 63 Name ENTPD4 protein
Enzyme 63 Synonyms Not Available
Enzyme 63 Gene Name ENTPD4
Enzyme 63 Protein Sequence >ENTPD4 protein
MGRIGISCLFPASWHFSISPVGCPRILNTNLRQIMVISVLAAAVSLLYFSVVIIRNKYGR
LTRDKKFQRYLARVTDIEATDTNNPNVNYGIVVDCGSSGSRVFVYCWPRHNGNPHDLLDI
RQMRDKNRKPVVMKIKPGISEFATSPEKVSDYISPLLNFAAEHVPRAKHKETPLYILCTA
GMRILPESQQKAILEDLLTDIPVHFDFLFSDSHAEVISGKQEGVYAWIGINFVLGRFEHI
EDDDEAVVEVNIPGSESSEAIVRKRTAGILDMGGVSTQIAYEVPKTEEVAKNLLAEFNLG
CDVHQTEHVYRVYVATFLGFGGNAARQRYEDRIFANTIQKNRLLGKQTGLTPDMPYLDPC
LPLDIKDEIQQNGQTIYLRGTGDFDLCRETIQPFMNKTNETQTSLNGVYQPPIHFQNSEF
YGFSEFYYCTEDVLRMGGDYNAAKFTKAAKDYCATKWSILRERFDRGLYASHADLHRLKY
QCFKSAWMFEVFHRGFSFPVNYKSLKTALQVYDKEVQWTLGAILYRTRFLPLRKIGMLII
PCSGGCPKLCCAVWQPPPYGATKHLQCAAWN
Enzyme 63 Number of Residues 571
Enzyme 63 Molecular Weight 64852.9
Enzyme 63 Theoretical pI 8.13
Enzyme 63 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 63 General Function Involved in hydrolase activity
Enzyme 63 Specific Function Not Available
Enzyme 63 Pathways Not Available
Enzyme 63 Reactions Not Available
Enzyme 63 Pfam Domain Function
Enzyme 63 Signals
  • None
Enzyme 63 Transmembrane Regions
  • None
Enzyme 63 Essentiality Not Available
Enzyme 63 GenBank ID Protein 21759777 Link Image
Enzyme 63 UniProtKB/Swiss-Prot ID Q8NE73 Link Image
Enzyme 63 UniProtKB/Swiss-Prot Entry Name Q8NE73_HUMAN Link Image
Enzyme 63 PDB ID Not Available
Enzyme 63 Cellular Location Not Available
Enzyme 63 Gene Sequence >1716 bp
ATGGGGAGGATTGGCATCTCCTGTCTTTTTCCTGCTTCTTGGCATTTTAGCATATCTCCA
GTAGGGTGTCCTCGAATTCTGAATACCAATTTACGCCAAATTATGGTCATTAGTGTCCTG
GCTGCTGCTGTTTCACTTTTATATTTTTCTGTTGTCATAATCCGAAATAAGTATGGGCGA
CTAACCAGAGACAAGAAATTTCAAAGGTACCTGGCACGAGTTACCGACATTGAAGCTACA
GACACCAATAACCCCAATGTGAACTATGGGATCGTGGTGGACTGTGGTAGCAGTGGGTCT
CGAGTATTTGTTTACTGCTGGCCAAGGCATAATGGCAATCCACATGATCTGTTGGATATC
AGGCAAATGAGGGATAAAAACCGAAAGCCAGTGGTCATGAAGATAAAACCGGGCATTTCA
GAATTTGCTACCTCTCCAGAGAAAGTCAGTGATTACATTTCTCCACTTTTGAACTTTGCT
GCAGAGCATGTGCCACGGGCAAAACACAAAGAGACACCTCTCTACATTCTCTGCACGGCT
GGAATGAGAATCCTCCCCGAAAGCCAGCAGAAAGCTATTCTGGAAGACCTTCTGACCGAT
ATCCCCGTGCACTTTGACTTTCTGTTTTCTGACTCTCATGCAGAAGTAATTTCTGGGAAA
CAAGAAGGTGTGTATGCTTGGATTGGCATTAATTTTGTCCTTGGACGATTTGAGCATATT
GAAGATGATGATGAGGCCGTTGTGGAAGTTAACATTCCTGGAAGTGAAAGCAGCGAAGCC
ATTGTCCGTAAAAGGACAGCGGGCATTCTCGACATGGGCGGCGTGTCGACTCAGATAGCG
TACGAAGTCCCCAAAACTGAAGAAGTAGCTAAAAACTTGTTAGCTGAATTTAACTTGGGA
TGTGATGTTCACCAAACTGAGCATGTGTATCGAGTCTATGTGGCCACGTTTCTTGGGTTT
GGTGGCAATGCTGCTCGACAGAGATACGAAGACAGAATATTTGCCAACACCATTCAAAAG
AACAGGCTCCTGGGTAAACAGACTGGTCTGACTCCTGATATGCCGTACTTGGACCCCTGC
CTACCCCTAGACATTAAAGATGAAATCCAGCAAAATGGACAAACCATATACCTACGAGGG
ACTGGAGACTTTGACCTGTGTCGAGAGACTATCCAGCCTTTCATGAATAAAACAAACGAG
ACCCAGACTTCCCTCAATGGGGTCTACCAGCCCCCAATTCACTTCCAGAACAGTGAATTC
TATGGCTTCTCCGAATTCTACTACTGCACCGAGGATGTGTTACGAATGGGGGGAGACTAC
AATGCTGCTAAATTTACTAAAGCTGCAAAGGATTATTGTGCAACAAAGTGGTCCATTTTG
CGGGAACGCTTTGACCGAGGACTGTACGCCTCTCATGCTGACCTCCACAGGCTTAAGTAT
CAGTGCTTCAAATCGGCCTGGATGTTTGAGGTGTTTCATAGGGGCTTTTCGTTTCCTGTC
AACTATAAAAGCTTAAAGACTGCCTTGCAAGTTTACGACAAGGAGGTTCAGTGGACCCTT
GGAGCCATCCTCTACAGGACCCGCTTTCTACCATTAAGGAAAATAGGGATGCTGATAATA
CCTTGCTCAGGGGGTTGTCCAAAGCTGTGTTGTGCAGTATGGCAGCCACCACCATATGGG
GCCACCAAACACTTGCAATGTGCTGCTTGGAATTGA
Enzyme 63 GenBank Gene ID BC034477 Link Image
Enzyme 63 GeneCard ID ENTPD4 Link Image
Enzyme 63 GenAtlas ID ENTPD4 Link Image
Enzyme 63 HGNC ID HGNC:14573 Link Image
Enzyme 63 Chromosome Location 8
Enzyme 63 Locus 8p21.3
Enzyme 63 SNPs SNPJam Report Link Image
Enzyme 63 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 63 Metabolite References Not Available
Enzyme 64 [top]
Enzyme 64 ID 9969
Enzyme 64 Name Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A
Enzyme 64 Synonyms
  1. cAMP and cGMP phosphodiesterase 11A
Enzyme 64 Gene Name PDE11A
Enzyme 64 Protein Sequence >Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A
MAASRLDFGEVETFLDRHPELFEDYLMRKGKQEMVEKWLQRHSQGQGALGPRPSLAGTSS
LAHSTCRGGSSVGGGTGPNGSAHSQPLPGGGDCGGVPLSPSWAGGSRGDGNLQRRASQKE
LRKSFARSKAIHVNRTYDEQVTSRAQEPLSSVRRRALLRKASSLPPTTAHILSALLESRV
NLPRYPPTAIDYKCHLKKHNERQFFLELVKDISNDLDLTSLSYKILIFVCLMVDADRCSL
FLVEGAAAGKKTLVSKFFDVHAGTPLLPCSSTENSNEVQVPWGKGIIGYVGEHGETVNIP
DAYQDRRFNDEIDKLTGYKTKSLLCMPIRSSDGEIIGVAQAINKIPEGAPFTEDDEKVMQ
MYLPFCGIAISNAQLFAASRKEYERSRALLEVVNDLFEEQTDLEKIVKKIMHRAQTLLKC
ERCSVLLLEDIESPVVKFTKSFELMSPKCSADAENSFKESMEKSSYSDWLINNSIAELVA
STGLPVNISDAYQDPRFDAEADQISGFHIRSVLCVPIWNSNHQIIGVAQVLNRLDGKPFD
DADQRLFEAFVIFCGLGINNTIMYDQVKKSWAKQSVALDVLSYHATCSKAEVDKFKAANI
PLVSELAIDDIHFDDFSLDVDAMITAALRMFMELGMVQKFKIDYETLCRWLLTVRKNYRM
VLYHNWRHAFNVCQLMFAMLTTAGFQDILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSG
SALAQLYGTSATLEHHHFNHAVMILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLY
FERRTEFFELVSKGEYDWNIKNHRDIFRSMLMTACDLGAVTKPWEISRQVAELVTSEFFE
QGDRERLELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNVKLKPMLDSVAT
NRSKWEELHQKRLLASTASSSPASVMVAKEDRN
Enzyme 64 Number of Residues 933
Enzyme 64 Molecular Weight 104750.6
Enzyme 64 Theoretical pI 6.57
Enzyme 64 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 64 General Function Involved in catalytic activity
Enzyme 64 Specific Function Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP. Catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'- GMP, respectively
Enzyme 64 Pathways
Enzyme 64 Reactions
  • guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate [RN:R01234]
Enzyme 64 Pfam Domain Function
Enzyme 64 Signals
  • None
Enzyme 64 Transmembrane Regions
  • None
Enzyme 64 Essentiality Not Available
Enzyme 64 GenBank ID Protein 116536085 Link Image
Enzyme 64 UniProtKB/Swiss-Prot ID Q9HCR9 Link Image
Enzyme 64 UniProtKB/Swiss-Prot Entry Name PDE11_HUMAN Link Image
Enzyme 64 PDB ID Not Available
Enzyme 64 Cellular Location Not Available
Enzyme 64 Gene Sequence >2802 bp
ATGGCAGCCTCCCGCCTGGACTTTGGGGAGGTGGAAACTTTCCTGGACAGGCACCCAGAG
TTGTTTGAAGATTACTTGATGCGGAAGGGGAAGCAGGAGATGGTTGAAAAGTGGCTGCAG
AGGCACAGTCAGGGTCAGGGGGCTTTAGGTCCAAGGCCCTCTTTGGCTGGTACCAGCAGC
TTGGCTCACAGCACCTGCAGAGGTGGCAGCAGCGTTGGTGGTGGCACTGGACCAAATGGC
TCTGCCCACAGCCAGCCCCTTCCCGGTGGCGGGGACTGTGGTGGGGTTCCCTTGAGTCCC
AGCTGGGCCGGTGGCAGCAGGGGCGATGGGAACCTGCAGCGGAGAGCTTCTCAGAAAGAG
CTAAGGAAGAGTTTTGCCCGCTCCAAGGCCATCCACGTGAACAGGACCTACGATGAACAG
GTGACCTCCCGGGCTCAGGAACCCCTGAGTAGTGTACGACGGAGGGCACTTCTCCGGAAG
GCAAGCTCCCTGCCCCCCACCACAGCCCATATTCTCAGTGCGCTGCTGGAATCGAGAGTG
AATCTGCCTCGGTATCCCCCTACAGCCATCGACTACAAGTGCCATCTGAAAAAGCATAAT
GAGCGTCAGTTCTTTCTGGAATTGGTCAAAGATATCTCCAATGACCTTGACCTCACCAGC
CTGAGCTACAAGATTCTCATCTTTGTCTGCCTTATGGTGGATGCTGACCGCTGCTCTCTT
TTCCTGGTGGAAGGGGCAGCTGCTGGCAAGAAGACCTTGGTCTCCAAATTCTTTGATGTG
CATGCAGGAACACCTCTGCTGCCTTGCAGCAGCACAGAGAACTCAAATGAGGTGCAGGTC
CCCTGGGGCAAAGGTATCATTGGCTATGTCGGGGAGCATGGAGAAACGGTCAACATTCCT
GATGCCTACCAGGATCGACGATTCAATGATGAAATCGACAAGCTAACTGGATACAAGACA
AAATCATTATTGTGCATGCCTATCCGAAGCAGTGATGGTGAGATTATTGGTGTGGCCCAA
GCGATAAATAAGATTCCTGAAGGAGCTCCATTTACTGAAGATGATGAAAAAGTTATGCAG
ATGTATCTTCCATTTTGTGGAATCGCCATATCTAACGCTCAGCTCTTTGCTGCCTCAAGG
AAAGAATATGAAAGAAGCAGAGCTTTGCTAGAGGTGGTTAATGACCTCTTTGAAGAACAG
ACTGACCTGGAGAAAATTGTCAAGAAAATAATGCATCGGGCCCAAACTCTGCTGAAATGT
GAACGCTGTTCTGTTTTACTCCTAGAGGACATCGAATCACCAGTGGTGAAATTTACCAAA
TCCTTTGAATTGATGTCCCCAAAGTGCAGTGCTGATGCTGAGAACAGTTTCAAAGAAAGC
ATGGAGAAATCATCATACTCCGACTGGCTAATAAATAACAGCATTGCTGAGCTGGTTGCT
TCAACAGGCCTTCCAGTGAACATCAGTGATGCCTACCAGGATCCGCGCTTTGATGCAGAG
GCAGACCAGATATCTGGTTTTCACATAAGATCTGTTCTTTGTGTCCCTATTTGGAATAGC
AACCACCAAATAATTGGAGTGGCTCAAGTGTTAAACAGACTTGATGGGAAACCTTTTGAT
GATGCAGATCAACGACTTTTTGAGGCTTTTGTCATCTTTTGTGGACTTGGCATCAACAAC
ACAATTATGTATGATCAAGTGAAGAAGTCCTGGGCCAAGCAGTCTGTGGCTCTTGATGTG
CTATCATACCATGCAACATGTTCAAAAGCTGAAGTTGACAAGTTTAAGGCAGCCAACATC
CCTCTGGTGTCAGAACTTGCCATCGATGACATTCATTTTGATGACTTTTCTCTCGACGTT
GATGCCATGATCACAGCTGCTCTCCGGATGTTCATGGAGCTGGGGATGGTACAGAAATTT
AAAATTGACTATGAGACACTGTGTAGGTGGCTTTTGACAGTGAGGAAAAACTATCGGATG
GTTCTATACCACAACTGGAGACATGCCTTCAACGTGTGTCAGCTGATGTTCGCGATGTTA
ACCACTGCTGGGTTTCAAGACATTCTGACCGAGGTGGAAATTTTAGCGGTGATTGTGGGA
TGCCTGTGTCATGACCTCGACCACAGGGGAACCAACAATGCCTTCCAAGCTAAGAGTGGC
TCTGCCCTGGCCCAACTCTATGGAACCTCTGCTACCTTGGAGCATCACCATTTCAACCAC
GCCGTGATGATCCTTCAAAGTGAGGGTCACAATATCTTTGCTAACCTGTCCTCCAAGGAA
TATAGTGACCTTATGCAGCTTTTGAAGCAGTCAATATTGGCAACAGACCTCACGCTGTAC
TTTGAGAGGAGAACTGAATTCTTTGAACTTGTCAGTAAAGGAGAATACGATTGGAACATC
AAAAACCATCGTGATATATTTCGATCAATGTTAATGACAGCCTGTGACCTTGGAGCCGTG
ACCAAACCGTGGGAGATCTCCAGACAGGTGGCAGAACTTGTAACCAGTGAGTTCTTCGAA
CAAGGAGATCGGGAGAGATTAGAGCTCAAACTCACTCCTTCAGCAATTTTTGATCGGAAC
CGGAAGGATGAACTGCCTCGGTTGCAACTGGAGTGGATTGATAGCATCTGCATGCCTTTG
TATCAGGCACTGGTGAAGGTCAACGTGAAACTGAAGCCGATGCTAGATTCAGTAGCTACA
AACAGAAGTAAGTGGGAAGAGCTACACCAAAAACGACTGCTGGCCTCAACTGCCTCATCC
TCCCCTGCCAGTGTTATGGTAGCCAAGGAAGACAGGAACTAA
Enzyme 64 GenBank Gene ID NM_016953.3 Link Image
Enzyme 64 GeneCard ID PDE11A Link Image
Enzyme 64 GenAtlas ID PDE11A Link Image
Enzyme 64 HGNC ID HGNC:8773 Link Image
Enzyme 64 Chromosome Location 2
Enzyme 64 Locus 2q31.2
Enzyme 64 SNPs SNPJam Report Link Image
Enzyme 64 General References
  1. Yuasa K, Kotera J, Fujishige K, Michibata H, Sasaki T, Omori K: Isolation and characterization of two novel phosphodiesterase PDE11A variants showing unique structure and tissue-specific expression. J Biol Chem. 2000 Oct 6;275(40):31469-79. [PubMed Link Image]
  2. Fawcett L, Baxendale R, Stacey P, McGrouther C, Harrow I, Soderling S, Hetman J, Beavo JA, Phillips SC: Molecular cloning and characterization of a distinct human phosphodiesterase gene family: PDE11A. Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3702-7. [PubMed Link Image]
  3. Hetman JM, Robas N, Baxendale R, Fidock M, Phillips SC, Soderling SH, Beavo JA: Cloning and characterization of two splice variants of human phosphodiesterase 11A. Proc Natl Acad Sci U S A. 2000 Nov 7;97(23):12891-5. [PubMed Link Image]
  4. Yuasa K, Kanoh Y, Okumura K, Omori K: Genomic organization of the human phosphodiesterase PDE11A gene. Evolutionary relatedness with other PDEs containing GAF domains. Eur J Biochem. 2001 Jan;268(1):168-78. [PubMed Link Image]
  5. 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]
  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. Loughney K, Taylor J, Florio VA: 3',5'-cyclic nucleotide phosphodiesterase 11A: localization in human tissues. Int J Impot Res. 2005 Jul-Aug;17(4):320-5. [PubMed Link Image]
  8. Francis SH: Phosphodiesterase 11 (PDE11): is it a player in human testicular function? Int J Impot Res. 2005 Sep-Oct;17(5):467-8. [PubMed Link Image]
  9. Gross-Langenhoff M, Hofbauer K, Weber J, Schultz A, Schultz JE: cAMP is a ligand for the tandem GAF domain of human phosphodiesterase 10 and cGMP for the tandem GAF domain of phosphodiesterase 11. J Biol Chem. 2006 Feb 3;281(5):2841-6. Epub 2005 Dec 5. [PubMed Link Image]
  10. Horvath A, Boikos S, Giatzakis C, Robinson-White A, Groussin L, Griffin KJ, Stein E, Levine E, Delimpasi G, Hsiao HP, Keil M, Heyerdahl S, Matyakhina L, Libe R, Fratticci A, Kirschner LS, Cramer K, Gaillard RC, Bertagna X, Carney JA, Bertherat J, Bossis I, Stratakis CA: A genome-wide scan identifies mutations in the gene encoding phosphodiesterase 11A4 (PDE11A) in individuals with adrenocortical hyperplasia. Nat Genet. 2006 Jul;38(7):794-800. Epub 2006 Jun 11. [PubMed Link Image]
Enzyme 64 Metabolite References Not Available
Enzyme 65 [top]
Enzyme 65 ID 12965
Enzyme 65 Name Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
Enzyme 65 Synonyms
  1. P-Rex1
  2. PtdIns(3,4,5)-dependent Rac exchanger 1
Enzyme 65 Gene Name PREX1
Enzyme 65 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 65 Number of Residues 1659
Enzyme 65 Molecular Weight 186201.7
Enzyme 65 Theoretical pI 6.40
Enzyme 65 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 65 General Function Involved in intracellular signaling pathway
Enzyme 65 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 65 Pathways Not Available
Enzyme 65 Reactions Not Available
Enzyme 65 Pfam Domain Function
Enzyme 65 Signals
  • None
Enzyme 65 Transmembrane Regions
  • None
Enzyme 65 Essentiality Not Available
Enzyme 65 GenBank ID Protein 34452732 Link Image
Enzyme 65 UniProtKB/Swiss-Prot ID Q8TCU6 Link Image
Enzyme 65 UniProtKB/Swiss-Prot Entry Name PREX1_HUMAN Link Image
Enzyme 65 PDB ID Not Available
Enzyme 65 Cellular Location Not Available
Enzyme 65 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 65 GenBank Gene ID NM_020820.3 Link Image
Enzyme 65 GeneCard ID PREX1 Link Image
Enzyme 65 GenAtlas ID PREX1 Link Image
Enzyme 65 HGNC ID HGNC:32594 Link Image
Enzyme 65 Chromosome Location 2
Enzyme 65 Locus 20q13.13
Enzyme 65 SNPs SNPJam Report Link Image
Enzyme 65 General References
  1. Welch HC, Coadwell WJ, Ellson CD, Ferguson GJ, Andrews SR, Erdjument-Bromage H, Tempst P, Hawkins PT, Stephens LR: P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-nucleotide exchange factor for Rac. Cell. 2002 Mar 22;108(6):809-21. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  4. Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Feb 28;7(1):65-73. [PubMed Link Image]
  5. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  8. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
Enzyme 65 Metabolite References Not Available
Enzyme 66 [top]
Enzyme 66 ID 13039
Enzyme 66 Name Guanine monphosphate synthetase, isoform CRA_b
Enzyme 66 Synonyms
  1. SubName: cDNA FLJ75406, highly similar to Homo sapiens guanine monphosphate synthetase (GMPS), mRNA
  2. SubName: cDNA, FLJ79481, highly similar to GMP synthase (glutamine-hydrolyzing) (EC6.3.5.2)
Enzyme 66 Gene Name GMPS
Enzyme 66 Protein Sequence >Guanine monphosphate synthetase, isoform CRA_b
MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETP
AFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHK
KSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANE
SKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVL
VLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAA
HSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPE
EVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVR
ILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPH
TLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDW
ESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILR
ESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVE
VVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE
Enzyme 66 Number of Residues 693
Enzyme 66 Molecular Weight 76714.8
Enzyme 66 Theoretical pI 6.86
Enzyme 66 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 66 General Function Involved in catalytic activity
Enzyme 66 Specific Function Not Available
Enzyme 66 Pathways Not Available
Enzyme 66 Reactions Not Available
Enzyme 66 Pfam Domain Function
Enzyme 66 Signals
  • None
Enzyme 66 Transmembrane Regions
  • None
Enzyme 66 Essentiality Not Available
Enzyme 66 GenBank ID Protein 158256440 Link Image
Enzyme 66 UniProtKB/Swiss-Prot ID A8K639 Link Image
Enzyme 66 UniProtKB/Swiss-Prot Entry Name A8K639_HUMAN Link Image
Enzyme 66 PDB ID Not Available
Enzyme 66 Cellular Location Not Available
Enzyme 66 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 66 GenBank Gene ID AK291504 Link Image
Enzyme 66 GeneCard ID GMPS Link Image
Enzyme 66 GenAtlas ID GMPS Link Image
Enzyme 66 HGNC ID HGNC:4378 Link Image
Enzyme 66 Chromosome Location 3
Enzyme 66 Locus 3q24
Enzyme 66 SNPs SNPJam Report Link Image
Enzyme 66 General References
  1. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 66 Metabolite References Not Available
Enzyme 67 [top]
Enzyme 67 ID 13379
Enzyme 67 Name Ectonucleoside triphosphate diphosphohydrolase 8
Enzyme 67 Synonyms
  1. E-NTPDase 8
  2. NTPDase 8
  3. NTPDase8
Enzyme 67 Gene Name ENTPD8
Enzyme 67 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 8
MGLSRKEQVFLALLGASGVSGLTALILLLVEATSVLLPTDIKFGIVFDAGSSHTSLFLYQ
WLANKENGTGVVSQALACQVEGPGISSYTSNAAQAGESLQGCLEEALVLIPEAQHRKTPT
FLGATAGMRLLSRKNSSQARDIFAAVTQVLGRSPVDFWGAELLAGQAEGAFGWITVNYGL
GTLVKYSFTGEWIQPPEEMLVGALDMGGASTQITFVPGGPILDKSTQADFRLYGSDYSVY
THSYLCFGRDQMLSRLLVGLVQSRPAALLRHPCYLSGYQTTLALGPLYESPCVHATPPLS
LPQNLTVEGTGNPGACVSAIRELFNFSSCQGQEDCAFDGVYQPPLRGQFYAFSNFYYTFH
FLNLTSRQPLSTVNATIWEFCQRPWKLVEASYPGQDRWLRDYCASGLYILTLLHEGYGFS
EETWPSLEFRKQAGGVDIGWTLGYMLNLTGMIPADAPAQWRAESYGVWVAKVVFMVLALV
AVVGAALVQLFWLQD
Enzyme 67 Number of Residues 495
Enzyme 67 Molecular Weight 53903.1
Enzyme 67 Theoretical pI 4.96
Enzyme 67 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 67 General Function Involved in hydrolase activity
Enzyme 67 Specific Function Canalicular ectonucleoside NTPDase responsible for the main hepatic NTPDase activity. Ectonucleoside NTPDases catalyze the hydrolyzis of gamma- and beta-phosphate residues of nucleotides, playing a central role in concentration of extracellular nucleotides. Has activity toward ATP, ADP, UTP and UDP, but not toward AMP
Enzyme 67 Pathways
Enzyme 67 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
Enzyme 67 Pfam Domain Function
Enzyme 67 Signals
  • None
Enzyme 67 Transmembrane Regions
  • 9-29 472-492
Enzyme 67 Essentiality Not Available
Enzyme 67 GenBank ID Protein 110431368 Link Image
Enzyme 67 UniProtKB/Swiss-Prot ID Q5MY95 Link Image
Enzyme 67 UniProtKB/Swiss-Prot Entry Name ENTP8_HUMAN Link Image
Enzyme 67 PDB ID Not Available
Enzyme 67 Cellular Location Not Available
Enzyme 67 Gene Sequence >1488 bp
ATGGGGCTGTCCCGGAAGGAGCAGGTCTTCTTGGCCCTGCTGGGGGCCTCGGGGGTCTCA
GGCCTCACGGCACTCATTCTCCTCCTGGTGGAGGCCACCAGCGTGCTCCTGCCCACAGAC
ATCAAGTTTGGGATCGTGTTTGATGCGGGCTCCTCCCACACGTCCCTCTTCCTGTATCAG
TGGCTGGCGAACAAGGAGAATGGCACGGGTGTGGTCAGCCAGGCCCTGGCCTGCCAGGTG
GAAGGGCCTGGAATCTCCTCCTACACTTCTAATGCTGCACAGGCTGGTGAGAGCCTGCAG
GGCTGCTTGGAGGAGGCGCTGGTGCTGATCCCAGAGGCCCAGCATCGGAAAACACCCACG
TTCCTGGGGGCCACGGCTGGCATGAGGTTGCTCAGCCGGAAGAACAGCTCTCAGGCCAGG
GACATCTTTGCAGCAGTCACCCAGGTCCTGGGCCGGTCTCCCGTGGACTTTTGGGGTGCC
GAGCTCCTGGCCGGGCAGGCCGAAGGTGCCTTTGGTTGGATCACTGTCAACTACGGCTTG
GGGACGCTGGTCAAGTACTCCTTCACTGGAGAATGGATCCAGCCTCCGGAGGAGATGCTG
GTGGGTGCCCTGGACATGGGAGGGGCCTCCACCCAGATCACGTTCGTGCCTGGGGGCCCC
ATCTTGGACAAGAGCACCCAGGCCGATTTTCGCCTCTACGGCTCCGACTACAGCGTCTAC
ACTCACAGCTACCTGTGCTTTGGACGGGACCAGATGCTGAGCAGGCTCCTCGTGGGGCTG
GTACAGAGCCGCCCGGCTGCCCTGCTCCGTCACCCGTGCTACCTCAGCGGCTACCAGACC
ACACTGGCCCTGGGCCCGCTGTATGAGTCACCCTGTGTCCACGCCACGCCCCCGCTGAGC
CTCCCCCAGAACCTCACAGTTGAAGGGACAGGCAACCCTGGAGCCTGCGTCTCAGCCATC
CGGGAACTTTTCAACTTCTCCAGCTGCCAGGGCCAGGAGGACTGCGCCTTTGACGGGGTC
TACCAGCCCCCGCTGCGGGGCCAGTTCTATGCCTTCTCCAACTTCTACTACACCTTCCAC
TTCCTGAACCTCACCTCCAGGCAGCCCCTGAGCACGGTCAACGCCACCATCTGGGAGTTT
TGCCAGAGGCCCTGGAAACTGGTGGAGGCCAGCTACCCTGGGCAGGACCGCTGGCTGCGG
GACTACTGTGCCTCAGGCCTGTACATCCTCACCCTCCTGCACGAGGGCTACGGGTTCAGC
GAGGAGACCTGGCCCAGCCTCGAGTTCCGAAAGCAGGCGGGCGGTGTGGACATTGGCTGG
ACACTGGGCTACATGCTGAACCTGACCGGGATGATCCCGGCCGATGCGCCGGCTCAGTGG
CGGGCAGAGAGCTACGGCGTCTGGGTGGCCAAAGTGGTGTTCATGGTGCTGGCCCTGGTG
GCGGTGGTGGGGGCTGCCTTGGTCCAGCTCTTCTGGTTGCAGGACTAG
Enzyme 67 GenBank Gene ID NM_001033113.1 Link Image
Enzyme 67 GeneCard ID ENTPD8 Link Image
Enzyme 67 GenAtlas ID ENTPD8 Link Image
Enzyme 67 HGNC ID HGNC:24860 Link Image
Enzyme 67 Chromosome Location 9
Enzyme 67 Locus 9q34.3
Enzyme 67 SNPs SNPJam Report Link Image
Enzyme 67 General References
  1. Knowles AF, Li C: Molecular cloning and characterization of expressed human ecto-nucleoside triphosphate diphosphohydrolase 8 (E-NTPDase 8) and its soluble extracellular domain. Biochemistry. 2006 Jun 13;45(23):7323-33. [PubMed Link Image]
  2. Fausther M, Lecka J, Kukulski F, Levesque SA, Pelletier J, Zimmermann H, Dranoff JA, Sevigny J: Cloning, purification, and identification of the liver canalicular ecto-ATPase as NTPDase8. Am J Physiol Gastrointest Liver Physiol. 2007 Mar;292(3):G785-95. Epub 2006 Nov 9. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Levesque SA, Lavoie EG, Lecka J, Bigonnesse F, Sevigny J: Specificity of the ecto-ATPase inhibitor ARL 67156 on human and mouse ectonucleotidases. Br J Pharmacol. 2007 Sep;152(1):141-50. Epub 2007 Jul 2. [PubMed Link Image]
Enzyme 67 Metabolite References Not Available
Enzyme 68 [top]
Enzyme 68 ID 13877
Enzyme 68 Name Synembryn-B
Enzyme 68 Synonyms
  1. Brain synembrin
  2. hSyn
  3. Protein Ric-8B
Enzyme 68 Gene Name RIC8B
Enzyme 68 Protein Sequence >Synembryn-B
MDEERALYIVRAGEAGAIERVLRDYSDKHRATFKFESTDEDKRKKLCEGIFKVLIKDIPT
TCQVSCLEVLRILSRDKKVLVPVTTKENMQILLRLAKLNELDDSLEKVSEFPVIVESLKC
LCNIVFNSQMAQQLSLELNLAAKLCNLLRKCKDRKFINDIKCFDLRLLFLLSLLHTDIRS
QLRYELQGLPLLTQILESAFSIKWTDEYESAIDHNGPPLSPQETDCAIEALKALFNVTVD
SWKVHKESDSHQFRVMAAVLRHCLLIVGPTEDKTEELHSNAVNLLSNVPVSCLDVLICPL
THEETAQEATTLDELPSNKTAEKETVLKNNTMVYNGMNMEAIHVLLNFMEKRIDKGSSYR
EGLTPVLSLLTECSRAHRNIRKFLKDQVLPPLRDVTNRPEVGSTVRNKLVRLMTHVDLGV
KQIAAEFLFVLCKERVDSLLKYTGYGNAAGLLAARGLLAGGRGDNWYSEDEDTDTEEYKN
AKPKEELLKPMGLKPDGTITPLEEALNQYSVIEETSSDTD
Enzyme 68 Number of Residues 520
Enzyme 68 Molecular Weight 58824.1
Enzyme 68 Theoretical pI 5.45
Enzyme 68 GO Classification
Function
  • binding
Process
Component
Enzyme 68 General Function Involved in binding
Enzyme 68 Specific Function Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins by exchanging bound GDP for free GTP. Able to potentiate G(olf)-alpha- dependent cAMP accumulation suggesting that it may be an important component for odorant signal transduction
Enzyme 68 Pathways Not Available
Enzyme 68 Reactions Not Available
Enzyme 68 Pfam Domain Function
Enzyme 68 Signals
  • None
Enzyme 68 Transmembrane Regions
  • None
Enzyme 68 Essentiality Not Available
Enzyme 68 GenBank ID Protein 124375842 Link Image
Enzyme 68 UniProtKB/Swiss-Prot ID Q9NVN3 Link Image
Enzyme 68 UniProtKB/Swiss-Prot Entry Name RIC8B_HUMAN Link Image
Enzyme 68 PDB ID Not Available
Enzyme 68 Cellular Location Not Available
Enzyme 68 Gene Sequence >1563 bp
ATGGATGAGGAGCGCGCCCTCTACATCGTCCGGGCCGGCGAAGCAGGGGCTATCGAGCGG
GTCCTGAGGGATTACAGCGACAAGCATAGGGCTACTTTCAAATTTGAATCAACAGATGAA
GATAAAAGAAAGAAACTCTGTGAAGGCATATTTAAAGTCCTTATAAAGGACATCCCAACA
ACATGTCAAGTGTCCTGCCTGGAAGTACTCCGCATTCTCTCCAGAGACAAAAAGGTTTTA
GTTCCTGTGACAACTAAGGAAAATATGCAGATACTGCTGCGACTAGCCAAGCTAAATGAG
TTAGATGATTCTTTGGAGAAAGTATCAGAGTTCCCAGTTATTGTGGAGTCATTAAAATGT
CTGTGTAATATAGTGTTCAACAGTCAGATGGCACAGCAGCTCAGCCTGGAACTTAATCTT
GCTGCAAAGCTCTGTAACCTCCTGAGAAAGTGCAAGGACCGGAAATTTATCAATGACATT
AAGTGCTTTGACTTGCGCTTGCTCTTCCTTCTGTCACTTTTGCACACCGACATCAGGTCA
CAATTGCGCTATGAGCTCCAGGGACTACCGCTGCTAACGCAGATCTTGGAAAGTGCCTTT
AGCATCAAGTGGACCGATGAGTATGAATCGGCCATAGACCATAATGGACCTCCTCTCTCA
CCTCAGGAGACAGACTGTGCCATTGAGGCCCTCAAAGCTCTCTTCAATGTGACGGTAGAC
AGTTGGAAGGTGCATAAAGAGAGTGATTCTCATCAGTTCCGTGTAATGGCAGCTGTCCTT
CGTCATTGTTTACTAATCGTAGGTCCAACTGAAGACAAAACAGAAGAGCTACACAGCAAT
GCAGTCAACCTTTTAAGCAATGTTCCAGTCTCTTGTTTGGATGTTCTCATTTGTCCGTTA
ACCCATGAAGAAACAGCCCAAGAGGCAACGACTCTAGATGAACTGCCCAGTAATAAAACA
GCTGAGAAAGAAACAGTTTTGAAAAACAATACCATGGTATACAATGGTATGAATATGGAG
GCCATTCATGTTTTACTGAATTTTATGGAGAAGAGAATAGACAAGGGAAGCAGCTATAGA
GAGGGTCTAACTCCAGTTCTCAGCTTATTAACCGAATGTTCCCGAGCCCATCGAAACATC
CGAAAATTTCTCAAAGATCAGGTTTTACCACCGTTGAGGGATGTGACAAATCGACCTGAA
GTTGGCTCAACTGTGAGAAATAAGCTGGTGCGCCTCATGACACATGTTGACCTTGGAGTC
AAGCAAATTGCTGCTGAATTCCTTTTTGTCCTTTGCAAAGAGAGAGTGGATAGTCTGCTG
AAATACACTGGCTATGGGAATGCTGCAGGACTGTTGGCGGCCAGGGGCCTCTTGGCTGGA
GGAAGAGGAGATAATTGGTACTCAGAGGATGAGGACACAGACACTGAAGAATACAAAAAT
GCAAAACCAAAAGAGGAGTTGCTTAAACCAATGGGACTAAAACCTGATGGGACAATAACG
CCTTTGGAGGAAGCACTCAACCAGTACTCTGTCATCGAAGAGACCAGCTCTGACACAGAC
TAA
Enzyme 68 GenBank Gene ID BC132689 Link Image
Enzyme 68 GeneCard ID RIC8B Link Image
Enzyme 68 GenAtlas ID RIC8B Link Image
Enzyme 68 HGNC ID HGNC:25555 Link Image
Enzyme 68 Chromosome Location 1
Enzyme 68 Locus 12q23.3
Enzyme 68 SNPs SNPJam Report Link Image
Enzyme 68 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Klattenhoff C, Montecino M, Soto X, Guzman L, Romo X, Garcia MA, Mellstrom B, Naranjo JR, Hinrichs MV, Olate J: Human brain synembryn interacts with Gsalpha and Gqalpha and is translocated to the plasma membrane in response to isoproterenol and carbachol. J Cell Physiol. 2003 May;195(2):151-7. [PubMed Link Image]
  5. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 68 Metabolite References Not Available
Enzyme 69 [top]
Enzyme 69 ID 13881
Enzyme 69 Name Rap guanine nucleotide exchange factor 6
Enzyme 69 Synonyms
  1. PDZ domain-containing guanine nucleotide exchange factor 2
  2. PDZ-GEF2
  3. RA-GEF-2
Enzyme 69 Gene Name RAPGEF6
Enzyme 69 Protein Sequence >Rap guanine nucleotide exchange factor 6
MNSPVDPGARQALRKKPPERTPEDLNTIYSYLHGMEILSNLREHQLRLMSARARYERYSG
NQVLFCSETIARCWYILLSGSVLVKGSMVLPPCSFGKQFGGKRGCDCLVLEPSEMIVVEN
AKDNEDSILQREIPARQSRRRFRKINYKGERQTITDDVEVNSYLSLPADLTKMHLTENPH
PQVTHVSSSQSGCSIASDSGSSSLSDIYQATESEVGDVDLTRLPEGPVDSEDDEEEDEEI
DRTDPLQGRDLVRECLEKEPADKTDDDIEQLLEFMHQLPAFANMTMSVRRELCSVMIFEV
VEQAGAIILEDGQELDSWYVILNGTVEISHPDGKVENLFMGNSFGITPTLDKQYMHGIVR
TKVDDCQFVCIAQQDYWRILNHVEKNTHKVEEEGEIVMVHEHRELDRSGTRKGHIVIKAT
PERLIMHLIEEHSIVDPTYIEDFLLTYRTFLESPLDVGIKLLEWFKIDSLRDKVTRIVLL
WVNNHFNDFEGDPAMTRFLEEFEKNLEDTKMNGHLRLLNIACAAKAKWRQVVLQKASRES
PLQFSLNGGSEKGFGIFVEGVEPGSEAADSGLKRGDQIMEVNGQNFENITFMKAVEILRN
NTHLALTVKTNIFVFKELPFRTEQEKSGVPHIPKIAKKKSNRHSIQHVPGDIEQTSQEKG
SKKVKANTASGGRNKIRKILDKTRFSILPPKLFSDGGLSQSQDDSIVGTRHCRHSLAIMP
IPGTLSSSSPDLLQPTTSMLDFSNPSDIPDQVIRVFKVDQQSCYIIISKDTTAKEVVFHA
VHEFGLTGASDTYSLCEVSVTPEGVIKQRRLPDQFSKLADRIQLNGRYYLKNNMETETLC
SDEDAQELVKESQLSMLQLSTIEVATQLSMRDFDLFRNIEPTEYIDDLFKLNSKTGNTHL
KRFEDIVNQETFWVASEILTEANQLKRMKIIKHFIKIALHCRECKNFNSMFAIISGLNLA
SVARLRGTWEKLPSKYEKHLQDLQDIFDPSRNMAKYRNILSSQSMQPPIIPLFPVVKKDM
TFLHEGNDSKVDGLVNFEKLRMISKEIRQVVRMTSANMDPAMMFRQRSLSQGSTNSNMLD
VQGGAHKKRARRSSLLNAKKLYEDAQMARKVKQYLSSLDVETDEEKFQMMSLQWEPAYGT
LTKNLSEKRSAKSSEMSPVPMRSAGQTTKAHLHQPHRVSQVLQVPAVNLHPIRKKGQTKD
PALNTSLPQKVLGTTEEISGKKHTEDTISVASSLHSSPPASPQGSPHKGYTLIPSAKSDN
LSDSSHSEISSRSSIVSNCSVDSMSAALQDERCSSQALAVPESTGALEKTEHASGIGDHS
QHGPGWTLLKPSLIKCLAVSSSVSNEEISQEHIIIEAADSGRGSWTSCSSSSHDNFQSLP
NPKSWDFLNSYRHTHLDDPIAEVEPTDSEPYSCSKSCSRTCGQCKGSLERKSWTSSSSLS
DTYEPNYGTVKRRVLESTPAESSEGLDPKDATDPVYKTVTSSTEKGLIVYCVTSPKKDDR
YREPPPTPPGYLGISLADLKEGPHTHLKPPDYSVAVQRSKMMHNSLSRLPPASLSSNLVA
CVPSKIVTQPQRHNLQPFHPKLGDVTDADSEADENEQVSAV
Enzyme 69 Number of Residues 1601
Enzyme 69 Molecular Weight 179405.2
Enzyme 69 Theoretical pI 6.40
Enzyme 69 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 69 General Function Involved in protein binding
Enzyme 69 Specific Function Guanine nucleotide exchange factor (GEF) for Rap1A, Rap2A and M-Ras GTPases. Does not interact with cAMP
Enzyme 69 Pathways Not Available
Enzyme 69 Reactions Not Available
Enzyme 69 Pfam Domain Function
Enzyme 69 Signals
  • None
Enzyme 69 Transmembrane Regions
  • None
Enzyme 69 Essentiality Not Available
Enzyme 69 GenBank ID Protein 256600194 Link Image
Enzyme 69 UniProtKB/Swiss-Prot ID Q8TEU7 Link Image
Enzyme 69 UniProtKB/Swiss-Prot Entry Name RPGF6_HUMAN Link Image
Enzyme 69 PDB ID Not Available
Enzyme 69 Cellular Location Not Available
Enzyme 69 Gene Sequence >4806 bp
ATGAACTCACCCGTGGACCCTGGCGCTAGGCAGGCGTTGAGGAAGAAGCCACCCGAGCGG
ACTCCCGAGGACTTAAATACTATTTATTCTTATCTTCATGGAATGGAAATATTATCAAAT
CTCAGGGAACATCAGCTTAGATTAATGTCTGCAAGAGCACGCTATGAGAGATACAGTGGC
AATCAGGTTCTCTTTTGTTCAGAAACGATTGCCAGATGTTGGTATATCCTACTTTCTGGA
TCTGTGCTTGTGAAAGGCTCCATGGTCTTGCCTCCTTGCAGTTTTGGTAAGCAGTTTGGA
GGAAAAAGAGGATGTGATTGTCTTGTATTAGAGCCTTCAGAAATGATTGTGGTAGAGAAT
GCCAAAGATAATGAAGATAGTATTCTACAAAGAGAAATTCCTGCCAGACAATCCCGAAGA
AGATTTCGGAAAATTAACTATAAAGGAGAGCGCCAAACCATTACTGATGATGTGGAGGTT
AACAGCTATCTTTCTCTTCCAGCTGATCTTACCAAGATGCATCTCACAGAAAACCCTCAT
CCACAGGTGACTCATGTGTCTTCTAGTCAGTCTGGTTGTAGCATTGCCAGTGACTCTGGA
AGCAGCAGTTTATCTGATATCTATCAGGCTACGGAGAGTGAGGTAGGAGATGTAGATTTG
ACACGTCTTCCAGAAGGACCTGTTGATTCTGAGGATGACGAAGAGGAAGATGAAGAGATT
GATCGAACAGATCCATTGCAGGGGCGAGATCTTGTTCGAGAATGTCTTGAAAAAGAACCT
GCAGACAAAACTGATGATGACATTGAACAATTGCTGGAGTTTATGCACCAGCTCCCTGCA
TTTGCAAACATGACCATGTCTGTAAGGAGAGAACTCTGCTCAGTGATGATTTTTGAAGTG
GTAGAGCAGGCTGGAGCTATTATTCTTGAAGATGGGCAAGAGCTTGACTCATGGTATGTT
ATTTTAAACGGCACTGTGGAAATCAGTCATCCAGATGGAAAAGTTGAAAATTTGTTTATG
GGAAATAGTTTTGGAATTACTCCCACTCTGGATAAGCAGTACATGCATGGAATTGTCAGG
ACTAAAGTAGATGATTGTCAGTTTGTCTGCATAGCCCAGCAAGATTATTGGAGAATTTTA
AACCATGTGGAAAAAAATACCCATAAAGTTGAGGAAGAGGGAGAAATTGTTATGGTACAT
GAGCATCGGGAACTAGACCGGAGTGGAACCAGGAAAGGACACATTGTGATCAAGGCAACA
CCTGAGCGTCTCATAATGCATTTAATAGAAGAACATTCCATCGTGGATCCAACTTATATA
GAAGATTTTCTATTAACTTACAGGACATTTCTTGAAAGTCCTTTGGATGTTGGGATCAAA
CTATTGGAATGGTTTAAGATCGACAGCTTAAGAGATAAGGTGACACGGATTGTATTATTA
TGGGTAAATAATCATTTTAATGATTTTGAAGGTGACCCTGCTATGACTCGATTTCTAGAG
GAATTTGAAAAAAATCTGGAAGATACAAAGATGAATGGTCATCTCCGGTTATTGAATATT
GCCTGTGCTGCAAAGGCTAAGTGGAGACAGGTTGTGCTGCAAAAGGCTTCCCGCGAGTCC
CCTCTACAATTCAGCCTTAATGGAGGGAGTGAGAAGGGATTTGGTATTTTTGTTGAAGGA
GTAGAACCTGGTAGCAAAGCTGCTGATTCAGGACTGAAACGTGGTGATCAGATTATGGAA
GTAAATGGACAAAACTTTGAGAATATTACATTTATGAAAGCCGTTGAAATTTTGAGGAAT
AATACTCATCTTGCACTTACTGTGAAGACCAACATTTTTGTGTTCAAAGAGTTACTTTTT
AGGACTGAACAAGAGAAATCTGGTGTTCCTCATATTCCCAAAATTGCTGAAAAAAAAAGT
AATCGCCATTCTATCCAGCATGTGCCAGGAGATATTGAACAGACATCACAGGAGAAAGGA
AGTAAGAAAGTTAAAGCAAATACTGTTTCAGGTGGAAGAAACAAAATCAGGAAGATTTTG
GATAAAACACGATTTAGTATCTTGCCTCCAAAGCTATTTAGTGATGGAGGCCTAAGCCAA
TCACAAGATGACAGCATTGTGGGAACAAGGCACTGTAGGCATAGTCTGGCTATAATGCCC
ATCCCTGGAACACTCTCATCCAGCAGCCCTGATCTCCTGCAGCCTACCACCAGTATGTTG
GATTTTTCCAATCCTTCAGATATCCCTGATCAAGTTATAAGAGTTTTCAAAGTGGATCAG
CAAAGTTGCTACATTATCATCAGTAAAGACACCACAGCTAAAGAAGTAGTTTTTCATGCT
GTTCATGAATTTGGTTTGACCGGTGCATCCGACACATATTCTCTCTGTGAAGTTTCTGTT
ACTCCTGAGGGTGTCATAAAACAGAGAAGACTTCCAGATCAGTTCTCCAAATTAGCTGAT
AGAATTCAACTCAATGGAAGGTATTACTTAAAAAATAACATGGAAACAGAAACCTTATGT
TCAGATGAAGATGCTCAAGAACTAGTTAAGGAAAGCCAGCTATCCATGCTGCAGCTCAGT
ACCATTGAGGTGGCCACCCAGCTGTCAATGAGGGACTTTGATTTGTTTCGTAATATTGAA
CCGACTGAGTACATCGATGACCTTTTTAAGTTAAATTCCAAAACAGGAAATACTCATTTG
AAGAGGTTTGAGGACATTGTAAACCAAGAGACATTCTGGGTTGCCTCAGAAATTTTAACT
GAAGCAAATCAGCTCAAACGAATGAAGATTATTAAGCATTTTATTAAAATTGCACTTCAT
TGTCGAGAATGTAAGAACTTCAATTCCATGTTTGCAATAATAAGTGGCTTGAACCTGGCA
TCTGTAGCAAGACTCAGAGGAACTTGGGAAAAGTTACCAAGCAAATACGAGAAACATCTT
CAAGATCTACAAGACATTTTTGATCCATCTAGAAACATGGCAAAGTATAGAAATATTCTT
AGTAGTCAAAGTATGCAGCCTCCAATTATTCCACTCTTCCCTGTTGTCAAGAAAGATATG
ACATTTCTACATGAAGGAAATGACTCCAAAGTAGATGGTTTAGTAAACTTTGAGAAGTTA
AGAATGATTTCCAAGGAAATCCGCCAAGTTGTTCGAATGACTTCTGCTAACATGGACCCA
GCTATGATGTTTCGACAGAGGTCACTGAGTCAAGGAAGCACAAATTCAAACATGCTGGAT
GTTCAGGGAGGTGCTCACAAAAAAAGGGCACGCCGCAGCTCTCTGCTTAATGCCAAGAAG
CTATATGAGGATGCCCAAATGGCAAGGAAGGTGAAGCAGTATCTTTCCAGTCTCGATGTA
GAGACAGATGAGGAGAAGTTCCAGATGATGTCATTACAGTGGGAGCCTGCATATGGTACC
TTGACCAAGAATTTAAGTGAGAAAAGATCAGCCAAATCATCTGAAATGTCTCCAGTGCCT
ATGAGGTCAGCTGGCCAAACAACTAAAGCCCACTTGCATCAACCCCACAGAGTAAGCCAG
GTGCTTCAGGTGCCAGCTGTTAATTTGCACCCCATCAGGAAGAAGGGACAAACAAAAGAC
CCTGCACTGAATACAAGTTTACCTCAGAAAGTTTTAGGAACAACTGAAGAAATAAGTGGT
AAGAAGCATACAGAAGACACTATTTCTGTGGCGTCATCTTTACATTCTAGTCCTCCTGCA
TCTCCTCAAGGCTCCCCTCACAAAGGTTACACACTTATTCCATCAGCTAAATCTGACAAC
TTGTCTGACTCCAGCCATAGTGAGATTTCTTCACGGTCCAGCATCGTGAGCAATTGTTCT
GTTGACTCCATGTCTGCAGCTCTACAGGATGAACGGTGTTCCTCTCAGGCCCTGGCAGTC
CCTGAATCCACTGGGGCATTGGAAAAGACAGAGCACGCTTCAGGGATAGGAGATCATAGT
CAACATGGCCCTGGGTGGACACTCTTGAAGCCATCTCTAATCAAGTGTTTAGCTGTCTCA
TCGTCTGTGAGCAATGAAGAGATTTCTCAAGAGCATATCATTATAGAAGCAGCTGACAGT
GGTCGTGGAAGTTGGACTTCGTGTTCAAGCAGCTCCCATGACAACTTCCAAAGCCTTCCA
AACCCAAAAAGCTGGGATTTTTTGAACTCTTACAGACATACCCATTTGGATGACCCCATT
GCTGAAGTTGAACCCACTGACTCTGAGCCCTATTCCTGTTCTAAAAGCTGCTCTAGAACT
TGTGGGCAGTGTAAAGGAAGCCTAGAGAGAAAGAGTTGGACCTCCTCCAGTTCTCTGTCT
GACACGTATGAACCAAACTATGGGACAGTTAAACAGAGAGTATTGGAGAGCACCCCAGCT
GAGTCATCTGAAGGCTTGGACCCCAAGGATGCCACTGACCCAGTTTATAAAACTGTCACT
TCAAGTACAGAAAAGGGCTTGATTGTGTACTGTGTCACCTCACCCAAGAAGGACGATAGG
TATAGGGAGCCACCTCCCACTCCTCCAGGATATTTGGGGATTTCTTTAGCGGACCTAAAG
GAAGGACCCCACACACACCTAAAACCTCCAGATTATAGTGTGGCAGTGCAGAGGTCAAAG
ATGATGCATAACAGCCTCTCTAGACTGCCACCAGCTTCTCTCAGTAGCAACCTCGTGGCC
TGTGTTCCATCGAAGATTGTAACTCAGCCTCAGAGGCATAATTTGCAGCCATTCCATCCT
AAACTAGGAGATGTGACTGATGCAGATAGCGAAGCAGATGAAAATGAACAAGTTTCAGCA
GTCTAG
Enzyme 69 GenBank Gene ID NM_016340.5 Link Image
Enzyme 69 GeneCard ID RAPGEF6 Link Image
Enzyme 69 GenAtlas ID RAPGEF6 Link Image
Enzyme 69 HGNC ID HGNC:20655 Link Image
Enzyme 69 Chromosome Location 5
Enzyme 69 Locus 5q31.1
Enzyme 69 SNPs SNPJam Report Link Image
Enzyme 69 General References
  1. Kuiperij HB, de Rooij J, Rehmann H, van Triest M, Wittinghofer A, Bos JL, Zwartkruis FJ: Characterisation of PDZ-GEFs, a family of guanine nucleotide exchange factors specific for Rap1 and Rap2. Biochim Biophys Acta. 2003 Feb 17;1593(2-3):141-9. [PubMed Link Image]
  2. Gao X, Satoh T, Liao Y, Song C, Hu CD, Kariya Ki K, Kataoka T: Identification and characterization of RA-GEF-2, a Rap guanine nucleotide exchange factor that serves as a downstream target of M-Ras. J Biol Chem. 2001 Nov 9;276(45):42219-25. Epub 2001 Aug 27. [PubMed Link Image]
  3. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  4. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  5. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  9. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 69 Metabolite References Not Available
Enzyme 70 [top]
Enzyme 70 ID 14023
Enzyme 70 Name Neuroepithelial cell-transforming gene 1 protein
Enzyme 70 Synonyms
  1. Proto-oncogene p65 Net1
  2. Rho guanine nucleotide exchange factor 8
Enzyme 70 Gene Name NET1
Enzyme 70 Protein Sequence >Neuroepithelial cell-transforming gene 1 protein
MEPELAAQKQPRPRRRSRRASGLSTEGATGPSADTSGSELDGRCSLRRGSSFTFLTPGPN
WDFTLKRKRREKDDDVVSLSSLDLKEPSNKRVRPLARVTSLANLISPVRNGAVRRFGQTI
QSFTLRGDHRSPASAQKFSSRSTVPTPAKRRSSALWSEMLDITMKESLTTREIRRQEAIY
EMSRGEQDLIEDLKLARKAYHDPMLKLSIMSEEELTHIFGDLDSYIPLHEDLLTRIGEAT
KPDGTVEQIGHILVSWLPRLNAYRGYCSNQLAAKALLDQKKQDPRVQDFLQRCLESPFSR
KLDLWSFLDIPRSRLVKYPLLLKEILKHTPKEHPDVQLLEDAILIIQGVLSDINLKKGES
ECQYYIDKLEYLDEKQRDPRIEASKVLLCHGELRSKSGHKLYIFLFQDILVLTRPVTRNE
RHSYQVYRQPIPVQELVLEDLQDGDVRMGGSFRGAFSNSEKAKNIFRIRFHDPSPAQSHT
LQANDVFHKQQWFNCIRAAIAPFQSAGSPPELQGLPELHEECEGNHPSARKLTAQRRAST
VSSVTQVEVDENAYRCGSGMQMAEDSKSLKTHQTQPGIRRARDKALSGGKRKETLV
Enzyme 70 Number of Residues 596
Enzyme 70 Molecular Weight 67739.3
Enzyme 70 Theoretical pI 9.70
Enzyme 70 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 70 General Function Involved in Rho guanyl-nucleotide exchange factor activity
Enzyme 70 Specific Function Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase. May be involved in activation of the SAPK/JNK pathway
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 114145479 Link Image
Enzyme 70 UniProtKB/Swiss-Prot ID Q7Z628 Link Image
Enzyme 70 UniProtKB/Swiss-Prot Entry Name ARHG8_HUMAN Link Image
Enzyme 70 PDB ID Not Available
Enzyme 70 Cellular Location Not Available
Enzyme 70 Gene Sequence >1791 bp
ATGGAGCCCGAGCTGGCGGCTCAGAAGCAGCCTCGACCGCGGAGGCGAAGCCGCCGGGCC
TCTGGGCTCAGCACGGAGGGAGCGACGGGGCCTTCGGCCGACACCTCCGGGTCGGAGCTG
GACGGGAGATGTTCCCTTCGGAGAGGCAGCTCCTTCACATTCTTAACACCTGGCCCCAAC
TGGGACTTCACTTTGAAAAGAAAACGCAGAGAGAAAGATGATGATGTTGTAAGCCTTAGC
AGCCTTGATCTGAAGGAGCCAAGCAATAAAAGAGTTCGACCTCTGGCTCGTGTCACGTCC
TTGGCAAATTTAATCTCTCCTGTAAGAAATGGAGCTGTCAGACGTTTTGGTCAAACAATA
CAGTCATTTACCCTTCGTGGTGACCACAGATCCCCAGCCTCTGCCCAGAAGTTTTCTAGC
AGGTCAACAGTCCCAACACCCGCCAAGAGAAGGAGCAGTGCACTGTGGTCAGAGATGCTG
GACATCACCATGAAGGAGTCTCTCACCACCAGGGAGATCAGACGGCAGGAGGCAATATAT
GAAATGTCCCGAGGTGAACAGGATTTAATTGAGGATCTCAAACTTGCAAGAAAGGCCTAC
CATGACCCCATGTTAAAGTTGTCCATCATGTCAGAAGAGGAACTCACACATATATTTGGT
GATCTGGACTCTTACATACCTCTGCATGAAGATTTGTTGACAAGAATAGGAGAAGCAACC
AAGCCTGATGGAACAGTGGAGCAGATTGGTCACATTCTCGTGAGCTGGTTACCGCGCTTG
AATGCCTACAGAGGTTACTGTAGTAACCAGCTGGCAGCCAAAGCTCTTCTTGATCAAAAG
AAACAGGATCCAAGAGTCCAAGACTTCCTCCAGCGATGTCTCGAGTCTCCCTTCAGTCGA
AAACTAGATCTTTGGAGTTTCCTAGATATCCCTCGAAGTCGCCTAGTCAAATACCCTTTA
CTGTTAAAAGAAATTCTTAAACACACTCCAAAAGAGCACCCTGATGTTCAGCTTCTGGAG
GATGCTATATTGATAATACAGGGAGTCCTCTCTGATATCAACTTGAAGAAAGGTGAATCC
GAGTGCCAGTATTACATCGACAAGCTGGAGTACCTGGATGAAAAGCAGAGGGACCCCAGA
ATCGAAGCGAGCAAAGTGCTGCTGTGCCATGGGGAGCTGCGGAGCAAGAGTGGACATAAA
CTTTACATTTTCCTGTTTCAAGACATCTTGGTTCTGACTCGGCCCGTCACACGGAACGAA
CGGCACTCTTACCAGGTTTACCGGCAGCCAATCCCAGTCCAAGAGCTAGTCCTAGAAGAC
CTGCAGGATGGAGATGTGAGAATGGGAGGCTCCTTTCGAGGAGCTTTCAGTAACTCAGAG
AAAGCTAAAAATATCTTTAGAATTCGCTTCCATGACCCCTCTCCAGCCCAGTCTCACACT
CTGCAAGCCAATGACGTGTTCCACAAGCAGCAGTGGTTCAACTGTATTCGAGCGGCCATT
GCCCCCTTCCAGTCGGCAGGCAGTCCACCTGAGCTGCAGGGCCTGCCGGAGCTGCACGAA
GAGTGTGAGGGGAACCACCCCTCTGCGAGGAAACTCACAGCCCAGAGGAGGGCATCCACA
GTTTCCAGTGTTACTCAGGTAGAAGTTGATGAAAACGCTTACAGATGTGGCTCTGGCATG
CAGATGGCAGAGGACAGCAAGAGCTTAAAGACACACCAGACACAGCCCGGCATCCGAAGA
GCGAGGGACAAAGCCCTTTCTGGTGGCAAACGGAAAGAGACTTTGGTGTAG
Enzyme 70 GenBank Gene ID NM_001047160.1 Link Image
Enzyme 70 GeneCard ID NET1 Link Image
Enzyme 70 GenAtlas ID NET1 Link Image
Enzyme 70 HGNC ID HGNC:14592 Link Image
Enzyme 70 Chromosome Location 1
Enzyme 70 Locus 10p15
Enzyme 70 SNPs SNPJam Report Link Image
Enzyme 70 General References
  1. Chan AM, Takai S, Yamada K, Miki T: Isolation of a novel oncogene, NET1, from neuroepithelioma cells by expression cDNA cloning. Oncogene. 1996 Mar 21;12(6):1259-66. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Shen X, Li J, Hu PP, Waddell D, Zhang J, Wang XF: The activity of guanine exchange factor NET1 is essential for transforming growth factor-beta-mediated stress fiber formation. J Biol Chem. 2001 May 4;276(18):15362-8. Epub 2001 Feb 2. [PubMed Link Image]
  4. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  5. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  6. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 70 Metabolite References Not Available
Enzyme 71 [top]
Enzyme 71 ID 14038
Enzyme 71 Name Cell cycle progression protein 1
Enzyme 71 Synonyms
  1. Cell cycle progression restoration protein 8
Enzyme 71 Gene Name CCPG1
Enzyme 71 Protein Sequence >Cell cycle progression protein 1
MSENSSDSDSSCGWTVISHEGSDIEMLNSVTPTDSCEPAPECSSLEQEELQALQIEQGES
SQNGTVLMEETAYPALEETSSTIEAEEQKIPEDSIYIGTASDDSDIVTLEPPKLEEIGNQ
EVVIVEEAQSSEDFNMGSSSSSQYTFCQPETVFSSQPSDDESSSDETSNQPSPAFRRRRA
RKKTVSASESEDRLVAEQETEPSKELSKRQFSSGLNKCVILALVIAISMGFGHFYGTIQI
QKRQQLVRKIHEDELNDMKDYLSQCQQEQESFIDYKSLKENLARCWTLTEAEKMSFETQK
TNLATENQYLRVSLEKEEKALSSLQEELNKLREQIRILEDKGTSTELVKENQKLKQHLEE
EKQKKHSFLSQRETLLTEAKMLKRELERERLVTTALRGELQQLSGSQLHGKSDSPNVYTE
KKEIAILRERLTELERKLTFEQQRSDLWERLYVEAKDQNGKQGTDGKKKGGRGSHRAKNK
SKETFLGSVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTT
KNIFDEKGNKRFGATKEAAEKPRTVFSDYLHPQYKAPTENHHNRGPTMQNDGRKEKPVHF
KEFRKNTNSKKCSPGHDCRENSHSFRKACSGVFDCAQQESMSLFNTVVNPIRMDEFRQII
QRYMLKELDTFCHWNELDQFINKFFLNGVFIHDQKLFTDFVNDVKDYLRNMKEYEVDNDG
VFEKLDEYIYRHFFGHTFSPPYGPRSVYIKPCHYSSL
Enzyme 71 Number of Residues 757
Enzyme 71 Molecular Weight 87339.7
Enzyme 71 Theoretical pI 5.78
Enzyme 71 GO Classification Not Available
Enzyme 71 General Function Replication, recombination and repair
Enzyme 71 Specific Function Acts as an assembly platform for Rho protein signaling complexes. Limits guanine nucleotide exchange activity of MCF2L toward RHOA, which results in an inhibition of both its transcriptional activation ability and its transforming activity. Does not inhibit activity of MCF2L toward CDC42, or activity of MCF2 toward either RHOA or CDC42. May be involved in cell cycle regulation
Enzyme 71 Pathways Not Available
Enzyme 71 Reactions Not Available
Enzyme 71 Pfam Domain Function Not Available
Enzyme 71 Signals
  • None
Enzyme 71 Transmembrane Regions
  • 218-238
Enzyme 71 Essentiality Not Available
Enzyme 71 GenBank ID Protein 75677585 Link Image
Enzyme 71 UniProtKB/Swiss-Prot ID Q9ULG6 Link Image
Enzyme 71 UniProtKB/Swiss-Prot Entry Name CCPG1_HUMAN Link Image
Enzyme 71 PDB ID Not Available
Enzyme 71 Cellular Location Not Available
Enzyme 71 Gene Sequence >2274 bp
ATGTCTGAAAATTCCAGTGACAGTGATTCATCTTGTGGTTGGACTGTCATCAGTCATGAG
GGGTCAGATATAGAAATGTTGAATTCTGTGACCCCCACTGACAGCTGTGAGCCCGCCCCA
GAATGTTCATCTTTAGAGCAAGAGGAGCTTCAAGCATTGCAGATAGAGCAAGGAGAAAGC
AGCCAAAATGGCACAGTGCTTATGGAAGAAACTGCTTATCCAGCTTTGGAGGAAACCAGC
TCAACAATTGAGGCAGAGGAACAAAAGATACCCGAAGACAGTATCTATATTGGAACTGCC
AGTGATGATTCTGATATTGTTACCCTTGAGCCACCTAAGTTAGAAGAAATTGGAAATCAA
GAAGTTGTCATTGTTGAAGAAGCACAGAGTTCAGAAGACTTTAACATGGGCTCTTCCTCT
AGCAGCCAGTATACTTTCTGTCAGCCAGAAACTGTATTTTCATCTCAGCCTAGTGACGAT
GAATCAAGTAGTGATGAAACCAGTAATCAGCCCAGTCCTGCCTTTAGACGACGCCGTGCT
AGGAAGAAGACCGTTTCTGCTTCAGAATCTGAAGACCGGCTAGTTGCTGAACAAGAAACT
GAACCTTCTAAGGAGTTGAGTAAACGTCAGTTCAGTAGTGGTCTCAATAAGTGTGTTATA
CTTGCTTTGGTGATTGCAATCAGCATGGGATTTGGCCATTTCTATGGCACAATTCAGATT
CAGAAGCGTCAACAGTTAGTCAGAAAGATACATGAAGATGAATTGAATGATATGAAGGAT
TATCTTTCCCAGTGTCAACAGGAACAAGAATCTTTTATAGATTATAAGTCATTGAAAGAA
AATCTTGCAAGGTGTTGGACACTTACTGAAGCAGAGAAGATGTCCTTTGAAACTCAGAAA
ACGAACCTTGCTACAGAAAATCAGTATTTAAGAGTATCCTTGGAGAAGGAAGAAAAAGCC
TTATCCTCATTACAGGAAGAGTTAAACAAACTAAGAGAACAGATTAGAATATTGGAAGAT
AAAGGGACAAGTACTGAATTAGTTAAAGAAAATCAGAAACTTAAGCAGCATTTGGAAGAG
GAAAAGCAGAAAAAACACAGCTTTCTTAGTCAAAGGGAGACTCTGTTGACAGAAGCAAAG
ATGCTAAAGAGAGAACTGGAGAGAGAACGACTAGTAACTACGGCTTTAAGGGGGGAACTC
CAGCAGTTAAGTGGTAGTCAGTTACATGGCAAGTCAGATTCTCCCAATGTATATACTGAA
AAAAAGGAAATAGCAATCTTACGGGAAAGACTCACTGAGCTGGAACGGAAGCTAACCTTC
GAACAGCAGCGTTCTGATTTGTGGGAAAGATTGTATGTTGAGGCAAAAGATCAAAATGGA
AAACAAGGAACAGATGGAAAAAAGAAAGGGGGCAGAGGAAGCCACAGGGCTAAAAATAAG
TCAAAGGAAACATTTTTGGGTTCAGTTAAGGAAACATTTGATGCCATGAAGAATTCTACC
AAGGAGTTTGTAAGGCATCATAAAGAGAAAATTAAGCAGGCTAAAGAAGCTGTGAAGGAA
AATCTGAAAAAATTCTCAGATTCAGTTAAATCCACTTTCAGACACTTTAAAGATACCACC
AAGAATATCTTTGATGAAAAGGGTAATAAAAGATTTGGTGCTACAAAAGAAGCAGCTGAA
AAACCAAGAACAGTTTTTAGTGACTATTTACATCCACAGTATAAGGCACCTACAGAAAAC
CATCATAATAGAGGCCCTACTATGCAAAATGATGGAAGGAAAGAAAAGCCAGTTCACTTT
AAAGAATTCAGAAAAAATACAAATTCAAAGAAATGCAGTCCTGGGCATGATTGTAGAGAA
AATTCTCATTCTTTCAGAAAGGCTTGTTCTGGTGTATTTGATTGTGCTCAACAAGAGTCC
ATGAGCCTTTTTAACACAGTGGTGAATCCTATAAGGATGGATGAATTTAGACAGATAATT
CAAAGGTACATGTTAAAAGAACTGGATACTTTTTGTCACTGGAACGAACTTGATCAGTTC
ATCAATAAGTTTTTCCTAAACGGTGTCTTTATACATGATCAGAAGCTCTTCACTGACTTT
GTTAATGATGTTAAAGATTATCTTAGAAACATGAAGGAATATGAAGTAGATAATGATGGA
GTATTTGAGAAGTTGGATGAATATATATATAGACACTTCTTTGGTCACACTTTTTCCCCT
CCATATGGACCCAGGTCGGTTTACATAAAACCGTGTCATTACAGTAGTTTGTAA
Enzyme 71 GenBank Gene ID NM_004748.3 Link Image
Enzyme 71 GeneCard ID CCPG1 Link Image
Enzyme 71 GenAtlas ID CCPG1 Link Image
Enzyme 71 HGNC ID HGNC:24227 Link Image
Enzyme 71 Chromosome Location 1
Enzyme 71 Locus 15q21.1
Enzyme 71 SNPs SNPJam Report Link Image
Enzyme 71 General References
  1. Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Oct 29;6(5):337-45. [PubMed Link Image]
  2. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Edwards MC, Liegeois N, Horecka J, DePinho RA, Sprague GF Jr, Tyers M, Elledge SJ: Human CPR (cell cycle progression restoration) genes impart a Far- phenotype on yeast cells. Genetics. 1997 Nov;147(3):1063-76. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
Enzyme 71 Metabolite References Not Available
Enzyme 72 [top]
Enzyme 72 ID 14055
Enzyme 72 Name Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein
Enzyme 72 Synonyms
  1. P-Rex2
  2. PtdIns(3,4,5)-dependent Rac exchanger 2
  3. DEP domain-containing protein 2
Enzyme 72 Gene Name PREX2
Enzyme 72 Protein Sequence >Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein
MSEDSRGDSRAESAKDLEKQLRLRVCVLSELQKTERDYVGTLEFLVSAFLHRMNQCAASK
VDKNVTEETVKMLFSNIEDILAVHKEFLKVVEECLHPEPNAQQEVGTCFLHFKDKFRIYD
EYCSNHEKAQKLLLELNKIRTIRTFLLNCMLLGGRKNTDVPLEGYLVTPIQRICKYPLIL
KELLKRTPRKHSDYAAVMEALQAMKAVCSNINEAKRQMEKLEVLEEWQSHIEGWEGSNIT
DTCTEMLMCGVLLKISSGNIQERVFFLFDNLLVYCKRKHRRLKNSKASTDGHRYLFRGRI
NTEVMEVENVDDGTADFHSSGHIVVNGWKIHNTAKNKWFVCMAKTPEEKHEWFEAILKER
ERRKGLKLGMEQDTWVMISEQGEKLYKMMCRQGNLIKDRKRKLTTFPKCFLGSEFVSWLL
EIGEIHRPEEGVHLGQALLENGIIHHVTDKHQFKPEQMLYRFRYDDGTFYPRNEMQDVIS
KGVRLYCRLHSLFTPVIRDKDYHLRTYKSVVMANKLIDWLIAQGDCRTREEAMIFGVGLC
DNGFMHHVLEKSEFKDEPLLFRFFSDEEMEGSNMKHRLMKHDLKVVENVIAKSLLIKSNE
GSYGFGLEDKNKVPIIKLVEKGSNAEMAGMEVGKKIFAINGDLVFMRPFNEVDCFLKSCL
NSRKPLRVLVSTKPRETVKIPDSADGLGFQIRGFGPSVVHAVGRGTVAAAAGLHPGQCII
KVNGINVSKETHASVIAHVTACRKYRRPTKQDSIQWVYNSIESAQEDLQKSHSKPPGDEA
GDAFDCKVEEVIDKFNTMAIIDGKKEHVSLTVDNVHLEYGVVYEYDSTAGIKCNVVEKMI
EPKGFFSLTAKILEALAKSDEHFVQNCTSLNSLNEVIPTDLQSKFSALCSERIEHLCQRI
SSYKKFSRVLKNRAWPTFKQAKSKISPLHSSDFCPTNCHVNVMEVSYPKTSTSLGSAFGV
QLDSRKHNSHDKENKSSEQGKLSPMVYIQHTITTMAAPSGLSLGQQDGHGLRYLLKEEDL
ETQDIYQKLLGKLQTALKEVEMCVCQIDDLLSSITYSPKLERKTSEGIIPTDSDNEKGER
NSKRVCFNVAGDEQEDSGHDTISNRDSYSDCNSNRNSIASFTSICSSQCSSYFHSDEMDS
GDELPLSVRISHDKQDKIHSCLEHLFSQVDSITNLLKGQAVVRAFDQTKYLTPGRGLQEF
QQEMEPKLSCPKRLRLHIKQDPWNLPSSVRTLAQNIRKFVEEVKCRLLLALLEYSDSETQ
LRRDMVFCQTLVATVCAFSEQLMAALNQMFDNSKENEMETWEASRRWLDQIANAGVLFHF
QSLLSPNLTDEQAMLEDTLVALFDLEKVSFYFKPSEEEPLVANVPLTYQAEGSRQALKVY
FYIDSYHFEQLPQRLKNGGGFKIHPVLFAQALESMEGYYYRDNVSVEEFQAQINAASLEK
VKQYNQKLRAFYLDKSNSPPNSTSKAAYVDKLMRPLNALDELYRLVASFIRSKRTAACAN
TACSASGVGLLSVSSELCNRLGACHIIMCSSGVHRCTLSVTLEQAIILARSHGLPPRYIM
QATDVMRKQGARVQNTAKNLGVRDRTPQSAPRLYKLCEPPPPAGEE
Enzyme 72 Number of Residues 1606
Enzyme 72 Molecular Weight 182620.5
Enzyme 72 Theoretical pI 7.46
Enzyme 72 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 72 General Function Involved in intracellular signaling pathway
Enzyme 72 Specific Function Functions as a RAC1 guanine nucleotide exchange factor (GEF), activating Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol-3,4,5-triphosphate and the beta gamma subunits of heterotrimeric G protein. Mediates the activation of RAC1 in a PI3K-dependent manner. May be an important mediator of Rac signaling, acting directly downstream of both G protein- coupled receptors and phosphoinositide 3-kinase
Enzyme 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 47578115 Link Image
Enzyme 72 UniProtKB/Swiss-Prot ID Q70Z35 Link Image
Enzyme 72 UniProtKB/Swiss-Prot Entry Name PREX2_HUMAN Link Image
Enzyme 72 PDB ID Not Available
Enzyme 72 Cellular Location Not Available
Enzyme 72 Gene Sequence >4821 bp
ATGAGCGAGGACAGCCGCGGAGACAGCCGCGCCGAGAGCGCCAAGGACCTGGAGAAGCAG
CTTCGCCTGCGCGTGTGCGTGCTCAGCGAGCTCCAGAAGACCGAGCGGGACTATGTGGGC
ACGCTGGAGTTCCTGGTGTCGGCATTCTTACACAGAATGAACCAGTGTGCAGCATCAAAA
GTTGACAAAAATGTGACAGAAGAAACAGTGAAGATGTTGTTCTCAAACATTGAAGACATC
CTTGCAGTACATAAAGAATTCTTAAAAGTCGTGGAAGAATGCTTACACCCCGAACCTAAT
GCTCAACAAGAAGTGGGAACCTGCTTTCTTCACTTTAAAGACAAGTTTCGTATCTATGAT
GAATATTGTAGTAACCATGAGAAGGCACAAAAATTACTTCTTGAACTCAACAAAATAAGA
ACAATCCGGACATTTCTTTTGAACTGCATGCTGCTTGGAGGACGGAAGAACACAGATGTT
CCCTTGGAAGGATATTTAGTAACACCAATACAAAGAATATGCAAGTACCCTCTTATTTTG
AAGGAGTTGCTGAAGCGGACTCCACGGAAACACAGTGACTATGCAGCAGTGATGGAAGCC
CTCCAAGCCATGAAAGCTGTCTGTTCCAACATAAACGAGGCCAAGAGACAGATGGAGAAG
TTAGAAGTTTTAGAGGAATGGCAGTCTCACATTGAAGGCTGGGAGGGGTCCAACATCACT
GACACCTGCACTGAAATGCTAATGTGTGGAGTCTTACTGAAAATTTCTTCTGGAAATATT
CAAGAACGGGTGTTTTTTCTTTTCGATAATCTTTTGGTGTACTGCAAAAGAAAACACAGA
CGGTTGAAGAACAGCAAGGCATCTACAGATGGACATCGGTACCTTTTTCGTGGCCGGATC
AACACGGAGGTGATGGAAGTGGAGAATGTGGATGATGGCACCGCTGATTTCCATAGCAGT
GGACACATTGTTGTTAATGGATGGAAGATACATAACACAGCAAAAAATAAATGGTTTGTT
TGTATGGCAAAAACACCTGAAGAGAAGCATGAATGGTTTGAAGCTATTTTGAAAGAAAGA
GAACGGCGGAAAGGTTTAAAATTAGGAATGGAGCAAGATACCTGGGTCATGATCTCTGAA
CAGGGTGAGAAACTTTATAAAATGATGTGCAGACAAGGAAATCTGATCAAAGACCGAAAG
