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Human Metabolome Database Version 2.5

 

Showing metabocard for Guanosine triphosphate (HMDB01273)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-01-20 11:59:55
Accession Number HMDB01273
Secondary Accession Numbers Not Available
Common Name Guanosine triphosphate
Description Guanosine triphosphate (GTP) is a guanine nucleotide containing three phosphate groups esterified to the sugar moiety. GTP functions as a carrier of phosphates and pyrophosphates involved in channeling chemical energy into specific biosynthetic pathways. GTP activates the signal transducing G proteins which are involved in various cellular processes including proliferation, differentiation, and activation of several intracellular kinase cascades. Proliferation and apoptosis are regulated in part by the hydrolysis of GTP by small GTPases Ras and Rho. Another type of small GTPase, Rab, plays a role in the docking and fusion of vesicles and may also be involved in vesicle formation. In addition to its role in signal transduction, GTP also serves as an energy-rich precursor of mononucleotide units in the enzymatic biosynthesis of DNA and RNA.
Synonyms
  1. 5'-GTP
  2. GTG
  3. GTP
  4. Guanosine 5'-(tetrahydrogen triphosphate)
  5. Guanosine 5'-triphosphate
  6. Guanosine 5'-triphosphorate
  7. Guanosine 5'-triphosphoric acid
  8. Guanosine Triphosphate
  9. Guanosine mono(tetrahydrogen triphosphate) (ester)
  10. H4gtp
Chemical IUPAC Name [(2R,3S,4R,5R)-5-(2-amino-6-oxo-3H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl (hydroxy-phosphonooxyphosphoryl) hydrogen phosphate
Chemical Formula C10H16N5O14P3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide triphosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-diol
  • primary amine
  • primary aromatic amine
  • oxo(het)arene
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Folate biosynthesis
  • Component of Pyruvate metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 523.180
Monoisotopic Molecular Weight 522.990662
Isomeric SMILES NC1=NC2=C(N=CN2[C@@H]2O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]2O)C(=O)N1
Canonical SMILES NC1=NC2=C(N=CN2C2OC(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)C(O)C2O)C(=O)N1
KEGG Compound ID C00044 Link Image
BioCyc ID GTP Link Image
BiGG ID 33641 Link Image
Wikipedia Link Guanosine triphosphate Link Image
NuGOwiki Link HMDB01273 Link Image
Metagene Link HMDB01273 Link Image
METLIN ID 6128 Link Image
PubChem Compound 6830 Link Image
PubChem Substance 819066 Link Image
ChEBI ID 15996 Link Image
CAS Registry Number 86-01-1
InChI Identifier InChI=1/C10H16N5O14P3/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(27-9)1-26-31(22,23)29-32(24,25)28-30(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H,24,25)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1
Synthesis Reference Stiller, Regine; Thiem, Joachim. Preparative enzymatic conversion of guanosine-5'-monophosphate to guanosine-5'-triphosphate. Synlett (1990), (11), 709-10.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 10.4 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -4
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.63 [Predicted by ALOGPS]; -5.8 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • Extracellular
  • mitochondria
  • nucleus
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
Tissue Location
Tissue References
Neuron —
Placenta —
Platelet —
Testes —
Concentrations (Normal)
Biofluid Blood
Value 56.0 +/- 7.0 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 108.0 +/- 35.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid CSF
Value 1.83 +/- 0.032 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid CSF
Value 1.59 +/- 1.42 uM
Age Adult:>18 yrs old
Sex Both
Condition Rachialgia
Comments Not Available
References
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Biofluid CSF
Value 2.80 +/- 1.80 uM
Age Adult:>18 yrs old
Sex Both
Condition Subarachnoid hemorrhage
Comments Not Available
References
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Biofluid CSF
Value 2.08 +/- 1.91 uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Not Available
References
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Biofluid CSF
Value 1.30 +/- 1.23 uM
Age Adult:>18 yrs old
Sex Both
Condition Stroke
Comments Cerebral stroke
References
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Biofluid CSF
Value 1.92 +/- 1.53 uM
Age Adult:>18 yrs old
Sex Both
Condition Neuroinfection
Comments Not Available
References
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Associated Disorders
Condition References
Epilepsy
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Neuroinfection
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Rachialgia
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Stroke
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Subarachnoid hemorrhage
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Citric Acid Cycle SMP00057 Link Image map00020 Link Image
DNA Replication Fork SMP00477 Link Image
Gluconeogenesis SMP00128 Link Image map00010 Link Image
Pterine Biosynthesis SMP00005 Link Image map00790 Link Image
Purine Metabolism SMP00050 Link Image map00230 Link Image
Transcription/Translation SMP00019 Link Image
General References
  1. Lester HA, Steer ML, Levitzki A: Prostaglandin-stimulated GTP hydrolysis associated with activation of adenylate cyclase in human platelet membranes. Proc Natl Acad Sci U S A. 1982 Feb;79(3):719-23. [PubMed Link Image]
  2. Naylor EW, Ennis D, Davidson AG, Wong LT, Applegarth DA, Niederwieser A: Guanosine triphosphate cyclohydrolase I deficiency: early diagnosis by routine urine pteridine screening. Pediatrics. 1987 Mar;79(3):374-8. [PubMed Link Image]
  3. Iwanaga N, Yamamasu S, Tachibana D, Nishio J, Nakai Y, Shintaku H, Ishiko O: Activity of synthetic enzymes of tetrahydrobiopterin in the human placenta. Int J Mol Med. 2004 Jan;13(1):117-20. [PubMed Link Image]
  4. Chantin C, Bonin B, Boulieu R, Bory C: Liquid-chromatographic study of purine metabolism abnormalities in purine nucleoside phosphorylase deficiency. Clin Chem. 1996 Feb;42(2):326-8. [PubMed Link Image]
  5. Reichert LE Jr, Dattatreyamurty B: The follicle-stimulating hormone (FSH) receptor in testis: interaction with FSH, mechanism of signal transduction, and properties of the purified receptor. Biol Reprod. 1989 Jan;40(1):13-26. [PubMed Link Image]
  6. Schmidt VA, Scudder L, Devoe CE, Bernards A, Cupit LD, Bahou WF: IQGAP2 functions as a GTP-dependent effector protein in thrombin-induced platelet cytoskeletal reorganization. Blood. 2003 Apr 15;101(8):3021-8. Epub 2002 Dec 19. [PubMed Link Image]
  7. Chen Q, He Y, Yang K: Gene therapy for Parkinson's disease: progress and challenges. Curr Gene Ther. 2005 Feb;5(1):71-80. [PubMed Link Image]
  8. Wikipedia Link Image
Metabolic Enzymes
  1. Phospholipase D1
  2. Ectonucleoside triphosphate diphosphohydrolase 1
  3. Soluble calcium-activated nucleotidase 1
  4. Uridine-cytidine kinase 1
  5. Nucleoside diphosphate kinase, mitochondrial precursor
  6. Nucleoside diphosphate kinase A
  7. Nucleoside diphosphate kinase 7
  8. Nucleoside diphosphate kinase B
  9. Nucleoside diphosphate kinase 3
  10. Nucleoside diphosphate kinase 6
  11. Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
  12. Fucose-1-phosphate guanylyltransferase
  13. Inosine triphosphate pyrophosphatase
  14. GMP synthase [glutamine-hydrolyzing]
  15. Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
  16. Adenylate kinase isoenzyme 5
  17. CTP synthase 1
  18. Glutamate dehydrogenase 1, mitochondrial precursor
  19. Adenylate cyclase type 7
  20. Adenylate cyclase type 6
  21. Adenylate cyclase type 5
  22. Adenylate cyclase type 8
  23. Adenylate cyclase type 3
  24. Adenylate cyclase type 1
  25. DNA-directed RNA polymerase III subunit D
  26. DNA-directed RNA polymerase II 140 kDa polypeptide
  27. DNA-directed RNA polymerase II largest subunit
  28. DNA-directed RNA polymerase, mitochondrial precursor
  29. DNA-directed RNA polymerase I 135 kDa polypeptide
  30. DNA-directed RNA polymerase III subunit 127.6 kDa polypeptide
  31. DNA-directed RNA polymerase I-associated factor 53 kDa subunit
  32. DNA-directed RNA polymerase III subunit 22.9 kDa polypeptide
  33. DNA-directed RNA polymerases III 12.5 kDa polypeptide
  34. Pyruvate kinase isozymes R/L
  35. Ectonucleoside triphosphate diphosphohydrolase 4
  36. Adenylosuccinate synthetase isozyme 2
  37. Adenylosuccinate synthetase isozyme 1
  38. Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial precursor
  39. Phosphoenolpyruvate carboxykinase [GTP], mitochondrial precursor
  40. Succinyl-CoA ligase [GDP-forming] beta-chain, mitochondrial precursor
  41. Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
  42. Adenylate cyclase type 2
  43. GTP cyclohydrolase I
  44. Atrial natriuretic peptide receptor B precursor
  45. Guanylate cyclase soluble subunit beta-1
  46. Retinal guanylyl cyclase 1 precursor
  47. Guanylate cyclase soluble subunit alpha-3
  48. Atrial natriuretic peptide receptor A precursor
  49. Heat-stable enterotoxin receptor precursor
  50. Guanylate cyclase soluble subunit alpha-2
  51. Retinal guanylyl cyclase 2 precursor
  52. Guanylate cyclase soluble subunit beta-2
  53. mRNA-capping enzyme
  54. Rap guanine nucleotide exchange factor 2
  55. Serine/threonine-protein kinase PAK 7
  56. Serine/threonine-protein kinase PAK 6
  57. Serine/threonine-protein kinase PAK 4
  58. Serine/threonine-protein kinase Nek9
  59. Citron Rho-interacting kinase
  60. Serine/threonine-protein kinase PAK 3
  61. Rho-associated protein kinase 1
  62. Serine/threonine-protein kinase PAK 2
  63. Ectonucleoside triphosphate diphosphohydrolase 2
  64. Rho-associated protein kinase 2
  65. Centaurin-gamma 1
  66. Rho guanine nucleotide exchange factor 1
  67. Development and differentiation-enhancing factor 2
  68. Guanine nucleotide-binding protein G(I)/G(S)/G(O) gamma-2 subunit precursor
  69. GTP-binding nuclear protein Ran
  70. Ras-related C3 botulinum toxin substrate 1 precursor
  71. Rap1 GTPase-GDP dissociation stimulator 1
  72. Rho GDP-dissociation inhibitor 3
  73. Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
  74. Rab GDP dissociation inhibitor alpha
  75. Proto-oncogene DBL
  76. Cell division control protein 42 homolog precursor
  77. Rab GDP dissociation inhibitor beta
  78. Rho GDP-dissociation inhibitor 1
  79. Rho GDP-dissociation inhibitor 2
  80. Ras-related C3 botulinum toxin substrate 2 precursor
  81. Elongation factor 1-alpha 1
  82. Elongation factor 1-alpha 2
  83. Vinexin
  84. Ras-related protein Rab-1A
  85. GTPase HRas precursor
  86. Transforming protein RhoA precursor
  87. GTP cyclohydrolase 1 feedback regulatory protein
  88. ADP-ribosylation factor 1
  89. Ras-related protein Rap-1A precursor
  90. Rho-related GTP-binding protein RhoQ precursor
  91. Breakpoint cluster region protein
  92. Molybdenum cofactor biosynthesis protein 1 A
  93. Guanine nucleotide-binding protein G(q) subunit alpha
  94. Guanine nucleotide-binding protein subunit alpha-11
  95. Guanine nucleotide-binding protein G(I)/G(S)/G(O) gamma-11 subunit precursor
  96. Tubulin beta-3 chain
  97. Eukaryotic translation initiation factor 2 subunit 1
  98. RalA-binding protein 1
  99. Guanine nucleotide-binding protein G(t), alpha-1 subunit
  100. Early endosome antigen 1
  101. Stress-activated map kinase-interacting protein 1
  102. Uridine-cytidine kinase 2
  103. Protein ALEX
  104. Rap guanine nucleotide exchange factor 3
  105. Lysophosphatidic acid receptor Edg-4
  106. Rho-related GTP-binding protein Rho6 precursor
  107. Selenocysteine-specific elongation factor
  108. Rap guanine nucleotide exchange factor 4
  109. Elongation factor 2
  110. Succinate-CoA ligase, ADP-forming, beta subunit
  111. Mannose-1-phosphate guanyltransferase subunit beta
  112. GDP-mannose pyrophosphorylase A
  113. Acyl-coenzyme A synthetase ACSM1, mitochondrial precursor
  114. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1
  115. Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
  116. Adenylate cyclase 1
  117. Guanylate cyclase 1, soluble, alpha 2
  118. Uncharacterized protein POLR3G
  119. Uridine/cytidine kinase-like 1
  120. Ectonucleoside triphosphate diphosphohydrolase 7
  121. Ectonucleoside triphosphate diphosphohydrolase 8
  122. RAS guanyl-releasing protein 1
  123. Calcium and DAG-regulated guanine nucleotide exchange factor I
  124. Ras-specific guanine nucleotide-releasing factor 2
  125. Rho GTPase-activating protein
  126. Regulating synaptic membrane exocytosis protein 1
  127. Protein transport protein Sec31A
  128. Synaptotagmin-like protein 3
  129. Tubulin beta-2C chain
  130. Tubulin beta-4 chain
  131. Tubulin beta chain
  132. Tubulin beta-6 chain
  133. Phosducin
  134. Ras-related protein Rap-2a precursor
  135. Rhophilin-2
  136. Synembryn-B
  137. Rap guanine nucleotide exchange factor 6
  138. Active breakpoint cluster region-related protein
  139. Uncharacterized protein C10orf129
  140. ADP-ribosylation factor-like protein 2-binding protein
  141. ADP-ribosylation factor 3
  142. ADP-ribosylation factor 4
  143. ADP-ribosylation factor 5
  144. ADP-ribosylation factor 6
  145. ADP-ribosylation factor GTPase-activating protein 1
  146. GTPase-activating protein ZNF289
  147. ADP-ribosylation factor GTPase-activating protein 3
  148. Arfaptin-1
  149. Arfaptin-2
  150. Rho/Rac guanine nucleotide exchange factor 2
  151. Neuroepithelial cell-transforming gene 1 protein
  152. ADP-ribosylation factor-like protein 17
  153. ADP-ribosylation factor-like protein 4C
  154. ADP-ribosylation factor-like protein 5B
  155. Uncharacterized protein ENSP00000269586
  156. Brain-specific angiogenesis inhibitor 1-associated protein 2
  157. Brefeldin A-inhibited guanine nucleotide-exchange protein 1
  158. Brefeldin A-inhibited guanine nucleotide-exchange protein 2
  159. Cdc42 effector protein 2
  160. Cdc42 effector protein 3
  161. Cdc42 effector protein 5
  162. Cdc42 effector protein 4
  163. Cdc42 effector protein 1
  164. CDC42 small effector 1
  165. CDC42 small effector 2
  166. Cell cycle progression protein 1
  167. Centaurin-beta-1
  168. Cdc42-interacting protein 4
  169. Coatomer subunit alpha
  170. Coatomer subunit beta'
  171. Coatomer subunit beta
  172. Coatomer subunit delta
  173. Coatomer subunit epsilon
  174. Coatomer subunit gamma-2
  175. Coatomer subunit gamma
  176. Coatomer subunit zeta-1
  177. Cytoplasmic FMR1-interacting protein 1
  178. Cytohesin-1
  179. Cytohesin-2
  180. Cytohesin-3
  181. Cytohesin-4
  182. Disheveled-associated activator of morphogenesis 1
  183. DEP domain-containing protein 2
  184. Protein diaphanous homolog 1
  185. Protein diaphanous homolog 2
  186. Protein diaphanous homolog 3
  187. GTP-binding protein Di-Ras1
  188. GTP-binding protein Di-Ras2
  189. Dynamin-1-like protein
  190. Dedicator of cytokinesis protein 10
  191. Dedicator of cytokinesis protein 11
  192. Dedicator of cytokinesis protein 1
  193. Dedicator of cytokinesis protein 2
  194. Dedicator of cytokinesis protein 3
  195. Dedicator of cytokinesis protein 4
  196. Dedicator of cytokinesis protein 5
  197. Dedicator of cytokinesis protein 6
  198. Dedicator of cytokinesis protein 7
  199. Dedicator of cytokinesis protein 8
  200. Dedicator of cytokinesis protein 9
  201. Developmentally-regulated GTP-binding protein 1
  202. Developmentally-regulated GTP-binding protein 2
  203. Dynamin-1
  204. Dynamin-2
  205. Dynamin-3
  206. Elongation factor 1-alpha
  207. Elongation factor 1-beta
  208. Elongation factor 1-delta
  209. Elongation factor G 1, mitochondrial precursor
  210. Elongation factor G 2, mitochondrial precursor
  211. Elongation factor Ts, mitochondrial precursor
  212. Elongation factor Tu, mitochondrial precursor
  213. EH domain-containing protein 2
  214. Translation initiation factor eIF-2B subunit alpha
  215. Translation initiation factor eIF-2B subunit beta
  216. Translation initiation factor eIF-2B subunit delta
  217. Translation initiation factor eIF-2B subunit epsilon
  218. Translation initiation factor eIF-2B subunit gamma
  219. Eukaryotic translation initiation factor 2A
  220. GTP-binding protein era homolog
  221. Eukaryotic peptide chain release factor subunit 1
  222. G1 to S phase transition protein 1 homolog
  223. G1 to S phase transition protein 2 homolog
  224. Elongation factor Tu GTP-binding domain-containing protein 1
  225. Exocyst complex component 2
  226. Exocyst complex component 7
  227. Exocyst complex component 8
  228. Formin-binding protein 1-like
  229. F-box only protein 8
  230. FYVE, RhoGEF and PH domain-containing protein 1
  231. FYVE, RhoGEF and PH domain-containing protein 2
  232. FYVE, RhoGEF and PH domain-containing protein 3
  233. FYVE, RhoGEF and PH domain-containing protein 4
  234. FYVE, RhoGEF and PH domain-containing protein 5
  235. FYVE, RhoGEF and PH domain-containing protein 6
  236. Formin-binding protein 1
  237. GTPase activating protein and VPS9 domain-containing protein 1
  238. Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
  239. Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2
  240. Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3
  241. Guanine nucleotide-binding protein subunit beta-4
  242. Guanine nucleotide-binding protein subunit beta-5
  243. Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
  244. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10 precursor
  245. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12 precursor
  246. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-13 precursor
  247. Guanine nucleotide-binding protein G(T) subunit gamma-T1 precursor
  248. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3 precursor
  249. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-4 precursor
  250. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5 precursor
  251. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7 precursor
  252. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-8 precursor
  253. Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-T2 precursor
  254. Interferon-induced guanylate-binding protein 1
  255. Interferon-induced guanylate-binding protein 2
  256. Guanylate-binding protein 3
  257. Guanylate-binding protein 4
  258. Guanylate-binding protein 6
  259. Guanylate-binding protein 7
  260. ADP-ribosylation factor-binding protein GGA1
  261. ADP-ribosylation factor-binding protein GGA2
  262. ADP-ribosylation factor-binding protein GGA3
  263. GTPase IMAP family member 1
  264. GTPase IMAP family member 2
  265. GTPase IMAP family member 4
  266. GTPase IMAP family member 5
  267. GTPase, IMAP family member 6
  268. GTPase IMAP family member 7
  269. GTPase IMAP family member 8
  270. Ral guanine nucleotide dissociation stimulator
  271. Guanine nucleotide-binding protein-like 1
  272. Guanine nucleotide-binding protein-like 3
  273. Guanine nucleotide-binding protein-like 3-like protein
  274. Golgin-45
  275. Golgin subfamily A member 2
  276. Golgin subfamily A member 5
  277. RAS guanyl-releasing protein 4
  278. GTP-binding protein 1
  279. GTP-binding protein 2
  280. tRNA modification GTPase GTPBP3, mitochondrial precursor
  281. GTP-binding protein 5
  282. Putative GTP-binding protein 6
  283. GTP-binding protein 10
  284. GTP-binding protein GUF1 homolog
  285. PTB domain-containing engulfment adapter protein 1
  286. HBS1-like protein
  287. HECT domain and RCC1-like domain-containing protein 1
  288. Protein-cysteine N-palmitoyltransferase HHAT
  289. Eukaryotic translation initiation factor 2 subunit 2
  290. Uncharacterized protein ENSP00000249480
  291. Eukaryotic translation initiation factor 2 subunit 3
  292. EFI-2-gamma
  293. Translation initiation factor IF-2, mitochondrial precursor
  294. Eukaryotic translation initiation factor 5
  295. Interferon-inducible GTPase 5
  296. Importin subunit alpha-1
  297. Importin subunit alpha-2
  298. Importin subunit alpha-3
  299. Importin subunit alpha-4
  300. Importin subunit alpha-6
  301. Importin subunit alpha-7
  302. Importin subunit beta-1
  303. Importin-11
  304. Importin-13
  305. Importin-4
  306. Importin subunit beta-3
  307. Importin-7
  308. Importin-8
  309. Importin-9
  310. IQ motif and Sec7 domain-containing protein 1
  311. Ras GTPase-activating-like protein IQGAP1
  312. Kalirin RhoGEF
  313. NF-kappa-B inhibitor-interacting Ras-like protein 1
  314. NF-kappa-B inhibitor-interacting Ras-like protein 2
  315. Kinesin-like protein KIF20A
  316. Leucine-rich repeat serine/threonine-protein kinase 1
  317. Large subunit GTPase 1 homolog
  318. MAP kinase-activating death domain protein
  319. Guanine nucleotide exchange factor DBS
  320. Melanophilin
  321. Mitofusin-1
  322. Mitofusin-2
  323. MOG1 isoform A
  324. Molybdenum cofactor biosynthesis protein 1 B
  325. Serine/threonine-protein kinase MRCK alpha
  326. Serine/threonine-protein kinase MRCK beta
  327. Serine/threonine-protein kinase MRCK gamma
  328. Mitochondrial GTPase 1, mitochondrial precursor
  329. Rab effector MyRIP
  330. Nucleolar GTP-binding protein 1
  331. Nucleolar GTP-binding protein 2
  332. Nucleolar protein 8
  333. NTF2-related export protein 1
  334. 2'-5'-oligoadenylate synthetase 3
  335. Obg-like ATPase 1
  336. Oligophrenin 1
  337. Phosphatidylinositol 4-kinase type 2-beta
  338. Polyadenylate-binding protein 2
  339. Serine/threonine-protein kinase PAK 1
  340. Partitioning defective 6 homolog alpha
  341. Partitioning defective 6 homolog beta
  342. Partitioning defective 6 homolog gamma
  343. Partitioning-defective 3 homolog
  344. Phosducin-like protein
  345. PRKCA-binding protein
  346. Plexin-B1 precursor
  347. Rab6-interacting protein 1
  348. Ras-related protein Rab-15
  349. Ras-related protein Rab-1B
  350. Ras-related protein Rab-5A
  351. Ras-related protein Rab-5B
  352. Rab GTPase-binding effector protein 1
  353. Rab GTPase-binding effector protein 2
  354. Rab9 effector protein with Kelch motifs
  355. Rab5 GDP/GTP exchange factor