AGAAAACTGACTACGTTCCCTAAATGCTTTCTTGGAAGCGAATTTGTGTCATGGCTGTTG
GAAATTGGAGAGATTCACAGGCCTGAGGAAGGCGTGCACTTGGGACAAGCATTATTAGAA
AATGGAATCATTCACCATGTTACTGATAAACATCAATTCAAACCAGAACAGATGTTATAT
AGATTTCGCTATGATGATGGAACATTTTATCCAAGAAATGAGATGCAGGACGTGATTTCA
AAGGGTGTAAGATTATATTGTCGTCTTCATAGCCTTTTTACTCCAGTGATAAGAGATAAA
GATTACCATTTAAGGACCTACAAATCTGTGGTCATGGCCAACAAACTGATAGACTGGTTA
ATTGCACAGGGAGATTGCCGCACCAGAGAAGAGGCAATGATATTTGGCGTTGGACTCTGT
GACAATGGATTTATGCACCATGTCCTTGAAAAAAGCGAATTCAAAGATGAACCCCTACTT
TTCCGTTTTTTTTCGGATGAGGAAATGGAGGGATCAAATATGAAACATCGACTTATGAAA
CATGACTTAAAAGTTGTGGAAAATGTTATAGCTAAGTCATTATTGATTAAATCCAATGAA
GGCAGCTATGGCTTTGGATTAGAAGACAAAAATAAAGTTCCAATAATAAAGTTGGTAGAA
AAGGGATCTAATGCTGAGATGGCTGGCATGGAAGTCGGGAAAAAGATTTTTGCTATTAAT
GGTGACCTAGTTTTTATGAGACCTTTCAATGAAGTGGATTGCTTCCTGAAATCGTGTTTA
AACAGCAGAAAACCTCTAAGAGTTCTTGTGAGCACAAAGCCAAGAGAGACAGTGAAAATT
CCAGATTCAGCTGATGGACTTGGCTTCCAGATCCGGGGATTTGGCCCTTCTGTTGTGCAT
GCTGTAGGAAGAGGAACTGTGGCTGCAGCAGCTGGTCTTCACCCTGGACAGTGCATTATC
AAGGTGAATGGAATCAATGTCAGCAAAGAGACACATGCCAGTGTCATTGCACACGTTACA
GCCTGCAGGAAGTACAGGCGGCCAACGAAGCAAGATTCCATACAATGGGTTTATAATAGC
ATTGAGAGTGCTCAAGAAGACCTTCAAAAATCTCACTCCAAGCCCCCTGGAGATGAAGCA
GGGGATGCTTTTGACTGTAAAGTAGAAGAGGTTATTGACAAATTCAACACTATGGCCATC
ATTGATGGGAAGAAGGAGCATGTGAGTCTGACAGTGGACAATGTCCACCTGGAATATGGT
GTCGTGTATGAGTACGACAGCACAGCTGGCATCAAGTGCAATGTGGTGGAAAAGATGATT
GAGCCCAAAGGTTTCTTCAGCTTAACTGCCAAGATTCTTGAAGCCCTGGCTAAAAGTGAT
GAGCATTTTGTACAAAACTGTACCAGCCTAAATTCTCTAAATGAAGTGATTCCTACTGAC
CTTCAGAGTAAATTCAGTGCCCTTTGCAGTGAAAGAATTGAACACCTATGTCAGAGAATA
TCCAGTTATAAAAAGTTTTCTCGTGTACTGAAGAATAGGGCCTGGCCTACTTTTAAACAG
GCCAAATCTAAAATCTCCCCACTGCACAGCAGTGATTTCTGCCCTACCAACTGCCATGTC
AATGTGATGGAAGTTTCTTATCCCAAAACATCAACCTCTTTGGGAAGTGCATTTGGTGTT
CAGTTGGATAGCAGGAAGCATAATTCTCATGATAAAGAAAACAAATCTTCGGAGCAAGGG
AAACTGAGCCCTATGGTGTACATTCAGCACACCATCACAACCATGGCGGCCCCTTCAGGT
CTGTCTCTGGGACAGCAGGATGGCCATGGTCTCAGGTATCTGCTAAAAGAAGAAGACTTA
GAAACCCAAGACATCTATCAGAAACTGCTGGGCAAACTTCAGACTGCACTGAAAGAGGTG
GAGATGTGTGTTTGTCAAATAGATGACCTTCTGTCTTCAATAACATATTCTCCTAAATTA
GAACGTAAGACATCAGAGGGCATAATACCAACAGACAGTGACAATGAGAAGGGAGAAAGA
AACAGCAAACGGGTATGTTTTAATGTAGCAGGAGATGAACAGGAAGATTCTGGTCATGAC
ACCATCAGCAACAGAGACTCTTACAGTGACTGCAACAGCAATAGGAATTCCATCGCCTCC
TTCACCAGCATCTGCAGCAGCCAGTGCAGCTCGTATTTCCACAGTGATGAAATGGACTCA
GGTGATGAACTTCCCTTAAGTGTTCGCATATCTCATGATAAACAGGACAAGATACATAGT
TGCCTTGAGCATCTTTTCAGCCAGGTGGATTCAATTACCAATCTCCTAAAAGGGCAGGCT
GTTGTGAGGGCCTTTGACCAAACCAAGTATCTCACTCCAGGCCGAGGATTGCAAGAATTT
CAACAGGAAATGGAACCAAAGCTGAGTTGTCCAAAAAGGCTACGGCTTCATATCAAGCAA
GATCCTTGGAATCTTCCCAGCAGCGTCCGGACTCTTGCTCAGAACATCAGGAAATTTGTT
GAAGAGGTAAAGTGTAGGCTACTCCTGGCTCTTCTTGAATATTCAGATAGTGAGACACAG
CTCCGTAGAGACATGGTTTTCTGCCAGACTCTTGTGGCCACTGTCTGTGCCTTCTCTGAG
CAGCTCATGGCGGCCTTGAACCAGATGTTTGACAACAGCAAGGAAAATGAGATGGAAACT
TGGGAAGCCAGCAGGAGGTGGCTGGACCAGATAGCGAATGCAGGTGTTCTTTTTCACTTT
CAGTCACTTCTGTCACCAAACTTGACAGATGAACAAGCCATGTTAGAAGATACACTGGTT
GCACTATTTGATTTGGAAAAGGTTTCCTTTTACTTTAAACCATCAGAAGAGGAACCTCTG
GTTGCAAATGTTCCTCTTACATATCAAGCAGAAGGAAGTCGGCAAGCTCTGAAAGTTTAC
TTCTACATTGATAGTTATCATTTTGAACAACTTCCTCAACGGCTGAAAAATGGAGGAGGG
TTTAAAATTCATCCTGTTCTTTTTGCACAAGCACTAGAGAGCATGGAAGGATATTATTAC
AGAGACAATGTTTCTGTGGAAGAATTTCAAGCTCAGATAAATGCAGCCTCACTGGAAAAG
GTCAAACAGTACAACCAGAAGCTCAGGGCATTCTACTTGGACAAGTCAAATTCACCACCA
AACTCCACATCCAAAGCTGCCTATGTAGATAAGCTAATGAGGCCTCTCAACGCTTTGGAT
GAACTTTACCGACTGGTAGCCTCGTTTATCAGATCCAAGCGCACAGCTGCCTGTGCAAAC
ACAGCTTGCAGTGCTTCTGGGGTTGGACTGCTGTCAGTTTCCTCGGAGCTGTGCAACAGG
CTGGGCGCCTGCCACATCATCATGTGCAGCAGCGGTGTGCATCGGTGCACCCTGAGCGTG
ACGCTGGAGCAAGCCATCATTCTGGCCAGAAGCCACGGACTGCCACCTCGTTACATCATG
CAGGCTACAGATGTGATGCGGAAGCAGGGAGCAAGAGTTCAGAACACAGCGAAGAATTTG
GGAGTCAGAGACCGGACTCCACAGTCTGCACCAAGGCTGTACAAGCTGTGCGAGCCACCT
CCCCCAGCTGGAGAAGAATGA
Enzyme 72 GenBank Gene ID NM_024870.2 Link Image
Enzyme 72 GeneCard ID PREX2 Link Image
Enzyme 72 GenAtlas ID PREX2 Link Image
Enzyme 72 HGNC ID HGNC:22950 Link Image
Enzyme 72 Chromosome Location 8
Enzyme 72 Locus 8q13.2
Enzyme 72 SNPs SNPJam Report Link Image
Enzyme 72 General References
  1. Donald S, Hill K, Lecureuil C, Barnouin R, Krugmann S, John Coadwell W, Andrews SR, Walker SA, Hawkins PT, Stephens LR, Welch HC: P-Rex2, a new guanine-nucleotide exchange factor for Rac. FEBS Lett. 2004 Aug 13;572(1-3):172-6. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed Link Image]
  4. Rosenfeldt H, Vazquez-Prado J, Gutkind JS: P-REX2, a novel PI-3-kinase sensitive Rac exchange factor. FEBS Lett. 2004 Aug 13;572(1-3):167-71. [PubMed Link Image]
  5. Joseph RE, Norris FA: Substrate specificity and recognition is conferred by the pleckstrin homology domain of the Dbl family guanine nucleotide exchange factor P-Rex2. J Biol Chem. 2005 Jul 29;280(30):27508-12. Epub 2005 May 16. [PubMed Link Image]
  6. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 72 Metabolite References Not Available
Enzyme 73 [top]
Enzyme 73 ID 14062
Enzyme 73 Name Dedicator of cytokinesis protein 10
Enzyme 73 Synonyms
  1. Zizimin-3
Enzyme 73 Gene Name DOCK10
Enzyme 73 Protein Sequence >Dedicator of cytokinesis protein 10
MAGERTRRFTRSLLRPGQAAELRHSAASAAAVAVSSRQQQRQEKPRLLEPLDYETVIEEL
EKTYRNDPLQDLLFFPSDDFSAATVSWDIRTLYSTVPEDAEHKAENLLVKEACKFYSSQW
HVVNYKYEQYSGDIRQLPRAEYKPEKLPSHSFEIDHEDADKDEDTTSHSSSKGGGGAGGT
GVFKSGWLYKGNFNSTVNNTVTVRSFKKRYFQLTQLPDNSYIMNFYKDEKISKEPKGCIF
LDSCTGVVQNNRLRKYAFELKMNDLTYFVLAAETESDMDEWIHTLNRILQISPEGPLQGR
RSTELTDLGLDSLDNSVTCECTPEETDSSENNLHADFAKYLTETEDTVKTTRNMERLNLF
SLDPDIDTLKLQKKDLLEPESVIKPFEEKAAKRIMIICKALNSNLQGCVTENENDPITNI
EPFFVSVALYDLRDSRKISADFHVDLNHAAVRQMLLGASVALENGNIDTITPRQSEEPHI
KGLPEEWLKFPKQAVFSVSNPHSEIVLVAKIEKVLMGNIASGAEPYIKNPDSNKYAQKIL
KSNRQFCSKLGKYRMPFAWAVRYVFKDNQGNVDRDSRFSPLFRQESSKISTEDLVKLVSD
YRRADRISKMQTIPGSLDIAVDNVPLEHPDCVTSSFIPVKPFNMMAQTEPTVEVEEFVYD
STKYCRPYRVYKNQIYIYPKHLKYDSQKCFNKARNITVCIEFKNSDEESAKPLKCIYGKP
GGPLFTSAAYTAVLHHSQNPDFSDEVKIELPTQLHEKHHILFSFYHVTCDINAKANAKKK
EALETSVGYAWLPLMKHDQIASQEYNIPIATSLPPNYLSFQDSASHGGSDIKWVDGGKPL
FKVSTFVVSTVNTQDPHVNAFFQECQKREKDMSQSPTSNFIRSCKNLLNVEKIHAIMSFL
PIILNQLFKVLVQNEEDEITTTVTRVLTDIVAKCHEEQLDHSVQSYIKFVFKTRACKERT
VHEELAKNVTGLLKSNDSTTVKHVLEHSWFFFAIILKSMAQHLIDTNKIQLPRPQRFPES
YQNELDNLVMVLSDHVIWKYKDALEETRRANHSVARFLKRCFTFMDRGYVFKMVNNYISM
FSSGDFQTLCQYKFDFLQEVCQHEHFIPLCLPIRSANIPDPLTPSESTQELHASDMPEYS
VTNEFCRKHFLIGILLREVGFALQEDQDVRHLALAVLKNLMAKHSFDDRYRERKQAQIAS
LYMPLYGMLLDNMPRIYLKDLYPFTVNTSNQGSRDDLSTNGGFQSQTAIKHANSVDTSFS
KDVLNSIAAFSSIAISTVNHADSRASLASLDSNPSTNEKSSEKTDNCEKVPRPLSLIGST
LRFDKLDQAETRSLLMCFLHIMKTISDETLIAYWQRAPSPEVSDFFSILEVCLQNFRYLG
KRNIIRKIAAAFKFVQSTQNNGTLKGSNPSCQTSGLLSQWMHSTSSHEGHKQHRSQTLPI
IRGKNALSNPKLLQMLDNTMTSNSNEIDIVHHVDTEANIATEVCLTILDLLSLFTQTHQR
QLQQCDCQNSLMKRVFDTYMLFFQVNQSATALKHVFASLRLFVCKFPSAFFQGPADLCGS
FCYEVLKCCNHRSRSTQTEASALLYFFMRKNFEFNKQKSIVRSHLQLIKAVSQLIADAGI
GGSRFQHSLAITNNFANGDKQMKNSNFPAEVKDLTKRIRTVLMATAQMKEHEKDPEMLVD
LQYSLANSYASTPELRRTWLESMAKIHARNGDLSEAAMCYIHIAALIAEYLKRKGYWKVE
KICTASLLSEDTHPCDSNSLLTTPSGGSMFSMGWPAFLSITPNIKEEGAMKEDSGMQDTP
YNENILVEQLYMCVEFLWKSERYELIADVNKPIIAVFEKQRDFKKLSDLYYDIHRSYLKV
AEVVNSEKRLFGRYYRVAFYGQGFFEEEEGKEYIYKEPKLTGLSEISQRLLKLYADKFGA
DNVKIIQDSNKVNPKDLDPKYAYIQVTYVTPFFEEKEIEDRKTDFEMHHNINRFVFETPF
TLSGKKHGGVAEQCKRRTILTTSHLFPYVKKRIQVISQSSTELNPIEVAIDEMSKKVSEL
NQLCTMEEVDMIRLQLKLQGSVSVKVNAGPMAYARAFLEETNAKKYPDNQVKLLKEIFRQ
FADACGQALDVNERLIKEDQLEYQEELRSHYKDMLSELSTVMNEQITGRDDLSKRGVDQT
CTRVISKATPALPTVSISSSAEV
Enzyme 73 Number of Residues 2183
Enzyme 73 Molecular Weight 249310.2
Enzyme 73 Theoretical pI 6.93
Enzyme 73 GO Classification
Function
  • GTP binding
  • GTPase binding
  • GTPase regulator activity
  • binding
  • enzyme binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
Process
Component
Enzyme 73 General Function Involved in guanyl-nucleotide exchange factor activity
Enzyme 73 Specific Function Potential guanine nucleotide exchange factor (GEF). GEF proteins activate some small GTPases by exchanging bound GDP for free GTP
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 154146189 Link Image
Enzyme 73 UniProtKB/Swiss-Prot ID Q96BY6 Link Image
Enzyme 73 UniProtKB/Swiss-Prot Entry Name DOC10_HUMAN Link Image
Enzyme 73 PDB ID Not Available
Enzyme 73 Cellular Location Not Available
Enzyme 73 Gene Sequence >6561 bp
ATGGCCGGTGAGCGGACCCGCAGGTTCACCCGGAGCCTGTTGAGACCTGGGCAGGCGGCC
GAGCTCCGGCACAGCGCCGCGTCCGCCGCCGCGGTGGCAGTCAGCAGCCGGCAGCAGCAG
CGGCAAGAAAAGCCTAGGCTTCTCGAGCCTTTGGATTATGAGACTGTCATTGAAGAACTT
GAAAAGACCTACCGGAATGATCCTCTTCAAGATCTCTTGTTCTTCCCCAGTGATGACTTT
TCAGCAGCCACAGTTTCCTGGGATATCCGCACGTTGTACTCAACAGTACCTGAAGATGCA
GAGCACAAGGCAGAAAATTTACTGGTTAAGGAGGCTTGTAAATTTTATAGTTCCCAGTGG
CATGTGGTAAACTACAAATATGAACAATATTCTGGAGACATTCGACAGCTACCCCGAGCA
GAATACAAACCAGAGAAGCTTCCTTCACATTCCTTTGAGATTGACCATGAAGATGCTGAT
AAGGATGAAGATACCACTTCCCACTCGTCTTCCAAGGGGGGTGGAGGAGCGGGAGGAACT
GGTGTTTTCAAGTCCGGCTGGCTCTACAAGGGGAATTTTAACAGCACCGTGAACAACACC
GTTACTGTTCGGTCATTCAAAAAGCGCTACTTCCAGCTGACTCAGTTACCAGATAACTCC
TACATTATGAACTTTTACAAAGATGAGAAAATATCCAAAGAACCCAAAGGATGCATCTTT
TTGGATTCCTGTACAGGAGTGGTGCAGAATAACAGACTAAGAAAATATGCCTTTGAATTG
AAAATGAATGATCTGACCTATTTTGTGCTGGCAGCTGAAACAGAGTCAGATATGGATGAA
TGGATCCACACCCTCAACCGCATTCTGCAAATCAGTCCTGAGGGGCCCCTCCAAGGGAGG
AGGAGCACAGAGCTCACTGATCTGGGTCTGGATTCGCTGGATAATTCTGTAACTTGTGAA
TGCACGCCAGAGGAAACAGATTCTTCAGAGAACAACCTACACGCAGACTTTGCAAAGTAC
CTCACAGAAACAGAAGATACTGTAAAAACAACTCGAAACATGGAGAGGCTAAATCTGTTC
TCTCTAGATCCAGACATAGATACCTTGAAACTTCAAAAAAAAGATCTCTTGGAACCTGAG
TCTGTGATCAAACCATTTGAAGAAAAAGCTGCCAAGAGAATCATGATCATCTGTAAAGCC
CTCAACTCAAATCTTCAGGGATGTGTTACGGAGAATGAAAATGATCCGATAACGAATATT
GAGCCTTTTTTTGTGAGTGTGGCACTTTATGACCTCAGAGACAGCAGGAAGATTTCTGCT
GATTTTCATGTGGATCTAAACCATGCTGCTGTCAGACAGATGCTCTTGGGGGCTTCTGTG
GCTTTGGAAAATGGCAACATCGACACCATCACTCCAAGACAATCAGAAGAACCTCACATC
AAGGGACTTCCAGAGGAATGGCTAAAATTTCCAAAGCAGGCTGTATTTTCTGTAAGCAAT
CCACATTCTGAAATTGTTTTGGTGGCCAAAATCGAAAAAGTCTTGATGGGAAACATTGCA
AGTGGTGCCGAACCTTATATTAAGAACCCAGACTCCAACAAGTATGCACAAAAGATACTA
AAATCCAACAGACAATTCTGCAGCAAATTGGGAAAATACCGTATGCCTTTTGCTTGGGCA
GTAAGATCAGTATTTAAGGACAACCAGGGAAATGTGGACAGAGACTCAAGATTTTCACCA
TTGTTTAGACAAGAAAGTAGCAAGATTTCAACTGAGGACCTAGTTAAACTAGTATCAGAT
TATAGAAGGGCCGACAGAATAAGCAAAATGCAGACCATTCCTGGAAGCCTGGATATTGCT
GTTGACAACGTTCCCTTGGAGCATCCAAATTGTGTAACATCGTCCTTTATCCCTGTCAAG
CCTTTCAACATGATGGCTCAAACAGAACCCACAGTGGAGGTGGAAGAATTTGTTTACGAT
TCAACAAAGTATTGTCGGCCTTACAGAGTATATAAAAATCAAATTTATATTTACCCCAAA
CACCTCAAGTATGATAGCCAGAAATGCTTCAACAAGGCACGGAATATAACTGTGTGCATT
GAATTCAAAAATTCAGATGAAGAAAGTGCCAAGCCCCTGAAGTGTATTTATGGAAAACCT
GGAGGGCCCCTCTTCACCTCAGCCGCCTACACAGCAGTTCTGCACCACTCTCAGAATCCG
GATTTCTCAGATGAGGTGAAAATTGAGCTACCAACACAACTCCATGAGAAACACCATATT
TTGTTTTCTTTTTATCACGTCACCTGTGACATCAATGCAAAAGCTAATGCCAAAAAGAAG
GAGGCTCTGGAAACGTCAGTTGGATATGCTTGGCTTCCTCTGATGAAACACGATCAGATA
GCTTCTCAAGAGTACAACATCCCAATAGCAACAAGTCTGCCTCCTAATTATTTAAGCTTT
CAAGATTCTGCAAGTGGAAAGCATGGTGGGAGTGACATTAAATGGGTTGATGGTGGCAAA
CCACTTTTCAAAGTGTCGACATTTGTTGTATCAACAGTAAATACTCAGGATCCACATGTG
AATGCATTTTTCCAAGAGTGCCAAAAAAGAGAGAAAGATATGTCTCAGTCACCTACCTCA
AATTTCATCCGCTCTTGTAAGAACTTATTGAATGTGGAAAAGATTCATGCAATCATGAGT
TTTCTGCCTATAATTTTGAATCAGCTCTTCAAAGTTCTGGTACAGAATGAGGAAGATGAA
ATAACTACAACTGTCACCAGGGTTCTGACCGACATTGTGGCCAAGTGCCATGAGGAGCAG
CTGGATCATTCTGTCCAGTCATATATTAAGTTCGTGTTCAAGACCAGGGCATGCAAGGAG
AGGACTGTACATGAGGAACTGGCTAAAAATGTGACTGGTCTTTTGAAATCAAATGACTCA
ACAACAGTAAAGCATGTCCTAAAGCATTCCTGGTTCTTCTTTGCAATTATCCTAAAATCG
ATGGCACAGCACTTGATTGACACAAATAAAATCCAGCTTCCCCGGCCTCAGAGATTTCCT
GAATCTTACCAAAATGAATTGGACAATCTTGTCATGGTCCTATCCGACCATGTGATTTGG
AAATACAAGGATGCACTTGAAGAAACAAGAAGGGCAAACCACAGCGTTGCCAGATTTCTC
AAGCGCTGCTTTACATTTATGGACCGAGGGTATGTGTTTAAGATGGTCAACAATTACATC
AGCATGTTCTCCTCCGGTGACCTTAAGACCTTGTGCCAGTATAAATTTGATTTTCTTCAA
GAAGTATGTCAACATGAACACTTTATCCCTTTGTGTCTGCCCATAAGATCAGCAAACATT
CCAGATCCTTTGACACCTTCAGAATCGACTCAAGAGTTACATGCATCAGATATGCCTGAA
TATTCAGTCACAAATGAATTTTGTCGCAAACACTTCTTAATCGGAATTCTGCTCCGAGAA
GTTGGCTTTGCCCTGCAGGAAGACCAAGATGTCAGACACTTAGCTTTAGCTGTCCTAAAA
AATCTAATGGCTAAGCATTCATTTGATGATCGATACAGAGAGCCAAGAAAGCAGGCCCAG
ATAGCAAGTTTATACATGCCCCTGTACGGCATGCTCCTGGACAATATGCCAAGGATTTAT
CTGAAGGACCTGTATCCTTTTACTGTCAATACATCTAATCAGGGGTCTAGAGATGATCTA
AGCACCAATGGAGGATTTCAAAGCCAGACAGCTATCAAACATGCAAACTCTGTGGATACA
TCATTTTCTAAAGATGTTTTAAATTCCATAGCAGCATTTTCATCAATAGCTATTTCTACA
GTAAACCATGCTGACTCCAGAGCATCTTTAGCAAGTCTTGACTCCAATCCAAGTACCAAT
GAGAAGAGCAGTGAGAAGACGGACAACTGTGAAAAGATCCCAAGACCCTTGTCTTTGATT
GGCTCAACTCTTCGATTTGACAAGTTAGATCAAGCAGAAACCAGGAGTCTCCTGATGTGT
TTTCTTCACATTATGAAAACGATTTCGTACGAGACTCTGATTGCCTACTGGCAGAGAGCT
CCCAGCCCAGAGGTGTCCGACTTCTTCAGCATCTTGGACGTTTGTCTTCAAAATTTCAGA
TACCTAGGAAAACGCAACATAATAAGAAAAATTGCTGCTGCATTTAAATTTGTGCAGTCC
ACCCAGAACAATGGAACTCTCAAAGGATCCAATCCTTCCTGCCAGACATCAGGTCTCTTG
TCACAATGGATGCACTCCACTTCCAGTCATGAAGGCCATAAGCAGCACAGATCACAAACT
TTACCTATAATTCGAGGCAAAAATGCACTTTCTAACCCCAAACTCTTACAGATGTTAGAC
AATACCATGACCAGCAACTCCAATGAAATAGACATCGTGCATCATGTAGACACTGAGGCC
AATATAGCTACGGAGGTTTGCCTCACTATTCTGGACCTGTTATCCCTCTTCACACAGACT
CATCAGAGACAACTCCAACAATGTGACTGTCAAAATTCATTGATGAAAAGGGTCTTTGAT
ACCTACATGCTCTTTTTCCAAGTCAATCAGTCAGCCACAGCGCTGAAGCATGTGTTTGCC
TCCTTGAGACTGTTTGTATGCAAGTTTCCTTCAGCGTTCTTTCAAGGGCCTGCTGACCTC
TGTGGATCATTCTGTTACGAAGTCCTAAAATGCTGTAACCACAGGTCACGGTCAACTCAG
ACAGAAGCCTCAGCCCTTCTGTACTTTTTCATGAGGAAGAATTTTGAATTTAACAAGCAG
AAGTCAATTGTCCGGTCCCACTTACAACTCATCAAAGCTGTGAGCCAGTTAATAGCCGAT
GCTGGGATTGGAGGCTCTCGGTTTCAACATTCGCTTGCAATTACCAATAATTTCGCCAAT
GGAGATAAGCAAATGAAAAACAGCAATTTCCCAGCAGAGGTGAAGGACCTGACTAAGCGT
ATAAGGACTGTTTTGATGGCCACAGCTCAGATGAAGGAGCACGAGAAGGACCCCGAGATG
CTGGTGGATCTCCAGTACAGCCTGGCAAACTCCTACGCAAGCACTCCTGAACTACGCAGG
ACCTGGCTGGAAAGTATGGCCAAGATTCATGCCAGAAACGGAGATTTATCTGAGGCTGCC
ATGTGTTACATCCATATTGCTGCTCTCATTGCAGAGTATCTGAAAAGAAAGGGTTACTGG
AAAGTGGAAAAGATTTGCACAGCATCCCTGCTCTCGGAGGATACCCACCCCTGTGATAGC
AACTCATTACTAACAACTCCCAGTGGAGGAAGCATGTTCTCTATGGGATGGCCAGCTTTT
TTGAGCATTACACCAAACATTAAGGAAGAAGGAGCGATGAAAGAGGATTCTGGAATGCAA
GATACACCATACAATGAGAATATCCTGGTGGAGCAGCTATACATGTGTGTGGAGTTTCTC
TGGAAGTCTGAGCGATATGAACTCATTGCTGATGTCAACAAGCCCATCATTGCTGTCTTT
GAGAAACAACGAGACTTCAAAAAATTGTCAGATCTCTACTACGACATTCATCGGTCATAT
CTGAAAGTGGCAGAGGTGGTGAATTCGGAGAAGCGGCTGTTTGGTCGCTACTATCGTGTG
GCATTTTATGGGCAGGGCTTTTTTGAAGAAGAAGAAGGTAAAGAGTATATTTATAAAGAG
CCTAAGCTGACAGGTCTGTCCGAGATTTCCCAAAGATTACTCAAGCTCTATGCAGATAAA
TTTGGAGCAGACAATGTGAAGATAATCCAGGATTCCAACAAGGTAAACCCCAAGGATTTG
GACCCCAAATATGCCTACATCCAGGTGACCTATGTGACGCCGTTCTTTGAGGAAAAGGAA
ATCGAAGACCGGAAGACAGATTTCGAAATGCACCACAACATCAACCGCTTTGTCTTCGAG
ACACCCTTCACGCTGTCGGGCAAGAAGCACGGTGGGGTGGCGGAGCAGTGCAAGCGGCGG
ACGATCCTGACAACGAGTCACCTGTTCCCCTACGTGAAGAAGAGAATACAAGTAATTAGC
CAATCGAGCACAGAACTGAATCCAATTGAAGTGGCAATTGACGAGATGTCCAAGAAGGTT
TCTGAGCTTAATCAGCTTTGCACAATGGAAGAAGTGGACATGATCAGACTGCAGCTCAAA
CTGCAAGGAAGTGTCAGCGTGAAGGTTAATGCTGGGCCAATGGCCTATGCACGAGCTTTT
CTTGAAGAAACCAATGCAAAGAAGTACCCTGACAACCAAGTAAAGCTTTTGAAGGAGATC
TTCAGGCAATTTGCAGATGCATGTGGGCAGGCCCTTGACGTGAATGAGCGCCTCATCAAA
GAGGACCAGCTGGAGTACCAGGAAGAACTGAGGTCCCACTACAAGGACATGCTCAGCGAA
CTCTCCACAGTCATGAATGAGCAGATTACGGGCAGGGACGACCTGTCAAAGCGCGGAGTG
GACCAAACCTGCACTCGAGTAATTAGCAAAGCAACTCCGGCCCTACCCACGGTCTCCATC
TCATCTAGTGCTGAAGTCTGA
Enzyme 73 GenBank Gene ID Not Available
Enzyme 73 GeneCard ID DOCK10 Link Image
Enzyme 73 GenAtlas ID DOCK10 Link Image
Enzyme 73 HGNC ID HGNC:23479 Link Image
Enzyme 73 Chromosome Location 2
Enzyme 73 Locus 2q36.2
Enzyme 73 SNPs SNPJam Report Link Image
Enzyme 73 General References
  1. Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Jun 30;5(3):169-76. [PubMed Link Image]
  2. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Cote JF, Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J Cell Sci. 2002 Dec 15;115(Pt 24):4901-13. [PubMed Link Image]
  7. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  8. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  9. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  10. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 73 Metabolite References Not Available
Enzyme 74 [top]
Enzyme 74 ID 14064
Enzyme 74 Name Dedicator of cytokinesis protein 1
Enzyme 74 Synonyms
  1. 180 kDa protein downstream of CRK
  2. DOCK180
Enzyme 74 Gene Name DOCK1
Enzyme 74 Protein Sequence >Dedicator of cytokinesis protein 1
MTRWVPTKREEKYGVAFYNYDARGADELSLQIGDTVHILETYEGWYRGYTLRKKSKKGIF
PASYIHLKEAIVEGKGQHETVIPGDLPLIQEVTTTLREWSTIWRQLYVQDNREMFRSVRH
MIYDLIEWRSQILSGTLPQDELKELKKKVTAKIDYGNRILDLDLVVRDEDGNILDPELTS
TISLFRAHEIASKQVEERLQEEKSQKQNIDINRQAKFAATPSLALFVNLKNVVCKIGEDA
EVLMSLYDPVESKFISENYLVRWSSSGLPKDIDRLHNLRAVFTDLGSKDLKREKISFVCQ
IVRVGRMELRDNNTRKLTSGLRRPFGVAVMDVTDIINGKVDDEDKQHFIPFQPVAGENDF
LQTVINKVIAAKEVNHKGQGLWVTLKLLPGDIHQIRKEFPHLVDRTTAVARKTGFPEIIM
PGDVRNDIYVTLVQGDFDKGSKTTAKNVEVTVSVYDEDGKRLEHVIFPGAGDEAISEYKS
VIYYQVKQPRWFETVKVAIPIEDVNRSHLRFTFRHRSSQDSKDKSEKIFALAFVKLMRYD
GTTLRDGEHDLIVYKAEAKKLEDAATYLSLPSTKAELEEKGHSATGKSMQSLGSCTISKD
SFQISTLVCSTKLTQNVDLLGLLKWRSNTSLLQQNLRQLMKVDGGEVVKFLQDTLDALFN
IMMENSESETFDTLVFDALVFIIGLIADRKFQHFNPVLETYIKKHFSATLAYTKLTKVLK
NYVDGAEKPGVNEQLYKAMKALESIFKFIVRSRILFNQLYENKGEADFVESLLQLFRSIN
DMMSSMSDQTVRVKGAALKYLPTIVNDVKLVFDPKELSKMFTEFILNVPMGLLTIQKLYC
LIEIVHSDLFTQHDCREILLPMMTDQLKYHLERQEDLEACCQLLSHILEVLYRKDVGPTQ
RHVQIIMEKLLRTVNRTVISMGRDSELIGNFVACMTAILRQMEDYHYAHLIKTFGKMRTD
VVDFLMETFIMFKNLIGKNVYPFDWVIMNMVQNKVFLRAINQYADMLNKKFLDQANFELQ
LWNNYFHLAVAFLTQESLQLENFSSAKRAKILNKYGDMRRQIGFEIRDMWYNLGQHKIKF
IPEMVGPILEMTLIPETELRKATIPIFFDMMQCEFHSTRSFQMFENEIITKLDHEVEGGR
GDEQYKVLFDKILLEHCRKHKYLAKTGETFVKLVVRLMERLLDYRTIMHDENKENRMSCT
VNVLNFYKEIEREEMYIRYLYKLCDLHKECDNYTEAAYTLLLHAKLLKWSEDVCVAHLTQ
RDGYQATTQGQLKEQLYQEIIHYFDKGKMWEEAIALGKELAEQYENEMFDYEQLSELLKK
QAQFYENIVKVIRPKPDYFAVGYYGQGFPTFLRGKVFIYRGKEYERREDFEARLLTQFPN
AEKMKTTSPPGDDIKNSPGQYIQCFTVKPKLDLPPKFHRPVSEQIVSFYRVNEVQRFEYS
RPIRKGEKNPDNEFANMWIERTIYTTAYKLPGILRWFEVKSVFMVEISPLENAIETMQLT
NDKINSMVQQHLDDPSLPINPLSMLLNGIVDPAVMGGFANYEKAFFTDRYLQEHPEAHEK
IEKLKDLIAWQIPFLAEGIRIHGDKVTEALRPFHERMEACFKQLKEKVEKEYGVRIMPSS
LDDRRGSRPRSMVRSFTMPSSSRPLSVASVSSLSSDSTPSRPGSDGFALEPLLPKKMHSR
SQDKLDKDDLEKEKKDKKKEKRNSKHQEIFEKEFKPTDISLQQSEAVILSETISPLRPQR
PKSQVMNVIGSERRFSVSPSSPSSQQTPPPVTPRAKLSFSMQSSLELNGMTGADVADVPP
PLPLKGSVADYGNLMENQDLLGSPTPPPPPPHQRHLPPPLPSKTPPPPPPKTTRKQASVD
SGIVQ
Enzyme 74 Number of Residues 1865
Enzyme 74 Molecular Weight 215344.1
Enzyme 74 Theoretical pI 7.61
Enzyme 74 GO Classification
Function
  • GTP binding
  • GTPase binding
  • GTPase regulator activity
  • binding
  • enzyme binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
Process
Component
Enzyme 74 General Function Involved in guanyl-nucleotide exchange factor activity
Enzyme 74 Specific Function Involved in cytoskeletal rearrangements required for phagocytosis of apoptotic cells and cell motility. Functions as a guanine nucleotide exchange factor (GEF), which activates Rac Rho small GTPases by exchanging bound GDP for free GTP. Its GEF activity may be enhanced by ELMO1
Enzyme 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 122889127 Link Image
Enzyme 74 UniProtKB/Swiss-Prot ID Q14185 Link Image
Enzyme 74 UniProtKB/Swiss-Prot Entry Name DOCK1_HUMAN Link Image
Enzyme 74 PDB ID Not Available
Enzyme 74 Cellular Location Not Available
Enzyme 74 Gene Sequence >5598 bp
ATGACGCGCTGGGTGCCCACCAAGCGCGAGGAGAAGTACGGCGTGGCTTTTTATAACTAT
GATGCCAGAGGAGCGGATGAACTTTCTTTACAGATCGGAGACACTGTGCACATCTTAGAA
ACATATGAAGGGTGGTACCGAGGTTACACGTTACGAAAAAAGTCTAAGAAGGGTATATTT
CCTGCTTCATATATTCATCTTAAAGAAGCGATAGTTGAAGGAAAAGGGCAACATGAAACA
GTCATCCCGGGTGACCTCCCCCTCATCCAGGAAGTCACCACGACACTCCGAGAGTGGTCC
ACCATCTGGAGGCAGCTCTACGTGCAAGATAACAGGGAGATGTTTCGAAGTGTGCGGCAC
ATGATCTATGACCTTATTGAATGGCGATCACAAATTCTTTCTGGAACTCTGCCTCAGGAT
GAACTCAAAGAACTGAAGAAGAAGGTCACAGCCAAAATTGATTATGGAAACAGAATTCTA
GATTTGGACCTGGTGGTTAGAGATGAAGATGGGAATATTTTGGATCCAGAATTAACTAGC
ACGATTAGTCTCTTCAGAGCTCATGAAATAGCTTCTAAACAAGTGGAGGAAAGGTTACAA
GAGGAAAAATCTCAAAAGCAGAACATAGATATTAACAGACAAGCCAAGTTTGCTGCAACC
CCTTCTCTGGCCTTGTTTGTGAACCTCAAAAATGTGGTTTGTAAAATAGGAGAAGATGCT
GAAGTCCTCATGTCTCTATATGACCCTGTGGAGTCCAAATTCATCAGTGAGAACTACCTG
GTTCGCTGGTCCAGTTCAGGATTACCTAAAGACATAGACAGATTACATAATTTGCGAGCC
GTGTTTACTGACCTCGGAAGCAAAGACCTGAAAAGGGAGAAAATCAGTTTTGTCTGTCAG
ATTGTTCGCGTGGGTCGCATGGAGCTGAGGGACAACAACACCAGGAAACTGACCTCGGGG
TTGCGGCGACCTTTTGGAGTGGCTGTGATGGATGTAACAGATATAATAAATGGAAAAGTA
GATGATGAAGATAAGCAGCATTTCATTCCCTTTCAGCCGGTGGCAGGGGAGAATGACTTC
CTTCAGACTGTTATAAACAAAGTCATCGCTGCCAAAGAAGTCAACCACAAGGGGCAGGGT
TTGTGGGTAACATTGAAATTACTTCCTGGAGATATCCATCAGATCCGAAAAGAGTTTCCG
CATTTAGTGGACAGGACCACAGCTGTGGCTCGAAAAACAGGGTTTCCGGAGATAATCATG
CCTGGTGATGTTCGAAATGATATCTATGTAACATTAGTTCAAGGAGATTTTGATAAAGGA
AGCAAAACAACAGCGAAGAACGTGGAGGTCACGGTGTCTGTGTACGATGAGGATGGGAAA
CGATTAGAGCATGTGATTTTCCCGGGTGCTGGTGATGAAGCGATTTCAGAGTACAAATCT
GTGATTTACTACCAAGTAAAGCAGCCACGCTGGTTTGAGACTGTTAAGGTGGCCATTCCC
ATCGAGGACGTTAACCGCAGTCACCTTCGGTTTACCTTCCGCCACAGGTCATCACAGGAC
TCTAAGGATAAATCTGAGAAAATATTTGCACTAGCATTTGTCAAGCTGATGAGATACGAT
GGTACCACCCTGCGAGACGGAGAGCACGATCTTATCGTCTATAAGGCCGAAGCAAAGAAG
CTGGAAGATGCTGCCACGTACTTGAGTCTGCCCTCCACGAAGGCAGAGTTGGAAGAAAAG
GGCCACTCGGCCACCGGCAAGAGCATGCAGAGCCTTGGGAGCTGCACCATTAGCAAGGAC
TCCTTCCAGATCTCCACGCTCGTGTGCTCCACCAAACTGACTCAGAACGTGGACCTTCTG
GGGCTCTTGAAATGGCGCTCCAACACCAGCCTGCTGCAGCAGAACTTGAGGCAGCTGATG
AAAGTCGATGGTGGTGAAGTAGTGAAGTTTCTTCAGGACACGTTGGATGCCCTCTTCAAC
ATCATGATGGAGAACTCAGAGAGTGAGACTTTTGACACGTTAGTCTTTGATGCTCTGGTA
TTTATCATTGGACTGATTGCTGATAGAAAATTTCAGCATTTTAATCCTGTTTTGGAAACT
TACATTAAGAAACACTTTAGTGCAACGTTAGCCTACACGAAGTTGACAAAAGTGTTGAAG
AACTACGTGGACGGTGCTGAGAAGCCGGGAGTAAATGAGCAGCTGTACAAAGCCATGAAA
GCGCTAGAATCCATCTTCAAGTTCATCGTGCGCTCCAGGATCCTGTTCAATCAACTGTAT
GAAAACAAGGGAGAGGCTGACTTCGTGGAATCTTTGCTGCAGCTCTTCAGGTCCATCAAT
GACATGATGAGCAGCATGTCAGACCAGACCGTCCGGGTGAAGGGGGCAGCACTGAAATAC
TTACCAACGATCGTCAACGATGTGAAATTGGTGTTTGATCCCAAAGAGCTCAGCAAAATG
TTTACTGAATTCATCCTCAATGTTCCCATGGGCTTGCTGACCATCCAGAAACTCTACTGC
TTGATCGAAATCGTCCACAGTGACCTCTTCACACAGCATGACTGCAGAGAGATCCTGCTT
CCCATGATGACCGATCAGCTCAAGTACCATCTGGAGAGACAGGAGGACCTGGAGGCCTGC
TGTCAGCTGCTCAGCCACATCCTGGAGGTGCTGTACAGGAAGGACGTGGGGCCAACCCAG
AGGCACGTCCAGATTATCATGGAGAAACTTCTCCGGACCGTGAACCGAACCGTCATTTCC
ATGGGACGAGATTCTGAACTCATTGGAAACTTCGTGGCTTGCATGACAGCTATTTTACGA
CAAATGGAAGATTACCATTATGCCCACTTGATCAAGACTTTTGGGAAAATGAGGACTGAT
GTGGTAGATTTCCTAATGGAAACATTCATCATGTTTAAGAACCTCATTGGAAAGAACGTT
TACCCCTTCGACTGGGTGATCATGAACATGGTGCAAAATAAAGTCTTCCTGCGAGCAATT
AATCAGTATGCAGATATGCTGAACAAAAAATTTCTGGATCAAGCCAACTTTGAGCTACAG
CTGTGGAACAACTACTTTCACCTGGCTGTTGCTTTCCTTACTCAAGAGTCCCTGCAACTG
GAGAATTTTTCAAGTGCCAAGAGAGCCAAAATCCTTAACAAGTACGGAGATATGAGGAGA
CAGATTGGCTTTGAAATCAGAGACATGTGGTACAACCTTGGTCAACACAAGATAAAGTTC
ATTCCAGAAATGGTGGGCCCAATATTAGAAATGACATTAATTCCCGAGACGGAGCTGCGC
AAAGCCACCATCCCCATCTTCTTTGATATGATGCAGTGTGAATTCCATTCGACCCGAAGC
TTCCAAATGTTTGAAAATGAGATCATCACCAAGCTGGATCATGAAGTCGAAGGAGGCAGA
GGAGACGAACAGTACAAAGTGTTATTTGATAAAATCCTTCTGGAACACTGCAGGAAGCAC
AAATACCTCGCCAAAACAGGAGAAACTTTTGTAAAACTCGTTGTGCGCTTAATGGAAAGG
CTTTTGGATTATAGAACCATCATGCACGACGAGAACAAAGAAAACCGCATGAGCTGCACC
GTCAATGTGCTGAATTTCTACAAAGAAATTGAAAGAGAAGAAATGTATATAAGGTATTTG
TACAAGCTCTGTGACCTGCACAAGGAGTGTGATAACTACACCGAAGCGGCTTACACCTTG
CTTCTCCATGCAAAGCTTCTTAAGTGGTCGGAGGATGTGTGTGTGGCCCACCTCACCCAG
CGGGACGGGTACCAGGCCACCACGCAGGGACAGCTGAAGGAGCAGCTCTACCAGGAAATC
ATCCACTACTTCGACAAAGGCAAGATGTGGGAGGAGGCCATTGCCTTGGGCAAGGAGCTA
GCCGAGCAGTATGAGAACGAAATGTTTGATTATGAGCAACTCAGCGAATTGCTGAAAAAA
CAGGCTCAGTTTTATGAAAACATCGTCAAAGTGATCAGGCCCAAGCCTGACTATTTTGCT
GTTGGCTACTACGGACAAGGGTTCCCCACATTCCTGCGGGGAAAAGTTTTCATTTACCGA
GGGAAAGAGTATGAGCGCCGGGAAGATTTTGAGGCTCGGCTCTTAACTCAGTTTCCAAAC
GCCGAGAAAATGAAGACAACATCTCCACCAGGCGACGATATTAAAAACTCTCCTGGCCAG
TATATTCAGTGCTTCACAGTGAAGCCCAAACTCGATCTGCCTCCTAAGTTTCACAGGCCA
GTGTCAGAGCAGATTGTAAGTTTTTACAGGGTGAACGAGGTCCAGCGATTTGAATATTCT
CGGCCAATCCGGAAGGGAGAGAAAAACCCAGACAATGAATTTGCGAATATGTGGATCGAG
AGAACCATATATACAACTGCATATAAATTACCTGGAATTTTAAGGTGGTTTGAGGTCAAG
TCTGTTTTCATGGTGGAAATCAGCCCCCTGGAGAATGCCATTGAGACCATGCAGCTGACG
AACGACAAGATCAACAGCATGGTGCAGCAGCACCTGGATGACCCCAGCCTGCCCATCAAC
CCGCTCTCCATGCTCCTGAACGGCATCGTGGACCCAGCTGTCATGGGGGGCTTCGCAAAC
TACGAAAAGGCCTTCTTTACAGACCGGTACCTGCAGGAGCACCCTGAGGCCCATGAAAAG
ATCGAGAAGCTCAAGGACCTGATTGCTTGGCAGATTCCTTTTCTGGCCGAAGGGATCAGA
ATCCATGGAGACAAAGTCACGGAGGCACTGAGGCCGTTCCACGAGAGGATGGAGGCCTGT
TTCAAACAGCTGAAGGAAAAGGTGGAGAAAGAGTACGGCGTCCGAATCATGCCCTCAAGT
CTGGATGATAGAAGAGGCAGCCGCCCCCGGTCCATGGTGCGGTCCTTCACGATGCCTTCC
TCATCCCGCCCTCTGTCTGTGGCCTCTGTCTCTTCCCTCTCATCGGACAGCACCCCTTCC
AGACCAGGCTCCGACGGGTTTGCCCTGGAGCCTCTCCTGCCAAAGAAAATGCACTCCAGG
TCCCAGGACAAGCTGGACAAGGATGACCTGGAGAAGGAGAAGAAGGACAAGAAGAAGGAA
AAAAGGAACAGCAAACATCAAGAGATATTTGAGAAAGAATTTAAACCCACCGACATTTCC
CTGCAGCAGTCTGAGGCTGTGATCCTTTCGGAAACGATAAGTCCCCTGCGGCCCCAGAGA
CCGAAGAGCCAGGTGATGAACGTCATTGGAAGCGAAAGGCGCTTCTCGGTGTCCCCCTCG
TCACCGTCCTCCCAGCAAACACCCCCTCCAGTTACACCAAGGGCCAAGCTCAGCTTCAGC
ATGCAGTCGAGCTTGGAGCTGAACGGCATGACGGGGGCGGACGTGGCCGATGTCCCACCC
CCTCTGCCTCTCAAAGGCAGCGTGGCAGATTACGGGAATTTGATGGAAAACCAGGACTTG
CTGGGCTCGCCAACACCTCCACCTCCCCCTCCACACCAGAGGCATCTGCCACCTCCACTG
CCCAGCAAAACTCCGCCTCCTCCCCCTCCAAAGACAACTCGCAAGCAGGCATCGGTGGAC
TCCGGGATCGTGCAGTGA
Enzyme 74 GenBank Gene ID AL157711 Link Image
Enzyme 74 GeneCard ID DOCK1 Link Image
Enzyme 74 GenAtlas ID DOCK1 Link Image
Enzyme 74 HGNC ID HGNC:2987 Link Image
Enzyme 74 Chromosome Location 1
Enzyme 74 Locus 10q26.13-q26.3
Enzyme 74 SNPs SNPJam Report Link Image
Enzyme 74 General References
  1. Hasegawa H, Kiyokawa E, Tanaka S, Nagashima K, Gotoh N, Shibuya M, Kurata T, Matsuda M: DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane. Mol Cell Biol. 1996 Apr;16(4):1770-6. [PubMed Link Image]
  2. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  3. Matsuda M, Ota S, Tanimura R, Nakamura H, Matuoka K, Takenawa T, Nagashima K, Kurata T: Interaction between the amino-terminal SH3 domain of CRK and its natural target proteins. J Biol Chem. 1996 Jun 14;271(24):14468-72. [PubMed Link Image]
  4. Kiyokawa E, Hashimoto Y, Kobayashi S, Sugimura H, Kurata T, Matsuda M: Activation of Rac1 by a Crk SH3-binding protein, DOCK180. Genes Dev. 1998 Nov 1;12(21):3331-6. [PubMed Link Image]
  5. Tu Y, Kucik DF, Wu C: Identification and kinetic analysis of the interaction between Nck-2 and DOCK180. FEBS Lett. 2001 Mar 2;491(3):193-9. [PubMed Link Image]
  6. Kobayashi S, Shirai T, Kiyokawa E, Mochizuki N, Matsuda M, Fukui Y: Membrane recruitment of DOCK180 by binding to PtdIns(3,4,5)P3. Biochem J. 2001 Feb 15;354(Pt 1):73-8. [PubMed Link Image]
  7. Brugnera E, Haney L, Grimsley C, Lu M, Walk SF, Tosello-Trampont AC, Macara IG, Madhani H, Fink GR, Ravichandran KS: Unconventional Rac-GEF activity is mediated through the Dock180-ELMO complex. Nat Cell Biol. 2002 Aug;4(8):574-82. [PubMed Link Image]
  8. Cote JF, Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J Cell Sci. 2002 Dec 15;115(Pt 24):4901-13. [PubMed Link Image]
  9. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  10. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  11. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
Enzyme 74 Metabolite References Not Available
Enzyme 75 [top]
Enzyme 75 ID 14065
Enzyme 75 Name Dedicator of cytokinesis protein 2
Enzyme 75 Synonyms Not Available
Enzyme 75 Gene Name DOCK2
Enzyme 75 Protein Sequence >Dedicator of cytokinesis protein 2
MAPWRKADKERHGVAIYNFQGSGAPQLSLQIGDVVRIQETCGDWYRGYLIKHKMLQGIFP
KSFIHIKEVTVEKRRNTENIIPAEIPLAQEVTTTLWEWGSIWKQLYVASKKERFLQVQSM
MYDLMEWRSQLLSGTLPKDELKELKQKVTSKIDYGNKILELDLIVRDEDGNILDPDNTSV
ISLFHAHEEATDKITERIKEEMSKDQPDYAMYSRISSSPTHSLYVFVRNFVCRIGEDAEL
FMSLYDPNKQTVISENYLVRWGSRGFPKEIEMLNNLKVVFTDLGNKDLNRDKIYLICQIV
RVGKMDLKDTGAKKCTQGLRRPFGVAVMDITDIIKGKAESDEEKQHFIPFHPVTAENDFL
HSLLGKVIASKGDSGGQGLWVTMKMLVGDIIQIRKDYPHLVDRTTVVARKLGFPEIIMPG
DVRNDIYITLLQGDFDKYNKTTQRNVEVIMCVCAEDGKTLPNAICVGAGDKPMNEYRSVV
YYQVKQPRWMETVKVAVPIEDMQRIHLRFMFRHRSSLESKDKGEKNFAMSYVKLMKEDGT
TLHDGFHDLVVLKGDSKKMEDASAYLTLPSYRHHVENKGATLSRSSSSVGGLSVSSRDVF
SISTLVCSTKLTQNVGLLGLLKWRMKPQLLQENLEKLKIVDGEEVVKFLQDTLDALFNIM
MEHSQSDEYDILVFDALIYIIGLIADRKFQHFNTVLEAYIQQHFSATLAYKKLMTVLKTY
LDTSSRGEQCEPILRTLKALEYVFKFIVRSRTLFSQLYEGKEQMEFEESMRRLFESINNL
MKSQYKTTILLQVAALKYIPSVLHDVEMVFDAKLLSQLLYEFYTCIPPVKLQKQKVQSMN
EIVQSNLFKKQECRDILLPVITKELKELLEQKDDMQHQVLERKYCVELLNSILEVLSYQD
AAFTYHHIQEIMVQLLRTVNRTVITMGRDHILISHFVACMTAILNQMGDQHYSFYIETFQ
TSSELVDFLMETFIMFKDLIGKNVYPGDWMAMSMVQNRVFLRAINKFAETMNQKFLEHTN
FEFQLWNNYFHLAVAFITQDSLQLEQFSHAKYNKILNKYGDMRRLIGFSIRDMWYKLGQN
KICFIPGMVGPILEMTLIPEAELRKATIPIFFDMMLCEYQRSGDFKKFENEIILKLDHEV
EGGRGDEQYMQLLESILMECAAEHPTIAKSVENFVNLVKGLLEKLLDYRGVMTDESKDNR
MSCTVNLLNFYKDNNREEMYIRYLYKLRDLHLDCDNYTEAAYTLLLHTWLLKWSDEQCAS
QVMQTGQQHPQTHRQLKETLYETIIGYFDKGKMWEEAISLCKELAEQYEMEIFDYELLSQ
NLIQQAKFYESIMKILRPKPDYFAVGYYGQGFPSFLRNKVFIYRGKEYERREDFQMQLMT
QFPNAEKMNTTSAPGDDVKNAPGQYIQCFTVQPVLDEHPRFKNKPVPDQIINFYKSNYVQ
RFHYSRPVRRGTVDPENEFASMWIERTSFVTAYKLPGILRWFEVVHMSQTTISPLENAIE
TMSTANEKILMMINQYQSDETLPINPLSMLLNGIVDPAVMGGFAKYEKAFFTEEYVRDHP
EDQDKLTHLKDLIAWQIPFLGAGIKIHEKRVSDNLRPFHDRMEECFKNLKMKVEKEYGVR
EMPDFDDRRVGRPRSMLRSYRQMSIISLASMNSDCSTPSKPTSESFDLELASPKTPRVEQ
EEPISPGSTLPEVKLRRSKKRTKRSSVVFADEKAAAESDLKRLSRKHEFMSDTNLSEHAA
IPLKASVLSQMSFASQSMPTIPALALSVAGIPGLDEANTSPRLSQTFLQLSDGDKKTLTR
KKVNQFFKTMLASKSAEEGKQIPDSLSTDL
Enzyme 75 Number of Residues 1830
Enzyme 75 Molecular Weight 211946.7
Enzyme 75 Theoretical pI 6.87
Enzyme 75 GO Classification
Function
  • GTP binding
  • GTPase binding
  • GTPase regulator activity
  • binding
  • cation binding
  • electron carrier activity
  • enzyme binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • guanyl-nucleotide exchange factor activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
  • transition metal ion binding
Process
Component
Enzyme 75 General Function Involved in iron ion binding
Enzyme 75 Specific Function Involved in cytoskeletal rearrangements required for lymphocyte migration in response of chemokines. Activates RAC1 and RAC2 small GTPases, probably by functioning as a guanine nucleotide exchange factor (GEF), which exchanges bound GDP for free GTP. May also participate in IL2 transcriptional activation via the activation of RAC2
Enzyme 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 31377468 Link Image
Enzyme 75 UniProtKB/Swiss-Prot ID Q92608 Link Image
Enzyme 75 UniProtKB/Swiss-Prot Entry Name DOCK2_HUMAN Link Image
Enzyme 75 PDB ID Not Available
Enzyme 75 Cellular Location Not Available
Enzyme 75 Gene Sequence >5493 bp
ATGGCCCCCTGGCGCAAAGCTGACAAGGAGCGGCACGGCGTGGCCATATACAACTTCCAA
GGCAGCGGAGCCCCCCAGCTCTCCCTGCAGATCGGCGATGTGGTGCGAATACAGGAGACG
TGTGGAGACTGGTATAGGGGATACCTCATAAAGCACAAAATGTTACAGGGCATTTTTCCT
AAGTCATTTATCCACATCAAGGAAGTGACAGTTGAGAAAAGAAGAAATACTGAGAACATC
ATTCCTGCAGAAATTCCTCTGGCACAAGAAGTGACAACGACACTTTGGGAATGGGGAAGC
ATCTGGAAACAACTCTATGTGGCCAGCAAAAAGGAGCGTTTTCTCCAGGTGCAGTCCATG
ATGTACGATCTGATGGAGTGGAGGTCCCAGCTTCTCTCAGGAACCTTACCCAAGGATGAG
CTGAAGGAACTGAAGCAGAAAGTCACGTCCAAAATTGACTATGGCAACAAAATCCTTGAG
CTTGATTTGATTGTCAGAGATGAAGACGGAAATATCTTGGACCCTGATAATACCAGTGTC
ATCAGCTTGTTCCATGCACATGAGGAAGCAACTGATAAAATCACAGAGCGTATCAAAGAA
GAAATGTCAAAAGACCAGCCAGATTATGCAATGTATTCCCGGATCTCCTCATCCCCCACC
CATAGCCTCTATGTGTTTGTGAGAAACTTTGTGTGCAGAATTGGGGAAGATGCTGAGCTC
TTCATGTCTCTCTACGACCCCAACAAGCAAACGGTCATAAGTGAGAACTACCTAGTGCGA
TGGGGCAGCCGGGGCTTCCCTAAGGAGATTGAGATGCTCAACAATCTGAAGGTGGTCTTC
ACGGATCTTGGAAACAAAGACCTCAACAGGGATAAAATTTACTTGATTTGTCAAATAGTC
CGGGTCGGCAAGATGGATCTTAAGGATACTGGTGCAAAGAAGTGCACGCAGGGACTGAGG
AGGCCCTTTGGGGTGGCAGTTATGGATATAACAGACATCATCAAGGGGAAAGCAGAGAGT
GATGAAGAAAAGCAGCACTTCATTCCTTTTCACCCGGTTACAGCTGAGAATGACTTCCTA
CACAGCCTGCTGGGCAAAGTCATAGCCTCCAAGGGGGACAGTGGAGGGCAAGGCCTCTGG
GTGACCATGAAGATGCTGGTGGGTGACATCATTCAGATTCGCAAGGACTATCCACACCTG
GTGGACAGGACCACCGTGGTGGCCAGGAAGCTGGGATTCCCAGAGATCATCATGCCAGGG
GATGTCAGGAACGACATCTACATTACTCTCTTACAAGGTGACTTTGACAAGTACAACAAG
ACCACACAGAGGAATGTGGAAGTCATCATGTGTGTGTGCGCGGAGGATGGCAAAACGCTG
CCTAATGCAATTTGCGTGGGAGCAGGGGACAAGCCCATGAATGAGTATCGCTCCGTTGTG
TACTATCAAGTCAAACAGCCACGCTGGATGGAAACAGTCAAGGTGGCTGTCCCTATTGAA
GACATGCAGAGGATCCATCTGCGATTCATGTTTCGACATCGGTCATCTCTGGAATCTAAA
GATAAAGGAGAAAAGAACTTTGCCATGTCCTATGTGAAGCTGATGAAAGAAGATGGGACT
ACTCTACACGATGGATTCCATGACTTAGTTGTCCTCAAGGGGGACAGCAAGAAGATGGAG
GATGCCAGCGCATACCTGACCCTTCCTTCTTATCGACACCATGTGGAAAACAAGGGGGCC
ACGCTGAGCAGGAGCTCCAGCAGTGTTGGGGGGCTTTCTGTCAGCTCCCGGGATGTGTTC
TCCATTTCCACCCTGGTGTGCTCCACAAAGCTCACTCAGAATGTGGGCTTGCTGGGTTTG
CTGAAGTGGCGTATGAAGCCTCAACTGCTACAGGAGAATTTAGAAAAGTTGAAGATTGTG
GATGGAGAGGAAGTGGTGAAGTTTCTCCAGGATACTCTGGATGCCCTCTTCAACATCATG
ATGGAGCATTCTCAAAGTGATGAATATGACATCCTCGTCTTTGATGCCTTGATTTACATA
ATAGGACTCATTGCAGACCGGAAATTTCAGCATTTCAACACCGTTCTGGAGGCTTACATC
CAACAGCATTTCAGTGCGACCTTGGCTTACAAGAAATTGATGACAGTGCTGAAGACTTAC
TTGGATACCTCCAGCAGAGGGGAGCAATGTGAGCCAATCCTAAGAACGCTGAAGGCTTTG
GAATATGTGTTCAAGTTCATTGTTCGGTCGAGGACATTATTTTCACAGCTTTATGAAGGC
AAAGAACAGATGGAGTTTGAAGAATCCATGAGACGGCTCTTTGAATCCATCAACAATCTG
ATGAAAAGTCAATACAAAACTACCATCCTTTTGCAGGTGGCGGCTTTGAAATACATCCCA
TCTGTCCTGCATGATGTAGAAATGGTCTTTGATGCGAAGTTACTCAGCCAACTCCTGTAT
GAGTTCTACACCTGCATCCCTCCTGTGAAACTCCAGAAGCAGAAAGTACAGTCTATGAAT
GAGATAGTCCAGAGCAACCTCTTTAAAAAGCAAGAATGCCGGGACATTCTGCTTCCTGTC
ATCACCAAAGAGCTGAAGGAGCTGCTGGAGCAGAAGGATGACATGCAACACCAGGTCCTG
GAGAGGAAGTACTGCGTTGAATTGCTCAACAGCATCTTGGAAGTCCTTAGCTACCAGGAT
GCGGCCTTCACCTACCACCATATCCAGGAGATCATGGTCCAGCTGCTGCGGACAGTGAAC
CGGACAGTCATCACCATGGGCCGGGATCACATTCTGATTAGTCACTTTGTGGCATGTATG
ACAGCCATCTTAAACCAGATGGGTGACCAGCACTACTCCTTCTACATTGAGACCTTCCAG
ACCAGCTCTGAACTTGTGGACTTCTTGATGGAGACCTTCATCATGTTCAAGGACCTCATT
GGAAAGAACGTGTACCCTGGAGACTGGATGGCCATGAGCATGGTTCAAAACAGGGTCTTC
CTGAGAGCTATCAACAAGTTTGCAGAAACCATGAACCAGAAGTTCCTAGAACACACGAAC
TTTGAGTTCCAGCTGTGGAACAACTATTTTCATCTGGCAGTGGCTTTTATCACCCAGGAT
TCTCTGCAGCTGGAGCAGTTCTCACACGCCAAATACAACAAAATCCTGAATAAGTATGGG
GACATGAGACGGCTAATTGGCTTCTCCATCCGTGATATGTGGTACAAGCTTGGTCAGAAC
AAAATCTGCTTCATCCCAGGCATGGTAGGACCTATATTAGAGATGACACTTATCCCTGAG
GCTGAGCTCCGGAAAGCCACCATACCAATCTTCTTCGACATGATGCTGTGTGAATATCAA
AGAAGTGGGGATTTCAAAAAGTTTGAAAACGAAATCATCCTGAAGCTGGACCACGAGGTA
GAAGGGGGCCGAGGCGACGAGCAGTACATGCAGCTCCTGGAGTCAATCCTGATGGAATGT
GCTGCAGAGCACCCAACCATTGCCAAGTCGGTGGAGAACTTCGTGAACCTGGTCAAAGGC
CTCCTGGAGAAGCTGCTGGATTACCGGGGTGTGATGACAGATGAGAGCAAAGACAACCGC
ATGAGCTGCACCGTGAACCTGCTGAATTTCTACAAAGATAACAACAGGGAGGAGATGTAC
ATAAGGTACCTGTACAAACTCCGCGATCTTCACCTGGACTGTGACAATTACACAGAGGCT
GCCTACACGCTCCTTCTCCACACCTGGCTTCTCAAGTGGTCGGATGAGCAGTGTGCATCA
CAGGTCATGCAGACAGGCCAGCAGCACCCCCAGACACACCGGCAGCTGAAGGAGACGCTC
TACGAGACCATCATAGGCTACTTTGACAAAGGAAAGATGTGGGAAGAGGCCATAAGTCTG
TGCAAGGAGCTGGCGGAACAGTACGAGATGGAGATCTTTGACTATGAGCTGCTCAGCCAG
AACCTGATCCAGCAGGCAAAATTCTATGAAAGCATCATGAAAATCCTCAGGCCCAAACCA
GACTACTTTGCTGTTGGATACTACGGCCAGGGATTCCCCTCCTTCCTGCGGAACAAAGTG
TTCATCTACCGCGGGAAGGAATATGAGCGAAGAGAAGATTTCCAGATGCAGCTGATGACC
CAGTTCCCCAATGCAGAGAAGATGAACACCACCTCTGCCCCGGGAGATGATGTGAAGAAT
GCCCCAGGCCAGTATATCCAGTGCTTCACTGTCCAGCCTGTCTTGGATGAACATCCCAGG
TTCAAGAATAAGCCAGTGCCTGACCAGATTATAAACTTCTACAAATCCAACTACGTGCAA
AGGTTCCACTACTCCCGGCCCGTGCGCAGGGGGACCGTAGACCCAGAGAATGAGTTTGCT
TCCATGTGGATTGAGAGAACCTCCTTCGTGACTGCATACAAGCTGCCGGGGATCCTGCGC
TGGTTTGAGGTGGTGCACATGTCGCAGACCACAATTAGTCCTCTGGAGAATGCCATAGAA
ACCATGTCCACGGCCAATGAGAAGATCCTGATGATGATAAACCAGTACCAGAGTGATGAG
ACCCTCCCCATCAACCCACTCTCCATGCTCCTGAACGGGATTGTGGACCCTGCTGTCATG
GGAGGCTTCGCCAAGTATGAGAAGGCCTTCTTCACTGAAGAGTATGTCAGGGACCACCCT
GAGGACCAGGACAAGCTGACCCACCTCAAGGACCTGATTGCATGGCAGATCCCCTTCTTG
GGAGCTGGGATTAAGATCCATGAGAAAAGGGTGTCAGATAACTTGCGACCCTTCCATGAC
CGGATGGAGGAATGTTTCAAGAACCTGAAAATGAAGGTGGAGAAGGAGTACGGTGTCCGA
GAGATGCCTGACTTTGACGACAGGAGAGTGGGCCGTCCCAGGTCTATGCTGCGCTCATAC
AGACAGATGTCCATCATCTCTCTGGCTTCCATGAATTCTGACTGCAGCACCCCCAGCAAG
CCTACCTCAGAGAGCTTTGACCTGGAATTAGCATCACCCAAGACGCCGAGAGTGGAGCAG
GAGGAACCGATCTCCCCGGGGAGCACCCTGCCTGAGGTCAAGCTGCGGAGGTCCAAGAAG
AGGACAAAGAGAAGCAGCGTAGTTTTTGCGGATGAGAAAGCAGCTGCAGAGTCGGACCTG
AAGCGGCTTTCCAGGAAGCATGAGTTCATGAGTGACACCAACCTCTCGGAGCATGCGGCC
ATCCCCCTCAAGGCGTCTGTCCTCTCTCAAATGAGCTTTGCCAGCCAGTCCATGCCTACC
ATCCCAGCCCTGGCGCTCTCAGTGGCAGGCATCCCTGGGTTGGATGAGGCCAACACATCT
CCCCGCCTCAGCCAGACCTTCCTCCAACTCTCAGATGGTGACAAGAAGACACTCACACGG
AAGAAGGTCAATCAGTTCTTCAAGACAATGCTGGCCAGCAAATCGGCTGAAGAAGGCAAA
CAGATCCCAGACTCGCTGTCCACGGACCTGTGA
Enzyme 75 GenBank Gene ID NM_004946.2 Link Image
Enzyme 75 GeneCard ID DOCK2 Link Image
Enzyme 75 GenAtlas ID DOCK2 Link Image
Enzyme 75 HGNC ID HGNC:2988 Link Image
Enzyme 75 Chromosome Location 5
Enzyme 75 Locus 5q35.1
Enzyme 75 SNPs SNPJam Report Link Image
Enzyme 75 General References
  1. Nagase T, Seki N, Ishikawa K, Ohira M, Kawarabayasi Y, Ohara O, Tanaka A, Kotani H, Miyajima N, Nomura N: Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. DNA Res. 1996 Oct 31;3(5):321-9, 341-54. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Nishihara H, Kobayashi S, Hashimoto Y, Ohba F, Mochizuki N, Kurata T, Nagashima K, Matsuda M: Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins. Biochim Biophys Acta. 1999 Nov 11;1452(2):179-87. [PubMed Link Image]
  4. Nishihara H, Maeda M, Oda A, Tsuda M, Sawa H, Nagashima K, Tanaka S: DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell lines. Blood. 2002 Dec 1;100(12):3968-74. Epub 2002 Jun 28. [PubMed Link Image]
  5. Nishihara H, Maeda M, Tsuda M, Makino Y, Sawa H, Nagashima K, Tanaka S: DOCK2 mediates T cell receptor-induced activation of Rac2 and IL-2 transcription. Biochem Biophys Res Commun. 2002 Aug 23;296(3):716-20. [PubMed Link Image]
  6. Cote JF, Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J Cell Sci. 2002 Dec 15;115(Pt 24):4901-13. [PubMed Link Image]
  7. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  8. Carrascal M, Ovelleiro D, Casas V, Gay M, Abian J: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. J Proteome Res. 2008 Dec;7(12):5167-76. [PubMed Link Image]
  9. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  10. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 75 Metabolite References Not Available
Enzyme 76 [top]
Enzyme 76 ID 14066
Enzyme 76 Name Dedicator of cytokinesis protein 3
Enzyme 76 Synonyms
  1. Modifier of cell adhesion
  2. Presenilin-binding protein
  3. PBP
Enzyme 76 Gene Name DOCK3
Enzyme 76 Protein Sequence >Dedicator of cytokinesis protein 3
MWTPTEEEKYGVVICSFRGSVPQGLVLEIGETVQILEKCEGWYRGVSTKKPNVKGIFPAN
YIHLKKAIVSNRGQYETVVPLEDSIVTEVTATLQEWASLWKQLYVKHKVDLFYKLRHVMN
ELIDLRRQLLSGHLTQDQVREVKRHITVRLDWGNEHLGLDLVPRKDFEVVDSDQISVSDL
YKMHLSSRQSVQQSTSQVDTMRPRHGETCRMPVPHHFFLSLKSFTYNTIGEDTDVFFSLY
DMREGKQISERFLVRLNKNGGPRNPEKIERMCALFTDLSSKDMKRDLYIVAHVIRIGRML
LNDSKKGPPHLHYRRPYGCAVLSILDVLQSLTEVKEEKDFVLKVYTCNNESEWSQIHENI
IRKSSAKYSAPSASHGLIISLQLLRGDMEQIRRENPMIFNRGLAITRKLGFPDVIMPGDI
RNDLYLTLEKGDFERGGKSVQKNIEVTMYVLYADGEILKDCISLGSGEPNRSSYHSFVLY
HSNSPRWGEIIKLPIPIDRFRGSHLRFEFRHCSTKDKGEKKLFGFAFSTLMRDDGTTLSD
DIHELYVYKCDENSTFNNHALYLGLPCCKEDYNGCPNIPSSLIFQRSTKESFFISTQLSS
TKLTQNVDLLALLKWKAFPDRIMDVLGRLRHVSGEEIVKFLQDILDTLFVILDDNTEKYG
LLVFQSLVFIINLLRDIKYFHFRPVMDTYIQKHFAGALAYKELIRCLKWYMDCSAELIRQ
DHIQEAMRALEYLFKFIVQSRILYSRATCGMEEEQFRSSIQELFQSIRFVLSLDSRNSET
LLFTQAALLNSFPTIFDELLQMFTVQEVAEFVRGTLGSMPSTVHIGQSMDVVKLQSIART
VDSRLFSFSESRRILLPVVLHHIHLHLRQQKELLICSGILGSIFSIVKTSSLEADVMEEV
EMMVESLLDVLLQTLLTIMSKSHAQEAVRGQRCPQCTAEITGEYVSCLLSLLRQMCDTHF
QHLLDNFQSKDELKEFLLKIFCVFRNLMKMSVFPRDWMVMRLLTSNIIVTTVQYLSSALH
KNFTETDFDFKVWNSYFSLAVLFINQPSLQLEIITSAKRKKILDKYGDMRVMMAYELFSM
WQNLGEHKIHFIPGMIGPFLGVTLVPQPEVRNIMIPIFHDMMDWEQRKNGNFKQVEAELI
DKLDSMVSEGKGDESYRELFSLLTQLFGPYPSLLEKVEQETWRETGISFVTSVTRLMERL
LDYRDCMKGEETENKKIGCTVNLMNFYKSEINKEEMYIRYIHKLCDMHLQAENYTEAAFT
LLLYCELLQWEDRPLREFLHYPSQTEWQRKEGLCRKIIHYFNKGKSWEFGIPLCRELACQ
YESLYDYQSLSWIRKMEASYYDNIMEQQRLEPEFFRVGFYGRKFPFFLRNKEYVCRGHDY
ERLEAFQQRMLSEFPQAVAMQHPNHPDDAILQCDAQYLQIYAVTPIPDYVDVLQMDRVPD
RVKSFYRVNNVRKFRYDRPFHKGPKDKENEFKSLWIERTTLTLTHSLPGISRWFEVERRE
LVEVSPLENAIQVVENKNQELRSLISQYQHKQVHGNINLLSMCLNGVIDAAVNGGIARYQ
EAFFDKDYINKHPGDAEKITQLKELMQEQVHVLGVGLAVHEKFVHPEMRPLHKKLIDQFQ
MMRASLYHEFPGLDKLSPACSGTSTPRGNVLASHSPMSPESIKMTHRHSPMNLMGTGRHS
SSSLSSHASSEAGNMVMLGDGSMGDAPEDLYHHMQLAYPNPRYQGSVTNVSVLSSSQASP
SSSSLSSTHSAPSQMITSAPSSARGSPSLPDKYRHAREMMLLLPTYRDRPSSAMYPAAIL
ENGQPPNFQRALFQQVVGACKPCSDPNLSVAEKGHYSLHFDAFHHPLGDTPPALPARTLR
KSPLHPIPASPTSPQSGLDGSNSTLSGSASSGVSSLSESNFGHSSEAPPRTDTMDSMPSQ
AWNADEDLEPPYLPVHYSLSESAVLDSIKAQPCRSHSAPGCVIPQDPMDPPALPPKPYHP
RLPALEHDEGVLLREETERPRGLHRKAPLPPGSAKEEQARMAWEHGRGEQ
Enzyme 76 Number of Residues 2030
Enzyme 76 Molecular Weight 233101.1
Enzyme 76 Theoretical pI 6.97
Enzyme 76 GO Classification
Function
  • GTP binding
  • GTPase binding
  • GTPase regulator activity
  • binding
  • enzyme binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
Process
Component
Enzyme 76 General Function Involved in guanyl-nucleotide exchange factor activity
Enzyme 76 Specific Function Potential guanine nucleotide exchange factor (GEF). GEF proteins activate some small GTPases by exchanging bound GDP for free GTP. Its interaction with presenilin proteins as well as its ability to stimulate Tau/MAPT phosphorylation suggest that it may be involved in Alzheimer disease. Ectopic expression in nerve cells decreases the secretion of beta-amyloid APBA1 protein and lowers the rate of cell-substratum adhesion, suggesting that it may affect the function of some small GTPase involved in the regulation of actin cytoskeleton or cell adhesion receptors
Enzyme 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 31415870 Link Image
Enzyme 76 UniProtKB/Swiss-Prot ID Q8IZD9 Link Image
Enzyme 76 UniProtKB/Swiss-Prot Entry Name DOCK3_HUMAN Link Image
Enzyme 76 PDB ID Not Available
Enzyme 76 Cellular Location Not Available
Enzyme 76 Gene Sequence >6093 bp
ATGTGGACCCCCACGGAGGAGGAGAAATACGGCGTAGTGATATGCAGCTTTCGAGGATCT
GTCCCTCAAGGGTTGGTCTTAGAAATAGGAGAAACAGTCCAGATTCTTGAAAAATGTGAA
GGTTGGTACAGAGGAGTTTCAACAAAGAAGCCAAATGTGAAGGGGATCTTTCCTGCAAAT
TACATTCACTTGAAAAAGGCAATTGTCAGTAATAGGGGGCAGTATGAAACTGTGGTTCCA
CTTGAAGATTCTATTGTGACTGAGGTTACAGCAACTCTACAAGAATGGGCAAGTTTGTGG
AAACAGTTGTATGTGAAACACAAAGTAGATCTTTTCTACAAACTACGCCATGTGATGAAT
GAACTTATTGACCTGCGAAGGCAGCTACTGTCTGGTCACCTGACTCAGGATCAGGTGCGG
GAGGTTAAGCGGCACATCACCGTGCGCCTGGACTGGGGTAATGAACATTTGGGCCTGGAC
CTGGTGCCTCGGAAGGACTTTGAAGTAGTGGACTCGGACCAGATTAGTGTCTCAGATCTC
TATAAGATGCATTTATCTAGCCGGCAGAGTGTACAGCAAAGCACATCCCAGGTAGATACA
ATGCGCCCACGTCATGGGGAAACATGTCGGATGCCAGTGCCACATCACTTCTTCCTCAGC
CTGAAGAGTTTCACTTACAATACTATTGGGGAAGATACCGATGTCTTCTTTTCCTTATAT
GACATGAGGGAAGGCAAGCAGATCAGTGAGCGGTTTCTGGTAAGACTGAACAAGAATGGT
GGGCCGAGGAACCCAGAGAAGATAGAACGAATGTGTGCCCTTTTTACAGATCTGAGCAGC
AAAGATATGAAGAGAGATTTGTATATCGTTGCCCATGTGATCCGAATAGGCCGGATGCTC
CTGAACGACTCAAAGAAAGGTCCTCCTCACCTGCACTACAGGCGACCATATGGCTGTGCG
GTCCTAAGCATCTTGGATGTCCTACAGTCACTCACAGAAGTAAAGGAAGAAAAGGATTTT
GTTCTTAAGGTTTACACGTGCAACAACGAGAGTGAGTGGTCCCAGATCCACGAGAACATC
ATCCGAAAGTCCAGTGCCAAGTACTCTGCCCCCAGCGCCAGCCATGGTCTTATCATTTCT
CTGCAGCTTCTTCGTGGAGACATGGAACAGATTCGGAGAGAAAATCCCATGATATTTAAT
AGGGGATTGGCAATTACAAGAAAATTGGGATTTCCTGATGTCATTATGCCAGGTGATATC
CGCAATGACCTGTACCTAACCCTGGAGAAGGGGGATTTCGAGAGAGGAGGAAAGAGTGTA
CAAAAGAATATTGAAGTGACCATGTATGTGCTTTATGCAGATGGAGAAATCTTGAAGGAT
TGCATCAGCTTGGGTTCAGGAGAGCCAAATAGGAGTTCCTACCACTCCTTTGTCCTCTAC
CACAGTAATAGTCCTCGCTGGGGAGAAATTATCAAATTGCCTATCCCCATTGACCGGTTC
CGGGGCTCCCACCTGCGCTTTGAGTTCAGACATTGTTCCACAAAGGACAAAGGGGAAAAG
AAACTCTTTGGCTTTGCATTCTCAACCCTGATGCGTGATGATGGCACCACCCTCTCAGAT
GATATTCACGAGCTTTATGTGTACAAGTGTGATGAGAATAGCACGTTTAATAACCATGCT
CTGTACCTGGGCCTGCCCTGCTGCAAAGAGGACTACAATGGCTGCCCTAATATTCCTTCT
AGCCTCATCTTCCAGCGCAGCACCAAAGAGTCTTTCTTCATCTCCACTCAGCTCTCCTCT
ACCAAACTCACCCAGAATGTGGACCTCCTAGCTCTGCTGAAGTGGAAAGCCTTCCCCGAC
CGGATCATGGATGTACTAGGGCGGCTGCGGCATGTCAGTGGGGAGGAAATTGTTAAGTTT
CTGCAGGACATCTTAGATACACTCTTTGTGATTTTGGATGATAATACAGAGAAGTACGGC
CTGTTGGTTTTTCAGTCTCTGGTGTTCATCATCAACCTGCTCCGAGACATCAAGTATTTT
CACTTTCGACCTGTGATGGACACGTATATCCAGAAGCACTTTGCTGGAGCTCTGGCATAC
AAGGAGCTCATCCGCTGTTTGAAGTGGTATATGGACTGCTCAGCAGAACTGATTCGACAG
GACCACATTCAAGAAGCTATGCGGGCCTTGGAGTACCTTTTCAAGTTCATTGTACAGTCA
CGGATCCTGTACTCACGAGCCACTTGTGGAATGGAAGAGGAACAATTCAGATCCAGTATC
CAAGAACTTTTCCAGTCCATCCGGTTTGTGCTCAGTCTGGACAGCCGAAACTCAGAAACA
CTCCTTTTTACTCAGGCTGCACTCCTCAATTCTTTCCCAACCATCTTTGATGAGCTTCTG
CAAATGTTCACCGTGCAAGAGGTGGCAGAGTTTGTGAGAGGGACACTGGGGAGCATGCCC
AGCACTGTGCACATTGGGCAGTCAATGGACGTGGTCAAGCTGCAGTCCATTGCCAGGACA
GTGGATAGCCGCCTGTTTTCTTTCTCAGAATCCCGCCGCATCCTGCTTCCTGTGGTTCTC
CATCACATTCACCTTCACCTGAGGCAGCAGAAAGAGCTGCTAATTTGCTCAGGGATTCTT
GGCAGCATCTTCTCCATCGTCAAGACCAGCTCTCTGGAGGCAGATGTCATGGAGGAAGTA
GAGATGATGGTGGAGAGCCTCCTGGACGTGCTCTTGCAGACTCTGCTCACCATCATGAGC
AAATCGCACGCTCAGGAGGCGGTAAGAGGGCAGCGGTGCCCGCAGTGCACAGCCGAGATC
ACTGGCGAGTATGTGTCCTGCCTTCTCTCACTGCTCCGCCAGATGTGTGACACCCATTTC
CAGCACCTCCTGGACAACTTCCAGAGCAAAGATGAACTCAAGGAATTTCTGCTGAAGATT
TTTTGCGTGTTCCGGAACCTGATGAAGATGAGTGTCTTCCCTCGGGACTGGATGGTAATG
AGACTGCTCACAAGCAATATTATAGTCACTACTGTCCAGTACCTGTCCTCTGCACTGCAC
AAGAATTTCACAGAGACTGACTTTGACTTTAAGGTGTGGAATTCTTACTTTAGCCTGGCA
GTTCTATTCATAAATCAGCCAAGCCTTCAGCTAGAAATTATCACCTCAGCCAAAAGGAAG
AAGATTCTAGATAAGTATGGGGACATGCGTGTAATGATGGCCTATGAACTGTTCAGCATG
TGGCAGAATTTGGGTGAACATAAGATCCACTTTATTCCGGGAATGATTGGTCCTTTTCTG
GGTGTGACACTGGTCCCACAGCCAGAAGTACGGAATATCATGATTCCCATCTTTCATGAC
ATGATGGACTGGGAGCAGAGAAAAAATGGCAACTTCAAACAGGTGGAGGCCGAGTTGATT
GACAAGCTGGACAGCATGGTGTCAGAAGGGAAAGGTGACGAGAGCTACAGGGAGCTCTTC
AGCCTACTAACCCAGCTGTTTGGGCCCTACCCCAGCCTGCTGGAGAAGGTTGAACAAGAA
ACATGGCGCGAGACCGGCATTTCCTTTGTGACCTCAGTCACCCGCCTCATGGAACGTCTT
CTTGACTACAGGGACTGCATGAAAGGAGAGGAAACAGAGAATAAGAAGATAGGCTGCACT
GTTAACCTGATGAATTTTTACAAATCTGAGATTAACAAGGAAGAAATGTATATCCGCTAC
ATCCATAAGCTTTGTGACATGCACTTGCAGGCCGAAAACTACACAGAGGCCGCATTTACC
CTGCTCCTTTACTGTGAGCTGCTGCAGTGGGAGGACCGGCCACTACGGGAATTCCTCCAC
TACCCATCGCAGACAGAGTGGCAGCGGAAGGAGGGACTGTGCCGGAAGATCATTCACTAC
TTCAACAAAGGCAAGAGCTGGGAGTTTGGGATCCCACTGTGCAGGGAGCTGGCGTGTCAG
TACGAGAGCCTCTATGATTACCAGAGCCTCAGCTGGATTCGGAAAATGGAGGCCAGCTAC
TATGACAACATTATGGAGCAGCAACGCCTGGAGCCTGAGTTCTTTCGGGTCGGCTTCTAT
GGCAGGAAGTTTCCTTTCTTTCTTCGGAACAAAGAATACGTGTGCCGTGGCCATGACTAC
GAGAGGCTGGAGGCCTTCCAGCAGAGGATGCTCAGTGAGTTTCCGCAGGCTGTCGCCATG
CAGCACCCCAACCATCCTGATGACGCCATCCTACAGTGCGATGCCCAGTACTTGCAGATC
TATGCAGTGACGCCCATTCCAGATTATGTGGATGTTCTGCAGATGGATAGGGTACCAGAT
CGAGTCAAGAGCTTCTATCGCGTCAACAATGTGAGGAAGTTCCGGTATGACAGGCCTTTT
CACAAAGGCCCCAAGGACAAGGAGAATGAATTCAAGAGCCTGTGGATTGAACGTACCACA
CTGACCCTGACCCACAGCTTGCCTGGCATCTCTCGGTGGTTTGAAGTGGAGAGGAGGGAA
CTGGTGGAGGTGAGCCCTCTGGAGAATGCCATCCAAGTGGTTGAGAATAAGAACCAGGAG
CTACGCTCCCTGATCAGCCAGTATCAACACAAGCAGGTGCATGGCAACATTAACCTGCTA
AGCATGTGCCTGAATGGTGTCATTGATGCAGCTGTCAATGGAGGCATTGCACGCTATCAG
GAGGCCTTCTTTGATAAAGATTACATCAACAAGCACCCAGGAGATGCTGAGAAGATCACC
CAGCTCAAGGAGCTTATGCAGGAGCAGGTTCATGTCCTTGGAGTTGGGCTAGCAGTTCAT
GAGAAGTTTGTGCACCCAGAAATGCGGCCTCTGCATAAGAAGCTAATTGATCAGTTCCAG
ATGATGCGGGCCAGTCTCTACCATGAGTTTCCAGGTTTGGATAAGCTAAGTCCTGCATGT
TCAGGCACCAGCACCCCACGGGGAAATGTTCTGGCATCCCATAGCCCCATGAGTCCGGAG
AGCATCAAGATGACCCACCGGCACAGCCCCATGAACTTGATGGGCACAGGCCGCCATTCA
TCATCCTCTCTCTCCTCACATGCGTCTAGTGAAGCAGGAAACATGGTGATGCTGGGTGAC
GGCTCCATGGGTGATGCTCCTGAGGACCTGTACCACCACATGCAGCTCGCGTATCCCAAC
CCCAGGTACCAAGGCTCAGTCACCAACGTCTCTGTTCTGTCCTCGTCCCAGGCAAGCCCT
TCTTCCTCCAGCCTGAGTTCCACTCACTCAGCACCATCCCAGATGATTACCTCTGCCCCT
TCCAGTGCCCGAGGCTCTCCCTCTCTGCCAGATAAGTACCGCCATGCCCGTGAAATGATG
TTGTTGCTGCCCACATACCGGGACCGCCCAAGCAGTGCCATGTATCCAGCAGCCATCCTG
GAGAACGGACAGCCGCCGAATTTCCAGCGAGCCCTGTTCCAGCAAGTGGTCGGAGCCTGC
AAACCCTGCAGTGATCCCAATCTGTCTGTGGCTGAAAAAGGTCATTACTCCCTACACTTT
GACGCCTTCCACCACCCTCTGGGTGATACCCCCCCAGCCCTCCCTGCCCGGACCCTGCGC