  356. Ras-related C3 botulinum toxin substrate 3 precursor
  357. Ras-interacting protein 1
  358. Ran-binding protein 3
  359. Ran-binding protein 9
  360. Ran-specific GTPase-activating protein
  361. Ras-related protein Rap-2b precursor
  362. GTPase ERas precursor
  363. RAS and EF-hand domain-containing protein
  364. Ras association domain-containing protein 2
  365. Ras association domain-containing protein 4
  366. GTPase KRas precursor
  367. GTPase NRas precursor
  368. Rab3 GTPase-activating protein catalytic subunit
  369. ELKS/RAB6-interacting/CAST family member 1
  370. Rab3 GTPase-activating protein non-catalytic subunit
  371. RNA-binding protein 4
  372. Rabenosyn-5
  373. Ran-binding protein 17
  374. E3 SUMO-protein ligase RanBP2
  375. Regulator of chromosome condensation
  376. Ras homolog enriched in brain-like protein 1
  377. GTP-binding protein REM 2
  378. Rab15 effector protein
  379. Ras-related and estrogen-regulated growth inhibitor
  380. CDNA: FLJ22655 fis, clone HSI07590
  381. Rab11 family-interacting protein 2
  382. Rab11 family-interacting protein 4
  383. Rab11 family-interacting protein 5
  384. Ral guanine nucleotide dissociation stimulator-like 2
  385. Ral guanine nucleotide dissociation stimulator-like 3
  386. RANBP2-like and GRIP domain-containing protein 8
  387. Ras-specific guanine nucleotide-releasing factor 1
  388. GTP-binding protein Rheb precursor
  389. GTP-binding protein Rhes precursor
  390. Rho GTPase-activating protein 21
  391. Rho-related GTP-binding protein RhoD precursor
  392. Rho-related GTP-binding protein RhoF precursor
  393. Rho-related GTP-binding protein RhoJ precursor
  394. Rhophilin-1
  395. Synembryn-A
  396. Regulating synaptic membrane exocytosis protein 2
  397. Ras and Rab interactor 1
  398. Ras and Rab interactor 2
  399. Ras and Rab interactor 3
  400. GTP-binding protein Rit1
  401. GTP-binding protein Rit2
  402. Rho-related GTP-binding protein RhoE precursor
  403. RNA U small nuclear RNA export adapter protein
  404. Rap guanine nucleotide exchange factor 5
  405. Rab effector Noc2
  406. Ras-related GTP-binding protein A
  407. Ras-related GTP-binding protein B
  408. Ras-related GTP-binding protein C
  409. Ras-related GTP-binding protein D
  410. Ras-related protein R-Ras2 precursor
  411. Rhotekin
  412. RUN and FYVE domain-containing protein 1
  413. RaP2 interacting protein 8 variant
  414. GTP-binding protein SAR1a
  415. Shwachman-Bodian-Diamond syndrome protein
  416. SEC16 homolog A
  417. Sterol regulatory element-binding protein cleavage-activating protein
  418. Septin-10
  419. Uncharacterized protein ENSP00000381893
  420. Putative SH3 domain-containing guanine exchange factor SGEF
  421. SH3 domain-containing RING finger protein 1
  422. Son of sevenless homolog 1
  423. Son of sevenless homolog 2
  424. Sperm-associated antigen 1
  425. Portein sprouty homolog 4
  426. Secretion-regulating guanine nucleotide exchange factor
  427. Signal recognition particle 54 kDa protein
  428. Signal recognition particle receptor subunit alpha
  429. Sex-determining region Y protein
  430. Double-stranded RNA-binding protein Staufen homolog 2
  431. Syntaxin-binding protein 1
  432. Synaptotagmin-like protein 1
  433. Synaptotagmin-like protein 2
  434. Synaptotagmin-like protein 5
  435. Tubulin alpha-1A chain
  436. Tubulin alpha-1B chain
  437. Tubulin alpha-1C chain
  438. Tubulin alpha-3C/D chain
  439. Tubulin alpha-3E chain
  440. Tubulin alpha-4A chain
  441. Tubulin alpha-8 chain
  442. Uncharacterized protein TUBAL3
  443. Tubulin beta-1 chain
  444. Tubulin beta-2A chain
  445. Tubulin beta-2B chain
  446. Tubulin beta-4q chain
  447. TUBB8 protein
  448. Uncharacterized protein ENSP00000309431
  449. Tubulin-specific chaperone D
  450. T-lymphoma invasion and metastasis-inducing protein 1
  451. KIAA2016 protein
  452. Transportin-1
  453. Transportin-2
  454. Tubulin polymerization-promoting protein
  455. Triple functional domain protein
  456. 116 kDa U5 small nuclear ribonucleoprotein component
  457. Protein vav-3
  458. WD repeat-containing protein 44
  459. Exportin-1
  460. Exportin-2
  461. Exportin-4
  462. Exportin-5
  463. Exportin-7
  464. Exportin-T
  465. Protein XRP2
  466. FLJ12595 protein
  467. Uncharacterized protein ENSP00000290377
  468. Putative nucleoside diphosphate kinase
  469. Not Available
  470. Adenylate cyclase 9 (Adenylate cyclase 9, isoform CRA_a)
  471. cDNA FLJ76131, highly similar to Homo sapiens non-metastatic cells 7, protein expressed in (nucleoside-diphosphate kinase) (NME7), transcript variant 1, mRNA (Non-metastatic cells 7, protein expressed in (Nucleoside-diphosphate kinase), isoform CRA_a)
  472. DNA-directed RNA polymerase III subunit RPC1
  473. DNA-directed RNA polymerase I subunit RPA1
  474. DNA-directed RNA polymerase subunit
  475. DNA-directed RNA polymerases I and III subunit RPAC2
  476. cDNA FLJ75210, highly similar to H.sapiens RNA polymerase II 140 kDa subunit (Polymerase (RNA) II (DNA directed) polypeptide B, 140kDa)
  477. DNA-directed RNA polymerase (EC 2.7.7.6)
  478. DNA-directed RNA polymerase III subunit RPC7-like
  479. POLR1C protein (Fragment)
  480. Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
  481. Leucine-rich repeat serine/threonine-protein kinase 2
  482. cDNA FLJ76814, highly similar to Homo sapiens dynamin 1-like (DNM1L), transcript variant 3, mRNA
  483. cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
  484. cDNA FLJ16206 fis, clone CTONG2019590, highly similar to Adenylate cyclase type 4 (EC 4.6.1.1)
  485. cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
  486. Adenylosuccinate synthetase
  487. Guanylate cyclase 2C (Heat stable enterotoxin receptor)
  488. Guanylate cyclase
  489. Guanylate cyclase
  490. Eukaryotic translation elongation factor 1 alpha 2
  491. EEF2 protein (Eukaryotic translation elongation factor 2, isoform CRA_a)
  492. Mitochondrial Rho GTPase 1
  493. Ninein
  494. Nucleolar phosphoprotein p130
  495. Centaurin-gamma-2
  496. Guanine nucleotide-binding protein G(i), alpha-1 subunit
  497. Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas
  498. Eukaryotic translation initiation factor 5B
  499. Guanine nucleotide exchange factor VAV2
  500. Rho-guanine nucleotide exchange factor
  501. Ras guanyl-releasing protein 3
  502. Protein RCC2
  503. Protein very KIND
  504. RNA-directed RNA polymerase catalytic subunit
  505. Genome polyprotein
  506. DNA-directed RNA polymerase 132 kDa polypeptide
  507. Non-structural polyprotein pORF1
  508. Genome polyprotein
  509. RNA-directed RNA polymerase
  510. Large structural protein
  511. RNA-directed RNA polymerase catalytic subunit
  512. Genome polyprotein
  513. DNA-directed RNA polymerase 30 kDa polypeptide
  514. RNA-directed RNA polymerase catalytic subunit
  515. RNA-directed RNA polymerase catalytic subunit
  516. Genome polyprotein
  517. Genome polyprotein
  518. Large structural protein
  519. RNA-directed RNA polymerase
  520. Non-structural polyprotein p200
  521. Genome polyprotein
  522. Genome polyprotein
  523. RNA-directed RNA polymerase
  524. Genome polyprotein
  525. DNA-directed RNA polymerase 35 kDa subunit
  526. RNA-directed RNA polymerase
  527. Large structural protein
  528. Genome polyprotein
  529. Large structural protein
  530. Genome polyprotein
  531. RNA-directed RNA polymerase
  532. RNA-directed RNA polymerase catalytic subunit
  533. Genome polyprotein
  534. DNA-directed RNA polymerase 7 kDa subunit
  535. Genome polyprotein
  536. Large structural protein
  537. DNA-directed RNA polymerase 147 kDa polypeptide
  538. Genome polyprotein
  539. Large structural protein
  540. Non-structural polyprotein p200
  541. Genome polyprotein
  542. RNA-directed RNA polymerase catalytic subunit
  543. Non-structural polyprotein pORF1
  544. Large structural protein
  545. Non-structural polyprotein
  546. Genome polyprotein
  547. RNA-directed RNA polymerase catalytic subunit
  548. Genome polyprotein
  549. Genome polyprotein
  550. Genome polyprotein
  551. Large structural protein
  552. Genome polyprotein
  553. Genome polyprotein
  554. Genome polyprotein
  555. Genome polyprotein
  556. DNA-directed RNA polymerase 132 kDa polypeptide
  557. RNA-directed RNA polymerase catalytic subunit
  558. RNA-directed RNA polymerase
  559. RNA-directed RNA polymerase catalytic subunit
  560. Genome polyprotein
  561. DNA-directed RNA polymerase 35 kDa subunit
  562. RNA-directed RNA polymerase catalytic subunit
  563. Genome polyprotein
  564. Non-structural polyprotein pORF1
  565. Large structural protein
  566. RNA-directed RNA polymerase
  567. Large structural protein
  568. RNA-directed RNA polymerase catalytic subunit
  569. Large structural protein
  570. DNA-directed RNA polymerase 132 kDa polypeptide
  571. RNA-directed RNA polymerase catalytic subunit
  572. RNA-directed RNA polymerase catalytic subunit
  573. RNA-directed RNA polymerase
  574. RNA-directed RNA polymerase
  575. Non-structural polyprotein 1A
  576. Large structural protein
  577. Replicase polyprotein 1ab
  578. Genome polyprotein
  579. Non-structural polyprotein pORF1
  580. RNA-directed RNA polymerase catalytic subunit
  581. Non-structural polyprotein
  582. RNA-directed RNA polymerase
  583. RNA-directed RNA polymerase catalytic subunit
  584. Non-structural polyprotein 1A
  585. Genome polyprotein
  586. RNA-directed RNA polymerase catalytic subunit
  587. RNA-directed RNA polymerase catalytic subunit
  588. Genome polyprotein
  589. Genome polyprotein
  590. RNA-directed RNA polymerase catalytic subunit
  591. Non-structural polyprotein
  592. RNA-directed RNA polymerase catalytic subunit
  593. Genome polyprotein
  594. Genome polyprotein
  595. RNA-directed RNA polymerase catalytic subunit
  596. RNA-directed RNA polymerase catalytic subunit
  597. Large structural protein
  598. Genome polyprotein
  599. Genome polyprotein
  600. RNA-directed RNA polymerase catalytic subunit
  601. RNA-directed RNA polymerase catalytic subunit
  602. Non-structural polyprotein
  603. Genome polyprotein
  604. Genome polyprotein
  605. RNA-directed RNA polymerase catalytic subunit
  606. Genome polyprotein
  607. RNA-directed RNA polymerase
  608. RNA-directed RNA polymerase catalytic subunit
  609. RNA-directed RNA polymerase catalytic subunit
  610. Genome polyprotein
  611. Genome polyprotein
  612. Large structural protein
  613. RNA-directed RNA polymerase catalytic subunit
  614. Genome polyprotein
  615. Non-structural polyprotein
  616. Replicase polyprotein 1ab
  617. Non-structural polyprotein p200
  618. Genome polyprotein
  619. DNA-directed RNA polymerase 18 kDa subunit
  620. Genome polyprotein
  621. DNA-directed RNA polymerase 19 kDa subunit
  622. RNA-directed RNA polymerase catalytic subunit
  623. Non-structural polyprotein
  624. Non-structural polyprotein
  625. Non-structural polyprotein p200
  626. Large structural protein
  627. Genome polyprotein
  628. Large structural protein
  629. RNA-directed RNA polymerase catalytic subunit
  630. DNA-directed RNA polymerase 19 kDa subunit
  631. RNA-directed RNA polymerase
  632. RNA-directed RNA polymerase
  633. Large structural protein
  634. RNA-directed RNA polymerase
  635. Genome polyprotein
  636. DNA-directed RNA polymerase 132 kDa polypeptide
  637. Genome polyprotein
  638. Genome polyprotein
  639. Non-structural polyprotein
  640. Large structural protein
  641. Non-structural polyprotein
  642. Genome polyprotein
  643. Large structural protein
  644. DNA-directed RNA polymerase 22 kDa subunit
  645. Replicase polyprotein 1ab
  646. Non-structural polyprotein p200
  647. RNA-directed RNA polymerase catalytic subunit
  648. Genome polyprotein
  649. Genome polyprotein
  650. Genome polyprotein
  651. RNA-directed RNA polymerase catalytic subunit
  652. Replicase polyprotein 1ab
  653. Large structural protein
  654. Genome polyprotein
  655. RNA-directed RNA polymerase
  656. DNA-directed RNA polymerase 35 kDa subunit
  657. Genome polyprotein
  658. Genome polyprotein
  659. RNA-directed RNA polymerase
  660. RNA-directed RNA polymerase catalytic subunit
  661. Large structural protein
  662. Non-structural polyprotein p200
  663. RNA-directed RNA polymerase catalytic subunit
  664. Genome polyprotein
  665. Large structural protein
  666. RNA-directed RNA polymerase catalytic subunit
  667. Genome polyprotein
  668. Large structural protein
  669. RNA-directed RNA polymerase
  670. Non-structural polyprotein 1AB
  671. RNA-directed RNA polymerase
  672. RNA-directed RNA polymerase catalytic subunit
  673. Non-structural polyprotein
  674. Genome polyprotein
  675. Non-structural polyprotein 1AB
  676. RNA-directed RNA polymerase catalytic subunit
  677. Non-structural polyprotein
  678. Genome polyprotein
  679. RNA-directed RNA polymerase catalytic subunit
  680. Genome polyprotein
  681. Genome polyprotein
  682. Genome polyprotein
  683. Genome polyprotein
  684. RNA-directed RNA polymerase catalytic subunit
  685. RNA-directed RNA polymerase
  686. Genome polyprotein
  687. Replicase polyprotein 1ab
  688. Genome polyprotein
  689. RNA-directed RNA polymerase catalytic subunit
  690. Non-structural polyprotein
  691. DNA-directed RNA polymerase 18 kDa subunit
  692. Genome polyprotein
  693. RNA-directed RNA polymerase catalytic subunit
  694. Genome polyprotein
  695. RNA-directed RNA polymerase catalytic subunit
  696. Large structural protein
  697. Genome polyprotein
  698. RNA-directed RNA polymerase catalytic subunit
  699. RNA-directed RNA polymerase catalytic subunit
  700. DNA-directed RNA polymerase 7 kDa subunit
  701. Genome polyprotein
  702. Genome polyprotein
  703. Large structural protein
  704. Genome polyprotein
  705. Non-structural polyprotein 1AB
  706. Genome polyprotein
  707. RNA-directed RNA polymerase catalytic subunit
  708. Genome polyprotein
  709. Non-structural polyprotein pORF1
  710. RNA-directed RNA polymerase
  711. Genome polyprotein
  712. DNA-directed RNA polymerase 22 kDa subunit
  713. Genome polyprotein
  714. RNA-directed RNA polymerase catalytic subunit
  715. Genome polyprotein
  716. Non-structural polyprotein
  717. Non-structural polyprotein
  718. Genome polyprotein
  719. Genome polyprotein
  720. DNA-directed RNA polymerase 35 kDa subunit
  721. Genome polyprotein
  722. RNA-directed RNA polymerase catalytic subunit
  723. DNA-directed RNA polymerase 7 kDa subunit
  724. RNA-directed RNA polymerase catalytic subunit
  725. RNA-directed RNA polymerase catalytic subunit
  726. RNA-directed RNA polymerase catalytic subunit
  727. Non-structural polyprotein pORF1
  728. Genome polyprotein
  729. RNA-directed RNA polymerase catalytic subunit
  730. Non-structural polyprotein
  731. RNA-directed RNA polymerase catalytic subunit
  732. Genome polyprotein
  733. DNA-directed RNA polymerase 7 kDa subunit
  734. Genome polyprotein
  735. Genome polyprotein
  736. Genome polyprotein
  737. Non-structural polyprotein
  738. Genome polyprotein
  739. Genome polyprotein
  740. Large structural protein
  741. DNA-directed RNA polymerase 147 kDa polypeptide
  742. Genome polyprotein
  743. Genome polyprotein
  744. RNA-directed RNA polymerase catalytic subunit
  745. Non-structural polyprotein p200
  746. Large structural protein
  747. DNA-directed RNA polymerase 132 kDa polypeptide
  748. Genome polyprotein
  749. RNA-directed RNA polymerase
  750. RNA-directed RNA polymerase
  751. RNA-directed RNA polymerase
  752. Genome polyprotein
  753. Non-structural polyprotein
  754. Genome polyprotein
  755. RNA-directed RNA polymerase catalytic subunit
  756. Genome polyprotein
  757. RNA-directed RNA polymerase catalytic subunit
  758. Genome polyprotein
  759. Non-structural polyprotein 1A
  760. RNA-directed RNA polymerase catalytic subunit
  761. Genome polyprotein
  762. RNA-directed RNA polymerase catalytic subunit
  763. RNA-directed RNA polymerase catalytic subunit
  764. Genome polyprotein
  765. RNA-directed RNA polymerase catalytic subunit
  766. RNA-directed RNA polymerase
  767. Genome polyprotein
  768. RNA-directed RNA polymerase catalytic subunit
  769. RNA-directed RNA polymerase catalytic subunit
  770. Large structural protein
  771. DNA-directed RNA polymerase 18 kDa subunit
  772. Non-structural polyprotein pORF1
  773. Genome polyprotein
  774. DNA-directed RNA polymerase 7 kDa subunit
  775. Genome polyprotein
  776. Non-structural polyprotein
  777. RNA-directed RNA polymerase catalytic subunit
  778. RNA-directed RNA polymerase catalytic subunit
  779. Genome polyprotein
  780. DNA-directed RNA polymerase 132 kDa polypeptide
  781. RNA-directed RNA polymerase catalytic subunit
  782. Large structural protein
  783. Non-structural polyprotein p200
  784. Genome polyprotein
  785. Genome polyprotein
  786. Large structural protein
  787. Large structural protein
  788. Genome polyprotein
  789. Genome polyprotein
  790. Non-structural polyprotein
  791. Genome polyprotein
  792. Non-structural polyprotein pORF1
  793. Genome polyprotein
  794. Genome polyprotein
  795. Large structural protein
  796. Genome polyprotein
  797. RNA-directed RNA polymerase catalytic subunit
  798. Genome polyprotein
  799. Genome polyprotein
  800. DNA-directed RNA polymerase 7 kDa subunit
  801. Genome polyprotein
  802. DNA-directed RNA polymerase 147 kDa polypeptide
  803. RNA-directed RNA polymerase catalytic subunit
  804. RNA-directed RNA polymerase
  805. RNA-directed RNA polymerase catalytic subunit
  806. RNA-directed RNA polymerase
  807. Large structural protein
  808. Genome polyprotein
  809. Non-structural polyprotein
  810. DNA-directed RNA polymerase 30 kDa polypeptide
  811. Genome polyprotein
  812. RNA-directed RNA polymerase catalytic subunit
  813. RNA-directed RNA polymerase
  814. Genome polyprotein
  815. DNA-directed RNA polymerase 30 kDa polypeptide
  816. Genome polyprotein
  817. Genome polyprotein
  818. Genome polyprotein
  819. Genome polyprotein
  820. Genome polyprotein
  821. Genome polyprotein
  822. Genome polyprotein
  823. RNA-directed RNA polymerase catalytic subunit
  824. Genome polyprotein
  825. RNA-directed RNA polymerase
  826. Genome polyprotein
  827. DNA-directed RNA polymerase 132 kDa polypeptide
  828. Replicase polyprotein 1ab
  829. RNA-directed RNA polymerase catalytic subunit
  830. Large structural protein
  831. Genome polyprotein
  832. Genome polyprotein
  833. Genome polyprotein
  834. Genome polyprotein
  835. RNA-directed RNA polymerase catalytic subunit
  836. RNA-directed RNA polymerase
  837. Genome polyprotein
  838. RNA-directed RNA polymerase catalytic subunit
  839. RNA-directed RNA polymerase catalytic subunit
  840. Genome polyprotein
  841. Genome polyprotein
  842. RNA-directed RNA polymerase
  843. Non-structural polyprotein 1AB
  844. Replicase polyprotein 1ab
  845. Non-structural polyprotein p200
  846. RNA-directed RNA polymerase catalytic subunit
  847. RNA-directed RNA polymerase catalytic subunit
  848. Non-structural polyprotein
  849. Non-structural polyprotein
  850. RNA-directed RNA polymerase
  851. RNA-directed RNA polymerase catalytic subunit
  852. RNA-directed RNA polymerase catalytic subunit
  853. RNA-directed RNA polymerase catalytic subunit
  854. Non-structural polyprotein 1A
  855. Genome polyprotein
  856. DNA-directed RNA polymerase 19 kDa subunit
  857. Genome polyprotein
  858. Large structural protein
  859. Genome polyprotein
  860. Guanine nucleotide binding protein (G protein), gamma transducing activity polypeptide 1
  861. Abl interactor 1
  862. GTP-binding protein SAR1b
  863. Ras-GEF domain-containing family member 1A
  864. G-protein-signaling modulator 1
  865. GTP-binding protein GEM
  866. Rap guanine nucleotide exchange factor-like 1
  867. Guanine nucleotide binding protein-like 1
  868. Rho guanine nucleotide exchange factor 6
  869. Guanine nucleotide binding protein (G protein), alpha 13, isoform CRA_a
  870. cDNA, FLJ92996, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta polypeptide 1 (GNB1), mRNA
  871. Guanine nucleotide-binding protein subunit alpha-14
  872. PH and SEC7 domain-containing protein 4
  873. Rho guanine nucleotide exchange factor 9
  874. Guanine nucleotide-binding protein G(k) subunit alpha
  875. Epithelial cell transforming sequence 2 oncogene-like
  876. cDNA, FLJ95645, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta 5(GNB5), transcript variant 1, mRNA
  877. Pleckstrin homology domain-containing family G member 6
  878. Guanine nucleotide-binding protein G(i), alpha-2 subunit
  879. cDNA FLJ78228, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta 5(GNB5), transcript variant 1, mRNA
  880. Guanine nucleotide binding protein (G protein), beta polypeptide 1
  881. Guanine nucleotide-binding protein G(t) subunit alpha-2
  882. Probable guanine nucleotide exchange factor FLJ41603
  883. PH and SEC7 domain-containing protein 3
  884. PH and SEC7 domain-containing protein 1
  885. Guanine nucleotide-binding protein G(o) subunit alpha
  886. Ras-GEF domain-containing family member 1B
  887. Rho guanine nucleotide exchange factor 18
  888. ALS2 C-terminal-like protein
  889. Switch-associated protein 70
  890. Ras-specific guanine nucleotide-releasing factor RalGPS2
  891. FERM, RhoGEF and pleckstrin domain-containing protein 2
  892. Ral guanine nucleotide dissociation stimulator-like 1
  893. Guanine nucleotide-binding protein subunit alpha-13
  894. Vav-like protein C9orf100
  895. Probable guanine nucleotide exchange factor MCF2L2
  896. Rho guanine nucleotide exchange factor 7
  897. Guanine nucleotide binding protein (G protein), alpha 14
  898. Guanine nucleotide binding protein-like 1
  899. cDNA FLJ78702, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), alpha activating activity polypeptide, olfactory type (GNAL), transcript variant 2, mRNA
  900. Guanine nucleotide-binding protein subunit alpha-12
  901. Ras-specific guanine nucleotide-releasing factor RalGPS1
  902. Rho guanine nucleotide exchange factor 11