AAGTCTCCTCTCCACCCTATCCCAGCCTCCCCCACAAGCCCCCAGTCAGGTCTGGACGGC
AGCAACTCTACGCTGTCCGGCAGTGCCAGCAGCGGCGTGTCCTCCTTGAGTGAGAGTAAC
TTTGGGCACTCCTCGGAGGCCCCACCTCGCACTGACACCATGGACTCCATGCCAAGTCAG
GCCTGGAATGCTGACGAAGATCTTGAGCCACCCTACCTCCCTGTCCACTACAGCCTCTCT
GAGTCTGCCGTCCTGGACTCCATCAAGGCCCAGCCATGCCGAAGCCACTCAGCCCCAGGG
TGCGTCATCCCTCAGGACCCCATGGACCCGCCTGCGCTGCCGCCCAAGCCCTACCACCCC
CGCCTGCCGGCCCTGGAGCACGATGAGGGGGTGCTGCTGCGTGAAGAGACTGAGAGGCCT
CGAGGCCTGCACCGCAAGGCTCCATTGCCTCCTGGGAGCGCTAAGGAGGAGCAGGCCCGC
ATGGCCTGGGAGCACGGCCGAGGGGAGCAGTGA
Enzyme 76 GenBank Gene ID NM_004947.4 Link Image
Enzyme 76 GeneCard ID DOCK3 Link Image
Enzyme 76 GenAtlas ID DOCK3 Link Image
Enzyme 76 HGNC ID HGNC:2989 Link Image
Enzyme 76 Chromosome Location 3
Enzyme 76 Locus 3p21.2
Enzyme 76 SNPs SNPJam Report Link Image
Enzyme 76 General References
  1. Kashiwa A, Yoshida H, Lee S, Paladino T, Liu Y, Chen Q, Dargusch R, Schubert D, Kimura H: Isolation and characterization of novel presenilin binding protein. J Neurochem. 2000 Jul;75(1):109-16. [PubMed Link Image]
  2. de Silva MG, Elliott K, Dahl HH, Fitzpatrick E, Wilcox S, Delatycki M, Williamson R, Efron D, Lynch M, Forrest S: Disruption of a novel member of a sodium/hydrogen exchanger family and DOCK3 is associated with an attention deficit hyperactivity disorder-like phenotype. J Med Genet. 2003 Oct;40(10):733-40. [PubMed Link Image]
  3. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
  4. Chen Q, Yoshida H, Schubert D, Maher P, Mallory M, Masliah E: Presenilin binding protein is associated with neurofibrillary alterations in Alzheimer's disease and stimulates tau phosphorylation. Am J Pathol. 2001 Nov;159(5):1597-602. [PubMed Link Image]
  5. Cote JF, Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J Cell Sci. 2002 Dec 15;115(Pt 24):4901-13. [PubMed Link Image]
Enzyme 76 Metabolite References Not Available
Enzyme 77 [top]
Enzyme 77 ID 14067
Enzyme 77 Name Dedicator of cytokinesis protein 4
Enzyme 77 Synonyms Not Available
Enzyme 77 Gene Name DOCK4
Enzyme 77 Protein Sequence >Dedicator of cytokinesis protein 4
MWIPTEHEKYGVVIASFRGTVPYGLSLEIGDTVQILEKCDGWYRGFALKNPNIKGIFPSS
YVHLKNACVKNKGQFEMVIPTEDSVITEMTSTLRDWGTMWKQLYVRNEGDLFHRLWHIMN
EILDLRRQVLVGHLTHDRMKDVKRHITARLDWGNEQLGLDLVPRKEYAMVDPEDISITEL
YRLMEHRHRKKDTPVQASSHHLFVQMKSLMCSNLGEELEVIFSLFDSKENRPISERFFLR
LNRNGLPKAPDKPERHCSLFVDLGSSELRKDIYITVHIIRIGRMGAGEKKNACSVQYRRP
FGCAVLSIADLLTGETKDDLILKVYMCNTESEWYQIHENIIKKLNARYNLTGSNAGLAVS
LQLLHGDIEQIRREYSSVFSHGVSITRKLGFSNIIMPGEMRNDLYITIERGEFEKGGKSV
ARNVEVTMFIVDSSGQTLKDFISFGSGEPPASEYHSFVLYHNNSPRWSELLKLPIPVDKF
RGAHIRFEFRHCSTKEKGEKKLFGFSFVPLMQEDGRTLPDGTHELIVHKCEENTNLQDTT
RYLKLPFSKGIFLGNNNQAMKATKESFCITSFLCSTKLTQNGDMLDLLKWRTHPDKITGC
LSKLKEIDGSEIVKFLQDTLDTLFGILDENSQKYGSKVFDSLVHIINLLQDSKFHHFKPV
MDTYIESHFAGALAYRDLIKVLKWYVDRITEAERQEHIQEVLKAQEYIFKYIVQSRRLFS
LATGGQNEEEFRCCIQELLMSVRFFLSQESKGSGALSQSQAVFLSSFPAVYSELLKLFDV
REVANLVQDTLGSLPTILHVDDSLQAIKLQCIGKTVESQLYTNPDSRYILLPVVLHHLHI
HLQEQKDLIMCARILSNVFCLIKKNSSEKSVLEEIDVIVASLLDILLRTILEITSRPQPS
SSAMRFQFQDVTGEFVACLLSLLRQMTDRHYQQLLDSFNTKEELRDFLLQIFTVFRILIR
PEMFPKDWTVMRLVANNVIITTVLYLSDALRKNFLNENFDYKIWDSYFYLAVIFINQLCL
QLEMFTPSKKKKVLEKYGDMRVTMGCEIFSMWQNLGEHKLHFIPALIGPFLEVTLIPQPD
LRNVMIPIFHDMMDWEQRRSGNFKQVEAKLIDKLDSLMSEGKGDETYRELFNSILLKKIE
RETWRESGVSLIATVTRLMERLLDYRDCMKMGEVDGKKIGCTVSLLNFYKTELNKEEMYI
RYIHKLYDLHLKAQNFTEAAYTLLLYDELLEWSDRPLREFLTYPMQTEWQRKEHLHLTII
QNFDRGKCWENGIILCRKIAEQYESYYDYRNLSKMRMMEASLYDKIMDQQRLEPEFFRVG
FYGKKFPFFLRNKEFVCRGHDYERLEAFQQRMLNEFPHAIAMQHANQPDETIFQAEAQYL
QIYAVTPIPESQEVLQREGVPDNIKSFYKVNHIWKFRYDRPFHKGTKDKENEFKSLWVER
TSLYLVQSLPGISRWFEVEKREVVEMSPLENAIEVLENKNQQLKTLISQCQTRQMQNINP
LTMCLNGVIDAAVNGGVSRYQEAFFVKEYILSHPEDGEKIARLRELMLEQAQILEFGLAV
HEKFVPQDMRPLHKKLVDQFFVMKSSLGIQEFSACMQASPVHFPNGSPRVCRNSAPASVS
PDGTRVIPRRSPLSYPAVNRYSSSSLSSQASAEVSNITGQSESSDEVFNMQPSPSTSSLS
STHSASPNVTSSAPSSARASPLLSDKHKHSRENSCLSPRERPCSAIYPTPVEPSQRMLFN
HIGDGALPRSDPNLSAPEKAVNPTPSSWSLDSGKEAKNMSDSGKLISPPVPPRPTQTASP
ARHTTSVSPSPAGRSPLKGSVQSFTPSPVEYHSPGLISNSPVLSGSYSSGISSLSRCSTS
ETSGFENQVNEQSAPLPVPVPVPVPSYGGEEPVRKESKTPPPYSVYERTLRRPVPLPHSL
SIPVTSEPPALPPKPLAARSSHLENGARRTDPGPRPRPLPRKVSQL
Enzyme 77 Number of Residues 1966
Enzyme 77 Molecular Weight 225204.3
Enzyme 77 Theoretical pI 7.68
Enzyme 77 GO Classification
Function
  • GTP binding
  • GTPase binding
  • GTPase regulator activity
  • binding
  • enzyme binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
Process
Component
Enzyme 77 General Function Involved in guanyl-nucleotide exchange factor activity
Enzyme 77 Specific Function Involved in regulation of adherens junction between cells. Functions as a guanine nucleotide exchange factor (GEF), which activates Rap1 small GTPase by exchanging bound GDP for free GTP
Enzyme 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 92091572 Link Image
Enzyme 77 UniProtKB/Swiss-Prot ID Q8N1I0 Link Image
Enzyme 77 UniProtKB/Swiss-Prot Entry Name DOCK4_HUMAN Link Image
Enzyme 77 PDB ID Not Available
Enzyme 77 Cellular Location Not Available
Enzyme 77 Gene Sequence >5901 bp
ATGTGGATACCTACGGAGCACGAGAAATACGGCGTGGTTATTGCCAGTTTCCGAGGAACC
GTTCCATATGGCCTGTCATTGGAAATTGGAGATACAGTTCAGATCCTGGAGAAGTGTGAT
GGCTGGTACAGAGGATTTGCCTTAAAAAACCCAAATATCAAGGGTATATTTCCTTCCAGC
TACGTTCACTTGAAAAATGCCTGTGTAAAGAACAAAGGACAATTTGAAATGGTTATTCCC
ACTGAAGACTCTGTTATCACAGAAATGACATCAACATTAAGAGACTGGGGAACCATGTGG
AAACAACTCTATGTGCGTAATGAAGGCGATCTCTTCCACCGGCTGTGGCACATCATGAAT
GAAATCCTGGACCTGAGGCGGCAGGTGCTGGTGGGCCACCTCACCCACGACCGGATGAAG
GACGTGAAGCGCCACATTACTGCCCGGCTTGACTGGGGCAATGAACAACTGGGACTGGAC
CTGGTGCCTAGGAAAGAGTACGCAATGGTGGATCCGGAAGACATCAGCATTACTGAGCTC
TACCGATTGATGGAACATCGACATCGGAAGAAAGACACCCCGGTGCAGGCCAGCAGTCAC
CACCTCTTTGTCCAGATGAAGAGCCTCATGTGTTCCAACCTGGGAGAGGAGCTGGAGGTC
ATCTTCTCACTCTTTGACAGTAAAGAGAACCGGCCAATCAGTGAGAGATTTTTCTTGAGG
CTGAATAGAAACGGGCTTCCCAAAGCCCCTGATAAACCGGAACGACATTGCTCCCTCTTT
GTGGATTTGGGCAGCAGTGAGCTAAGAAAGGACATTTATATCACCGTGCACATTATCCGA
ATCGGTCGAATGGGAGCAGGAGAAAAAAAGAATGCCTGTAGTGTCCAGTACCGACGACCC
TTTGGCTGTGCAGTTCTTAGCATCGCTGACCTGCTAACAGGAGAGACAAAGGATGACCTC
ATTCTGAAAGTATACATGTGTAACACAGAGAGTGAGTGGTACCAAATCCATGAGAACATC
ATCAAAAAGCTGAATGCACGTTATAACTTGACTGGCTCCAATGCAGGTTTAGCAGTTTCC
TTACAGCTATTGCACGGAGACATTGAACAAATCAGAAGGGAATATTCATCAGTATTTTCT
CATGGAGTATCCATAACAAGGAAGCTGGGATTTTCAAATATTATTATGCCTGGTGAAATG
AGGAATGATTTATATATCACTATTGAAAGGGGAGAATTTGAGAAAGGAGGGAAGAGCGTG
GCCAGAAATGTGGAAGTTACGATGTTCATTGTAGACAGTAGTGGCCAAACCCTGAAGGAT
TTTATCTCCTTCGGCTCTGGGGAGCCACCAGCCAGTGAGTACCACTCCTTTGTGCTTTAC
CATAACAACAGTCCCAGGTGGTCTGAACTGCTGAAACTTCCCATTCCTGTGGATAAATTC
CGGGGTGCACACATCCGCTTCGAGTTTCGGCATTGTTCCACAAAGGAGAAAGGAGAGAAG
AAGTTGTTTGGGTTTTCTTTTGTCCCTCTGATGCAAGAAGATGGTAGGACTCTTCCAGAT
GGCACTCATGAGCTCATCGTGCATAAGTGTGAAGAAAACACAAATCTTCAGGATACTACC
CGCTACCTCAAACTTCCCTTTTCCAAGGGCATTTTCCTTGGGAATAATAATCAAGCCATG
AAGGCCACAAAGGAGTCCTTTTGTATTACATCTTTTCTCTGTTCCACAAAACTCACACAA
AATGGTGATATGCTTGATCTTTTGAAATGGAGAACCCACCCAGACAAGATCACTGGCTGT
CTCTCTAAATTAAAAGAAATTGATGGCTCAGAGATAGTAAAGTTTCTGCAGGATACACTG
GATACCTTATTTGGAATTTTAGATGAAAATTCCCAAAAATATGGGTCTAAAGTGTTTGAT
TCTTTGGTTCACATAATAAATTTGCTGCAAGATAGCAAATTTCATCATTTTAAACCTGTA
ATGGACACTTACATTGAGAGTCATTTTGCTGGGGCACTTGCATACAGAGATCTCATCAAA
GTGCTCAAATGGTACGTGGACCGGATCACAGAAGCAGAGCGGCAAGAGCATATCCAGGAG
GTGCTGAAGGCACAAGAATACATTTTTAAGTATATAGTTCAATCTCGAAGGCTGTTTTCC
CTTGCCACTGGTGGGCAAAACGAAGAGGAGTTCCGCTGCTGCATTCAGGAGCTTCTCATG
TCAGTCCGTTTCTTTCTTTCGCAAGAGAGCAAAGGGTCTGGAGCATTATCTCAGTCACAG
GCTGTGTTTCTGAGCTCTTTCCCTGCCGTGTACTCAGAACTGTTGAAGCTCTTTGATGTC
CGGGAAGTAGCCAACTTGGTCCAGGACACCCTGGGCAGTCTGCCGACCATCCTGCATGTG
GATGATTCCCTGCAGGCCATCAAACTGCAGTGCATTGGCAAAACCGTGGAAAGCCAGCTT
TATACCAACCCAGATTCCCGATACATTCTTCTGCCTGTCGTGTTACATCACCTCCACATT
CACTTGCAAGAACAGAAGGACCTGATCATGTGTGCACGTATCCTTAGCAACGTATTTTGT
CTTATCAAGAAAAATAGCTCAGAAAAATCTGTGCTGGAGGAAATAGATGTGATAGTGGCC
AGCTTGCTGGATATTCTGCTGAGGACCATATTGGAGATCACCAGCCGACCTCAGCCATCC
AGCTCAGCAATGCGGTTCCAGTTCCAGGATGTCACTGGGGAGTTTGTTGCTTGTCTCCTG
TCCCTATTACGACAAATGACAGATAGACATTATCAACAGCTTCTTGATAGTTTTAATACA
AAGGAAGAACTAAGGGATTTCCTGCTGCAGATATTTACTGTGTTCCGAATATTGATACGC
CCGGAGATGTTTCCAAAGGACTGGACTGTTATGCGCTTGGTTGCTAACAATGTTATTATT
ACAACAGTTCTATACCTCTCAGATGCACTTCGTAAGAACTTCTTAAATGAAAACTTTGAT
TATAAGATCTGGGATTCCTACTTTTACCTCGCAGTCATTTTTATAAACCAGTTGTGTCTG
CAGTTGGAGATGTTCACACCTTCCAAGAAGAAAAAGGTGTTAGAAAAGTATGGTGACATG
CGGGTAACAATGGGTTGTGAAATTTTCAGCATGTGGCAAAACCTAGGAGAGCACAAGCTT
CATTTTATCCCTGCCCTGATTGGCCCCTTCCTAGAAGTGACCTTGATACCCCAGCCAGAT
CTTCGGAATGTCATGATTCCAATTTTTCATGATATGATGGACTGGGAGCAGAGGCGGAGT
GGCAACTTTAAACAGGTGGAAGCCAAGCTAATTGACAAACTGGATAGCCTGATGTCAGAA
GGCAAAGGTGACGAAACATACCGCGAGCTCTTCAACAGTATTCTACTAAAGAAAATTGAG
CGGGAAACATGGCGGGAAAGTGGCGTTTCATTAATTGCTACTGTAACTCGTCTAATGGAG
AGGTTGTTAGATTACAGGGACTGCATGAAAATGGGAGAGGTAGATGGCAAAAAGATTGGC
TGCACAGTTAGCCTTCTGAACTTCTATAAGACTGAACTGAACAAGGAGGAGATGTATATA
CGCTACATTCACAAACTCTATGATCTGCATCTCAAAGCACAGAACTTTACAGAAGCTGCA
TATACCCTCCTCTTATATGACGAGCTACTGGAATGGTCTGATCGGCCCCTCAGGGAGTTC
CTGACCTACCCCATGCAAACAGAATGGCAGCGCAAAGAGCACCTGCACCTCACCATCATC
CAGAACTTTGACAGAGGCAAATGTTGGGAGAATGGCATTATCTTGTGCCGGAAGATTGCA
GAGCAGTATGAGAGTTATTATGACTACAGAAACCTGAGCAAGATGCGGATGATGGAAGCC
TCTTTGTATGACAAAATTATGGACCAGCAACGTCTTGAACCAGAGTTCTTCAGAGTTGGA
TTTTATGGAAAAAAATTTCCATTTTTCTTAAGAAATAAGGAGTTTGTGTGTCGAGGGCAT
GACTACGAGAGGCTGGAAGCCTTCCAACAGAGAATGCTGAACGAGTTCCCCCATGCCATC
GCCATGCAGCACGCCAACCAGCCCGATGAGACCATCTTCCAGGCAGAAGCTCAGTATTTG
CAGATATATGCTGTGACTCCCATTCCAGAGAGCCAGGAGGTCCTGCAGAGAGAGGGTGTT
CCGGACAACATCAAAAGCTTCTATAAAGTGAATCACATCTGGAAATTCCGCTATGACCGA
CCATTTCACAAAGGCACAAAAGATAAAGAGAATGAATTCAAGAGTCTCTGGGTGGAGAGA
ACGTCATTATACTTGGTGCAGAGTTTGCCTGGCATCTCTCGCTGGTTTGAAGTGGAAAAG
CGTGAAGTGGTAGAAATGAGTCCTCTGGAAAATGCAATTGAAGTGCTAGAAAATAAGAAT
CAGCAGCTGAAGACTCTGATTAGTCAGTGTCAGACAAGACAGATGCAGAATATTAATCCC
CTGACTATGTGCCTGAATGGAGTTATAGATGCTGCAGTTAATGGTGGCGTTTCCAGGTAT
CAAGAGGCATTCTTTGTCAAAGAATATATCTTAAGTCACCCTGAAGATGGGGAGAAAATT
GCACGATTAAGAGAGCTGATGCTTGAGCAGGCACAGATTCTGGAATTTGGTTTGGCCGTG
CATGAGAAGTTTGTACCTCAAGATATGAGACCCCTTCACAAAAAGCTGGTTGACCAATTC
TTTGTGATGAAGTCGAGCTTAGGGATACAGGAGTTCTCTGCTTGTATGCAAGCCAGTCCT
GTCCATTTTCCTAATGGAAGCCCTCGTGTGTGTAGAAACTCAGCACCTGCTTCTGTGAGC
CCAGATGGTACCAGGGTAATTCCTAGACGCAGCCCGTTAAGTTACCCAGCTGTCAACCGA
TATTCTTCCTCCTCACTGTCCTCACAAGCTTCTGCTGAAGTAAGCAATATTACAGGGCAA
TCAGAAAGCTCTGATGAAGTCTTTAACATGCAGCCAAGTCCATCTACCTCAAGCTTGAGT
TCTACTCACTCGGCTTCACCTAATGTGACAAGTTCTGCTCCATCGAGTGCCAGAGCTTCT
CCTTTGTTGTCTGACAAACACAAACATTCCCGAGAAAACTCTTGCCTGTCACCAAGAGAG
AGACCATGCAGTGCCATCTATCCAACACCTGTGGAGCCTTCGCAGAGGATGCTGTTTAAT
CATATTGGAGACGGGGCCTTGCCACGCAGTGACCCAAATCTCTCTGCACCTGAAAAAGCT
GTGAACCCCACCCCTAGCAGCTGGAGCCTGGACAGTGGGAAGGAAGCCAAGAACATGTCG
GATAGTGGGAAACTTATCTCTCCCCCTGTCCCTCCAAGACCCACACAGACTGCTTCACCA
GCAAGACACACGACATCAGTATCCCCCTCGCCTGCCGGGCGATCTCCATTGAAGGGCTCT
GTGCAGTCTTTCACCCCCTCTCCAGTGGAGTACCACTCGCCAGGACTCATCTCCAACTCC
CCTGTCTTGTCGGGCAGCTACAGCAGTGGGATTTCTTCTCTCAGCCGGTGCAGCACGTCG
GAAACCTCAGGCTTTGAAAATCAGGTGAATGAACAGTCGGCCCCCCTGCCGGTGCCAGTG
CCGGTGCCCGTGCCGAGCTACGGCGGGGAGGAGCCAGTGCGCAAGGAGAGCAAGACTCCG
CCCCCGTACAGCGTCTACGAGCGGACTCTGCGGCGCCCCGTCCCGCTACCTCACAGCCTC
TCCATCCCCGTCACGTCGGAGCCGCCCGCGCTGCCCCCCAAGCCTCTGGCAGCGCGATCC
AGCCACCTGGAGAATGGGGCCCGGAGGACTGACCCCGGCCCGCGGCCCAGGCCCCTGCCC
CGCAAGGTCTCTCAGTTATAA
Enzyme 77 GenBank Gene ID NM_014705.3 Link Image
Enzyme 77 GeneCard ID DOCK4 Link Image
Enzyme 77 GenAtlas ID DOCK4 Link Image
Enzyme 77 HGNC ID HGNC:19192 Link Image
Enzyme 77 Chromosome Location 7
Enzyme 77 Locus 7q31.1
Enzyme 77 SNPs SNPJam Report Link Image
Enzyme 77 General References
  1. Yajnik V, Paulding C, Sordella R, McClatchey AI, Saito M, Wahrer DC, Reynolds P, Bell DW, Lake R, van den Heuvel S, Settleman J, Haber DA: DOCK4, a GTPase activator, is disrupted during tumorigenesis. Cell. 2003 Mar 7;112(5):673-84. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  4. Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Oct 30;5(5):277-86. [PubMed Link Image]
  5. Cote JF, Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J Cell Sci. 2002 Dec 15;115(Pt 24):4901-13. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  7. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  8. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 77 Metabolite References Not Available
Enzyme 78 [top]
Enzyme 78 ID 14068
Enzyme 78 Name Dedicator of cytokinesis protein 5
Enzyme 78 Synonyms Not Available
Enzyme 78 Gene Name DOCK5
Enzyme 78 Protein Sequence >Dedicator of cytokinesis protein 5
MARWIPTKRQKYGVAIYNYNASQDVELSLQIGDTVHILEMYEGWYRGYTLQNKSKKGIFP
ETYIHLKEATVEDLGQHETVIPGELPLVQELTSTLREWAVIWRKLYVNNKLTLFRQLQQM
TYSLIEWRSQILSGTLPKDELAELKKKVTAKIDHGNRMLGLDLVVRDDNGNILDPDETST
IALFKAHEVASKRIEEKIQEEKSILQNLDLRGQSIFSTIHTYGLYVNFKNFVCNIGEDAE
LFMALYDPDQSTFISENYLIRWGSNGMPKEIEKLNNLQAVFTDLSSMDLIRPRVSLVCQI
VRVGHMELKEGKKHTCGLRRPFGVAVMDITDIIHGKVDDEEKQHFIPFQQIAMETYIRQR
QLIMSPLITSHVIGENEPLTSVLNKVIAAKEVNHKGQGLWVSLKLLPGDLTQVQKNFSHL
VDRSTAIARKMGFPEIILPGDVRNDIYVTLIHGEFDKGKKKTPKNVEVTMSVHDEEGKLL
EKAIHPGAGYEGISEYKSVVYYQVKQPCWYETVKVSIAIEEVTRCHIRFTFRHRSSQETR
DKSERAFGVAFVKLMNPDGTTLQDGRHDLVVYKGDNKKMEDAKFYLTLPGTKMEMEEKEL
QASKNLVTFTPSKDSTKDSFQIATLICSTKLTQNVDLLGLLNWRSNSQNIKHNLKKLMEV
DGGEIVKFLQDTLDALFNIMMEMSDSETYDFLVFDALVFIISLIGDIKFQHFNPVLETYI
YKHFSATLAYVKLSKVLNFYVANADDSSKTELLFAALKALKYLFRFIIQSRVLYLRFYGQ
SKDGDEFNNSIRQLFLAFNMLMDRPLEEAVKIKGAALKYLPSIINDVKLVFDPVELSVLF
CKFIQSIPDNQLVRQKLNCMTKIVESTLFRQSECREVLLPLLTDQLSGQLDDNSNKPDHE
ASSQLLSNILEVLDRKDVGATAVHIQLIMERLLRRINRTVIGMNRQSPHIGSFVACMIAL
LQQMDDSHYSHYISTFKTRQDIIDFLMETFIMFKDLIGKNVYAKDWMVMNMTQNRVFLRA
INQFAEVLTRFFMDQASFELQLWNNYFHLAVAFLTHESLQLETFSQAKRNKIVKKYGDMR
KEIGFRIRDMWYNLGPHKIKFIPSMVGPILEVTLTPEVELRKATIPIFFDMMQCEFNFSG
NGNFHMFENELITKLDQEVEGGRGDEQYKVLLEKLLLEHCRKHKYLSSSGEVFALLVSSL
LENLLDYRTIIMQDESKENRMSCTVNVLNFYKEKKREDIYIRYLYKLRDLHRDCENYTEA
AYTLLLHAELLQWSDKPCVPHLLQKDSYYVYTQQELKEKLYQEIISYFDKGKMWEKAIKL
SKELAETYESKVFDYEGLGNLLKKRASFYENIIKAMRPQPEYFAVGYYGQGFPSFLRNKI
FIYRGKEYERREDFSLRLLTQFPNAEKMTSTTPPGEDIKSSPKQYMQCFTVKPVMSLPPS
YKDKPVPEQILNYYRANEVQQFRYSRPFRKGEKDPDNEFATMWIERTTYTTAYTFPGILK
WFEVKQISTEEISPLENAIETMELTNERISNCVQQHAWDRSLSVHPLSMLLSGIVDPAVM
GGFSNYEKAFFTEKYLQEHPEDQEKVELLKRLIALQMPLLTEGIRIHGEKLTEQLKPLHE
RLSSCFRELKEKVEKHYGVITLPPNLTERKQSRTGSIVLPYIMSSTLRRLSITSVTSSVV
STSSNSSDNAPSRPGSDGSILEPLLERRASSGARVEDLSLREENSENRISKFKRKDWSLS
KSQVIAEKAPEPDLMSPTRKAQRPKSLQLMDNRLSPFHGSSPPQSTPLSPPPLTPKATRT
LSSPSLQTDGIAATPVPPPPPPKSKPYEGSQRNSTELAPPLPVRREAKAPPPPPPKARKS
GIPTSEPGSQ
Enzyme 78 Number of Residues 1870
Enzyme 78 Molecular Weight 215306.9
Enzyme 78 Theoretical pI 8.08
Enzyme 78 GO Classification
Function
  • GTP binding
  • GTPase binding
  • GTPase regulator activity
  • binding
  • enzyme binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
Process
Component
Enzyme 78 General Function Involved in binding
Enzyme 78 Specific Function Guanine nucleotide exchange factor (GEF) for Rho and Rac. GEF proteins activate small GTPases by exchanging bound GDP for free GTP
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 117553586 Link Image
Enzyme 78 UniProtKB/Swiss-Prot ID Q9H7D0 Link Image
Enzyme 78 UniProtKB/Swiss-Prot Entry Name DOCK5_HUMAN Link Image
Enzyme 78 PDB ID Not Available
Enzyme 78 Cellular Location Not Available
Enzyme 78 Gene Sequence >5613 bp
ATGGCCCGCTGGATCCCGACCAAGAGGCAGAAGTACGGGGTTGCGATCTATAACTACAAT
GCTTCTCAAGATGTGGAGCTCTCCTTGCAGATCGGTGACACAGTTCACATCCTGGAGATG
TACGAGGGTTGGTACAGAGGATATACCCTCCAAAATAAATCTAAAAAGGGCATTTTCCCT
GAAACATATATCCATTTGAAAGAGGCAACTGTGGAAGACCTGGGGCAGCATGAAACCGTG
ATTCCTGGCGAGCTCCCCCTGGTGCAGGAGCTCACGTCCACTCTGCGAGAATGGGCTGTC
ATCTGGCGAAAGCTCTACGTGAACAACAAGCTCACCCTCTTCCGCCAGCTGCAGCAGATG
ACGTACAGCCTGATCGAGTGGCGGTCCCAGATCCTGTCTGGGACGCTCCCCAAGGATGAA
CTGGCAGAGCTCAAGAAGAAAGTCACAGCCAAAATTGATCATGGGAACAGAATGCTGGGG
TTAGATCTGGTGGTGCGAGATGACAATGGGAACATCCTAGACCCTGACGAAACCAGCACC
ATTGCCCTCTTCAAGGCCCATGAGGTGGCCTCCAAAAGGATTGAGGAAAAGATCCAAGAA
GAGAAGTCAATCCTGCAGAACCTCGATTTGCGGGGCCAGTCCATCTTCAGTACCATCCAC
ACCTATGGCCTCTATGTGAACTTCAAGAACTTTGTCTGCAACATCGGGGAAGATGCAGAG
TTGTTTATGGCCCTCTACGACCCAGACCAGTCCACTTTTATCAGTGAGAACTATCTAATT
CGTTGGGGCAGTAACGGGATGCCCAAGGAAATAGAGAAGCTCAATAACCTCCAAGCAGTG
TTTACAGACCTTAGCAGCATGGACCTCATCCGGCCCCGCGTCAGCCTTGTGTGCCAGATT
GTCCGCGTGGGCCATATGGAGCTGAAGGAAGGCAAGAAGCACACCTGTGGACTCCGAAGA
CCTTTTGGAGTGGCAGTGATGGATATTACTGATATCATACATGGGAAGGTGGATGATGAA
GAAAAGCAGCATTTTATTCCCTTTCAGCAAATTGCGATGGAAACCTACATCCGCCAGAGG
CAGCTCATCATGTCGCCTTTGATAACATCACACGTGATTGGGGAGAATGAGCCACTCACT
TCAGTCTTGAATAAAGTGATTGCAGCAAAGGAAGTGAATCACAAAGGGCAAGGCCTTTGG
GTATCCTTGAAGCTCTTGCCCGGTGACCTCACCCAGGTTCAGAAGAATTTTTCACACTTG
GTTGATAGATCAACAGCAATAGCCCGGAAGATGGGCTTTCCTGAAATCATACTGCCAGGA
GATGTTCGGAATGACATTTATGTCACCCTGATCCACGGTGAGTTTGACAAAGGGAAGAAG
AAGACGCCAAAGAATGTGGAGGTGACGATGTCTGTGCACGATGAGGAGGGCAAGCTCTTG
GAGAAAGCAATTCACCCTGGTGCTGGATATGAAGGCATTTCAGAATACAAATCAGTAGTC
TATTACCAAGTCAAGCAGCCCTGTTGGTATGAGACTGTCAAGGTATCCATTGCTATAGAA
GAAGTCACACGCTGTCATATAAGATTTACCTTCCGACACAGGTCATCTCAGGAAACCAGA
GATAAATCGGAGCGAGCATTTGGGGTGGCCTTCGTGAAGCTGATGAACCCGGATGGCACC
ACTCTGCAGGATGGGAGGCACGATCTGGTGGTTTATAAGGGTGACAACAAAAAAATGGAA
GATGCTAAATTCTACCTGACCCTGCCTGGAACCAAGATGGAGATGGAAGAAAAAGAGCTT
CAAGCATCCAAAAACCTGGTCACCTTCACCCCAAGCAAGGATAGCACTAAAGACAGCTTT
CAGATTGCCACCCTCATCTGCTCCACAAAGCTCACCCAGAATGTTGACCTGTTAGGCTTG
TTAAATTGGCGTTCCAACTCCCAGAACATTAAACACAACCTAAAGAAGTTAATGGAAGTG
GATGGAGGAGAGATTGTTAAGTTTTTGCAAGATACACTAGATGCACTCTTTAACATAATG
ATGGAAATGTCAGACAGTGAAACCTATGACTTCCTTGTGTTTGACGCACTGGTATTTATT
ATTTCACTGATAGGAGACATCAAGTTCCAGCATTTTAATCCTGTACTTGAAACCTACATT
TACAAGCACTTCAGCGCCACTTTGGCATATGTGAAACTCTCCAAGGTACTGAACTTCTAT
GTGGCTAATGCAGATGACTCCAGCAAGACTGAACTGCTTTTTGCTGCGTTGAAAGCCTTG
AAGTACTTGTTTAGATTCATCATCCAATCCCGAGTGCTCTACTTGAGATTTTATGGGCAG
AGCAAAGATGGAGATGAGTTTAATAATTCAATTCGCCAGTTATTTCTTGCTTTCAATATG
CTGATGGACAGGCCTCTGGAGGAAGCCGTCAAGATCAAGGGGGCAGCTTTGAAGTACCTT
CCTAGCATAATTAATGATGTCAAACTTGTATTTGATCCTGTTGAGCTCAGCGTGCTCTTC
TGCAAATTCATTCAAAGCATTCCTGACAACCAGCTGGTTCGGCAGAAACTTAACTGCATG
ACCAAGATAGTAGAGAGCACTCTTTTTCGACAGTCAGAGTGCAGAGAAGTGCTGCTGCCA
CTGCTGACAGACCAGCTCAGCGGCCAGTTAGATGACAACTCCAACAAGCCTGACCACGAG
GCAAGCTCGCAGCTTCTGAGCAACATCCTGGAGGTGCTGGACAGGAAGGATGTGGGTGCC
ACTGCGGTGCACATTCAGCTTATAATGGAACGGCTGCTGAGAAGGATCAACCGGACAGTG
ATTGGGATGAACCGGCAGTCTCCCCACATCGGGAGTTTTGTGGCTTGCATGATTGCCCTG
CTGCAGCAAATGGACGACAGCCACTATAGCCACTACATCAGCACTTTCAAAACCAGACAA
GACATCATCGACTTCCTCATGGAAACTTTTATCATGTTCAAGGACCTGATTGGAAAGAAT
GTCTATGCCAAAGATTGGATGGTGATGAATATGACTCAAAACAGGGTTTTTCTCCGTGCT
ATAAATCAGTTTGCTGAAGTTCTCACAAGATTCTTCATGGATCAGGCAAGCTTTGAACTT
CAGCTCTGGAACAATTACTTCCATTTGGCAGTTGCATTTCTCACCCATGAGTCCCTTCAG
CTTGAAACCTTCTCACAAGCCAAGCGCAACAAAATTGTTAAAAAATATGGGGACATGAGA
AAGGAAATCGGCTTTAGAATCCGGGACATGTGGTATAACCTGGGTCCCCACAAAATCAAA
TTCATCCCATCCATGGTGGGTCCCATTCTGGAGGTCACTCTGACCCCTGAAGTAGAGCTC
CGGAAAGCCACAATCCCCATTTTCTTTGATATGATGCAGTGTGAGTTCAATTTCAGTGGA
AATGGCAATTTCCATATGTTTGAGAATGAGCTGATCACAAAGCTGGACCAGGAGGTAGAA
GGGGGCAGAGGAGACGAACAATACAAGGTTCTTCTGGAAAAACTGCTCCTAGAACATTGC
CGGAAACACAAATACCTCTCCAGCTCTGGGGAGGTCTTCGCCCTCCTGGTCAGCAGCCTC
TTAGAGAACCTGCTGGACTATAGAACCATCATCATGCAAGATGAGAGCAAGGAGAACCGT
ATGAGCTGCACTGTGAACGTGCTGAACTTTTATAAAGAAAAGAAGAGAGAGGACATATAC
ATAAGATATCTGTACAAGCTTCGAGATTTGCACCGAGACTGTGAGAACTACACAGAAGCT
GCCTACACGCTTCTCTTGCACGCTGAGCTTCTGCAGTGGTCTGACAAGCCCTGTGTGCCT
CATTTGCTTCAGAAGGACAGTTACTATGTTTATACCCAGCAAGAGCTTAAAGAGAAGCTG
TATCAAGAAATCATATCATATTTCGACAAAGGCAAAATGTGGGAGAAGGCCATCAAGCTG
AGCAAAGAGTTGGCTGAGACTTACGAAAGCAAAGTATTTGACTACGAGGGCCTTGGCAAC
CTCCTGAAAAAAAGGGCCTCATTTTATGAGAACATCATTAAGGCAATGAGGCCTCAGCCT
GAATACTTTGCTGTTGGATACTATGGACAGGGCTTTCCTTCTTTCCTACGGAATAAAATC
TTCATCTATCGGGGAAAGGAGTATGAGAGGCGAGAGGACTTCAGCCTGAGGTTGTTAACC
CAGTTCCCCAATGCGGAGAAGATGACCAGTACCACGCCTCCTGGGGAAGACATCAAGTCG
TCCCCCAAGCAGTACATGCAGTGCTTCACTGTAAAGCCAGTGATGAGCTTGCCGCCCAGC
TACAAGGATAAACCTGTTCCAGAGCAGATCTTAAACTACTACAGAGCCAATGAAGTGCAG
CAGTTCAGATACTCCCGGCCGTTCCGGAAAGGAGAAAAGGATCCAGACAATGAATTTGCT
ACGATGTGGATTGAACGGACCACGTATACGACTGCATATACCTTTCCTGGGATTCTCAAG
TGGTTTGAAGTCAAACAGATTTCAACAGAAGAGATCAGTCCTCTGGAGAATGCCATCGAA
ACCATGGAGCTGACCAACGAGAGGATCAGCAACTGTGTTCAGCAGCATGCCTGGGACCGG
TCCCTCTCTGTGCACCCTCTCTCCATGCTGCTCAGTGGCATCGTGGACCCGGCCGTCATG
GGGGGCTTCTCCAACTATGAAAAGGCTTTTTTTACAGAAAAGTACTTGCAGGAGCATCCT
GAAGACCAGGAGAAGGTTGAGCTGCTAAAGCGACTAATAGCATTACAGATGCCCCTGCTA
ACAGAAGGGATCCGCATCCATGGGGAGAAACTCACAGAGCAGCTGAAGCCGCTGCATGAG
CGGTTGTCTTCTTGCTTCCGGGAACTCAAGGAGAAAGTAGAAAAGCACTATGGGGTTATA
ACACTGCCACCCAACTTGACGGAGAGGAAGCAAAGCCGCACGGGGTCTATTGTGCTCCCC
TACATCATGTCTTCCACTCTGCGGAGGTTGTCCATCACCTCAGTCACTTCCTCTGTGGTT
TCCACCTCTTCAAACTCGTCTGACAATGCTCCTTCCAGACCGGGATCTGATGGCTCAATC
TTGGAGCCACTTTTGGAGCGCAGGGCCTCGTCAGGTGCCAGAGTTGAAGATCTGTCCCTT
AGAGAGGAGAACAGCGAGAACCGGATCAGCAAGTTTAAGAGAAAAGACTGGAGTCTGAGC
AAGTCCCAGGTCATTGCAGAGAAAGCACCAGAACCCGATTTGATGAGCCCAACCAGAAAA
GCACAAAGGCCAAAGAGTCTCCAGTTGATGGATAATCGGCTATCACCATTTCACGGTTCT
TCACCTCCTCAGTCAACACCCTTGAGCCCACCTCCACTCACTCCCAAAGCCACCAGGACC
CTAAGCTCCCCATCGTTGCAGACAGATGGAATCGCGGCCACTCCTGTCCCACCTCCACCT
CCCCCCAAAAGCAAGCCCTATGAAGGCAGCCAGAGGAACTCCACTGAGCTCGCTCCCCCA
CTGCCTGTCCGAAGAGAAGCCAAAGCACCACCCCCTCCACCTCCAAAGGCTCGGAAGTCT
GGCATCCCTACTTCCGAGCCTGGATCCCAGTAA
Enzyme 78 GenBank Gene ID NM_024940.6 Link Image
Enzyme 78 GeneCard ID DOCK5 Link Image
Enzyme 78 GenAtlas ID DOCK5 Link Image
Enzyme 78 HGNC ID HGNC:23476 Link Image
Enzyme 78 Chromosome Location 8
Enzyme 78 Locus 8p21.2
Enzyme 78 SNPs SNPJam Report Link Image
Enzyme 78 General References
  1. Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Cote JF, Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J Cell Sci. 2002 Dec 15;115(Pt 24):4901-13. [PubMed Link Image]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  9. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  10. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 78 Metabolite References Not Available
Enzyme 79 [top]
Enzyme 79 ID 14069
Enzyme 79 Name Dedicator of cytokinesis protein 6
Enzyme 79 Synonyms Not Available
Enzyme 79 Gene Name DOCK6
Enzyme 79 Protein Sequence >Dedicator of cytokinesis protein 6
MAASERRAFAHKINRTVAAEVRKQVSRERSGSPHSSRRCSSSLGVPLTEVVEPLDFEDVL
LSRPPDAEPGPLRDLVEFPADDLELLLQPRECRTTEPGIPKDEKLDAQVRAAVEMYIEDW
VIVHRRYQYLSAAYSPVTTDTQRERQKGLPRQVFEQDASGDERSGPEDSNDSRRGSGSPE
DTPRSSGASSIFDLRNLAADSLLPSLLERAAPEDVDRRNETLRRQHRPPALLTLYPAPDE
DEAVERCSRPEPPREHFGQRILVKCLSLKFEIEIEPIFGILALYDVREKKKISENFYFDL
NSDSMKGLLRAHGTHPAISTLARSAIFSVTYPSPDIFLVIKLEKVLQQGDISECCEPYMV
LKEVDTAKNKEKLEKLRLAAEQFCTRLGRYRMPFAWTAVHLANIVSSAGQLDRDSDSEGE
RRPAWTDRRRRGPQDRASSGDDACSFSGFRPATLTVTNFFKQEAERLSDEDLFKFLADMR
RPSSLLRRLRPVTAQLKIDISPAPENPHFCLSPELLHIKPYPDPRGRPTKEILEFPAREV
YAPHTSYRNLLYVYPHSLNFSSRQGSVRNLAVRVQYMTGEDPSQALPVIFGKSSCSEFTR
EAFTPVVYHNKSPEFYEEFKLHLPACVTENHHLLFTFYHVSCQPRPGTALETPVGFTWIP
LLQHGRLRTGPFCLPVSVDQPPPSYSVLTPDVALPGMRWVDGHKGVFSVELTAVSSVHPQ
DPYLDKFFTLVHVLEEGAFPFRLKDTVLSEGNVEQELRASLAALRLASPEPLVAFSHHVL
DKLVRLVIRPPIISGQIVNLGRGAFEAMAHVVSLVHRSLEAAQDARGHCPQLAAYVHYAF
RLPGTEPSLPDGAPPVTVQAATLARGSGRPASLYLARSKSISSSNPDLAVAPGSVDDEVS
RILASKLLHEELALQWVVSSSAVREAILQHAWFFFQLMVKSMALHLLLGQRLDTPRKLRF
PGRFLDDITALVGSVGLEVITRVHKDVELAEHLNASLAFFLSDLLSLVDRGFVFSLVRAH
YKQVATRLQSSPNPAALLTLRMEFTRILCSHEHYVTLNLPCCPLSPPASPSPSVSSTTSQ
SSTFSSQAPDPKVTSMFELSGPFRQQHFLAGLLLTELALALEPEAEGAFLLHKKAISAVH
SLLCGHDTDPRYAEATVKARVAELYLPLLSIARDTLPRLHDFAEGPGQRSRLASMLDSDT
EGEGDIAGTINPSVAMAIAGGPLAPGSRASISQGPPTASRAGCALSAESSRTLLACVLWV
LKNTEPALLQRWATDLTLPQLGRLLDLLYLCLAAFEYKGKKAFERINSLTFKKSLDMKAR
LEEAILGTIGARQEMVRRSRERSPFGNPENVRWRKSVTHWKQTSDRVDKTKDEMEHEALV
EGNLATEASLVVLDTLEIIVQTVMLSEARESVLGAVLKVVLYSLGSAQSALFLQHGLATQ
RALVSKFPELLFEEDTELCADLCLRLLRHCGSRISTIRTHASASLYLLMRQNFEIGHNFA
RVKMQVTMSLSSLVGTTQNFSEEHLRRSLKTILTYAEEDMGLRDSTFAEQVQDLMFNLHM
ILTDTVKMKEHQEDPEMLIDLMYRIARGYQGSPDLRLTWLQNMAGKHAELGNHAEAAQCM
VHAAALVAEYLALLEDHRHLPVGCVSFQNISSNVLEESAISDDILSPDEEGFCSGKHFTE
LGLVGLLEQAAGYFTMGGLYEAVNEVYKNLIPILEAHRDYKKLAAVHGKLQEAFTKIMHQ
SSGWERVFGTYFRVGFYGAHFGDLDEQEFVYKEPSITKLAEISHRLEEFYTERFGDDVVE
IIKDSNPVDKSKLDSQKAYIQITYVEPYFDTYELKDRVTYFDRNYGLRTFLFCTPFTPDG
RAHGELPEQHKRKTLLSTDHAFPYIKTRIRVCHREETVLTPVEVAIEDMQKKTRELAFAT
EQDPPDAKMLQMVLQGSVGPTVNQGPLEVAQVFLAEIPEDPKLFRHHNKLRLCFKDFCKK
CEDALRKNKALIGPDQKEYHRELERNYCRLREALQPLLTQRLPQLMAPTPPGLRNSLNRA
SFRKADL
Enzyme 79 Number of Residues 2047
Enzyme 79 Molecular Weight 229555.6
Enzyme 79 Theoretical pI 6.72
Enzyme 79 GO Classification
Function
  • GTP binding
  • GTPase binding
  • GTPase regulator activity
  • binding
  • enzyme binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
Process
Component
Enzyme 79 General Function Involved in guanyl-nucleotide exchange factor activity
Enzyme 79 Specific Function Potential guanine nucleotide exchange factor (GEF). GEF proteins activate some small GTPases by exchanging bound GDP for free GTP
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 157426887 Link Image
Enzyme 79 UniProtKB/Swiss-Prot ID Q96HP0 Link Image
Enzyme 79 UniProtKB/Swiss-Prot Entry Name DOCK6_HUMAN Link Image
Enzyme 79 PDB ID Not Available
Enzyme 79 Cellular Location Not Available
Enzyme 79 Gene Sequence >6144 bp
ATGGCTGCCTCCGAGCGCCGCGCCTTCGCGCACAAGATCAACAGGACGGTGGCCGCAGAG
GTGCGGAAGCAGGTGTCCCGGGAACGCAGTGGCTCCCCCCACTCCAGCAGGCGCTGCAGC
AGCTCCCTGGGGGTCCCACTGACTGAAGTTGTCGAGCCCCTGGACTTTGAGGATGTACTT
CTGAGCCGGCCACCAGATGCTGAGCCCGGGCCCCTCAGGGACCTGGTAGAATTCCCAGCT
GATGACTTGGAGCTGCTGCTGCAGCCCCGGGAATGCCGGACCACGGAGCCCGGGATCCCC
AAGGATGAAAAACTGGATGCCCAGGTGAGGGCCGCGGTGGAGATGTATATTGAGGACTGG
GTCATTGTCCACAGAAGGTATCAGTACCTGAGTGCAGCATACAGCCCCGTCACCACAGAC
ACACAGCGGGAGCGACAGAAGGGCCTCCCCCGCCAGGTCTTTGAGCAGGATGCTTCTGGA
GACGAGAGGTCCGGCCCTGAGGACTCGAATGACTCCCGGCGTGGCTCGGGCTCCCCGGAA
GACACCCCTCGAAGCAGTGGTGCCTCTAGCATCTTCGACCTGAGGAACCTGGCAGCTGAC
TCATTGCTGCCCTCTCTGCTAGAGCGGGCGGCCCCAGAAGATGTGGACCGGCGCAATGAA
ACCCTTCGACGGCAGCACCGGCCCCCGGCCCTGCTCACCCTCTACCCGGCACCTGACGAG
GATGAAGCCGTGGAACGCTGTAGCCGCCCAGAGCCACCCCGCGAGCACTTTGGACAAAGG
ATCTTGGTCAAGTGTCTGTCGCTCAAGTTCGAGATTGAAATTGAGCCCATCTTTGGGATC
TTGGCTCTGTATGATGTGCGGGAGAAAAAGAAGATCTCGGAGAACTTCTACTTCGACCTG
AACTCGGACTCCATGAAGGGGCTGCTTCGGGCTCATGGCACCCACCCTGCCATCTCCACC
CTGGCCCGCTCTGCCATCTTCTCTGTGACCTACCCCTCACCTGACATCTTCCTGGTCATC
AAGTTGGAGAAGGTGCTTCAGCAAGGGGACATCAGTGAGTGCTGTGAGCCTTACATGGTG
TTGAAAGAAGTGGACACAGCCAAGAACAAAGAGAAGCTAGAGAAGCTGCGCCTGGCGGCC
GAGCAGTTCTGCACCCGCCTGGGCCGCTACCGCATGCCCTTCGCCTGGACGGCCGTGCAC
TTGGCCAACATCGTGAGCAGCGCTGGGCAGCTGGACCGGGACTCTGACTCGGAGGGCGAG
CGCCGGCCAGCCTGGACAGACCGCCGCCGTCGGGGGCCCCAGGACCGGGCGAGTAGTGGG
GACGACGCCTGCAGCTTCTCTGGCTTCCGTCCAGCCACGCTAACTGTCACAAACTTCTTT
AAGCAGGAGGCTGAGCGACTCAGTGACGAGGACCTCTTCAAGTTCCTGGCTGACATGAGG
CGCCCGTCGTCCCTGCTGCGGCGACTACGTCCTGTGACTGCCCAGCTCAAGATCGACATT
TCTCCGGCTCCTGAAAATCCCCACTTCTGCCTCTCCCCTGAGCTGCTTCATATCAAGCCC
TACCCGGACCCCAGGGGCCGGCCCACCAAGGAGATTCTGGAGTTCCCCGCCCGCGAAGTC
TATGCCCCCCATACCAGCTACAGGAACCTGCTGTACGTGTACCCGCACAGCCTCAACTTC
AGCAGCCGCCAGGGCTCCGTGCGCAACCTTGCTGTGCGAGTGCAGTACATGACAGGCGAG
GACCCCAGCCAGGCTCTGCCGGTCATCTTTGGCAAGTCCAGCTGCAGTGAATTTACCCGC
GAGGCCTTCACACCGGTGGTCTACCATAACAAGTCCCCCGAGTTCTACGAGGAGTTCAAG
CTGCATCTTCCAGCCTGCGTGACAGAGAACCATCACCTGCTGTTCACCTTCTACCATGTC
AGCTGCCAGCCCCGGCCGGGCACTGCCCTGGAGACACCCGTGGGCTTTACTTGGATCCCA
CTGCTGCAGCACGGGCGCCTGAGGACCGGCCCCTTCTGTCTCCCAGTGTCTGTGGACCAG
CCGCCGCCCAGCTATTCCGTGCTCACACCCGATGTGGCGCTTCCGGGCATGCGCTGGGTG
GACGGTCACAAGGGCGTGTTCAGTGTGGAGCTCACAGCCGTGTCCTCTGTGCACCCCCAG
GACCCCTACCTGGACAAATTCTTCACCCTGGTGCACGTCCTGGAGGAGGGAGCCTTCCCA
TTCCGGCTCAAGGACACTGTGCTGAGCGAGGGCAACGTGGAGCAGGAGCTGCGGGCCAGT
CTTGCAGCACTGCGCCTGGCCAGCCCCGAACCCCTTGTGGCCTTCTCCCACCACGTGCTG
GACAAGCTCGTGCGTCTGGTCATCAGGCCCCCGATCATCAGTGGCCAGATTGTGAACCTG
GGCCGTGGAGCCTTTGAAGCAATGGCCCATGTAGTCAGCCTTGTTCACCGGAGCCTGGAG
GCAGCCCAGGATGCCCGCGGTCACTGCCCACAGCTGGCTGCCTACGTCCACTACGCCTTT
CGCCTTCCTGGCACTGAGCCCAGCCTCCCGGATGGGGCCCCTCCAGTGACAGTGCAGGCT
GCCACACTGGCCCGTGGCTCTGGTCGCCCCGCAAGCCTCTACCTGGCGCGTTCCAAGAGC
ATCAGCAGCAGCAACCCTGACCTCGCCGTGGCCCCTGGCTCTGTGGATGACGAGGTTTCC
CGCATCCTGGCCAGCAAGCTGCTTCACGAGGAGCTGGCTCTGCAGTGGGTGGTCAGCAGC
AGTGCCGTACGCGAGGCCATCCTCCAGCACGCCTGGTTCTTCTTCCAGCTCATGGTGAAG
AGTATGGCGCTGCACCTGCTGCTTGGCCAGCGACTAGACACACCCCGCAAGCTGCGCTTC
CCCGGACGCTTCCTGGACGACATCACTGCCTTGGTGGGCTCTGTGGGCCTGGAGGTCATC
ACCCGTGTCCACAAGGATGTGGAGCTGGCCGAGCACCTCAACGCCAGCCTGGCTTTCTTC
CTCAGTGACCTTCTGTCCCTGGTGGACCGGGGCTTTGTCTTCAGCCTGGTCCGGGCCCAC
TACAAGCAGGTGGCCACGCGGCTCCAGTCGTCCCCTAATCCAGCAGCCCTGCTGACCCTG
CGCATGGAATTCACCCGCATCCTGTGCAGCCACGAGCACTACGTGACCCTCAACCTCCCC
TGCTGCCCCCTGTCACCTCCAGCCTCGCCCTCCCCCTCTGTGTCCTCCACCACCTCCCAG
AGCTCCACCTTCTCCAGCCAAGCCCCGGACCCCAAGGTGACCAGCATGTTCGAACTGAGT
GGACCATTCCGGCAGCAGCACTTCCTAGCTGGGCTCCTGCTGACGGAGCTGGCACTGGCC
CTCGAACCTGAGGCTGAAGGGGCATTCCTGTTGCACAAGAAGGCCATCAGTGCTGTGCAC
AGCCTGCTATGTGGCCATGACACTGACCCCCGCTACGCCGAGGCCACTGTGAAGGCTCGT
GTGGCCGAGCTGTACCTGCCACTGCTATCGATTGCACGGGATACCTTGCCACGGCTGCAT
GACTTTGCTGAGGGCCCAGGTCAGCGGTCAAGACTGGCCTCAATGCTTGACTCAGACACA
GAAGGCGAAGGGGACATTGCGGGTACCATCAACCCCTCTGTGGCCATGGCCATTGCTGGT
GGCCCCCTAGCCCCTGGCTCCCGGGCCAGCATCTCCCAGGGGCCACCAACGGCTTCTCGC
GCAGGCTGTGCCCTCTCTGCTGAGTCAAGCCGGACCTTGCTGGCGTGTGTGCTGTGGGTG
CTGAAAAACACCGAGCCGGCGCTCCTGCAGCGCTGGGCCACTGACCTGACACTCCCCCAG
CTGGGACGTCTGTTGGATTTGCTGTACCTTTGCCTAGCTGCCTTTGAGTACAAGGGGAAA
AAGGCCTTTGAACGCATCAACAGCCTCACATTCAAAAAATCTCTGGATATGAAGGCGCGG
CTAGAGGAAGCCATTCTGGGTACCATCGGAGCTCGACAAGAAATGGTTCGGCGAAGTCGT
GAGAGGAGCCCGTTTGGGAATCCGGAGAATGTGCGCTGGCGGAAGAGCGTCACACACTGG
AAGCAAACCTCAGACCGCGTGGACAAGACCAAGGATGAAATGGAACACGAGGCCTTGGTG
GAAGGGAACCTGGCAACCGAGGCAAGCCTAGTGGTTCTGGACACACTGGAGATCATCGTG
CAGACGGTGATGCTTTCAGAAGCCCGGGAGAGCGTCTTGGGGGCAGTGCTGAAGGTTGTG
CTGTACAGCCTGGGCAGTGCCCAGAGTGCCCTCTTCTTGCAGCATGGCCTGGCCACCCAG
AGGGCCCTTGTGTCCAAGTTCCCGGAGCTGCTGTTCGAGGAGGACACGGAGCTGTGTGCC
GACCTGTGCCTGAGGCTCCTACGACACTGTGGCAGCCGCATCAGCACCATCCGCACGCAC
GCCAGCGCCTCGCTGTACCTGCTCATGCGACAGAACTTCGAGATCGGCCACAACTTTGCC
CGTGTGAAGATGCAGGTCACCATGTCTCTCTCGTCCCTGGTGGGGACGACGCAGAACTTC
AGTGAAGAGCACCTGCGACGTTCACTCAAAACCATCCTCACCTATGCTGAGGAGGACATG
GGGCTGCGGGACAGCACCTTCGCAGAGCAGGTCCAGGACCTGATGTTCAACCTGCACATG
ATCCTGACGGACACGGTGAAGATGAAGGAACACCAGGAGGACCCTGAGATGCTCATCGAC
CTCATGTACAGAATTGCCCGGGGCTACCAGGGCTCACCGGACCTTCGGCTGACCTGGTTG
CAGAACATGGCCGGGAAGCACGCGGAGCTGGGCAACCACGCCGAGGCCGCCCAGTGCATG
GTGCACGCGGCCGCCCTCGTGGCTGAGTACCTCGCCCTGCTCGAGGACCACCGCCACCTG
CCCGTGGGCTGCGTTTCCTTCCAGAACATCTCATCCAACGTGCTAGAGGAGTCCGCCATC
TCCGACGACATCCTGTCGCCCGACGAGGAGGGCTTCTGCTCCGGGAAGCACTTCACTGAG
CTGGGGCTGGTAGGGTTGCTGGAACAGGCAGCCGGCTACTTCACCATGGGCGGGCTCTAC
GAGGCGGTGAATGAGGTCTACAAGAACCTCATCCCCATCCTGGAAGCCCACCGTGACTAC
AAGAAGCTGGCCGCGGTGCACGGCAAACTGCAGGAGGCCTTCACCAAGATCATGCACCAG
AGTTCCGGCTGGGAGCGCGTGTTCGGGACGTATTTCCGCGTGGGCTTCTACGGCGCCCAC
TTCGGTGACCTGGATGAGCAGGAGTTTGTGTACAAGGAGCCATCGATCACGAAGCTGGCA
GAGATCTCACACCGGCTGGAGGAGTTCTACACGGAGAGATTTGGCGACGACGTCGTTGAG
ATTATCAAAGACTCTAACCCTGTGGACAAGTCCAAGCTTGACTCACAAAAGGCCTACATC
CAGATCACGTATGTGGAACCGTACTTTGATACCTACGAGCTCAAGGACCGGGTGACCTAC
TTTGACCGCAACTATGGGCTTCGCACATTCCTGTTCTGCACGCCGTTCACGCCGGATGGG
CGCGCACACGGGGAGCTGCCCGAGCAACACAAGCGTAAGACGCTGCTCAGCACCGACCAC
GCCTTCCCCTACATCAAGACTCGCATCCGTGTGTGCCACCGGGAGGAGACGGTGCTGACG
CCAGTGGAGGTGGCCATCGAGGACATGCAGAAGAAGACACGGGAGCTGGCCTTTGCCACC
GAGCAGGACCCACCAGATGCTAAGATGCTACAGATGGTGCTTCAGGGCTCTGTAGGGCCC
ACCGTGAACCAGGGTCCCCTGGAGGTGGCCCAGGTGTTTTTAGCAGAGATCCCGGAAGAC
CCCAAGCTCTTCCGGCATCACAACAAATTGCGGCTCTGCTTCAAGGACTTCTGCAAGAAA
TGTGAGGATGCGCTGCGGAAAAATAAGGCCCTGATTGGGCCGGACCAGAAGGAGTACCAC
CGTGAGCTGGAGCGCAACTACTGCCGCCTGCGGGAGGCTCTGCAGCCCCTGCTTACCCAG
CGCCTGCCCCAGCTGATGGCACCCACCCCACCCGGCCTCAGGAACTCCTTGAACAGAGCA
AGTTTCCGAAAGGCAGACCTCTGA
Enzyme 79 GenBank Gene ID NM_020812.2 Link Image
Enzyme 79 GeneCard ID DOCK6 Link Image
Enzyme 79 GenAtlas ID DOCK6 Link Image
Enzyme 79 HGNC ID HGNC:19189 Link Image
Enzyme 79 Chromosome Location 1
Enzyme 79 Locus 19p13.2
Enzyme 79 SNPs SNPJam Report Link Image
Enzyme 79 General References
  1. Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Feb 28;7(1):65-73. [PubMed Link Image]
  2. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Cote JF, Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J Cell Sci. 2002 Dec 15;115(Pt 24):4901-13. [PubMed Link Image]
  5. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  6. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
Enzyme 79 Metabolite References Not Available
Enzyme 80 [top]
Enzyme 80 ID 14070
Enzyme 80 Name Dedicator of cytokinesis protein 7
Enzyme 80 Synonyms Not Available
Enzyme 80 Gene Name DOCK7
Enzyme 80 Protein Sequence >Dedicator of cytokinesis protein 7
MAERRAFAQKISRTVAAEVRKQISGQYSGSPQLLKNLNIVGNISHHTTVPLTEAVDPVDL
EDYLITHPLAVDSGPLRDLIEFPPDDIEVVYSPRDCRTLVSAVPEESEMDPHVRDCIRSY
TEDWAIVIRKYHKLGTGFNPNTLDKQKERQKGLPKQVFESDEAPDGNSYQDDQDDLKRRS
MSIDDTPRGSWACSIFDLKNSLPDALLPNLLDRTPNEEIDRQNDDQRKSNRHKELFALHP
SPDEEEPIERLSVPDIPKEHFGQRLLVKCLSLKFEIEIEPIFASLALYDVKEKKKISENF
YFDLNSEQMKGLLRPHVPPAAITTLARSAIFSITYPSQDVFLVIKLEKVLQQGDIGECAE
PYMIFKEADATKNKEKLEKLKSQADQFCQRLGKYRMPFAWTAIHLMNIVSSAGSLERDST
EVEISTGERKGSWSERRNSSIVGRRSLERTTSGDDACNLTSFRPATLTVTNFFKQEGDRL
SDEDLYKFLADMRRPSSVLRRLRPITAQLKIDISPAPENPHYCLTPELLQVKLYPDSRVR
PTREILEFPARDVYVPNTTYRNLLYIYPQSLNFANRQGSARNITVKVQFMYGEDPSNAMP
VIFGKSSCSEFSKEAYTAVVYHNRSPDFHEEIKVKLPATLTDHHHLLFTFYHVSCQQKQN
TPLETPVGYTWIPMLQNGRLKTGQFCLPVSLEKPPQAYSVLSPEVPLPGMKWVDNHKGVF
NVEVVAVSSIHTQDPYLDKFFALVNALDEHLFPVRIGDMRIMENNLENELKSSISALNSS
QLEPVVRFLHLLLDKLILLVIRPPVIAGQIVNLGQASFEAMASIINRLHKNLEGNHDQHG
RNSLLASYIHYVFRLPNTYPNSSSPGPGGLGGSVHYATMARSAVRPASLNLNRSRSLSNS
NPDISGTPTSPDDEVRSIIGSKGLDRSNSWVNTGGPKAAPWGSNPSPSAESTQAMDRSCN
RMSSHTETSSFLQTLTGRLPTKKLFHEELALQWVVCSGSVRESALQQAWFFFELMVKSMV
HHLYFNDKLEAPRKSRFPERFMDDIAALVSTIASDIVSRFQKDTEMVERLNTSLAFFLND
LLSVMDRGFVFSLIKSCYKQVSSKLYSLPNPSVLVSLRLDFLRIICSHEHYVTLNLPCSL
LTPPASPSPSVSSATSQSSGFSTNVQDQKIANMFELSVPFRQQHYLAGLVLTELAVILDP
DAEGLFGLHKKVINMVHNLLSSHDSDPRYSDPQIKARVAMLYLPLIGIIMETVPQLYDFT
ETHNQRGRPICIATDDYESESGSMISQTVAMAIAGTSVPQLTRPGSFLLTSTSGRQHTTF
SAESSRSLLICLLWVLKNADETVLQKWFTDLSVLQLNRLLDLLYLCVSCFEYKGKKVFER
MNSLTFKKSKDMRAKLEEAILGSIGARQEMVRRSRGQLGTYTIASPPERSPSGSAFGSQE
NLRWRKDMTHWRQNTEKLDKSRAEIEHEALIDGNLATEANLIILDTLEIVVQTVSVTESK
ESILGGVLKVLLHSMACNQSAVYLQHCFATQRALVSKFPELLFEEETEQCADLCLRLLRH
CSSSIGTIRSHASASLYLLMRQNFEIGNNFARVKMQVTMSLSSLVGTSQNFNEEFLRRSL
KTILTYAEEDLELRETTFPDQVQDLVFNLHMILSDTVKMKEHQEDPEMLIDLMYRIAKGY
QTSPDLRLTWLQNMAGKHSERSNHAEAAQCLVHSAALVAEYLSMLEDRKYLPVGCVTFQN
ISSNVLEESAVSDDVVSPDEEGICSGKYFTESGLVGLLEQAAASFSMAGMYEAVNEVYKV
LIPIHEANRDAKKLSTIHGKLQEAFSKIVHQSTGWERMFGTYFRVGFYGTKFGDLDEQEF
VYKEPAITKLAEISHRLEGFYGERFGEDVVEVIKDSNPVDKCKLDPNKAYIQITYVEPYF
DTYEMKDRITYFDKNYNLRRFMYCTPFTLDGRAHGELHEQFKRKTILTTSHAFPYIKTRV
NVTHKEEIILTPIEVAIEDMQKKTQELAFATHQDPADPKMLQMVLQGSVGTTVNQGPLEV
AQVFLSEIPSDPKLFRHHNKLRLCFKDFTKRCEDALRKNKSLIGPDQKEYQRELERNYHR
LKEALQPLINRKIPQLYKAVLPVTCHRDSFSRMSLRKMDL
Enzyme 80 Number of Residues 2140
Enzyme 80 Molecular Weight 242558.3
Enzyme 80 Theoretical pI 6.78
Enzyme 80 GO Classification
Function
  • GTP binding
  • GTPase binding
  • GTPase regulator activity
  • binding
  • enzyme binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
Process
Component
Enzyme 80 General Function Involved in guanyl-nucleotide exchange factor activity
Enzyme 80 Specific Function Functions as a guanine nucleotide exchange factor (GEF), which activates Rac1 and Rac3 Rho small GTPases by exchanging bound GDP for free GTP. Does not have a GEF activity for CDC42. Required for STMN1 'Ser-15' phosphorylation during axon formation and consequently for neuronal polarization
Enzyme 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 54112429 Link Image
Enzyme 80 UniProtKB/Swiss-Prot ID Q96N67 Link Image
Enzyme 80 UniProtKB/Swiss-Prot Entry Name DOCK7_HUMAN Link Image
Enzyme 80 PDB ID Not Available
Enzyme 80 Cellular Location Not Available
Enzyme 80 Gene Sequence >6330 bp
ATGGCCGAGCGCCGCGCCTTCGCCCAGAAGATCAGCAGAACGGTGGCAGCCGAAGTTAGG
AAGCAGATCTCCGGACAATATAGTGGTTCTCCCCAACTGCTCAAAAACCTTAATATTGTT
GGCAATATATCCCATCACACCACAGTGCCCCTTACCGAAGCAGTAGATCCAGTGGATTTG
GAAGATTACCTCATTACTCATCCTTTGGCTGTGGATTCTGGGCCTTTACGGGATTTGATT
GAATTTCCTCCAGATGATATTGAAGTTGTTTATAGTCCTCGGGACTGCAGAACTCTTGTT
TCAGCTGTACCTGAAGAAAGTGAAATGGATCCACATGTTAGAGACTGTATAAGAAGTTAT
ACAGAAGACTGGGCAATTGTCATCAGAAAATATCATAAATTGGGAACAGGATTTAATCCC
AATACATTAGATAAACAGAAAGAAAGGCAAAAAGGTTTGCCAAAACAAGTTTTTGAATCT
GATGAAGCTCCAGATGGCAACAGCTACCAGGATGATCAAGATGACCTTAAAAGACGTTCA
ATGTCAATAGATGATACCCCAAGGGGTAGCTGGGCCTGTAGTATCTTTGACTTGAAAAAT
TCACTTCCTGATGCTTTGCTTCCCAATTTACTTGATCGAACTCCAAATGAAGAAATAGAC
CGTCAGAATGATGACCAAAGGAAATCAAACCGTCACAAAGAACTTTTTGCTTTGCATCCA
TCACCAGATGAGGAAGAACCAATAGAACGGCTTAGTGTTCCTGATATACCCAAAGAACAT
TTTGGTCAAAGACTTCTTGTAAAATGCTTATCACTCAAGTTTGAAATTGAAATTGAACCC
ATTTTTGCAAGTTTGGCTTTATATGATGTCAAGGAAAAGAAAAAGATTTCAGAAAACTTT
TATTTTGACCTTAATTCTGAGCAGATGAAAGGGTTGTTACGTCCACATGTACCACCTGCT
GCCATTACTACCCTGGCAAGATCAGCAATTTTTTCTATCACTTATCCTTCCCAAGATGTT
TTTCTTGTAATAAAGCTAGAAAAAGTCCTACAGCAAGGAGACATTGGAGAGTGTGCAGAA
CCATATATGATTTTCAAAGAAGCAGATGCCACCAAGAATAAAGAAAAACTGGAGAAACTG
AAGAGTCAAGCAGATCAGTTTTGCCAAAGACTTGGGAAATATCGCATGCCTTTTGCTTGG
ACTGCAATCCATTTAATGAATATTGTTAGCAGTGCTGGGAGTTTGGAAAGAGATTCTACA
GAAGTAGAAATCAGTACTGGAGAACGAAAAGGGTCTTGGTCAGAGAGGAGGAATTCTAGT
ATTGTTGGCAGACGATCACTTGAAAGGACAACAAGTGGAGATGATGCTTGTAACTTGACG
AGCTTTCGACCAGCTACTCTCACAGTGACAAATTTTTTTAAGCAGGAAGGAGACCGCTTA
AGTGATGAAGATCTCTACAAATTCCTTGCTGATATGAGAAGGCCATCTTCTGTCTTACGG
CGACTAAGACCTATTACAGCTCAGCTCAAGATAGACATTTCTCCCGCACCTGAAAATCCC
CATTATTGCCTAACTCCGGAGCTGCTTCAAGTGAAGCTTTACCCTGACAGTAGAGTTAGA
CCTACCAGAGAAATCTTAGAGTTTCCCGCAAGGGATGTTTATGTTCCAAACACTACTTAC
AGAAATCTTCTCTACATATACCCTCAGAGTCTTAATTTTGCCAATCGTCAAGGTTCTGCT
AGAAATATAACAGTGAAAGTCCAGTTTATGTATGGAGAGGATCCAAGCAATGCCATGCCG
GTAATCTTTGGTAAATCTAGCTGTTCAGAATTTTCAAAGGAAGCCTATACAGCCGTAGTA
TATCATAACAGGTCTCCTGATTTTCATGAAGAAATCAAGGTTAAGCTTCCTGCTACTTTA
ACTGACCATCATCACTTGCTTTTTACTTTTTATCATGTTAGTTGTCAACAAAAACAAAAT
ACTCCTCTTGAAACACCAGTTGGATATACATGGATACCAATGCTTCAGAATGGACGGTTG
AAGACTGGCCAGTTTTGCTTGCCAGTCTCATTGGAAAAACCACCACAGGCTTATTCTGTA
CTGTCTCCTGAGGTTCCTCTACCTGGCATGAAATGGGTAGATAATCACAAAGGTGTTTTT
AATGTTGAAGTTGTTGCTGTTTCGTCTATCCATACACAAGATCCTTATCTTGACAAATTT
TTTGCTCTGGTCAATGCTCTGGATGAACACCTGTTCCCAGTCCGAATTGGGGACATGCGA
ATCATGGAAAATAACTTAGAAAATGAATTGAAGAGCAGTATTTCAGCACTGAATTCATCC
CAGCTGGAACCAGTGGTCCGATTTCTTCATCTTCTGCTAGATAAACTGATACTTTTAGTT
ATTAGACCTCCTGTCATTGCTGGCCAAATAGTTAACCTAGGTCAAGCATCTTTTGAAGCC
ATGGCATCAATTATAAATCGACTTCACAAAAACTTGGAAGGAAATCATGACCAGCATGGC
AGAAACAGCCTTCTTGCATCATATATTCATTATGTTTTCCGCCTACCAAATACTTACCCT
AATTCATCATCACCAGGTCCTGGGGGTTTGGGAGGATCAGTGCATTATGCCACAATGGCT
AGATCTGCGGTGAGACCTGCAAGCCTTAATTTAAATCGTTCTCGAAGCCTTAGTAATAGC
AATCCAGATATATCTGGGACTCCCACGTCACCAGATGATGAAGTTCGATCAATCATCGGG
AGTAAGGCTATGGATCGAAGTTGTAATCGTATGTCTTCGCACACAGAGACGTCAAGTTTC
TTACAAACATTAACGGGACGCTTACCAACTAAAAAGCTTTTTCACGAGGAGCTGGCTTTG
CAGTGGGTTGTTTGCAGTGGCAGCGTTCGGGAATCAGCTTTGCAACAAGCCTGGTTCTTT
TTTGAATTAATGGTAAAGAGCATGGTGCACCATTTATACTTTAATGATAAACTTGAGGCT
CCAAGGAAAAGTCGTTTTCCAGAACGTTTCATGGATGACATTGCAGCTCTTGTCAGCACG
ATTGCTAGTGATATAGTTTCACGATTTCAGAAGGACACAGAAATGGTTGAGAGACTCAAT
ACAAGCCTTGCATTCTTTCTCAATGATCTGTTGTCTGTTATGGACAGAGGATTTGTTTTT
AGCCTTATAAAGTCCTGCTATAAACAGGTGTCTTCAAAGCTTTACTCATTACCGAATCCC
AGTGTTCTGGTGTCCTTGAGGCTGGATTTTCTACGAATCATCTGCAGTCATGAGCACTAT
GTTACATTAAACTTACCCTGCAGCTTACTTACTCCACCTGCATCTCCATCACCTTCTGTT
TCTTCTGCAACATCTCAGAGTTCTGGATTTTCTACGAATGTACAAGACCAAAAGATTGCA
AATATGTTTGAATTATCCGTGCCTTTCCGCCAACAGCATTATTTGGCAGGACTTGTGTTA
ACAGAGCTGGCTGTCATTTTAGACCCTGATGCTGAAGGACTGTTTGGATTGCATAAGAAA
GTCATCAATATGGTACACAATTTACTCTCCAGTCACGACTCAGACCCGCGGTACTCTGAC
CCTCAGATAAAGGCTCGAGTGGCCATGTTGTATCTACCTCTGATTGGTATTATCATGGAA
ACTGTACCTCAGCTGTATGATTTTACAGAAACTCACAATCAACGAGGAAGACCAATTTGT
ATAGCCACTGATGATTATGAAAGTGAGAGCGGAAGTATGATAAGCCAGACCGTTGCCATG
GCAATCGCAGGGACATCGGTCCCTCAACTAACAAGGCCTGGCAGTTTCCTCCTCACGTCA
ACGAGTGGCAGGCAACACACTACCTTTTCAGCAGAATCAAGTCGAAGCCTTTTGATCTGT
CTACTTTGGGTTCTCAAAAATGCAGATGAAACAGTTCTACAGAAGTGGTTTACAGATCTC
TCAGTCTTGCAGCTAAACCGGCTATTAGATCTGCTTTATCTCTGTGTGTCTTGCTTTGAG
TATAAAGGGAAAAAAGTGTTTGAACGAATGAATAGCTTGACCTTTAAGAAATCAAAAGAC
ATGAGAGCAAAGCTTGAAGAAGCTATTCTTGGGAGCATAGGTGCCAGGCAAGAAATGGTA
CGGCGAAGCCGAGGACAGCTCGGTACGTACACAATAGCTTCTCCTCCTGAGAGAAGCCCA
TCTGGAAGTGCCTTTGGAAGTCAAGAAAATTTGAGGTGGAGGAAAGATATGACTCACTGG
CGTCAAAACACAGAGAAGCTTGACAAATCAAGAGCAGAGATTGAACACGAAGCACTGATT
GATGGAAACCTGGCTACAGAAGCAAACCTAATCATTTTAGATACATTAGAGATTGTTGTT
CAGACCGTTTCTGTAACGGAATCCAAAGAGAGCATTCTTGGTGGAGTGCTAAAAGTGCTA
CTACACAGCATGGCCTGTAACCAAAGTGCAGTTTATCTACAACACTGTTTTGCTACACAG
AGAGCCTTGGTTTCAAAGTTTCCTGAACTCTTATTTGAAGAAGAGACAGAGCAGTGTGCT
GATTTATGCCTCAGGCTTCTCCGACACTGTAGCAGTAGCATCGGTACAATACGGTCACAC
GCCAGTGCCTCCCTTTACCTACTAATGAGGCAAAACTTTGAGATTGGGAATAACTTTGCC
AGGGTTAAAATGCAGGTAACAATGTCACTATCCTCCTTGGTGGGCACATCTCAGAATTTT
AATGAAGAATTCTTAAGACGTTCTCTAAAGACTATATTGACATATGCTGAAGAAGATCTG
GAATTGAGGGAAACAACATTTCCTGATCAGGTCCAGGATCTGGTTTTCAATCTCCATATG
ATTCTTTCTGATACTGTGAAAATGAAGGAACACCAGGAGGATCCTGAAATGTTGATTGAT
CTAATGTACAGAATTGCCAAGGGTTACCAGACCTCTCCAGATCTGCGATTGACCTGGTTG
CAGAACATGGCAGGCAAGCACTCAGAACGAAGCAATCATGCTGAAGCTGCACAGTGTCTA
GTCCACTCAGCAGCACTTGTTGCTGAATATTTGAGCATGCTGGAGGACCGGAAATATCTT
CCTGTGGGATGTGTAACATTTCAGAATATTTCATCTAATGTTTTAGAAGAATCTGCGGTC
TCAGATGATGTGGTATCTCCAGATGAAGAAGGTATCTGCTCTGGAAAATACTTTACTGAG
TCAGGACTTGTGGGATTACTGGAACAAGCAGCTGCTTCCTTCTCTATGGCTGGCATGTAT
GAAGCAGTTAATGAAGTTTACAAAGTACTTATTCCTATTCATGAAGCTAATCGGGATGCA
AAGAAACTATCCACAATTCATGGTAAACTTCAAGAAGCATTCAGCAAAATTGTTCATCAG
AGTACTGGCTGGGAGCGGATGTTTGGCACCTATTTTCGTGTTGGTTTTTATGGAACCAAG
TTCGGGGATTTGGATGAACAAGAATTTGTTTACAAGGAGCCTGCAATAACCAAACTTGCA
GAGATATCTCACAGATTGGAGGGATTTTACGGAGAAAGATTTGGAGAGGATGTGGTTGAA
GTAATCAAAGACTCTAATCCTGTAGACAAGTGTAAATTAGATCCTAACAAGGCATATATT
CAGATTACCTATGTGGAGCCATACTTTGACACATATGAGATGAAGGACAGAATCACCTAT
TTCGACAAAAATTACAATCTTCGTCGATTCATGTACTGTACACCCTTTACTTTAGATGGC
CGTGCCCATGGGGAACTTCATGAACAATTCAAAAGGAAGACCATTCTGACTACGTCTCAT
GCCTTTCCTTATATTAAAACAAGGGTCAATGTCACTCATAAAGAAGAGATCATCTTAACA
CCAATTGAAGTTGCTATTGAGGACATGCAGAAAAAGACACAGGAGTTGGCATTTGCAACA
CATCAGGATCCCGCAGACCCCAAAATGCTTCAGATGGTACTCCAGGGATCTGTAGGCACC
ACAGTGAATCAGGGGCCTTTGGAAGTTGCCCAGGTTTTTCTGTCTGAAATACCTAGTGAC
CCAAAGCTCTTCAGACATCATAATAAACTGCGACTCTGCTTTAAAGATTTTACTAAAAGG
TGTGAAGATGCCTTAAGAAAAAATAAGAGCTTAATTGGGCCGGATCAAAAGGAGTATCAA
AGGGAACTGGAGAGAAACTATCATCGCCTTAAAGAGGCCCTACAGCCACTGATCAACAGA
AAGATCCCTCAGTTATACAAGGCAGTATTGCCTGTCACCTGCCACAGAGATTCCTTCAGT
CGAATGAGCCTTCGCAAAATGGATCTCTAA
Enzyme 80 GenBank Gene ID Not Available
Enzyme 80 GeneCard ID DOCK7 Link Image
Enzyme 80 GenAtlas ID DOCK7 Link Image
Enzyme 80 HGNC ID HGNC:19190 Link Image
Enzyme 80 Chromosome Location 1
Enzyme 80 Locus 1p31.3
Enzyme 80 SNPs SNPJam Report Link Image
Enzyme 80 General References
  1. Watabe-Uchida M, John KA, Janas JA, Newey SE, Van Aelst L: The Rac activator DOCK7 regulates neuronal polarity through local phosphorylation of stathmin/Op18. Neuron. 2006 Sep 21;51(6):727-39. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Nagase T, Kikuno R, Hattori A, Kondo Y, Okumura K, Ohara O: Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Dec 31;7(6):347-55. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Cote JF, Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J Cell Sci. 2002 Dec 15;115(Pt 24):4901-13. [PubMed Link Image]
  7. Nellist M, Burgers PC, van den Ouweland AM, Halley DJ, Luider TM: Phosphorylation and binding partner analysis of the TSC1-TSC2 complex. Biochem Biophys Res Commun. 2005 Aug 5;333(3):818-26. [PubMed Link Image]
  8. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  9. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
  10. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  11. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  12. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  13. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  14. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 80 Metabolite References Not Available
Enzyme 81 [top]
Enzyme 81 ID 14071
Enzyme 81 Name Dedicator of cytokinesis protein 8
Enzyme 81 Synonyms Not Available
Enzyme 81 Gene Name DOCK8
Enzyme 81 Protein Sequence >Dedicator of cytokinesis protein 8
MATLPSAERRAFALKINRYSSAEIRKQFTLPPNLGQYHRQSISTSGFPSLQLPQFYDPVE
PVDFEGLLMTHLNSLDVQLAQELGDFTDDDLDVVFTPKECRTLQPSLPEEGVELDPHVRD
CVQTYIREWLIVNRKNQGSPEICGFKKTGSRKDFHKTLPKQTFESETLECSEPAAQAGPR
HLNVLCDVSGKGPVTACDFDLRSLQPDKRLENLLQQVSAEDFEKQNEEARRTNRQAELFA
LYPSVDEEDAVEIRPVPECPKEHLGNRILVKLLTLKFEIEIEPLFASIALYDVKERKKIS
ENFHCDLNSDQFKGFLRAHTPSVAASSQARSAVFSVTYPSSDIYLVVKIEKVLQQGEIGD
CAEPYTVIKESDGGKSKEKIEKLKLQAESFCQRLGKYRMPFAWAPISLSSFFNVSTLERE
VTDVDSVVGRSSVGERRTLAQSRRLSERALSLEENGVGSNFKTSTLSVSSFFKQEGDRLS
DEDLFKFLADYKRSSSLQRRVKSIPGLLRLEISTAPEIINCCLTPEMLPVKPFPENRTRP
HKEILEFPTREVYVPHTVYRNLLYVYPQRLNFVNKLASARNITIKIQFMCGEDASNAMPV
IFGKSSGPEFLQEVYTAVTYHNKSPDFYEEVKIKLPAKLTVNHHLLFTFYHISCQQKQGA
SVETLLGYSWLPILLNERLQTGSYCLPVALEKLPPNYSMHSAEKVPLQNPPIKWAEGHKG
VFNIEVQAVSSVHTQDNHLEKFFTLCHSLESQVTFPIRVLDQKISEMALEHELKLSIICL
NSSRLEPLVLFLHLVLDKLFQLSVQPMVIAGQTANFSQFAFESVVAIANSLHNSKDLSKD
QHGRNCLLASYVHYVFRLPEVQRDVPKSGAPTALLDPRSYHTYGRTSAAAVSSKLLQARV
MSSSNPDLAGTHSAADEEVKNIMSSKIADRNCSRMSYYCSGSSDAPSSPAAPRPASKKHF
HEELALQMVVSTGMVRETVFKYAWFFFELLVKSMAQHVHNMDKRDSFRRTRFSDRFMDDI
TTIVNVVTSEIAALLVKPQKENEQAEKMNISLAFFLYDLLSLMDRGFVFNLIRHYCSQLS
AKLSNLPTLISMRLEFLRILCSHEHYLNLNLFFMNADTAPTSPCPSISSQNSSSCSSFQD
QKIASMFDLTSEYRQQHFLTGLLFTELAAALDAEGEGISKVQRKAVSAIHSLLSSHDLDP
RCVKPEVKVKIAALYLPLVGIILDALPQLCDFTVADTRRYRTSGSDEEQEGAGAINQNVA
LAIAGNNFNLKTSGIVLSSLPYKQYNMLNADTTRNLMICFLWIMKNADQSLIRKWIADLP
STQLNRILDLLFICVLCFEYKGKQSSDKVSTQVLQKSRDVKARLEEALLRGEGARGEMMR
RRAPGNDRFPGLNENLRWKKEQTHWRQANEKLDKTKAELDQEALISGNLATEAHLIILDM
QENIIQASSALDCKDSLLGGVLRVLVNSLNCDQSTTYLTHCFATLRALIAKFGDLLFEEE
VEQCFDLCHQVLHHCSSSMDVTRSQACATLYLLMRFSFGATSNFARVKMQVTMSLASLVG
RAPDFNEEHLRRSLRTILAYSEEDTAMQMTPFPTQVEELLCNLNSILYDTVKMREFQEDP
EMLMDLMYRIAKSYQASPDLRLTWLQNMAEKHTKKKCYTEAAMCLVHAAALVAEYLSMLE
DHSYLPVGSVSFQNISSNVLEESVVSEDTLSPDEDGVCAGQYFTESGLVGLLEQAAELFS
TGGLYETVNEVYKLVIPILEAHREFRKLTLTHSKLQRAFDSIVNKDHKRMFGTYFRVGFF
GSKFGDLDEQEFVYKEPAITKLPEISHRLEAFYGQCFGAEFVEVIKDSTPVDKTKLDPNK
AYIQITFVEPYFDEYEMKDRVTYFEKNFNLRRFMYTTPFTLEGRPRGELHEQYRRNTVLT
TMHAFPYIKTRISVIQKEEFVLTPIEVAIEDMKKKTLQLAVAINQEPPDAKMLQMVLQGS
VGATVNQGPLEVAQVFLAEIPADPKLYRHHNKLRLCFKEFIMRCGEAVEKNKRLITADQR
EYQQELKKNYNKLKENLRPMIERKIPELYKPIFRVESQKRDSFHRSSFRKCETQLSQGS
Enzyme 81 Number of Residues 2099
Enzyme 81 Molecular Weight 238526.7
Enzyme 81 Theoretical pI 6.86
Enzyme 81 GO Classification
Function
  • GTP binding
  • GTPase binding
  • GTPase regulator activity
  • binding
  • enzyme binding
  • enzyme regulator activity
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
  • nucleotide binding
  • protein binding
  • purine nucleotide binding
Process
Component
Enzyme 81 General Function Involved in binding
Enzyme 81 Specific Function Potential guanine nucleotide exchange factor (GEF). GEF proteins activate some small GTPases by exchanging bound GDP for free GTP
Enzyme 81 Pathways Not Available
Enzyme 81 Reactions Not Available
Enzyme 81 Pfam Domain Function
Enzyme 81 Signals
  • None
Enzyme 81 Transmembrane Regions
  • None
Enzyme 81 Essentiality Not Available
Enzyme 81 GenBank ID Protein 76150613 Link Image
Enzyme 81 UniProtKB/Swiss-Prot ID Q8NF50 Link Image
Enzyme 81 UniProtKB/Swiss-Prot Entry Name DOCK8_HUMAN Link Image
Enzyme 81 PDB ID Not Available
Enzyme 81 Cellular Location Not Available
Enzyme 81 Gene Sequence >6300 bp
ATGGCCACTCTGCCGAGCGCAGAGCGCCGCGCGTTCGCGCTCAAGATCAACAGGTATTCT
TCAGTGGAAATAAGGAAACAGTTTACTCTCCCACCAAACCTTGGCCAGTACCATCGACAG
AGCATAAGTACCTCTGGCTTCCCCTCTCTTCAACTACCTCAGTTTTATGACCCTGTGGAG
CCAGTGGACTTTGAAGGACTTCTGATGACACACCTGAACAGCCTGGATGTGCAGCTTGCC
CAGGAGCTCGGGGACTTCACTGATGACGACTTGGACGTGGTGTTCACGACAAAGGAATGT
AGGACTTTGCAGCCCTCTTTGCCGGAGGAAGGGGTTGAACTGGACCCTCATGTCAGGGAC
TGTGTTCAGACCTACATCCGTGAGTGGCTAATCGTGAACCGGAAAAACCAAGGAAGTCCA
GAAATCTGTGGCTTTAAAAAGACTGGATCTCGAAAAGATTTTCACAAGACGCTTCCGAAA
CAGACGTTTGAGTCGGAAACCTTGGAGTGCAGTGAACCCGCTGCTCAGGCAGGCCCCCGC
CACTTAAACGTGCTGTGCGACGTGTCTGGGAAAGGCCCCGTCACTGCCTGTGACTTTGAC
CTCCGCAGCCTGCAGCCTGACAAGCGGCTAGAAAACCTCCTGCAGCAAGTGAGTGCCGAG
GACTTTGAGAAGCAGAACGAGGAGGCCCGGAGGACCAATAGGCAGGCCGAGCTCTTTGCC
CTTTACCCATCAGTGGACGAGGAGGATGCTGTGGAAATACGTCCAGTACCAGAATGTCCC
AAGGAACACCTGGGCAACAGAATATTGGTCAAGTTGCTGACCTTGAAGTTCGAGATTGAA
ATTGAGCCCCTGTTTGCCAGCATTGCCCTCTACGATGTTAAAGAAAGGAAAAAGATCTCA
GAAAATTTTCACTGTGACCTGAACTCTGACCAGTTCAAAGGATTTCTGCGAGCTCACACG
CCTTCAGTGGCCGCATCAAGTCAGGCGAGATCTGCAGTCTTCTCAGTCACCTACCCGTCC
TCAGACATCTACCTGGTAGTCAAGATTGAAAAAGTCCTGCAGCAGGGAGAGATTGGAGAC
TGTGCAGAGCCCTACACGGTTATCAAAGAAAGTGATGGTGGAAAGAGTAAAGAAAAGATT
GAAAAACTAAAACTCCAAGCTGAATCCTTCTGCCAGCGTTTGGGGAAATACCGGATGCCC
TTTGCCTGGGCACCCATAAGCTTATCAAGCTTCTTCAATGTCTCCACCCTTGAGAGGGAG
GTAACTGATGTGGACTCTGTGGTTGGGAGAAGCTCAGTGGGTGAACGGAGGACATTGGCC
CAATCTAGAAGGCTTTCTGAAAGAGCCCTCTCCTTGGAGGAAAATGGGGTTGGATCCAAC
TTCAAAACCTCCACTCTGAGCGTTAGCAGCTTTTTCAAGCAGGAAGGAGATCGCCTTAGC
GATGAAGACTTATTCAAGTTTTTAGCTGACTACAAAAGATCATCATCCTTACAGAGACGA
GTCAAGTCAATTCCAGGCTTGCTAAGACTGGAGATTTCTACAGCTCCAGAGATCATCAAT
TGCTGTCTGACTCCTGAAATGCTGCCCGTGAAACCCTTTCCTGAAAACCGGACACGCCCG
CACAAAGAGATTTTGGAATTTCCAACACGAGAAGTATATGTCCCTCACACTGTGTACAGA
AACCTTCTCTATGTCTACCCACAGAGGCTGAACTTTGTAAACAAACTAGCATCAGCCCGG
AACATTACAATAAAGATCCAGTTTATGTGTGGAGAAGATGCTAGCAATGCGATGCCGGTC
ATCTTTGGAAAGTCCAGCGGGCCTGAATTTCTGCAGGAAGTGTACACAGCTGTTACATAC
CATAATAAGTCTCCTGACTTTTATGAAGAAGTGAAAATTAAGCTCCCCGCTAAGCTCACA
GTAAATCACCACCTCCTGTTCACCTTCTACCATATCAGCTGTCAGCAGAAGCAAGGAGCC
TCCGTGGAAACTCTCCTGGGATATTCATGGCTGCCAATTCTCTTAAATGAACGTCTTCAA
ACTGGATCCTACTGTCTCCCAGTTGCCTTGGAAAAATTGCCACCCAACTACTCCATGCAT
TCTGCTGAGAAAGTCCCATTACAGAATCCTCCCATTAAGTGGGCTGAAGGACATAAGGGA
GTATTTAATATTGAAGTGCAAGCTGTTTCTTCTGTACACACCCAGGACAACCACCTGGAG
AAGTTCTTCACCCTCTGCCACTCCCTGGAGAGCCAGGTGACCTTCCCCATCCGCGTGCTG
GATCAGAAAATCAGCGAGATGGCGCTGGAGCATGAGCTGAAGCTCAGCATCATCTGCCTC
AACTCCTCCCGCCTGGAGCCGCTCGTGCTCTTCCTGCACCTGGTGCTGGACAAGCTCTTC
CAGCTGTCCGTGCAGCCCATGGTCATCGCTGGCCAGACAGCCAACTTCTCCCAGTTTGCC
TTCGAGTCCGTGGTGGCCATCGCCAACAGTCTGCACAACAGCAAGGACCTGAGCAAGGAC
CAGCATGGGAGGAACTGCCTGCTGGCTTCCTACGTGCACTACGTCTTCCGCCTGCCAGAG
GTGCAAAGGGATGTGCCCAAGTCAGGCGCTCCCACTGCCCTCCTAGACCCTCGGAGCTAC
CACACGTATGGCCGCACATCAGCTGCTGCTGTGAGTTCAAAGCTGCTGCAGGCCCGGGTG
ATGAGCAGCAGTAACCCAGACCTCGCGGGGACACACTCCGCAGCAGACGAGGAAGTGAAG
AACATCATGTCTTCAAAGATCGCCGATCGCAACTGCAGCCGAATGTCTTACTATTGCTCT
GGCAGTAGTGATGCTCCAAGTTCACCTGCAGCCCCAAGGCCAGCCAGCAAAAAGCATTTC
CATGAGGAGCTTGCCCTTCAGATGGTGGTCAGCACCGGAATGGTGAGAGAAACAGTCTTC
AAGTATGCCTGGTTCTTCTTTGAGCTTCTGGTGAAAAGCATGGCCCAGCACGTACATAAC
ATGGACAAACGGGACAGTTTTCGGAGGACTCGTTTTTCTGACCGTTTCATGGATGACATA
ACTACTATTGTTAATGTGGTCACCTCGGAAATTGCAGCCCTTTTAGTAAAACCACAGAAG
GAAAATGAACAGGCGGAAAAGATGAACATCAGCCTGGCTTTCTTCTTGTATGACCTTCTC
TCCCTCATGGATCGGGGCTTTGTGTTTAACCTCATCAGACATTATTGCAGCCAGCTGTCA
GCCAAGCTCAGTAACCTTCCAACGCTCATTTCCATGAGGCTAGAGTTCCTGAGAATCCTC
TGTAGCCATGAGCATTACCTCAATCTGAACCTTTTTTTTATGAATGCTGATACTGCTCCA
ACATCTCCTTGTCCTTCCATATCTTCCCAGAACTCAAGCTCCTGCTCCAGCTTCCAGGAC
CAGAAGATCGCCAGCATGTTCGATCTGACTTCCGAGTACCGCCAGCAGCACTTCCTCACC
GGGCTCCTCTTCACAGAACTGGCTGCTGCCCTGGATGCCGAAGGGGAAGGAATCAGCAAA
GTACAAAGGAAAGCTGTCAGTGCAATTCACAGCCTGCTAAGTTCTCACGACCTGGACCCA
CGCTGTGTCAAACCAGAGGTGAAGGTCAAAATCGCCGCCCTTTACCTACCTTTAGTTGGC
ATCATTTTGGATGCTTTGCCACAGCTCTGTGACTTTACAGTTGCAGATACTCGCAGATAC
CGCACCAGTGGCTCGGATGAAGAACAAGAAGGAGCCGGTGCCATTAACCAGAATGTGGCT
CTGGCCATAGCAGGGAATAATTTCAATTTGAAAACAAGTGGAATAGTGCTGTCTTCCTTG
CCCTATAAGCAGTACAACATGCTGAACGCGGACACTACTCGCAACCTCATGATCTGCTTC
CTCTGGATCATGAAAAATGCTGATCAGAGCCTCATTAGGAAGTGGATTGCTGACCTGCCA
TCAACGCAGCTCAACAGGATTTTAGATCTACTTTTCATCTGTGTGTTATGTTTTGAGTAT
AAGGGAAAACAGAGTTCTGACAAAGTCAGTACCCAAGTCCTGCAGAAGTCAAGGGATGTC
AAGGCCCGGCTGGAAGAGGCTTTGCTCCGTGGGGAAGGGGCCAGAGGGGAGATGATGCGC
CGCCGGGCTCCAGGGAACGACCGATTTCCAGGCCTAAATGAAAATTTGAGATGGAAGAAA
GAGCAGACACATTGGCGGCAAGCTAATGAGAAGCTAGATAAAACAAAGGCCGAGTTAGAT
CAAGAAGCCTTGATCAGTGGCAATCTGGCTACAGAAGCACATTTAATCATCCTGGATATG
CAGGAAAACATTATCCAGGCGAGCTCGGCTCTGGACTGTAAAGACAGCCTGCTGGGAGGT
GTTCTGAGGGTGCTGGTGAATTCTCTGAACTGTGATCAGAGTACCACCTACCTGACTCAC
TGCTTTGCAACACTCCGTGCTCTCATCGCCAAGTTTGGAGACTTACTCTTCGAAGAGGAG
GTGGAACAGTGTTTCGACCTATGTCACCAAGTCCTGCACCACTGCAGCAGCAGCATGGAT
GTCACCCGGAGCCAAGCCTGTGCCACCCTTTACCTCCTCATGAGGTTCAGTTTTGGAGCC
ACCAGTAATTTTGCAAGAGTAAAGATGCAAGTAACCATGTCCCTGGCATCTTTGGTGGGA
AGAGCACCAGACTTTAATGAAGAGCACCTGAGAAGATCCTTGAGGACAATTTTGGCCTAT
TCAGAAGAGGACACAGCCATGCAGATGACTCCTTTTCCCACCCAGGTGGAGGAACTTCTC
TGTAATCTGAATAGCATCTTATATGACACAGTGAAAATGAGGGAATTTCAGGAAGATCCT
GAGATGCTTATGGATCTCATGTACAGAATTGCCAAGAGTTACCAGGCATCTCCTGATCTG
CGGCTGACCTGGCTCCAGAACATGGCAGAGAAACACACCAAGAAGAAGTGCTACACGGAG
GCTGCCATGTGCCTGGTGCACGCCGCTGCGTTAGTGGCTGAGTATCTGAGCATGCTGGAG
GACCACAGCTACCTGCCCGTGGGCAGTGTCAGCTTCCAGAATATTTCTTCCAATGTGCTG
GAGGAGTCTGTGGTCTCTGAGGACACCCTGTCACCTGACGAGGATGGGGTGTGCGCAGGC
CAGTACTTCACCGAGAGTGGCCTGGTAGGCCTCCTGGAGCAGGCCGCGGAGCTCTTCAGC
ACGGGAGGCTTATATGAGACAGTTAATGAGGTCTACAAGCTGGTCATCCCCATCCTAGAA
GCGCATCGAGAATTCCGGAAGCTGACACTCACTCACAGCAAGCTGCAGAGAGCCTTCGAC
AGCATCGTTAACAAGGATCATAAGAGAATGTTTGGAACCTACTTCCGAGTTGGTTTCTTT
GGATCCAAATTTGGGGATTTGGATGAACAGGAGTTTGTCTACAAAGAGCCTGCAATTACC
AAGCTTCCTGAGATCTCACATAGACTAGAGGCATTTTATGGTCAATGTTTTGGTGCAGAA
TTTGTGGAAGTGATTAAAGACTCCACTCCTGTGGACAAAACCAAGTTGGATCCTAACAAG
GCCTACATACAGATCACTTTTGTGGAGCCCTACTTTGATGAGTATGAGATGAAAGACAGG
GTCACATACTTTGAGAAGAATTTCAACCTCCGGAGGTTCATGTACACCACCCCGTTCACC
CTGGAGGGGCGGCCTCGGGGAGAGCTGCATGAGCAGTACAGAAGGAACACAGTCCTGACC
ACTATGCACGCCTTCCCCTACATCAAGACCAGGATCAGCGTCATCCAGAAGGAGGAGTTT
GTTTTGACACCGATTGAAGTTGCCATTGAAGACATGAAGAAGAAGACCCTGCAGTTAGCA
GTTGCCATTAACCAGGAGCCGCCTGATGCAAAGATGCTTCAGATGGTGCTGCAAGGCTCT
GTGGGAGCTACTGTAAATCAGGGACCACTGGAAGTAGCCCAAGTGTTTTTGGCTGAAATT
CCTGCTGATCCAAAACTCTATCGACATCACAACAAGTTGAGGTTATGCTTTAAGGAATTC
ATCATGAGATGTGGTGAAGCTGTAGAGAAAAACAAGCGTCTCATCACGGCAGACCAGAGG
GAATATCAGCAGGAACTCAAAAAGAACTATAACAAGCTAAAAGAGAACCTCAGGCCAATG
ATCGAGCGGAAAATTCCAGAACTGTACAAGCCAATATTCAGAGTTGAGAGTCAAAAGAGG
GACTCCTTCCACAGATCTAGTTTCAGGAAATGTGAAACCCAGTTGTCACAGGGCAGCTAA
Enzyme 81 GenBank Gene ID AB191037 Link Image
Enzyme 81 GeneCard ID DOCK8 Link Image
Enzyme 81 GenAtlas ID DOCK8 Link Image
Enzyme 81 HGNC ID HGNC:19191 Link Image
Enzyme 81 Chromosome Location 9
Enzyme 81 Locus 9p24.3
Enzyme 81 SNPs SNPJam Report Link Image
Enzyme 81 General References
  1. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Jikuya H, Takano J, Kikuno R, Hirosawa M, Nagase T, Nomura N, Ohara O: Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones. DNA Res. 2003 Feb 28;10(1):49-57. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Ottolenghi C, Veitia R, Quintana-Murci L, Torchard D, Scapoli L, Souleyreau-Therville N, Beckmann J, Fellous M, McElreavey K: The region on 9p associated with 46,XY sex reversal contains several transcripts expressed in the urogenital system and a novel doublesex-related domain. Genomics. 2000 Mar 1;64(2):170-8. [PubMed Link Image]
  7. Cote JF, Vuori K: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity. J Cell Sci. 2002 Dec 15;115(Pt 24):4901-13. [PubMed Link Image]
  8. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
Enzyme 81 Metabolite References Not Available
Enzyme 82 [top]
Enzyme 82 ID 14109
Enzyme 82 Name GTPase-activating protein and VPS9 domain-containing protein 1
Enzyme 82 Synonyms
  1. GAPex-5
  2. Rab5-activating protein 6
Enzyme 82 Gene Name GAPVD1
Enzyme 82 Protein Sequence >GTPase-activating protein and VPS9 domain-containing protein 1
MVKLDIHTLAHHLKQERLYVNSEKQLIQRLNADVLKTAEKLYRTAWIAKQQRINLDRLII
TSAEASPAECCQHAKILEDTQFVDGYKQLGFQETAYGEFLSRLRENPRLIASSLVAGEKL
NQENTQSVIYTVFTSLYGNCIMQEDESYLLQVLRYLIEFELKESDNPRRLLRRGTCAFSI
LFKLFSEGLFSAKLFLTATLHEPIMQLLVEDEDHLETDPNKLIERFSPSQQEKLFGEKGS
DRFRQKVQEMVESNEAKLVALVNKFIGYLKQNTYCFPHSLRWIVSQMYKTLSCVDRLEVG
EVRAMCTDLLLACFICPAVVNPEQYGIISDAPINEVARFNLMQVGRLLQQLAMTGSEEGD
PRTKSSLGKFDKSCVAAFLDVVIGGRAVETPPLSSVNLLEGLSRTVVYITYSQLITLVNF
MKSVMSGDQLREDRMALDNLLANLPPAKPGKSSSLEMTPYNTPQLSPATTPANKKNRLPI
ATRSRSRTNMLMDLHMDHEGSSQETIQEVQPEEVLVISLGTGPQLTPGMMSENEVLNMQL
SDGGQGDVPVDENKLHGKPDKTLRFSLCSDNLEGISEGPSNRSNSVSSLDLEGESVSELG
AGPSGSNGVEALQLLEHEQATTQDNLDDKLRKFEIRDMMGLTDDRDISETVSETWSTDVL
GSDFDPNIDEDRLQEIAGAAAENMLGSLLCLPGSGSVLLDPCTGSTISETTSEAWSVEVL
PSDSEAPDLKQEERLQELESCSGLGSTSDDTDVREVSSRPSTPGLSVVSGISATSEDIPN
KIEDLRSECSSDFGGKDSVTSPDMDEITHGAHQLTSPPSQSESLLAMFDPLSSHEGASAV
VRPKVHYARPSHPPPDPPILEGAVGGNEARLPNFGSHVLTPAEMEAFKQRHSYPERLVRS
RSSDIVSSVRRPMSDPSWNRRPGNEERELPPAAAIGATSLVAAPHSSSSSPSKDSSRGET
EERKDSDDEKSDRNRPWWRKRFVSAMPKAPIPFRKKEKQEKDKDDLGPDRFSTLTDDPSP
RLSAQAQVAEDILDKYRNAIKRTSPSDGAMANYESTGDNHDRDLSSKLLYHSDKEVMGDG
ESAHDSPRDEALQNISADDLPDSASQAAHPQDSAFSYRDAKKKLRLALCSADSVAFPVLT
HSTRNGLPDHTDPEDNEIVCFLKVQIAEAINLQDKNLMAQLQETMRCVCRFDNRTCRKLL
ASIAEDYRKRAPYIAYLTRCRQGLQTTQAHLERLLQRVLRDKEVANRYFTTVCVRLLLES
KEKKIREFIQDFQKLTAADDKTAQVEDFLQFLYGAMAQDVIWQNASEEQLQDAQLAIERS
VMNRIFKLAFYPNQDGDILRDQVLHEHIQRLSKVVTANHRALQIPEVYLREAPWPSAQSE
IRTISAYKTPRDKVQCILRMCSTIMNLLSLANEDSVPGADDFVPVLVFVLIKANPPCLLS
TVQYISSFYASCLSGEESYWWMQFTAAVEFIKTIDDRK
Enzyme 82 Number of Residues 1478
Enzyme 82 Molecular Weight 164978.1
Enzyme 82 Theoretical pI 4.86
Enzyme 82 GO Classification
Function
  • GTPase activator activity
  • enzyme activator activity
  • enzyme regulator activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
Component
  • cell part
  • intracellular
Enzyme 82 General Function Involved in GTPase activator activity
Enzyme 82 Specific Function Acts both as a GTPase-activating protein (GAP) and a guanine nucleotide exchange factor (GEF), and participates in various processes such as endocytosis, insulin receptor internalization or LC2A4/GLUT4 trafficking. Acts as a GEF for the Ras-related protein RAB31 by exchanging bound GDP for free GTP, leading to regulate LC2A4/GLUT4 trafficking. In the absence of insulin, it maintains RAB31 in an active state and promotes a futile cycle between LC2A4/GLUT4 storage vesicles and early endosomes, retaining LC2A4/GLUT4 inside the cells. Upon insulin stimulation, it is translocated to the plasma membrane, releasing LC2A4/GLUT4 from intracellular storage vesicles. Also involved in EGFR trafficking and degradation, possibly by promoting EGFR ubiquitination and subsequent degradation by the proteasome. Has GEF activity for Rab5 and GAP activity for Ras
Enzyme 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 51093832 Link Image
Enzyme 82 UniProtKB/Swiss-Prot ID Q14C86 Link Image
Enzyme 82 UniProtKB/Swiss-Prot Entry Name GAPD1_HUMAN Link Image
Enzyme 82 PDB ID Not Available
Enzyme 82 Cellular Location Not Available
Enzyme 82 Gene Sequence >4464 bp
ATGGTGAAACTAGATATTCATACTCTGGCTCATCACCTCAAGCAGGAACGCTTATATGTA
AACTCTGAGAAACAGCTCATTCAGAGGCTCAATGCAGATGTACTTAAGACAGCTGAAAAG
TTGTATCGTACAGCATGGATTGCGAAGCAACAGAGAATCAATTTGGATCGGCTTATCATA
ACCAGTGCTGAAGCTTCCCCTGCTGAATGTTGCCAACATGCCAAAATTTTGGAAGATACA
CAATTTGTTGATGGGTATAAGCAATTGGGATTTCAGGAGACTGCTTATGGAGAATTCTTG
AGTCGATTGAGGGAAAATCCTCGTCTTATTGCCTCCTCTTTGGTTGCTGGAGAGAAACTT
AATCAGGAGAACACACAAAGTGTTATTTACACAGTTTTTACCTCCCTGTATGGCAATTGC
ATCATGCAAGAAGATGAAAGCTACCTCCTTCAGGTTTTGCGATACTTGATTGAATTTGAA
CTTAAAGAAAGTGACAACCCTAGGCGACTTTTGAGGAGAGGAACTTGTGCCTTCAGCATC
TTATTTAAACTTTTTTCTGAAGGACTGTTTTCTGCCAAACTTTTCCTCACAGCCACTTTA
CATGAGCCAATTATGCAACTGCTTGTTGAAGATGAAGATCACCTGGAAACAGATCCAAAC
AAGCTAATTGAGAGGTTCTCTCCATCTCAGCAGGAAAAACTCTTTGGAGAGAAGGGCTCA
GATAGATTCAGGCAAAAAGTTCAAGAAATGGTGGAGTCCAATGAAGCAAAGCTAGTGGCT
TTGGTGAACAAATTTATTGGTTATCTCAAACAGAACACATATTGTTTTCCACATAGTTTA
AGGTGGATCGTGTCTCAGATGTACAAAACCCTCTCCTGTGTAGATAGGCTGGAAGTTGGG
GAGGTCAGGGCAATGTGTACTGATCTCCTGTTGGCCTGCTTCATTTGTCCTGCAGTTGTC
AATCCAGAACAATATGGAATAATTTCCGATGCTCCTATTAATGAAGTAGCACGATTTAAT
CTGATGCAGGTAGGCCGCCTTTTGCAGCAGTTAGCAATGACTGGCTCTGAAGAGGGAGAT
CCCCGAACAAAGAGCAGCCTTGGAAAGTTTGACAAAAGCTGTGTTGCCGCTTTCCTTGAT
GTTGTGATTGGGGGCCGTGCAGTGGAGACCCCTCCATTGTCTTCCGTCAATCTTCTGGAA
GGATTGAGCAGAACTGTGGTTTATATAACCTACAGTCAGCTTATTACTCTGGTGAATTTT
ATGAAGAGTGTGATGTCTGGAGATCAACTGAGAGAAGATAGAATGGCTCTTGACAATTTA
TTGGCAAACCTACCCCCGGCCAAGCCAGGAAAAAGTAGCAGTTTAGAAATGACTCCCTAC
AATACACCTCAGCTATCTCCAGCAACCACTCCAGCAAATAAAAAGAATCGATTACCTATA
GCAACTCGGAGCAGAAGCCGCACCAATATGCTAATGGACCTACATATGGACCATGAAGGA
TCATCTCAAGAAACCATCCAGGAGGTGCAACCAGAAGAGGTGTTGGTCATTTCCTTAGGT
ACAGGTCCCCAGCTTACTCCAGGGATGATGTCAGAAAATGAGGTCCTAAACATGCAGCTT
TCGGATGGAGGACAAGGAGATGTCCCTGTTGATGAAAACAAACTCCATGGTAAACCTGAT
AAAACCTTGCGCTTTTCCCTCTGCAGTGATAATCTGGAAGGAATATCTGAAGGTCCTTCA
AATCGCTCCAATTCAGTGTCCTCCCTAGACCTAGAAGGAGAGTCTGTGTCAGAACTTGGA
GCAGGACCTTCTGGCAGTAATGGAGTTGAAGCTCTACAGCTGTTAGAACATGAGCAAGCT
ACAACACAGGATAACCTTGATGATAAGCTAAGGAAGTTTGAAATTCGTGACATGATGGGA
TTAACAGATGATAGGGACATATCAGAAACAGTGAGTGAGACCTGGAGTACAGACGTCTTG
GGAAGTGACTTTGACCCTAATATTGATGAAGATCGCTTGCAAGAAATTGCAGGTGCTGCA
GCAGAGAACATGTTAGGCAGTTTGCTGTGCCTCCCAGGTTCAGGGTCAGTGCTTCTTGAC
CCCTGCACTGGTTCTACCATATCAGAGACAACAAGTGAAGCTTGGAGTGTAGAGGTATTG
CCAAGTGACTCAGAGGCCCCAGACCTAAAGCAGGAGGAGCGTCTGCAAGAACTGGAGAGC
TGTTCTGGACTGGGTAGCACATCTGATGATACGGATGTCAGGGAGGTCAGTTCCCGCCCC
AGCACACCAGGCCTCAGTGTTGTGTCCGGCATAAGTGCAACCTCTGAGGATATTCCCAAT
AAGATTGAAGACCTGAGATCTGAGTGCAGCTCTGATTTTGGGGGTAAAGATTCTGTCACT
AGTCCAGACATGGATGAAATAACTCACGATTTTCTTTATATACTTCAGCCAAAACAACAT
TTTCAACACATTGAAGCAGAAGCAGACATGAGAATCCAGCTGTCTTCTAGTGCCCACCAG
CTGACCTCTCCTCCTTCTCAGTCAGAGTCTCTGCTGGCCATGTTTGATCCACTGTCTTCA
CATGAAGGGGCTTCTGCTGTGGTAAGGCCAAAGGTTCACTATGCTAGGCCATCGCATCCA
CCACCAGATCCCCCAATCCTGGAAGGAGCTGTGGGAGGAAATGAGGCCAGGTTGCCAAAC
TTTGGTTCCCATGTTTTAACTCCAGCTGAAATGGAGGCATTCAAGCAAAGGCATTCTTAC
CCTGAGAGACTAGTTCGAAGCAGGAGCTCTGATATAGTATCTTCTGTCCGGAGACCCATG
AGTGACCCCAGCTGGAACCGGCGTCCAGGAAATGAAGAGCGAGAACTCCCTCCAGCTGCA
GCCATTGGTGCTACTTCTTTGGTGGCTGCACCTCATTCATCATCTTCATCCCCGAGTAAG
GACTCCTCAAGAGGAGAGACTGAAGAACGCAAAGATAGCGATGATGAGAAATCAGACAGG
AACAGACCTTGGTGGAGAAAACGTTTTGTTTCAGCCATGCCTAAAGCTCCTATACCATTT
AGAAAGAAAGAAAAACAAGAAAAAGACAAAGATGATCTGGGGCCTGACAGATTCTCAACA
CTCACAGATGATCCCAGCCCTAGACTCAGTGCACAAGCTCAGGTGGCTGAGGATATTCTG
GACAAATACAGGAATGCCATTAAACGGACCAGCCCCAGTGATGGAGCAATGGCAAACTAT
GAAAGTACAGAGGTTATGGGTGATGGTGAAAGTGCACATGATTCTCCCCGTGACGAAGCA
CTGCAGAACATCTCGGCTGATGATCTCCCAGACTCTGCAAGCCAAGCAGCCCACCCGCAG
GATTCAGCTTTCTCTTACAGAGATGCAAAAAAGAAACTGAGGCTTGCTCTTTGCTCTGCG
GACTCTGTTGCCTTCCCAGTGCTGACCCATTCAACAAGGAATGGTTTACCAGACCACACA
GACCCAGAAGACAATGAAATTGTATGCTTCTTAAAAGTTCAAATAGCTGAAGCAATTAAT
TTACAAGATAAGAATCTAATGGCTCAACTTCAAGAAACAATGCGCTGTGTGTGCCGTTTT
GATAATAGGACTTGTAGGAAACTGCTGGCTTCGATTGCTGAGGACTACAGAAAAAGAGCC
CCATATATTGCTTATCTCACTCGTTGTCGACAAGGACTACAGACCACACAGGCTCACCTG
GAAAGGCTATTGCAAAGAGTTTTGCGGGACAAAGAAGTGGCCAATCGATACTTTACCACT
GTCTGTGTGAGATTACTGCTTGAGAGCAAAGAAAAGAAGATCAGGGAATTCATTCAAGAC
TTTCAGAAACTCACCGCAGCTGACGATAAAACTGCTCAGGTAGAAGATTTTCTGCAGTTT
CTTTATGGTGCAATGGCCCAGGATGTCATATGGCAAAACGCGAGTGAAGAACAGCTTCAA
GATGCACAGCTGGCCATTGAGCGAAGCGTGATGAACCGGATTTTCAAGCTCGCCTTCTAC
CCTAATCAAGATGGGGACATACTTCGCGACCAGGTTCTTCATGAACATATCCAGAGATTG
TCTAAAGTAGTGACTGCAAATCACAGAGCTCTTCAGATACCAGAGGTTTATCTTCGAGAA
GCACCATGGCCATCTGCACAATCAGAAATCAGGACAATAAGTGCTTATAAAACCCCCCGG
GACAAAGTGCAGTGCATCCTGAGAATGTGCTCTACGATTATGAACCTCCTGAGCCTGGCC
AATGAGGACTCTGTCCCTGGAGCGGATGACTTTGTTCCTGTGTTGGTGTTTGTGTTGATA
AAGGCAAATCCACCCTGTTTGCTGTCTACTGTGCAGTATATCAGTAGCTTTTATGCTAGC
TGTCTGTCTGGAGAGGAGTCCTATTGGTGGATGCAGTTCACAGCAGCAGTAGAATTCATT
AAAACCATCGATGACCGAAAGTGA
Enzyme 82 GenBank Gene ID Not Available
Enzyme 82 GeneCard ID GAPVD1 Link Image
Enzyme 82 GenAtlas ID GAPVD1 Link Image
Enzyme 82 HGNC ID HGNC:23375 Link Image
Enzyme 82 Chromosome Location 9
Enzyme 82 Locus 9q33.3
Enzyme 82 SNPs SNPJam Report Link Image
Enzyme 82 General References
  1. Hunker CM, Galvis A, Kruk I, Giambini H, Veisaga ML, Barbieri MA: Rab5-activating protein 6, a novel endosomal protein with a role in endocytosis. Biochem Biophys Res Commun. 2006 Feb 17;340(3):967-75. Epub 2006 Jan 4. [PubMed Link Image]
  2. Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Apr 28;7(2):143-50. [PubMed Link Image]
  3. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  4. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  7. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  9. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  10. Nousiainen M, Sillje HH, Sauer G, Nigg EA, Korner R: Phosphoproteome analysis of the human mitotic spindle. Proc Natl Acad Sci U S A. 2006 Apr 4;103(14):5391-6. Epub 2006 Mar 24. [PubMed Link Image]
  11. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  12. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  13. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  14. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  15. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  16. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  17. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 82 Metabolite References Not Available
Enzyme 83 [top]
Enzyme 83 ID 14110
Enzyme 83 Name Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Enzyme 83 Synonyms
  1. Transducin beta chain 1
Enzyme 83 Gene Name GNB1
Enzyme 83 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
MSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYA
MHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNI
CSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTF
TGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNA
FATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDAL
KADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
Enzyme 83 Number of Residues 340
Enzyme 83 Molecular Weight 37376.6
Enzyme 83 Theoretical pI 5.85
Enzyme 83 GO Classification Not Available
Enzyme 83 General Function Involved in GTPase activity
Enzyme 83 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 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 31669 Link Image
Enzyme 83 UniProtKB/Swiss-Prot ID P62873 Link Image
Enzyme 83 UniProtKB/Swiss-Prot Entry Name GBB1_HUMAN Link Image
Enzyme 83 PDB ID 1OMW Link Image
Enzyme 83 PDB File Show
Enzyme 83 3D Structure
Enzyme 83 Cellular Location Not Available
Enzyme 83 Gene Sequence >1023 bp
ATGAGTGAGCTTGACCAGTTACGGCAGGAGGCCGAGCAACTTAAGAACCAGATTCGAGAC
GCCAGGAAAGCATGTGCAGATGCAACTCTCTCTCAGATCACAAACAACATCGACCCAGTG
GGAAGAATCCAAATGCGCACGAGGAGGACACTGCGGGGGCACCTGGCCAAGATCTACGCC
ATGCACTGGGGCACAGACTCCAGGCTTCTCGTCAGTGCCTCGCAGGATGGTAAACTTATC
ATCTGGGACAGCTACACCACCAACAAGGTCCACGCCATCCCTCTGCGCTCCTCCTGGGTC
ATGACCTGTGCATATGCCCCTTCTGGGAACTATGTGGCCTGCGGTGGCCTGGATAACATT
TGCTCCATTTACAATCTGAAAACTCGTGAGGGGAACGTGCGCGTGAGTCGTGAGCTGGCA
GGACACACAGGTTACCTGTCCTGCTGCCGATTCCTGGATGACAATCAGATCGTCACCAGC
TCTGGAGACACCACGTGTGCCCTGTGGGACATCGAGACCGGCCAGCAGACGACCACGTTT
ACCGGACACACTGGAGATGTCATGAGCCTTTCTCTTGCTCCTGACACCAGACTGTTCGTC
TCTGGTGCTTGTGATGCTTCAGCCAAACTCTGGGATGTGCGAGAAGGCATGTGCCGGCAG
ACCTTCACTGGCCACGAGTCTGACATCAATGCCATATGCTTCTTTCCAAATGGCAATGCA
TTTGCCACTGGCTCAGACGACGCCACCTGCAGGCTGTTTGACCTTCGTGCTGACCAGGAG
CTCATGACTTACTCCCATGACAACATCATCTGCGGGATCACCTCTGTCTCCTTCTCCAAG
AGCGGGCGCCTCCTCCTTGCTGGGTACGACGACTTCAACTGCAACGTCTGGGATGCACTC
AAAGCCGACCGGGCAGGTGTCTTGGCTGGGCATGACAACCGCGTCAGCTGCCTGGGCGTG
ACTGACGATGGCATGGCTGTGGCGACAGGGTCCTGGGATAGCTTCCTCAAGATCTGGAAC
TAA
Enzyme 83 GenBank Gene ID X04526 Link Image
Enzyme 83 GeneCard ID GNB1 Link Image
Enzyme 83 GenAtlas ID GNB1 Link Image
Enzyme 83 HGNC ID HGNC:4396 Link Image
Enzyme 83 Chromosome Location 1
Enzyme 83 Locus 1p36.33
Enzyme 83 SNPs SNPJam Report Link Image
Enzyme 83 General References
  1. Codina J, Stengel D, Woo SL, Birnbaumer L: Beta-subunits of the human liver Gs/Gi signal-transducing proteins and those of bovine retinal rod cell transducin are identical. FEBS Lett. 1986 Oct 27;207(2):187-92. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Niu J, Profirovic J, Pan H, Vaiskunaite R, Voyno-Yasenetskaya T: G Protein betagamma subunits stimulate p114RhoGEF, a guanine nucleotide exchange factor for RhoA and Rac1: regulation of cell shape and reactive oxygen species production. Circ Res. 2003 Oct 31;93(9):848-56. Epub 2003 Sep 25. [PubMed Link Image]
  5. Hill C, Goddard A, Ladds G, Davey J: The cationic region of Rhes mediates its interactions with specific Gbeta subunits. Cell Physiol Biochem. 2009;23(1-3):1-8. Epub 2009 Feb 18. [PubMed Link Image]
Enzyme 83 Metabolite References Not Available
Enzyme 84 [top]
Enzyme 84 ID 14111
Enzyme 84 Name Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2
Enzyme 84 Synonyms
  1. G protein subunit beta-2
  2. Transducin beta chain 2
Enzyme 84 Gene Name GNB2
Enzyme 84 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2
MSELEQLRQEAEQLRNQIRDARKACGDSTLTQITAGLDPVGRIQMRTRRTLRGHLAKIYA
MHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNI
CSIYSLKTREGNVRVSRELPGHTGYLSCCRFLDDNQIITSSGDTTCALWDIETGQQTVGF
AGHSGDVMSLSLAPDGRTFVSGACDASIKLWDVRDSMCRQTFIGHESDINAVAFFPNGYA
FTTGSDDATCRLFDLRADQELLMYSHDNIICGITSVAFSRSGRLLLAGYDDFNCNIWDAM
KGDRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
Enzyme 84 Number of Residues 340
Enzyme 84 Molecular Weight 37330.6
Enzyme 84 Theoretical pI 5.85
Enzyme 84 GO Classification Not Available
Enzyme 84 General Function Involved in GTPase activity
Enzyme 84 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 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 3135310 Link Image
Enzyme 84 UniProtKB/Swiss-Prot ID P62879 Link Image
Enzyme 84 UniProtKB/Swiss-Prot Entry Name GBB2_HUMAN Link Image
Enzyme 84 PDB ID Not Available
Enzyme 84 Cellular Location Not Available
Enzyme 84 Gene Sequence >1023 bp
ATGAGTGAGCTGGAGCAACTGAGACAGGAGGCCGAGCAGCTCCGGAACCAGATCCGGGAT
GCCCGAAAAGCATGTGGGGACTCAACACTGACCCAGATCACAGCTGGGCTGGACCCAGTG
GGGAGAATCCAGATGAGGACCCGGAGGACCCTCCGTGGGCACCTGGCAAAGATCTATGCC
ATGCACTGGGGGACCGACTCAAGGCTGCTGGTCAGCGCCTCCCAGGATGGGAAGCTCATC
ATCTGGGACAGCTACACCACCAACAAGGTCCACGCCATCCCGCTGCGCTCCTCCTGGGTA
ATGACCTGTGCCTACGCGCCCTCAGGGAACTTTGTGGCCTGTGGGGGGTTGGACAACATC
TGCTCCATCTACAGCCTCAAGACCCGCGAGGGCAACGTCAGGGTCAGCCGGGAGCTGCCT
GGCCACACTGGGTACCTGTCGTGTTGCCGCTTCCTGGATGACAACCAAATCATCACCAGC
TCTGGGGATACCACCTGTGCCCTGTGGGACATTGAGACAGGCCAGCAGACAGTGGGTTTT
GCTGGACACAGTGGGGATGTGATGTCCCTGTCCCTGGCCCCCGATGGCCGCACGTTTGTG
TCAGGCGCCTGTGATGCCTCTATCAAGCTGTGGGACGTGCGGGATTCCATGTGCCGACAG
ACCTTCATCGGCCATGAATCCGACATCAATGCAGTGGCTTTCTTCCCCAACGGCTACGCC
TTCACCACCGGCTCTGACGACGCCACGTGCCGCCTCTTCGACCTGCGGGCCGATCAGGAG
CTCCTCATGTACTCCCATGACAACATCATCTGTGGCATCACCTCTGTTGCCTTCTCGCGC
AGCGGACGGCTGCTGCTCGCTGGCTACGACGACTTCAACTGCAACATCTGGGATGCCATG
AAGGGCGACCGTGCAGGAGTCCTCGCTGGCCACGACAACCGCGTGAGCTGCCTCGGGGTC
ACCGACGATGGCATGGCTGTGGCCACGGGCTCCTGGGACTCCTTCCTCAAGATCTGGAAC
TAA
Enzyme 84 GenBank Gene ID AF053356 Link Image
Enzyme 84 GeneCard ID GNB2 Link Image
Enzyme 84 GenAtlas ID GNB2 Link Image
Enzyme 84 HGNC ID HGNC:4398 Link Image
Enzyme 84 Chromosome Location 7
Enzyme 84 Locus 7q21.3-q22.1|7q22
Enzyme 84 SNPs SNPJam Report Link Image
Enzyme 84 General References
  1. Fong HK, Amatruda TT 3rd, Birren BW, Simon MI: Distinct forms of the beta subunit of GTP-binding regulatory proteins identified by molecular cloning. Proc Natl Acad Sci U S A. 1987 Jun;84(11):3792-6. [PubMed Link Image]
  2. Gao B, Gilman AG, Robishaw JD: A second form of the beta subunit of signal-transducing G proteins. Proc Natl Acad Sci U S A. 1987 Sep;84(17):6122-5. [PubMed Link Image]
  3. Glockner G, Scherer S, Schattevoy R, Boright A, Weber J, Tsui LC, Rosenthal A: Large-scale sequencing of two regions in human chromosome 7q22: analysis of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17 genes. Genome Res. 1998 Oct;8(10):1060-73. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Niu J, Profirovic J, Pan H, Vaiskunaite R, Voyno-Yasenetskaya T: G Protein betagamma subunits stimulate p114RhoGEF, a guanine nucleotide exchange factor for RhoA and Rac1: regulation of cell shape and reactive oxygen species production. Circ Res. 2003 Oct 31;93(9):848-56. Epub 2003 Sep 25. [PubMed Link Image]
  6. Waragai M, Nagamitsu S, Xu W, Li YJ, Lin X, Ashizawa T: Ataxin 10 induces neuritogenesis via interaction with G-protein beta2 subunit. J Neurosci Res. 2006 May 15;83(7):1170-8. [PubMed Link Image]
  7. Hill C, Goddard A, Ladds G, Davey J: The cationic region of Rhes mediates its interactions with specific Gbeta subunits. Cell Physiol Biochem. 2009;23(1-3):1-8. Epub 2009 Feb 18. [PubMed Link Image]
Enzyme 84 Metabolite References Not Available
Enzyme 85 [top]
Enzyme 85 ID 14112
Enzyme 85 Name Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3
Enzyme 85 Synonyms
  1. Transducin beta chain 3
Enzyme 85 Gene Name GNB3
Enzyme 85 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3
MGEMEQLRQEAEQLKKQIADARKACADVTLAELVSGLEVVGRVQMRTRRTLRGHLAKIYA
MHWATDSKLLVSASQDGKLIVWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNM
CSIYNLKSREGNVKVSRELSAHTGYLSCCRFLDDNNIVTSSGDTTCALWDIETGQQKTVF
VGHTGDCMSLAVSPDFNLFISGACDASAKLWDVREGTCRQTFTGHESDINAICFFPNGEA
ICTGSDDASCRLFDLRADQELICFSHESIICGITSVAFSLSGRLLFAGYDDFNCNVWDSM
KSERVGILSGHDNRVSCLGVTADGMAVATGSWDSFLKIWN
Enzyme 85 Number of Residues 340
Enzyme 85 Molecular Weight 37220.8
Enzyme 85 Theoretical pI 5.38
Enzyme 85 GO Classification Not Available
Enzyme 85 General Function Involved in GTPase activity
Enzyme 85 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 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 20257502 Link Image
Enzyme 85 UniProtKB/Swiss-Prot ID P16520 Link Image
Enzyme 85 UniProtKB/Swiss-Prot Entry Name GBB3_HUMAN Link Image
Enzyme 85 PDB ID Not Available
Enzyme 85 Cellular Location Not Available
Enzyme 85 Gene Sequence >1023 bp
ATGGGGGAGATGGAGCAACTGCGTCAGGAAGCGGAGCAGCTCAAGAAGCAGATTGCAGAT
GCCAGGAAAGCCTGTGCTGACGTTACTCTGGCAGAGCTGGTGTCTGGCCTAGAGGTGGTG
GGACGAGTCCAGATGCGGACGCGGCGGACGTTAAGGGGACACCTGGCCAAGATTTACGCC
ATGCACTGGGCCACTGATTCTAAGCTGCTGGTAAGTGCCTCGCAAGATGGGAAGCTGATC
GTGTGGGACAGCTACACCACCAACAAGGTGCACGCCATCCCACTGCGCTCCTCCTGGGTC
ATGACCTGTGCCTATGCCCCATCAGGGAACTTTGTGGCGTGTGGGGGGCTGGACAACATG
TGTTCCATCTACAACCTCAAATCCCGTGAGGGCAATGTCAAGGTCAGCCGGGAGCTTTCT
GCTCACACAGGTTATCTCTCCTGCTGCCGCTTCCTGGATGACAACAATATTGTGACCAGC
TCGGGGGACACCACGTGTGCCTTGTGGGACATTGAGACTGGGCAGCAGAAGACTGTATTT
GTGGGACACACGGGTGACTGCATGAGCCTGGCTGTGTCTCCTGACTTCAATCTCTTCATT
TCGGGGGCCTGTGATGCCAGTGCCAAGCTCTGGGATGTGCGAGAGGGGACCTGCCGACAG
ACTTTCACTGGCCACGAGTCGGACATCAACGCCATCTGTTTCTTCCCCAATGGAGAGGCC
ATCTGCACGGGCTCGGATGACGCTTCCTGCCGCTTGTTTGACCTGCGGGCAGACCAGGAG
CTGATCTGCTTCTCCCACGAGAGCATCATCTGCGGCATCACGTCTGTGGCCTTCTCCCTC
AGTGGCCGCCTACTATTCGCTGGCTACGACGACTTCAACTGCAATGTCTGGGACTCCATG
AAGTCTGAGCGTGTGGGCATCCTCTCTGGCCACGATAACAGGGTGAGCTGCCTGGGAGTC
ACAGCTGACGGGATGGCTGTGGCCACAGGTTCCTGGGACAGCTTCCTCAAAATCTGGAAC
TGA
Enzyme 85 GenBank Gene ID AF501884 Link Image
Enzyme 85 GeneCard ID GNB3 Link Image
Enzyme 85 GenAtlas ID GNB3 Link Image
Enzyme 85 HGNC ID HGNC:4400 Link Image
Enzyme 85 Chromosome Location 1
Enzyme 85 Locus 12p13
Enzyme 85 SNPs SNPJam Report Link Image
Enzyme 85 General References
  1. Levine MA, Smallwood PM, Moen PT Jr, Helman LJ, Ahn TG: Molecular cloning of beta 3 subunit, a third form of the G protein beta-subunit polypeptide. Proc Natl Acad Sci U S A. 1990 Mar;87(6):2329-33. [PubMed Link Image]
  2. Ansari-Lari MA, Muzny DM, Lu J, Lu F, Lilley CE, Spanos S, Malley T, Gibbs RA: A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13. Genome Res. 1996 Apr;6(4):314-26. [PubMed Link Image]
  3. Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA: Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. Genome Res. 1997 Mar;7(3):268-80. [PubMed Link Image]
  4. Rosskopf D, Busch S, Manthey I, Siffert W: G protein beta 3 gene: structure, promoter, and additional polymorphisms. Hypertension. 2000 Jul;36(1):33-41. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Hill C, Goddard A, Ladds G, Davey J: The cationic region of Rhes mediates its interactions with specific Gbeta subunits. Cell Physiol Biochem. 2009;23(1-3):1-8. Epub 2009 Feb 18. [PubMed Link Image]
Enzyme 85 Metabolite References Not Available
Enzyme 86 [top]
Enzyme 86 ID 14113
Enzyme 86 Name Guanine nucleotide-binding protein subunit beta-4
Enzyme 86 Synonyms
  1. Transducin beta chain 4
Enzyme 86 Gene Name GNB4
Enzyme 86 Protein Sequence >Guanine nucleotide-binding protein subunit beta-4
MSELEQLRQEAEQLRNQIQDARKACNDATLVQITSNMDSVGRIQMRTRRTLRGHLAKIYA
MHWGYDSRLLVSASQDGKLIIWDSYTTNKMHAIPLRSSWVMTCAYAPSGNYVACGGLDNI
CSIYNLKTREGNVRVSRELPGHTGYLSCCRFLDDSQIVTSSGDTTCALWDIETAQQTTTF
TGHSGDVMSLSLSPDMRTFVSGACDASSKLWDIRDGMCRQSFTGHVSDINAVSFFPNGYA
FATGSDDATCRLFDLRADQELLLYSHDNIICGITSVAFSKSGRLLLAGYDDFNCNVWDTL
KGDRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLRIWN
Enzyme 86 Number of Residues 340
Enzyme 86 Molecular Weight 37566.8
Enzyme 86 Theoretical pI 5.85
Enzyme 86 GO Classification Not Available
Enzyme 86 General Function Involved in signal transducer activity
Enzyme 86 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 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 20257506 Link Image
Enzyme 86 UniProtKB/Swiss-Prot ID Q9HAV0 Link Image
Enzyme 86 UniProtKB/Swiss-Prot Entry Name GBB4_HUMAN Link Image
Enzyme 86 PDB ID 1OMW Link Image
Enzyme 86 PDB File Show
Enzyme 86 3D Structure
Enzyme 86 Cellular Location Not Available
Enzyme 86 Gene Sequence >1023 bp
ATGAGCGAGCTGGAGCAGCTGAGGCAGGAGGCTGAACAGCTTCGGAATCAGATCCAGGAT
GCTCGGAAGGCCTGCAATGATGCCACGCTGGTTCAGATCACGTCTAATATGGACTCCGTG
GGCCGAATACAAATGCGAACAAGGCGCACGCTGCGCGGCCACCTCGCTAAGATCTACGCC
ATGCACTGGGGATATGATTCCAGGCTACTAGTCAGTGCTTCGCAAGATGGAAAATTAATT
ATTTGGGATAGCTATACGACAAATAAGATGCACGCCATCCCTCTGAGGTCCTCCTGGGTG
ATGACCTGTGCCTACGCCCCGTCCGGGAACTACGTTGCCTGTGGAGGCTTGGATAACATC
TGCTCCATATACAACCTAAAGACCCGAGAGGGGAATGTGCGGGTGAGCCGAGAATTGCCA
GGACACACGGGCTACTTGTCCTGCTGCCGATTCTTAGATGATGGACAAATCATTACAAGT
TCGGGAGACACGACTTGTGCTTTGTGGGACATTGAGACCGGACAGCAGACTACGACCTTC
ACGGGACACTCGGGTGACGTGATGAGCCTCTCACTGAGTCCTGACTTGAAGACCTTTGTG
TCTGGTGCTTGTGATGCATCCTCAAAGCTGTGGGATATCCGAGATGGGATGTGTAGACAG
TCTTTCACCGGACACATCTCAGACATCAACGCTGTCAGTTTCTTCCCGAGTGTATATGCC
TTTGCCACTGGTTCTGATGATGCCACATGCCGACTCTTTGACCTCCGTGCAGACCAGGAG
CTCCTGCTATACTCTCATGACAATATCATCTGTGGCATTACTTCTGTGGCCTTCTCAAAG
AGTGGGCGCCTCCTGTTAGCCGGCTATGACGACTTCAACTGCAGTGTGTGGGACGCTCTG
AAAGGAGGCCGGTCAGGTGTCCTTGCTGGTCATGACAACCGTGTTAGCTGCTTAGGTGTG
ACTGATGACGGCATGGCTGTGGCCACTGGCTCCTGGGACAGTTTTCTTAGAATCTGGAAT
TGA
Enzyme 86 GenBank Gene ID AF501886 Link Image
Enzyme 86 GeneCard ID GNB4 Link Image
Enzyme 86 GenAtlas ID GNB4 Link Image
Enzyme 86 HGNC ID HGNC:20731 Link Image
Enzyme 86 Chromosome Location 3
Enzyme 86 Locus 3q26.33
Enzyme 86 SNPs SNPJam Report Link Image
Enzyme 86 General References
  1. Ruiz-Velasco V, Ikeda SR, Puhl HL: Cloning, tissue distribution, and functional expression of the human G protein beta 4-subunit. Physiol Genomics. 2002 Feb 11;8(1):41-50. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 86 Metabolite References Not Available
Enzyme 87 [top]
Enzyme 87 ID 14114
Enzyme 87 Name Guanine nucleotide-binding protein subunit beta-5
Enzyme 87 Synonyms
  1. Gbeta5
  2. Transducin beta chain 5
Enzyme 87 Gene Name GNB5
Enzyme 87 Protein Sequence >Guanine nucleotide-binding protein subunit beta-5
MCDQTFLVNVFGSCDKCFKQRALRPVFKKSQQLSYCSTCAEIMATEGLHENETLASLKSE
AESLKGKLEEERAKLHDVELHQVAERVEALGQFVMKTRRTLKGHGNKVLCMDWCKDKRRI
VSSSQDGKVIVWDSFTTNKEHAVTMPCTWVMACAYAPSGCAIACGGLDNKCSVYPLTFDK
NENMAAKKKSVAMHTNYLSACSFTNSDMQILTASGDGTCALWDVESGQLLQSFHGHGADV
LCLDLAPSETGNTFVSGGCDKKAMVWDMRSGQCVQAFETHESDINSVRYYPSGDAFASGS
DDATCRLYDLRADREVAIYSKESIIFGASSVDFSLSGRLLFAGYNDYTINVWDVLKGSRV
SILFGHENRVSTLRVSPDGTAFCSGSWDHTLRVWA
Enzyme 87 Number of Residues 395
Enzyme 87 Molecular Weight 43565.9
Enzyme 87 Theoretical pI 6.42
Enzyme 87 GO Classification Not Available
Enzyme 87 General Function Involved in GTPase activity
Enzyme 87 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 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 20336270 Link Image
Enzyme 87 UniProtKB/Swiss-Prot ID O14775 Link Image
Enzyme 87 UniProtKB/Swiss-Prot Entry Name GBB5_HUMAN Link Image
Enzyme 87 PDB ID Not Available
Enzyme 87 Cellular Location Not Available
Enzyme 87 Gene Sequence >1188 bp
ATGTGTGATCAGACCTTTCTCGTTAATGTATTTGGCTCATGTGACAAATGTTTCAAACAA
CGAGCTCTGAGACCAGTTTTCAAGAAGTCTCAACAACTCAGCTACTGTTCAACATGTGCA
GAAATTATGGCAACCGAGGGGCTGCACGAGAACGAGACGCTGGCGTCGCTGAAGAGCGAG
GCCGAGAGCCTCAAGGGCAAGCTGGAGGAGGAGCGAGCCAAGCTGCACGATGTGGAGCTG
CACCAGGTGGCGGAGCGGGTGGAGGCCCTGGGGCAGTTTGTCATGAAGACCAGAAGGACC
CTCAAAGGCCACGGGAACAAAGTCCTGTGCATGGACTGGTGCAAAGATAAGAGGAGGATC
GTGAGCTCGTCACAGGATGGGAAGGTGATCGTGTGGGATTCCTTCACCACAAACAAGGAG
CACGCGGTCACCATGCCCTGCACGTGGGTGATGGCATGTGCTTATGCCCCATCGGGATGT
GCCATTGCTTGTGGTGGTTTGGATAATAAGTGTTCTGTGTACCCCTTGACGTTTGACAAA
AATGAAAACATGGCTGCCAAAAAGAAGTCTGTTGCTATGCACACCAACTACCTGTCGGCC
TGCAGCTTCACCAACTCTGACATGCAGATCCTGACAGCGAGCGGCGATGGCACATGTGCC
CTGTGGGACGTGGAGAGCGGGCAGCTGCTGCAGAGCTTCCACGGACATGGGGCTGACGTC
CTCTGCTTGGACCTGGCCCCCTCAGAAACTGGAAACACCTTCGTGTCTGGGGGATGTGAC
AAGAAAGCCATGGTGTGGGACATGCGCTCCGGCCAGTGCGTGCAGGCCTTTGAAACACAT
GAATCTGACATCAACAGTGTCCGGTACTACCCCAGTGGAGATGCCTTTGCTTCAGGGTCA
GATGACGCTACGTGTCGCCTCTATGACCTGCGGGCAGATAGGGAGGTTGCCATCTATTCC
AAAGAAAGCATCATATTTGGAGCATCCAGCGTGGACTTCTCCCTCAGTGGTCGCCTGCTG
TTTGCTGGATACAATGATTACACTATCAACGTCTGGGATGTTCTCAAAGGGTCCCGGGTC
TCCATCCTGTTTGGACATGAAAACCGCGTTAGCACTCTACGAGTTTCCCCCGATGGGACT
GCTTTCTGCTCTGGATCATGGGATCATACCCTCAGAGTCTGGGCCTAA
Enzyme 87 GenBank Gene ID NM_016194.3 Link Image
Enzyme 87 GeneCard ID GNB5 Link Image
Enzyme 87 GenAtlas ID GNB5 Link Image
Enzyme 87 HGNC ID HGNC:4401 Link Image
Enzyme 87 Chromosome Location 1
Enzyme 87 Locus 15q21.2
Enzyme 87 SNPs SNPJam Report Link Image
Enzyme 87 General References
  1. Jones PG, Lombardi SJ, Cockett MI: Cloning and tissue distribution of the human G protein beta 5 cDNA. Biochim Biophys Acta. 1998 Apr 24;1402(3):288-91. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 87 Metabolite References Not Available
Enzyme 88 [top]
Enzyme 88 ID 14116
Enzyme 88 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10
Enzyme 88 Synonyms Not Available
Enzyme 88 Gene Name GNG10
Enzyme 88 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10
MSSGASASALQRLVEQLKLEAGVERIKVSQAAAELQQYCMQNACKDALLVGVPAGSNPFR
EPRSCALL
Enzyme 88 Number of Residues 68
Enzyme 88 Molecular Weight 7205.2
Enzyme 88 Theoretical pI 8.04
Enzyme 88 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 88 General Function Involved in signal transducer activity
Enzyme 88 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. Interacts with beta-1 and beta-2, but not with beta-3
Enzyme 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 20147647 Link Image
Enzyme 88 UniProtKB/Swiss-Prot ID P50151 Link Image
Enzyme 88 UniProtKB/Swiss-Prot Entry Name GBG10_HUMAN Link Image
Enzyme 88 PDB ID Not Available
Enzyme 88 Cellular Location Not Available
Enzyme 88 Gene Sequence >207 bp
ATGTCCTCCGGGGCTAGCGCGAGCGCCCTGCAGCGCTTGGTAGAGCAGCTCAAGTTGGAG
GCTGGCGTGGAGAGGATCAAGGTCTCTCAGGCAGCTGCAGAGCTTCAACAGTACTGTATG
CAGAATGCCTGCAAGGATGCCCTGCTGGTGGGTGTTCCAGCTGGAAGTAACCCCTTCCGG
GAGCCTAGATCCTGTGCTTTACTCTGA
Enzyme 88 GenBank Gene ID AF493877 Link Image
Enzyme 88 GeneCard ID GNG10 Link Image
Enzyme 88 GenAtlas ID GNG10 Link Image
Enzyme 88 HGNC ID HGNC:4402 Link Image
Enzyme 88 Chromosome Location 9
Enzyme 88 Locus 9q31.3
Enzyme 88 SNPs SNPJam Report Link Image
Enzyme 88 General References
  1. Ray K, Kunsch C, Bonner LM, Robishaw JD: Isolation of cDNA clones encoding eight different human G protein gamma subunits, including three novel forms designated the gamma 4, gamma 10, and gamma 11 subunits. J Biol Chem. 1995 Sep 15;270(37):21765-71. [PubMed Link Image]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 88 Metabolite References Not Available
Enzyme 89 [top]
Enzyme 89 ID 14117
Enzyme 89 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12
Enzyme 89 Synonyms Not Available
Enzyme 89 Gene Name GNG12
Enzyme 89 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12
MSSKTASTNNIAQARRTVQQLRLEASIERIKVSKASADLMSYCEEHARSDPLLIGIPTSE
NPFKDKKTCIIL
Enzyme 89 Number of Residues 72
Enzyme 89 Molecular Weight 8006.1
Enzyme 89 Theoretical pI 9.38
Enzyme 89 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 89 General Function Involved in signal transducer activity
Enzyme 89 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 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 6563252 Link Image
Enzyme 89 UniProtKB/Swiss-Prot ID Q9UBI6 Link Image
Enzyme 89 UniProtKB/Swiss-Prot Entry Name GBG12_HUMAN Link Image
Enzyme 89 PDB ID Not Available
Enzyme 89 Cellular Location Not Available
Enzyme 89 Gene Sequence >219 bp
ATGTCCAGCAAAACAGCAAGCACCAACAATATAGCCCAGGCAAGGAGAACTGTGCAGCAG
TTAAGATTAGAAGCCTCCATTGAAAGAATAAAGGTTTCGAAGGCATCAGCGGACCTCATG
TCCTACTGTGAGGAACATGCCAGGAGTGACCCTTTGCTGATAGGAATACCAACTTCAGAA
AACCCTTTCAAGGATAAAAAAACTTGCATCATCTTATAG
Enzyme 89 GenBank Gene ID AF119663 Link Image
Enzyme 89 GeneCard ID GNG12 Link Image
Enzyme 89 GenAtlas ID GNG12 Link Image
Enzyme 89 HGNC ID HGNC:19663 Link Image
Enzyme 89 Chromosome Location 1
Enzyme 89 Locus 1p31.3
Enzyme 89 SNPs SNPJam Report Link Image
Enzyme 89 General References
  1. Hurowitz EH, Melnyk JM, Chen YJ, Kouros-Mehr H, Simon MI, Shizuya H: Genomic characterization of the human heterotrimeric G protein alpha, beta, and gamma subunit genes. DNA Res. 2000 Apr 28;7(2):111-20. [PubMed Link Image]
  2. Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed Link Image]
  3. Cook LA, Schey KL, Cleator JH, Wilcox MD, Dingus J, Hildebrandt JD: Identification of a region in G protein gamma subunits conserved across species but hypervariable among subunit isoforms. Protein Sci. 2001 Dec;10(12):2548-55. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  6. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 89 Metabolite References Not Available
Enzyme 90 [top]
Enzyme 90 ID 14118
Enzyme 90 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13
Enzyme 90 Synonyms Not Available
Enzyme 90 Gene Name GNG13
Enzyme 90 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13
MEEWDVPQMKKEVESLKYQLAFQREMASKTIPELLKWIEDGIPKDPFLNPDLMKNNPWVE
KGKCTIL
Enzyme 90 Number of Residues 67
Enzyme 90 Molecular Weight 7949.3
Enzyme 90 Theoretical pI 4.76
Enzyme 90 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 90 General Function Involved in signal transducer activity
Enzyme 90 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 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 7259306 Link Image
Enzyme 90 UniProtKB/Swiss-Prot ID Q9P2W3 Link Image
Enzyme 90 UniProtKB/Swiss-Prot Entry Name GBG13_HUMAN Link Image
Enzyme 90 PDB ID Not Available
Enzyme 90 Cellular Location Not Available
Enzyme 90 Gene Sequence >204 bp
ATGGAGGAGTGGGACGTGCCACAGATGAAGAAAGAGGTGGAGAGCCTTAAGTACCAGCTG
GCCTTCCAGCGGGAGATGGCGTCCAAGACCATCCCCGAGCTGCTGAAGTGGATCGAGGAC
GGGATCCCCAAGGACCCCTTCCTGAACCCCGACCTGATGAAGAACAACCCATGGGTGGAA
AAGGGCAAATGCACCATCCTGTGA
Enzyme 90 GenBank Gene ID AB030207 Link Image
Enzyme 90 GeneCard ID GNG13 Link Image
Enzyme 90 GenAtlas ID GNG13 Link Image
Enzyme 90 HGNC ID HGNC:14131 Link Image
Enzyme 90 Chromosome Location 1
Enzyme 90 Locus 16p13.3
Enzyme 90 SNPs SNPJam Report Link Image
Enzyme 90 General References
  1. Huang L, Shanker YG, Dubauskaite J, Zheng JZ, Yan W, Rosenzweig S, Spielman AI, Max M, Margolskee RF: Ggamma13 colocalizes with gustducin in taste receptor cells and mediates IP3 responses to bitter denatonium. Nat Neurosci. 1999 Dec;2(12):1055-62. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  4. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 90 Metabolite References Not Available
Enzyme 91 [top]
Enzyme 91 ID 14119
Enzyme 91 Name Guanine nucleotide-binding protein G(T) subunit gamma-T1
Enzyme 91 Synonyms
  1. Transducin gamma chain
Enzyme 91 Gene Name GNGT1
Enzyme 91 Protein Sequence >Guanine nucleotide-binding protein G(T) subunit gamma-T1
MPVINIEDLTEKDKLKMEVDQLKKEVTLERMLVSKCCEEVRDYVEERSGEDPLVKGIPED
KNPFKELKGGCVIS
Enzyme 91 Number of Residues 74
Enzyme 91 Molecular Weight 8495.8
Enzyme 91 Theoretical pI 4.47
Enzyme 91 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 91 General Function Involved in signal transducer activity
Enzyme 91 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 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 41393496 Link Image
Enzyme 91 UniProtKB/Swiss-Prot ID P63211 Link Image
Enzyme 91 UniProtKB/Swiss-Prot Entry Name GBG1_HUMAN Link Image
Enzyme 91 PDB ID 1B9Y Link Image
Enzyme 91 PDB File Show
Enzyme 91 3D Structure
Enzyme 91 Cellular Location Not Available
Enzyme 91 Gene Sequence >225 bp
ATGCCAGTAATCAATATTGAGGACCTGACAGAAAAGGACAAATTGAAGATGGAAGTTGAC
CAGCTCAAGAAAGAAGTGACACTGGAAAGAATGCTAGTTTCCAAATGTTGTGAAGAAGTA
AGAGATTACGTTGAAGAACGATCTGGCGAGGATCCACTGGTAAAGGGCATCCCAGAGGAC
AAAAATCCCTTCAAGGAGCTCAAAGGAGGCTGTGTGATTTCATAA
Enzyme 91 GenBank Gene ID AC002076 Link Image
Enzyme 91 GeneCard ID GNGT1 Link Image
Enzyme 91 GenAtlas ID GNGT1 Link Image
Enzyme 91 HGNC ID HGNC:4411 Link Image
Enzyme 91 Chromosome Location 7
Enzyme 91 Locus 7q21.3
Enzyme 91 SNPs SNPJam Report Link Image
Enzyme 91 General References
  1. Tao L, Pandey S, Simon MI, Fong HK: Structure of the bovine transducin gamma subunit gene and analysis of promoter function in transgenic mice. Exp Eye Res. 1993 Apr;56(4):497-507. [PubMed Link Image]
  2. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Scherer SW, Feinstein DS, Oliveira L, Tsui LC, Pittler SJ: Gene structure and chromosome localization to 7q21.3 of the human rod photoreceptor transducin gamma-subunit gene (GNGT1). Genomics. 1996 Jul 1;35(1):241-3. [PubMed Link Image]
Enzyme 91 Metabolite References Not Available
Enzyme 92 [top]
Enzyme 92 ID 14120
Enzyme 92 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3
Enzyme 92 Synonyms Not Available
Enzyme 92 Gene Name GNG3
Enzyme 92 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3
MKGETPVNSTMSIGQARKMVEQLKIEASLCRIKVSKAAADLMTYCDAHACEDPLITPVPT
SENPFREKKFFCALL
Enzyme 92 Number of Residues 75
Enzyme 92 Molecular Weight 8304.7
Enzyme 92 Theoretical pI 7.93
Enzyme 92 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 92 General Function Involved in signal transducer activity
Enzyme 92 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 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 33150642 Link Image
Enzyme 92 UniProtKB/Swiss-Prot ID P63215 Link Image
Enzyme 92 UniProtKB/Swiss-Prot Entry Name GBG3_HUMAN Link Image
Enzyme 92 PDB ID Not Available
Enzyme 92 Cellular Location Not Available
Enzyme 92 Gene Sequence >228 bp
ATGAAAGGTGAGACCCCGGTGAACAGCACTATGAGTATTGGGCAAGCACGCAAGATGGTG
GAACAGCTTAAGATTGAAGCCAGCTTGTGTCGGATAAAGGTGTCCAAGGCAGCAGCAGAC
CTGATGACTTACTGTGATGCCCACGCCTGTGAGGATCCCCTCATCACCCCTGTGCCCACT
TCGGAGAACCCCTTCCGGGAGAAGAAGTTCTTCTGTGCTCTCCTCTGA
Enzyme 92 GenBank Gene ID AF087900 Link Image
Enzyme 92 GeneCard ID GNG3 Link Image
Enzyme 92 GenAtlas ID GNG3 Link Image
Enzyme 92 HGNC ID HGNC:4405 Link Image
Enzyme 92 Chromosome Location 1
Enzyme 92 Locus 11p11
Enzyme 92 SNPs SNPJam Report Link Image
Enzyme 92 General References
  1. Hurowitz EH, Melnyk JM, Chen YJ, Kouros-Mehr H, Simon MI, Shizuya H: Genomic characterization of the human heterotrimeric G protein alpha, beta, and gamma subunit genes. DNA Res. 2000 Apr 28;7(2):111-20. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 92 Metabolite References Not Available
Enzyme 93 [top]
Enzyme 93 ID 14121
Enzyme 93 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-4
Enzyme 93 Synonyms Not Available
Enzyme 93 Gene Name GNG4
Enzyme 93 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-4
MKEGMSNNSTTSISQARKAVEQLKMEACMDRVKVSQAAADLLAYCEAHVREDPLIIPVPA
SENPFREKKFFCTIL
Enzyme 93 Number of Residues 75
Enzyme 93 Molecular Weight 8388.6
Enzyme 93 Theoretical pI 7.19
Enzyme 93 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 93 General Function Involved in signal transducer activity
Enzyme 93 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 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 20147637 Link Image
Enzyme 93 UniProtKB/Swiss-Prot ID P50150 Link Image
Enzyme 93 UniProtKB/Swiss-Prot Entry Name GBG4_HUMAN Link Image
Enzyme 93 PDB ID Not Available
Enzyme 93 Cellular Location Not Available
Enzyme 93 Gene Sequence >228 bp
ATGAAAGAGGGCATGTCTAATAACAGCACCACTAGCATCTCCCAAGCCAGGAAAGCTGTG
GAGCAGCTAAAGATGGAAGCCTGTATGGACAGGGTCAAGGTCTCCCAGGCAGCCGCGGAC
CTCCTGGCCTACTGTGAAGCTCACGTGCGGGAAGATCCTCTCATCATTCCAGTGCCTGCA
TCAGAAAACCCCTTTCGCGAGAAGAAGTTCTTTTGTACCATTCTCTAA
Enzyme 93 GenBank Gene ID AF493872 Link Image
Enzyme 93 GeneCard ID GNG4 Link Image
Enzyme 93 GenAtlas ID GNG4 Link Image
Enzyme 93 HGNC ID HGNC:4407 Link Image
Enzyme 93 Chromosome Location 1
Enzyme 93 Locus 1q42.3
Enzyme 93 SNPs SNPJam Report Link Image
Enzyme 93 General References
  1. Ray K, Kunsch C, Bonner LM, Robishaw JD: Isolation of cDNA clones encoding eight different human G protein gamma subunits, including three novel forms designated the gamma 4, gamma 10, and gamma 11 subunits. J Biol Chem. 1995 Sep 15;270(37):21765-71. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 93 Metabolite References Not Available
Enzyme 94 [top]
Enzyme 94 ID 14122
Enzyme 94 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5
Enzyme 94 Synonyms Not Available
Enzyme 94 Gene Name GNG5
Enzyme 94 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5
MSGSSSVAAMKKVVQQLRLEAGLNRVKVSQAAADLKQFCLQNAQHDPLLTGVSSSTNPFR
PQKVCSFL
Enzyme 94 Number of Residues 68
Enzyme 94 Molecular Weight 7318.4
Enzyme 94 Theoretical pI 10.62
Enzyme 94 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 94 General Function Involved in signal transducer activity
Enzyme 94 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 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 3329380 Link Image
Enzyme 94 UniProtKB/Swiss-Prot ID P63218 Link Image
Enzyme 94 UniProtKB/Swiss-Prot Entry Name GBG5_HUMAN Link Image
Enzyme 94 PDB ID Not Available
Enzyme 94 Cellular Location Not Available
Enzyme 94 Gene Sequence >207 bp
ATGTCTGGCTCCTCCAGCGTCGCCGCTATGAAGAAAGTGGTTCAACAGCTCCGGCTGGAG
GCCGGACTCAACCGCGTAAAAGTTTCCCAGGCAGCTGCAGACTTGAAACAGTTCTGTCTG
CAGAATGCTCAACATGACCCTCTGCTGACTGGAGTATCTTCAAGTACAAATCCCTTCAGA
CCCCAGAAAGTCTGTTCCTTTTTGTAG
Enzyme 94 GenBank Gene ID AF038955 Link Image
Enzyme 94 GeneCard ID GNG5 Link Image
Enzyme 94 GenAtlas ID GNG5 Link Image
Enzyme 94 HGNC ID HGNC:4408 Link Image
Enzyme 94 Chromosome Location 1
Enzyme 94 Locus 1p22
Enzyme 94 SNPs SNPJam Report Link Image
Enzyme 94 General References
  1. Liu B, Aronson NN Jr: Structure of human G protein G gamma 5 gene GNG5. Biochem Biophys Res Commun. 1998 Oct 9;251(1):88-94. [PubMed Link Image]