  903. cDNA FLJ76843, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), alpha 15 (Gq class) (GNA15), mRNA
  904. Growth factor receptor-bound protein 2
  905. Guanine nucleotide binding protein (G protein), beta polypeptide 1
  906. Rho guanine nucleotide exchange factor 10-like protein
  907. Guanine nucleotide binding protein (G protein), q polypeptide
  908. Protein SOLO
  909. Prolactin regulatory element-binding protein
  910. Rho guanine nucleotide exchange factor 4
  911. cDNA FLJ11028 fis, clone PLACE1004128, highly similar to Guanine nucleotide-binding protein subunit beta 4
  912. Guanine nucleotide exchange factor for Rab3A
  913. cDNA FLJ77654, highly similar to Homo sapiens guanine nucleotide binding protein (G protein), beta polypeptide 4 (GNB4), mRNA
  914. Guanine nucleotide binding protein-like 1
  915. Engulfment and cell motility protein 1
  916. GRB2-related adapter protein
  917. Guanine nucleotide-binding protein G(z) subunit alpha
  918. Engulfment and cell motility protein 3
  919. Guanine nucleotide exchange factor GEFT
  920. Differentially expressed in FDCP 6 homolog
  921. Alpha-catulin
  922. Guanine nucleotide binding protein (G protein), beta polypeptide 1
  923. IQ motif and SEC7 domain-containing protein 3
  924. Engulfment and cell motility protein 2
  925. Rho guanine nucleotide exchange factor 17
  926. Ras-GEF domain-containing family member 1C
  927. Rho guanine nucleotide exchange factor 12
  928. Ephexin-1
  929. Guanine nucleotide binding protein-like 1
  930. Guanine nucleotide-binding protein G(olf) subunit alpha
  931. Guanine nucleotide-binding protein subunit alpha-15
  932. Rho guanine nucleotide exchange factor 3
Enzyme 1 [top]
Enzyme 1 ID 5311
Enzyme 1 Name Phospholipase D1
Enzyme 1 Synonyms
  1. PLD 1
  2. Choline phosphatase 1
  3. Phosphatidylcholine-hydrolyzing phospholipase D1
  4. hPLD1
Enzyme 1 Gene Name PLD1
Enzyme 1 Protein Sequence >Phospholipase D1 
MSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEGEEVDYDVSPSDPKIQEVYIPFSA
IYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRVPSINLYTIELTHGEFKWQVKRKF
KHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEPREMPSLPRSSENMIREEQFLGRR
KQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDLGPKGIEGMIMKRSGGHRIPGLNC
CGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFKIKVGKKETETKYGIRID
NLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKDHRFGSYAAIQENALAKWYVNAKG
YFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFIMLY
KEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSTVYLWAHHEKLVIIDQSVAFVGGI
DLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAMESMESLRLKDKNEPVQNLPIQKS
IDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSISSIDSTSSYFNHYRSHHNLIHGL
KPHFKLFHPSSESEQGLTRPHADTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQL
DKPFADFIDRYSTPRMPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLL
PKSQTTAHELRYQVPGSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIE
NQFFISCADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQ
AIMHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLL
IADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCF
RVVLGYLDDPSEDIQDPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFI
NKPVLAKEDPIRAEEELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT
Enzyme 1 Number of Residues 1074
Enzyme 1 Molecular Weight 124186
Enzyme 1 Theoretical pI 9.07
Enzyme 1 GO Classification
Function
  • catalytic activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • metabolism
  • physiological process
  • signal transduction
Component
—
Enzyme 1 General Function Lipid transport and metabolism
Enzyme 1 Specific Function Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic
Enzyme 1 Pathways
Enzyme 1 Reactions
  • A phosphatidylcholine + H2O = choline + a phosphatidate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1185463 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q13393 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PLD1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >3225 bp 
ATGTCACTGAAAAACGAGCCACGGGTAAATACCTCTGCACTGCAGAAAATTGCTGCTGAC
ATGAGTAATATCATAGAAAATCTGGACACGCGGGAACTCCACTTTGAGGGAGAGGAGGTA
GACTACGACGTGTCTCCCAGCGATCCCAAGATACAAGAAGTGTATATCCCTTTCTCTGCT
ATTTATAACACTCAAGGATTTAAGGAGCCTAATATACAGACGTATCTCTCCGGCTGTCCA
ATAAAAGCACAAGTTCTGGAAGTGGAACGCTTCACATCTACAACAAGGGTACCAAGTATT
AATCTTTACACTATTGAATTAACACATGGGGAATTTAAATGGCAAGTTAAGAGGAAATTC
AAGCATTTTCAAGAATTTCACAGAGAGCTGCTCAAGTACAAAGCCTTTATCCGCATCCCC
ATTCCCACTAGAAGACACACGTTTAGGAGGCAAAACGTCAGAGAGGAGCCTCGAGAGATG
CCCAGTTTGCCCCGTTCATCTGAAAACATGATAAGAGAAGAACAATTCCTTGGTAGAAGA
AAACAACTGGAAGATTACTTGACAAAGATACTAAAAATGCCCATGTATAGAAACTATCAT
GCCACAACAGAGTTTCTTGATATAAGCCAGCTGTCTTTCATCCATGATTTGGGACCAAAG
GGCATAGAAGGTATGATAATGAAAAGATCTGGAGGACACAGAATACCAGGCTTGAATTGC
TGTGGTCAGGGAAGAGCCTGCTACAGATGGTCAAAAAGATGGTTAATAGTGAAAGATTCC
TTTTTATTGTATATGAAACCAGACAGCGGTGCCATTGCCTTCGTCCTGCTGGTAGACAAA
GAATTCAAAATTAAGGTGGGGAAGAAGGAGACAGAAACGAAATATGGAATCCGAATTGAT
AATCTTTCAAGGACACTTATTTTAAAATGCAACAGCTATAGACATGCTCGGTGGTGGGGA
GGGGCTATAGAAGAATTCATCCAGAAACATGGCACCAACTTTCTCAAAGATCATCGATTT
GGGTCATATGCTGCTATCCAAGAGAATGCTTTAGCTAAATGGTATGTTAATGCCAAAGGA
TATTTTGAAGATGTGGCAAATGCAATGGAAGAGGCAAATGAAGAGATTTTTATCACAGAC
TGGTGGCTGAGTCCAGAAATCTTCCTGAAACGCCCAGTGGTTGAGGGAAATCGTTGGAGG
TTGGACTGCATTCTTAAACGAAAAGCACAACAAGGAGTGAGGATCTTCATAATGCTCTAC
AAAGAGGTGGAACTCGCTCTTGGCATCAATAGTGAATACACCAAGAGGACTTTGATGCGT
CTACATCCCAACATAAAGGTGATGAGACACCCGGATCATGTGTCATCCACCGTCTATTTG
TGGGCTCACCATGAGAAGCTTGTCATCATTGACCAATCGGTGGCCTTTGTGGGAGGGATT
GACCTGGCCTATGGAAGGTGGGACGACAATGAGCACAGACTCACAGACGTGGGCAGTGTG
AAGCGGGTCACTTCAGGACCGTCTCTGGGTTCCCTCCCACCTGCCGCAATGGAGTCTATG
GAATCCTTAAGACTCAAAGATAAAAATGAGCCTGTTCAAAACCTACCCATCCAGAAGAGT
ATTGATGATGTGGATTCAAAACTGAAAGGAATAGGAAAGCCAAGAAAGTTCTCCAAATTT
AGTCTCTACAAGCAGCTCCACAGGCACCACCTGCACGACGCAGATAGCATCAGCAGCATT
GACAGCACCTCCAGTTATTTTAATCACTATAGAAGTCATCACAATTTAATCCATGGTTTA
AAACCCCACTTCAAACTCTTTCACCCGTCCAGTGAGTCTGAGCAAGGACTCACTAGACCT
CATGCTGATACCGGGTCCATCCGTAGTTTACAGACAGGTGTGGGAGAGCTGCATGGGGAA
ACCAGATTCTGGCATGGAAAGGACTACTGCAATTTCGTCTTCAAAGACTGGGTTCAACTT
GATAAACCTTTTGCTGATTTCATTGACAGGTACTCCACGCCCCGGATGCCCTGGCATGAC
ATTGCCTCTGCAGTCCACGGGAAGGCGGCTCGTGATGTGGCACGTCACTTCATCCAGCGC
TGGAACTTCACAAAAATTATGAAATCAAAATATCGGTCCCTTTCTTATCCTTTTCTGCTT
CCAAAGTCTCAAACAACAGCCCATGAGTTGAGATATCAAGTGCCTGGGTCTGTCCATGCT
AACGTACAGTTGCTCCGCTCTGCTGCTGATTGGTCTGCTGGTATAAAGTACCATGAAGAG
TCCATCCACGCCGCTTACGTCCATGTGATAGAGAACAGCAGGCACTATATCTATATCGAA
AACCAGTTTTTCATAAGCTGTGCTGATGACAAAGTTGTGTTCAACAAGATAGGCGATGCC
ATTGCCCAGAGGATCCTGAAAGCTCACAGGGAAAACCAGAAATACCGGGTATATGTCGTG
ATACCACTTCTGCCAGGGTTCGAAGGAGACATTTCAACCGGCGGAGGAAATGCTCTACAG
GCAATCATGCACTTCAACTACAGAACCATGTGCAGAGGAGAAAATTCCATCCTTGGACAG
TTAAAAGCAGAGCTTGGTAATCAGTGGATAAATTACATATCATTCTGTGGTCTTAGAACA
CATGCAGAGCTCGAAGGAAACCTAGTAACTGAGCTTATCTATGTCCACAGCAAGTTGTTA
ATTGCTGATGATAACACTGTTATTATTGGCTCTGCCAACATAAATGACCGCAGCATGCTG
GGAAAGCGTGACAGTGAAATGGCTGTCATTGTGCAAGATACAGAGACTGTTCCTTCAGTA
ATGGATGGAAAAGAGTACCAAGCTGGCCGGTTTGCCCGAGGACTTCGGCTACAGTGCTTT
AGGGTTGTCCTTGGCTATCTTGATGACCCAAGTGAGGACATTCAGGATCCAGTGAGTGAC
AAATTCTTCAAGGAGGTGTGGGTTTCAACAGCAGCTCGAAATGCTACAATTTATGACAAG
GTTTTCCGGTGCCTTCCCAATGATGAAGTACACAATTTAATTCAGCTGAGAGACTTTATA
AACAAGCCCGTATTAGCTAAGGAAGATCCCATTCGAGCTGAGGAGGAACTGAAGAAGATC
CGTGGATTTTTGGTGCAATTCCCCTTTTATTTCTTGTCTGAAGAAAGCCTACTGCCTTCT
GTTGGGACCAAAGAGGCCATAGTGCCCATGGAGGTTTGGACTTAA
Enzyme 1 GenBank Gene ID U38545 Link Image
Enzyme 1 GeneCard ID PLD1 Link Image
Enzyme 1 GenAtlas ID PLD1 Link Image
Enzyme 1 HGNC ID HGNC:9067 Link Image
Enzyme 1 Chromosome Location 3
Enzyme 1 Locus 3q26
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Hammond SM, Altshuller YM, Sung TC, Rudge SA, Rose K, Engebrecht J, Morris AJ, Frohman MA: Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family. J Biol Chem. 1995 Dec 15;270(50):29640-3. [PubMed Link Image]
  2. Hammond SM, Jenco JM, Nakashima S, Cadwallader K, Gu Q, Cook S, Nozawa Y, Prestwich GD, Frohman MA, Morris AJ: Characterization of two alternately spliced forms of phospholipase D1. Activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding proteins and protein kinase C-alpha. J Biol Chem. 1997 Feb 7;272(6):3860-8. [PubMed Link Image]
  3. Steed PM, Clark KL, Boyar WC, Lasala DJ: Characterization of human PLD2 and the analysis of PLD isoform splice variants. FASEB J. 1998 Oct;12(13):1309-17. [PubMed Link Image]
  4. Lopez I, Arnold RS, Lambeth JD: Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2. J Biol Chem. 1998 May 22;273(21):12846-52. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5313
Enzyme 2 Name Ectonucleoside triphosphate diphosphohydrolase 1
Enzyme 2 Synonyms
  1. NTPDase 1
  2. Ecto-ATP diphosphohydrolase
  3. ATPDase
  4. Lymphoid cell activation antigen
  5. Ecto-apyrase
  6. CD39 antigen
Enzyme 2 Gene Name ENTPD1
Enzyme 2 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 1 
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
Enzyme 2 Number of Residues 510
Enzyme 2 Molecular Weight 57965
Enzyme 2 Theoretical pI 6.29
Enzyme 2 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation. Hydrolyzes ATP and ADP equally well
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 17-37 479-499
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 765256 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P49961 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ENTP1_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1533 bp 
ATGGAAGATACAAAGGAGTCTAACGTGAAGACATTTTGCTCCAAGAATATCCTAGCCATC
CTTGGCTTCTCCTCTATCATAGCTGTGATAGCTTTGCTTGCTGTGGGGTTGACCCAGAAC
AAAGCATTGCCAGAAAACGTTAAGTATGGGATTGTGCTGGATGCGGGTTCTTCTCACACA
AGTTTATACATCTATAAGTGGCCAGCAGAAAAGGAGAATGACACAGGCGTGGTGCATCAA
GTAGAAGAATGCAGGGTTAAAGGTCCTGGAATCTCAAAATTTGTTCAGAAAGTAAATGAA
ATAGGCATTTACCTGACTGATTGCATGGAAAGAGCTAGGGAAGTGATTCCAAGGTCCCAG
CACCAAGAGACACCCGTTTACCTGGGAGCCACGGCAGGCATGCGGTTGCTCAGGATGGAA
AGTGAAGAGTTGGCAGACAGGGTTCTGGATGTGGTGGAGAGGAGCCTCAGCAACTACCCC
TTTGACTTCCAGGGTGCCAGGATCATTACTGGCCAAGAGGAAGGTGCCTATGGCTGGATT
ACTATCAACTATCTGCTGGGCAAATTCAGTCAGAAAACAAGGTGGTTCAGCATAGTCCCA
TATGAAACCAATAATCAGGAAACCTTTGGAGCTTTGGACCTTGGGGGAGCCTCTACACAA
GTCACTTTTGTACCCCAAAACCAGACTATCGAGTCCCCAGATAATGCTCTGCAATTTCGC
CTCTATGGCAAGGACTACAATGTCTACACACATAGCTTCTTGTGCTATGGGAAGGATCAG
GCACTCTGGCAGAAACTGGCCAAGGACATTCAGGTTGCAAGTAATGAAATTCTCAGGGAC
CCATGCTTTCATCCTGGATATAAGAAGGTAGTGAACGTAAGTGACCTTTACAAGACCCCC
TGCACCAAGAGATTTGAGATGACTCTTCCATTCCAGCAGTTTGAAATCCAGGGTATTGGA
AACTATCAACAATGCCATCAAAGCATCCTGGAGCTCTTCAACACCAGTTACTGCCCTTAC
TCCCAGTGTGCCTTCAATGGGATTTTCTTGCCACCACTCCAGGGGGATTTTGGGGCATTT
TCAGCTTTTTACTTTGTGATGAAGTTTTTAAACTTGACATCAGAGAAAGTCTCTCAGGAA
AAGGTGACTGAGATGATGAAAAAGTTCTGTGCTCAGCCTTGGGAGGAGATAAAAACATCT
TACGCTGGAGTAAAGGAGAAGTACCTGAGTGAATACTGCTTTTCTGGTACCTACATTCTC
TCCCTCCTTCTGCAAGGCTATCATTTCACAGCTGATTCCTGGGAGCACATCCATTTCATT
GGCAAGATCCAGGGCAGCGACGCCGGCTGGACTTTGGGCTACATGCTGAACCTGACCAAC
ATGATCCCAGCTGAGCAACCATTGTCCACACCTCTCTCCCACTCCACCTATGTCTTCCTC
ATGGTTCTATTCTCCCTGGTCCTTTTCACAGTGGCCATCATAGGCTTGCTTATCTTTCAC
AAGCCTTCATATTTCTGGAAAGATATGGTATAG
Enzyme 2 GenBank Gene ID S73813 Link Image
Enzyme 2 GeneCard ID ENTPD1 Link Image
Enzyme 2 GenAtlas ID ENTPD1 Link Image
Enzyme 2 HGNC ID HGNC:3363 Link Image
Enzyme 2 Chromosome Location 10
Enzyme 2 Locus 10q24