  2. Mao M, Fu G, Wu JS, Zhang QH, Zhou J, Kan LX, Huang QH, He KL, Gu BW, Han ZG, Shen Y, Gu J, Yu YP, Xu SH, Wang YX, Chen SJ, Chen Z: Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning. Proc Natl Acad Sci U S A. 1998 Jul 7;95(14):8175-80. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
Enzyme 94 Metabolite References Not Available
Enzyme 95 [top]
Enzyme 95 ID 14123
Enzyme 95 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7
Enzyme 95 Synonyms Not Available
Enzyme 95 Gene Name GNG7
Enzyme 95 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7
MSATNNIAQARKLVEQLRIEAGIERIKVSKAASDLMSYCEQHARNDPLLVGVPASENPFK
DKKPCIIL
Enzyme 95 Number of Residues 68
Enzyme 95 Molecular Weight 7521.7
Enzyme 95 Theoretical pI 8.77
Enzyme 95 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 95 General Function Involved in signal transducer activity
Enzyme 95 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction. Plays a role in the regulation of adenylyl cyclase signaling in certain regions of the brain. Plays a role in the formation or stabilzation of a G protein heterotrimer (G(olf) subunit alpha-beta-gamma-7) that is required for adenylyl cyclase activity in the striatum
Enzyme 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 3149954 Link Image
Enzyme 95 UniProtKB/Swiss-Prot ID O60262 Link Image
Enzyme 95 UniProtKB/Swiss-Prot Entry Name GBG7_HUMAN Link Image
Enzyme 95 PDB ID Not Available
Enzyme 95 Cellular Location Not Available
Enzyme 95 Gene Sequence >207 bp
ATGTCAGCCACTAACAACATAGCCCAGGCCCGGAAGCTGGTGGAACAGCTACGCATAGAA
GCCGGGATTGAGCGCATCAAGGTCTCCAAAGCGGCGTCTGACCTCATGAGCTACTGTGAG
CAACATGCTCGGAACGACCCCCTGCTGGTCGGAGTCCCTGCCTCGGAGAACCCCTTTAAG
GACAAGAAACCTTGTATTATTTTATAA
Enzyme 95 GenBank Gene ID AB010414 Link Image
Enzyme 95 GeneCard ID GNG7 Link Image
Enzyme 95 GenAtlas ID GNG7 Link Image
Enzyme 95 HGNC ID HGNC:4410 Link Image
Enzyme 95 Chromosome Location 1
Enzyme 95 Locus 19p13.3
Enzyme 95 SNPs SNPJam Report Link Image
Enzyme 95 General References
  1. Shibata K, Mori M, Tanaka S, Kitano S, Akiyoshi T: Identification and cloning of human G-protein gamma 7, down-regulated in pancreatic cancer. Biochem Biophys Res Commun. 1998 May 8;246(1):205-9. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Ohta M, Mimori K, Fukuyoshi Y, Kita Y, Motoyama K, Yamashita K, Ishii H, Inoue H, Mori M: Clinical significance of the reduced expression of G protein gamma 7 (GNG7) in oesophageal cancer. Br J Cancer. 2008 Jan 29;98(2):410-7. Epub 2008 Jan 22. [PubMed Link Image]
Enzyme 95 Metabolite References Not Available
Enzyme 96 [top]
Enzyme 96 ID 14124
Enzyme 96 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-8
Enzyme 96 Synonyms
  1. Gamma-9
Enzyme 96 Gene Name GNG8
Enzyme 96 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-8
MSNNMAKIAEARKTVEQLKLEVNIDRMKVSQAAAELLAFCETHAKDDPLVTPVPAAENPF
RDKRLFCVLL
Enzyme 96 Number of Residues 70
Enzyme 96 Molecular Weight 7841.1
Enzyme 96 Theoretical pI 7.27
Enzyme 96 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 96 General Function Involved in signal transducer activity
Enzyme 96 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 96 Pathways Not Available
Enzyme 96 Reactions Not Available
Enzyme 96 Pfam Domain Function
Enzyme 96 Signals
  • None
Enzyme 96 Transmembrane Regions
  • None
Enzyme 96 Essentiality Not Available
Enzyme 96 GenBank ID Protein 6164867 Link Image
Enzyme 96 UniProtKB/Swiss-Prot ID Q9UK08 Link Image
Enzyme 96 UniProtKB/Swiss-Prot Entry Name GBG8_HUMAN Link Image
Enzyme 96 PDB ID Not Available
Enzyme 96 Cellular Location Not Available
Enzyme 96 Gene Sequence >213 bp
ATGTCCAACAACATGGCCAAGATTGCCGAGGCCCGCAAGACGGTGGAACAGCTGAAGCTG
GAGGTGAACATCGACCGCATGAAGGTGTCGCAGGCAGCAGCGGAACTCCTGGCTTTCTGC
GAGACGCATGCCAAAGATGACCCGCTGGTGACGCCAGTACCCGCCGCGGAGAACCCCTTC
CGCGACAAGCGCCTCTTTTGTGTTCTGCTCTGA
Enzyme 96 GenBank Gene ID AF188179 Link Image
Enzyme 96 GeneCard ID GNG8 Link Image
Enzyme 96 GenAtlas ID GNG8 Link Image
Enzyme 96 HGNC ID HGNC:19664 Link Image
Enzyme 96 Chromosome Location 1
Enzyme 96 Locus 19q13.32
Enzyme 96 SNPs SNPJam Report Link Image
Enzyme 96 General References
  1. Hurowitz EH, Melnyk JM, Chen YJ, Kouros-Mehr H, Simon MI, Shizuya H: Genomic characterization of the human heterotrimeric G protein alpha, beta, and gamma subunit genes. DNA Res. 2000 Apr 28;7(2):111-20. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 96 Metabolite References Not Available
Enzyme 97 [top]
Enzyme 97 ID 14125
Enzyme 97 Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-T2
Enzyme 97 Synonyms
  1. G gamma-C
  2. G-gamma-8
  3. G-gamma-9
Enzyme 97 Gene Name GNGT2
Enzyme 97 Protein Sequence >Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-T2
MAQDLSEKDLLKMEVEQLKKEVKNTRIPISKAGKEIKEYVEAQAGNDPFLKGIPEDKNPF
KEKGGCLIS
Enzyme 97 Number of Residues 69
Enzyme 97 Molecular Weight 7746.9
Enzyme 97 Theoretical pI 6.73
Enzyme 97 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 97 General Function Involved in signal transducer activity
Enzyme 97 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein- effector interaction
Enzyme 97 Pathways Not Available
Enzyme 97 Reactions Not Available
Enzyme 97 Pfam Domain Function
Enzyme 97 Signals
  • None
Enzyme 97 Transmembrane Regions
  • None
Enzyme 97 Essentiality Not Available
Enzyme 97 GenBank ID Protein 2392823 Link Image
Enzyme 97 UniProtKB/Swiss-Prot ID O14610 Link Image
Enzyme 97 UniProtKB/Swiss-Prot Entry Name GBGT2_HUMAN Link Image
Enzyme 97 PDB ID Not Available
Enzyme 97 Cellular Location Not Available
Enzyme 97 Gene Sequence >210 bp
ATGGCCCAGGATCTCAGCGAGAAGGACCTGTTGAAGATGGAGGTGGAGCAGCTGAAGAAA
GAAGTGAAAAACACAAGAATTCCGATTTCCAAAGCGGGAAAGGAAATCAAGGAGTACGTG
GAGGCCCAAGCAGGAAACGATCCTTTTCTCAAAGGCATCCCTGAGGACAAGAATCCCTTC
AAGGAGAAAGGTGGCTGTCTGATAAGCTGA
Enzyme 97 GenBank Gene ID AF001160 Link Image
Enzyme 97 GeneCard ID GNGT2 Link Image
Enzyme 97 GenAtlas ID GNGT2 Link Image
Enzyme 97 HGNC ID HGNC:4412 Link Image
Enzyme 97 Chromosome Location 1
Enzyme 97 Locus 17q21
Enzyme 97 SNPs SNPJam Report Link Image
Enzyme 97 General References
  1. Ong OC, Hu K, Rong H, Lee RH, Fung BK: Gene structure and chromosome localization of the G gamma c subunit of human cone G-protein (GNGT2). Genomics. 1997 Aug 15;44(1):101-9. [PubMed Link Image]
  2. Cook LA, Schey KL, Cleator JH, Wilcox MD, Dingus J, Hildebrandt JD: Identification of a region in G protein gamma subunits conserved across species but hypervariable among subunit isoforms. Protein Sci. 2001 Dec;10(12):2548-55. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 97 Metabolite References Not Available
Enzyme 98 [top]
Enzyme 98 ID 14143
Enzyme 98 Name Guanine nucleotide-binding protein-like 1
Enzyme 98 Synonyms
  1. GTP-binding protein HSR1
Enzyme 98 Gene Name GNL1
Enzyme 98 Protein Sequence >Guanine nucleotide-binding protein-like 1
MPRKKPFSVKQKKKQLQDKRERKRGLQDGLRSSSNSRSGSRERREEQTDTSDGESVTHHI
RRLNQQPSQGLGPRGYDPNRYRLHFERDSREEVERRKRAAREQVLQPVSAELLELDIREV
YQPGSVLDFPRRPPWSYEMSKEQLMSQEERSFQDYLGKIHGAYSSEKLSYFEHNLETWRQ
LWRVLEMSDIVLLITDIRHPVVNFPPALYEYVTGELGLALVLVLNKVDLAPPALVVAWKH
YFHQHYPQLHVVLFTSFPRDPRTPQDPSSVLKKSRRRGRGWTRALGPEQLLRACEAITVG
KVDLSSWREKIARDVAGATWGNGSGEEEEEEDGPAVLVEQQTDSAMEPTGPTQERYKDGV
VTIGCVGFPNVGKSSLINGLVGRKVVSVSRTPGHTRYFQTYFLTPSVKLCDCPGLIFPSL
LPRQLQVLAGIYPIAQIQEPYTAVGYLASRIPVQALLHLRHPEAEDPSAEHPWCAWDICE
AWAEKRGYKTAKAARNDVYRAANSLLRLAVDGRLSLCFHPPGYSEQKGTWESHPETTELV
VLQGRVGPAGDEEEEEEEELSSSCEEEGEEDRDADEEGEGDEETPTSAPGSSLAGRNPYA
LLGEDEC
Enzyme 98 Number of Residues 607
Enzyme 98 Molecular Weight 68660.3
Enzyme 98 Theoretical pI 5.58
Enzyme 98 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
Component
  • cell part
  • intracellular
Enzyme 98 General Function Involved in GTP binding
Enzyme 98 Specific Function Possible regulatory or functional link with the histocompatibility cluster
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 55961299 Link Image
Enzyme 98 UniProtKB/Swiss-Prot ID P36915 Link Image
Enzyme 98 UniProtKB/Swiss-Prot Entry Name GNL1_HUMAN Link Image
Enzyme 98 PDB ID Not Available
Enzyme 98 Cellular Location Not Available
Enzyme 98 Gene Sequence >1824 bp
ATGCCGAGGAAGAAGCCATTCAGCGTGAAGCAGAAGAAGAAGCAGTTGCAGGACAAACGG
GAGCGGAAGAGAGGGCTTCAAGATGGGCTGCGCTCCAGTTCCAACAGCCGCAGCGGGAGC
CGGGAGCGGCGAGAGGAACAGACCGACACCTCGGACGGGGAGTCTGTGACCCATCATATC
CGCAGGCTTAACCAGCAGCCTTCTCAGGGGCTGGGTCCACGAGGCTACGACCCAAATCGA
TACCGACTGCATTTTGAGAGAGACAGCAGGGAGGAGGTAGAGAGGAGAAAGAGAGCAGCC
CGGGAGCAAGTTCTACAGCCGGTCAGTGCTGAGTTGTTGGAGCTGGACATCCGGGAGGTG
TATCAGCCTGGCTCAGTTCTGGACTTTCCTCGACGTCCTCCTTGGAGCTATGAGATGTCC
AAGGAGCAACTAATGAGCCAAGAGGAACGGAGCTTCCAAGACTATCTTGGGAAGATTCAT
GGGGCTTACTCCTCTGAGAAACTCAGCTACTTTGAGCACAATCTGGAGACATGGAGGCAG
CTGTGGCGGGTGTTAGAGATGTCTGACATCGTCCTGCTTATCACTGATATCCGACATCCA
GTTGTGAATTTCCCGCCAGCACTTTATGAGTATGTGACTGGAGAACTTGGACTGGCCCTG
GTGCTGGTTTTGAACAAGGTGGATCTGGCCCCGCCAGCTCTTGTGGTTGCCTGGAAGCAT
TATTTCCATCAACACTATCCCCAGCTCCACGTCGTCCTTTTCACCTCTTTTCCTCGGGAC
CCCCGCACCCCACAGGACCCTAGTAGTGTCTTGAAGAAGAGTCGGAGGCGGGGGAGAGGA
TGGACTCGGGCCCTGGGGCCAGAGCAGTTGCTGAGAGCCTGTGAAGCCATCACTGTGGGG
AAAGTGGACTTGAGCAGCTGGCGGGAGAAGATTGCTCGGGATGTGGCTGGGGCCACCTGG
GGTAATGGCTCTGGGGAGGAGGAGGAAGAGGAGGATGGCCCAGCAGTCCTGGTGGAGCAG
CAGACTGATTCAGCAATGGAGCCAACTGGCCCAACCCAAGAGCGCTACAAGGATGGGGTG
GTGACCATCGGCTGTGTGGGTTTCCCTAATGTGGGAAAGTCCTCGCTGATCAATGGGCTG
GTGGGGCGGAAAGTCGTGAGTGTCTCCAGAACCCCGGGCCATACCCGATACTTTCAGACC
TACTTTCTTACCCCCTCTGTGAAGCTCTGTGACTGCCCAGGCCTCATCTTCCCATCTCTT
CTGCCTAGGCAGTTGCAGGTTCTGGCAGGGATCTACCCTATCGCCCAGATCCAGGAGCCC
TACACTGCTGTGGGCTACCTGGCCTCCCGAATTCCCGTGCAGGCCCTGCTCCACCTGCGC
CACCCAGAGGCTGAGGACCCCTCAGCGGAACACCCCTGGTGTGCCTGGGACATCTGTGAA
GCCTGGGCAGAGAAACGTGGTTACAAGACAGCCAAGGCGGCTCGGAATGATGTGTACAGA
GCAGCCAACAGTCTCTTGCGGCTGGCAGTGGACGGCCGCCTCAGCCTGTGTTTTCATCCC
CCAGGCTACAGTGAACAGAAAGGCACCTGGGAGTCCCATCCAGAGACCACGGAGCTGGTG
GTTTTGCAGGGCAGGGTGGGGCCAGCAGGTGACGAGGAGGAGGAGGAAGAGGAAGAGCTG
AGCAGCTCCTGTGAGGAGGAGGGAGAGGAGGACCGGGATGCGGATGAGGAGGGAGAAGGG
GATGAGGAGACCCCAACCTCGGCTCCAGGGTCCAGCCTGGCTGGCCGAAACCCTTATGCC
CTGCTGGGTGAGGATGAGTGCTGA
Enzyme 98 GenBank Gene ID AL662800 Link Image
Enzyme 98 GeneCard ID GNL1 Link Image
Enzyme 98 GenAtlas ID GNL1 Link Image
Enzyme 98 HGNC ID HGNC:4413 Link Image
Enzyme 98 Chromosome Location 6
Enzyme 98 Locus 6p21.3
Enzyme 98 SNPs SNPJam Report Link Image
Enzyme 98 General References
  1. Vernet C, Ribouchon MT, Chimini G, Pontarotti P: Structure and evolution of a member of a new subfamily of GTP-binding proteins mapping to the human MHC class I region. Mamm Genome. 1994 Feb;5(2):100-5. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  5. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  7. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 98 Metabolite References Not Available
Enzyme 99 [top]
Enzyme 99 ID 14159
Enzyme 99 Name Probable E3 ubiquitin-protein ligase HERC1
Enzyme 99 Synonyms
  1. HECT domain and RCC1-like domain-containing protein 1
  2. p532
  3. p619
Enzyme 99 Gene Name HERC1
Enzyme 99 Protein Sequence >Probable E3 ubiquitin-protein ligase HERC1
MATMIPPVKLKWLEHLNSSWITEDSESIATREGVAVLYSKLVSNKEVVPLPQQVLCLKGP
QLPDFERESLSSDEQDHYLDALLSSQLALAKMVCSDSPFAGALRKRLLVLQRVFYALSNK
YHDKGKVKQQQHSPESSSGSADVHSVSERPRSSTDALIEMGVRTGLSLLFALLRQSWMMP
VSGPGLSLCNDVIHTAIEVVSSLPPLSLANESKIPPMGLDCLSQVTTFLKGVTIPNSGAD
TLGRRLASELLLGLAAQRGSLRYLLEWIEMALGASAVVHTMEKGKLLSSQEGMISFDCFM
TILMQMRRSLGSSADRSQWREPTRTSDGLCSLYEAALCLFEEVCRMASDYSRTCASPDSI
QTGDAPIVSETCEVYVWGSNSSHQLVEGTQEKILQPKLAPSFSDAQTIEAGQYCTFVIST
DGSVRACGKGSYGRLGLGDSNNQSTLKKLTFEPHRSIKKVSSSKGSDGHTLAFTTEGEVF
SWGDGDYGKLGHGNSSTQKYPKLIQGPLQGKVVVCVSAGYRHSAAVTEDGELYTWGEGDF
GRLGHGDSNSRNIPTLVKDISNVGEVSCGSSHTIALSKDGRTVWSFGGGDNGKLGHGDTN
RVYKPKVIEALQGMFIRKVCAGSQSSLALTSTGQVYAWGCGACLGCGSSEATALRPKLIE
ELAATRIVDVSIGDSHCLALSHDNEVYAWGNNSMGQCGQGNSTGPITKPKKVSGLDGIAI
QQISAGTSHSLAWTALPRDRQVVAWHRPYCVDLEESTFSHLRSFLERYCDKINSEIPPLP
FPSSREHHSFLKLCLKLLSNHLALALAGGVATSILGRQAGPLRNLLFRLMDSTVPDEIQE
VVIETLSVGATMLLPPLRERMELLHSLLPQGPDRWESLSKGQRMQLDIILTSLQDHTHVA
SLLGYSSPSDAADLSSVCTGYGNLSDQPYGTQSCHPDTHLAEILMKTLLRNLGFYTDQAF
GELEKNSDKFLLGTSSSENSQPAHLHELLCSLQKQLLAFCHINNISENSSSVALLHKHLQ
LLLPHATDIYSRSANLLKESPWNGSVGEKLRDVIYVSAAGSMLCQIVNSLLLLPVSVARP
LLSYLLDLLPPLDCLNRLLPAADLLEDQELQWPLHGGPELIDPAGLPLPQPAQSWVWLVD
LERTIALLIGRCLGGMLQGSPVSPEEQDTAYWMKTPLFSDGVEMDTPQLDKCMSCLLEVA
LSGNEEQKPFDYKLRPEIAVYVDLALGCSKEPARSLWISMQDYAVSKDWDSATLSNESLL
DTVSRFVLAALLKHTNLLSQACGESRYQPGKHLSEVYRCVYKVRSRLLACKNLELIQTRS
SSRDRWISENQDSADVDPQEHSFTRTIDEEAEMEEQAERDREEGHPEPEDEEEEREHEVM
TAGKIFQCFLSAREVARSRDRDRMNSGAGSGARADDPPPQSQQERRVSTDLPEGQDVYTA
ACNSVIHRCALLILGVSPVIDELQKRREEGQLQQPSTSASEGGGLMTRSESLTAESRLVH
TSPNYRLIKSRSESDLSQPESDEEGYALSGRRNVDLDLAASHRKRGPMHSQLESLSDSWA
RLKHSRDWLCNSSYSFESDFDLTKSLGVHTLIENVVSFVSGDVGNAPGFKEPEESMSTSP
QASIIAMEQQQLRAELRLEALHQILVLLSGMEEKGSISLAGSRLSSGFQSSTLLTSVRLQ
FLAGCFGLGTVGHTGGKGESGRLHHYQDGIRAAKRNIQIEIQVAVHKIYQQLSATLERAL
QANKHHIEAQQRLLLVTVFALSVHYQPVDVSLAISTGLLNVLSQLCGTDTMLGQPLQLLP
KTGVSQLSTALKVASTRLLQILAITTGTYADKLSPKVVQSLLDLLCSQLKNLLSQTGVLH
MASFGEGEQEDGEEEEKKVDSSGETEKKDFRAALRKQHAAELHLGDFLVFLRRVVSSKAI
QSKMASPKWTEVLLNIASQKCSSGIPLVGNLRTRLLALHVLEAVLPACESGVEDDQMAQI
VERLFSLLSDCMWETPIAQAKHAIQIKEKEQEIKLQKQGELEEEDENLPIQEVSFDPEKA
QCCLVENGQILTHGSGGKGYGLASTGVTSGCYQWKFYIVKENRGNEGTCVGVSRWPVHDF
NHRTTSDMWLYRAYSGNLYHNGEQTLTLSSFTQGDFITCVLDMEARTISFGKNGEEPKLA
FEDVDAAELYPCVMFYSSNPGEKVKICDMQMRGTPRDLLPGDPICSPVAAVLAEATIQLI
RILHRTDRWTYCINKKMMERLHKIKICIKESGQKLKKSRSVQSREENEMREEKESKEEEK
GKHTRHGLADLSELQLRTLCIEVWPVLAVIGGVDAGLRVGGRCVHKQTGRHATLLGVVKE
GSTSAKVQWDEAEITISFPTFWSPSDTPLYNLEPCEPLPFDVARFRGLTASVLLDLTYLT
GVHEDMGKQSTKRHEKKHRHESEEKGDVEQKPESESALDMRTGLTSDDVKSQSTTSSKSE
NEIASFSLDPTLPSVESQHQITEGKRKNHEHMSKNHDVAQSEIRAVQLSYLYLGAMKSLS
ALLGCSKYAELLLIPKVLAENGHNSDCASSPVVHEDVEMRAALQFLMRHMVKRAVMRSPI
KRALGLADLERAQAMIYKLVVHGLLEDQFGGKIKQEIDQQAEESDPAQQAQTPVTTSPSA
SSTTSFMSSSLEDTTTATTPVTDTETVPASESPGVMPLSLLRQMFSSYPTTTVLPTRRAQ
TPPISSLPTSPSDEVGRRQSLTSPDSQSARPANRTALSDPSSRLSTSPPPPAIAVPLLEM
GFSLRQIAKAMEATGARGEADAQNITVLAMWMIEHPGHEDEEEPQSGSTADSRPGAAVLG
SGGKSNDPCYLQSPGDIPSADAAEMEEGFSESPDNLDHTENAASGSGPSARGRSAVTRRH
KFDLAARTLLARAAGLYRSVQAHRNQSRREGISLQQDPGALYDFNLDEELEIDLDDEAME
AMFGQDLTSDNDILGMWIPEVLDWPTWHVCESEDREEVVVCELCECSVVSFNQHMKRNHP
GCGRSANRQGYRSNGSYVDGWFGGECGSGNPYYLLCGTCREKYLAMKTKSKSTSSERYKG
QAPDLIGKQDSVYEEDWDMLDVDEDEKLTGEEEFELLAGPLGLNDRRIVPEPVQFPDSDP
LGASVAMVTATNSMEETLMQIGCHGSVEKSSSGRITLGEQAAALANPHDRVVALRRVTAA
AQVLLARTMVMRALSLLSVSGSSCSLAAGLESLGLTDIRTLVRLMCLAAAGRAGLSTSPS
AMASTSERSRGGHSKANKPISCLAYLSTAVGCLASNAPSAAKLLVQLCTQNLISAATGVN
LTTVDDSIQRKFLPSFLRGIAEENKLVTSPNFVVTQALVALLADKGAKLRPNYDKSEVEK
KGPLELANALAACCLSSRLSSQHRQWAAQQLVRTLAAHDRDNQTTLQTLADMGGDLRKCS
FIKLEAHQNRVMTCVWCNKKGLLATSGNDGTIRVWNVTKKQYSLQQTCVFNRLEGDAEES
LGSPSDPSFSPVSWSISGKYLAGALEKMVNIWQVNGGKGLVDIQPHWVSALAWPEEGPAT
AWSGESPELLLVGRMDGSLGLIEVVDVSTMHRRELEHCYRKDVSVTCIAWFSEDRPFAVG
YFDGKLLLGTKEPLEKGGIVLIDAHKDTLISMKWDPTGHILMTCAKEDSVKLWGSISGCW
CCLHSLCHPSIVNGIAWCRLPGKGSKLQLLMATGCQSGLVCVWRIPQDTTQTNVTSAEGW
WEQESNCQDGYRKSSGAKCVYQLRGHITPVRTVAFSSDGLALVSGGLGGLMNIWSLRDGS
VLQTVVIGSGAIQTTVWIPEVGVAACSNRSKDVLVVNCTAEWAAANHVLATCRTALKQQG
VLGLNMAPCMRAFLERLPMMLQEQYAYEKPHVVCGDQLVHSPYMQCLASLAVGLHLDQLL
CNPPVPPHHQNCLPDPASWNPNEWAWLECFSTTIKAAEALTNGAQFPESFTVPDLEPVPE
DELVFLMDNSKWINGMDEQIMSWATSRPEDWHLGGKCDVYLWGAGRHGQLAEAGRNVMVP
AAAPSFSQAQQVICGQNCTFVIQANGTVLACGEGSYGRLGQGNSDDLHVLTVISALQGFV
VTQLVTSCGSDGHSMALTESGEVFSWGDGDYGKLGHGNSDRQRRPRQIEALQGEEVVQMS
CGFKHSAVVTSDGKLFTFGNGDYGRLGLGNTSNKKLPERVTALEGYQIGQVACGLNHTLA
VSADGSMVWAFGDGDYGKLGLGNSTAKSSPQKIDVLCGIGIKKVACGTQFSVALTKDGHV
YTFGQDRLIGLPEGRARNHNRPQQIPVLAGVIIEDVAVGAEHTLALASNGDVYAWGSNSE
GQLGLGHTNHVREPTLVTGLQGKNVRQISAGRCHSAAWTAPPVPPRAPGVSVPLQLGLPD
TVPPQYGALREVSIHTVRARLRLLYHFSDLMYSSWRLLNLSPNNQNSTSHYNAGTWGIVQ
GQLRPLLAPRVYTLPMVRSIGKTMVQGKNYGPQITVKRISTRGRKCKPIFVQIARQVVKL
NASDLRLPSRAWKVKLVGEGADDAGGVFDDTITEMCQELETGIVDLLIPSPNATAEVGYN
RDRFLFNPSACLDEHLMQFKFLGILMGVAIRTKKPLDLHLAPLVWKQLCCVPLTLEDLEE
VDLLYVQTLNSILHIEDSGITEESFHEMIPLDSFVGQSADGKMVPIIPGGNSIPLTFSNR
KEYVERAIEYRLHEMDRQVAAVREGMSWIVPVPLLSLLTAKQLEQMVCGMPEISVEVLKK
VVRYREVDEQHQLVQWFWHTLEEFSNEERVLFMRFVSGRSRLPANTADISQRFQIMKVDR
PYDSLPTSQTCFFQLRLPPYSSQLVMAERLRYAINNCRSIDMDNYMLSRNVDNAEGSDTD
Y
Enzyme 99 Number of Residues 4861
Enzyme 99 Molecular Weight 532223.1
Enzyme 99 Theoretical pI 5.93
Enzyme 99 GO Classification
Function
  • acid-amino acid ligase activity
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein modification process
Component
  • cell part
  • intracellular
Enzyme 99 General Function Involved in acid-amino acid ligase activity
Enzyme 99 Specific Function Involved in membrane trafficking via some guanine nucleotide exchange factor (GEF) activity and its ability to bind clathrin. Acts as a GEF for Arf and Rab, by exchanging bound GDP for free GTP. Binds phosphatidylinositol-4,5-bisphosphate, which is required for GEF activity. May also act as a E3 ubiquitin- protein ligase which accepts ubiquitin from an E2 ubiquitin- conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates
Enzyme 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 126131099 Link Image
Enzyme 99 UniProtKB/Swiss-Prot ID Q15751 Link Image
Enzyme 99 UniProtKB/Swiss-Prot Entry Name HERC1_HUMAN Link Image
Enzyme 99 PDB ID Not Available
Enzyme 99 Cellular Location Not Available
Enzyme 99 Gene Sequence >14586 bp
ATGGCAACTATGATTCCACCAGTGAAGCTGAAATGGCTTGAACACTTGAACAGCTCCTGG
ATTACAGAGGACAGTGAATCTATTGCTACAAGAGAGGGAGTTGCTGTTCTGTATTCTAAA
CTGGTTAGCAATAAGGAAGTAGTACCTTTGCCCCAACAAGTTTTATGCCTCAAAGGACCA
CAGTTGCCAGACTTTGAACGTGAGTCTCTTTCAAGTGATGAGCAGGACCACTATTTGGAT
GCCCTTCTTAGCAGCCAGCTAGCATTGGCAAAGATGGTATGTTCAGATTCCCCATTTGCC
GGGGCACTTAGAAAACGACTGCTTGTACTCCAGCGTGTCTTTTATGCACTTTCTAATAAA
TACCATGACAAAGGCAAGGTGAAGCAGCAGCAGCATTCTCCGGAGAGCAGTTCTGGTTCA
GCAGATGTCCATTCTGTTAGTGAACGCCCCCGGTCAAGCACTGATGCACTTATAGAAATG
GGTGTTCGAACTGGTCTAAGTTTATTATTTGCGCTTCTAAGACAAAGTTGGATGATGCCT
GTGTCAGGACCTGGTCTCAGTCTTTGCAACGATGTCATTCATACTGCAATTGAAGTTGTG
AGCTCTTTGCCACCATTATCATTAGCAAATGAAAGCAAGATTCCTCCTATGGGCTTGGAC
TGCTTATCGCAAGTAACAACATTTCTTAAAGGAGTCACTATTCCTAATTCTGGGGCAGAC
ACTTTAGGTCGTAGATTAGCTTCTGAGTTGCTGCTTGGTTTGGCAGCTCAACGAGGCTCA
TTGCGATATCTTCTTGAATGGATAGAAATGGCTTTGGGGGCTTCGGCAGTTGTACACACC
ATGGAGAAAGGCAAACTACTCTCAAGCCAGGAAGGAATGATCAGCTTTGACTGCTTTATG
ACCATATTAATGCAGATGAGGCGTTCTTTGGGTTCATCTGCTGATCGGAGTCAGTGGAGA
GAACCAACCAGAACATCGGATGGCTTGTGCTCCCTTTACGAGGCAGCATTATGTCTCTTT
GAAGAGGTTTGCAGAATGGCTTCTGATTATTCGAGAACATGTGCTAGCCCAGATAGCATT
CAGACTGGTGATGCTCCCATTGTCTCCGAAACCTGTGAGGTTTATGTTTGGGGGAGCAAT
AGCAGCCATCAGTTGGTAGAAGGTACACAGGAGAAAATACTGCAACCCAAACTGGCTCCT
AGTTTCTCTGATGCACAGACCATTGAAGCTGGACAGTACTGCACTTTTGTCATTTCTACG
GATGGCTCTGTTAGAGCTTGCGGGAAAGGCAGCTATGGGAGACTGGGCCTTGGAGACTCC
AATAATCAGTCAACTTTAAAAAAGTTAACATTCGAGCCTCACAGATCCATTAAAAAGGTT
TCATCTTCTAAAGGATCTGATGGTCACACTTTAGCCTTTACGACAGAAGGAGAAGTCTTC
AGTTGGGGAGATGGTGATTATGGGAAACTGGGGCATGGAAATAGTTCAACACAGAAATAT
CCCAAGCTTATTCAGGGACCTCTACAAGGAAAGGTAGTTGTTTGTGTGTCAGCTGGATAC
AGACATAGTGCTGCTGTCACAGAGGATGGGGAATTATACACATGGGGTGAAGGAGACTTT
GGAAGATTAGGTCATGGTGACAGCAATAGTCGTAACATTCCAACATTAGTAAAAGACATC
AGCAATGTAGGAGAGGTTTCTTGTGGCAGTTCACATACTATTGCTCTGTCTAAAGATGGG
AGAACTGTATGGTCTTTTGGAGGAGGAGACAATGGTAAACTTGGTCATGGTGATACCAAC
AGAGTGTATAAACCTAAAGTTATTGAAGCTTTACAAGGAATGTTCATTCGCAAAGTTTGT
GCTGGGAGCCAGTCTTCACTTGCTTTGACATCAACAGGGCAGGTCTATGCTTGGGGCTGT
GGAGCTTGTCTAGGTTGTGGTTCTTCAGAAGCTACTGCTTTGAGACCCAAGCTTATTGAA
GAACTGGCTGCCACAAGAATAGTTGATGTTTCTATTGGAGACAGTCATTGTTTGGCTCTT
TCTCATGATAATGAAGTTTATGCCTGGGGCAATAACTCAATGGGGCAATGTGGTCAGGGA
AATTCCACAGGTCCTATTACTAAACCAAAGAAAGTGAGTGGCTTAGATGGCATAGCTATT
CAGCAGATTTCGGCTGGAACATCACATAGTCTGGCATGGACTGCTCTTCCTAGGGACAGA
CAAGTTGTTGCATGGCACCGACCTTATTGTGTAGATCTTGAAGAGAGTACCTTCTCACAC
CTGCGTTCTTTTCTTGAGAGATACTGTGATAAAATAAACAGTGAGATTCCCCCACTCCCT
TTCCCTTCATCAAGAGAACACCACAGTTTTCTCAAGCTGTGCCTGAAGCTACTTTCAAAT
CACCTTGCTCTTGCACTTGCGGGAGGGGTAGCTACCAGCATTCTCGGGAGGCAGGCAGGT
CCACTTCGAAATTTGCTCTTCAGACTGATGGACTCAACTGTCCCAGATGAAATCCAAGAG
GTGGTAATTGAAACTTTATCAGTGGGAGCAACCATGCTGTTACCTCCATTACGAGAACGG
ATGGAATTACTTCATTCTCTTTTACCTCAAGGACCTGATAGATGGGAAAGCTTATCTAAA
GGACAGAGAATGCAACTGGATATCATCCTGACAAGTTTGCAAGATCATACCCACGTAGCC
TCCCTACTTGGCTATAGTTCACCCTCTGATGCTGCTGACCTATCTTCTGTGTGTACTGGC
TACGGAAATCTGTCAGATCAACCTTACGGCACTCAGAGCTGCCATCCAGATACCCACCTG
GCTGAAATTTTGATGAAGACCCTCTTAAGAAATTTAGGATTTTATACAGATCAAGCATTT
GGAGAGCTAGAAAAGAATAGTGATAAATTTCTACTTGGAACATCATCATCAGAAAACAGT
CAGCCTGCTCATCTTCATGAACTGCTATGTTCACTACAGAAACAGCTGCTGGCATTTTGC
CATATCAATAACATTAGTGAGAACTCAAGCAGTGTGGCATTGCTTCATAAACATCTTCAG
CTTTTGTTGCCTCATGCCACAGATATTTATTCACGTTCTGCAAATTTGCTCAAAGAAAGT
CCTTGGAATGGCAGTGTTGGAGAAAAATTAAGAGATGTGATATACGTCTCAGCTGCTGGC
AGTATGCTCTGCCAGATTGTTAACTCCCTGCTGTTACTCCCTGTGTCAGTGGCTCGGCCT
TTATTGAGTTACCTCCTCGACTTGTTGCCACCTCTTGATTGCCTTAATAGACTCCTGCCA
GCTGCTGATCTTTTAGAAGACCAGGAGTTACAGTGGCCTCTTCATGGAGGGCCAGAACTA
ATTGATCCTGCTGGTCTGCCATTACCTCAGCCAGCTCAGTCCTGGGTATGGCTTGTGGAT
CTAGAAAGAACAATTGCTCTCCTTATTGGGCGGTGTCTTGGTGGCATGCTTCAGGGCTCC
CCTGTGTCTCCAGAGGAACAGGACACTGCATATTGGATGAAAACGCCACTGTTCAGTGAC
GGTGTAGAAATGGACACTCCTCAATTGGATAAATGTATGAGTTGCCTGTTAGAAGTAGCA
CTTTCTGGAAATGAAGAACAGAAGCCTTTTGATTATAAATTGCGGCCTGAAATTGCTGTC
TATGTAGACTTGGCATTGGGTTGTTCTAAAGAGCCTGCCCGAAGCCTTTGGATCAGCATG
CAGGACTATGCTGTTAGTAAAGATTGGGACAGTGCAACTTTAAGTAATGAGTCACTCTTG
GACACTGTGTCTAGATTTGTTCTTGCAGCTCTTCTGAAACACACAAATTTACTTAGTCAA
GCATGTGGAGAAAGCCGATATCAACCTGGTAAACACTTATCAGAAGTGTACCGTTGTGTA
TACAAAGTTCGAAGTCGTTTACTTGCTTGCAAGAACCTTGAACTTATTCAAACAAGGTCA
TCATCACGGGACAGATGGATATCAGAAAACCAGGACTCTGCAGATGTTGATCCTCAGGAG
CATTCATTTACTCGAACTATTGATGAAGAAGCTGAAATGGAAGAACAGGCTGAGAGAGAC
CGGGAAGAGGGGCATCCGGAGCCAGAGGATGAAGAGGAGGAACGGGAACATGAAGTGATG
ACAGCTGGCAAAATCTTTCAGTGTTTCCTCTCAGCCCGTGAAGTAGCTCGTAGCCGAGAC
CGAGATAGAATGAACAGTGGGGCAGGGTCTGGGGCTCGAGCTGATGATCCACCTCCTCAG
TCTCAGCAAGAGCGAAGGGTCAGCACAGACCTTCCTGAGGGTCAGGATGTGTACACTGCT
GCATGCAACTCCGTGATCCATCGGTGTGCCCTGTTAATATTAGGAGTAAGTCCTGTGATA
GATGAGCTTCAGAAGCGAAGAGAAGAAGGACAGTTGCAGCAACCTTCAACAAGTGCCTCT
GAAGGGGGTGGACTTATGACCAGGAGTGAAAGTCTTACTGCAGAGAGCCGGCTAGTCCAC
ACAAGCCCAAATTATAGACTGATCAAATCGAGGAGTGAATCTGATTTGTCTCAGCCTGAA
TCAGATGAAGAGGGTTACGCACTGAGTGGCAGACGAAATGTTGATTTGGATTTGGCAGCA
TCTCACAGAAAGAGAGGTCCTATGCACAGTCAATTGGAATCCCTGAGTGACTCTTGGGCT
CGCCTGAAACATAGCAGAGACTGGTTATGCAACTCCTCCTATTCCTTTGAGTCAGATTTT
GATCTTACCAAGTCTTTGGGAGTTCACACTTTGATTGAAAATGTTGTAAGCTTTGTGAGT
GGAGATGTGGGGAATGCCCCAGGTTTTAAAGAGCCAGAGGAAAGTATGTCTACAAGTCCC
CAGGCCTCCATCATTGCAATGGAACAGCAGCAGTTAAGGGCAGAACTTCGTTTAGAGGCA
CTTCATCAGATCCTCGTTCTATTGTCTGGGATGGAAGAAAAAGGTAGCATCTCACTGGCA
GGAAGCAGATTGAGTTCAGGCTTCCAGTCCTCCACACTACTCACGTCTGTGAGGCTGCAG
TTCCTAGCAGGGTGTTTTGGTTTAGGCACTGTTGGACACACAGGAGGCAAGGGAGAGAGT
GGCCGATTGCATCACTATCAGGATGGGATCAGAGCAGCTAAGAGAAATATTCAGATTGAA
ATCCAGGTAGCTGTGCATAAAATTTATCAACAGTTGTCTGCTACCCTGGAAAGAGCCCTG
CAAGCAAACAAGCATCACATTGAAGCCCAGCAACGTCTGCTTCTGGTTACAGTTTTTGCC
CTAAGTGTTCATTATCAACCAGTAGATGTTTCTTTGGCAATTTCCACTGGTCTGCTAAAC
GTATTGTCACAGTTGTGTGGTACAGACACCATGCTAGGACAGCCCCTGCAGTTGTTGCCA
AAGACGGGTGTTTCCCAGCTTAGCACAGCTTTGAAAGTGGCCAGTACAAGGTTGCTCCAG
ATTCTAGCCATCACTACTGGGACCTATGCTGATAAACTGAGTCCCAAAGTAGTTCAATCC
TTGTTGGATCTACTCTGTAGTCAGTTGAAGAATTTATTGTCCCAAACTGGTGTACTACAT
ATGGCCTCTTTCGGAGAAGGGGAGCAAGAAGACGGTGAAGAAGAAGAAAAAAAAGTTGAC
TCCAGTGGAGAAACTGAGAAGAAAGATTTCAGAGCTGCTCTTAGGAAACAACATGCAGCC
GAACTCCATCTAGGGGATTTTTTAGTTTTTCTTCGCAGAGTTGTATCTTCAAAAGCAATT
CAATCAAAAATGGCTTCCCCAAAGTGGACCGAAGTGCTTCTAAATATAGCATCTCAGAAA
TGTTCTTCAGGTATCCCTCTGGTTGGTAACTTAAGAACAAGGCTCCTTGCACTTCATGTC
CTTGAAGCTGTGCTGCCAGCTTGTGAATCTGGTGTAGAAGATGATCAAATGGCCCAGATT
GTTGAGCGCTTATTTTCCCTTCTCTCTGATTGTATGTGGGAGACACCCATTGCTCAGGCC
AAACATGCTATTCAGATAAAGGAAAAAGAACAAGAAATAAAACTACAGAAGCAGGGCGAG
TTGGAAGAAGAAGATGAGAATCTTCCTATCCAAGAAGTATCCTTTGACCCGGAGAAAGCT
CAGTGTTGCCTAGTGGAGAATGGACAGATTTTAACTCACGGCAGTGGAGGGAAAGGATAT
GGATTGGCATCTACAGGAGTAACTTCTGGGTGCTATCAGTGGAAGTTTTATATTGTGAAG
GAAAACAGAGGTAATGAAGGCACGTGTGTTGGAGTTTCTCGCTGGCCAGTACATGACTTT
AATCACCGCACTACCTCGGATATGTGGCTCTATAGGGCCTACAGTGGTAACCTCTATCAC
AATGGAGAACAGACTCTCACATTGTCCAGCTTTACTCAAGGAGATTTCATTACCTGTGTG
TTAGACATGGAAGCCAGGACCATTTCTTTTGGGAAAAATGGAGAGGAACCCAAATTAGCT
TTTGAAGATGTGGATGCAGCAGAGTTGTACCCATGTGTGATGTTCTATAGTAGCAATCCA
GGGGAAAAGGTGAAAATTTGTGATATGCAGATGCGTGGCACACCCCGAGACTTACTTCCA
GGAGACCCTATTTGTAGTCCAGTAGCAGCAGTGCTGGCTGAGGCCACTATTCAGCTCATC
CGTATCCTTCACCGAACAGACCGTTGGACTTACTGCATTAACAAAAAAATGATGGAAAGG
CTTCACAAAATTAAGATATGTATTAAAGAGTCAGGTCAGAAGCTAAAGAAAAGCCGCTCG
GTTCAGAGCCGAGAGGAAAATGAAATGAGAGAGGAGAAGGAGAGCAAAGAGGAAGAGAAA
GGTAAACATACTAGGCATGGCCTCGCTGACCTCTCAGAGCTGCAGCTGAGGACTCTTTGC
ATAGAGGTGTGGCCCGTGCTGGCTGTGATAGGAGGAGTTGATGCTGGTCTTAGAGTTGGA
GGTCGGTGTGTTCACAAGCAAACTGGGCGCCATGCCACGCTGCTGGGAGTGGTCAAAGAG
GGCAGCACGTCTGCCAAGGTCCAATGGGATGAAGCAGAAATTACTATCAGCTTCCCAACT
TTTTGGTCGCCTAGTGATACTCCATTGTATAATCTGGAACCCTGTGAACCATTGCCGTTT
GATGTGGCGCGATTCCGAGGCCTGACGGCTTCTGTGCTGCTGGACCTAACATATCTCACT
GGCGTTCATGAAGACATGGGCAAACAGAGCACCAAACGACATGAAAAGAAACACCGACAT
GAATCCGAGGAGAAAGGGGATGTTGAGCAGAAACCTGAGAGTGAATCCGCTTTAGATATG
CGAACAGGCCTAACATCTGATGACGTCAAAAGTCAGAGTACCACAAGCTCCAAATCAGAA
AATGAAATCGCTTCATTTTCTTTAGATCCAACACTGCCAAGTGTGGAATCCCAACATCAA
ATAACAGAAGGGAAAAGAAAAAATCATGAACACATGTCCAAAAACCATGATGTAGCCCAG
TCAGAAATCAGAGCAGTCCAGCTGTCCTATCTTTACCTCGGTGCTATGAAGTCACTTAGT
GCCCTTCTTGGCTGTAGTAAATATGCTGAGCTGTTGCTGATACCAAAAGTTCTGGCTGAA
AATGGCCACAACTCAGACTGTGCAAGTTCTCCAGTTGTTCATGAAGACGTGGAGATGCGA
GCAGCCCTGCAGTTCTTGATGCGACACATGGTGAAGCGAGCAGTCATGCGGTCACCCATA
AAGAGAGCATTGGGATTAGCTGATCTGGAACGAGCGCAAGCCATGATCTATAAATTAGTG
GTTCATGGGCTTTTGGAAGACCAGTTTGGGGGCAAAATTAAGCAAGAGATTGATCAACAA
GCTGAAGAAAGTGACCCTGCCCAGCAGGCACAGACACCAGTTACTACTAGCCCATCAGCC
TCAAGCACGACCTCCTTTATGAGCAGCTCTCTGGAGGACACCACAACTGCCACCACTCCA
GTCACTGACACAGAAACAGTGCCTGCATCCGAGTCCCCGGGAGTGATGCCTCTTAGTCTT
CTCAGGCAAATGTTCTCTAGTTACCCAACTACCACTGTACTTCCCACACGTCGGGCACAG
ACTCCTCCAATATCTTCGTTACCAACCTCTCCTTCTGATGAAGTAGGAAGGAGGCAAAGT
TTAACTTCTCCTGATTCCCAGTCAGCAAGGCCAGCTAACCGCACAGCCTTGTCAGACCCA
AGCAGTAGACTTTCAACTTCTCCTCCTCCTCCAGCAATTGCAGTTCCCTTGCTGGAAATG
GGGTTCTCTCTTCGGCAGATTGCCAAAGCCATGGAAGCTACAGGTGCTAGGGGAGAGGCT
GATGCCCAGAATATCACTGTCCTTGCCATGTGGATGATAGAGCACCCTGGGCATGAGGAT
GAAGAGGAGCCCCAGTCGGGCAGCACAGCAGACTCTAGGCCTGGAGCAGCCGTTCTAGGC
AGTGGCGGGAAGTCAAATGATCCCTGTTATTTGCAGTCACCTGGAGACATACCATCAGCT
GATGCTGCTGAAATGGAGGAAGGTTTTAGTGAAAGCCCTGATAATTTGGATCATACAGAG
AATGCAGCTTCTGGAAGTGGACCATCAGCTAGAGGTCGCTCAGCGGTAACAAGAAGACAC
AAGTTTGACTTAGCTGCTCGCACACTGCTAGCAAGAGCAGCGGGATTATACCGCTCTGTG
CAGGCCCACAGGAATCAAAGTCGGAGAGAAGGAATATCTTTGCAGCAAGACCCAGGGGCG
TTGTATGACTTTAATTTAGATGAGGAATTGGAAATTGATCTTGATGATGAGGCGATGGAA
GCTATGTTTGGACAAGACCTGACCAGTGACAATGATATTCTGGGAATGTGGATCCCAGAG
GTACTGGATTGGCCTACCTGGCATGTTTGTGAGTCTGAAGACAGGGAAGAAGTGGTGGTG
TGTGAACTGTGTGAATGCAGCGTCGTCAGCTTCAATCAGCACATGAAGAGAAACCATCCA
GGCTGTGGGCGCAGTGCAAACCGCCAGGGCTATCGCAGCAATGGTTCCTATGTGGATGGC
TGGTTTGGCGGTGAATGTGGGAGTGGAAATCCGTACTACCTGTTATGTGGCACCTGCAGG
GAGAAGTACTTAGCCATGAAGACCAAATCTAAGTCAACAAGTTCTGAAAGGTACAAGGGA
CAAGCTCCAGATCTAATTGGCAAGCAAGACAGTGTGTATGAAGAAGACTGGGACATGTTG
GATGTTGATGAAGATGAAAAGCTAACTGGTGAAGAAGAATTTGAATTACTTGCTGGACCG
CTTGGTTTAAATGACCGGCGCATTGTACCAGAACCAGTTCAGTTCCCTGACAGCGATCCA
CTGGGAGCATCAGTAGCAATGGTCACAGCCACCAACAGTATGGAAGAGACTCTGATGCAA
ATAGGTTGCCATGGCTCCGTAGAAAAGAGCTCCTCTGGGAGAATAACGTTAGGAGAGCAG
GCAGCTGCCCTAGCAAACCCTCATGACCGTGTGGTGGCTTTAAGGAGAGTGACTGCTGCT
GCTCAGGTTCTTCTGGCCAGAACCATGGTCATGAGAGCGCTGTCTCTTCTCTCAGTCAGT
GGTTCCAGTTGTAGCCTGGCTGCTGGTCTTGAGTCTCTGGGGCTAACAGATATCCGAACG
CTAGTTCGATTAATGTGCTTGGCAGCAGCAGGGAGAGCTGGCCTCTCCACCAGCCCTTCT
GCCATGGCTAGCACCTCAGAACGATCACGAGGTGGGCATAGCAAGGCTAACAAGCCTATC
TCTTGCCTGGCCTATTTGAGCACAGCAGTGGGATGTCTGGCATCAAATGCTCCTAGTGCT
GCCAAACTGCTTGTACAGTTGTGTACACAGAACTTGATTTCTGCTGCAACAGGTGTAAAT
CTAACCACAGTTGATGACTCAATTCAGCGAAAGTTTCTACCCAGCTTTCTCCGAGGAATT
GCTGAAGAGAACAAGCTTGTGACCTCCCCAAACTTTGTTGTAACACAGGCCCTTGTGGCA
TTGCTAGCAGACAAAGGGGCCAAACTAAGACCTAACTATGATAAGTCAGAAGTTGAAAAG
AAAGGCCCTCTGGAGTTGGCTAATGCCCTGGCAGCCTGCTGCCTCTCCTCCAGGCTGTCC
TCACAGCATCGGCAATGGGCAGCTCAGCAACTCGTGCGCACTCTTGCTGCACACGACCGT
GACAACCAAACTACTCTGCAGACACTTGCTGATATGGGAGGAGATCTTAGAAAATGCTCC
TTTATCAAATTGGAGGCTCATCAGAACAGAGTAATGACATGTGTTTGGTGTAATAAAAAA
GGTCTTTTGGCTACAAGTGGCAATGATGGCACCATCCGCGTATGGAATGTTACCAAGAAG
CAATATTCACTGCAACAGACCTGTGTGTTCAACAGATTGGAAGGGGATGCTGAGGAAAGC
CTGGGATCACCCAGTGATCCAAGTTTCTCACCAGTTTCCTGGAGTATCAGTGGCAAATAT
CTAGCAGGCGCTTTGGAAAAGATGGTGAATATCTGGCAAGTTAATGGAGGAAAAGGATTA
GTAGATATTCAGCCTCATTGGGTATCTGCCCTGGCTTGGCCAGAAGAGGGTCCGGCTACA
GCCTGGTCAGGAGAGTCTCCAGAATTGTTGTTGGTGGGACGGATGGATGGATCTCTGGGA
CTGATTGAAGTTGTTGATGTGTCCACCATGCACCGTCGAGAATTGGAGCATTGCTATCGA
AAGGATGTGTCTGTTACTTGCATTGCATGGTTCAGTGAAGACAGACCATTTGCAGTGGGA
TATTTTGATGGAAAACTGTTACTGGGAACAAAGGAACCACTTGAGAAAGGAGGCATTGTT
CTAATTGATGCACATAAGGATACTCTTATTAGCATGAAGTGGGACCCTACAGGTCATATT
CTTATGACATGTGCCAAAGAAGACAGTGTGAAACTCTGGGGCTCTATTTCGGGATGCTGG
TGCTGTCTACATTCACTCTGCCATCCATCTATTGTAAATGGCATTGCTTGGTGCCGCCTT
CCAGGGAAAGGATCCAAGTTGCAGTTACTGATGGCTACTGGCTGTCAGAGTGGCTTAGTA
TGTGTTTGGCGCATTCCTCAAGATACTACACAGACCAATGTGACTAGTGCAGAAGGATGG
TGGGAGCAGGAATCAAATTGCCAGGATGGATATAGGAAATCATCAGGAGCCAAGTGTGTT
TATCAGCTGCGGGGACACATCACTCCTGTTCGGACTGTTGCCTTTAGTTCTGATGGGTTG
GCCCTGGTGTCTGGTGGACTAGGTGGGCTCATGAACATTTGGTCTTTAAGGGATGGCTCT
GTCTTGCAAACTGTTGTGATAGGCTCTGGAGCTATTCAGACCACAGTATGGATTCCAGAA
GTTGGAGTAGCTGCTTGCTCAAATAGATCAAAGGATGTTTTGGTCGTGAATTGTACAGCA
GAATGGGCAGCTGCCAATCATGTTTTGGCAACCTGTAGGACAGCATTGAAACAGCAGGGT
GTTCTGGGATTGAACATGGCTCCCTGCATGAGAGCATTTTTGGAGCGGCTCCCCATGATG
CTTCAGGAGCAGTATGCCTATGAAAAGCCTCATGTGGTTTGTGGTGACCAACTTGTTCAT
AGCCCCTATATGCAATGCTTGGCTTCCCTTGCTGTGGGACTTCATCTGGATCAGCTGTTG
TGTAACCCTCCAGTGCCACCACACCACCAGAACTGTCTCCCTGACCCTGCATCCTGGAAT
CCAAATGAATGGGCCTGGTTAGAATGTTTCTCAACCACTATAAAAGCTGCCGAAGCCCTG
ACCAATGGAGCCCAGTTTCCAGAATCTTTTACCGTTCCAGATCTAGAACCTGTTCCAGAG
GATGAACTTGTATTTCTAATGGATAACAGTAAATGGATTAACGGCATGGATGAACAAATT
ATGTCTTGGGCAACTTCCAGACCTGAGGACTGGCACCTGGGAGGTAAATGTGATGTCTAC
TTATGGGGTGCTGGTAGGCATGGACAGCTGGCAGAAGCTGGAAGAAATGTAATGGTACCT
GCAGCAGCTCCCTCATTCTCACAGGCCCAACAGGTCATTTGTGGTCAGAATTGTACCTTT
GTCATCCAGGCCAATGGCACAGTGTTGGCTTGTGGGGAAGGAAGTTATGGCAGATTAGGA
CAAGGAAATTCAGATGACCTTCATGTGCTGACAGTTATTTCAGCCTTACAAGGCTTTGTG
GTGACCCAGCTGGTGACTTCCTGTGGTTCTGATGGGCACTCTATGGCCCTAACTGAAAGT
GGTGAGGTCTTTAGCTGGGGAGATGGTGACTATGGTAAACTTGGCCATGGGAACAGCGAC
AGGCAGCGGCGGCCCAGGCAGATCGAGGCCTTACAAGGAGAAGAAGTGGTGCAGATGTCT
TGTGGCTTCAAGCACTCAGCAGTGGTCACTTCAGATGGCAAACTGTTCACCTTTGGGAAT
GGTGACTATGGTCGTCTGGGTCTTGGAAATACCTCTAACAAAAAACTTCCAGAGAGAGTG
ACTGCACTGGAGGGATATCAGATTGGACAGGTGGCCTGTGGATTAAACCACACTTTGGCA
GTGTCAGCAGATGGTTCCATGGTGTGGGCTTTTGGAGATGGAGACTATGGAAAACTAGGC
TTAGGAAATTCCACTGCAAAATCTTCACCTCAGAAAATTGACGTCCTTTGTGGAATTGGA
ATAAAAAAGGTTGCTTGTGGAACTCAGTTTTCTGTTGCTTTGACCAAAGATGGTCATGTG
TATACCTTTGGTCAAGATCGCCTGATAGGCTTGCCAGAGGGGCGTGCTCGCAATCACAAT
CGACCGCAACAAATCCCTGTCCTGGCTGGAGTAATCATAGAAGATGTGGCAGTTGGAGCT
GAACACACACTTGCTTTGGCATCAAATGGAGATGTGTATGCCTGGGGGAGCAATTCAGAA
GGGCAGCTCGGCTTAGGCCATACCAACCATGTTCGAGAACCAACCCTGGTAACAGGTCTG
CAAGGGAAAAATGTTCGGCAGATCTCGGCTGGCCGCTGCCACAGTGCTGCATGGACAGCA
CCACCTGTCCCACCAAGAGCACCAGGTGTGTCAGTACCTCTGCAGCTGGGCCTGCCTGAC
ACAGTGCCCCCCCAGTATGGGGCGCTGAGAGAAGTCAGCATTCACACGGTGCGGGCCAGG
CTCCGGCTGCTCTACCACTTCTCTGACCTCATGTACTCATCCTGGAGACTGCTGAACCTT
AGCCCCAACAACCAGAACAGCACATCCCATTATAATGCTGGAACTTGGGGCATTGTACAG
GGACAACTTCGGCCTTTGTTAGCCCCAAGAGTCTACACTCTGCCAATGGTGCGCTCCATA
GGAAAAACCATGGTTCAAGGCAAAAACTATGGACCTCAGATAACTGTAAAGAGGATATCA
ACCAGAGGACGGAAGTGTAAGCCTATTTTTGTCCAAATAGCGAGACAAGTAGTTAAGCTG
AATGCTTCAGACCTCCGCCTGCCTTCCCGAGCGTGGAAGGTTAAGCTGGTTGGAGAAGGG
GCTGATGATGCTGGAGGAGTGTTTGATGACACCATCACAGAGATGTGCCAGGAACTTGAA
ACTGGTATTGTTGACCTTCTTATACCCTCTCCCAATGCCACCGCAGAAGTGGGTTACAAT
AGGGACAGGTTCCTTTTTAACCCTTCTGCCTGCCTCGATGAACACTTAATGCAGTTTAAG
TTTTTAGGAATTTTAATGGGGGTTGCCATTCGCACAAAGAAGCCTCTGGACCTCCACTTG
GCCCCTCTGGTGTGGAAGCAGCTGTGCTGTGTCCCACTCACCCTAGAGGACCTGGAGGAG
GTGGATCTGCTCTACGTGCAGACTCTCAACAGCATTCTTCACATTGAAGACAGTGGGATT
ACCGAGGAGAGTTTCCATGAGATGATTCCTCTTGATTCTTTTGTTGGCCAGAGTGCTGAT
GGCAAAATGGTTCCTATAATCCCTGGTGGAAATAGTATCCCACTCACATTTTCCAACAGG
AAGGAATATGTGGAGAGGGCCATTGAATATCGACTTCATGAGATGGACAGACAGGTGGCT
GCAGTCCGAGAAGGGATGTCCTGGATTGTTCCTGTGCCGCTGCTGTCCCTCCTCACAGCA
AAACAACTGGAGCAGATGGTGTGTGGGATGCCCGAGATCTCTGTGGAAGTCTTGAAGAAA
GTGGTGCGGTACCGTGAGGTGGATGAGCAGCATCAGCTGGTGCAGTGGTTCTGGCACACG
CTGGAAGAGTTCTCCAATGAGGAGCGGGTGCTTTTCATGAGGTTTGTGTCAGGAAGATCT
CGACTACCAGCCAACACTGCTGACATTTCTCAGAGATTTCAAATCATGAAGGTTGATAGG
CCTTACGACAGTCTGCCTACCTCACAGACCTGCTTCTTCCAGCTGAGGCTGCCCCCGTAC
TCCAGCCAGCTGGTCATGGCCGAGCGCCTGCGCTATGCCATCAACAACTGCCGCTCAATC
GACATGGACAACTACATGCTCTCGAGAAACGTGGACAACGCCGAGGGCTCCGACACTGAC
TACTGA
Enzyme 99 GenBank Gene ID NM_003922.3 Link Image
Enzyme 99 GeneCard ID HERC1 Link Image
Enzyme 99 GenAtlas ID HERC1 Link Image
Enzyme 99 HGNC ID HGNC:4867 Link Image
Enzyme 99 Chromosome Location 1
Enzyme 99 Locus 15q22
Enzyme 99 SNPs SNPJam Report Link Image
Enzyme 99 General References
  1. Rosa JL, Casaroli-Marano RP, Buckler AJ, Vilaro S, Barbacid M: p619, a giant protein related to the chromosome condensation regulator RCC1, stimulates guanine nucleotide exchange on ARF1 and Rab proteins. EMBO J. 1996 Aug 15;15(16):4262-73. [PubMed Link Image]
  2. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Rosa JL, Barbacid M: A giant protein that stimulates guanine nucleotide exchange on ARF1 and Rab proteins forms a cytosolic ternary complex with clathrin and Hsp70. Oncogene. 1997 Jul 3;15(1):1-6. [PubMed Link Image]
  5. Garcia-Gonzalo FR, Cruz C, Munoz P, Mazurek S, Eigenbrodt E, Ventura F, Bartrons R, Rosa JL: Interaction between HERC1 and M2-type pyruvate kinase. FEBS Lett. 2003 Mar 27;539(1-3):78-84. [PubMed Link Image]
  6. Garcia-Gonzalo FR, Munoz P, Gonzalez E, Casaroli-Marano RP, Vilaro S, Bartrons R, Ventura F, Rosa JL: The giant protein HERC1 is recruited to aluminum fluoride-induced actin-rich surface protrusions in HeLa cells. FEBS Lett. 2004 Feb 13;559(1-3):77-83. [PubMed Link Image]
  7. Garcia-Gonzalo FR, Bartrons R, Ventura F, Rosa JL: Requirement of phosphatidylinositol-4,5-bisphosphate for HERC1-mediated guanine nucleotide release from ARF proteins. FEBS Lett. 2005 Jan 17;579(2):343-8. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  9. Chong-Kopera H, Inoki K, Li Y, Zhu T, Garcia-Gonzalo FR, Rosa JL, Guan KL: TSC1 stabilizes TSC2 by inhibiting the interaction between TSC2 and the HERC1 ubiquitin ligase. J Biol Chem. 2006 Mar 31;281(13):8313-6. Epub 2006 Feb 7. [PubMed Link Image]
  10. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  11. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  12. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  13. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  14. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  15. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 99 Metabolite References Not Available
Enzyme 100 [top]
Enzyme 100 ID 14166
Enzyme 100 Name Eukaryotic translation initiation factor 5
Enzyme 100 Synonyms
  1. eIF-5
Enzyme 100 Gene Name EIF5
Enzyme 100 Protein Sequence >Eukaryotic translation initiation factor 5
MSVNVNRSVSDQFYRYKMPRLIAKVEGKGNGIKTVIVNMVDVAKALNRPPTYPTKYFGCE
LGAQTQFDVKNDRYIVNGSHEANKLQDMLDGFIKKFVLCPECENPETDLHVNPKKQTIGN
SCKACGYRGMLDTHHKLCTFILKNPPENSDSGTGKKEKEKKNRKGKDKENGSVSSSETPP
PPPPPNEINPPPHTMEEEEDDDWGEDTTEEAQRRRMDEISDHAKVLTLSDDLERTIEERV
NILFDFVKKKKEEGVIDSSDKEIVAEAERLDVKAMGPLVLTEVLFNEKIREQIKKYRRHF
LRFCHNNKKAQRYLLHGLECVVAMHQAQLISKIPHILKEMYDADLLEEEVIISWSEKASK
KYVSKELAKEIRVKAEPFIKWLKEAEEESSGGEEEDEDENIEVVYSKAASVPKVETVKSD
NKDDDIDIDAI
Enzyme 100 Number of Residues 431
Enzyme 100 Molecular Weight 49222.4
Enzyme 100 Theoretical pI 5.26
Enzyme 100 GO Classification
Function
  • RNA binding
  • binding
  • nucleic acid binding
  • translation factor activity, nucleic acid binding
  • translation initiation factor activity
Process
  • cellular process
  • translational initiation
Component
Enzyme 100 General Function Involved in binding
Enzyme 100 Specific Function Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F])
Enzyme 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 10439908 Link Image
Enzyme 100 UniProtKB/Swiss-Prot ID P55010 Link Image
Enzyme 100 UniProtKB/Swiss-Prot Entry Name IF5_HUMAN Link Image
Enzyme 100 PDB ID Not Available
Enzyme 100 Cellular Location Not Available
Enzyme 100 Gene Sequence >1296 bp
ATGTCTGTCAATGTCAACCGCAGCGTGTCAGACCAGTTCTATCGCTACAAGATGCCCCGT
CTGATTGCCAAGGTTGAGGGCAAAGGCAATGGAATCAAGACAGTTATAGTCAACATGGTT
GACGTTGCAAAGGCGCTTAATCGGCCTCCAACGTATCCCACCAAATATTTTGGTTGTGAG
CTGGGAGCACAGACCCAGTTTGATGTTAAGAATGACCGTTACATTGTCAATGGATCTCAT
GAGGCGAATAAGCTGCAAGACATGTTGGATGGATTCATTAAAAAATTTGTTCTCTGTCCT
GAATGTGAGAATCCTGAAACAGATTTGCATGTCAATCCAAAGAAGCAAACAATAGGTAAT
TCTTGTAAAGCCTGTGGCTATCGAGGCATGCTTGACACACATCATAAACTCTGCACATTC
ATTCTCAAAAACCCACCTGAGAATAGTGACAGTGGTACAGGAAAGAAAGAAAAAGAAAAG
AAAAACAGAAAGGGCAAAGACAAGGAAAATGGCTCCGTATCCAGCAGTGAGACACCACCA
CCACCACCACCACCAAATGAAATTAATCCTCCTCCACATACAATGGAAGAAGAGGAGGAT
GATGACTGGGGAGAAGATACAACTGAGGAAGCTCAAAGGCGTCGAATGGATGAAATCAGT
GACCATGCAAAAGTTCTGACACTCAGTGATGATTTGGAAAGAACAATTGAGGAGAGGGTC
AATATCCTCTTTGATTTTGTTAAGAAAAAGAAAGAAGAGGGTGTTATTGATTCATCTGAC
AAAGAAATCGTTGCTGAAGCAGAAAGACTGGATGTAAAAGCCATGGGCCCTCTTGTTCTA
ACTGAAGTTCTTTTTAATGAGAAGATTAGAGAACAGATTAAGAAATACAGGCGCCATTTC
CTACGATTTTGTCACAACAACAAAAAAGCCCAACGGTACCTTCTTCATGGTTTGGAGTGT
GTGGTAGCAATGCATCAAGCTCAGCTTATCTCCAAGATTCCACATATCTTGAAGGAGATG
TACGATGCAGACCTTTTAGAAGAAGAGGTCATCATCAGCTGGTCGGAAAAGGCCTCTAAG
AAATATGTCTCCAAAGAACTTGCCAAAGAGATTCGTGTCAAAGCAGAACCATTTATAAAA
TGGTTGAAGGAGGCAGAGGAAGAATCTTCTGGTGGCGAAGAAGAAGATGAAGATGAGAAC
ATTGAGGTGGTGTATTCGAAGGCTGCCAGTGTACCGAAAGTTGAGACTGTAAAGTCAGAC
AACAAGGATGACGACATCGATATTGATGCCATTTAA
Enzyme 100 GenBank Gene ID AK026933 Link Image
Enzyme 100 GeneCard ID EIF5 Link Image
Enzyme 100 GenAtlas ID EIF5 Link Image
Enzyme 100 HGNC ID HGNC:3299 Link Image
Enzyme 100 Chromosome Location 1
Enzyme 100 Locus 14q32.32
Enzyme 100 SNPs SNPJam Report Link Image
Enzyme 100 General References
  1. Si K, Das K, Maitra U: Characterization of multiple mRNAs that encode mammalian translation initiation factor 5 (eIF-5). J Biol Chem. 1996 Jul 12;271(28):16934-8. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  8. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  9. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  10. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  11. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  12. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 100 Metabolite References Not Available
Enzyme 101 [top]
Enzyme 101 ID 14182
Enzyme 101 Name IQ motif and SEC7 domain-containing protein 1
Enzyme 101 Synonyms
  1. ADP-ribosylation factors guanine nucleotide-exchange protein 100
  2. ADP-ribosylation factors guanine nucleotide-exchange protein 2
  3. Brefeldin-resistant Arf-GEF 2 protein
Enzyme 101 Gene Name IQSEC1
Enzyme 101 Protein Sequence >IQ motif and SEC7 domain-containing protein 1
MWCLHCNSERTQSLLELELDSGVEGEAPSSETGTSLDSPSAYPQGPLVPGSSLSPDHYEH
TSVGAYGLYSGPPGQQQRTRRPKLQHSTSILRKQAEEEAIKRSRSLSESYELSSDLQDKQ
VEMLERKYGGRLVTRHAARTIQTAFRQYQMNKNFERLRSSMSENRMSRRIVLSNMRMQFS
FEGPEKVHSSYFEGKQVSVTNDGSQLGALVSPECGDLSEPTTLKSPAPSSDFADAITELE
DAFSRQVKSLAESIDDALNCRSLHTEEAPALDAARARDTEPQTALHGMDHRKLDEMTASY
SDVTLYIDEEELSPPLPLSQAGDRPSSTESDLRLRAGGAAPDYWALAHKEDKADTDTSCR
STPSLERQEQRLRVEHLPLLTIEPPSDSSVDLSDRSERGSLKRQSAYERSLGGQQGSPKH
GPHSGAPKSLPREEPELRPRPPRPLDSHLAINGSANRQSKSESDYSDGDNDSINSTSNSN
DTINCSSESSSRDSLREQTLSKQTYHKEARNSWDSPAFSNDVIRKRHYRIGLNLFNKKPE
KGVQYLIERGFVPDTPVGVAHFLLQRKGLSRQMIGEFLGNRQKQFNRDVLDCVVDEMDFS
TMELDEALRKFQAHIRVQGEAQKVERLIEAFSQRYCICNPGVVRQFRNPDTIFILAFAII
LLNTDMYSPNVKPERKMKLEDFIKNLRGVDDGEDIPREMLMGIYERIRKRELKTNEDHVS
QVQKVEKLIVGKKPIGSLHPGLGCVLSLPHRRLVCYCRLFEVPDPNKPQKLGLHQREIFL
FNDLLVVTKIFQKKKNSVTYSFRQSFSLYGMQVLLFENQYYPNGIRLTSSVPGADIKVLI
NFNAPNPQDRKKFTDDLRESIAEVQEMEKHRIESELEKQKGVVRPSMSQCSSLKKESGNG
TLSRACLDDSYASGEGLKRSALSSSLRDLSEAGKRGRRSSAGSLESNVEFQPFEPLQPSV
LCS
Enzyme 101 Number of Residues 963
Enzyme 101 Molecular Weight 108313.3
Enzyme 101 Theoretical pI 6.93
Enzyme 101 GO Classification
Function
  • ARF guanyl-nucleotide exchange factor activity
  • GTPase regulator activity
  • enzyme regulator activity
  • nucleoside-triphosphatase regulator activity
  • small GTPase regulator activity
Process
  • biological regulation
  • regulation of ARF protein signal transduction
  • regulation of Ras protein signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 101 General Function Involved in ARF guanyl-nucleotide exchange factor activity
Enzyme 101 Specific Function In addition to accelerate GTP gamma S binding by ARFs of all three classes, it appears to function preferentially as a guanine nucleotide exchange protein for ARF6, mediating internalisation of beta-1 integrin
Enzyme 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 50582989 Link Image
Enzyme 101 UniProtKB/Swiss-Prot ID Q6DN90 Link Image
Enzyme 101 UniProtKB/Swiss-Prot Entry Name IQEC1_HUMAN Link Image
Enzyme 101 PDB ID Not Available
Enzyme 101 Cellular Location Not Available
Enzyme 101 Gene Sequence >2892 bp
ATGTGGTGCCTGCACTGCAACTCGGAGAGGACCCAGTCCCTTCTGGAGCTAGAGCTTGAC
AGCGGCGTCGAGGGCGAGGCCCCCAGCAGTGAGACTGGCACATCCCTGGACAGCCCCTCA
GCCTACCCCCAGGGCCCCTTGGTGCCCGGTTCCAGCCTGAGCCCGGATCACTACGAGCAC
ACGTCAGTGGGAGCCTATGGGCTGTACTCGGGGCCGCCGGGGCAACAGCAGCGCACGCGG
AGGCCCAAGCTGCAGCACTCGACCTCCATCCTGCGCAAGCAGGCTGAGGAGGAGGCCATC
AAGCGCTCACGCTCACTCTCCGAGAGCTATGAGCTCTCCTCGGACCTGCAGGACAAGCAG
GTGGAGATGCTAGAACGAAAGTATGGGGGGCGCCTGGTAACCCGCCATGCGGCCCGCACC
ATCCAGACGGCGTTTCGCCAGTACCAGATGAACAAGAACTTCGAGCGCTTGCGCAGCTCC
ATGTCAGAGAACCGCATGTCACGCCGGATTGTGCTGTCCAACATGAGGATGCAGTTCTCC
TTTGAGGGGCCTGAGAAAGTGCACAGCTCCTACTTCGAGGGGAAGCAGGTCTCAGTGACT
AACGACGGCTCCCAGCTGGGAGCCCTGGTGTCCCCTGAGTGTGGTGACCTCAGCGAGCCC
ACCACCCTCAAGTCTCCGGCCCCCTCCAGTGACTTTGCGGACGCCATCACCGAGCTGGAG
GACGCCTTCTCTAGGCAAGTGAAATCACTGGCCGAGTCCATCGACGATGCCCTCAACTGC
CGCAGCCTGCACACTGAGGAGGCACCGGCCCTGGATGCGGCGCGGGCCCGGGACACCGAA
CCCCAGACAGCCCTGCACGGCATGGACCACCGCAAACTGGACGAGATGACGGCCTCGTAC
AGTGATGTCACCCTGTACATCGATGAGGAGGAGCTGTCGCCCCCTCTGCCCCTCTCGCAG
GCAGGGGACCGGCCGTCCAGCACCGAGTCGGACCTGCGGCTACGGGCTGGGGGCGCAGCC
CCAGACTACTGGGCCCTGGCCCACAAAGAGGACAAGGCTGACACGGACACGAGCTGCCGG
AGCACGCCGTCGCTGGAGCGGCAGGAGCAGCGGCTGCGGGTGGAGCATCTGCCGCTGCTC
ACCATCGAGCCACCCAGCGACAGCTCTGTGGACCTTAGTGACCGCTCGGAGCGGGGGTCA
CTCAAGAGGCAGAGTGCTTACGAGCGCAGCCTTGGCGGGCAGCAGGGCAGTCCCAAGCAT
GGTCCCCACAGCGGCGCCCCCAAGAGCCTCCCCCGGGAGGAGCCTGAGTTGCGGCCCCGG
CCCCCCAGGCCCCTGGACAGCCACTTGGCCATCAATGGCTCAGCCAACCGGCAGAGCAAG
TCTGAGTCGGACTACTCAGACGGTGACAATGACAGCATCAACAGCACGTCCAACTCCAAC
GATACCATCAACTGCAGCTCCGAGTCATCGTCCCGTGACAGCCTGCGGGAGCAGACGCTC
AGCAAGCAGACCTACCACAAGGAGGCCCGCAACAGCTGGGACTCGCCTGCCTTTAGCAAC
GATGTCATCCGCAAGAGGCACTACCGCATCGGCCTGAACCTCTTCAACAAGAAGCCTGAG
AAGGGAGTCCAGTACCTCATCGAGCGTGGCTTTGTGCCCGACACGCCCGTCGGGGTGGCC
CACTTCCTGCTGCAGCGCAAGGGCCTCAGCCGGCAGATGATCGGCGAGTTCCTGGGCAAC
CGGCAGAAGCAGTTCAACCGTGACGTGCTCGACTGCGTCGTGGACGAGATGGACTTCTCT
ACCATGGAGCTGGATGAGGCCCTCAGGAAATTCCAGGCGCACATCCGTGTCCAAGGGGAG
GCTCAGAAAGTGGAGCGGCTCATAGAGGCGTTCAGCCAGCGCTACTGCATCTGCAACCCT
GGGGTGGTGCGGCAATTCCGGAACCCAGACACCATTTTCATCCTGGCCTTCGCCATCATC
CTGCTGAACACCGACATGTACAGCCCCAATGTCAAGCCCGAGCGGAAAATGAAGCTAGAG
GACTTCATCAAGAACCTCCGAGGTGTGGACGATGGTGAGGACATTCCCCGTGAGATGCTG
ATGGGGATCTATGAACGGATCCGTAAGCGAGAGCTAAAGACCAATGAGGACCATGTGTCC
CAGGTGCAGAAGGTGGAGAAGCTCATTGTGGGGAAAAAGCCGATCGGATCCCTGCATCCC
GGGCTCGGCTGTGTGCTCTCTCTGCCCCACCGTCGGTTGGTCTGCTACTGCCGGCTCTTT
GAGGTTCCAGACCCAAACAAGCCCCAGAAACTCGGACTACACCAGCGAGAAATCTTCCTG
TTCAACGACCTCCTGGTGGTCACCAAGATCTTCCAGAAGAAGAAGAACTCGGTGACGTAC
AGCTTCCGACAGTCCTTCTCCTTGTACGGCATGCAGGTCCTGCTCTTCGAGAACCAGTAC
TACCCCAATGGCATCCGGCTCACCTCGTCTGTCCCCGGAGCAGATATCAAAGTGTTAATA
AACTTCAACGCCCCCAACCCTCAAGACCGGAAGAAATTCACCGATGACCTGCGGGAGTCC
ATTGCGGAAGTCCAAGAGATGGAGAAGCACAGGATAGAGTCGGAGCTCGAGAAGCAGAAA
GGCGTCGTGCGGCCCAGCATGTCCCAGTGCTCTAGCCTCAAAAAGGAGTCGGGCAACGGA
ACACTGAGCCGGGCCTGCCTGGACGACAGCTATGCCAGCGGTGAGGGCCTCAAGCGCAGC
GCCCTCAGCAGCTCCCTGCGGGACCTCTCGGAAGCCGGGAAGCGAGGGCGTCGCAGCAGT
GCGGGATCGCTAGAGAGCAATGTGGAATTTCAGCCTTTCGAGCCACTGCAGCCGTCAGTG
CTGTGCTCCTAA
Enzyme 101 GenBank Gene ID NM_014869.4 Link Image
Enzyme 101 GeneCard ID IQSEC1 Link Image
Enzyme 101 GenAtlas ID IQSEC1 Link Image
Enzyme 101 HGNC ID HGNC:29112 Link Image
Enzyme 101 Chromosome Location 3
Enzyme 101 Locus 3p25.2
Enzyme 101 SNPs SNPJam Report Link Image
Enzyme 101 General References
  1. Dunphy JL, Moravec R, Ly K, Lasell TK, Melancon P, Casanova JE: The Arf6 GEF GEP100/BRAG2 regulates cell adhesion by controlling endocytosis of beta1 integrins. Curr Biol. 2006 Feb 7;16(3):315-20. [PubMed Link Image]
  2. Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Oct 30;5(5):277-86. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Someya A, Sata M, Takeda K, Pacheco-Rodriguez G, Ferrans VJ, Moss J, Vaughan M: ARF-GEP(100), a guanine nucleotide-exchange protein for ADP-ribosylation factor 6. Proc Natl Acad Sci U S A. 2001 Feb 27;98(5):2413-8. [PubMed Link Image]
  5. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  8. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 101 Metabolite References Not Available
Enzyme 102 [top]
Enzyme 102 ID 14191
Enzyme 102 Name Guanine nucleotide exchange factor DBS
Enzyme 102 Synonyms
  1. DBL's big sister
  2. MCF2-transforming sequence-like protein
Enzyme 102 Gene Name MCF2L
Enzyme 102 Protein Sequence >Guanine nucleotide exchange factor DBS
MFDCWRFILCKRPGSNSYSSPQRPNEAKKEETDHQIDVSDVIRLVQDTPEATAMATDEIM
HQDIVPLCAADIQDQLKKRFAYLSGGRGQDGSPVITFPDYPAFSEIPDKEFQNVMTYLTS
IPSLQDAGIGFILVIDRRRDKWTSVKASVLRIAASFPANLQLVLVLRPTGFFQRTLSDIA
FKFNRDDFKMKVPVIMLSSVPDLHGYIDKSQLTEDLGGTLDYCHSRWLCQRTAIESFALM
VKQTAQMLQSFGTELAETELPNDVQSTSSVLCAHTEKKDKAKEDLRLALKEGHSVLESLR
ELQAEGSEPSVNQDQLDNQATVQRLLAQLNETEAAFDEFWAKHQQKLEQCLQLRHFEQGF
REVKAILDAASQKIATFTDIGNSLAHVEHLLRDLASFEEKSGVAVERARALSLDGEQLIG
NKHYAVDSIRPKCQELRHLCDQFSAEIARRRGLLSKSLELHRRLETSMKWCDEGIYLLAS
QPVDKCQSQDGAEAALQEIEKFLETGAENKIQELNAIYKEYESILNQDLMEHVRKVFQKQ
ASMEEVFHRRQASLKKLAARQTRPVQPVAPRPEALAKSPCPSPGIRRGSENSSSEGGALR
RGPYRRAKSEMSESRQGRGSAGEEEESLAILRRHVMSELLDTERAYVEELLCVLEGYAAE
MDNPLMAHLLSTGLHNKKDVLFGNMEEIYHFHNRIFLRELENYTDCPELVGRCFLERMED
FQIYEKYCQNKPRSESLWRQCSDCPFFQECQRKLDHKLSLDSYLLKPVQRITKYQLLLKE
MLKYSRNCEGAEDLQEALSSILGILKAVNDSMHLIAITGYDGNLGDLGKLLMQGSFSVWT
DHKRGHTKVKELARFKPMQRHLFLHEKAVLFCKKREENGEGYEKAPSYSYKQSLNMAAVG
ITENVKGDAKKFEIWYNAREEVYIVQAPTPEIKAAWVNEIRKVLTSQLQACREASQHRAL
EQSQSLPLPAPTSTSPSRGNSRNIKKLEERKTDPLSLEGYVSSAPLTKPPEKGKGWSKTS
HSLEAPEDDGGWSSAEEQINSSDAEEDGGLGPKKLVPGKYTVVADHEKGGPDALRVRSGD
VVELVQEGDEGLWYVRDPTTGKEGWVPASSLSVRLGPSGSAQCLSSSGKAHVPRAHP
Enzyme 102 Number of Residues 1137
Enzyme 102 Molecular Weight 128107.9
Enzyme 102 Theoretical pI 6.39
Enzyme 102 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 102 General Function Involved in Rho guanyl-nucleotide exchange factor activity
Enzyme 102 Specific Function Guanine nucleotide exchange factor that potentially links pathways that signal through RAC1, RHOA and CDC42. Catalyzes guanine nucleotide exchange on RHOA and CDC42 and interacts specifically with the GTP-bound form of RAC1, suggesting that it functions as an effector of RAC1. May also participate in axonal transport in the brain. Becomes activated and highly tumorigenic by truncation of the N-terminus. Isoform 5 activates CDC42
Enzyme 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 163644323 Link Image
Enzyme 102 UniProtKB/Swiss-Prot ID O15068 Link Image
Enzyme 102 UniProtKB/Swiss-Prot Entry Name MCF2L_HUMAN Link Image
Enzyme 102 PDB ID 1RJ2 Link Image
Enzyme 102 PDB File Show
Enzyme 102 3D Structure
Enzyme 102 Cellular Location Not Available
Enzyme 102 Gene Sequence >3390 bp
ATGGCCGAGAAGGGAGCATCCCGGGGAACCCTGCGGCGGCTGTGGTCACTGCCCAGGAGG
CGCCGGGGAACTGCAGGGCGCTCGAGGCCAGATGAAATCATGCACCAGGACATCGTCCCG
CTCTGTGCTGCCGACATCCAGGACCAGCTAAAGAAGCGCTTTGCTTACCTGTCCGGTGGG
CGGGGGCAGGACGGAAGCCCGGTTATCACCTTCCCTGACTACCCGGCCTTCAGCGAGATT
CCGGACAAGGAGTTCCAGAATGTCATGACCTACCTCACCAGCATCCCCAGCCTGCAGGAC
GCTGGCATCGGATTCATCCTGGTGATAGACCGGCGACGGGACAAATGGACCTCCGTGAAG
GCGTCCGTCCTGCGCATCGCAGCATCTTTCCCGGCAAACCTGCAGCTCGTCCTCGTGCTT
CGCCCGACGGGTTTTTTCCAAAGGACTCTCTCCGACATCGCTTTCAAATTCAATAGAGAT
GACTTTAAGATGAAGGTGCCGGTCATAATGCTGAGCTCCGTACCAGACTTACACGGTTAC
ATCGATAAGTCGCAGCTGACCGAGGACCTGGGTGGGACCCTGGACTACTGCCACTCCCGG
TGGCTGTGCCAGCGCACGGCCATCGAAAGTTTCGCCCTCATGGTGAAGCAGACGGCTCAG
ATGCTGCAGTCCTTCGGGACCGAGCTGGCTGAAACAGAGCTGCCCAATGACGTCCAGTCG
ACAAGCTCAGTGCTGTGTGCGCACACAGAGAAGAAGGACAAGGCGAAGGAGGATTTGAGG
CTGGCACTGAAAGAGGGGCACAGTGTCCTGGAGAGCCTCAGGGAGCTGCAGGCTGAGGGC
TCAGAGCCCAGTGTGAACCAGGACCAGCTTGACAACCAGGCCACCGTGCAGAGGCTCCTG
GCCCAGCTGAACGAAACCGAGGCTGCCTTCGATGAGTTCTGGGCAAAGCATCAGCAGAAA
CTGGAGCAGTGTCTGCAGCTCCGGCACTTTGAGCAGGGCTTCCGGGAGGTCAAAGCCATC
TTGGACGCAGCGTCCCAGAAGATAGCAACCTTCACAGACATCGGCAACAGCCTGGCGCAT
GTGGAGCACCTGCTGAGGGACCTGGCCAGCTTCGAGGAGAAATCAGGCGTGGCCGTGGAG
AGGGCCCGGGCCCTGTCTCTGGACGGCGAGCAGCTCATTGGGAACAAGCACTACGCGGTA
GACTCCATCCGCCCAAAGTGCCAGGAGCTCCGGCACCTCTGTGACCAGTTCTCTGCGGAG
ATCGCAAGGAGGAGGGGGCTGCTCAGCAAGTCCCTGGAGCTGCACCGCCGCCTGGAGACG
TCCATGAAGTGGTGTGATGAAGGGATTTACCTGCTGGCCTCACAACCTGTGGACAAGTGC
CAGTCCCAGGACGGCGCGGAGGCTGCCCTCCAGGAAATCGAGAAGTTTTTGGAGACCGGT
GCGGAAAATAAGATCCAGGAGCTCAACGCGATTTACAAGGAATACGAATCCATCCTCAAC
CAAGATCTCATGGAGCACGTGCGAAAGGTCTTCCAGAAGCAGGCAAGCATGGAGGAGGTG
TTCCACCGCAGGCAGGCCAGCCTGAAGAAGCTGGCGGCCAGGCAGACGCGGCCCGTGCAG
CCGGTGGCCCCCAGACCCGAGGCACTGGCAAAGTCGCCCTGCCCCTCCCCAGGCATTCGG
CGAGGCTCTGAGAACTCCAGCTCCGAGGGCGGTGCGCTCCGGAGAGGGCCCTACCGGAGG
GCCAAGAGTGAGATGAGTGAGAGCCGGCAGGGCCGCGGCTCAGCGGGGGAGGAGGAGGAA
AGCCTGGCCATCCTGCGCAGGCACGTGATGAGCGAGCTCCTGGACACAGAACGGGCCTAC
GTGGAGGAGCTGCTGTGCGTCCTGGAGGGCTACGCCGCGGAGATGGATAACCCACTGATG
GCTCACCTCCTGTCAACAGGCCTTCACAACAAGAAGGATGTTTTGTTTGGAAACATGGAG
GAAATCTATCACTTCCACAACAGGATATTCCTCAGGGAGCTGGAAAACTACACTGACTGC
CCAGAACTGGTTGGAAGATGCTTTCTGGAGAGGATGGAAGATTTCCAGATCTATGAGAAG
TACTGTCAGAACAAGCCCCGCTCTGAGAGCCTGTGGAGACAGTGCTCCGACTGCCCGTTT
TTCCAGGAATGCCAGAGAAAGCTGGACCACAAGCTGAGCCTGGACTCCTACCTGCTGAAG
CCAGTGCAGAGGATCACCAAGTACCAGCTGCTGCTCAAGGAAATGCTGAAATACAGCAGG
AACTGCGAGGGGGCTGAGGACCTGCAGGAGGCGCTGAGCTCCATCCTGGGCATCCTGAAG
GCCGTGAACGACTCCATGCACCTCATCGCTATCACCGGCTATGACGGGAATCTCGGCGAC
CTGGGCAAGCTGCTGATGCAGGGCTCGTTCAGCGTCTGGACCGACCACAAGAGGGGCCAC
ACCAAGGTGAAGGAGCTGGCCAGGTTCAAGCCCATGCAGCGGCACCTGTTCCTGCACGAG
AAGGCAGTGCTCTTCTGCAAGAAGAGGGAGGAGAATGGGGAGGGGTATGAGAAAGCTCCC
TCCTACAGCTACAAGCAGTCCTTAAACATGGCTGCCGTTGGCATTACGGAGAACGTGAAG
GGAGATGCTAAGAAGTTCGAGATCTGGTACAACGCGCGCGAGGAGGTCTACATCGTCCAG
GCGCCAACTCCTGAGATTAAAGCCGCGTGGGTGAATGAAATTCGGAAAGTGCTGACCAGC
CAGCTGCAGGCTTGTAGAGAAGCCAGCCAGCACCGGGCGCTGGAGCAGTCACAGAGCCTG
CCCCTGCCGGCCCCGACCAGCACCAGTCCCTCAAGAGGAAACTCAAGGAACATCAAGAAG
CTGGAAGAAAGGAAAACAGACCCCCTAAGCCTGGAGGGATACGTCAGCTCAGCGCCACTG
ACAAAGCCCCCCGAAAAGGGCAAAGGTTGGAGCAAAACGTCCCACTCACTGGAGGCACCT
GAGGACGACGGGGGCTGGTCAAGTGCAGAGGAGCAGATTAACTCGTCCGACGCAGAGGAG
GACGGCGGGTTGGGCCCCAAGAAGCTGGTTCCAGGTAAATACACGGTCGTGGCGGACCAC
GAGAAGGGAGGCCCCGATGCGCTGCGCGTGAGGAGCGGGGACGTGGTGGAGCTGGTGCAG
GAGGGCGACGAGGGCCTCTGGTACGTCAGGGACCCGACCACTGGCAAGGAGGGCTGGGTG
CCGGCCAGCAGCCTGTCCGTCCGGCTCGGCCCGTCCGGCTCGGCCCAGTGCCTGAGCAGC
TCAGAGTCGAGCCCGGGGTCGGCCGTGCTGAGCAACTCGTCCAGCTGCAGCGAGGGCGGC
CAGGCCCCCTTCTCCGACCTGCAGGGGTAG
Enzyme 102 GenBank Gene ID NM_024979 Link Image
Enzyme 102 GeneCard ID MCF2L Link Image
Enzyme 102 GenAtlas ID MCF2L Link Image
Enzyme 102 HGNC ID HGNC:14576 Link Image
Enzyme 102 Chromosome Location 1
Enzyme 102 Locus 13q34
Enzyme 102 SNPs SNPJam Report Link Image
Enzyme 102 General References
  1. Ueda S, Kataoka T, Satoh T: Role of the Sec14-like domain of Dbl family exchange factors in the regulation of Rho family GTPases in different subcellular sites. Cell Signal. 2004 Aug;16(8):899-906. [PubMed Link Image]
  2. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
Enzyme 102 Metabolite References Not Available
Enzyme 103 [top]
Enzyme 103 ID 14222
Enzyme 103 Name Ras-related protein Rab-5A
Enzyme 103 Synonyms Not Available
Enzyme 103 Gene Name RAB5A
Enzyme 103 Protein Sequence >Ras-related protein Rab-5A
MASRGATRPNGPNTGNKICQFKLVLLGESAVGKSSLVLRFVKGQFHEFQESTIGAAFLTQ
TVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNEESFARAKNWVKELQR
QASPNIVIALSGNKADLANKRAVDFQEAQSYADDNSLLFMETSAKTSMNVNEIFMAIAKK
LPKNEPQNPGANSARGRGVDLTEPTQPTRNQCCSN
Enzyme 103 Number of Residues 215
Enzyme 103 Molecular Weight 23658.5
Enzyme 103 Theoretical pI 8.31
Enzyme 103 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 103 General Function Involved in GTP binding
Enzyme 103 Specific Function Required for the fusion of plasma membranes and early endosomes
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 20379048 Link Image
Enzyme 103 UniProtKB/Swiss-Prot ID P20339 Link Image
Enzyme 103 UniProtKB/Swiss-Prot Entry Name RAB5A_HUMAN Link Image
Enzyme 103 PDB ID 1R2Q Link Image
Enzyme 103 PDB File Show
Enzyme 103 3D Structure
Enzyme 103 Cellular Location Not Available
Enzyme 103 Gene Sequence >648 bp
ATGGCTAGTCGAGGCGCAACAAGACCCAACGGGCCAAATACGGGAAATAAAATATGCCAG
TTCAAACTAGTACTTCTGGGAGAGTCCGCTGTTGGCAAATCAAGCCTAGTGCTTCGTTTT
GTGAAAGGCCAATTTCATGAATTTCAAGAGAGTACCATTGGGGCTGCTTTTCTAACCCAA
ACTGTATGTCTTGATGACACTACAGTAAAGTTTGAAATATGGGATACAGCTGGTCAAGAA
CGATACCATAGCCTAGCACCAATGTACTACAGAGGAGCACAAGCAGCCATAGTTGTATAT
GATATCACAAATGAGGAGTCCTTTGCAAGAGCAAAAAATTGGGTTAAAGAACTTCAGAGG
CAAGCAAGTCCTAACATTGTAATAGCTTTATCGGGAAACAAGGCCGACCTAGCAAATAAA
AGAGCAGTAGATTTCCAGGAAGCACAGTCCTATGCAGATGACAATAGTTTATTATTCATG
GAGACATCCGCTAAAACATCAATGAATGTAAATGAAATATTCATGGCAATAGCTAAAAAA
TTGCCAAAGAATGAACCACAAAATCCAGGAGCAAATTCTGCCAGAGGAAGAGGAGTAGAC
CTTACCGAACCCACACAACCAACCAGGAATCAGTGTTGTAGTAACTAA
Enzyme 103 GenBank Gene ID AF498936 Link Image
Enzyme 103 GeneCard ID RAB5A Link Image
Enzyme 103 GenAtlas ID RAB5A Link Image
Enzyme 103 HGNC ID HGNC:9783 Link Image
Enzyme 103 Chromosome Location 3
Enzyme 103 Locus 3p24-p22
Enzyme 103 SNPs SNPJam Report Link Image
Enzyme 103 General References
  1. Zahraoui A, Touchot N, Chardin P, Tavitian A: The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion. J Biol Chem. 1989 Jul 25;264(21):12394-401. [PubMed Link Image]
  2. Farnsworth CC, Seabra MC, Ericsson LH, Gelb MH, Glomset JA: Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A. Proc Natl Acad Sci U S A. 1994 Dec 6;91(25):11963-7. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Callaghan J, Nixon S, Bucci C, Toh BH, Stenmark H: Direct interaction of EEA1 with Rab5b. Eur J Biochem. 1999 Oct 1;265(1):361-6. [PubMed Link Image]
  5. Hoffenberg S, Liu X, Nikolova L, Hall HS, Dai W, Baughn RE, Dickey BF, Barbieri MA, Aballay A, Stahl PD, Knoll BJ: A novel membrane-anchored Rab5 interacting protein required for homotypic endosome fusion. J Biol Chem. 2000 Aug 11;275(32):24661-9. [PubMed Link Image]
  6. Nielsen E, Christoforidis S, Uttenweiler-Joseph S, Miaczynska M, Dewitte F, Wilm M, Hoflack B, Zerial M: Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain. J Cell Biol. 2000 Oct 30;151(3):601-12. [PubMed Link Image]
  7. Tall GG, Barbieri MA, Stahl PD, Horazdovsky BF: Ras-activated endocytosis is mediated by the Rab5 guanine nucleotide exchange activity of RIN1. Dev Cell. 2001 Jul;1(1):73-82. [PubMed Link Image]
  8. Hadano S, Otomo A, Suzuki-Utsunomiya K, Kunita R, Yanagisawa Y, Showguchi-Miyata J, Mizumura H, Ikeda JE: ALS2CL, the novel protein highly homologous to the carboxy-terminal half of ALS2, binds to Rab5 and modulates endosome dynamics. FEBS Lett. 2004 Sep 24;575(1-3):64-70. [PubMed Link Image]
  9. Fouraux MA, Deneka M, Ivan V, van der Heijden A, Raymackers J, van Suylekom D, van Venrooij WJ, van der Sluijs P, Pruijn GJ: Rabip4' is an effector of rab5 and rab4 and regulates transport through early endosomes. Mol Biol Cell. 2004 Feb;15(2):611-24. Epub 2003 Nov 14. [PubMed Link Image]
  10. Eathiraj S, Pan X, Ritacco C, Lambright DG: Structural basis of family-wide Rab GTPase recognition by rabenosyn-5. Nature. 2005 Jul 21;436(7049):415-9. [PubMed Link Image]
  11. Hunker CM, Galvis A, Kruk I, Giambini H, Veisaga ML, Barbieri MA: Rab5-activating protein 6, a novel endosomal protein with a role in endocytosis. Biochem Biophys Res Commun. 2006 Feb 17;340(3):967-75. Epub 2006 Jan 4. [PubMed Link Image]
  12. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed Link Image]
  13. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  14. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  15. Zhu G, Liu J, Terzyan S, Zhai P, Li G, Zhang XC: High resolution crystal structures of human Rab5a and five mutants with substitutions in the catalytically important phosphate-binding loop. J Biol Chem. 2003 Jan 24;278(4):2452-60. Epub 2002 Nov 13. [PubMed Link Image]
  16. Zhu G, Zhai P, Liu J, Terzyan S, Li G, Zhang XC: Structural basis of Rab5-Rabaptin5 interaction in endocytosis. Nat Struct Mol Biol. 2004 Oct;11(10):975-83. Epub 2004 Sep 19. [PubMed Link Image]
Enzyme 103 Metabolite References Not Available
Enzyme 104 [top]
Enzyme 104 ID 14223
Enzyme 104 Name Ras-related protein Rab-5B
Enzyme 104 Synonyms Not Available
Enzyme 104 Gene Name RAB5B
Enzyme 104 Protein Sequence >Ras-related protein Rab-5B
MTSRSTARPNGQPQASKICQFKLVLLGESAVGKSSLVLRFVKGQFHEYQESTIGAAFLTQ
SVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNQETFARAKTWVKELQR
QASPSIVIALAGNKADLANKRMVEYEEAQAYADDNSLLFMETSAKTAMNVNDLFLAIAKK
LPKSEPQNLGGAAGRSRGVDLHEQSQQNKSQCCSN
Enzyme 104 Number of Residues 215
Enzyme 104 Molecular Weight 23706.6
Enzyme 104 Theoretical pI 8.30
Enzyme 104 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 104 General Function Involved in GTP binding
Enzyme 104 Specific Function Protein transport. Probably involved in vesicular traffic
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 20379050 Link Image
Enzyme 104 UniProtKB/Swiss-Prot ID P61020 Link Image
Enzyme 104 UniProtKB/Swiss-Prot Entry Name RAB5B_HUMAN Link Image
Enzyme 104 PDB ID 1R2Q Link Image
Enzyme 104 PDB File Show
Enzyme 104 3D Structure
Enzyme 104 Cellular Location Not Available
Enzyme 104 Gene Sequence >648 bp
ATGACTAGCAGAAGCACAGCTAGGCCCAATGGGCAACCCCAGGCCAGCAAAATTTGCCAG
TTCAAATTGGTCCTGCTGGGAGAATCTGCAGTGGGAAAGTCAAGCCTGGTATTACGTTTT
GTCAAAGGGCAGTTCCATGAGTACCAGGAGAGCACCATTGGAGCGGCCTTCCTCACCCAG
TCCGTTTGTCTAGATGACACAACAGTGAAGTTTGAGATCTGGGACACAGCTGGGCAGGAG
CGATATCACAGCTTAGCCCCCATGTACTACAGGGGTGCCCAAGCTGCAATCGTGGTTTAC
GACATTACTAATCAGGAAACCTTTGCCCGAGCAAAGACATGGGTGAAGGAACTACAGCGA
CAGGCCAGTCCTAGCATCGTTATTGCCCTGGCAGGGAACAAAGCTGACCTGGCCAACAAA
CGTATGGTGGAGTATGAAGAGGCCCAGGCATATGCAGATGACAACAGCTTATTGTTCATG
GAGACTTCAGCCAAGACAGCTATGAACGTGAATGATCTCTTCCTGGCAATAGCTAAGAAG
TTGCCAAAGAGTGAACCCCAGAATCTGGGAGGTGCAGCAGGCCGAAGCCGGGGTGTGGAT
CTCCATGAACAGTCCCAGCAGAACAAGAGCCAGTGTTGTAGCAACTGA
Enzyme 104 GenBank Gene ID AF498937 Link Image
Enzyme 104 GeneCard ID RAB5B Link Image
Enzyme 104 GenAtlas ID RAB5B Link Image
Enzyme 104 HGNC ID HGNC:9784 Link Image
Enzyme 104 Chromosome Location 1
Enzyme 104 Locus 12q13
Enzyme 104 SNPs SNPJam Report Link Image
Enzyme 104 General References
  1. Wilson DB, Wilson MP: Identification and subcellular localization of human rab5b, a new member of the ras-related superfamily of GTPases. J Clin Invest. 1992 Mar;89(3):996-1005. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Callaghan J, Nixon S, Bucci C, Toh BH, Stenmark H: Direct interaction of EEA1 with Rab5b. Eur J Biochem. 1999 Oct 1;265(1):361-6. [PubMed Link Image]
  6. Saito K, Murai J, Kajiho H, Kontani K, Kurosu H, Katada T: A novel binding protein composed of homophilic tetramer exhibits unique properties for the small GTPase Rab5. J Biol Chem. 2002 Feb 1;277(5):3412-8. Epub 2001 Dec 3. [PubMed Link Image]
  7. Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed Link Image]
Enzyme 104 Metabolite References Not Available
Enzyme 105 [top]
Enzyme 105 ID 14230
Enzyme 105 Name Ran-binding protein 3
Enzyme 105 Synonyms
  1. RanBP3
Enzyme 105 Gene Name RANBP3
Enzyme 105 Protein Sequence >Ran-binding protein 3
MADLANEEKPAIAPPVFVFQKDKGQKSPAEQKNLSDSGEEPRGEAEAPHHGTGHPESAGE
HALEPPAPAGASASTPPPPAPEAQLPPFPRELAGRSAGGSSPEGGEDSDREDGNYCPPVK
RERTSSLTQFPPSQSEERSSGFRLKPPTLIHGQAPSAGLPSQKPKEQQRSVLRPAVLQAP
QPKALSQTVPSSGTNGVSLPADCTGAVPAASPDTAAWRSPSEAADEVCALEEKEPQKNES
SNASEEEACEKKDPATQQAFVFGQNLRDRVKLINESVDEADMENAGHPSADTPTATNYFL
QYISSSLENSTNSADASSNKFVFGQNMSERVLSPPKLNEVSSDANRENAAAESGSESSSQ
EATPEKESLAESAAAYTKATARKCLLEKVEVITGEEAESNVLQMQCKLFVFDKTSQSWVE
RGRGLLRLNDMASTDDGTLQSRLVMRTQGSLRLILNTKLWAQMQIDKASEKSIRITAMDT
EDQGVKVFLISASSKDTGQLYAALHHRILALRSRVEQEQEAKMPAPEPGAAPSNEEDDSD
DDDVLAPSGATAAGAGDEGDGQTTGST
Enzyme 105 Number of Residues 567
Enzyme 105 Molecular Weight 60209.3
Enzyme 105 Theoretical pI 4.42
Enzyme 105 GO Classification
Function
Process
  • establishment of localization
  • intracellular transport
  • transport
Component
Enzyme 105 General Function Involved in intracellular transport
Enzyme 105 Specific Function Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner
Enzyme 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 6466466 Link Image
Enzyme 105 UniProtKB/Swiss-Prot ID Q9H6Z4 Link Image
Enzyme 105 UniProtKB/Swiss-Prot Entry Name RANB3_HUMAN Link Image
Enzyme 105 PDB ID Not Available
Enzyme 105 Cellular Location Not Available
Enzyme 105 Gene Sequence >1704 bp
ATGGCGGACCTGGCGAACGAAGAAAAGCCTGCCATTGCTCCGCCCGTCTTTGTGTTTCAG
AAGGATAAAGGACAAAAGTCCCCTGCAGAGCAAAAAAACTTGTCGGATTCGGGAGAGGAG
CCTCGGGGGGAGGCTGAGGCCCCCCACCATGGCACGGGTCACCCCGAGTCAGCTGGCGAG
CATGCCCTAGAACCTCCTGCCCCTGCTGGCGCCTCAGCCAGCACTCCTCCGCCTCCCGCT
CCTGAAGCCCAGCTTCCTCCTTTTCCGCGAGAACTGGCAGGGAGGTCAGCTGGCGGCTCC
AGTCCTGAAGGCGGAGAAGATTCTGACAGAGAAGATGGAAATTACTGCCCTCCTGTCAAG
CGAGAAAGAACATCCTCTTTAACCCAGTTCCCACCCTCACAGTCAGAGGAAAGGAGCAGT
GGCTTCCGGTTGAAGCCACCAACGCTGATCCACGGCCAAGCCCCCAGCGCAGGTCTGCCA
AGCCAGAAGCCCAAGGAGCAGCAGCGGAGCGTGCTTCGCCCGGCAGTGTTACAAGCTCCG
CAGCCAAAGGCGCTGTCCCAGACTGTCCCCAGCAGTGGCACCAACGGGGTCAGCCTCCCA
GCAGACTGCACGGGGGCAGTGCCCGCAGCATCCCCTGACACTGCTGCATGGAGAAGTCCT
TCCGAAGCTGCCGATGAGGTGTGTGCACTTGAGGAGAAAGAGCCCCAGAAAAATGAGTCC
AGCAATGCCTCTGAAGAGGAAGCCTGTGAGAAAAAAGACCCCGCCACACAGCAAGCCTTT
GTATTTGGGCAGAACTTGAGGGACAGAGTTAAGCTGATAAATGAGAGCGTGGACGAAGCC
GACATGGAGAATGCTGGACACCCCAGCGCAGACACGCCAACCGCAACGAACTATTTCCTC
CAGTATATCAGTTCCAGTTTAGAGAACTCAACCAATAGTGCCGACGCCTCCAGCAACAAA
TTTGTATTTGGCCAGAACATGAGCGAGCGAGTTTTGAGCCCCCCAAAATTAAACGAGGTC
AGTTCAGATGCCAACAGGGAAAATGCAGCTGCCGAGTCAGGGTCTGAGTCCTCGTCCCAG
GAGGCCACCCCTGAGAAAGAGTCCCTGGCTGAGTCGGCAGCCGCCTACACCAAGGCAACA
GCGCGGAAGTGTTTGTTGGAAAAAGTGGAAGTCATCACCGGGGAGGAGGCGGAGAGCAAT
GTGTTACAGATGCAGTGCAAGCTGTTTGTCTTTGACAAGACCTCACAGTCCTGGGTGGAG
AGAGGCCGGGGGCTGCTCAGACTCAATGACATGGCGTCCACCGATGACGGCACACTACAG
TCCCGACTAGTGATGCGGACCCAGGGGAGCCTGCGACTGATCCTCAACACCAAGCTGTGG
GCCCAGATGCAGATCGACAAGGCCAGCGAGAAGAGCATTCGCATCACAGCCATGGACACC
GAGGACCAGGGCGTGAAGGTCTTCCTGATCTCGGCCAGCTCCAAGGACACAGGTCAGTTG
TATGCAGCCCTGCACCACCGCATCCTGGCCCTGCGCAGCCGCGTGGAGCAGGAGCAGGAG
GCCAAGATGCCCGCGCCTGAGCCTGGGGCAGCCCCATCCAACGAGGAGGACGACAGCGAC
GATGACGATGTCCTGGCTCCTTCAGGGGCCACCGCAGCTGGTGCTGGTGACGAAGGGGAC
GGGCAGACGACCGGGAGCACATAG
Enzyme 105 GenBank Gene ID NM_007322.2 Link Image
Enzyme 105 GeneCard ID RANBP3 Link Image
Enzyme 105 GenAtlas ID RANBP3 Link Image
Enzyme 105 HGNC ID HGNC:9850 Link Image
Enzyme 105 Chromosome Location 1
Enzyme 105 Locus 19p13.3
Enzyme 105 SNPs SNPJam Report Link Image
Enzyme 105 General References
  1. Mueller L, Cordes VC, Bischoff FR, Ponstingl H: Human RanBP3, a group of nuclear RanGTP binding proteins. FEBS Lett. 1998 May 15;427(3):330-6. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Englmeier L, Fornerod M, Bischoff FR, Petosa C, Mattaj IW, Kutay U: RanBP3 influences interactions between CRM1 and its nuclear protein export substrates. EMBO Rep. 2001 Oct;2(10):926-32. Epub 2001 Sep 24. [PubMed Link Image]
  7. Lindsay ME, Holaska JM, Welch K, Paschal BM, Macara IG: Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export. J Cell Biol. 2001 Jun 25;153(7):1391-402. [PubMed Link Image]
  8. Nemergut ME, Lindsay ME, Brownawell AM, Macara IG: Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor. J Biol Chem. 2002 May 17;277(20):17385-8. Epub 2002 Apr 3. [PubMed Link Image]
  9. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  10. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  11. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  12. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  13. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  14. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  15. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 105 Metabolite References Not Available
Enzyme 106 [top]
Enzyme 106 ID 14256
Enzyme 106 Name Ral guanine nucleotide dissociation stimulator-like 2
Enzyme 106 Synonyms
  1. RalGDS-like 2
  2. RalGDS-like factor
  3. Ras-associated protein RAB2L
Enzyme 106 Gene Name RGL2
Enzyme 106 Protein Sequence >Ral guanine nucleotide dissociation stimulator-like 2
MLPRPLRLLLDTSPPGGVVLSSFRSRDPEEGGGPGGLVVGGGQEEEEEEEEEAPVSVWDE
EEDGAVFTVTSRQYRPLDPLVPMPPPRSSRRLRAGTLEALVRHLLDTRTSGTDVSFMSAF
LATHRAFTSTPALLGLMADRLEALESHPTDELERTTEVAISVLSTWLASHPEDFGSEAKG
QLDRLESFLLQTGYAAGKGVGGGSADLIRNLRSRVDPQAPDLPKPLALPGDPPADPTDVL
VFLADHLAEQLTLLDAELFLNLIPSQCLGGLWGHRDRPGHSHLCPSVRATVTQFNKVAGA
VVSSVLGATSTGEGPGEVTIRPLRPPQRARLLEKWIRVAEECRLLRNFSSVYAVVSALQS
SPIHRLRAAWGEATRDSLRVFSSLCQIFSEEDNYSQSRELLVQEVKLQSPLEPHSKKAPR
SGSRGGGVVPYLGTFLKDLVMLDAASKDELENGYINFDKRRKEFAVLSELRRLQNECRGY
NLQPDHDIQRWLQGLRPLTEAQSHRVSCEVEPPGSSDPPAPRVLRPTLVISQWTEVLGSV
GVPTPLVSCDRPSTGGDEAPTTPAPLLTRLAQHMKWPSVSSLDSALESSPSLHSPADPSH
LSPPASSPRPSRGHRRSASCGSPLSGGAEEASGGTGYGGEGSGPGASDCRIIRVQMELGE
DGSVYKSILVTSQDKAPSVISRVLKKNNRDSAVASEYELVQLLPGERELTIPASANVFYA
MDGASHDFLLRQRRRSSTATPGVTSGPSASGTPPSEGGGGSFPRIKATGRKIARALF
Enzyme 106 Number of Residues 777
Enzyme 106 Molecular Weight 83548.1
Enzyme 106 Theoretical pI 6.09
Enzyme 106 GO Classification
Function
  • GTPase regulator activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 106 General Function Involved in signal transduction
Enzyme 106 Specific Function Probable guanine nucleotide exchange factor. Putative effector of Ras and/or Rap. Associates with the GTP-bound form of Rap 1A and H-Ras in vitro
Enzyme 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 4886477 Link Image
Enzyme 106 UniProtKB/Swiss-Prot ID O15211 Link Image
Enzyme 106 UniProtKB/Swiss-Prot Entry Name RGL2_HUMAN Link Image
Enzyme 106 PDB ID 1RLF Link Image
Enzyme 106 PDB File Show
Enzyme 106 3D Structure
Enzyme 106 Cellular Location Not Available
Enzyme 106 Gene Sequence >2334 bp
ATGCTCCCGCGGCCCCTGCGGCTGCTTTTGGACACGAGCCCCCCCGGGGGAGTCGTACTG
AGCAGCTTCCGAAGCCGGGACCCCGAAGAGGGTGGGGGCCCAGGTGGCCTGGTCGTGGGC
GGGGGGCAGGAGGAAGAGGAGGAGGAAGAAGAAGAGGCCCCTGTGTCCGTCTGGGATGAG
GAGGAGGATGGTGCCGTGTTTACCGTCACAAGCCGCCAATATCGACCTCTTGATCCCTTG
GTCCCTATGCCTCCCCCACGTTCCTCCCGACGGCTCCGAGCTGGCACTCTGGAGGCCCTG
GTCAGACACCTACTGGATACCCGGACATCAGGGACTGATGTGAGCTTCATGTCAGCCTTC
CTGGCTACCCACCGGGCCTTCACCTCCACGCCTGCCTTGCTAGGGCTTATGGCTGACAGG
CTGGAAGCCCTTGAATCTCATCCTACCGACGAACTAGAGAGGACAACAGAGGTAGCCATC
TCTGTACTGTCAACCTGGCTGGCCTCTCACCCTGAGGATTTTGGCTCTGAGGCCAAGGGT
CAGCTTGACCGGCTTGAGAGCTTCTTACTTCAGACAGGGTATGCAGCAGGGAAGGGTGTT
GGGGGGGGCAGCGCTGACCTCATCCGCAATCTCCGGTCCCGGGTGGACCCCCAGGCCCCC
GACCTTCCTAAGCCCCTGGCCCTCCCCGGCGATCCCCCTGCTGACCCCACGGATGTCCTG
GTGTTCCTCGCTGACCACTTGGCCGAACAGCTGACCCTGCTAGATGCGGAACTTTTTCTC
AATTTGATCCCCTCTCAGTGCCTGGGAGGCCTGTGGGGTCACAGAGACCGGCCAGGACAT
TCTCACCTCTGCCCATCTGTCCGAGCTACTGTCACACAGTTTAACAAGGTGGCAGGGGCA
GTGGTTAGTTCTGTCCTGGGGGCTACTTCCACTGGAGAGGGACCTGGGGAGGTGACCATA
CGGCCACTCCGTCCCCCACAGAGGGCCCGGCTCCTGGAGAAGTGGATCCGCGTGGCAGAG
GAGTGCCGGCTGCTCCGAAACTTCTCTTCAGTTTATGCCGTGGTGTCAGCCCTGCAGTCC
AGCCCCATCCACAGGCTTCGGGCAGCCTGGGGGGAAGCAACCAGGGACAGCCTCAGAGTC
TTTTCCAGCCTCTGCCAGATTTTCTCCGAGGAGGATAATTATTCCCAGAGTCGGGAGCTG
CTCGTGCAGGAGGTGAAGCTGCAGTCTCCTCTGGAGCCACACTCCAAGAAGGCCCCGAGG
TCTGGCTCCCGGGGTGGGGGTGTGGTCCCATACCTTGGCACCTTCCTGAAGGACCTTGTG
ATGCTGGATGCAGCCTCCAAGGATGAGTTGGAGAATGGATACATCAATTTTGACAAGCGG
AGGAAGGAGTTTGCAGTCCTTTCTGAGTTGCGACGGCTCCAGAATGAATGTCGTGGCTAT
AACCTCCAACCTGACCATGATATCCAGAGGTGGCTACAGGGGCTCCGGCCACTGACAGAG
GCTCAGAGCCATCGTGTATCCTGTGAGGTGGAGCCACCTGGTTCCAGTGACCCTCCTGCC
CCACGGGTGCTTCGGCCAACATTGGTCATCTCGCAGTGGACAGAGGTTTTGGGCTCTGTT
GGGGTCCCTACCCCGCTTGTGTCCTGTGACCGGCCCAGTACTGGGGGAGATGAGGCGCCT
ACAACTCCTGCTCCTCTGCTGACTCGGCTGGCCCAGCACATGAAGTGGCCATCTGTCTCG
TCACTAGACTCTGCCTTGGAAAGCAGTCCATCCCTGCACAGTCCAGCTGACCCCAGCCAC
CTCTCCCCACCAGCCTCCTCCCCTAGGCCTTCTCGAGGTCACCGCCGCTCAGCCTCCTGT
GGCTCCCCGCTGAGTGGGGGTGCAGAAGAGGCCTCCGGGGGGACTGGATATGGGGGAGAG
GGATCTGGGCCAGGGGCCTCTGATTGCCGTATCATCCGAGTCCAGATGGAGTTGGGGGAA
GATGGCAGTGTCTATAAGAGCATTTTGGTGACAAGCCAGGACAAGGCTCCAAGTGTCATC
AGTCGTGTCCTTAAGAAAAACAATCGTGACTCTGCAGTGGCTTCAGAGTATGAGCTGGTA
CAGCTGCTACCAGGGGAGCGAGAGCTGACTATCCCAGCCTCGGCTAATGTATTCTACGCC
ATGGATGGAGCTTCACACGATTTCCTCCTGCGGCAGCGGCGAAGGTCCTCTACTGCTACA
CCTGGCGTCACCAGTGGCCCGTCTGCCTCAGGAACTCCTCCGAGTGAGGGAGGAGGGGGC
TCCTTTCCCAGGATCAAGGCCACAGGGAGGAAGATTGCACGGGCACTGTTCTGA
Enzyme 106 GenBank Gene ID AL050259 Link Image
Enzyme 106 GeneCard ID RGL2 Link Image
Enzyme 106 GenAtlas ID RGL2 Link Image
Enzyme 106 HGNC ID HGNC:9769 Link Image
Enzyme 106 Chromosome Location 6
Enzyme 106 Locus 6p21.3
Enzyme 106 SNPs SNPJam Report Link Image
Enzyme 106 General References
  1. Herberg JA, Beck S, Trowsdale J: TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form a dense cluster at the centromeric end of the MHC. J Mol Biol. 1998 Apr 10;277(4):839-57. [PubMed Link Image]
  2. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Isomura M, Okui K, Fujiwara T, Shin S, Nakamura Y: Isolation and mapping of RAB2L, a human cDNA that encodes a protein homologous to RalGDS. Cytogenet Cell Genet. 1996;74(4):263-5. [PubMed Link Image]
  6. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
Enzyme 106 Metabolite References Not Available
Enzyme 107 [top]
Enzyme 107 ID 14257
Enzyme 107 Name Ral guanine nucleotide dissociation stimulator-like 3
Enzyme 107 Synonyms
  1. RalGDS-like 3
Enzyme 107 Gene Name RGL3
Enzyme 107 Protein Sequence >Ral guanine nucleotide dissociation stimulator-like 3
MERTAGKELALAPLQDWGEETEDGAVYSVSLRRQRSQRRSPAEGPGGSQAPSPIANTFLH
YRTSKVRVLRAARLERLVGELVFGDREQDPSFMPAFLATYRTFVPTACLLGFLLPPMPPP
PPPGVEIKKTAVQDLSFNKNLRAVVSVLGSWLQDHPQDFRDPPAHSDLGSVRTFLGWAAP
GSAEAQKAEKLLEDFLEEAEREQEEEPPQVWTGPPRVAQTSDPDSSEACAEEEEGLMPQG
PQLLDFSVDEVAEQLTLIDLELFSKVRLYECLGSVWSQRDRPGAAGASPTVRATVAQFNT
VTGCVLGSVLGAPGLAAPQRAQRLEKWIRIAQRCRELRNFSSLRAILSALQSNPIYRLKR
SWGAVSREPLSTFRKLSQIFSDENNHLSSREILFQEEATEGSQEEDNTPGSLPSKPPPGP
VPYLGTFLTDLVMLDTALPDMLEGDLINFEKRRKEWEILARIQQLQRRCQSYTLSPHPPI
LAALHAQNQLTEEQSYRLSRVIEPPAASCPSSPRIRRRISLTKRLSAKLAREKSSSPSGS
PGDPSSPTSSVSPGSPPSSPRSRDAPAGSPPASPGPQGPSTKLPLSLDLPSPRPFALPLG
SPRIPLPAQQSSEARVIRVSIDNDHGNLYRSILLTSQDKAPSVVRRALQKHNVPQPWACD
YQLFQVLPGDRVLLIPDNANVFYAMSPVAPRDFMLRRKEGTRNTLSVSPS
Enzyme 107 Number of Residues 710
Enzyme 107 Molecular Weight 78078.5
Enzyme 107 Theoretical pI 7.76
Enzyme 107 GO Classification
Function
  • GTPase regulator activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 107 General Function Involved in signal transduction
Enzyme 107 Specific Function Guanine nucleotide exchange factor (GEF) for Ral-A. Potential effector of GTPase HRas and Ras-related protein M-Ras. Negatively regulates Elk-1-dependent gene induction downstream of HRas and MEKK1
Enzyme 107 Pathways Not Available
Enzyme 107 Reactions Not Available
Enzyme 107 Pfam Domain Function
Enzyme 107 Signals
  • None
Enzyme 107 Transmembrane Regions
  • None
Enzyme 107 Essentiality Not Available
Enzyme 107 GenBank ID Protein 239582763 Link Image
Enzyme 107 UniProtKB/Swiss-Prot ID Q3MIN7 Link Image
Enzyme 107 UniProtKB/Swiss-Prot Entry Name RGL3_HUMAN Link Image
Enzyme 107 PDB ID Not Available
Enzyme 107 Cellular Location Not Available
Enzyme 107 Gene Sequence >2133 bp
ATGGAGCGCACAGCAGGCAAAGAGCTGGCCCTGGCACCGCTGCAGGACTGGGGTGAAGAG
ACCGAGGACGGCGCGGTGTACAGTGTCTCCCTGCGGCGGCAGCGCAGTCAGCGCAGGAGC
CCGGCGGAGGGCCCCGGGGGCAGCCAGGCTCCCAGCCCCATTGCCAATACCTTCCTCCAC
TATCGAACCAGCAAGGTGAGGGTGCTGAGGGCAGCGCGCCTGGAGCGGCTGGTGGGAGAG
TTGGTGTTTGGAGACCGTGAGCAGGACCCCAGCTTCATGCCCGCCTTCCTGGCCACCTAC
CGGACCTTTGTACCCACTGCCTGCCTGCTGGGCTTTCTGCTGCCACCAATGCCACCGCCC
CCACCTCCCGGGGTAGAGATCAAGAAGACAGCGGTACAAGATCTGAGCTTCAACAAGAAC
CTGAGGGCTGTGGTGTCAGTGCTGGGCTCCTGGCTGCAGGACCACCCTCAGGATTTCCGA
GACCCCCCTGCCCATTCGGACCTGGGCAGTGTCCGAACCTTTCTGGGCTGGGCGGCCCCA
GGGAGTGCTGAGGCTCAAAAAGCAGAGAAGCTTCTGGAAGATTTTTTGGAGGAGGCTGAG
CGAGAGCAGGAAGAGGAGCCGCCTCAGGTGTGGACAGGACCTCCCAGAGTTGCCCAAACT
TCTGACCCAGACTCTTCAGAGGCCTGCGCGGAGGAAGAGGAAGGGCTCATGCCTCAAGGT
CCCCAGCTCCTGGACTTCAGCGTGGACGAGGTGGCCGAGCAGCTGACCCTCATAGACTTG
GAGCTCTTCTCCAAGGTGAGGCTCTACGAGTGCTTGGGCTCCGTGTGGTCGCAGAGGGAC
CGGCCGGGGGCTGCAGGCGCCTCCCCCACTGTGCGCGCCACCGTGGCCCAGTTCAACACC
GTGACCGGCTGTGTGCTGGGTTCCGTGCTCGGAGCACCGGGCTTGGCCGCCCCGCAGAGG
GCGCAGCGGCTGGAGAAGTGGATCCGCATCGCCCAGCGCTGCCGAGAACTGCGGAACTTC
TCCTCCTTGCGCGCCATCCTGTCCGCCCTGCAATCTAACCCCATCTACCGGCTCAAGCGC
AGCTGGGGGGCAGTGAGCCGGGAACCGCTATCTACTTTCAGGAAACTTTCGCAGATTTTC
TCCGATGAGAACAACCACCTCAGCAGCAGAGAGATTCTTTTCCAGGAGGAGGCCACTGAG
GGATCCCAAGAAGAGGACAACACCCCAGGCAGCCTGCCCTCAAAACCACCCCCAGGCCCT
GTCCCCTACCTTGGCACCTTCCTTACGGACCTGGTTATGCTGGACACAGCCCTGCCGGAT
ATGTTGGAGGGGGATCTCATTAACTTTGAGAAGAGGAGGAAGGAGTGGGAGATCCTGGCC
CGCATCCAGCAGCTGCAGAGGCGCTGTCAGAGCTACACCCTGAGCCCCCACCCGCCCATC
CTGGCTGCCCTGCATGCCCAGAACCAGCTCACCGAGGAGCAGAGCTACCGGCTCTCCCGG
GTCATTGAGCCACCAGCTGCCTCCTGCCCCAGCTCCCCACGCATCCGACGGCGGATCAGC
CTCACCAAGCGTCTCAGTGCGAAGCTTGCCCGAGAGAAAAGCTCATCACCTAGTGGGAGT
CCCGGGGACCCCTCATCCCCCACCTCCAGTGTGTCCCCAGGGTCACCCCCCTCAAGTCCT
AGAAGCAGAGATGCTCCTGCTGGCAGTCCCCCGGCCTCTCCAGGGCCCCAGGGCCCCAGC
ACCAAGCTGCCCCTGAGCCTGGACCTGCCCAGCCCCCGGCCCTTCGCTTTGCCTCTGGGC
AGCCCTCGAATCCCCCTCCCGGCGCAGCAGAGCTCGGAGGCCCGTGTCATCCGCGTCAGC
ATCGACAATGACCACGGGAACCTGTATCGAAGCATCTTGCTGACCAGTCAGGACAAAGCC
CCCAGCGTGGTCCGGCGAGCCTTGCAGAAGCACAATGTGCCCCAGCCCTGGGCCTGTGAC
TATCAGCTCTTTCAAGTCCTTCCTGGGGACCGGGTGCTCCTGATTCCTGACAATGCCAAC
GTCTTCTATGCCATGAGTCCAGTCGCCCCCAGAGACTTCATGCTGCGGCGGAAAGAGGGG
ACCCGGAACACTCTGTCTGTCTCCCCAAGCTGA
Enzyme 107 GenBank Gene ID NM_001035223.2 Link Image
Enzyme 107 GeneCard ID RGL3 Link Image
Enzyme 107 GenAtlas ID RGL3 Link Image
Enzyme 107 HGNC ID HGNC:30282 Link Image
Enzyme 107 Chromosome Location 1
Enzyme 107 Locus 19p13.2
Enzyme 107 SNPs SNPJam Report Link Image
Enzyme 107 General References
  1. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 107 Metabolite References Not Available
Enzyme 108 [top]
Enzyme 108 ID 14268
Enzyme 108 Name Synembryn-A
Enzyme 108 Synonyms
  1. Protein Ric-8A
Enzyme 108 Gene Name RIC8A
Enzyme 108 Protein Sequence >Synembryn-A
MEPRAVAEAVETGEEDVIMEALRSYNQEHSQSFTFDDAQQEDRKRLAELLVSVLEQGLPP
SHRVIWLQSVRILSRDRNCLDPFTSRQSLQALACYADISVSEGSVPESADMDVVLESLKC
LCNLVLSSPVAQMLAAEARLVVKLTERVGLYRERSFPHDVQFFDLRLLFLLTALRTDVRQ
QLFQELKGVRLLTDTLELTLGVTPEGNPPPTLLPSQETERAMEILKVLFNITLDSIKGEV
DEEDAALYRHLGTLLRHCVMIATAGDRTEEFHGHAVNLLGNLPLKCLDVLLTLEPHGDST
EFMGVNMDVIRALLIFLEKRLHKTHRLKESVAPVLSVLTECARMHRPARKFLKAQVLPPL
RDVRTRPEVGEMLRNKLVRLMTHLDTDVKRVAAEFLFVLCSESVPRFIKYTGYGNAAGLL
AARGLMAGGRPEGQYSEDEDTDTDEYKEAKASINPVTGRVEEKPPNPMEGMTEEQKEHEA
MKLVTMFDKLSRNRVIQPMGMSPRGHLTSLQDAMCETMEQQLSSDPDSDPD
Enzyme 108 Number of Residues 531
Enzyme 108 Molecular Weight 59708.9
Enzyme 108 Theoretical pI 4.98
Enzyme 108 GO Classification Not Available
Enzyme 108 General Function Involved in binding
Enzyme 108 Specific Function Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein, possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex. Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation
Enzyme 108 Pathways Not Available
Enzyme 108 Reactions Not Available
Enzyme 108 Pfam Domain Function
Enzyme 108 Signals
  • None
Enzyme 108 Transmembrane Regions
  • None
Enzyme 108 Essentiality Not Available
Enzyme 108 GenBank ID Protein 9368538 Link Image
Enzyme 108 UniProtKB/Swiss-Prot ID Q9NPQ8 Link Image
Enzyme 108 UniProtKB/Swiss-Prot Entry Name RIC8A_HUMAN Link Image
Enzyme 108 PDB ID Not Available
Enzyme 108 Cellular Location Not Available
Enzyme 108 Gene Sequence >1596 bp
ATGGAGCCCCGGGCGGTTGCAGAAGCCGTGGAGACGGGTGAGGAGGATGTGATTATGGAA
GCTCTGCGGTCATACAACCAGGAGCACTCCCAGAGCTTCACGTTTGATGATGCCCAACAG
GAGGACCGGAAGAGACTGGCGGAGCTGCTGGTCTCCGTCCTGGAACAGGGCTTGCCACCC
TCCCACCGTGTCATCTGGCTGCAGAGTGTCCGAATCCTGTCCCGGGACCGCAACTGCCTG
GACCCGTTCACCAGCCGCCAGAGCCTGCAGGCACTAGCCTGCTATGCTGACATCTCTGTC
TCTGAGGGGTCCGTCCCAGAGTCCGCAGACATGGATGTTGTACTGGAGTCCCTCAAGTGC
CTGTGCAACCTCGTGCTCAGCAGCCCTGTGGCACAGATGCTGGCAGCAGAGGCCCGCCTA
GTGGTGAAGCTCACAGAGCGTGTGGGGCTGTACCGTGAGAGGAGCTTCCCCCACGATGTC
CAGTTCTTTGACTTGCGGCTCCTCTTCCTGCTAACGGCACTCCGCACCGATGTGCGCCAG
CAGCTGTTTCAGGAGCTGAAAGGAGTGCGCCTGCTAACTGACACACTGGAGCTGACGCTG
GGGGTGACTCCTGAAGGGAACCCCCCACCCACGCTCCTTCCTTCCCAAGAGACTGAGCGG
GCCATGGAGATCCTCAAAGTGCTCTTCAACATCACCCTGGACTCCATCAAGGGGGAGGTG
GACGAGGAAGACGCTGCCCTTTACCGACACCTGGGGACCCTTCTCCGGCACTGTGTGATG
ATCGCTACTGCTGGAGACCGCACAGAGGAGTTCCACGGCCACGCAGTGAACCTCCTGGGG
AACTTGCCCCTCAAGTGTCTGGATGTTCTCCTCACCCTGGAGCCACATGGAGACTCCACG
GAGTTCATGGGAGTGAATATGGATGTGATTCGTGCCCTCCTCATCTTCCTAGAGAAGCGT
TTGCACAAGACACACAGGCTGAAGGAGAGTGTAGCTCCCGTGCTGAGCGTGCTGACTGAA
TGTGCCCGGATGCACCGCCCAGCCAGGAAGTTCCTGAAGGCCCAGGTGCTGCCCCCTCTG
CGGGATGTGAGGACACGGCCTGAGGTTGGGGAGATGCTGCGGAACAAGCTTGTCCGCCTC
ATGACACACCTGGACACAGATGTGAAGAGGGTGGCTGCCGAGTTCTTGTTTGTCCTGTGC
TCTGAGAGTGTGCCCCGATTCATCAAGTACACAGGCTATGGGAATGCTGCTGGCCTTCTG
GCTGCCAGGGGCCTCATGGCAGGAGGCCGGCCCGAGGGCCAGTACTCAGAGGATGAGGAC
ACAGACACAGATGAGTACAAGGAAGCCAAAGCCAGCATAAACCCTGTGACCGGGAGGGTG
GAGGAGAAGCCGCCTAACCCTATGGAGGGCATGACAGAGGAGCAGAAGGAGCACGAGGCC
ATGAAGCTGGTGACCATGTTTGACAAGCTCTCCAGGAACAGAGTCATCCAGCCAATGGGG
ATGAGTCCCCGGGGTCATCTTACGTCCCTGCAGGATGCCATGTGCGAGACTATGGAGCAG
CAGCTCTCCTCGGACCCTGACTCGGACCCTGACTGA
Enzyme 108 GenBank Gene ID AL390088 Link Image
Enzyme 108 GeneCard ID RIC8A Link Image
Enzyme 108 GenAtlas ID RIC8A Link Image
Enzyme 108 HGNC ID HGNC:29550 Link Image
Enzyme 108 Chromosome Location 1
Enzyme 108 Locus 11p15.5
Enzyme 108 SNPs SNPJam Report Link Image
Enzyme 108 General References
  1. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Nishimura A, Okamoto M, Sugawara Y, Mizuno N, Yamauchi J, Itoh H: Ric-8A potentiates Gq-mediated signal transduction by acting downstream of G protein-coupled receptor in intact cells. Genes Cells. 2006 May;11(5):487-98. [PubMed Link Image]
  7. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  8. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  9. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  10. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed Link Image]
  11. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  12. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 108 Metabolite References Not Available
Enzyme 109 [top]
Enzyme 109 ID 14270
Enzyme 109 Name Ras and Rab interactor 1
Enzyme 109 Synonyms
  1. Ras inhibitor JC99
  2. Ras interaction/interference protein 1
Enzyme 109 Gene Name RIN1
Enzyme 109 Protein Sequence >Ras and Rab interactor 1
MESPGESGAGSPGAPSPSSFTTGHLAREKPAQDPLYDVPNASGGQAGGPQRPGRVVSLRE
RLLLTRPVWLQLQANAAAALHMLRTEPPGTFLVRKSNTRQCQALCMRLPEASGPSFVSSH
YILESPGGVSLEGSELMFPDLVQLICAYCHTRDILLLPLQLPRAIHHAATHKELEAISHL
GIEFWSSSLNIKAQRGPAGGPVLPQLKARSPQELDQGTGAALCFFNPLFPGDLGPTKREK
FKRSFKVRVSTETSSPLSPPAVPPPPVPVLPGAVPSQTERLPPCQLLRRESSVGYRVPAG
SGPSLPPMPSLQEVDCGSPSSSEEEGVPGSRGSPATSPHLGRRRPLLRSMSAAFCSLLAP
ERQVGRAAAALMQDRHTAAGQLVQDLLTQVRAGPEPQELQGIRQALSRARAMLSAELGPE
KLLSPKRLEHVLEKSLHCSVLKPLRPILAARLRRRLAADGSLGRLAEGLRLARAQGPGAF
GSHLSLPSPVELEQVRQKLLQLLRTYSPSAQVKRLLQACKLLYMALRTQEGEGAGADEFL
PLLSLVLAHCDLPELLLEAEYMSELLEPSLLTGEGGYYLTSLSASLALLSGLGQAHTLPL
SPVQELRRSLSLWEQRRLPATHCFQHLLRVAYQDPSSGCTSKTLAVPPEASIATLNQLCA
TKFRVTQPNTFGLFLYKEQGYHRLPPGALAHRLPTTGYLVYRRAEWPETQGAVTEEEGSG
QSEARSRGEEQGCQGDGDAGVKASPRDIREQSETTAEGGQGQAQEGPAQPGEPEAEGSRA
AEE
Enzyme 109 Number of Residues 783
Enzyme 109 Molecular Weight 84098.0
Enzyme 109 Theoretical pI 8.08
Enzyme 109 GO Classification
Function
  • binding
  • protein binding
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 109 General Function Involved in signal transduction
Enzyme 109 Specific Function Ras effector protein, which may serve as an inhibitory modulator of neuronal plasticity in aversive memory formation. Can affect Ras signaling at different levels. First, by competing with RAF1 protein for binding to activated Ras. Second, by enhancing signaling from ABL1 and ABL2, which regulate cytoskeletal remodeling. Third, by activating RAB5A, possibly by functioning as a guanine nucleotide exchange factor (GEF) for RAB5A, by exchanging bound GDP for free GTP, and facilitating Ras-activated receptor endocytosis
Enzyme 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 15680148 Link Image
Enzyme 109 UniProtKB/Swiss-Prot ID Q13671 Link Image
Enzyme 109 UniProtKB/Swiss-Prot Entry Name RIN1_HUMAN Link Image
Enzyme 109 PDB ID Not Available
Enzyme 109 Cellular Location Not Available
Enzyme 109 Gene Sequence >2352 bp
ATGGAAAGCCCTGGAGAGTCAGGCGCGGGCTCTCCTGGAGCCCCCAGCCCGTCCAGCTTC
ACTACTGGGCACCTGGCGAGAGAAAAGCCAGCCCAGGACCCACTGTATGACGTGCCCAAT
GCCAGCGGCGGGCAGGCAGGCGGGCCGCAGCGGCCGGGGCGCGTTGTGAGCCTGCGGGAG
CGCCTGCTGCTCACCCGGCCCGTGTGGCTGCAGCTGCAAGCCAACGCAGCGGCCGCACTG
CACATGCTGAGGACCGAGCCCCCGGGGACGTTCCTCGTGCGGAAATCTAACACCCGCCAG
TGCCAGGCCCTGTGCATGCGGTTGCCTGAAGCCAGTGGCCCCTCCTTCGTCTCCAGCCAC
TACATCCTGGAGAGCCCTGGCGGCGTCTCCTTGGAGGGCTCGGAGCTCATGTTCCCAGAC
CTAGTCCAGCTCATCTGTGCCTACTGCCACACCCGGGACATCCTTCTCCTCCCGCTGCAG
CTCCCCAGAGCCATCCACCACGCAGCCACTCACAAAGAGCTGGAGGCCATCTCCCATCTG
GGCATTGAGTTCTGGAGCTCCTCCCTCAACATCAAGGCTCAGCGGGGCCCGGCTGGAGGC
CCAGTGTTGCCCCAGCTGAAGGCCCGGTCCCCTCAAGAGCTGGACCAGGGCACCGGAGCC
GCCTTGTGCTTCTTCAACCCCCTGTTCCCGGGGGACCTAGGGCCCACCAAGCGGGAGAAA
TTCAAGAGAAGCTTCAAAGTGCGCGTGTCCACAGAGACCTCCAGCCCCCTGTCTCCACCT
GCCGTGCCACCTCCCCCCGTCCCCGTGCTGCCAGGGGCAGTCCCCAGCCAGACAGAGCGG
CTGCCCCCTTGCCAGCTGCTACGGAGGGAGAGCTCAGTGGGGTACCGCGTGCCAGCAGGC
AGTGGCCCTAGCCTTCCGCCTATGCCCTCCCTCCAAGAGGTGGACTGCGGCTCCCCCAGC
AGCTCCGAGGAGGAGGGGGTGCCAGGGTCCCGGGGGAGCCCAGCGACCTCACCCCACCTG
GGCCGCCGACGACCTCTGCTTCGGTCCATGAGCGCCGCCTTCTGCTCCCTACTGGCACCG
GAGCGGCAGGTGGGCCGGGCTGCGGCAGCACTGATGCAGGACCGACACACAGCCGCGGGC
CAGCTGGTGCAGGACCTACTGACCCAGGTGCGGGCTGGGCCCGAGCCCCAGGAGCTGCAG
GGCATCCGTCAGGCGCTGAGCCGGGCCCGGGCCATGCTGAGTGCGGAGCTGGGCCCTGAG
AAGCTGCTGTCGCCTAAGAGGCTGGAACATGTCCTGGAGAAGTCATTGCATTGCTCTGTG
CTCAAGCCTCTCCGGCCCATCCTGGCAGCCCGCCTGCGGCGCCGGCTTGCCGCAGACGGC
TCCCTGGGCCGCCTAGCTGAGGGCCTCCGCCTGGCCCGGGCCCAGGGCCCCGGAGCCTTC
GGGTCCCACCTGAGCCTGCCCTCCCCAGTAGAGTTGGAGCAAGTGCGCCAGAAGCTGCTG
CAGCTGCTCCGCACCTACTCACCCAGCGCCCAGGTCAAGCGGCTCCTGCAGGCCTGCAAG
CTGCTCTACATGGCCCTGAGGACCCAGGAAGGGGAGGGCGCGGGTGCCGACGAGTTCCTG
CCTCTGCTGAGCCTCGTCTTGGCCCACTGTGACCTTCCTGAGCTGCTGCTGGAGGCCGAG
TACATGTCGGAGCTGCTGGAGCCCAGCCTGCTTACTGGAGAGGGTGGCTACTACCTGACC
AGCCTCTCTGCCAGCCTGGCCCTGCTGAGTGGCCTGGGTCAGGCCCACACCCTCCCACTG
AGCCCCGTGCAGGAGCTACGGCGCTCCCTCAGCCTCTGGGAGCAGCGCCGCCTGCCTGCC
ACCCACTGCTTCCAGCACCTCCTCCGAGTAGCCTATCAGGATCCCAGCAGTGGCTGCACC
TCCAAGACCCTGGCCGTGCCCCCAGAGGCCTCGATTGCCACCCTGAACCAGCTCTGTGCC
ACCAAGTTCCGAGTGACCCAGCCCAACACTTTTGGCCTCTTCCTGTACAAGGAGCAGGGC
TACCACCGCCTGCCCCCTGGGGCCCTGGCCCACAGGCTGCCCACCACTGGCTACCTCGTC
TACCGCCGGGCAGAGTGGCCTGAGACCCAGGGGGCTGTGACAGAGGAGGAGGGCAGTGGG
CAGTCAGAGGCAAGAAGCAGAGGGGAGGAGCAAGGGTGCCAGGGAGATGGGGATGCTGGG
GTCAAAGCCAGCCCCAGGGACATTCGGGAACAGTCTGAGACAACTGCTGAAGGGGGCCAG
GGTCAAGCCCAGGAAGGCCCTGCTCAGCCAGGGGAACCAGAGGCAGAGGGAAGCCGGGCA
GCAGAGGAGTAG
Enzyme 109 GenBank Gene ID BC014417 Link Image
Enzyme 109 GeneCard ID RIN1 Link Image
Enzyme 109 GenAtlas ID RIN1 Link Image
Enzyme 109 HGNC ID HGNC:18749 Link Image
Enzyme 109 Chromosome Location 1
Enzyme 109 Locus 11q13.2
Enzyme 109 SNPs SNPJam Report Link Image
Enzyme 109 General References
  1. Colicelli J, Nicolette C, Birchmeier C, Rodgers L, Riggs M, Wigler M: Expression of three mammalian cDNAs that interfere with RAS function in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2913-7. [PubMed Link Image]
  2. Han L, Colicelli J: A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1. Mol Cell Biol. 1995 Mar;15(3):1318-23. [PubMed Link Image]
  3. Han L, Wong D, Dhaka A, Afar D, White M, Xie W, Herschman H, Witte O, Colicelli J: Protein binding and signaling properties of RIN1 suggest a unique effector function. Proc Natl Acad Sci U S A. 1997 May 13;94(10):4954-9. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Afar DE, Han L, McLaughlin J, Wong S, Dhaka A, Parmar K, Rosenberg N, Witte ON, Colicelli J: Regulation of the oncogenic activity of BCR-ABL by a tightly bound substrate protein RIN1. Immunity. 1997 Jun;6(6):773-82. [PubMed Link Image]
  6. Tall GG, Barbieri MA, Stahl PD, Horazdovsky BF: Ras-activated endocytosis is mediated by the Rab5 guanine nucleotide exchange activity of RIN1. Dev Cell. 2001 Jul;1(1):73-82. [PubMed Link Image]
  7. Wang Y, Waldron RT, Dhaka A, Patel A, Riley MM, Rozengurt E, Colicelli J: The RAS effector RIN1 directly competes with RAF and is regulated by 14-3-3 proteins. Mol Cell Biol. 2002 Feb;22(3):916-26. [PubMed Link Image]
  8. Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM: Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics. 2005 Sep;4(9):1240-50. Epub 2005 Jun 11. [PubMed Link Image]
  9. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed Link Image]
  10. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  11. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  12. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  13. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
Enzyme 109 Metabolite References Not Available
Enzyme 110 [top]
Enzyme 110 ID 14271
Enzyme 110 Name Ras and Rab interactor 2
Enzyme 110 Synonyms
  1. Ras association domain family 4
  2. Ras inhibitor JC265
  3. Ras interaction/interference protein 2
Enzyme 110 Gene Name RIN2
Enzyme 110 Protein Sequence >Ras and Rab interactor 2
MTAWTMGARGLDKRGSFFKLIDTIASEIGELKQEMVRTDVNLENGLEPAETHSMVRHKDG
GYSEEEDVKTCARDSGYDSLSNRLSILDRLLHTHPIWLQLSLSEEEAAEVLQAQPPGIFL
VHKSTKMQKKVLSLRLPCEFGAPLKEFAIKESTYTFSLEGSGISFADLFRLIAFYCISRD
VLPFTLKLPYAISTAKSEAQLEELAQMGLNFWSSPADSKPPNLPPPHRPLSSDGVCPASL
RQLCLINGVHSIKTRTPSELECSQTNGALCFINPLFLKVHSQDLSGGLKRPSTRTPNANG
TERTRSPPPRPPPPAINSLHTSPRLARTETQTSMPETVNHNKHGNVALPGTKPTPIPPPR
LKKQASFLEAEGGAKTLSGGRPGAGPELELGTAGSPGGAPPEAAPGDCTRAPPPSSESRP
PCHGGRQRLSDMSISTSSSDSLEFDRSMPLFGYEADTNSSLEDYEGESDQETMAPPIKSK
KKRSSSFVLPKLVKSQLQKVSGVFSSFMTPEKRMVRRIAELSRDKCTYFGCLVQDYVSFL
QENKECHVSSTDMLQTIRQFMTQVKNYLSQSSELDPPIESLIPEDQIDVVLEKAMHKCIL
KPLKGHVEAMLKDFHMADGSWKQLKENLQLVRQRNPQELGVFAPTPDFVDVEKIKVKFMT
MQKMYSPEKKVMLLLRVCKLIYTVMENNSGRMYGADDFLPVLTYVIAQCDMLELDTEIEY
MMELLDPSLLHGEGGYYLTSAYGALSLIKNFQEEQAARLLSSETRDTLRQWHKRRTTNRT
IPSVDDFQNYLRVAFQEVNSGCTGKTLLVRPYITTEDVCQICAEKFKVGDPEEYSLFLFV
DETWQQLAEDTYPQKIKAELHSRPQPHIFHFVYKRIKNDPYGIIFQNGEEDLTTS
Enzyme 110 Number of Residues 895
Enzyme 110 Molecular Weight 100162.3
Enzyme 110 Theoretical pI 6.55
Enzyme 110 GO Classification
Function
  • binding
  • protein binding
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 110 General Function Involved in signal transduction
Enzyme 110 Specific Function Ras effector protein. May function as an upstream activator and/or downstream effector for RAB5B in endocytic pathway. May function as a guanine nucleotide exchange (GEF) of RAB5B, required for activating the RAB5 proteins by exchanging bound GDP for free GTP
Enzyme 110 Pathways Not Available
Enzyme 110 Reactions Not Available
Enzyme 110 Pfam Domain Function
Enzyme 110 Signals
  • None
Enzyme 110 Transmembrane Regions
  • None
Enzyme 110 Essentiality Not Available
Enzyme 110 GenBank ID Protein 18413654 Link Image
Enzyme 110 UniProtKB/Swiss-Prot ID Q8WYP3 Link Image
Enzyme 110 UniProtKB/Swiss-Prot Entry Name RIN2_HUMAN Link Image
Enzyme 110 PDB ID Not Available
Enzyme 110 Cellular Location Not Available
Enzyme 110 Gene Sequence >2688 bp
ATGACAGCTTGGACCATGGGCGCCCGCGGTCTGGACAAGCGAGGAAGTTTCTTTAAGCTC
ATTGACACAATTGCCTCGGAGATCGGAGAACTGAAACAGGAGATGGTGCGGACAGATGTC
AACCTGGAAAATGGCCTGGAACCCGCTGAAACCCACAGCATGGTAAGACACAAGGATGGT
GGCTATTCCGAGGAAGAGGACGTGAAGACCTGTGCCCGGGACTCAGGCTATGACAGCCTC
TCCAACAGGCTCAGCATCTTGGACCGGCTCCTCCACACCCACCCCATATGGCTGCAGCTG
AGTCTGAGTGAGGAGGAGGCAGCAGAGGTCCTGCAGGCCCAGCCTCCGGGGATCTTCCTG
GTTCATAAATCTACCAAGATGCAGAAGAAAGTCCTCTCCCTCCGCCTGCCCTGTGAATTT
GGGGCCCCACTCAAGGAATTTGCCATAAAGGAAAGCACATACACCTTTTCCCTGGAAGGA
TCCGGAATCAGTTTCGCAGATTTATTCCGGCTCATTGCTTTCTACTGCATCAGCAGGGAT
GTTCTACCATTTACCTTGAAGTTGCCTTATGCCATTTCAACAGCCAAGTCGGAGGCTCAG
CTTGAAGAACTGGCCCAGATGGGACTAAATTTCTGGAGCTCCCCAGCTGACAGCAAACCC
CCGAACCTTCCACCTCCCCATAGGCCTCTTTCCTCCGACGGTGTCTGTCCTGCCTCCCTG
CGTCAGCTCTGCCTTATAAATGGAGTGCATTCTATCAAAACCAGGACGCCTTCAGAGCTG
GAGTGCAGCCAGACCAACGGGGCTCTGTGCTTTATTAATCCCCTTTTCTTGAAAGTGCAC
AGCCAGGACCTCAGTGGAGGCCTGAAACGGCCGAGCACAAGGACTCCCAACGCGAATGGC
ACGGAGCGGACTCGGTCCCCCCCACCCAGGCCCCCGCCACCCGCTATTAATAGTCTCCAC
ACAAGCCCTCGGCTGGCCAGGACTGAAACCCAGACGAGCATGCCAGAAACAGTCAACCAT
AACAAACATGGGAACGTAGCTCTGCCTGGAACGAAACCAACTCCCATCCCTCCACCCCGG
CTGAAGAAGCAGGCTTCTTTTCTGGAAGCAGAGGGCGGTGCAAAGACCTTGAGCGGCGGC
CGGCCGGGCGCAGGCCCGGAGCTGGAGCTGGGCACAGCTGGCAGCCCAGGTGGGGCCCCG
CCTGAGGCCGCCCCGGGGGATTGCACAAGGGCCCCGCCGCCCAGCTCTGAATCACGGCCC
CCGTGCCATGGAGGCCGGCAGCGGCTGAGCGACATGAGCATTTCTACTTCCTCCTCCGAC
TCGCTGGAGTTCGACCGGAGCATGCCTCTGTTTGGCTACGAGGCGGACACCAACAGCAGC
CTGGAGGACTACGAGGGGGAAAGTGACCAAGAGACCATGGCGCCCCCCATCAAGTCCAAA
AAGAAAAGGAGCAGCTCCTTCGTGCTGCCCAAGCTCGTCAAGTCCCAGCTGCAGAAGGTG
AGCGGGGTGTTCAGCTCCTTCATGACCCCGGAGAAGCGGATGGTCCGCAGGATCGCCGAG
CTTTCCCGGGACAAATGCACCTACTTCGGGTGCTTAGTGCAGGACTACGTGAGCTTCCTG
CAGGAGAACAAGGAGTGCCACGTGTCCAGCACCGACATGCTGCAGACCATCCGGCAGTTC
ATGACCCAGGTCAAGAACTATTTGTCTCAGAGCTCGGAGCTGGACCCCCCCATCGAGTCG
CTGATCCCTGAAGACCAAATAGATGTGGTGCTGGAAAAAGCCATGCACAAGTGCATCTTG
AAGCCCCTCAAGGGGCACGTGGAGGCCATGCTGAAGGACTTTCACATGGCCGATGGCTCA
TGGAAGCAACTCAAGGAGAACCTGCAGCTTGTGCGGCAGAGGAATCCGCAGGAGCTGGGG
GTCTTCGCCCCGACCCCTGATTTTGTGGATGTGGAGAAAATCAAAGTCAAGTTCATGACC
ATGCAGAAGATGTATTCGCCGGAAAAGAAGGTCATGCTGCTGCTGCGGGTCTGCAAGCTC
ATTTACACGGTCATGGAGAACAACTCAGGGAGGATGTATGGCGCTGATGACTTCTTGCCA
GTCCTGACCTATGTCATAGCCCAGTGTGACATGCTTGAATTGGACACTGAAATCGAGTAC
ATGATGGAGCTCCTAGACCCATCGCTGTTACATGGAGAAGGAGGCTATTACTTGACAAGC
GCATATGGAGCACTTTCTCTGATAAAGAATTTCCAAGAAGAACAAGCAGCGCGACTGCTC
AGCTCAGAAACCAGAGACACCCTGAGGCAGTGGCACAAACGGAGAACCACCAACCGGACC
ATCCCCTCTGTGGACGACTTCCAGAATTACCTCCGAGTTGCATTTCAGGAGGTCAACAGT
GGTTGCACAGGAAAGACCCTCCTTGTGAGACCTTACATCACCACTGAGGATGTGTGTCAG
ATCTGCGCTGAGAAGTTCAAGGTGGGGGACCCTGAGGAGTACAGCCTCTTTCTCTTCGTT
GACGAGACATGGCAGCAGCTGGCAGAGGACACTTACCCTCAAAAAATCAAGGCGGAGCTG
CACAGCCGACCACAGCCCCACATCTTCCACTTTGTCTACAAACGCATCAAGAACGATCCT
TATGGCATCATTTTCCAGAACGGGGAAGAAGACCTCACCACCTCCTAG
Enzyme 110 GenBank Gene ID AB060339 Link Image
Enzyme 110 GeneCard ID RIN2 Link Image
Enzyme 110 GenAtlas ID RIN2 Link Image
Enzyme 110 HGNC ID HGNC:18750 Link Image
Enzyme 110 Chromosome Location 2
Enzyme 110 Locus 20p11.22
Enzyme 110 SNPs SNPJam Report Link Image
Enzyme 110 General References
  1. Saito K, Murai J, Kajiho H, Kontani K, Kurosu H, Katada T: A novel binding protein composed of homophilic tetramer exhibits unique properties for the small GTPase Rab5. J Biol Chem. 2002 Feb 1;277(5):3412-8. Epub 2001 Dec 3. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  5. Colicelli J, Nicolette C, Birchmeier C, Rodgers L, Riggs M, Wigler M: Expression of three mammalian cDNAs that interfere with RAS function in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2913-7. [PubMed Link Image]
  6. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed Link Image]
  7. Basel-Vanagaite L, Sarig O, Hershkovitz D, Fuchs-Telem D, Rapaport D, Gat A, Isman G, Shirazi I, Shohat M, Enk CD, Birk E, Kohlhase J, Matysiak-Scholze U, Maya I, Knopf C, Peffekoven A, Hennies HC, Bergman R, Horowitz M, Ishida-Yamamoto A, Sprecher E: RIN2 deficiency results in macrocephaly, alopecia, cutis laxa, and scoliosis: MACS syndrome. Am J Hum Genet. 2009 Aug;85(2):254-63. Epub 2009 Jul 23. [PubMed Link Image]
Enzyme 110 Metabolite References Not Available
Enzyme 111 [top]
Enzyme 111 ID 14272
Enzyme 111 Name Ras and Rab interactor 3
Enzyme 111 Synonyms
  1. Ras interaction/interference protein 3
Enzyme 111 Gene Name RIN3
Enzyme 111 Protein Sequence >Ras and Rab interactor 3
MIRHAGAPARGDPTGPVPVVGKGEEEEEEDGMRLCLPANPKNCLPHRRGISILEKLIKTC
PVWLQLSLGQAEVARILHRVVAGMFLVRRDSSSKQLVLCVHFPSLNESSAEVLEYTIKEE
KSILYLEGSALVFEDIFRLIAFYCVSRDLLPFTLRLPQAILEASSFTDLETIANLGLGFW
DSSLNPPQERGKPAEPPRDRAPGFPLVSSLRPTAHDANCACEIELSVGNDRLWFVNPIFI
EDCSSALPTDQPPLGNCPARPLPPTSDATSPTSRWAPRRPPPPPPVLPLQPCSPAQPPVL
PALAPAPACPLPTSPPVPAPHVTPHAPGPPDHPNQPPMMTCERLPCPTAGLGPLREEAMK
PGAASSPLQQVPAPPLPAKKNLPTAPPRRRVSERVSLEDQSPGMAAEGDQLSLPPQGTSD
GPEDTPRESTEQGQDTEVKASDPHSMPELPRTAKQPPVPPPRKKRISRQLASTLPAPLEN
AELCTQAMALETPTPGPPREGQSPASQAGTQHPPAQATAHSQSSPEFKGSLASLSDSLGV
SVMATDQDSYSTSSTEEELEQFSSPSVKKKPSMILGKARHRLSFASFSSMFHAFLSNNRK
LYKKVVELAQDKGSYFGSLVQDYKVYSLEMMARQTSSTEMLQEIRTMMTQLKSYLLQSTE
LKALVDPALHSEEELEAIVESALYKCVLKPLKEAINSCLHQIHSKDGSLQQLKENQLVIL
ATTTTDLGVTTSVPEVPMMEKILQKFTSMHKAYSPEKKISILLKTCKLIYDSMALGNPGK
PYGADDFLPVLMYVLARSNLTEMLLNVEYMMELMDPALQLGEGSYYLTTTYGALEHIKSY
DKITVTRQLSVEVQDSIHRWERRRTLNKARASRSSVQDFICVSYLEPEQQARTLASRADT
QAQALCAQCAEKFAVERPQAHRLFVLVDGRCFQLADDALPHCIKGYLLRSEPKRDFHFVY
RPLDGGGGGGGGSPPCLVVREPNFL
Enzyme 111 Number of Residues 985
Enzyme 111 Molecular Weight 107852.4
Enzyme 111 Theoretical pI 6.58
Enzyme 111 GO Classification
Function
  • binding
  • protein binding
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 111 General Function Involved in signal transduction
Enzyme 111 Specific Function Potential Ras effector protein. May function as a guanine nucleotide exchange (GEF), by exchanging bound GDP for free GTP
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 40353729 Link Image
Enzyme 111 UniProtKB/Swiss-Prot ID Q8TB24 Link Image
Enzyme 111 UniProtKB/Swiss-Prot Entry Name RIN3_HUMAN Link Image
Enzyme 111 PDB ID Not Available
Enzyme 111 Cellular Location Not Available
Enzyme 111 Gene Sequence >2958 bp
ATGATCCGACACGCCGGGGCGCCCGCGCGCGGGGACCCCACGGGTCCGGTTCCAGTTGTT
GGCAAAGGAGAGGAAGAGGAAGAGGAAGATGGCATGCGGCTTTGTCTGCCAGCCAACCCG
AAAAACTGCCTTCCTCACCGCCGGGGCATCAGCATCCTGGAGAAGCTCATCAAAACATGC
CCGGTGTGGCTGCAGCTGAGTCTGGGCCAGGCAGAGGTGGCCAGGATCCTGCACCGGGTG
GTGGCTGGGATGTTCCTGGTTCGCCGGGACAGCAGCTCGAAGCAGCTGGTGCTCTGTGTC
CACTTTCCTTCTCTGAACGAAAGCTCGGCCGAGGTGCTCGAATACACCATTAAGGAAGAA
AAGTCGATATTGTACCTGGAAGGCTCGGCTCTTGTGTTTGAGGACATCTTCAGATTGATT