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Maliszewski CR, Delespesse GJ, Schoenborn MA, Armitage RJ, Fanslow WC, Nakajima T, Baker E, Sutherland GR, Poindexter K, Birks C, et al.: The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. J Immunol. 1994 Oct 15;153(8):3574-83. [PubMed Link Image]
  2. Robson SC, Kaczmarek E, Siegel JB, Candinas D, Koziak K, Millan M, Hancock WW, Bach FH: Loss of ATP diphosphohydrolase activity with endothelial cell activation. J Exp Med. 1997 Jan 6;185(1):153-63. [PubMed Link Image]
  3. Matsumoto M, Sakurai Y, Kokubo T, Yagi H, Makita K, Matsui T, Titani K, Fujimura Y, Narita N: The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II. FEBS Lett. 1999 Jun 25;453(3):335-40. [PubMed Link Image]
  4. Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O: Purification and properties of human placental ATP diphosphohydrolase. Eur J Biochem. 1995 Nov 15;234(1):66-74. [PubMed Link Image]
  5. Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y: Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. Int J Hematol. 1998 Oct;68(3):297-310. [PubMed Link Image]
  6. Kaczmarek E, Koziak K, Sevigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC: Identification and characterization of CD39/vascular ATP diphosphohydrolase. J Biol Chem. 1996 Dec 20;271(51):33116-22. [PubMed Link Image]
  7. Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed Link Image]
  8. Koziak K, Kaczmarek E, Kittel A, Sevigny J, Blusztajn JK, Schulte Am Esch J 2nd, Imai M, Guckelberger O, Goepfert C, Qawi I, Robson SC: Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae. J Biol Chem. 2000 Jan 21;275(3):2057-62. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5314
Enzyme 3 Name Soluble calcium-activated nucleotidase 1
Enzyme 3 Synonyms
  1. SCAN-1
  2. Apyrase homolog
  3. Putative NF-kappa-B-activating protein 107
  4. Putative MAPK-activating protein PM09
Enzyme 3 Gene Name CANT1
Enzyme 3 Protein Sequence >Soluble calcium-activated nucleotidase 1 
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
Enzyme 3 Number of Residues 401
Enzyme 3 Molecular Weight 44840
Enzyme 3 Theoretical pI 5.98
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP
Enzyme 3 Pathways
Enzyme 3 Reactions
  • A nucleoside diphosphate + H2O = a nucleotide + phosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 45-62
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 22218108 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q8WVQ1 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name CANT1_HUMAN Link Image
Enzyme 3 PDB ID 1S1D Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1116 bp 
ATGACCAAGGCCGCGGACCCCCGCTTCCGCCCCCGCTGGAAGGTGATCCTGACGTTCTTT
GTGGGTGCTGCCATCCTCTGGCTGCTCTGCTCCCACCGCCCGGCCCCCGGCAGGCCCCCC
ACCCACAATGCACACAACTGGAGGCTCGGCCAGGCGCCCGCCAACTGGTACAATGACACC
TACCCCCTGTCTCCCCCACAAAGGACACCGGCTGGGATTCGGTATCGAATCGCAGTTATC
GCAGACCTGGACACAGAGTCAAGGGCCCAAGAGGAAAACACCTGGTTCAGTTACCTGAAA
AAGGGCTACCTGACCCTGTCAGACAGTGGGGACAAGGTGGCCGTGGAATGGGACAAAGAC
CATGGGGTCCTGGAGTCCCACCTGGCGGAGAAGGGGAGAGGCATGGAGCTATCCGACCTG
ATTGTTTTCAATGGGAAACTCTACTCCGTGGATGACCGGACGGGGGTCGTCTACCAGATC
GAAGGCAGCAAAGCCGTGCCCTGGGTGATTCTGTCCGACGGCGACGGCACCGTGGAGAAA
GGCTTCAAGGCCGAATGGCTGGCAGTGAAGGACGAGCGTCTGTACGTGGGCGGCCTGGGC
AAGGAGTGGACGACCACTACGGGTGATGTGGTGAACGAGAACCCGGAGTGGGTGAAGGTG
GTGGGCTACAAGGGCAGCGTGGACCACGAGAACTGGGTGTCCAACTACAACGCCCTGCGG
GCTGCTGCCGGCATCCAGCCGCCAGGCTACCTCATCCATGAGTCTGCCTGCTGGAGTGAC
ACGCTGCAGCGCTGGTTCTTCCTGCCGCGCCGCGCCAGCCAGGAGCGCTACAGCGAGAAG
GACGACGAGCGCAAGGGCGCCAACCTGCTGCTGAGCGCCTCCCCTGACTTCGGCGACATC
GCTGTGAGCCACGTCGGGGCGGTGGTCCCCACTCACGGCTTCTCGTCCTTCAAGTTCATC
CCCAACACCGACGACCAGATCATTGTGGCCCTCAAATCCGAGGAGGACAGCGGCAGAGTC
GCCTCCTACATCATGGCCTTCACGCTGGACGGGCGCTTCCTGTTGCCGGAGACCAAGATC
GGAAGCGTGAAATACGAAGGCATCGAGTTCATTTAA
Enzyme 3 GenBank Gene ID AF328554 Link Image
Enzyme 3 GeneCard ID CANT1 Link Image
Enzyme 3 GenAtlas ID CANT1 Link Image
Enzyme 3 HGNC ID HGNC:19721 Link Image
Enzyme 3 Chromosome Location 17
Enzyme 3 Locus 17q25.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Smith TM, Hicks-Berger CA, Kim S, Kirley TL: Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases. Arch Biochem Biophys. 2002 Oct 1;406(1):105-15. [PubMed Link Image]
  2. Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S: Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003 May 22;22(21):3307-18. [PubMed Link Image]
  3. Failer BU, Braun N, Zimmermann H: Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J Biol Chem. 2002 Oct 4;277(40):36978-86. Epub 2002 Aug 6. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5337
Enzyme 4 Name Uridine-cytidine kinase 1
Enzyme 4 Synonyms
  1. UCK 1
  2. Uridine monophosphokinase 1
  3. Cytidine monophosphokinase 1
Enzyme 4 Gene Name UCK1
Enzyme 4 Protein Sequence >Uridine-cytidine kinase 1 
MASAGGEDCESPAPEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRKVV
ILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTH
SRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRVLRDVRRGRDL
EQILTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNGDICKWHR
GGSNGRSYKRTFSEPGDHPGMLTSGKRSHLESSSRPH
Enzyme 4 Number of Residues 277
Enzyme 4 Molecular Weight 31435
Enzyme 4 Theoretical pI 7.33
Enzyme 4 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleoside kinase activity
  • nucleotide binding
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • uridine kinase activity
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
—
Enzyme 4 General Function Nucleotide transport and metabolism
Enzyme 4 Specific Function Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, 4-N-acetylcytidine, 4-N- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and 4-N-anisoylcytidine
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + uridine = ADP + UMP
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 13506765 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9HA47 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name UCK1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >834 bp 
ATGGCTTCGGCGGGAGGCGAAGACTGCGAGAGCCCCGCGCCGGAGGCCGACCGTCCGCAC
CAGCGGCCCTTCCTGATAGGGGTGAGCGGCGGCACTGCCAGCGGGAAGTCGACCGTGTGT
GAGAAGATCATGGAGTTGCTGGGACAGAACGAGGTGGAACAGCGGCAGCGGAAGGTGGTC
ATCCTGAGCCAGGACAGGTTCTACAAGGTCCTGACGGCAGAGCAGAAGGCCAAGGCCTTG
AAAGGACAGTACAATTTTGACCATCCAGATGCCTTTGATAATGATTTGATGCACAGGACT
CTGAAGAACATCGTGGAGGGCAAAACGGTGGAGGTGCCGACCTATGATTTTGTGACACAC
TCAAGGTTACCAGAGACCACGGTGGTCTACCCTGCGGACGTGGTTCTGTTTGAGGGCATC
TTGGTGTTCTACAGCCAGGAGATCCGGGACATGTTCCACCTGCGCCTCTTCGTGGACACC
GACTCCGACGTCAGGCTGTCTCGAAGAGTTCTCCGGGACGTGCGCCGAGGGAGGGACCTG
GAGCAGATTCTGACGCAGTACACCACCTTCGTGAAGCCGGCCTTCGAGGAGTTCTGCCTG
CCGACAAAGAAGTATGCCGATGTGATCATCCCGCGAGGAGTGGACAATATGGTTGCCATC
AACCTGATCGTGCAGCACATCCAGGACATTCTGAATGGTGACATCTGCAAATGGCACCGA
GGAGGGTCCAATGGGCGGAGCTACAAGCGGACCTTTTCTGAGCCAGGGGACCACCCTGGG
ATGCTGACCTCTGGCAAACGGTCACATTTGGAGTCCAGCAGCAGACCCCACTGA
Enzyme 4 GenBank Gene ID AF237290 Link Image
Enzyme 4 GeneCard ID UCK1 Link Image
Enzyme 4 GenAtlas ID UCK1 Link Image
Enzyme 4 HGNC ID HGNC:14859 Link Image
Enzyme 4 Chromosome Location 9
Enzyme 4 Locus 9q34.13
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Van Rompay AR, Norda A, Linden K, Johansson M, Karlsson A: Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases. Mol Pharmacol. 2001 May;59(5):1181-6. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5338
Enzyme 5 Name Nucleoside diphosphate kinase, mitochondrial precursor
Enzyme 5 Synonyms
  1. NDP kinase, mitochondrial
  2. NDK
  3. nm23-H4
  4. Nucleoside diphosphate kinase D
  5. NDPKD
Enzyme 5 Gene Name NME4
Enzyme 5 Protein Sequence >Nucleoside diphosphate kinase, mitochondrial precursor 
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
Enzyme 5 Number of Residues 187
Enzyme 5 Molecular Weight 20659
Enzyme 5 Theoretical pI 10.75
Enzyme 5 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
—
Enzyme 5 General Function Nucleotide transport and metabolism
Enzyme 5 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-15
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 1945762 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID O00746 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name NDKM_HUMAN Link Image
Enzyme 5 PDB ID 1EHW Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >564 bp 
ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCA
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
Enzyme 5 GenBank Gene ID Y07604 Link Image
Enzyme 5 GeneCard ID NME4 Link Image
Enzyme 5 GenAtlas ID NME4 Link Image
Enzyme 5 HGNC ID HGNC:7852 Link Image
Enzyme 5 Chromosome Location 16
Enzyme 5 Locus 16p13.3
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Milon L, Rousseau-Merck MF, Munier A, Erent M, Lascu I, Capeau J, Lacombe ML: nm23-H4, a new member of the family of human nm23/nucleoside diphosphate kinase genes localised on chromosome 16p13. Hum Genet. 1997 Apr;99(4):550-7. [PubMed Link Image]
  2. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  3. Milon L, Meyer P, Chiadmi M, Munier A, Johansson M, Karlsson A, Lascu I, Capeau J, Janin J, Lacombe ML: The human nm23-H4 gene product is a mitochondrial nucleoside diphosphate kinase. J Biol Chem. 2000 May 12;275(19):14264-72. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5341
Enzyme 6 Name Nucleoside diphosphate kinase A
Enzyme 6 Synonyms
  1. NDK A
  2. NDP kinase A
  3. Tumor metastatic process-associated protein
  4. Metastasis inhibition factor nm23
  5. nm23-H1
  6. Granzyme A-activated DNase
  7. GAAD
Enzyme 6 Gene Name NME1
Enzyme 6 Protein Sequence >Nucleoside diphosphate kinase A 
MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
Enzyme 6 Number of Residues 152
Enzyme 6 Molecular Weight 17149
Enzyme 6 Theoretical pI 6.11
Enzyme 6 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
—
Enzyme 6 General Function Nucleotide transport and metabolism
Enzyme 6 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP
Enzyme 6 Pathways
Enzyme 6 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 35068 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P15531 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name NDKA_HUMAN Link Image
Enzyme 6 PDB ID 1JXV Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >543 bp 
TGCTGCGAACCACGTGGGTCCCGGGCGCGTTTCGGGTGCTGGCGGCTGCAGCCGGAGTTC
AAACCTAAGCAGCTGGAAGGAACCATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAA
CCAGATGGGGTCCAGCGGGGTCTTGTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGA
TTCCGCCTTGTTGGTCTGAAATTCATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTAC
GTTGACCTGAAGGACCGTCCATTCTTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCG
GTAGTTGCCATGGTCTGGGAGGGGCTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGG
GAGACCAACCCTGCAGACTCCAAGCCTGGGACCATCCGTGGAGACTTCTGCATACAAGTT
GGCAGGAACATTATACATGGCAGTGATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTG
TGGTTTCACCCTGAGGAACTGGTAGATTACACGAGCTGTGCTCAGAACTGGATCTATGAA
TGA
Enzyme 6 GenBank Gene ID X17620 Link Image
Enzyme 6 GeneCard ID NME1 Link Image
Enzyme 6 GenAtlas ID NME1 Link Image
Enzyme 6 HGNC ID HGNC:7849 Link Image
Enzyme 6 Chromosome Location 17