GCGTTCTACTGTGTCAGTAGAGACTTACTGCCCTTCACACTGCGGCTACCCCAGGCCATC
CTTGAGGCCAGCAGCTTCACGGACCTTGAGACCATCGCCAACCTGGGTCTGGGTTTCTGG
GACTCCTCGCTGAATCCTCCACAAGAAAGAGGGAAGCCAGCAGAGCCCCCAAGAGACCGG
GCCCCCGGATTCCCCCTAGTCTCCAGCCTCAGGCCCACAGCCCATGACGCAAACTGTGCC
TGTGAAATCGAGCTGTCGGTAGGAAATGACCGCCTGTGGTTTGTGAATCCTATTTTCATC
GAGGACTGCAGCAGCGCCCTGCCCACCGACCAGCCACCTCTTGGAAATTGCCCTGCACGC
CCTTTGCCGCCCACCTCTGATGCCACCTCACCCACCTCCAGGTGGGCCCCACGCCGCCCA
CCACCCCCTCCCCCAGTGCTGCCCCTGCAGCCCTGCAGCCCAGCCCAGCCCCCTGTGCTC
CCTGCTCTTGCCCCCGCCCCTGCCTGTCCTTTGCCCACCTCTCCCCCAGTGCCTGCCCCC
CACGTCACACCCCATGCCCCAGGTCCCCCAGACCATCCGAACCAGCCGCCCATGATGACC
TGCGAGAGACTCCCATGCCCCACTGCAGGCCTGGGCCCCCTCAGGGAGGAAGCGATGAAG
CCAGGGGCAGCCTCCAGTCCCTTGCAGCAGGTCCCCGCCCCGCCACTGCCTGCGAAGAAG
AACCTTCCCACTGCCCCTCCCAGACGCCGCGTTTCCGAGAGGGTGTCCTTAGAAGACCAA
AGTCCGGGGATGGCGGCAGAGGGGGACCAGCTCAGCCTGCCTCCCCAAGGGACCTCAGAC
GGCCCTGAGGACACGCCCCGGGAGAGCACGGAGCAAGGCCAGGACACAGAGGTGAAAGCC
AGCGATCCTCACAGCATGCCAGAGCTGCCCAGGACAGCCAAACAACCCCCAGTCCCGCCC
CCCAGGAAAAAACGGATCTCTCGACAACTGGCCTCGACCCTCCCAGCTCCCTTAGAGAAC
GCTGAGCTCTGCACACAGGCGATGGCCTTGGAGACACCCACGCCGGGTCCACCCAGAGAG
GGCCAAAGCCCTGCTTCTCAGGCTGGGACTCAGCACCCTCCTGCCCAGGCCACTGCCCAT
TCCCAGAGCTCTCCAGAGTTCAAGGGCTCCCTGGCCTCCCTCTCAGACAGCTTGGGGGTG
TCTGTCATGGCCACCGACCAGGACTCCTACTCCACCAGCAGCACGGAGGAGGAGCTGGAG
CAGTTCAGCAGCCCCAGCGTGAAGAAGAAGCCCTCCATGATCCTGGGCAAGGCTCGGCAC
CGGCTGAGCTTTGCCAGTTTCAGCAGCATGTTCCACGCTTTCCTCTCCAACAACCGCAAG
CTGTACAAGAAGGTGGTGGAGCTGGCGCAGGACAAGGGCTCGTACTTTGGCAGCCTGGTG
CAGGACTACAAGGTGTACAGCCTGGAGATGATGGCGCGCCAGACCTCCAGCACGGAGATG
CTGCAGGAGATTCGCACCATGATGACCCAGCTCAAGAGCTACCTGCTGCAGAGCACCGAG
CTCAAGGCCCTGGTGGACCCCGCCCTGCACTCCGAGGAGGAGCTCGAAGCAATTGTAGAG
TCTGCCTTGTACAAATGTGTCCTGAAGCCCCTGAAGGAAGCCATCAACTCATGCCTGCAT
CAGATCCACAGCAAGGATGGTTCGCTGCAGCAGCTCAAGGAGAACCAGTTAGTGATCCTG
GCCACCACCACCACTGACCTAGGTGTGACCACCAGCGTGCCGGAGGTGCCCATGATGGAG
AAGATCCTGCAGAAGTTCACCAGCATGCACAAGGCCTACTCACCTGAGAAGAAGATCTCC
ATCCTGCTCAAGACCTGCAAACTCATCTACGACTCCATGGCCCTCGGCAACCCAGGGAAG
CCCTATGGGGCGGATGACTTCCTGCCTGTGCTCATGTATGTGCTGGCCCGCAGCAACCTC
ACGGAGATGCTTCTCAATGTGGAGTACATGATGGAGCTCATGGACCCCGCCCTGCAGCTG
GGGGAGGGTTCCTACTATCTGACCACCACCTACGGGGCCCTGGAGCACATCAAGAGCTAC
GACAAGATCACGGTGACCCGGCAGCTGAGTGTGGAGGTGCAGGACTCCATCCACCGCTGG
GAGCGCCGGCGTACTCTCAACAAGGCCCGGGCCTCCCGCTCCTCCGTACAGGACTTCATC
TGCGTGTCGTACCTGGAGCCCGAGCAGCAGGCGCGGACGCTGGCGTCGCGGGCGGACACC
CAGGCCCAGGCGCTGTGCGCGCAGTGCGCGGAGAAGTTCGCGGTGGAGCGGCCGCAGGCG
CACCGGCTGTTCGTGCTGGTGGACGGGCGCTGCTTCCAGCTGGCGGACGACGCGCTGCCG
CACTGCATCAAGGGCTACCTGCTGCGCAGCGAGCCCAAGCGCGACTTCCACTTTGTCTAC
CGGCCCCTGGACGGTGGTGGCGGCGGCGGCGGCGGGAGCCCGCCCTGCCTGGTGGTGCGG
GAGCCCAACTTCCTGTGA
Enzyme 111 GenBank Gene ID NM_024832.3 Link Image
Enzyme 111 GeneCard ID RIN3 Link Image
Enzyme 111 GenAtlas ID RIN3 Link Image
Enzyme 111 HGNC ID HGNC:18751 Link Image
Enzyme 111 Chromosome Location 1
Enzyme 111 Locus 14q32.12
Enzyme 111 SNPs SNPJam Report Link Image
Enzyme 111 General References
  1. Kajiho H, Saito K, Tsujita K, Kontani K, Araki Y, Kurosu H, Katada T: RIN3: a novel Rab5 GEF interacting with amphiphysin II involved in the early endocytic pathway. J Cell Sci. 2003 Oct 15;116(Pt 20):4159-68. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Saito K, Murai J, Kajiho H, Kontani K, Kurosu H, Katada T: A novel binding protein composed of homophilic tetramer exhibits unique properties for the small GTPase Rab5. J Biol Chem. 2002 Feb 1;277(5):3412-8. Epub 2001 Dec 3. [PubMed Link Image]
  6. Yoshikawa M, Kajiho H, Sakurai K, Minoda T, Nakagawa S, Kontani K, Katada T: Tyr-phosphorylation signals translocate RIN3, the small GTPase Rab5-GEF, to early endocytic vesicles. Biochem Biophys Res Commun. 2008 Jul 18;372(1):168-72. Epub 2008 May 16. [PubMed Link Image]
Enzyme 111 Metabolite References Not Available
Enzyme 112 [top]
Enzyme 112 ID 14273
Enzyme 112 Name GTP-binding protein Rit1
Enzyme 112 Synonyms
  1. Ras-like protein expressed in many tissues
  2. Ras-like without CAAX protein 1
Enzyme 112 Gene Name RIT1
Enzyme 112 Protein Sequence >GTP-binding protein Rit1
MDSGTRPVGSCCSSPAGLSREYKLVMLGAGGVGKSAMTMQFISHRFPEDHDPTIEDAYKI
RIRIDDEPANLDILDTAGQAEFTAMRDQYMRAGEGFIICYSITDRRSFHEVREFKQLIYR
VRRTDDTPVVLVGNKSDLKQLRQVTKEEGLALAREFSCPFFETSAAYRYYIDDVFHALVR
EIRRKEKEAVLAMEKKSKPKNSVWKRLKSPFRKKKDSVT
Enzyme 112 Number of Residues 219
Enzyme 112 Molecular Weight 25144.6
Enzyme 112 Theoretical pI 9.50
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
  • 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 112 General Function Involved in GTP binding
Enzyme 112 Specific Function Plays a crucial role in coupling NGF stimulation to the activation of both EPHB2 and MAPK14 signaling pathways and in NGF- dependent neuronal differentiation
Enzyme 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 4234918 Link Image
Enzyme 112 UniProtKB/Swiss-Prot ID Q92963 Link Image
Enzyme 112 UniProtKB/Swiss-Prot Entry Name RIT1_HUMAN Link Image
Enzyme 112 PDB ID Not Available
Enzyme 112 Cellular Location Not Available
Enzyme 112 Gene Sequence >660 bp
ATGGATTCTGGAACTCGCCCAGTTGGTAGCTGCTGTAGCAGCCCCGCTGGGCTCTCACGG
GAGTACAAACTAGTGATGCTGGGTGCTGGTGGTGTAGGGAAGAGTGCCATGACCATGCAG
TTCATCAGCCACCGATTCCCAGAAGATCATGATCCCACCATTGAAGATGCTTATAAGATC
AGGATCCGTATTGATGATGAGCCTGCCAATCTGGACATTTTGGATACAGCTGGACAGGCA
GAGTTTACAGCCATGCGGGACCAGTATATGAGGGCAGGAGAAGGGTTTATCATCTGTTAC
TCTATCACGGATCGTCGAAGTTTCCATGAAGTTCGAGAGTTTAAACAGCTTATTTATCGA
GTCCGACGTACTGACGATACACCTGTGGTTCTTGTGGGAAACAAGTCAGACCTCAAACAG
CTAAGACAGGTCACCAAGGAAGAAGGATTGGCCTTGGCCCGAGAATTCAGCTGTCCCTTT
TTTGAGACATCTGCTGCATACCGCTACTATATTGATGATGTTTTCCATGCCCTTGTACGG
GAGATACGTAGGAAAGAAAAGGAGGCAGTACTGGCCATGGAGAAAAAATCTAAGCCCAAA
AACAGTGTATGGAAGAGGCTAAAATCACCATTCCGGAAGAAGAAAGATTCAGTAACTTGA
Enzyme 112 GenBank Gene ID AF084462 Link Image
Enzyme 112 GeneCard ID RIT1 Link Image
Enzyme 112 GenAtlas ID RIT1 Link Image
Enzyme 112 HGNC ID HGNC:10023 Link Image
Enzyme 112 Chromosome Location 1
Enzyme 112 Locus 1q22
Enzyme 112 SNPs SNPJam Report Link Image
Enzyme 112 General References
  1. Lee CH, Della NG, Chew CE, Zack DJ: Rin, a neuron-specific and calmodulin-binding small G-protein, and Rit define a novel subfamily of ras proteins. J Neurosci. 1996 Nov 1;16(21):6784-94. [PubMed Link Image]
  2. Wes PD, Yu M, Montell C: RIC, a calmodulin-binding Ras-like GTPase. EMBO J. 1996 Nov 1;15(21):5839-48. [PubMed Link Image]
  3. Shao H, Kadono-Okuda K, Finlin BS, Andres DA: Biochemical characterization of the Ras-related GTPases Rit and Rin. Arch Biochem Biophys. 1999 Nov 15;371(2):207-19. [PubMed Link Image]
  4. Shi GX, Andres DA: Rit contributes to nerve growth factor-induced neuronal differentiation via activation of B-Raf-extracellular signal-regulated kinase and p38 mitogen-activated protein kinase cascades. Mol Cell Biol. 2005 Jan;25(2):830-46. [PubMed Link Image]
Enzyme 112 Metabolite References Not Available
Enzyme 113 [top]
Enzyme 113 ID 14274
Enzyme 113 Name GTP-binding protein Rit2
Enzyme 113 Synonyms
  1. Ras-like protein expressed in neurons
  2. Ras-like without CAAX protein 2
Enzyme 113 Gene Name RIT2
Enzyme 113 Protein Sequence >GTP-binding protein Rit2
MEVENEASCSPGSASGGSREYKVVMLGAGGVGKSAMTMQFISHQFPDYHDPTIEDAYKTQ
VRIDNEPAYLDILDTAGQAEFTAMREQYMRGGEGFIICYSVTDRQSFQEAAKFKELIFQV
RHTYEIPLVLVGNKIDLEQFRQVSTEEGLSLAQEYNCGFFETSAALRFCIDDAFHGLVRE
IRKKESMPSLMEKKLKRKDSLWKKLKGSLKKKRENMT
Enzyme 113 Number of Residues 217
Enzyme 113 Molecular Weight 24667.9
Enzyme 113 Theoretical pI 6.52
Enzyme 113 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 113 General Function Involved in GTP binding
Enzyme 113 Specific Function Binds and exchanges GTP and GDP
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 20147737 Link Image
Enzyme 113 UniProtKB/Swiss-Prot ID Q99578 Link Image
Enzyme 113 UniProtKB/Swiss-Prot Entry Name RIT2_HUMAN Link Image
Enzyme 113 PDB ID Not Available
Enzyme 113 Cellular Location Not Available
Enzyme 113 Gene Sequence >654 bp
ATGGAGGTAGAAAATGAAGCCAGCTGCTCCCCGGGCAGCGCATCAGGCGGGTCCAGAGAG
TACAAGGTGGTAATGCTGGGAGCAGGGGGAGTTGGTAAAAGCGCAATGACAATGCTGTTT
ATTAGTCATCAGTTCCCTGATTATCATGACCCTACTATAGAAGATGCTTATAAGACCCAG
GTCAGGATTGACAATGAGCCAGCTTACTTGGACATCTTGGACACTGCTGGCCAGGCAGAA
TTCACAGCCATGCGGGAGCAGTACATGCGAGGTGGGGAAGGCTTCATCATCTGCTACTCC
GTCACTGACCGTCAATCATTTCAGGAGGCTGCCAAGTTTAAAGAGCTCATTTTTCAGGTC
CGCCACACCTATGAAATTCCCCTGGTGCTGGTGGGTAACAAAATTGATCTGGAACAGTTC
CGCCAGGTTTCTACAGAAGAAGGCTTGAGTCTTGCCCAAGAATATAATTGTGGTTTTTTT
GAGACCTCTGCAGCCCTCAGATTCTGTATTGATGATGCTTTTCATGGCTTAGTGAGGGAA
ATTCGCAAGAAGGAGTCCATGCCATCCTTGATGGAAAAGAAACTGAAGAGAAAAGACAGC
CTGTGGAAGAAGCTCAAAGGTTCTTTGAAGAAGAAGAGAGAAAATATGACATGA
Enzyme 113 GenBank Gene ID AF493922 Link Image
Enzyme 113 GeneCard ID RIT2 Link Image
Enzyme 113 GenAtlas ID RIT2 Link Image
Enzyme 113 HGNC ID HGNC:10017 Link Image
Enzyme 113 Chromosome Location 1
Enzyme 113 Locus 18q12.3
Enzyme 113 SNPs SNPJam Report Link Image
Enzyme 113 General References
  1. Lee CH, Della NG, Chew CE, Zack DJ: Rin, a neuron-specific and calmodulin-binding small G-protein, and Rit define a novel subfamily of ras proteins. J Neurosci. 1996 Nov 1;16(21):6784-94. [PubMed Link Image]
  2. Wes PD, Yu M, Montell C: RIC, a calmodulin-binding Ras-like GTPase. EMBO J. 1996 Nov 1;15(21):5839-48. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 113 Metabolite References Not Available
Enzyme 114 [top]
Enzyme 114 ID 14277
Enzyme 114 Name Rap guanine nucleotide exchange factor 5
Enzyme 114 Synonyms
  1. Guanine nucleotide exchange factor for Rap1
  2. M-Ras-regulated Rap GEF
  3. MR-GEF
  4. Related to Epac
  5. Repac
Enzyme 114 Gene Name RAPGEF5
Enzyme 114 Protein Sequence >Rap guanine nucleotide exchange factor 5
MGSSRLRVFDPHLERKDSAAALSDRELPLPTFDVPYFKYIDEEDEDDEWSSRSQSSTEDD
SVDSLLSDRYVVVSGTPEKILEHLLNDLHLEEVQDKETETLLDDFLLTYTVFMTTDDLCQ
ALLRHYSAKKYQGKEENSDVPRRKRKVLHLVSQWIALYKDWLPEDEHSKMFLKTIYRNVL
DDVYEYPILEKELKEFQKILGMHRRHTVDEYSPQKKNKALFHQFSLKENWLQHRGTVTET
EEIFCHVYITEHSYVSVKAKVSSIAQEILKVVAEKIQYAEEDLALVAITFSGEKHELQPN
DLVISKSLEASGRIYVYRKDLADTLNPFAENEESQQRSMRILGMNTWDLALELMNFDWSL
FNSIHEQELIYFTFSRQGSGEHTANLSLLLQRCNEVQLWVATEILLCSQLGKRVQLVKKF
IKIAAHCKAQRNLNSFFAIVMGLNTASVSRLSQTWEKIPGKFKKLFSELESLTDPSLNHK
AYRDAFKKMKPPKIPFMPLLLKDVTFIHEGNKTFLDNLVNFEKLHMIADTVRTLRHCRTN
QFGDLSPKEHQELKSYVNHLYVIDSQQALFELSHRIEPRV
Enzyme 114 Number of Residues 580
Enzyme 114 Molecular Weight 67732.6
Enzyme 114 Theoretical pI 6.27
Enzyme 114 GO Classification
Function
  • GTPase regulator activity
  • enzyme regulator activity
  • guanyl-nucleotide exchange factor activity
  • nucleoside-triphosphatase regulator activity
Process
  • biological regulation
  • intracellular signal transduction
  • regulation of biological process
  • regulation of cell communication
  • regulation of cellular process
  • regulation of signal transduction
  • regulation of small GTPase mediated signal transduction
  • signal transduction
  • small GTPase mediated signal transduction
Component
  • cell part
  • intracellular
Enzyme 114 General Function Involved in guanyl-nucleotide exchange factor activity
Enzyme 114 Specific Function Guanine nucleotide exchange factor (GEF) for RAP1A, RAP2A and MRAS/M-Ras-GTP. Its association with MRAS inhibits Rap1 activation
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 40788937 Link Image
Enzyme 114 UniProtKB/Swiss-Prot ID Q92565 Link Image
Enzyme 114 UniProtKB/Swiss-Prot Entry Name RPGF5_HUMAN Link Image
Enzyme 114 PDB ID 1WGY Link Image
Enzyme 114 PDB File Show
Enzyme 114 3D Structure
Enzyme 114 Cellular Location Not Available
Enzyme 114 Gene Sequence >1752 bp
CCGTTCACAATGGGCAGCTCCCGGCTGAGGGTCTTTGACCCTCATTTGGAGAGGAAAGAT
TCCGCCGCGGCGCTCTCAGACCGAGAGCTGCCCTTGCCTACCTTCGATGTGCCTTATTTC
AAATACATCGACGAGGAGGATGAGGACGATGAATGGAGCAGCCGTTCGCAGTCTTCCACC
GAGGATGACTCAGTGGACTCTCTGCTCTCTGACAGATATGTGGTGGTGTCCGGGACCCCG
GAGAAGATTTTGGAGCACCTTTTGAATGACTTGCACCTGGAAGAAGTCCAGGACAAAGAA
ACAGAGACCCTCCTGGATGACTTCCTTCTCACGTACACTGTCTTCATGACAACTGATGAC
TTGTGCCAGGCTCTGTTAAGGCACTATTCTGCTAAGAAGTATCAAGGCAAAGAGGAAAAC
TCAGATGTTCCGCGTAGGAAACGTAAAGTCTTGCATCTTGTTTCCCAGTGGATTGCTCTG
TACAAAGACTGGTTACCTGAAGATGAACATTCAAAAATGTTTTTAAAGACCATATATAGG
AATGTACTGGATGATGTTTATGAATATCCAATACTTGAAAAAGAATTGAAAGAATTTCAA
AAGATACTTGGAATGCACCGTCGTCACACTGTAGATGAATATTCACCACAAAAAAAGAAT
AAAGCCCTTTTCCACCAATTCAGTCTTAAGGAGAACTGGCTCCAGCATAGAGGAACTGTG
ACTGAAACGGAGGAAATTTTCTGCCACGTGTATATAACAGAGCACTCCTATGTCAGTGTG
AAGGCAAAAGTTTCCAGTATAGCCCAAGAGATCCTAAAAGTCGTGGCAGAAAAGATCCAG
TATGCAGAAGAGGATCTGGCTCTGGTGGCCATCACATTCTCTGGGGAAAAGCATGAACTT
CAGCCAAATGACTTAGTCATCTCCAAATCCCTCGAGGCATCTGGTCGAATATATGTCTAC
CGGAAAGACCTGGCGGACACTTTGAACCCATTTGCAGAAAATGAGGAATCACAGCAAAGG
TCGATGAGGATTTTGGGAATGAACACTTGGGATCTTGCTCTGGAATTAATGAATTTTGAT
TGGAGTCTATTCAATTCAATTCACGAGCAAGAGCTGATCTACTTCACGTTCAGCAGACAG
GGAAGTGGGGAACACACTGCAAATCTCAGCCTTCTGCTCCAGAGATGCAATGAGGTCCAG
CTTTGGGTGGCCACGGAGATTCTGCTCTGCAGCCAGCTGGGCAAGCGAGTGCAGCTGGTG
AAAAAATTCATCAAAATTGCGGCTCACTGCAAAGCCCAGAGAAACCTGAATTCTTTCTTT
GCCATTGTGATGGGTCTCAACACTGCTTCTGTCAGTCGACTGTCGCAGACCTGGGAGAAA
ATCCCTGGGAAGTTTAAGAAACTTTTCTCTGAACTTGAAAGTTTAACAGATCCTTCCCTA
AATCACAAAGCCTACAGAGATGCATTCAAAAAGATGAAGCCACCAAAAATCCCTTTCATG
CCCTTATTGCTTAAAGATGTAACATTTATTCATGAAGGAAATAAAACTTTTTTGGATAAT
CTTGTCAATTTTGAAAAGCTGCATATGATCGCAGACACTGTCCGAACCCTGAGACACTGC
AGGACTAACCAGTTTGGTGACCTGTCTCCAAAAGAGCATCAAGAGTTAAAGTCCTATGTT
AATCACCTGTATGTCATTGACAGCCAGCAGGCTCTGTTTGAGCTCTCACACAGGATCGAG
CCTCGGGTGTGA
Enzyme 114 GenBank Gene ID D87467 Link Image
Enzyme 114 GeneCard ID RAPGEF5 Link Image
Enzyme 114 GenAtlas ID RAPGEF5 Link Image
Enzyme 114 HGNC ID HGNC:16862 Link Image
Enzyme 114 Chromosome Location 7
Enzyme 114 Locus 7p15.3
Enzyme 114 SNPs SNPJam Report Link Image
Enzyme 114 General References
  1. Nagase T, Seki N, Ishikawa K, Ohira M, Kawarabayasi Y, Ohara O, Tanaka A, Kotani H, Miyajima N, Nomura N: Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain. DNA Res. 1996 Oct 31;3(5):321-9, 341-54. [PubMed Link Image]
  2. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ichiba T, Hoshi Y, Eto Y, Tajima N, Kuraishi Y: Characterization of GFR, a novel guanine nucleotide exchange factor for Rap1. FEBS Lett. 1999 Aug 20;457(1):85-9. [PubMed Link Image]
  5. de Rooij J, Rehmann H, van Triest M, Cool RH, Wittinghofer A, Bos JL: Mechanism of regulation of the Epac family of cAMP-dependent RapGEFs. J Biol Chem. 2000 Jul 7;275(27):20829-36. [PubMed Link Image]
  6. Rebhun JF, Castro AF, Quilliam LA: Identification of guanine nucleotide exchange factors (GEFs) for the Rap1 GTPase. Regulation of MR-GEF by M-Ras-GTP interaction. J Biol Chem. 2000 Nov 10;275(45):34901-8. [PubMed Link Image]
Enzyme 114 Metabolite References Not Available
Enzyme 115 [top]
Enzyme 115 ID 14279
Enzyme 115 Name Ras-related GTP-binding protein A
Enzyme 115 Synonyms
  1. Rag A
  2. RagA
  3. Adenovirus E3 14.7 kDa-interacting protein 1
  4. FIP-1
Enzyme 115 Gene Name RRAGA
Enzyme 115 Protein Sequence >Ras-related GTP-binding protein A
MPNTAMKKKVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNL
WDCGGQDTFMENYFTSQRDNIFRNVEVLIYVFDVESRELEKDMHYYQSCLEAILQNSPDA
KIFCLVHKMDLVQEDQRDLIFKEREEDLRRLSRPLECACFRTSIWDETLYKAWSSIVYQL
IPNVQQLEMNLRNFAQIIEADEVLLFERATFLVISHYQCKEQRDVHRFEKISNIIKQFKL
SCSKLAASFQSMEVRNSNFAAFIDIFTSNTYVMVVMSDPSIPSAATLINIRNARKHFEKL
ERVDGPKHSLLMR
Enzyme 115 Number of Residues 313
Enzyme 115 Molecular Weight 36565.8
Enzyme 115 Theoretical pI 7.81
Enzyme 115 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
Component
  • cell part
  • cytoplasm
  • intracellular membrane-bounded organelle
  • intracellular part
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 115 General Function Involved in GTP binding
Enzyme 115 Specific Function Involved in the RCC1/Ran-GTPase pathway. May play a direct role in a TNF-alpha signaling pathway leading to induction of cell death. May alternatively act as a cellular target for adenovirus E3-14.7K, an inhibitor of TNF-alpha functions, thereby affecting cell death. Has guanine nucleotide-binding activity but undetectable intrinsic GTPase activity
Enzyme 115 Pathways Not Available
Enzyme 115 Reactions Not Available
Enzyme 115 Pfam Domain Function
Enzyme 115 Signals
  • None
Enzyme 115 Transmembrane Regions
  • None
Enzyme 115 Essentiality Not Available
Enzyme 115 GenBank ID Protein 189053606 Link Image
Enzyme 115 UniProtKB/Swiss-Prot ID Q7L523 Link Image
Enzyme 115 UniProtKB/Swiss-Prot Entry Name RRAGA_HUMAN Link Image
Enzyme 115 PDB ID Not Available
Enzyme 115 Cellular Location Not Available
Enzyme 115 Gene Sequence >942 bp
ATGCCAAATACAGCCATGAAGAAAAAGGTGCTGCTGATGGGGAAGAGCGGGTCGGGGAAG
ACCAGCATGAGGTCGATAATCTTCGCCAATTACATTGCTCGCGACACCCGGCGCCTGGGG
GCCACCATTGACGTGGAACACTCCCACGTCCGATTCCTAGGGAACCTGGTGCTGAACCTG
TGGGACTGTGGCGGTCAGGACACCTTCATGGAAAATTACTTCACCAGCCAGCGAGACAAT
ATCTTCCGTAACGTGGAAGTTTTGATTTACGTGTTTGACGTGGAGAGCCGCGAACTGGAA
AAGGACATGCATTATTACCAGTCGTGTCTGGAGGCCATCCTCCAGAACTCTCCTGACGCC
AAAATCTTCTGCCTGGTGCACAAAATGGATCTGGTTCAGGAGGATCAGCGTGACCTGATT
TTTAAAGAGCGAGAGGAAGACCTGAGGCGTCTGTCTCGCCCGCTGGAGTGTGCTTGTTTT
CGAACGTCCATCTGGGATGAGACGCTCTACAAAGCCTGGTCCAGCATCGTCTACCAGCTG
ATTCCCAACGTTCAGCAGCTGGAGATGAACCTCAGGAATTTTGCCCAAATCATTGAGGCC
GATGAAGTTCTGCTGTTCGAAAGAGCTACATTCTTGGTTATTTCCCACTACCAGTGCAAA
GAGCAGCGCGACGTCCACCGGTTTGAGAAGATCAGCAACATCATCAAACAGTTCAAGCTG
AGCTGCAGTAAATTGGCCGCTTCCTTCCAGAGCATGGAAGTTAGGAATTCCAACTTCGCT
GCTTTCATCGACATCTTCACCTCAAATACGTACGTGATGGTGGTCATGTCAGATCCGTCG
ATCCCTTCTGCGGCCACTCTGATCAACATTCGCAATGCCCGGAAACACTTTGAGAAGCTG
GAGAGAGTGGATGGCCCCAAGCACAGTCTCCTTATGCGTTGA
Enzyme 115 GenBank Gene ID AK313023 Link Image
Enzyme 115 GeneCard ID RRAGA Link Image
Enzyme 115 GenAtlas ID RRAGA Link Image
Enzyme 115 HGNC ID HGNC:16963 Link Image
Enzyme 115 Chromosome Location 9
Enzyme 115 Locus 9p22.1
Enzyme 115 SNPs SNPJam Report Link Image
Enzyme 115 General References
  1. Schurmann A, Brauers A, Massmann S, Becker W, Joost HG: Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs, RagB1) with remote similarity to the Ras-related GTPases. J Biol Chem. 1995 Dec 1;270(48):28982-8. [PubMed Link Image]
  2. Li Y, Kang J, Horwitz MS: Interaction of an adenovirus 14.7-kilodalton protein inhibitor of tumor necrosis factor alpha cytolysis with a new member of the GTPase superfamily of signal transducers. J Virol. 1997 Feb;71(2):1576-82. [PubMed Link Image]
  3. Hirose E, Nakashima N, Sekiguchi T, Nishimoto T: RagA is a functional homologue of S. cerevisiae Gtr1p involved in the Ran/Gsp1-GTPase pathway. J Cell Sci. 1998 Jan;111 ( Pt 1):11-21. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Sekiguchi T, Hirose E, Nakashima N, Ii M, Nishimoto T: Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B. J Biol Chem. 2001 Mar 9;276(10):7246-57. Epub 2000 Nov 9. [PubMed Link Image]
  8. Sekiguchi T, Todaka Y, Wang Y, Hirose E, Nakashima N, Nishimoto T: A novel human nucleolar protein, Nop132, binds to the G proteins, RRAG A/C/D. J Biol Chem. 2004 Feb 27;279(9):8343-50. Epub 2003 Dec 4. [PubMed Link Image]
Enzyme 115 Metabolite References Not Available
Enzyme 116 [top]
Enzyme 116 ID 14280
Enzyme 116 Name Ras-related GTP-binding protein B
Enzyme 116 Synonyms
  1. Rag B
  2. RagB
Enzyme 116 Gene Name RRAGB
Enzyme 116 Protein Sequence >Ras-related GTP-binding protein B
MEESDSEKTTEKENLGPRMDPPLGEPEGSLGWVLPNTAMKKKVLLMGKSGSGKTSMRSII
FANYIARDTRRLGATILDRIHSLQINSSLSTYSLVDSVGNTKTFDVEHSHVRFLGNLVLN
LWDCGGQDTFMENYFTSQRDNIFRNVEVLIYVFDVESRELEKDMHYYQSCLEAILQNSPD
AKIFCLVHKMDLVQEDQRDLIFKEREEDLRRLSRPLECSCFRTSIWDETLYKAWSSIVYQ
LIPNVQQLEMNLRNFAEIIEADEVLLFERATFLVISHYQCKEQRDAHRFEKISNIIKQFK
LSCSKLAASFQSMEVRNSNFAAFIDIFTSNTYVMVVMSDPSIPSAATLINIRNARKHFEK
LERVDGPKQCLLMR
Enzyme 116 Number of Residues 374
Enzyme 116 Molecular Weight 43250.0
Enzyme 116 Theoretical pI 6.13
Enzyme 116 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
Component
  • cell part
  • cytoplasm
  • intracellular membrane-bounded organelle
  • intracellular part
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 116 General Function Involved in GTP binding
Enzyme 116 Specific Function Involved in the RCC1/Ran-GTPase pathway. Has guanine nucleotide-binding activity but undetectable intrinsic GTPase activity
Enzyme 116 Pathways Not Available
Enzyme 116 Reactions Not Available
Enzyme 116 Pfam Domain Function
Enzyme 116 Signals
  • None
Enzyme 116 Transmembrane Regions
  • None
Enzyme 116 Essentiality Not Available
Enzyme 116 GenBank ID Protein 46249397 Link Image
Enzyme 116 UniProtKB/Swiss-Prot ID Q5VZM2 Link Image
Enzyme 116 UniProtKB/Swiss-Prot Entry Name RRAGB_HUMAN Link Image
Enzyme 116 PDB ID Not Available
Enzyme 116 Cellular Location Not Available
Enzyme 116 Gene Sequence >1125 bp
ATGGAAGAATCTGACTCTGAGAAAACGACGGAGAAAGAAAATCTGGGGCCGAGAATGGAT
CCACCACTAGGGGAACCGGAAGGATCGCTTGGGTGGGTGCTACCAAATACAGCCATGAAG
AAAAAGGTGCTGTTGATGGGTAAAAGTGGGTCTGGTAAGACCAGCATGAGGTCTATTATC
TTTGCAAATTATATTGCCAGAGACACACGTCGCCTTGGCGCAACAATACTAGACCGTATA
CATAGTCTTCAAATTAATAGCAGTTTGAGCACCTACTCTCTCGTAGACTCTGTTGGAAAT
ACAAAGACATTTGATGTAGAACATTCTCATGTTCGATTTCTGGGAAACCTGGTATTGAAC
CTGTGGGATTGTGGTGGGCAAGACACCTTCATGGAAAATTATTTCACTAGCCAACGGGAC
AACATCTTCCGAAATGTGGAGGTTCTGATTTATGTCTTTGATGTGGAGAGCCGCGAACTG
GAAAAGGACATGCACTATTACCAATCATGCCTGGAGGCCATTCTGCAGAATTCTCCAGAT
GCCAAAATATTTTGCTTGGTACACAAAATGGATCTGGTACAGGAGGATCAACGGGACCTG
ATTTTTAAAGAGCGAGAAGAAGATTTGAGGCGTTTGTCTCGCCCATTGGAATGTTCTTGT
TTCCGAACATCTATCTGGGATGAAACCCTCTATAAGGCTTGGTCCAGCATAGTTTATCAG
CTGATTCCCAATGTTCAGCAGCTGGAAATGAACCTAAGGAATTTTGCTGAAATTATCGAA
GCTGATGAAGTACTTCTTTTTGAGAGAGCTACTTTTCTGGTAATTTCTCACTATCAGTGT
AAAGAGCAGCGTGATGCCCATAGATTTGAGAAAATAAGCAACATTATTAAGCAGTTCAAG
CTGAGCTGCAGCAAGCTGGCTGCCTCTTTCCAGAGTATGGAAGTCAGGAACTCTAACTTC
GCTGCTTTCATTGACATCTTTACATCCAACACTTATGTGATGGTTGTGATGTCTGATCCG
TCCATTCCTTCTGCAGCTACTCTGATCAACATCCGCAATGCCAGGAAACACTTTGAAAAG
CTGGAAAGAGTGGATGGACCAAAGCAGTGTCTTCTCATGCGCTAA
Enzyme 116 GenBank Gene ID NM_016656.3 Link Image
Enzyme 116 GeneCard ID RRAGB Link Image
Enzyme 116 GenAtlas ID RRAGB Link Image
Enzyme 116 HGNC ID HGNC:19901 Link Image
Enzyme 116 Chromosome Location Not Available
Enzyme 116 Locus Not Available
Enzyme 116 SNPs SNPJam Report Link Image
Enzyme 116 General References
  1. Schurmann A, Brauers A, Massmann S, Becker W, Joost HG: Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs, RagB1) with remote similarity to the Ras-related GTPases. J Biol Chem. 1995 Dec 1;270(48):28982-8. [PubMed Link Image]
  2. Hirose E, Nakashima N, Sekiguchi T, Nishimoto T: RagA is a functional homologue of S. cerevisiae Gtr1p involved in the Ran/Gsp1-GTPase pathway. J Cell Sci. 1998 Jan;111 ( Pt 1):11-21. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Sekiguchi T, Hirose E, Nakashima N, Ii M, Nishimoto T: Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B. J Biol Chem. 2001 Mar 9;276(10):7246-57. Epub 2000 Nov 9. [PubMed Link Image]
Enzyme 116 Metabolite References Not Available
Enzyme 117 [top]
Enzyme 117 ID 14281
Enzyme 117 Name Ras-related GTP-binding protein C
Enzyme 117 Synonyms
  1. Rag C
  2. RagC
  3. GTPase-interacting protein 2
  4. TIB929
Enzyme 117 Gene Name RRAGC
Enzyme 117 Protein Sequence >Ras-related GTP-binding protein C
MSLQYGAEETPLAGSYGAADSFPKDFGYGVEEEEEEAAAAGGGVGAGAGGGCGPGGADSS
KPRILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKIYKDDISNSSFVNFQIWDFPGQ
MDFFDPTFDYEMIFRGTGALIYVIDAQDDYMEALTRLHITVSKAYKVNPDMNFEVFIHKV
DGLSDDHKIETQRDIHQRANDDLADAGLEKLHLSFYLTSIYDHSIFEAFSKVVQKLIPQL
PTLENLLNIFISNSGIEKAFLFDVVSKIYIATDSSPVDMQSYELCCDMIDVVIDVSCIYG
LKEDGSGSAYDKESMAIIKLNNTTVLYLKEVTKFLALVCILREESFERKGLIDYNFHCFR
KAIHEVFEVGVTSHRSCGHQTSASSLKALTHNGTPRNAI
Enzyme 117 Number of Residues 399
Enzyme 117 Molecular Weight 44223.5
Enzyme 117 Theoretical pI 4.72
Enzyme 117 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
Component
  • cell part
  • cytoplasm
  • intracellular membrane-bounded organelle
  • intracellular part
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 117 General Function Involved in GTP binding
Enzyme 117 Specific Function Has guanine nucleotide-binding activity but weak intrinsic GTPase activity
Enzyme 117 Pathways Not Available
Enzyme 117 Reactions Not Available
Enzyme 117 Pfam Domain Function
Enzyme 117 Signals
  • None
Enzyme 117 Transmembrane Regions
  • None
Enzyme 117 Essentiality Not Available
Enzyme 117 GenBank ID Protein 11181618 Link Image
Enzyme 117 UniProtKB/Swiss-Prot ID Q9HB90 Link Image
Enzyme 117 UniProtKB/Swiss-Prot Entry Name RRAGC_HUMAN Link Image
Enzyme 117 PDB ID Not Available
Enzyme 117 Cellular Location Not Available
Enzyme 117 Gene Sequence >1200 bp
ATGTCCCTGCAGTACGGGGCGGAGGAGACGCCCCTCGCCGGCAGTTACGGCGCGGCCGAT
TCGTTTCCAAAGGACTTCGGCTACGGCGTGGAGGAGGAGGAAGAGGAGGCGGCGGCGGCG
GGCGGAGGGGTTGGGGCAGGGGCAGGCGGTGGCTGTGGTCCGGGGGGCGCTGACAGCTCC
AAGCCGAGGATTCTGCTCATGGGACTCCGGCGCAGCGGCAAGTCCTCCATCCAGAAGGTG
GTGTTTCATAAGATGTCACCCAACGAGACCCTCTTTTTGGAAAGTACCAACAAGATTTAT
AAGGATGACATTTCCAATAGCTCCTTTGTGAATTTCCAGATATGGGATTTTCCTGGGCAA
ATGGACTTTTTTGACCCAACCTTTGACTATGAGATGATCTTCAGGGGAACAGGAGCATTG
ATATACGTCATTGACGCACAGGATGACTACATGGAGGCTTTAACAAGACTTCACATTACT
GTTTCTAAAGCCTACAAAGTTAACCCAGACATGAATTTTGAGGTTTTTATTCACAAAGTT
GATGGTCTGTCTGATGATCACAAAATAGAAACACAGAGGGACATTCATCAAAGGGCCAAT
GATGACCTTGCAGATGCTGGGCTAGAAAAACTCCATCTTAGCTTTTATCTGACTAGTATC
TATGACCATTCAATATTTGAAGCCTTTAGTAAGGTGGTGCAGAAACTCATTCCACAACTG
CCGACCTTGGAAAACCTATTAAATATCTTTATATCAAATTCAGGTATTGAAAAAGCTTTT
CTCTTTGATGTTGTCAGCAAAATCTACATTGCAACAGACAGTTCCCCTGTGGATATGCAA
TCTTATGAACTTTGCTGTGACATGATCGATGTTGTAATTGATGTGTCTTGTATATATGGG
TTAAAGGAAGATGGAAGTGGAAGTGCTTATGACAAAGAATCTATGGCAATTATCAAGCTG
AATAATACAACTGTCCTTTATTTAAAGGAGGTGACTAAATTTTTGGCACTGGTCTGCATT
CTAAGGGAAGAAAGCTTTGAAAGAAAAGGTTTAATAGACTACAACTTCCACTGTTTCCGA
AAAGCTATTCATGAGGTTTTTGAGGTGGGTGTGACTTCTCACAGGAGCTGTGGTCACCAG
ACTAGTGCCTCCAGTCTGAAAGCGCTGACACACAATGGCACGCCACGAAACGCCATCTAG
Enzyme 117 GenBank Gene ID AF272035 Link Image
Enzyme 117 GeneCard ID RRAGC Link Image
Enzyme 117 GenAtlas ID RRAGC Link Image
Enzyme 117 HGNC ID HGNC:19902 Link Image
Enzyme 117 Chromosome Location 1
Enzyme 117 Locus 1p34
Enzyme 117 SNPs SNPJam Report Link Image
Enzyme 117 General References
  1. Horwitz MS: Adenovirus immunoregulatory genes and their cellular targets. Virology. 2001 Jan 5;279(1):1-8. [PubMed Link Image]
  2. Sekiguchi T, Hirose E, Nakashima N, Ii M, Nishimoto T: Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B. J Biol Chem. 2001 Mar 9;276(10):7246-57. Epub 2000 Nov 9. [PubMed Link Image]
  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. 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. Sekiguchi T, Todaka Y, Wang Y, Hirose E, Nakashima N, Nishimoto T: A novel human nucleolar protein, Nop132, binds to the G proteins, RRAG A/C/D. J Biol Chem. 2004 Feb 27;279(9):8343-50. Epub 2003 Dec 4. [PubMed Link Image]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  8. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 117 Metabolite References Not Available
Enzyme 118 [top]
Enzyme 118 ID 14282
Enzyme 118 Name Ras-related GTP-binding protein D
Enzyme 118 Synonyms
  1. Rag D
  2. RagD
Enzyme 118 Gene Name RRAGD
Enzyme 118 Protein Sequence >Ras-related GTP-binding protein D
MSQVLGKPQPQDEDDAEEEEEEDELVGLADYGDGPDSSDADPDSGTEEGVLDFSDPFSTE
VKPRILLMGLRRSGKSSIQKVVFHKMSPNETLFLESTNKICREDVSNSSFVNFQIWDFPG
QIDFFDPTFDYEMIFRGTGALIFVIDSQDDYMEALARLHLTVTRAYKVNTDINFEVFIHK
VDGLSDDHKIETQRDIHQRANDDLADAGLEKIHLSFYLTSIYDHSIFEAFSKVVQKLIPQ
LPTLENLLNIFISNSGIEKAFLFDVVSKIYIATDSTPVDMQTYELCCDMIDVVIDISCIY
GLKEDGAGTPYDKESTAIIKLNNTTVLYLKEVTKFLALVCFVREESFERKGLIDYNFHCF
RKAIHEVFEVRMKVVKSRKVQNRLQKKKRATPNGTPRVLL
Enzyme 118 Number of Residues 400
Enzyme 118 Molecular Weight 45587.2
Enzyme 118 Theoretical pI 4.52
Enzyme 118 GO Classification
Function
  • GTP binding
  • binding
  • guanyl nucleotide binding
  • guanyl ribonucleotide binding
  • nucleotide binding
  • purine nucleotide binding
Process
Component
  • cell part
  • cytoplasm
  • intracellular membrane-bounded organelle
  • intracellular part
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 118 General Function Involved in GTP binding
Enzyme 118 Specific Function Has guanine nucleotide-binding activity but lacks intrinsic GTPase activity
Enzyme 118 Pathways Not Available
Enzyme 118 Reactions Not Available
Enzyme 118 Pfam Domain Function
Enzyme 118 Signals
  • None
Enzyme 118 Transmembrane Regions
  • None
Enzyme 118 Essentiality Not Available
Enzyme 118 GenBank ID Protein 11181620 Link Image
Enzyme 118 UniProtKB/Swiss-Prot ID Q9NQL2 Link Image
Enzyme 118 UniProtKB/Swiss-Prot Entry Name RRAGD_HUMAN Link Image
Enzyme 118 PDB ID Not Available
Enzyme 118 Cellular Location Not Available
Enzyme 118 Gene Sequence >1203 bp
ATGAGCCAGGTGCTGGGGAAGCCGCAGCCGCAGGACGAGGACGACGCGGAGGAGGAGGAG
GAGGAGGATGAGCTGGTGGGGCTAGCGGACTACGGAGACGGGCCCGACTCCTCCGACGCC
GATCCGGACAGCGGCACAGAGGAGGGAGTTCTGGACTTCAGTGACCCCTTCAGCACTGAA
GTGAAGCCGAGAATCCTGCTCATGGGCCTGAGGAGAAGCGGCAAGTCGTCTATTCAGAAA
GTTGTCTTTCACAAAATGTCTCCCAACGAAACTCTGTTCTTGGAGAGCACTAATAAGATA
TGCCGGGAAGATGTTTCCAACAGCTCCTTTGTCAATTTTCAGATTTGGGACTTCCCAGGA
CAGATTGACTTTTTTGACCCTACATTTGACTATGAGATGATCTTCCGGGGAACAGGAGCA
CTGATATTTGTCATTGACTCACAGGATGATTACATGGAAGCCCTGGCCAGGCTCCACCTC
ACGGTGACCAGGGCCTACAAAGTGAATACTGACATCAACTTCGAGGTGTTTATTCATAAA
GTGGATGGTCTGTCAGATGACCACAAAATTGAAACCCAAAGAGATATTCACCAGAGGGCA
AACGATGACCTTGCAGATGCTGGATTAGAAAAAATTCACCTCAGCTTTTATCTGACAAGC
ATATATGATCATTCAATATTTGAAGCTTTTAGCAAAGTTGTTCAGAAACTGATTCCACAA
CTCCCAACTCTGGAGAATTTGCTGAACATCTTTATCTCAAATTCTGGAATTGAAAAGGCA
TTTCTATTTGATGTGGTCAGTAAAATTTATATTGCAACTGATAGTACTCCGGTGGATATG
CAAACCTATGAGCTCTGCTGTGATATGATAGATGTGGTTATTGACATCTCTTGTATTTAT
GGTCTCAAAGAAGATGGAGCAGGAACCCCCTATGACAAGGAATCCACAGCCATCATAAAG
CTTAATAATACAACCGTGCTTTATTTAAAAGAGGTGACAAAGTTCCTGGCTCTCGTTTGC
TTTGTCAGAGAGGAAAGCTTTGAAAGAAAAGGGCTAATTGACTATAATTTTCATTGCTTC
CGGAAGGCCATTCATGAAGTTTTTGAGGTGAGAATGAAAGTAGTAAAATCTCGAAAGGTT
CAGAATCGGCTGCAGAAGAAAAAGAGAGCCACCCCTAATGGGACCCCTAGAGTGCTGCTG
TAG
Enzyme 118 GenBank Gene ID AF272036 Link Image
Enzyme 118 GeneCard ID RRAGD Link Image
Enzyme 118 GenAtlas ID RRAGD Link Image
Enzyme 118 HGNC ID HGNC:19903 Link Image
Enzyme 118 Chromosome Location 6
Enzyme 118 Locus 6q15-q16
Enzyme 118 SNPs SNPJam Report Link Image
Enzyme 118 General References
  1. Sekiguchi T, Hirose E, Nakashima N, Ii M, Nishimoto T: Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B. J Biol Chem. 2001 Mar 9;276(10):7246-57. Epub 2000 Nov 9. [PubMed Link Image]
  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. 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. 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. Sekiguchi T, Todaka Y, Wang Y, Hirose E, Nakashima N, Nishimoto T: A novel human nucleolar protein, Nop132, binds to the G proteins, RRAG A/C/D. J Biol Chem. 2004 Feb 27;279(9):8343-50. Epub 2003 Dec 4. [PubMed Link Image]
Enzyme 118 Metabolite References Not Available
Enzyme 119 [top]
Enzyme 119 ID 14299
Enzyme 119 Name Secretion-regulating guanine nucleotide exchange factor
Enzyme 119 Synonyms
  1. Deafness locus-associated putative guanine nucleotide exchange factor
  2. DelGEF
  3. Guanine nucleotide exchange factor-related protein
Enzyme 119 Gene Name SERGEF
Enzyme 119 Protein Sequence >Secretion-regulating guanine nucleotide exchange factor
MEREPSASEAAPAAAALFAWGANSYGQLGLGHKEDVLLPQQLNDFCKPRSVRRITGGGGH
SAVVTDGGDLFVCGLNKDGQLGLGHTEDIPYFTPCKSLFGCPIQQVACGWDFTIMLTENG
QVLSCGSNSFGQLGVPHGPRRCVVPQAIELHKEKVVCIAAGLRHAVAATASGIVFQWGTG
LASCGRRLCPGQTLPLFFTAKEPSRVTGLENSKAMCVLAGSDHSASLTDAGEVYVWGSNK
HGQLANEAAFLPVPQKIEAHCFQNEKVTAIWSGWTHLVAQTETGKMFTWGRADYGQLGRK
LETYEGWKLEKQDSFLPCSRPPNSMPSSPHCLTGATEVSCGSEHNLAIIGGVCYSWGWNE
HGMCGDGTEANVWAPKPVQALLSSSGLLVGCGAGHSLALCQLPAHPALVQDPKVTYLSPD
AIEDTESQKAMDKERNWKERQSETSTQSQSDWSRNGGL
Enzyme 119 Number of Residues 458
Enzyme 119 Molecular Weight 48981.0
Enzyme 119 Theoretical pI 6.44
Enzyme 119 GO Classification Not Available
Enzyme 119 General Function Involved in protein binding
Enzyme 119 Specific Function Probable guanine nucleotide exchange factor (GEF), which may be involved in the secretion process
Enzyme 119 Pathways Not Available
Enzyme 119 Reactions Not Available
Enzyme 119 Pfam Domain Function
Enzyme 119 Signals
  • None
Enzyme 119 Transmembrane Regions
  • None
Enzyme 119 Essentiality Not Available
Enzyme 119 GenBank ID Protein 6434157 Link Image
Enzyme 119 UniProtKB/Swiss-Prot ID Q9UGK8 Link Image
Enzyme 119 UniProtKB/Swiss-Prot Entry Name SRGEF_HUMAN Link Image
Enzyme 119 PDB ID Not Available
Enzyme 119 Cellular Location Not Available
Enzyme 119 Gene Sequence >1377 bp
ATGGAGCGCGAGCCCAGCGCCTCGGAGGCCGCCCCCGCGGCGGCCGCGCTCTTCGCCTGG
GGTGCAAATAGCTATGGGCAACTTGGCCTCGGCCATAAGGAAGATGTGCTGTTGCCCCAG
CAACTGAATGACTTCTGTAAACCCAGGAGTGTCAGGAGGATCACAGGAGGAGGGGGCCAC
TCTGCAGTTGTCACAGATGGAGGAGACCTCTTTGTTTGTGGCCTGAACAAAGATGGGCAA
CTGGGGCTTGGTCACACAGAGGATATCCCATATTTTACCCCCTGCAAATCCCTCTTTGGC
TGTCCCATCCAACAGGTGGCCTGTGGCTGGGATTTTACGATTATGCTCACAGAAAATGGT
CAAGTTCTATCATGTGGATCCAACTCCTTTGGCCAGTTAGGAGTTCCTCATGGACCTCGA
AGATGTGTGGTTCCCCAGGCCATTGAGCTCCATAAAGAGAAGGTTGTTTGTATTGCTGCT
GGACTGAGGCATGCAGTAGCTGCTACAGCGAGTGGCATCGTGTTCCAGTGGGGGACTGGT
TTGGCATCATGTGGACGACGGTTGTGCCCTGGGCAGACTCTTCCATTGTTTTTCACAGCA
AAGGAACCAAGCAGAGTGACAGGTCTAGAGAATTCTAAAGCAATGTGTGTTCTTGCTGGC
TCAGACCACTCAGCTTCATTAACAGATGCAGGAGAGGTGTATGTTTGGGGAAGCAACAAG
CATGGGCAACTGGCTAATGAGGCTGCTTTCCTTCCTGTGCCCCAGAAAATAGAAGCACAT
TGTTTCCAGAATGAAAAGGTCACTGCCATCTGGAGTGGATGGACACACCTGGTTGCCCAG
ACAGAAACTGGCAAGATGTTTACCTGGGGCCGAGCAGACTATGGTCAGCTAGGGAGGAAG
TTGGAGACTTATGAAGGCTGGAAACTAGAAAAGCAAGATTCATTTCTCCCCTGTTCAAGA
CCACCGAACAGCATGCCTTCATCTCCGCATTGCTTAACTGGAGCAACTGAGGTCTCTTGT
GGCTCAGAGCATAATTTGGCAATAATTGGTGGAGTGTGTTACTCTTGGGGCTGGAATGAG
CATGGCATGTGCGGAGATGGCACTGAAGCCAACGTCTGGGCCCCAAAGCCGGTGCAGGCT
CTGCTGTCATCGTCAGGACTCCTTGTGGGCTGTGGGGCTGGCCACTCCTTGGCCCTCTGC
CAGCTGCCAGCTCACCCTGCATTGGTCCAGGACCCCAAGGTCACCTACCTTTCCCCAGAT
GCCATCGAGGACACTGAATCTCAGAAAGCCATGGACAAAGAGAGAAACTGGAAGGAAAGA
CAATCAGAAACTTCAACCCAAAGCCAATCTGACTGGTCCAGAAATGGGGGACTGTGA
Enzyme 119 GenBank Gene ID AJ243950 Link Image
Enzyme 119 GeneCard ID SERGEF Link Image
Enzyme 119 GenAtlas ID SERGEF Link Image
Enzyme 119 HGNC ID HGNC:17499 Link Image
Enzyme 119 Chromosome Location 1
Enzyme 119 Locus 11p14.3
Enzyme 119 SNPs SNPJam Report Link Image
Enzyme 119 General References
  1. Uhlmann J, Wiemann S, Ponstingl H: DelGEF, an RCC1-related protein encoded by a gene on chromosome 11p14 critical for two forms of hereditary deafness. FEBS Lett. 1999 Oct 22;460(1):153-60. [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. Sjolinder M, Uhlmann J, Ponstingl H: DelGEF, a homologue of the Ran guanine nucleotide exchange factor RanGEF, binds to the exocyst component Sec5 and modulates secretion. FEBS Lett. 2002 Dec 4;532(1-2):211-5. [PubMed Link Image]
  4. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
Enzyme 119 Metabolite References Not Available
Enzyme 120 [top]
Enzyme 120 ID 14324
Enzyme 120 Name T-lymphoma invasion and metastasis-inducing protein 2
Enzyme 120 Synonyms
  1. TIAM-2
  2. SIF and TIAM1-like exchange factor
Enzyme 120 Gene Name TIAM2
Enzyme 120 Protein Sequence >T-lymphoma invasion and metastasis-inducing protein 2
MGNSDSQYTLQGSKNHSNTITGAKQIPCSLKIRGIHAKEEKSLHGWGHGSNGAGYKSRSL
ARSCLSHFKSNQPYASRLGGPTCKVSRGVAYSTHRTNAPGKDFQGISAAFSTENGFHSVG
HELADNHITSRDCNGHLLNCYGRNESIASTPPGEDRKSPRVLIKTLGKLDGCLRVEFHNG
GNPSKVPAEDCSEPVQLLRYSPTLASETSPVPEARRGSSADSLPSHRPSPTDSRLRSSKG
SSLSSESSWYDSPWGNAGELSEAEGSFLAPGMPDPSLHASFPPGDAKKPFNQSSSLSSLR
ELYKDANLGSLSPSGIRLSDEYMGTHASLSNRVSFASDIDVPSRVAHGDPIQYSSFTLPC
RKPKAFVEDTAKKDSLKARMRRISDWTGSLSRKKRKLQEPRSKEGSDYFDSRSDGLNTDV
QGSSQASAFLWSGGSTQILSQRSESTHAIGSDPLRQNIYENFMRELEMSRTNTENIETST
ETAESSSESLSSLEQLDLLFEKEQGVVRKAGWLFFKPLVTVQKERKLELVARRKWKQYWV
TLKGCTLLFYETYGKNSMDQSSAPRCALFAEDSIVQSVPEHPKKENVFCLSNSFGDVYLF
QATSQTDLENWVTAVHSACASLFAKKHGKEDTLRLLKNQTKNLLQKIDMDSKMKKMAELQ
LSVVSDPKNRKAIENQIQQWEQNLEKFHMDLFRMRCYLASLQGGELPNPKSLLAAASRPS
KLALGRLGILSVSSFHALVCSRDDSALRKRTLSLTQRGRNKKGIFSSLKGLDTLARKGKE
KRPSITQVDELLHIYGSTVDGVPRDNAWEIQTYVHFQDNHGVTVGIKPEHRVEDILTLAC
KMRQLEPSHYGLQLRKLVDDNVEYCIPAPYEYMQQQVYDEIEVFPLNVYDVQLTKTGSVC
DFGFAVTAQVDERQHLSRIFISDVLPDGLAYGEGLRKGNEIMTLNGEAVSDLDLKQMEAL
FSEKSVGLTLIARPPDTKATLCTSWSDSDLFSRDQKSLLPPPNQSQLLEEFLDNFKKNTA
NDFSNVPDITTGLKRSQTDGTLDQVSHREKMEQTFRSAEQITALCRSFNDSQANGMEGPR
ENQDPPPRSLARHLSDADRLRKVIQELVDTEKSYVKDLSCLFELYLEPLQNETFLTQDEM
ESLFGSLPEMLEFQKVFLETLEDGISASSDFNTLETPSQFRKLLFSLGGSFLYYADHFKL
YSGFCANHIKVQKVLERAKTDKAFKAFLDARNPTKQHSSTLESYLIKPVQRVLKYPLLLK
ELVSLTDQESEEHYHLTEALKAMEKVASHINEMQKIYEDYGTVFDQLVAEQSGTEKEVTE
LSMGELLMHSTVSWLNPFLSLGKARKDLELTVFVFKRAVILVYKENCKLKKKLPSNSRPA
HNSTDLDPFKFRWLIPISALQVRLGNPAGTENNSIWELIHTKSEIEGRPETIFQLCCSDS
ESKTNIVKVIRSILRENFRRHIKCELPLEKTCKDRLVPLKNRVPVSAKLASSRSLKVLKN
SSSNEWTGETGKGTLLDSDEGSLSSGTQSSGCPTAEGRQDSKSTSPGKYPHPGLADFADN
LIKESDILSDEDDDHRQTVKQGSPTKDIEIQFQRLRISEDPDVHPEAEQQPGPESGEGQK
GGEQPKLVRGHFCPIKRKANSTKRDRGTLLKAQIRHQSLDSQSENATIDLNSVLEREFSV
QSLTSVVSEECFYETESHGKS
Enzyme 120 Number of Residues 1701
Enzyme 120 Molecular Weight 190101.0
Enzyme 120 Theoretical pI 7.21
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
  • molecular transducer activity
  • nucleoside-triphosphatase regulator activity
  • protein binding
  • receptor signaling protein activity
  • signal transducer 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
  • signal transduction
  • signaling
  • signaling pathway
Component
  • cell part
  • intracellular
Enzyme 120 General Function Involved in Rho guanyl-nucleotide exchange factor activity
Enzyme 120 Specific Function Modulates the activity of RHO-like proteins and connects extracellular signals to cytoskeletal activities. Acts as a GDP- dissociation stimulator protein that stimulates the GDP-GTP exchange activity of RHO-like GTPases and activates them. Mediates extracellular laminin signals to activate Rac1, contributing to neurite growth. Involved in lamellipodial formation and advancement of the growth cone of embryonic hippocampal neurons. Promotes migration of neurons in the cerebral cortex. When overexpressed, induces membrane ruffling accompanied by the accumulation of actin filaments along the altered plasma membrane. Activates specifically RAC1, but not CDC42 and RHOA
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 58331187 Link Image
Enzyme 120 UniProtKB/Swiss-Prot ID Q8IVF5 Link Image
Enzyme 120 UniProtKB/Swiss-Prot Entry Name TIAM2_HUMAN Link Image
Enzyme 120 PDB ID Not Available
Enzyme 120 Cellular Location Not Available
Enzyme 120 Gene Sequence >5106 bp
ATGGGCAACTCCGACAGTCAGTACACCCTTCAAGGATCTAAAAATCATAGCAATACTATT
ACTGGTGCTAAGCAAATTCCTTGCTCCCTGAAAATACGTGGCATTCATGCAAAAGAGGAA
AAGTCATTGCATGGATGGGGTCACGGAAGCAACGGAGCAGGTTACAAGTCCAGGTCCCTG
GCCCGAAGCTGCCTTTCTCACTTTAAGAGTAACCAGCCTTACGCATCGAGACTCGGTGGC
CCCACATGCAAGGTCTCCAGAGGTGTTGCCTACTCCACGCACAGGACAAATGCCCCAGGG
AAGGATTTCCAGGGCATCAGTGCTGCTTTCTCAACTGAGAATGGCTTCCACTCTGTTGGC
CACGAGCTGGCAGATAACCACATCACCTCCAGAGACTGCAACGGACACCTTCTCAACTGC
TACGGGAGGAATGAGAGCATTGCCTCCACCCCACCGGGCGAAGACCGCAAGAGCCCCCGA
GTGCTCATCAAAACGCTGGGGAAGCTGGATGGGTGTTTAAGGGTCGAGTTCCACAATGGT
GGCAACCCCAGCAAAGTGCCTGCAGAGGACTGCAGTGAGCCGGTGCAGCTGCTGAGGTAC
TCACCTACCTTAGCATCGGAAACCTCCCCTGTGCCTGAAGCCAGGAGGGGGTCCAGCGCC
GATTCCCTGCCCAGCCATCGCCCCTCTCCCACGGACTCTCGCCTGCGGTCCAGCAAAGGC
AGCTCCCTGAGTTCTGAGTCATCCTGGTACGACTCCCCTTGGGGCAATGCTGGAGAGCTG
AGCGAGGCTGAGGGCTCCTTCCTGGCCCCCGGCATGCCTGACCCCAGTCTCCATGCCAGC
TTCCCACCTGGCGATGCCAAAAAGCCTTTCAACCAAAGCTCTTCCCTCTCCTCCCTCCGG
GAACTGTACAAAGATGCCAACCTGGGGAGCCTCTCCCCCTCAGGTATCCGCCTTTCTGAT
GAATACATGGGCACGCATGCCAGCCTGAGCAACCGTGTCTCTTTTGCTTCCGACATTGAT
GTGCCCTCCAGAGTGGCACACGGGGACCCCATCCAGTACAGTTCCTTCACTCTCCCCTGT
CGGAAGCCCAAAGCCTTTGTTGAGGATACTGCGAAGAAGGACTCCCTCAAAGCCAGGATG
CGACGGATCAGTGACTGGACGGGAAGCCTCTCAAGGAAGAAAAGGAAACTCCAGGAGCCG
AGGTCCAAGGAGGGCAGTGACTACTTTGACAGTCGCTCTGATGGACTGAATACAGATGTG
CAGGGATCCTCCCAGGCATCTGCTTTTCTGTGGTCAGGGGGCTCTACTCAGATCCTGTCT
CAGAGAAGTGAATCCACACATGCGATTGGCAGCGATCCCCTCCGGCAGAACATTTATGAG
AATTTCATGCGAGAGTTGGAAATGAGCAGGACCAACACTGAGAACATAGAAACATCTACA
GAAACCGCCGAGTCCAGCAGCGAGTCACTCAGCTCTCTGGAACAGCTGGATCTGCTCTTT
GAGAAGGAACAGGGGGTGGTCCGGAAGGCCGGGTGGCTCTTCTTCAAGCCCCTGGTCACT
GTGCAGAAGGAAAGGAAGCTTGAGCTGGTGGCACGAAGGAAATGGAAACAGTACTGGGTA
ACGCTGAAAGGATGCACGCTGCTGTTTTATGAGACCTATGGGAAGAATTCCATGGATCAG
AGCAGTGCCCCTCGGTGTGCTCTGTTTGCAGAAGACAGCATAGTGCAGTCTGTTCCAGAG
CATCCCAAGAAAGAAAATGTGTTCTGCCTCAGCAACTCCTTTGGAGATGTCTACCTTTTC
CAGGCCACCAGCCAGACAGATCTAGAAAACTGGGTCACTGCTGTACACTCTGCTTGTGCA
TCCCTTTTTGCAAAGAAGCATGGGAAAGAGGACACGCTGCGGCTGCTGAAGAACCAGACC
AAAAACCTGCTTCAGAAGATAGACATGGACAGCAAGATGAAGAAGATGGCAGAGCTGCAG
CTGTCCGTGGTGAGCGACCCAAAGAACAGGAAAGCCATAGAGAACCAGATCCAGCAATGG
GAGCAGAATCTTGAGAAATTTCACATGGATCTGTTCAGGATGCGCTGCTATCTGGCCAGC
CTACAAGGTGGGGAGTTACCGAACCCAAAGAGTCTCCTTGCAGCCGCCAGCCGCCCCTCC
AAGCTGGCCCTCGGCAGGCTGGGCATCTTGTCTGTTTCCTCTTTCCATGCTCTGGTATGT
TCTAGAGATGACTCTGCTCTCCGGAAAAGGACACTGTCACTGACCCAGCGAGGGAGAAAC
AAGAAGGGAATATTTTCTTCGTTAAAAGGGCTGGACACACTGGCCAGAAAAGGCAAGGAG
AAGAGACCTTCTATAACTCAGGTCGATGAACTTCTGCATATATATGGTTCAACAGTAGAC
GGTGTTCCCCGAGACAATGCATGGGAAATCCAGACTTATGTCCACTTTCAGGACAATCAC
GGAGTTACTGTAGGGATCAAGCCAGAGCACAGAGTAGAAGATATTTTGACTTTGGCATGC
AAGATGAGGCAGTTGGAACCCAGCCATTATGGCCTACAGCTTCGAAAATTAGTAGATGAC
AATGTTGAGTATTGCATCCCTGCACCATATGAATATATGCAACAACAGGTTTATGATGAA
ATAGAAGTCTTTCCACTAAATGTTTATGACGTGCAGCTCACGAAGACTGGGAGTGTGTGT
GACTTTGGGTTTGCAGTTACAGCGCAGGTGGATGAGCGTCAGCATCTCAGCCGGATATTT
ATAAGCGACGTTCTTCCCGATGGCCTGGCGTATGGGGAAGGGCTGAGAAAGGGCAATGAG
ATCATGACCTTAAATGGGGAAGCTGTGTCTGATCTTGACCTTAAGCAGATGGAGGCCCTG
TTTTCTGAGAAGAGCGTCGGACTCACTCTGATTGCCCGGCCTCCGGACACAAAAGCAACC
CTGTGTACATCCTGGTCAGACAGTGACCTGTTCTCCAGGGACCAGAAGAGTCTGCTGCCC
CCTCCTAACCAGTCCCAACTGCTGGAGGAATTCCTGGATAACTTTAAAAAGAATACAGCC
AATGATTTCAGCAACGTCCCTGATATCACAACAGGTCTGAAAAGGAGTCAGACAGATGGC
ACTCTGGATCAGGTTTCCCACAGGGAGAAAATGGAGCAGACATTCAGGAGTGCTGAGCAG
ATCACTGCACTGTGCAGGAGTTTTAACGACAGTCAGGCCAACGGCATGGAAGGACCGCGG
GAGAATCAGGATCCTCCTCCGAGGCCTCTGGCCCGCCACCTGTCTGATGCAGACCGCCTC
CGCAAAGTCATCCAGGAGCTTGTGGACACAGAGAAGTCCTACGTGAAGGATTTGAGCTGC
CTCTTTGAATTATACTTGGAGCCACTTCAGAATGAGACCTTTCTTACCCAAGATGAGATG
GAGTCACTTTTTGGAAGTTTGCCAGAGATGCTTGAGTTTCAGAAGGTGTTTCTGGAGACC
CTGGAGGATGGGATTTCAGCATCATCTGACTTTAACACCCTAGAAACCCCCTCACAGTTT
AGAAAATTACTGTTTTCCCTTGGAGGCTCTTTCCTTTATTACGCGGACCACTTTAAACTG
TACAGTGGATTCTGTGCTAACCATATCAAAGTACAGAAGGTTCTGGAGCGAGCTAAAACT
GACAAAGCCTTCAAGGCTTTTCTGGACGCCCGGAACCCCACCAAGCAGCATTCCTCCACG
CTGGAGTCCTACCTCATCAAGCCGGTTCAGAGAGTGCTCAAGTACCCGCTGCTGCTCAAG
GAGCTGGTGTCCCTGACGGACCAGGAGAGCGAGGAGCACTACCACCTGACGGAAGCACTA
AAGGCAATGGAGAAAGTAGCGAGCCACATCAATGAGATGCAGAAGATCTATGAGGATTAT
GGGACCGTGTTTGACCAGCTAGTAGCTGAGCAGAGCGGAACAGAGAAGGAGGTAACAGAA
CTTTCGATGGGAGAGCTTCTGATGCACTCTACGGTTTCCTGGTTGAATCCATTTCTGTCT
CTAGGAAAAGCTAGAAAGGACCTTGAGCTCACAGTATTTGTTTTTAAGAGAGCCGTCATA
CTGGTTTATAAAGAAAACTGCAAACTGAAAAAGAAATTGCCCTCGAATTCCCGGCCTGCA
CACAACTCTACTGACTTGGACCCATTTAAATTCCGCTGGTTGATCCCCATCTCCGCGCTT
CAAGTCAGACTGGGGAATCCAGCAGGGACAGAAAATAATTCCATATGGGAACTGATCCAT
ACGAAGTCAGAAATAGAAGGACGGCCAGAAACCATCTTTCAGTTGTGTTGCAGTGACAGT
GAAAGCAAAACCAACATTGTTAAGGTGATTCGTTCTATTCTGAGGGAGAACTTCAGGCGT
CACATAAAGTGTGAATTACCACTGGAGAAAACGTGTAAGGATCGCCTGGTACCTCTTAAG
AACCGAGTTCCTGTTTCGGCCAAATTAGCTTCATCCAGGTCTTTAAAAGTCCTGAAGAAT
TCCTCCAGCAACGAGTGGACCGGTGAGACTGGCAAGGGAACCTTGCTGGACTCTGACGAG
GGCAGCTTGAGCAGCGGCACCCAGAGCAGCGGCTGCCCCACGGCTGAGGGCAGGCAGGAC
TCCAAGAGCACTTCTCCCGGGAAATACCCACACCCCGGCTTGGCAGATTTTGCCGACAAT
CTCATCAAAGAGAGTGACATCCTGAGCGATGAAGATGATGACCACCGTCAGACTGTGAAG
CAGGGCAGCCCTACTAAAGACATCGAAATTCAGTTCCAGAGACTGAGGATTTCCGAGGAC
CCAGACGTTCACCCCGAGGCTGAGCAGCAGCCTGGCCCGGAGTCGGGTGAGGGTCAGAAA
GGAGGAGAGCAGCCCAAACTGGTCCGGGGGCACTTCTGCCCCATTAAACGAAAAGCCAAC
AGCACCAAGAGGGACAGAGGAACTTTGCTCAAGGCGCAGATCCGTCACCAGTCCCTTGAC
AGTCAGTCTGAAAATGCCACCATCGACCTAAATTCTGTTCTAGAGCGAGAATTCAGTGTC
CAGAGTTTAACATCTGTTGTCAGTGAGGAGTGTTTTTATGAAACAGAGAGCCACGGAAAA
TCATAG
Enzyme 120 GenBank Gene ID NM_012454.3 Link Image
Enzyme 120 GeneCard ID TIAM2 Link Image
Enzyme 120 GenAtlas ID TIAM2 Link Image
Enzyme 120 HGNC ID HGNC:11806 Link Image
Enzyme 120 Chromosome Location 6
Enzyme 120 Locus 6q25.2
Enzyme 120 SNPs SNPJam Report Link Image
Enzyme 120 General References
  1. Chiu CY, Leng S, Martin KA, Kim E, Gorman S, Duhl DM: Cloning and characterization of T-cell lymphoma invasion and metastasis 2 (TIAM2), a novel guanine nucleotide exchange factor related to TIAM1. Genomics. 1999 Oct 1;61(1):66-73. [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. 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. 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]
Enzyme 120 Metabolite References Not Available
Enzyme 121 [top]
Enzyme 121 ID 14338
Enzyme 121 Name Protein XRP2
Enzyme 121 Synonyms Not Available
Enzyme 121 Gene Name RP2
Enzyme 121 Protein Sequence >Protein XRP2
MGCFFSKRRKADKESRPENEEERPKQYSWDQREKVDPKDYMFSGLKDETVGRLPGTVAGQ
QFLIQDCENCNIYIFDHSATVTIDDCTNCIIFLGPVKGSVFFRNCRDCKCTLACQQFRVR
DCRKLEVFLCCATQPIIESSSNIKFGCFQWYYPELAFQFKDAGLSIFNNTWSNIHDFTPV
SGELNWSLLPEDAVVQDYVPIPTTEELKAVRVSTEANRSIVPISRGQRQKSSDESCLVVL
FAGDYTIANARKLIDEMVGKGFFLVQTKEVSMKAEDAQRVFREKAPDFLPLLNKGPVIAL
EFNGDGAVEVCQLIVNEIFNGTKMFVSESKETASGDVDSFYNFADIQMGI
Enzyme 121 Number of Residues 350
Enzyme 121 Molecular Weight 39640.7
Enzyme 121 Theoretical pI 4.73
Enzyme 121 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 121 General Function Involved in cell morphogenesis
Enzyme 121 Specific Function Stimulates the GTPase activity of tubulin, but does not enhance tubulin heterodimerization. Acts as guanine nucleotide dissociation inhibitor for ARL3
Enzyme 121 Pathways Not Available
Enzyme 121 Reactions Not Available
Enzyme 121 Pfam Domain Function
Enzyme 121 Signals
  • None
Enzyme 121 Transmembrane Regions
  • None
Enzyme 121 Essentiality Not Available
Enzyme 121 GenBank ID Protein 3550283 Link Image
Enzyme 121 UniProtKB/Swiss-Prot ID O75695 Link Image
Enzyme 121 UniProtKB/Swiss-Prot Entry Name XRP2_HUMAN Link Image
Enzyme 121 PDB ID Not Available
Enzyme 121 Cellular Location Not Available
Enzyme 121 Gene Sequence >1053 bp
ATGGGCTGCTTCTTCTCCAAGAGACGGAAGGCTGACAAGGAGTCGCGGCCCGAGAACGAG
GAGGAGCGGCCAAAGCAGTACAGCTGGGATCAGCGCGAGAAGGTTGATCCAAAAGACTAC
ATGTTCAGTGGACTGAAGGATGAAACAGTAGGTCGCTTACCTGGGACGGTAGCAGGACAA
CAGTTTCTCATTCAAGACTGTGAGAACTGTAACATCTATATTTTTGATCACTCTGCTACA
GTTACCATTGATGACTGTACTAACTGCATAATTTTTCTGGGACCCGTGAAAGGCAGCGTG
TTTTTCCGGAATTGCAGAGATTGCAAGTGCACATTAGCCTGCCAACAATTTCGTGTGCGA
GATTGTAGAAAGCTGGAAGTCTTTTTGTGTTGTGCCACTCAACCCATCATTGAGTCTTCC
TCAAATATCAAATTTGGATGTTTTCAATGGTACTATCCTGAATTAGCTTTCCAGTTCAAA
GATGCAGGGCTAAGTATCTTCGACAATACATGGAGTAACATTCATGACTTTACACCTGTG
TCAGGAGAACTCAACTGGAGCCTTCTTCCAGAAGATGCTGTGGTTCAGGACTATGTTCCT
ATACCTACTACCGAAGAGCTCAAAGCTGTTCGTGTTTCCACAGAAGCCAATAGAAGCATT
GTTCCAATATCCCGGGGTCAGAGACAGAAGAGCAGCGATGAATCATGCTTAGTGGTATTA
TTTGCTGGTGATTACACTATTGCAAATGCCAGAAAACTAATTGATGAGATGGTTGGTAAA
GGCTTTTTCCTAGTTCAGACAAAGGAAGTGTCCATGAAAGCTGAGGATGCTCAAAGGGTT
TTTCGGGAAAAAGCACCTGACTTCCTTCCTCTTCTGAACAAAGGTCCTGTTATTGCCTTG
GAGTTTAATGGGGATGGTGCTGTAGAAGTATGTCAACTTATTGTAAACGAGATATTCAAT
GGGACCAAGATGTTTGTATCTGAAAGCAAGGAGACGGCATCTGGAGATGTAGACAGCTTC
TACAACTTTGCTGATATACAGATGGGAATATGA
Enzyme 121 GenBank Gene ID AJ007590 Link Image
Enzyme 121 GeneCard ID RP2 Link Image
Enzyme 121 GenAtlas ID RP2 Link Image
Enzyme 121 HGNC ID HGNC:10274 Link Image
Enzyme 121 Chromosome Location Not Available
Enzyme 121 Locus Not Available
Enzyme 121 SNPs SNPJam Report Link Image
Enzyme 121 General References
  1. Schwahn U, Lenzner S, Dong J, Feil S, Hinzmann B, van Duijnhoven G, Kirschner R, Hemberger M, Bergen AA, Rosenberg T, Pinckers AJ, Fundele R, Rosenthal A, Cremers FP, Ropers HH, Berger W: Positional cloning of the gene for X-linked retinitis pigmentosa 2. Nat Genet. 1998 Aug;19(4):327-32. [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. 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. Chapple JP, Hardcastle AJ, Grayson C, Spackman LA, Willison KR, Cheetham ME: Mutations in the N-terminus of the X-linked retinitis pigmentosa protein RP2 interfere with the normal targeting of the protein to the plasma membrane. Hum Mol Genet. 2000 Aug 12;9(13):1919-26. [PubMed Link Image]
  5. Bartolini F, Bhamidipati A, Thomas S, Schwahn U, Lewis SA, Cowan NJ: Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C. J Biol Chem. 2002 Apr 26;277(17):14629-34. Epub 2002 Feb 14. [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. Kuhnel K, Veltel S, Schlichting I, Wittinghofer A: Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3. Structure. 2006 Feb;14(2):367-78. [PubMed Link Image]
  8. Hardcastle AJ, Thiselton DL, Van Maldergem L, Saha BK, Jay M, Plant C, Taylor R, Bird AC, Bhattacharya S: Mutations in the RP2 gene cause disease in 10% of families with familial X-linked retinitis pigmentosa assessed in this study. Am J Hum Genet. 1999 Apr;64(4):1210-5. [PubMed Link Image]
  9. Rosenberg T, Schwahn U, Feil S, Berger W: Genotype-phenotype correlation in X-linked retinitis pigmentosa 2 (RP2). Ophthalmic Genet. 1999 Sep;20(3):161-72. [PubMed Link Image]
  10. Thiselton DL, Zito I, Plant C, Jay M, Hodgson SV, Bird AC, Bhattacharya SS, Hardcastle AJ: Novel frameshift mutations in the RP2 gene and polymorphic variants. Hum Mutat. 2000 Jun;15(6):580. [PubMed Link Image]
  11. Wada Y, Nakazawa M, Abe T, Tamai M: A new Leu253Arg mutation in the RP2 gene in a Japanese family with X-linked retinitis pigmentosa. Invest Ophthalmol Vis Sci. 2000 Jan;41(1):290-3. [PubMed Link Image]
  12. Sharon D, Bruns GA, McGee TL, Sandberg MA, Berson EL, Dryja TP: X-linked retinitis pigmentosa: mutation spectrum of the RPGR and RP2 genes and correlation with visual function. Invest Ophthalmol Vis Sci. 2000 Aug;41(9):2712-21. [PubMed Link Image]
  13. Miano MG, Testa F, Filippini F, Trujillo M, Conte I, Lanzara C, Millan JM, De Bernardo C, Grammatico B, Mangino M, Torrente I, Carrozzo R, Simonelli F, Rinaldi E, Ventruto V, D'Urso M, Ayuso C, Ciccodicola A: Identification of novel RP2 mutations in a subset of X-linked retinitis pigmentosa families and prediction of new domains. Hum Mutat. 2001 Aug;18(2):109-19. [PubMed Link Image]
  14. Breuer DK, Yashar BM, Filippova E, Hiriyanna S, Lyons RH, Mears AJ, Asaye B, Acar C, Vervoort R, Wright AF, Musarella MA, Wheeler P, MacDonald I, Iannaccone A, Birch D, Hoffman DR, Fishman GA, Heckenlively JR, Jacobson SG, Sieving PA, Swaroop A: A comprehensive mutation analysis of RP2 and RPGR in a North American cohort of families with X-linked retinitis pigmentosa. Am J Hum Genet. 2002 Jun;70(6):1545-54. Epub 2002 Apr 30. [PubMed Link Image]
  15. Sharon D, Sandberg MA, Rabe VW, Stillberger M, Dryja TP, Berson EL: RP2 and RPGR mutations and clinical correlations in patients with X-linked retinitis pigmentosa. Am J Hum Genet. 2003 Nov;73(5):1131-46. Epub 2003 Oct 16. [PubMed Link Image]
  16. Bader I, Brandau O, Achatz H, Apfelstedt-Sylla E, Hergersberg M, Lorenz B, Wissinger B, Wittwer B, Rudolph G, Meindl A, Meitinger T: X-linked retinitis pigmentosa: RPGR mutations in most families with definite X linkage and clustering of mutations in a short sequence stretch of exon ORF15. Invest Ophthalmol Vis Sci. 2003 Apr;44(4):1458-63. [PubMed Link Image]
Enzyme 121 Metabolite References Not Available
Enzyme 122 [top]
Enzyme 122 ID 14868
Enzyme 122 Name Rho-related GTP-binding protein RhoU
Enzyme 122 Synonyms
  1. CDC42-like GTPase 1
  2. GTP-binding protein-like 1
  3. Rho GTPase-like protein ARHU
  4. Ryu GTPase
  5. Wnt-1 responsive Cdc42 homolog 1
  6. WRCH-1
Enzyme 122 Gene Name RHOU
Enzyme 122 Protein Sequence >Rho-related GTP-binding protein RhoU
MPPQQGDPAFPDRCEAPPVPPRRERGGRGGRGPGEPGGRGRAGGAEGRGVKCVLVGDGAV
GKTSLVVSYTTNGYPTEYIPTAFDNFSAVVSVDGRPVRLQLCDTAGQDEFDKLRPLCYTN
TDIFLLCFSVVSPSSFQNVSEKWVPEIRCHCPKAPIILVGTQSDLREDVKVLIELDKCKE
KPVPEEAAKLCAEEIKAASYIECSALTQKNLKEVFDAAIVAGIQYSDTQQQPKKSKSRTP
DKMKNLSKSWWKKYCCFV
Enzyme 122 Number of Residues 258
Enzyme 122 Molecular Weight 28218.0
Enzyme 122 Theoretical pI 8.14
Enzyme 122 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 122 General Function Involved in GTP binding
Enzyme 122 Specific Function Acts upstream of PAK1 to regulate the actin cytoskeleton, adhesion turnover and increase cell migration. Stimulates quiescent cells to reenter the cell cycle. Has no detectable GTPase activity but its high intrinsic guanine nucleotide exchange activity suggests it is constitutively GTP- bound
Enzyme 122 Pathways Not Available
Enzyme 122 Reactions Not Available
Enzyme 122 Pfam Domain Function
Enzyme 122 Signals
  • None
Enzyme 122 Transmembrane Regions
  • None
Enzyme 122 Essentiality Not Available
Enzyme 122 GenBank ID Protein Not Available
Enzyme 122 UniProtKB/Swiss-Prot ID Q7L0Q8 Link Image
Enzyme 122 UniProtKB/Swiss-Prot Entry Name RHOU_HUMAN Link Image
Enzyme 122 PDB ID Not Available
Enzyme 122 Cellular Location Not Available
Enzyme 122 Gene Sequence >777 bp
ATGCCCCCGCAGCAGGGGGACCCCGCGTTCCCCGACCGCTGCGAGGCGCCTCCGGTGCCG
CCGCGTCGGGAGCGCGGTGGACGCGGGGGACGCGGGCCTGGGGAGCCGGGGGGCCGGGGG
CGTGCGGGGGGTGCCGAGGGGCGCGGCGTCAAGTGCGTGCTGGTCGGCGACGGCGCGGTG
GGCAAGACGAGCCTGGTGGTGAGTTACACCACCAACGGCTACCCCACCGAGTACATCCCT
ACTGCCTTCGACAACTTCTCCGCGGTGGTGTCTGTGGATGGGCGGCCCGTGAGACTCCAA
CTCTGTGACACTGCCGGACAGGATGAATTTGACAAGCTGAGGCCTCTCTGCTACACCAAC
ACAGACATCTTCCTGCTCTGCTTCAGTGTCGTGAGCCCCTCATCCTTCCAGAACGTCAGT
GAGAAATGGGTGCCGGAGATTCGATGCCACTGTCCCAAAGCCCCCATCATCCTAGTTGGA
ACGCAGTCGGATCTCAGAGAAGATGTCAAAGTCCTCATTGAGTTGGACAAATGCAAAGAA
AAGCCAGTGCCTGAAGAGGCGGCTAAGCTGTGCGCCGAGGAAATCAAAGCCGCCTCCTAC
ATCGAGTGTTCAGCCTTGACTCAAAAAAACCTCAAAGAGGTCTTTGATGCAGCCATCGTC
GCTGGCATTCAATACTCGGACACTCAGCAACAGCCAAAGAAGTCTAAAAGCAGGACTCCA
GATAAAATGAAAAACCTCTCCAAGTCCTGGTGGAAGAAGTACTGCTGTTTCGTATGA
Enzyme 122 GenBank Gene ID AF378087 Link Image
Enzyme 122 GeneCard ID RHOU Link Image
Enzyme 122 GenAtlas ID RHOU Link Image
Enzyme 122 HGNC ID HGNC:17794 Link Image
Enzyme 122 Chromosome Location 1
Enzyme 122 Locus 1q42.11-q42.3
Enzyme 122 SNPs SNPJam Report Link Image
Enzyme 122 General References
  1. Tao W, Pennica D, Xu L, Kalejta RF, Levine AJ: Wrch-1, a novel member of the Rho gene family that is regulated by Wnt-1. Genes Dev. 2001 Jul 15;15(14):1796-807. [PubMed Link Image]
  2. Kirikoshi H, Katoh M: Expression of WRCH1 in human cancer and down-regulation of WRCH1 by beta-estradiol in MCF-7 cells. Int J Oncol. 2002 Apr;20(4):777-83. [PubMed Link Image]
  3. Daigo Y, Takayama I, Ponder BA, Caldas C, Ward SM, Sanders KM, Fujino MA: Novel human, mouse and xenopus genes encoding a member of the RAS superfamily of low-molecular-weight GTP-binding proteins and its downregulation in W/WV mouse jejunum. J Gastroenterol Hepatol. 2004 Feb;19(2):211-7. [PubMed Link Image]
  4. Bubb KL, Bovee D, Buckley D, Haugen E, Kibukawa M, Paddock M, Palmieri A, Subramanian S, Zhou Y, Kaul R, Green P, Olson MV: Scan of human genome reveals no new Loci under ancient balancing selection. Genetics. 2006 Aug;173(4):2165-77. Epub 2006 Jun 4. [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. 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]
  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. Berzat AC, Buss JE, Chenette EJ, Weinbaum CA, Shutes A, Der CJ, Minden A, Cox AD: Transforming activity of the Rho family GTPase, Wrch-1, a Wnt-regulated Cdc42 homolog, is dependent on a novel carboxyl-terminal palmitoylation motif. J Biol Chem. 2005 Sep 23;280(38):33055-65. Epub 2005 Jul 26. [PubMed Link Image]
  9. Shutes A, Berzat AC, Chenette EJ, Cox AD, Der CJ: Biochemical analyses of the Wrch atypical Rho family GTPases. Methods Enzymol. 2006;406:11-26. [PubMed Link Image]
  10. Ory S, Brazier H, Blangy A: Identification of a bipartite focal adhesion localization signal in RhoU/Wrch-1, a Rho family GTPase that regulates cell adhesion and migration. Biol Cell. 2007 Dec;99(12):701-16. [PubMed Link Image]
Enzyme 122 Metabolite References Not Available
Enzyme 123 [top]
Enzyme 123 ID 15061
Enzyme 123 Name cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
Enzyme 123 Synonyms Not Available
Enzyme 123 Gene Name Not Available
Enzyme 123 Protein Sequence >cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
MSTSWSDRLQNAADMPANMDKHALKKYRREAYHRVFVNRSLAMEKIKCFGFDMDYTLAVY
KSPEYESLGFELTVERLVSIGYPQELLSFAYDSTFPTRGLVFDTLYGNLLKVDAYGNLLV
CAHGFNFIRGPETREQYPNKFIQRDDTERFYILNTLFNLPETYLLACLVDFFTNCPRYTS
CETGFKDGDLFMSYRSMFQDVRDAVDWVHYKGSLKEKTVENLEKYVVKDGKLPLLLSRMK
EVGKVFLATNSDYKYTDKIMTYLFDFPHGPKPGSSHRPWQSYFDLILVDARKPLFFGEGT
VLRQVDTKTGKLKIGTYTGPLQHGIVYSGGSSDTICDLLGAKGKDILYIGDHIFGDILKS
KKRQGWRTFLVIPELAQELHVWTDKSSLFEELQSLDIFLAELYKHLDSSSNERPDISSIQ
RRIKKVTHDMDMCYGMMGSLFRSGSRQTLFASQVMRYADLYAASFINLLYYPFSYLFRAA
HVLMPHESTVEHTHVDINEMESPLATRNRTSVDFKDTDYKRHQLTRSISEIKPPNLFPLA
SQEITHCHDEDDDEEEEEEEE
Enzyme 123 Number of Residues 561
Enzyme 123 Molecular Weight 64959.2
Enzyme 123 Theoretical pI 6.05
Enzyme 123 GO Classification Not Available
Enzyme 123 General Function Not Available
Enzyme 123 Specific Function Not Available
Enzyme 123 Pathways Not Available
Enzyme 123 Reactions Not Available
Enzyme 123 Pfam Domain Function
Enzyme 123 Signals
  • None
Enzyme 123 Transmembrane Regions
  • None
Enzyme 123 Essentiality Not Available
Enzyme 123 GenBank ID Protein 158256766 Link Image
Enzyme 123 UniProtKB/Swiss-Prot ID A8K6K2 Link Image
Enzyme 123 UniProtKB/Swiss-Prot Entry Name A8K6K2_HUMAN Link Image
Enzyme 123 PDB ID Not Available
Enzyme 123 Cellular Location Not Available
Enzyme 123 Gene Sequence >1686 bp
ATGTCAACCTCCTGGAGTGATCGGTTACAGAATGCAGCAGATATGCCTGCTAACATGGAT
AAGCATGCCCTGAAAAAGTATCGTCGAGAAGCCTATCATCGGGTGTTTGTGAACCGAAGT
TTAGCAATGGAAAAGATAAAGTGTTTTGGTTTTGATATGGATTATACCCTTGCTGTGTAC
AAGTCCCCAGAGTATGAGTCCCTTGGTTTTGAGCTTACTGTGGAGAGATTAGTTTCTATT
GGCTATCCCCAGGAGTTGCTCAGCTTTGCTTATGATTCTACATTCCCTACCAGGGGACTT
GTCTTTGACACACTGTATGGAAATCTTTTGAAAGTCGATGCCTATGGAAACCTCTTGGTC
TGTGCACATGGATTTAACTTTATAAGGGGACCAGAAACTAGAGAACAGTATCCAAATAAA
TTTATCCAGCGAGATGATACTGAAAGATTTTACATTCTGAACACACTATTCAACCTACCA
GAGACCTACCTGTTGGCCTGCCTAGTAGATTTTTTTACTAATTGTCCCAGATATACCAGT
TGTGAAACAGGATTTAAAGATGGGGACCTCTTCATGTCCTACCGGAGTATGTTCCAGGAT
GTAAGAGATGCTGTTGACTGGGTTCATTACAAGGGCTCCCTTAAGGAAAAGACAGTTGAA
AATCTTGAGAAGTATGTAGTCAAAGATGGAAAACTGCCTTTGCTTCTGAGCCGGATGAAG
GAAGTAGGGAAAGTATTTCTTGCTACCAACAGTGACTATAAATATACAGATAAAATTATG
ACTTACCTGTTTGACTTCCCACATGGCCCCAAGCCTGGGAGCTCCCATCGACCATGGCAG
TCCTACTTTGACTTGATCTTGGTGGATGCACGGAAACCACTCTTTTTTGGAGAAGGCACA
GTACTGCGTCAGGTGGATACTAAAACTGGCAAGCTGAAAATTGGTACCTACACAGGGCCC
CTACAGCATGGTATCGTCTACTCAGGAGGTTCTTCTGATACGATCTGTGACCTGTTGGGA
GCCAAGGGAAAAGACATTTTGTATATTGGAGATCACATTTTTGGGGACATTTTAAAATCA
AAGAAACGGCAAGGGTGGCGAACTTTTTTGGTGATTCCTGAACTCGCACAGGAGCTACAT
GTCTGGACTGACAAGAGTTCACTTTTCGAAGAACTTCAGAGCTTGGATATTTTCTTGGCT
GAACTCTACAAGCATCTTGACAGCAGTAGCAATGAGCGTCCAGACATCAGTTCCATCCAG
AGACGTATTAAGAAAGTAACTCATGACATGGACATGTGCTATGGGATGATGGGAAGCCTG
TTTCGCAGTGGCTCCCGGCAGACCCTTTTTGCCAGTCAAGTGATGCGTTATGCTGACCTC
TATGCAGCATCTTTCATCAACCTGCTGTATTACCCTTTCAGCTACCTCTTCAGGGCTGCC
CATGTCTTGATGCCTCATGAATCAACGGTGGAGCACACACACGTAGATATCAATGAGATG
GAGTCTCCTCTTGCCACCCGGAACCGCACATCAGTGGATTTCAAAGACACTGACTACAAG
CGGCACCAGCTGACACGGTCAATTAGTGAGATTAAACCTCCCAACCTCTTCCCACTGGCC
TCCCAGGAAATTACACACTGCCATGATGAAGATGATGATGAAGAGGAGGAGGAGGAGGAA
GAATAA
Enzyme 123 GenBank Gene ID AK291667 Link Image
Enzyme 123 GeneCard ID Not Available
Enzyme 123 GenAtlas ID Not Available
Enzyme 123 HGNC ID HGNC:8022 Link Image
Enzyme 123 Chromosome Location Not Available
Enzyme 123 Locus Not Available
Enzyme 123 SNPs Not Available
Enzyme 123 General References Not Available
Enzyme 123 Metabolite References Not Available
Enzyme 124 [top]
Enzyme 124 ID 15071
Enzyme 124 Name 3',5'-cyclic nucleotide phosphodiesterase 10A2
Enzyme 124 Synonyms Not Available
Enzyme 124 Gene Name PDE10A2
Enzyme 124 Protein Sequence >3',5'-cyclic nucleotide phosphodiesterase 10A2
MEDGPSNNASCFRRLTECFLSPSLTDEKVKAYLSLHPQVLDEFVSESVSAETVEKWLKRK
NNKSEDESAPKEVSRYQDTNMQGVVYELNSYIEQRLDTGGDNQLLLYELSSIIKIATKAD
GFALYFLGECNNSLCIFTPPGIKEGKPRLIPAGPITQGTTVSAYVAKSRKTLLVEDILGD
ERFPRGTGLESGTRIQSVLCLPIVTAIGDLIGILELYRHWGKEAFCLSHQEVATANLAWA
SVAIHQVQVCRGLAKQTELNDFLLDVSKTYFDNIVAIDSLLEHIMIYAKNLVNADRCALF
QVDHKNKELYSDLFDIGEEKEGKPVFKKTKEIRFSIEKGIAGQVARTGEVLNIPDAYADP
RFNREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCAL
ALHCANMYHRIRHSECIYRVTMEKLSYHSICTSEEWQGLMQFTLPVRLCKEIELFHFDIG
PFENMWPGIFVYMVHRSCGTSCFELEKLCRFIMSVKKNYRRVPYHNWKHAVTVAHCMYAI
LQNNHTLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYSTSTMEQHHFSQTV
SILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSLNLNNQS
HRDRVIGLMMTACDLCSVTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKD
EVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKACRDNLSQWEKVIRGEETATWISSPSV
AQKAAASED
Enzyme 124 Number of Residues 789
Enzyme 124 Molecular Weight 89388.7
Enzyme 124 Theoretical pI 6.40
Enzyme 124 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
Enzyme 124 General Function Involved in catalytic activity
Enzyme 124 Specific Function Not Available
Enzyme 124 Pathways Not Available
Enzyme 124 Reactions Not Available
Enzyme 124 Pfam Domain Function
Enzyme 124 Signals
  • None
Enzyme 124 Transmembrane Regions
  • None
Enzyme 124 Essentiality Not Available
Enzyme 124 GenBank ID Protein 5902442 Link Image
Enzyme 124 UniProtKB/Swiss-Prot ID Q9ULW9 Link Image
Enzyme 124 UniProtKB/Swiss-Prot Entry Name Q9ULW9_HUMAN Link Image
Enzyme 124 PDB ID Not Available
Enzyme 124 Cellular Location Not Available
Enzyme 124 Gene Sequence >2370 bp
ATGGAAGATGGACCTTCTAATAATGCGAGCTGCTTCCGAAGGCTGACCGAGTGCTTCCTG
AGCCCCAGTTTGACAGATGAAAAAGTGAAGGCATATCTTTCTCTTCACCCCCAGGTATTA
GATGAATTTGTATCTGAAAGTGTTAGTGCAGAGACAGTAGAGAAATGGCTGAAGAGGAAG
AACAACAAATCAGAAGATGAATCAGCTCCTAAGGAAGTCAGCAGGTACCAAGATACGAAT
ATGCAGGGAGTTGTATATGAACTAAACAGCTATATAGAACAACGGTTGGACACAGGAGGA
GACAACCAGCTACTCCTCTATGAACTGAGCAGCATCATTAAAATAGCCACAAAAGCCGAT
GGATTTGCACTGTATTTCCTTGGAGAGTGCAATAATAGCCTGTGTATATTCACGCCACCT
GGGATAAAGGAAGGAAAACCCCGCCTCATCCCTGCTGGGCCCATCACTCAGGGCACCACC
GTCTCTGCTTATGTGGCCAAGTCCAGGAAAACACTGCTAGTAGAAGACATCCTTGGAGAT
GAACGATTTCCAAGAGGTACTGGACTGGAATCAGGGACTCGTATCCAGTCTGTTCTTTGC
TTACCAATTGTCACTGCAATTGGTGACTTGATTGGTATTCTCGAGCTGTATCGGCACTGG
GGCAAAGAAGCCTTCTGTCTTAGTCACCAGGAGGTTGCAACAGCAAATCTTGCCTGGGCT
TCAGTAGCAATACATCAGGTGCAGGTATGCAGAGGCCTTGCCAAACAGACAGAATTGAAT
GACTTCCTACTCGACGTATCAAAAACATATTTTGATAACATAGTTGCAATAGATTCTCTA
CTTGAACACATAATGATATATGCAAAAAACCTGGTGAATGCCGATCGTTGTGCGCTTTTC
CAGGTGGACCATAAGAACAAGGAGTTATATTCAGACCTTTTTGATATTGGAGAGGAAAAG
GAAGGAAAACCTGTCTTCAAGAAGACCAAAGAGATAAGATTTTCAATTGAGAAAGGAATT
GCTGGCCAAGTAGCAAGAACAGGGGAAGTCCTGAACATTCCAGATGCCTATGCAGACCCA
CGCTTTAACAGAGAAGTAGACTTGTACACAGGCTACACCACGCGGAACATCCTGTGCATG
CCCATCGTCAGCCGAGGCAGCGTGATAGGTGTGGTGCAGATGGTCAACAAAATCAGTGGC
AGTGCCTTCTCTAAAACAGATGAAAACAACTTCAAAATGTTTGCCGTCTTTTGTGCTTTA
GCCTTACACTGTGCTAATATGTATCATAGAATTCGCCACTCAGAGTGCATTTACCGGGTA
ACGATGGAAAAGCTGTCCTACCATAGCATTTGTACTTCAGAAGAGTGGCAAGGTCTCATG
CAATTCACCCTTCCCGTGCGTCTCTGCAAAGAAATTGAATTATTCCACTTTGACATTGGT
CCTTTTGAAAACATGTGGCCTGGAATTTTTGTCTACATGGTTCATCGGTCCTGTGGGACA
TCCTGCTTTGAGCTTGAAAAGTTGTGTCGTTTTATTATGTCTGTGAAGAAGAACTATCGG
CGGGTTCCTTATCACAACTGGAAGCATGCGGTCACTGTAGCACACTGCATGTATGCCATA
CTTCAGAACAATCACACGCTTTTCACAGACCTTGAGCGCAAAGGACTGCTGATTGCGTGT
CTGTGTCATGACCTGGACCACAGGGGCTTCAGTAACAGCTACCTGCAGAAGTTCGACCAC
CCTCTGGCCGCTCTCTACTCCACTTCCACCATGGAGCAGCACCACTTCTCCCAGACTGTG
TCCATCCTTCAGTTGGAAGGGCACAATATCTTCTCCACTCTGAGCTCCAGTGAATATGAG
CAGGTGCTTGAGATCATCCGCAAAGCCATCATTGCCACAGACCTTGCTTTATACTTTGGA
AACAGGAAGCAGTTGGAAGAGATGTACCAGACCGGATCACTAAACCTTAATAATCAATCA
CATAGAGACCGTGTAATTGGTTTGATGATGACTGCCTGTGACCTTTGTTCTGTGACAAAA
CTGTGGCCCGTTACAAAATTGACGGCAAATGATATATATGCAGAATTCTGGGCTGAGGGT
GATGAAATGAAGAAATTGGGAATACAGCCTATTCCTATGATGGACAGAGACAAGAAGGAT
GAAGTCCCCCAAGGCCAGCTTGGGTTCTACAATGCCGTGGCCATTCCCTGCTATACAACC
CTTACCCAGATCCTCCCTCCCACGGAGCCTCTTCTGAAAGCATGCAGGGATAATCTCAGT
CAGTGGGAGAAGGTGATTCGAGGGGAGGAGACTGCAACCTGGATTTCATCCCCATCCGTG
GCTCAGAAGGCAGCTGCATCTGAAGATTGA
Enzyme 124 GenBank Gene ID AB026816 Link Image
Enzyme 124 GeneCard ID PDE10A2 Link Image
Enzyme 124 GenAtlas ID PDE10A2 Link Image
Enzyme 124 HGNC ID HGNC:8772 Link Image
Enzyme 124 Chromosome Location Not Available
Enzyme 124 Locus Not Available
Enzyme 124 SNPs SNPJam Report Link Image
Enzyme 124 General References
  1. Kotera J, Fujishige K, Yuasa K, Omori K: Characterization and phosphorylation of PDE10A2, a novel alternative splice variant of human phosphodiesterase that hydrolyzes cAMP and cGMP. Biochem Biophys Res Commun. 1999 Aug 11;261(3):551-7. [PubMed Link Image]
Enzyme 124 Metabolite References Not Available
Enzyme 125 [top]
Enzyme 125 ID 15232
Enzyme 125 Name Putative uncharacterized protein DKFZp761J1915 (Ectonucleoside triphosphate diphosphohydrolase 6 (Putative function), isoform CRA_a)
Enzyme 125 Synonyms Not Available
Enzyme 125 Gene Name DKFZp761J1915
Enzyme 125 Protein Sequence >Putative uncharacterized protein DKFZp761J1915 (Ectonucleoside triphosphate diphosphohydrolase 6 (Putative function), isoform CRA_a)
MQPQHGPWQTRMRKISNHGSLRVAKVAYPLGLCVGVFIYVAYIKWHRATATQAFFSITRA
APGARWGQQAHSPLGTAADGHEVFYGIMFDAGSTGTRVHVFQFTRPPRETPTLTHETFKA
LKPGLSAYADDVEKSAQGIRELLDVAKQDIPFDFWKATPLVLKATAGLRLLPGEKAQKLL
QKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITINFLTGSLKTPGGSSVGMLDLGGGST
QIAFLPRVEGTLQASPPGYLTALRMFNRTYKLYSYSYLGLGLMSARLAILGGVEGQPAKD
GKELVSPCLSPSFKGEWEHAEVTYRVSGQKAAASLHELCAARVSEVLQNRVHRTEEVKHV
DFYAFSYYYDLAAGVGLIDAEKGGSLVVGDFEIAAKYVCRTLETQPQSSPFSCMDLTYVS
LLLQEFGFPRSKVLKLTRKIDNVETSWALGAIFHYIDSLNRQKSPAS
Enzyme 125 Number of Residues 467
Enzyme 125 Molecular Weight 51160
Enzyme 125 Theoretical pI 9.14
Enzyme 125 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 125 General Function Not Available
Enzyme 125 Specific Function Not Available
Enzyme 125 Pathways Not Available
Enzyme 125 Reactions Not Available
Enzyme 125 Pfam Domain Function
Enzyme 125 Signals
  • None
Enzyme 125 Transmembrane Regions
  • None
Enzyme 125 Essentiality Not Available
Enzyme 125 GenBank ID Protein 50949564 Link Image
Enzyme 125 UniProtKB/Swiss-Prot ID Q8N3H3 Link Image
Enzyme 125 UniProtKB/Swiss-Prot Entry Name Q8N3H3_HUMAN Link Image
Enzyme 125 PDB ID Not Available
Enzyme 125 Cellular Location Not Available
Enzyme 125 Gene Sequence >1404 bp
ATGCAGCCGCAGCACGGTCCTTGGCAAACAAGGATGAGAAAAATATCCAACCACGGGAGC
CTGCGGGTGGCGAAGGTGGCATACCCCCTGGGGCTGTGTGTGGGCGTGTTCATCTATGTT
GCCTACATCAAGTGGCACCGGGCCACCGCCACCCAGGCCTTCTTCAGCATCACCAGGGCA
GCCCCGGGGGCCCGGTGGGGTCAGCAGGCCCACAGCCCCCTGGGGACAGCTGCAGACGGG
CACGAGGTCTTCTACGGGATCATGTTTGATGCAGGAAGCACTGGCACCCGAGTACACGTC
TTCCAGTTCACCCGGCCCCCCAGAGAAACTCCCACGTTAACCCACGAAACCTTCAAAGCA
CTGAAGCCAGGTCTTTCTGCCTATGCTGATGATGTTGAAAAGAGCGCTCAGGGAATCCGG
GAACTACTGGATGTTGCTAAACAGGACATTCCGTTCGACTTCTGGAAGGCCACCCCTCTG
GTCCTCAAGGCCACAGCTGGCTTACGCCTGTTACCTGGAGAAAAGGCCCAGAAGTTACTG
CAGAAGGTGAAAGAAGTATTTAAAGCATCGCCTTTCCTTGTAGGGGATGACTGTGTTTCC
ATCATGAACGGAACAGATGAAGGCGTTTCGGCGTGGATCACCATCAACTTCCTGACAGGC
AGCTTGAAAACTCCAGGAGGGAGCAGCGTGGGCATGCTGGACTTGGGCGGAGGATCCACT
CAGATCGCCTTCCTGCCACGCGTGGAGGGCACCCTGCAGGCCTCCCCACCCGGCTACCTG
ACGGCACTGCGGATGTTTAACAGGACCTACAAGCTCTATTCCTACAGCTACCTCGGGCTC
GGGCTGATGTCGGCACGCCTGGCGATCCTGGGCGGCGTGGAGGGGCAGCCTGCTAAGGAT
GGAAAGGAGTTGGTCAGCCCTTGCTTGTCTCCCAGTTTCAAAGGAGAGTGGGAACACGCA
GAAGTCACGTACAGGGTTTCAGGGCAGAAAGCAGCGGCAAGCCTGCACGAGCTGTGTGCT
GCCAGAGTGTCAGAGGTCCTTCAAAACAGAGTGCACAGGACGGAGGAAGTGAAGCATGTG
GACTTCTATGCTTTCTCCTACTATTACGACCTTGCAGCTGGTGTGGGCCTCATAGATGCG
GAGAAGGGAGGCAGCCTGGTGGTGGGGGACTTCGAGATCGCAGCCAAGTACGTGTGTCGG
ACCCTGGAGACACAGCCGCAGAGCAGCCCCTTCTCATGCATGGACCTCACCTACGTCAGC
CTGCTACTCCAGGAGTTCGGCTTTCCCAGGAGCAAAGTGCTGAAGCTCACTCGGAAAATT
GACAATGTTGAGACCAGCTGGGCTCTGGGGGCCATTTTTCATTACATCGACTCCCTGAAC
AGACAGAAGAGTCCAGCCTCATAG
Enzyme 125 GenBank Gene ID AL834158 Link Image
Enzyme 125 GeneCard ID Q8N3H3 Link Image
Enzyme 125 GenAtlas ID DKFZp761J1915 Link Image
Enzyme 125 HGNC ID HGNC:3368 Link Image
Enzyme 125 Chromosome Location Not Available
Enzyme 125 Locus Not Available
Enzyme 125 SNPs SNPJam Report Link Image
Enzyme 125 General References Not Available
Enzyme 125 Metabolite References Not Available
Enzyme 126 [top]
Enzyme 126 ID 15233
Enzyme 126 Name Ectonucleoside triphosphate diphosphohydrolase 5
Enzyme 126 Synonyms
  1. SubName: Ectonucleoside triphosphate diphosphohydrolase 5, isoform CRA_d
Enzyme 126 Gene Name ENTPD5
Enzyme 126 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 5
MATSWGTVFFMLVVSCVCSAVSHRNQQTWFEGIFLSSMCPINVSASTLYGIMFDAGSTGT
RIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHW
KKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTV
NFLTGQLHGHRQETVGTLDLGGASTQITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTH
SYLGFGLKAARLATLGALETEGTDGHTFRSACLPRWLEAEWIFGGVKYQYGGNQEGEVGF
EPCYAEVLRVVRGKLHQPEEVQRGSFYAFSYYYDRAVDTDMIDYEKGGILKVEDFERKAR
EVCDNLENFTSGSPFLCMDLSYITALLKDGFGFADSTVLQLTKKVNNIETGWALGATFHL
LQSLGISH
Enzyme 126 Number of Residues 428
Enzyme 126 Molecular Weight 47517.0
Enzyme 126 Theoretical pI 6.29
Enzyme 126 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 126 General Function Involved in hydrolase activity
Enzyme 126 Specific Function Not Available
Enzyme 126 Pathways Not Available
Enzyme 126 Reactions Not Available
Enzyme 126 Pfam Domain Function
Enzyme 126 Signals
  • None
Enzyme 126 Transmembrane Regions
  • None
Enzyme 126 Essentiality Not Available
Enzyme 126 GenBank ID Protein 120660392 Link Image
Enzyme 126 UniProtKB/Swiss-Prot ID A1L4C5 Link Image
Enzyme 126 UniProtKB/Swiss-Prot Entry Name A1L4C5_HUMAN Link Image
Enzyme 126 PDB ID Not Available
Enzyme 126 Cellular Location Not Available
Enzyme 126 Gene Sequence >1287 bp
ATGGCCACTTCTTGGGGCACAGTCTTTTTCATGCTGGTGGTATCCTGTGTTTGCAGCGCT
GTCTCCCACAGGAACCAGCAGACTTGGTTTGAGGGTATCTTCCTGTCTTCCATGTGCCCC
ATCAATGTCAGCGCCAGCACCTTGTATGGAATTATGTTTGATGCAGGGAGCACTGGAACT
CGAATTCATGTTTACACCTTTGTGCAGAAAATGCCAGGACAGCTTCCAATTCTAGAAGGG
GAAGTTTTTGATTCTGTGAAGCCAGGACTTTCTGCTTTTGTAGATCAACCTAAGCAGGGT
GCTGAGACCGTTCAAGGGCTCTTAGAGGTGGCCAAAGACTCAATCCCCCGAAGTCACTGG
AAAAAGACCCCAGTGGTCCTAAAGGCAACAGCAGGACTACGCTTACTGCCAGAACACAAA
GCCAAGGCTCTGCTCTTTGAGGTAAAGGAGATCTTCAGGAAGTCACCTTTCCTGGTACCA
AAGGGCAGTGTTAGCATCATGGATGGATCCGACGAAGGCATATTAGCTTGGGTTACTGTG
AATTTTCTGACAGGTCAGCTGCATGGCCACAGACAGGAGACTGTGGGGACCTTGGACCTA
GGGGGAGCCTCCACCCAAATCACGTTCCTGCCCCAGTTTGAGAAAACTCTGGAACAAACT
CCTAGGGGCTACCTCACTTCCTTTGAGATGTTTAACAGCACTTATAAGCTCTATACACAT
AGTTACCTGGGATTTGGATTGAAAGCTGCAAGACTAGCAACCCTGGGAGCCCTGGAGACA
GAAGGGACTGATGGGCACACTTTCCGGAGTGCCTGTTTACCGAGATGGTTGGAAGCAGAG
TGGATCTTTGGGGGTGTGAAATACCAGTATGGTGGCAACCAAGAAGGGGAGGTGGGCTTT
GAGCCCTGCTATGCCGAAGTGCTGAGGGTGGTACGAGGAAAACTTCACCAGCCAGAGGAG
GTCCAGAGAGGTTCCTTCTATGCTTTCTCTTACTATTATGACCGAGCTGTTGACACAGAC
ATGATTGATTATGAAAAGGGGGGTATTTTAAAAGTTGAAGATTTTGAAAGAAAAGCCAGG
GAAGTGTGTGATAACTTGGAAAACTTCACCTCAGGCAGTCCTTTCCTGTGCATGGATCTC
AGCTACATCACAGCCCTGTTAAAGGATGGCTTTGGCTTTGCAGACAGCACAGTCTTACAG
CTCACAAAGAAAGTGAACAACATAGAGACGGGCTGGGCCTTGGGGGCCACCTTTCACCTG
TTGCAGTCTCTGGGCATCTCCCATTGA
Enzyme 126 GenBank Gene ID BC130485 Link Image
Enzyme 126 GeneCard ID ENTPD5 Link Image
Enzyme 126 GenAtlas ID ENTPD5 Link Image
Enzyme 126 HGNC ID HGNC:3367 Link Image
Enzyme 126 Chromosome Location 1
Enzyme 126 Locus 14q24
Enzyme 126 SNPs SNPJam Report Link Image
Enzyme 126 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. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 126 Metabolite References Not Available
Enzyme 127 [top]
Enzyme 127 ID 16422
Enzyme 127 Name cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
Enzyme 127 Synonyms Not Available
Enzyme 127 Gene Name Not Available
Enzyme 127 Protein Sequence >cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
MCPRAARAPATLLLALGAVLWPAAGAWELTILHTNDVHSRLEQTSEDSSKCVNASRCMGG
VARLFTKVQQIRRAEPNVLLLDAGDQYQGTIWFTVYRGAEVAHFMNALRYDAMALGNHEF
DNGVEGLIEPLLKEAKFPILSANIKAKGPLASQISGLYLPYKVLPVGDEVVGIVGYTSKE
TPFLSNPGTNLVFEDEITALQPEVDKLKTLNVNKIIALGHSGFEMDKLIAQKVRGVDVVV
GGHSNTFLYTGNPPSKEVPAGKYPFIVTSDDGRKVPVVQAYAFGKYLGYLKIEFDERGNV
ISSHGNPILLNSSIPEDPSIKADINKWRIKLDNYSTQELGKTIVYLDGSSQSCRFRECNM
GNLICDAMINNNLRHTDEMFWNHVSMCILNGGGIRSPIDERNNGTITWENLAAVLPFGGT
FDLVQLKGSTLKKAFEHSVHRYGQSTGEFLQVGGIHVVYDLSRKPGDRVVKLDVLCTKCR
VPSYDPLKMDEVYKVILPNFLANGGDGFQMIKDELLRHDSGDQDINVVSTYISKMKVIYP
AVEGRIKFSTGSHCHGSFSLIFLSLWAVIFVLYQ
Enzyme 127 Number of Residues 574
Enzyme 127 Molecular Weight 63395.3
Enzyme 127 Theoretical pI 7.04
Enzyme 127 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • 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 catabolic process
  • nucleotide metabolic process
Component
Enzyme 127 General Function Involved in hydrolase activity
Enzyme 127 Specific Function Not Available
Enzyme 127 Pathways Not Available
Enzyme 127 Reactions Not Available
Enzyme 127 Pfam Domain Function
Enzyme 127 Signals
  • None
Enzyme 127 Transmembrane Regions
  • None
Enzyme 127 Essentiality Not Available
Enzyme 127 GenBank ID Protein 189054446 Link Image
Enzyme 127 UniProtKB/Swiss-Prot ID B2RBH2 Link Image
Enzyme 127 UniProtKB/Swiss-Prot Entry Name B2RBH2_HUMAN Link Image
Enzyme 127 PDB ID Not Available
Enzyme 127 Cellular Location Not Available
Enzyme 127 Gene Sequence >1725 bp
ATGTGTCCCCGAGCCGCGCGGGCGCCCGCGACGCTACTCCTCGCCCTGGGCGCGGTGCTG
TGGCCTGCGGCTGGCGCCTGGGAGCTTACGATTTTGCACACCAACGACGTGCACAGCCGG
CTGGAGCAGACCAGCGAGGACTCCAGCAAGTGCGTCAACGCCAGCCGCTGCATGGGTGGC
GTGGCTCGGCTCTTCACCAAGGTTCAGCAGATCCGCCGCGCCGAACCCAACGTGCTGCTG
CTGGACGCCGGCGACCAGTACCAGGGCACTATCTGGTTCACCGTGTACAGGGGCGCCGAG
GTGGCGCACTTCATGAACGCCCTGCGCTACGATGCCATGGCACTGGGAAATCATGAATTT
GATAATGGTGTGGAAGGACTGATCGAGCCACTCCTCAAAGAGGCCAAATTTCCAATTCTG
AGTGCAAACATTAAAGCAAAGGGGCCACTAGCATCTCAAATATCAGGACTTTATTTGCCA
TATAAAGTTCTTCCTGTTGGTGATGAAGTTGTGGGAATCGTTGGATACACTTCCAAAGAA
ACCCCTTTTCTCTCAAATCCAGGGACAAATTTAGTGTTTGAAGATGAAATCACTGCATTA
CAACCTGAAGTAGATAAGTTAAAAACTCTAAATGTGAACAAAATTATTGCACTGGGACAT
TCGGGTTTTGAAATGGATAAACTCATCGCTCAGAAAGTGAGGGGTGTGGACGTCGTGGTG
GGAGGACACTCCAACACATTTCTTTACACAGGCAATCCACCTTCCAAAGAGGTGCCTGCT
GGGAAGTACCCATTCATAGTCACTTCTGATGATGGGCGGAAGGTTCCTGTAGTCCAGGCC
TATGCTTTTGGCAAATACCTAGGCTATCTGAAGATCGAGTTTGATGAAAGAGGAAACGTC
ATCTCTTCCCATGGAAATCCCATTCTTCTAAACAGCAGCATTCCTGAAGATCCAAGCATA
AAAGCAGACATTAACAAATGGAGGATAAAATTGGATAATTATTCTACCCAGGAATTAGGG
AAAACAATTGTCTATCTGGATGGCTCCTCTCAATCATGCCGCTTTAGAGAATGCAACATG
GGCAACCTGATTTGTGATGCAATGATTAACAACAACCTGAGACACACGGATGAAATGTTC
TGGAACCACGTATCCATGTGCATTTTAAATGGAGGTGGTATCCGGTCGCCCATTGATGAA
CGCAACAATGGCACAATTACCTGGGAGAACCTGGCTGCTGTATTGCCCTTTGGAGGCACA
TTTGACCTAGTCCAGTTAAAAGGTTCCACCCTGAAGAAGGCCTTTGAGCATAGCGTGCAC
CGCTACGGCCAGTCCACTGGAGAGTTCCTGCAGGTGGGCGGAATCCATGTGGTGTATGAT
CTTTCCCGAAAACCTGGAGACAGAGTAGTCAAATTAGATGTTCTTTGCACCAAGTGTCGA
GTGCCCAGTTATGACCCTCTCAAAATGGACGAGGTATATAAGGTGATCCTCCCAAACTTC
CTGGCCAATGGTGGAGATGGGTTCCAGATGATAAAAGATGAATTATTAAGACATGACTCT
GGTGACCAAGATATCAACGTGGTTTCTACATATATCTCCAAAATGAAAGTAATTTATCCA
GCAGTTGAAGGTCGGATCAAGTTTTCCACAGGAAGTCACTGCCATGGAAGCTTTTCTTTA
ATATTTCTTTCACTTTGGGCAGTGATCTTTGTTTTATACCAATAG
Enzyme 127 GenBank Gene ID AK314661 Link Image
Enzyme 127 GeneCard ID Not Available
Enzyme 127 GenAtlas ID Not Available
Enzyme 127 HGNC ID HGNC:8021 Link Image
Enzyme 127 Chromosome Location Not Available
Enzyme 127 Locus Not Available
Enzyme 127 SNPs Not Available
Enzyme 127 General References Not Available
Enzyme 127 Metabolite References Not Available
Enzyme 128 [top]
Enzyme 128 ID 16435
Enzyme 128 Name Phosphodiesterase 7B (Phosphodiesterase 7B, isoform CRA_b)
Enzyme 128 Synonyms Not Available
Enzyme 128 Gene Name PDE7B
Enzyme 128 Protein Sequence >Phosphodiesterase 7B (Phosphodiesterase 7B, isoform CRA_b)
MSCLMVERCGEILFENPDQNAKCVCMLGDIRLRGQTGVRAERRGSYPFIDFRLLNSTTYS
GEIGTKKKVKRLLSFQRYFHASRLLRGIIPQAPLHLLDEDYLGQARHMLSKVGMWDFDIF
LFDRLTNGNSLVTLLCHLFNTHGLIHHFKLDMVTLHRFLVMVQEDYHSQNPYHNAVHAAD
VTQAMHCYLKEPKLASFLTPLDIMLGLLAAAAHDVDHPGVNQPFLIKTNHHLANLYQNMS
VLENHHWRSTIGMLRESRLLAHLPKEMTQDIEQQLGSLILATDINRQNEFLTRLKAHLHN
KDLRLEDAQDRHFMLQIALKCADICNPCRIWEMSKQWSERVCEEFYRQGELEQKFELEIS
PLCNQQKDSIPSIQIGFMSYIVEPLFREWAHFTGNSTLSENMLGHLAHNKAQWKSLLPRQ
HRSRGSSGSGPDHDHAGQGTESEEQEGDSP
Enzyme 128 Number of Residues 450
Enzyme 128 Molecular Weight 51836
Enzyme 128 Theoretical pI 7.03
Enzyme 128 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • signal transduction
Component
Enzyme 128 General Function Not Available
Enzyme 128 Specific Function Not Available
Enzyme 128 Pathways Not Available
Enzyme 128 Reactions Not Available
Enzyme 128 Pfam Domain Function
Enzyme 128 Signals
  • None
Enzyme 128 Transmembrane Regions
  • None
Enzyme 128 Essentiality Not Available
Enzyme 128 GenBank ID Protein Not Available
Enzyme 128 UniProtKB/Swiss-Prot ID Q5W154 Link Image
Enzyme 128 UniProtKB/Swiss-Prot Entry Name Q5W154_HUMAN Link Image
Enzyme 128 PDB ID Not Available
Enzyme 128 Cellular Location Not Available
Enzyme 128 Gene Sequence Not Available
Enzyme 128 GenBank Gene ID AL360178 Link Image
Enzyme 128 GeneCard ID Q5W154 Link Image
Enzyme 128 GenAtlas ID PDE7B Link Image
Enzyme 128 HGNC ID HGNC:8792 Link Image
Enzyme 128 Chromosome Location Not Available
Enzyme 128 Locus Not Available
Enzyme 128 SNPs SNPJam Report Link Image
Enzyme 128 General References Not Available
Enzyme 128 Metabolite References Not Available
Enzyme 129 [top]
Enzyme 129 ID 16436
Enzyme 129 Name cDNA FLJ38065 fis, clone CTONG2015316, highly similar to cAMP-specific 3',5'-cyclic phosphodiesterase 4C (EC 3.1.4.17)
Enzyme 129 Synonyms
  1. SubName: Phosphodiesterase 4C, cAMP-specific (Phosphodiesterase E1 dunce homolog, Drosophila), isoform CRA_c
Enzyme 129 Gene Name PDE4C
Enzyme 129 Protein Sequence >cDNA FLJ38065 fis, clone CTONG2015316, highly similar to cAMP-specific 3',5'-cyclic phosphodiesterase 4C (EC 3.1.4.17)
MENLGVGEGAEACSRLSRSRGRHSMTRAPKHLWRQPRRPIRIQQRFYSDPDKSAGCRERD
LSPRPELRKSRLSWPVSSCRRFDLENGLSCGRRALDPQSSPGLGRIMQAPVPHSQRRESF
LYRSDSDYELSPKAMSRNSSVASDLHGEDMIVTPFAQVLASLRTVRSNVAALARQQCLGA
AKQGPVGNPSSSNQLPPAEDTGQKLALETLDELDWCLDQLETLQTRHSVGEMASNKFKRI
LNRELTHLSETSRSGNQVSEYISRTFLDQQTEVELPKVTAEEAPQPMSRISGLHGLCHSA
SLSSATVPRFGVQTDQEEQLAKELEDTNKWGLDVFKVAELSGNRPLTAIIFSIFQERDLL
KTFQIPADTLATYLLMLEGHYHANVAYHNSLHAADVAQSTHVLLATPALEAVFTDLEILA
ALFASAIHDVDHPGVSNQFLINTNSELALMYNDASVLENHHLAVGFKLLQAENCDIFQNL
SAKQRLSLRRMVIDMVLATDMSKHMNLLADLKTMVETKKVTSLGVLLLDNYSDRIQVLQN
LVHCADLSNPTKPLPLYRQWTDRIMAEFFQQGDRERESGLDISPMCDKHTASVEKSQVGF
IDYIAHPLWETWADLVHPDAQDLLDTLEDNREWYQSKIPRSPSDLTNPERDGPDRFQFEL
TLEEAEEEDEEEEEEGEETALAKEALELPDTELLSPEAGPDPGDLPLDNQRT
Enzyme 129 Number of Residues 712
Enzyme 129 Molecular Weight 79902
Enzyme 129 Theoretical pI 4.84
Enzyme 129 GO Classification
Function
  • 3',5'-cyclic-nucleotide phosphodiesterase activity
  • catalytic activity
  • cyclic-nucleotide phosphodiesterase activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • signal transduction
Component
Enzyme 129 General Function Not Available
Enzyme 129 Specific Function Not Available
Enzyme 129 Pathways Not Available
Enzyme 129 Reactions
  • nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate [RN:R03259] ALL_REAC R03259 > R00191 R01234
Enzyme 129 Pfam Domain Function
Enzyme 129 Signals
  • None
Enzyme 129 Transmembrane Regions
  • None
Enzyme 129 Essentiality Not Available
Enzyme 129 GenBank ID Protein Not Available
Enzyme 129 UniProtKB/Swiss-Prot ID B3KTC4 Link Image
Enzyme 129 UniProtKB/Swiss-Prot Entry Name B3KTC4_HUMAN Link Image
Enzyme 129 PDB ID Not Available
Enzyme 129 Cellular Location Not Available
Enzyme 129 Gene Sequence Not Available
Enzyme 129 GenBank Gene ID AK095384 Link Image
Enzyme 129 GeneCard ID B3KTC4 Link Image
Enzyme 129 GenAtlas ID Not Available
Enzyme 129 HGNC ID Not Available
Enzyme 129 Chromosome Location 19
Enzyme 129 Locus 19p13.11
Enzyme 129 SNPs SNPJam Report Link Image
Enzyme 129 General References Not Available
Enzyme 129 Metabolite References Not Available
Enzyme 130 [top]
Enzyme 130 ID 16437
Enzyme 130 Name cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
Enzyme 130 Synonyms Not Available
Enzyme 130 Gene Name ENTPD3
Enzyme 130 Protein Sequence >cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
Enzyme 130 Number of Residues 529
Enzyme 130 Molecular Weight 59106
Enzyme 130 Theoretical pI 6.40
Enzyme 130 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 130 General Function Not Available
Enzyme 130 Specific Function Not Available
Enzyme 130 Pathways Not Available
Enzyme 130 Reactions Not Available
Enzyme 130 Pfam Domain Function
Enzyme 130 Signals
  • None
Enzyme 130 Transmembrane Regions
  • None
Enzyme 130 Essentiality Not Available
Enzyme 130 GenBank ID Protein Not Available
Enzyme 130 UniProtKB/Swiss-Prot ID B2R8D0 Link Image
Enzyme 130 UniProtKB/Swiss-Prot Entry Name B2R8D0_HUMAN Link Image
Enzyme 130 PDB ID Not Available
Enzyme 130 Cellular Location Not Available
Enzyme 130 Gene Sequence Not Available
Enzyme 130 GenBank Gene ID AK313322 Link Image
Enzyme 130 GeneCard ID B2R8D0 Link Image
Enzyme 130 GenAtlas ID Not Available
Enzyme 130 HGNC ID Not Available
Enzyme 130 Chromosome Location Not Available
Enzyme 130 Locus Not Available
Enzyme 130 SNPs SNPJam Report Link Image
Enzyme 130 General References Not Available
Enzyme 130 Metabolite References Not Available
Enzyme 131 [top]
Enzyme 131 ID 17025
Enzyme 131 Name Guanine nucleotide-binding protein G(i) subunit alpha-1
Enzyme 131 Synonyms
  1. Adenylate cyclase-inhibiting G alpha protein
Enzyme 131 Gene Name GNAI1
Enzyme 131 Protein Sequence >Guanine nucleotide-binding protein G(i) subunit alpha-1
MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAG
YSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMT
AELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVK
TTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEM
NRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAA
AYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
Enzyme 131 Number of Residues 354
Enzyme 131 Molecular Weight 40360.7
Enzyme 131 Theoretical pI 5.76
Enzyme 131 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 131 General Function Involved in signal transducer activity
Enzyme 131 Specific Function Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase:they inhibit the cyclase in response to beta-adrenergic stimuli
Enzyme 131 Pathways Not Available
Enzyme 131 Reactions Not Available
Enzyme 131 Pfam Domain Function
Enzyme 131 Signals
  • None
Enzyme 131 Transmembrane Regions
  • None
Enzyme 131 Essentiality Not Available
Enzyme 131 GenBank ID Protein 20147703 Link Image
Enzyme 131 UniProtKB/Swiss-Prot ID P63096 Link Image
Enzyme 131 UniProtKB/Swiss-Prot Entry Name GNAI1_HUMAN Link Image
Enzyme 131 PDB ID 1CIP Link Image
Enzyme 131 PDB File Show
Enzyme 131 3D Structure
Enzyme 131 Cellular Location Not Available
Enzyme 131 Gene Sequence >1065 bp
ATGGGCTGCACGCTGAGCGCCGAGGACAAGGCGGCGGTGGAGCGGAGTAAGATGATCGAC
CGCAACCTCCGTGAGGACGGCGAGAAGGCGGCGCGCGAGGTCAAGCTGCTGCTGCTCGGT
GCTGGTGAATCTGGTAAAAGTACAATTGTGAAGCAGATGAAAATTATCCATGAAGCTGGT
TATTCAGAAGAGGAGTGTAAACAATACAAAGCAGTGGTCTACAGTAACACCATCCAGTCA
ATTATTGCTATCATTAGGGCTATGGGGAGGTTGAAGATAGACTTTGGTGACTCAGCCCGG
GCGGATGATGCACGCCAACTCTTTGTGCTAGCTGGAGCTGCTGAAGAAGGCTTTATGACT
GCAGAACTTGCTGGAGTTATAAAGAGATTGTGGAAAGATAGTGGTGTACAAGCCTGTTTC
AACAGATCCCGAGAGTACCAGCTTAATGATTCTGCAGCATACTATTTGAATGACTTGGAC
AGAATAGCTCAACCAAATTACATCCCGACTCAACAAGATGTTCTCAGAACTAGAGTGAAA
ACTACAGGAATTGTTGAAACCCATTTTACTTTCAAAGATCTTCATTTTAAAATGTTTGAT
GTGGGAGGTCAGAGATCTGAGCGGAAGAAGTGGATTCATTGCTTCGAAGGAGTGACGGCG
ATCATCTTCTGTGTAGCACTGAGTGACTACGACCTGGTTCTAGCTGAAGATGAAGAAATG
AACCGAATGCATGAAAGCATGAAATTGTTTGACAGCATATGTAACAACAAGTGGTTTACA
GATACATCCATTATACTTTTTCTAAACAAGAAGGATCTCTTTGAAGAAAAAATCAAAAAG
AGCCCTCTCACTATATGCTATCCAGAATATGCAGGATCAAACACATATGAAGAGGCAGCT
GCATATATTCAATGTCAGTTTGAAGACCTCAATAAAAGAAAGGACACAAAGGAAATATAC
ACCCACTTCACATGTGCCACAGATACTAAGAATGTGCAGTTTGTTTTTGATGCTGTAACA
GATGTCATCATAAAAAATAATCTAAAAGATTGTGGTCTCTTTTAA
Enzyme 131 GenBank Gene ID AF493905 Link Image
Enzyme 131 GeneCard ID GNAI1 Link Image
Enzyme 131 GenAtlas ID GNAI1 Link Image
Enzyme 131 HGNC ID HGNC:4384 Link Image
Enzyme 131 Chromosome Location 7
Enzyme 131 Locus 7q21
Enzyme 131 SNPs SNPJam Report Link Image
Enzyme 131 General References
  1. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. 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. Itoh H, Toyama R, Kozasa T, Tsukamoto T, Matsuoka M, Kaziro Y: Presence of three distinct molecular species of Gi protein alpha subunit. Structure of rat cDNAs and human genomic DNAs. J Biol Chem. 1988 May 15;263(14):6656-64. [PubMed Link Image]
  5. Bray P, Carter A, Guo V, Puckett C, Kamholz J, Spiegel A, Nirenberg M: Human cDNA clones for an alpha subunit of Gi signal-transduction protein. Proc Natl Acad Sci U S A. 1987 Aug;84(15):5115-9. [PubMed Link Image]
  6. 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]
  7. Kimple RJ, Kimple ME, Betts L, Sondek J, Siderovski DP: Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits. Nature. 2002 Apr 25;416(6883):878-81. [PubMed Link Image]
  8. Johnston CA, Willard FS, Jezyk MR, Fredericks Z, Bodor ET, Jones MB, Blaesius R, Watts VJ, Harden TK, Sondek J, Ramer JK, Siderovski DP: Structure of Galpha(i1) bound to a GDP-selective peptide provides insight into guanine nucleotide exchange. Structure. 2005 Jul;13(7):1069-80. [PubMed Link Image]
Enzyme 131 Metabolite References Not Available
Enzyme 132 [top]
Enzyme 132 ID 17026
Enzyme 132 Name Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas
Enzyme 132 Synonyms
  1. Adenylate cyclase-stimulating G alpha protein
  2. Extra large alphas protein
  3. XLalphas
Enzyme 132 Gene Name GNAS
Enzyme 132 Protein Sequence >Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas
MGVRNCLYGNNMSGQRDIPPEIGEQPEQPPLEAPGAAAPGAGPSPAEEMETEPPHNEPIP
VENDGEACGPPEVSRPNFQVLNPAFREAGAHGSYSPPPEEAMPFEAEQPSLGGFWPTLEQ
PGFPSGVHAGLEAFGPALMEPGAFSGARPGLGGYSPPPEEAMPFEFDQPAQRGCSQLLLQ
VPDLAPGGPGAAGVPGAPPEEPQALRPAKAGSRGGYSPPPEETMPFELDGEGFGDDSPPP
GLSRVIAQVDGSSQFAAVAASSAVRLTPAANAPPLWVPGAIGSPSQEAVRPPSNFTGSSP
WMEISGPPFEIGSAPAGVDDTPVNMDSPPIALDGPPIKVSGAPDKRERAERPPVEEEAAE
MEGAADAAEGGKVPSPGYGSPAAGAASADTAARAAPAAPADPDSGATPEDPDSGTAPADP
DSGAFAADPDSGAAPAAPADPDSGAAPDAPADPDSGAAPDAPADPDAGAAPEAPAAPAAA
ETRAAHVAPAAPDAGAPTAPAASATRAAQVRRAASAAPASGARRKIHLRPPSPEIQAADP
PTPRPTRASAWRGKSESSRGRRVYYDEGVASSDDDSSGDESDDGTSGCLRWFQHRRNRRR
RKPQRNLLRNFLVQAFGGCFGRSESPQPKASRSLKVKKVPLAEKRRQMRKEALEKRAQKR
AEKKRSKLIDKQLQDEKMGYMCTHRLLLLGAGESGKSTIVKQMRILHVNGFNGEGGEEDP
QAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELANPENQFRVDYILSVMNV
PDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQADYVPSDQDL
LRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVI
REDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFAR
YTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCYPHFTCAVDTENIRRVFN
DCRDIIQRMHLRQYELL
Enzyme 132 Number of Residues 1037
Enzyme 132 Molecular Weight 111023.3
Enzyme 132 Theoretical pI 4.65
Enzyme 132 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 132 General Function Involved in signal transducer activity
Enzyme 132 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. XLas isoforms interact with the same set of receptors as Gnas isoforms
Enzyme 132 Pathways Not Available
Enzyme 132 Reactions Not Available
Enzyme 132 Pfam Domain Function
Enzyme 132 Signals
  • None
Enzyme 132 Transmembrane Regions
  • None
Enzyme 132 Essentiality Not Available
Enzyme 132 GenBank ID Protein 117938759 Link Image
Enzyme 132 UniProtKB/Swiss-Prot ID Q5JWF2 Link Image
Enzyme 132 UniProtKB/Swiss-Prot Entry Name GNAS1_HUMAN Link Image
Enzyme 132 PDB ID 1U0H Link Image
Enzyme 132 PDB File Show
Enzyme 132 3D Structure
Enzyme 132 Cellular Location Not Available
Enzyme 132 Gene Sequence >3114 bp
ATGGGCGTGCGCAACTGCCTCTACGGCAATAATATGTCAGGACAACGCGATATCCCCCCT
GAAATCGGGGAACAGCCCGAGCAACCACCTTTGGAGGCCCCAGGGGCAGCTGCCCCCGGT
GCTGGGCCTAGCCCAGCCGAAGAGATGGAGACCGAACCGCCTCACAACGAGCCCATCCCC
GTCGAGAATGATGGCGAGGCCTGTGGACCCCCAGAGGTCTCCAGACCCAACTTTCAGGTC
CTCAACCCGGCATTCAGGGAAGCTGGAGCCCATGGAAGCTACAGCCCACCTCCTGAGGAA
GCAATGCCCTTCGAGGCTGAACAGCCCAGCTTGGGAGGCTTCTGGCCTACACTGGAGCAG
CCTGGATTCCCCAGTGGGGTCCATGCAGGCCTTGAGGCCTTCGGCCCAGCACTCATGGAG
CCCGGAGCCTTCAGTGGTGCCAGACCAGGCCTGGGAGGATACAGCCCTCCACCAGAAGAA
GCTATGCCCTTTGAGTTTGACCAGCCTGCCCAGAGAGGCTGCAGTCAACTTCTCTTACAG
GTCCCAGACCTTGCTCCAGGAGGCCCAGGTGCTGCAGGGGTCCCCGGAGCTCCTCCCGAG
GAGCCCCAAGCCCTCAGGCCTGCAAAGGCTGGCTCCAGAGGAGGCTACAGCCCTCCCCCT
GAGGAGACTATGCCATTTGAGCTTGATGGAGAAGGATTTGGGGACGACAGCCCACCCCCG
GGGCTTTCCCGAGTTATCGCACAAGTCGACGGCAGCAGCCAGTTCGCGGCAGTCGCGGCC
TCGAGTGCGGTCCGCCTCACTCCCGCCGCGAACGCGCCTCCCCTCTGGGTCCCAGGCGCC
ATCGGCAGCCCATCCCAAGAGGCTGTCAGACCTCCTTCTAACTTCACGGGCAGCAGCCCC
TGGATGGAGATCTCCGGACCCCCGTTCGAGATTGGCAGCGCCCCCGCTGGGGTCGACGAC
ACTCCCGTCAACATGGACAGCCCCCCAATCGCGCTTGACGGCCCGCCCATCAAGGTCTCC
GGAGCCCCAGATAAGAGAGAGCGAGCAGAGAGACCCCCAGTTGAGGAGGAAGCAGCAGAG
ATGGAAGGAGCCGCTGATGCCGCGGAGGGAGGAAAAGTACCCTCTCCGGGGTACGGATCC
CCTGCCGCCGGGGCAGCCTCAGCGGATACCGCTGCCAGGGCAGCCCCTGCAGCCCCAGCC
GATCCTGACTCCGGGGCAACCCCAGAAGATCCCGACTCCGGGACAGCACCAGCCGATCCT
GACTCCGGGGCATTCGCAGCCGATCCCGACTCCGGGGCAGCCCCTGCCGCCCCAGCCGAT
CCCGACTCCGGGGCGGCCCCTGACGCCCCAGCCGATCCCGACTCCGGGGCGGCCCCTGAC
GCCCCAGCCGATCCAGATGCCGGGGCGGCCCCTGAGGCTCCCGCCGCCCCTGCGGCTGCT
GAGACCCGGGCAGCCCATGTCGCCCCAGCTGCGCCAGACGCAGGGGCTCCCACTGCCCCA
GCCGCTTCTGCCACCCGGGCAGCCCAAGTCCGCCGGGCGGCCTCTGCAGCCCCTGCCTCC
GGGGCCAGACGCAAGATCCATCTCAGACCCCCCAGCCCCGAGATCCAGGCTGCCGATCCG
CCTACTCCGCGGCCTACTCGCGCGTCTGCCTGGCGGGGCAAGTCCGAGAGCAGCCGCGGC
CGCCGCGTGTACTACGATGAAGGGGTGGCCAGCAGCGACGATGACTCCAGCGGAGACGAG
TCCGACGATGGGACCTCCGGATGCCTCCGCTGGTTTCAGCATCGGCGAAATCGCCGCCGC
CGAAAGCCCCAGCGCAACTTACTCCGCAACTTTCTCGTGCAAGCCTTCGGGGGCTGCTTC
GGTCGATCTGAGAGTCCCCAGCCCAAAGCCTCGCGCTCTCTCAAGGTCAAGAAGGTACCC
CTGGCGGAGAAGCGCAGACAGATGCGCAAAGAAGCCCTGGAGAAGCGGGCCCAGAAGCGC
GCAGAGAAGAAACGCAGTAAGCTCATCGACAAACAACTCCAGGACGAAAAGATGGGCTAC
ATGTGTACGCACCGCCTGCTGCTTCTAGGTGCTGGAGAATCTGGTAAAAGCACCATTGTG
AAGCAGATGAGGATCCTGCATGTTAATGGGTTTAATGGAGAGGGCGGCGAAGAGGACCCG
CAGGCTGCAAGGAGCAACAGCGATGGTGAGAAGGCAACCAAAGTGCAGGACATCAAAAAC
AACCTGAAAGAGGCGATTGAAACCATTGTGGCCGCCATGAGCAACCTGGTGCCCCCCGTG
GAGCTGGCCAACCCCGAGAACCAGTTCAGAGTGGACTACATCCTGAGTGTGATGAACGTG
CCTGACTTTGACTTCCCTCCCGAATTCTATGAGCATGCCAAGGCTCTGTGGGAGGATGAA
GGAGTGCGTGCCTGCTACGAACGCTCCAACGAGTACCAGCTGATTGACTGTGCCCAGTAC
TTCCTGGACAAGATCGACGTGATCAAGCAGGCTGACTATGTGCCGAGCGATCAGGACCTG
CTTCGCTGCCGTGTCCTGACTTCTGGAATCTTTGAGACCAAGTTCCAGGTGGACAAAGTC
AACTTCCACATGTTTGACGTGGGTGGCCAGCGCGATGAACGCCGCAAGTGGATCCAGTGC
TTCAACGATGTGACTGCCATCATCTTCGTGGTGGCCAGCAGCAGCTACAACATGGTCATC
CGGGAGGACAACCAGACCAACCGCCTGCAGGAGGCTCTGAACCTCTTCAAGAGCATCTGG
AACAACAGATGGCTGCGCACCATCTCTGTGATCCTGTTCCTCAACAAGCAAGATCTGCTC
GCTGAGAAAGTCCTTGCTGGGAAATCGAAGATTGAGGACTACTTTCCAGAATTTGCTCGC
TACACTACTCCTGAGGATGCTACTCCCGAGCCCGGAGAGGACCCACGCGTGACCCGGGCC
AAGTACTTCATTCGAGATGAGTTTCTGAGGATCAGCACTGCCAGTGGAGATGGGCGTCAC
TACTGCTACCCTCATTTCACCTGCGCTGTGGACACTGAGAACATCCGCCGTGTGTTCAAC
GACTGCCGTGACATCATTCAGCGCATGCACCTTCGTCAGTACGAGCTGCTCTAA
Enzyme 132 GenBank Gene ID NM_080425.2 Link Image
Enzyme 132 GeneCard ID GNAS Link Image
Enzyme 132 GenAtlas ID GNAS Link Image
Enzyme 132 HGNC ID HGNC:4392 Link Image
Enzyme 132 Chromosome Location 2
Enzyme 132 Locus 20q13.3
Enzyme 132 SNPs SNPJam Report Link Image
Enzyme 132 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. Hayward BE, Bonthron DT: An imprinted antisense transcript at the human GNAS1 locus. Hum Mol Genet. 2000 Mar 22;9(5):835-41. [PubMed Link Image]
  3. Hayward BE, Kamiya M, Strain L, Moran V, Campbell R, Hayashizaki Y, Bonthron DT: The human GNAS1 gene is imprinted and encodes distinct paternally and biallelically expressed G proteins. Proc Natl Acad Sci U S A. 1998 Aug 18;95(17):10038-43. [PubMed Link Image]
  4. Nekrutenko A, Wadhawan S, Goetting-Minesky P, Makova KD: Oscillating evolution of a mammalian locus with overlapping reading frames: an XLalphas/ALEX relay. PLoS Genet. 2005 Aug;1(2):e18. Epub 2005 Aug 12. [PubMed Link Image]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. Freson K, Hoylaerts MF, Jaeken J, Eyssen M, Arnout J, Vermylen J, Van Geet C: Genetic variation of the extra-large stimulatory G protein alpha-subunit leads to Gs hyperfunction in platelets and is a risk factor for bleeding. Thromb Haemost. 2001 Sep;86(3):733-8. [PubMed Link Image]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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 132 Metabolite References Not Available
Enzyme 133 [top]
Enzyme 133 ID 17267
Enzyme 133 Name Guanine nucleotide exchange factor VAV2
Enzyme 133 Synonyms
  1. VAV-2
Enzyme 133 Gene Name VAV2
Enzyme 133 Protein Sequence >Guanine nucleotide exchange factor VAV2
MEQWRQCGRWLIDCKVLPPNHRVVWPSAVVFDLAQALRDGVLLCQLLHNLSPGSIDLKDI
NFRPQMSQFLCLKNIRTFLKVCHDKFGLRNSELFDPFDLFDVRDFGKVISAVSRLSLHSI
AQNKGIRPFPSEETTENDDDVYRSLEELADEHDLGEDIYDCVPCEDGGDDIYEDIIKVEV
QQPMIRYMQKMGMTEDDKRNCCLLEIQETEAKYYRTLEDIEKNYMSPLRLVLSPADMAAV
FINLEDLIKVHHSFLRAIDVSVMVGGSTLAKVFLDFKERLLIYGEYCSHMEHAQNTLNQL
LASREDFRQKVEECTLKVQDGKFKLQDLLVVPMQRVLKYHLLLKELLSHSAERPERQQLK
EALEAMQDLAMYINEVKRDKETLRKISEFQSSIENLQVKLEEFGRPKIDGELKVRSIVNH
TKQDRYLFLFDKVVIVCKRKGYSYELKEIIELLFHKMTDDPMNNKDVKKSHGKMWSYGFY
LIHLQGKQGFQFFCKTEDMKRKWMEQFEMAMSNIKPDKANANHHSFQMYTFDKTTNCKAC
KMFLRGTFYQGYMCTKCGVGAHKECLEVIPPCKFTSPADLDASGAGPGPKMVAMQNYHGN
PAPPGKPVLTFQTGDVLELLRGDPESPWWEGRLVQTRKSGYFPSSSVKPCPVDGRPPISR
PPSREIDYTAYPWFAGNMERQQTDNLLKSHASGTYLIRERPAEAERFAISIKFNDEVKHI
KVVEKDNWIHITEAKKFDSLLELVEYYQCHSLKESFKQLDTTLKYPYKSRERSASRASSR
SPASCASYNFSFLSPQGLSFASQGPSAPFWSVFTPRVIGTAVARYNFAARDMRELSLREG
DVVRIYSRIGGDQGWWKGETNGRIGWFPSTYVEEEGIQ
Enzyme 133 Number of Residues 878
Enzyme 133 Molecular Weight 101288.2
Enzyme 133 Theoretical pI 7.08
Enzyme 133 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 133 General Function Involved in Rho guanyl-nucleotide exchange factor activity
Enzyme 133 Specific Function Guanine nucleotide exchange factor for the Rho family of Ras-related GTPases. Plays an important role in angiogenesis. Its recruitement by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly
Enzyme 133 Pathways Not Available
Enzyme 133 Reactions Not Available
Enzyme 133 Pfam Domain Function