Enzyme 6 Locus 17q21.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Rosengard AM, Krutzsch HC, Shearn A, Biggs JR, Barker E, Margulies IM, King CR, Liotta LA, Steeg PS: Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development. Nature. 1989 Nov 9;342(6246):177-80. [PubMed Link Image]
  2. Dooley S, Seib T, Engel M, Theisinger B, Janz H, Piontek K, Zang KD, Welter C: Isolation and characterization of the human genomic locus coding for the putative metastasis control gene nm23-H1. Hum Genet. 1994 Jan;93(1):63-6. [PubMed Link Image]
  3. Wang L, Patel U, Ghosh L, Chen HC, Banerjee S: Mutation in the nm23 gene is associated with metastasis in colorectal cancer. Cancer Res. 1993 Feb 15;53(4):717-20. [PubMed Link Image]
  4. Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed Link Image]
  5. Hailat N, Keim DR, Melhem RF, Zhu XX, Eckerskorn C, Brodeur GM, Reynolds CP, Seeger RC, Lottspeich F, Strahler JR, et al.: High levels of p19/nm23 protein in neuroblastoma are associated with advanced stage disease and with N-myc gene amplification. J Clin Invest. 1991 Jul;88(1):341-5. [PubMed Link Image]
  6. Manda R, Kohno T, Matsuno Y, Takenoshita S, Kuwano H, Yokota J: Identification of genes (SPON2 and C20orf2) differentially expressed between cancerous and noncancerous lung cells by mRNA differential display. Genomics. 1999 Oct 1;61(1):5-14. [PubMed Link Image]
  7. Min K, Song HK, Chang C, Kim SY, Lee KJ, Suh SW: Crystal structure of human nucleoside diphosphate kinase A, a metastasis suppressor. Proteins. 2002 Feb 15;46(3):340-2. [PubMed Link Image]
  8. Chen Y, Gallois-Montbrun S, Schneider B, Veron M, Morera S, Deville-Bonne D, Janin J: Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases. J Mol Biol. 2003 Sep 26;332(4):915-26. [PubMed Link Image]
  9. Fan Z, Beresford PJ, Oh DY, Zhang D, Lieberman J: Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Cell. 2003 Mar 7;112(5):659-72. [PubMed Link Image]
  10. Chang CL, Zhu XX, Thoraval DH, Ungar D, Rawwas J, Hora N, Strahler JR, Hanash SM, Radany E: Nm23-H1 mutation in neuroblastoma. Nature. 1994 Aug 4;370(6488):335-6. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5342
Enzyme 7 Name Nucleoside diphosphate kinase 7
Enzyme 7 Synonyms
  1. NDK 7
  2. NDP kinase 7
  3. nm23-H7
Enzyme 7 Gene Name NME7
Enzyme 7 Protein Sequence >Nucleoside diphosphate kinase 7 
MNHSERFVFIAEWYDPNASLLRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYDNLHLEDL
FIGNKVNVFSRQLVLIDYGDQYTARQLGSRKEKTLALIKPDAISKAGEIIEIINKAGFTI
TKLKMMMLSRKEALDFHVDHQSRPFFNELIQFITTGPIIAMEILRDDAICEWKRLLGPAN
SGVARTDASESIRALFGTDGIRNAAHGPDSFASAAREMELFFPSSGGCGPANTAKFTNCT
CCIVKPHAVSEGLLGKILMAIRDAGFEISAMQMFNMDRVNVEEFYEVYKGVVTEYHDMVT
EMYSGPCVAMEIQQNNATKTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLP
EDGLLEVQYFFKILDN
Enzyme 7 Number of Residues 376
Enzyme 7 Molecular Weight 42492
Enzyme 7 Theoretical pI 6.44
Enzyme 7 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
—
Enzyme 7 General Function Nucleotide transport and metabolism
Enzyme 7 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate
Enzyme 7 Pathways
Enzyme 7 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 4960169 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9Y5B8 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name NDK7_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1131 bp 
ATGAATCATAGTGAAAGATTCGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
Enzyme 7 GenBank Gene ID AF153191 Link Image
Enzyme 7 GeneCard ID NME7 Link Image
Enzyme 7 GenAtlas ID NME7 Link Image
Enzyme 7 HGNC ID HGNC:20461 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 1q24
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5344
Enzyme 8 Name Nucleoside diphosphate kinase B
Enzyme 8 Synonyms
  1. NDK B
  2. NDP kinase B
  3. nm23-H2
  4. C-myc purine-binding transcription factor PUF
Enzyme 8 Gene Name NME2
Enzyme 8 Protein Sequence >Nucleoside diphosphate kinase B 
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
Enzyme 8 Number of Residues 152
Enzyme 8 Molecular Weight 17298
Enzyme 8 Theoretical pI 8.69
Enzyme 8 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
—
Enzyme 8 General Function Nucleotide transport and metabolism
Enzyme 8 Specific Function Acts as a transcriptional activator of the c-Myc gene; binds DNA nonspecifically (Ref.3)
Enzyme 8 Pathways
Enzyme 8 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 4467843 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P22392 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name NDKB_HUMAN Link Image
Enzyme 8 PDB ID 1NSK Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >459 bp 
ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
Enzyme 8 GenBank Gene ID X58965 Link Image
Enzyme 8 GeneCard ID NME2 Link Image
Enzyme 8 GenAtlas ID NME2 Link Image
Enzyme 8 HGNC ID HGNC:7850 Link Image
Enzyme 8 Chromosome Location 17
Enzyme 8 Locus 17q21.3
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed Link Image]
  2. Stahl JA, Leone A, Rosengard AM, Porter L, King CR, Steeg PS: Identification of a second human nm23 gene, nm23-H2. Cancer Res. 1991 Jan 1;51(1):445-9. [PubMed Link Image]
  3. Postel EH, Berberich SJ, Flint SJ, Ferrone CA: Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis. Science. 1993 Jul 23;261(5120):478-80. [PubMed Link Image]
  4. Webb PA, Perisic O, Mendola CE, Backer JM, Williams RL: The crystal structure of a human nucleoside diphosphate kinase, NM23-H2. J Mol Biol. 1995 Aug 25;251(4):574-87. [PubMed Link Image]
  5. Morera S, Lacombe ML, Xu Y, LeBras G, Janin J: X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution. Structure. 1995 Dec 15;3(12):1307-14. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5345
Enzyme 9 Name Nucleoside diphosphate kinase 3
Enzyme 9 Synonyms
  1. NDK 3
  2. NDP kinase 3
  3. Nucleoside diphosphate kinase C
  4. NDPKC
  5. nm23-H3
  6. DR-nm23
Enzyme 9 Gene Name NME3
Enzyme 9 Protein Sequence >Nucleoside diphosphate kinase 3 
MICLVLTIFANLFPAACTGAHERTFLAVKPDGVQRRLVGEIVRRFERKGFKLVALKLVQA
SEELLREHYAELRERPFYGRLVKYMASGPVVAMVWQGLDVVRTSRALIGATNPADAPPGT
IRGDFCIEVGKNLIHGSDSVESARREIALWFRADELLCWEDSAGHWLYE
Enzyme 9 Number of Residues 169
Enzyme 9 Molecular Weight 19015
Enzyme 9 Theoretical pI 7.97
Enzyme 9 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
—
Enzyme 9 General Function Nucleotide transport and metabolism
Enzyme 9 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Probably has a role in normal hematopoiesis by inhibition of granulocyte differentiation and induction of apoptosis
Enzyme 9 Pathways
Enzyme 9 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-19
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 1051256 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q13232 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name NDK3_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >507 bp 
ATGATCTGCCTGGTGCTGACCATCTTCGCTAACCTCTTCCCCGCGGCCTGCACCGGCGCA
CACGAACGCACCTTCCTGGCCGTGAAGCCGGACGGCGTGCAGCGGCGGCTGGTGGGCGAG
ATTGTGCGGCGCTTCGAGAGGAAGGGCTTCAAGTTGGTGGCGCTGAAGCTGGTGCAGTCC
TCCGAGGAGCTGCTGCGTGAGCACTACGCCGAGCTGCGTGAACGCCCGTTCTACGGCCGC
CTTGTCAAGTATATGGCCTCCGGGCCGGTGGTGGCCATGGTTTGGCAGGGGCTGGACGTG
GTGCGCACCTCGCGGGCGCTCATCGGAGCCACGAACCCGGCCGACGCCCCGCCCGGCACC
ATCCGCGGGGATTTCTGCATCGAGGTTGGCAACCTGATTCACGGCAGCGACTCGGTGGAG
AGTGCCCGCCGCGAGATCGCTCTCTGGTTCCGCGCAGACGAGCTCCTCTGCTGGGAGGAC
AGCGCTGGGCACTGGCTGTATGAGTAG
Enzyme 9 GenBank Gene ID U29656 Link Image
Enzyme 9 GeneCard ID NME3 Link Image
Enzyme 9 GenAtlas ID NME3 Link Image
Enzyme 9 HGNC ID HGNC:7851 Link Image
Enzyme 9 Chromosome Location 16
Enzyme 9 Locus 16q13
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Venturelli D, Martinez R, Melotti P, Casella I, Peschle C, Cucco C, Spampinato G, Darzynkiewicz Z, Calabretta B: Overexpression of DR-nm23, a protein encoded by a member of the nm23 gene family, inhibits granulocyte differentiation and induces apoptosis in 32Dc13 myeloid cells. Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7435-9. [PubMed Link Image]
  2. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5346
Enzyme 10 Name Nucleoside diphosphate kinase 6
Enzyme 10 Synonyms
  1. NDK 6
  2. NDP kinase 6
  3. nm23-H6
  4. Inhibitor of p53-induced apoptosis-alpha
  5. IPIA-alpha
Enzyme 10 Gene Name NME6
Enzyme 10 Protein Sequence >Nucleoside diphosphate kinase 6 
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA
Enzyme 10 Number of Residues 186
Enzyme 10 Molecular Weight 21142
Enzyme 10 Theoretical pI 8.49
Enzyme 10 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
—
Enzyme 10 General Function Nucleotide transport and metabolism
Enzyme 10 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Inhibitor of p53-induced apoptosis
Enzyme 10 Pathways
Enzyme 10 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-24
Enzyme 10 Transmembrane Regions Not Available
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 3228530 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID O75414 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name NDK6_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >561 bp 
ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA
Enzyme 10 GenBank Gene ID AF051941 Link Image
Enzyme 10 GeneCard ID NME6 Link Image
Enzyme 10 GenAtlas ID NME6 Link Image
Enzyme 10 HGNC ID HGNC:20567 Link Image
Enzyme 10 Chromosome Location 3
Enzyme 10 Locus 3p21
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Mehus JG, Deloukas P, Lambeth DO: NME6: a new member of the nm23/nucleoside diphosphate kinase gene family located on human chromosome 3p21.3. Hum Genet. 1999 Jun;104(6):454-9. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5351
Enzyme 11 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Enzyme 11 Synonyms
  1. E- NPP 1
  2. Phosphodiesterase I/nucleotide pyrophosphatase 1
  3. Plasma-cell membrane glycoprotein PC-1[Includes: Alkaline phosphodiesterase I
  4. NPPase]
Enzyme 11 Gene Name ENPP1
Enzyme 11 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 1 
MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPL
EKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNC
RCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINY
SSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKK
CGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEW
YKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLP
KDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLIL
ISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSC
REPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNV
FSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVY
TPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYG
RPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPL
SPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTL
LRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKD
TSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSF
YQQRKEPVSDILKLKTHLPTFSQED
Enzyme 11 Number of Residues 925
Enzyme 11 Molecular Weight 104925
Enzyme 11 Theoretical pI 7.14
Enzyme 11 GO Classification
Function
  • binding
  • catalytic activity
  • endonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
—
Enzyme 11 General Function Not Available
Enzyme 11 Specific Function Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity
Enzyme 11 Pathways
Enzyme 11 Reactions
  • A dinucleotide + H2O = 2 mononucleotides
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • 77-97
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 189650 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P22413 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name ENPP1_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >2622 bp 
ATGGACGTGGGGGAGGAGCCGCTGGAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCC
AACACCTATAAAGTACTCTCGCTGGTATTGTCAGTATGTGTGTTAACAACAATACTTGGT
TGTATATTTGGGTTGAAACCAAGCTGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGT
TTCGAGAGAACATTTGGGAACTGTCGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGC
TGTTTAGATTACCAGGAGACGTGCATAGAACCAGAACATATATGGACTTGCAACAAATTC
AGGTGTGGTGAGAAAAGGTTGACCAGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGAC
AAGGGCGACTGCTGCATCAACTACAGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAA
GAACCATGTGAGAGCATTAATGAGCCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACC
CTCTTATTTTCTTTGGATGGATTCAGGGCAGAATATTTACACACTTGGGGTGGACTTCTT
CCTGTTATTAGCAAACTAAAAAAATGTGGAACATATACTAAAAACATGAGACCGGTATAT
CCAACAAAAACTTTCCCCAATCACTACAGCATTGTCACCGGATTGTATCCAGAATCTCAT
GGCATAATCGACAATAAAATGTATGATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGT
AAAGAGAAATTTAATCCTGAGTGGTACAAAGGAGAACCAATTTGGGTCACAGCTAAGTAT
CAAGGCCTCAAGTCTGGCACATTTTTCTGGCCAGGATCAGATGTGGAAATTAACGGAATT
TTCCCAGACATCTATAAAATGTATAATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCT
GTTCTTCAGTGGCTACAGCTTCCTAAAGATGAAAGACCACACTTTTACACTCTGTATTTA
GAAGAACCAGATTCTTCAGGTCATTCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCC
TTGCAGAGGGTTGATGGTATGGTTGGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTG
CACAGATGCCTGAACCTCATCCTTATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAG
AAATACATATATCTGAATAAATATTTGGGGGATGTTAAAAATATTAAAGTTATCTATGGA
CCTGCAGCTCGATTGAGACCCTCTGATGTCCCAGATAAATACTATTCATTTAACTATGAA
GGCATTGCCCGAAATCTTTCTTGCCGGGAACCAAACCAGCACTTCAAACCTTACCTGAAA
CATTTCTTACCTAAGCGTTTGCACTTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTC
TATTTGGACCCTCAGTGGCAACTTGCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGT
GGATTTCATGGCTCTGACAATGTATTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGA
CCTGGATTCAAGCATGGCATTGAGGCTGACACCTTTGAAAACATTGAAGTCTATAACTTA
ATGTGTGATTTACTGAATTTGACACCGGCTCCTAATAACGGAACTCATGGAAGTCTTAAC
CACCTTCTAAAGAATCCTGTTTATACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTA
CAGTGCCCCTTCACAAGAAACCCCAGAGATAACCTTGGCTGCTCATGTAACCCTTCGATT
TTGCCGATTGAGGATTTTCAAACACAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATT
AAGCATGAAACTTTACCCTATGGAAGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGT
CTTCTTTCCCAGCACCAGTTTATGAGTGGATACAGCCAAGACATCTTAATGCCCCTTTGG
ACATCCTATACCGTGGACAGAAATGACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTG
TACCAGGACTTTAGAATTCCTCTTAGTCCTGTCCATAAATGTTCATTTTATAAAAATAAC
ACCAAAGTGAGTTACGGGTTCCTCTCCCCACCACAACTAAATAAAAATTCAAGTGGAATA
TATTCTGAAGCTTTGCTTACTACAAATATAGTGCCAATGTACCAGAGTTTTCAAGTTATA
TGGCGCTACTTTCATGACACCCTACTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAAT
GTCGTCAGTGGTCCTGTGTTTGACTTTGATTATGATGGACGTTGTGATTCCTTAGAGAAT
CTGAGGCAAAAAAGAAGAGTCATCCGTAACCAAGAAATTTTGATTCCAACTCACTTCTTT
ATTGTGCTAACAAGCTGTAAAGATACATCTCAGACGCCTTTGCACTGTGAAAACCTAGAC
ACCTTAGCTTTCATTTTGCCTCACAGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAG
CATGACTCCTCATGGGTTGAAGAATTGTTAATGTTACACAGAGCACGGATCACAGATGTT
GAGCACATCACTGGACTCAGCTTCTATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTA
AAGTTGAAAACACATTTGCCAACCTTTAGCCAAGAAGACTGA
Enzyme 11 GenBank Gene ID M57736 Link Image
Enzyme 11 GeneCard ID ENPP1 Link Image
Enzyme 11 GenAtlas ID ENPP1 Link Image
Enzyme 11 HGNC ID HGNC:3356 Link Image
Enzyme 11 Chromosome Location 6
Enzyme 11 Locus 6q22-q23
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Buckley MF, Loveland KA, McKinstry WJ, Garson OM, Goding JW: Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. J Biol Chem. 1990 Oct 15;265(29):17506-11. [PubMed Link Image]
  2. Funakoshi I, Kato H, Horie K, Yano T, Hori Y, Kobayashi H, Inoue T, Suzuki H, Fukui S, Tsukahara M, et al.: Molecular cloning of cDNAs for human fibroblast nucleotide pyrophosphatase. Arch Biochem Biophys. 1992 May 15;295(1):180-7. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Pizzuti A, Frittitta L, Argiolas A, Baratta R, Goldfine ID, Bozzali M, Ercolino T, Scarlato G, Iacoviello L, Vigneri R, Tassi V, Trischitta V: A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding region is strongly associated with insulin resistance. Diabetes. 1999 Sep;48(9):1881-4. [PubMed Link Image]
  5. Belli SI, Goding JW: Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities. Eur J Biochem. 1994 Dec 1;226(2):433-43. [PubMed Link Image]
  6. Belli SI, Mercuri FA, Sali A, Goding JW: Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide pyrophosphatase) and analysis of the active site. Eur J Biochem. 1995 Mar 15;228(3):669-76. [PubMed Link Image]
  7. Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed Link Image]
  8. Nakamura I, Ikegawa S, Okawa A, Okuda S, Koshizuka Y, Kawaguchi H, Nakamura K, Koyama T, Goto S, Toguchida J, Matsushita M, Ochi T, Takaoka K, Nakamura Y: Association of the human NPPS gene with ossification of the posterior longitudinal ligament of the spine (OPLL). Hum Genet. 1999 Jun;104(6):492-7. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5486
Enzyme 12 Name Fucose-1-phosphate guanylyltransferase
Enzyme 12 Synonyms
  1. GDP-L-fucose pyrophosphorylase
  2. GDP-L-fucose diphosphorylase
Enzyme 12 Gene Name FPGT
Enzyme 12 Protein Sequence >Fucose-1-phosphate guanylyltransferase 
MAAARDPPEVSLREATQRKLRRFSELRGKLVARGEFWDIVAITAADEKQELAYNQQLSEK
LKRKELPLGVQYHVFVDPAGAKIGNGGSTLCALQCLEKLYGDKWNSFTILLIHSGGYSQR
LPNASALGKIFTALPLGNPIYQMLELKLAMYIDFPLNMNPGILVTCADDIELYSIGEFEF
IRFDKPGFTALAHPSSLTIGTTHGVFVLDPFDDLKHRDLEYRSCHRFLHKPSIEKMYQFN
AVCRPGNFCQQDFAGGDIADLKLDSDYVYTDSLFYMDHKSAKMLLAFYEKIGTLSCEIDA
YGDFLQALGPGATVEYTRNTSNVIKEESELVEMRQRIFHLLKGTSLNVVVLNNSKFYHIG
TTEEYLFYFTSDNSLKSELGLQSITFSIFPDIPECSGKTSCIIQSILDSRCSVAPGSVVE
YSRLGPDVSVGENCIISGSYILTKAALPAHSFVCSLSLKMNRCLKYATMAFGVQDNLKKS
VKTLSDIKLLQFFGVCFLSCLDVWNLKVTEELFSGNKTCLSLWTARIFPVCSSLSDSVIT
SLKMLNAVKNKSAFSLNSYKLLSIEEMLIYKDVEDMITYREQIFLEISLKSSLM
Enzyme 12 Number of Residues 594
Enzyme 12 Molecular Weight 66600
Enzyme 12 Theoretical pI 6.44
Enzyme 12 GO Classification Not Available
Enzyme 12 General Function Not Available
Enzyme 12 Specific Function Catalyzes the formation of GDP-L-fucose from GTP and L- fucose-1-phosphate. Functions as a salvage pathway to reutilize L- fucose arising from the turnover of glycoproteins and glycolipids
Enzyme 12 Pathways
Enzyme 12 Reactions
  • GTP + beta-L-fucose 1-phosphate = diphosphate + GDP-L-fucose
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 2582185 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID O14772 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name FPGT_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1785 bp 
ATGGCAGCTGCTAGGGACCCTCCGGAAGTATCGCTGCGAGAAGCCACCCAGCGAAAATTG
CGGAGGTTTTCCGAGCTAAGAGGCAAACTTGTAGCACGTGGAGAATTCTGGGACATAGTT
GCAATAACAGCGGCTGATGAAAAACAGGAACTTGCTTACAACCAACAGCTGTCAGAAAAG
CTGAAAAGAAAGGAGTTACCCCTTGGAGTTCAATATCACGTTTTTGTGGATCCTGCTGGA
GCCAAAATTGGAAATGGAGGATCAACACTTTGTGCCCTTCAATGTTTGGAAAAGCTATAT
GGAGATAAATGGAATTCTTTTACCATCTTATTAATTCACTCTGGTGGCTACAGTCAACGA
CTTCCAAATGCAAGTGCTCTGGGAAAAATTTTCACTGCTTTACCTCTTGGTAACCCCATT
TATCAGATGCTAGAATTAAAGCTAGCCATGTACATTGATTTCCCCTTAAATATGAATCCT
GGAATTCTGGTTACCTGTGCAGATGATATTGAACTTTATAGTATTGGAGAATTTGAGTTT
ATTAGGTTTGACAAACCTGGCTTTACTGCTTTAGCTCATCCTTCTAGTTTGACGATAGGT
ACCACACATGGAGTATTTGTCTTAGATCCTTTTGATGATTTAAAACATAGAGACCTTGAA
TACAGGTCTTGCCATCGTTTCCTTCATAAGCCCAGCATAGAAAAGATGTATCAGTTTAAT
GCTGTGTGTAGACCTGGAAATTTTTGTCAACAGGACTTTGCTGGGGGTGACATTGCCGAT
CTTAAATTAGACTCTGACTATGTCTACACAGATAGCCTATTTTATATGGATCATAAATCA
GCAAAAATGTTACTTGCTTTTTATGAAAAAATAGGCACACTGAGCTGTGAAATAGATGCC
TATGGTGACTTTCTGCAGGCTTTGGGACCTGGAGCAACTGTGGAGTACACCAGAAACACA
TCACATGTCATTAAAGAAGAGTCAGAGTTGGTAGAAATGAGGCAGAGAATATTTCATCTT
CTTAAAGGAACATCACTAAATGTTGTTGTTCTTAATAACTCCAAATTTTATCACATTGGA
ACAACCGAAGAATATTTGTTTTACTTTACCTCAGATAACAGTTTAAAGTCAGAGCTCGGC
TTACAGTCCATAACTTTTAGTATCTTTCCAGATATACCAGAATGCTCTGGCAAAACATCC
TGTATCATTCAAAGCATACTGGATTCAAGATGTTCTGTGGCACCTGGCTCAGTTGTGGAG
TATTCCAGATTGGGGCCTGATGTTTCAGTTGGGGAAAACTGCATTATTAGTGGTTCTTAC
ATCCTAACAAAAGCTGCCCTCCCCGCACATTCTTTTGTATGTTCCTTAAGCTTAAAGATG
AATAGATGCTTAAAGTATGCAACTATGGCATTTGGAGTGCAAGACAACTTGAAAAAGAGT
GTGAAAACATTGTCAGATATAAAGTTACTTCAATTCTTTGGAGTCTGTTTCCTGTCATGC
TTAGATGTTTGGAATCTTAAAGTTACAGAGGAACTGTTCTCTGGTAACAAGACATGTCTG
AGTTTGTGGACTGCACGCATTTTCCCAGTTTGTTCTTCTTTGAGTGACTCAGTTATAACA
TCCCTAAAGATGTTAAATGCTGTTAAGAACAAGTCAGCATTCAGCCTGAATAGCTATAAG
TTGCTGTCCATTGAAGAAATGCTTATCTACAAAGATGTAGAAGATATGATAACTTACAGG
GAACAAATTTTTCTAGAAATCAGTTTAAAAAGCAGTTTGATGTAG
Enzyme 12 GenBank Gene ID AF017445 Link Image
Enzyme 12 GeneCard ID FPGT Link Image
Enzyme 12 GenAtlas ID FPGT Link Image
Enzyme 12 HGNC ID HGNC:3825 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 1p31.1
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Pastuszak I, Ketchum C, Hermanson G, Sjoberg EJ, Drake R, Elbein AD: GDP-L-fucose pyrophosphorylase. Purification, cDNA cloning, and properties of the enzyme. J Biol Chem. 1998 Nov 13;273(46):30165-74. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5668
Enzyme 13 Name Inosine triphosphate pyrophosphatase
Enzyme 13 Synonyms
  1. ITPase
  2. Inosine triphosphatase
  3. Putative oncogene protein hlc14-06-p
Enzyme 13 Gene Name ITPA
Enzyme 13 Protein Sequence >Inosine triphosphate pyrophosphatase 
MAASLVGKKIVFVTGNAKKLEEVVQILGDKFPCTLVAQKIDLPEYQGEPDEISIQKCQEA
VRQVQGPVLVEDTCLCFNALGGLPGPYIKWFLEKLKPEGLHQLLAGFEDKSAYALCTFAL
STGDPSQPVRLFRGRTSGRIVAPRGCQDFGWDPCFQPDGYEQTYAEMPKAEKNAVSHRFR
ALLELQEYFGSLAA
Enzyme 13 Number of Residues 194
Enzyme 13 Molecular Weight 21446
Enzyme 13 Theoretical pI 5.34
Enzyme 13 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 13 General Function Nucleotide transport and metabolism
Enzyme 13 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 13 Pathways
Enzyme 13 Reactions
  • A nucleoside triphosphate + H2O = a nucleotide + diphosphate
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 13398328 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q9BY32 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name ITPA_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >585 bp 
ATGGCGGCCTCATTGGTGGGGAAGAAGATCGTGTTTGTAACGGGGAACGCCAAGAAGCTG
GAGGAGGTCGTTCAGATTCTAGGAGATAAGTTTCCACGCACTTTGGTGGCACAGAAAATT
GACCTGCCGGAGTACCAGGGGGAGCCGGATGAGATTTCCATACAGAAATGTCAGGAGGCA
GTTCGCCAGGTACAGGGGCCCGTGCTGGTTGAGGACACTTGTCTGTGCTTCAATGCCCTT
GGAGGGCTCCCCGGCCCCTACATAAAGTGGTTTCTGGAGAAGTTAAAGCCTGAAGGTCTC
CACCAGCTCCTGGCCGGGTTCGAGGACAAGTCAGCCTATGCGCTCTGCACGTTTGCACTC
AGCACCGGGGACCCAAGCCAGCCCGTGCGCCTGTTCAGGGGCCGGACCTCGGGCCGGATC
GTGGCACCCAGAGGCTGCCAGGACTTTGGCTGGGACCCCTGCTTTCAGCCTGATGGATAT
GAGCAGACGTACGCAGAGATGCCTAAGGCGGAGAAGAACGCTGTCTCCCATCGCTTCCGG
GCCCTGCTGGAGCTGCAGGAGTACTTTGGCAGTTTGGCAGCTTGA
Enzyme 13 GenBank Gene ID AF219116 Link Image
Enzyme 13 GeneCard ID ITPA Link Image
Enzyme 13 GenAtlas ID ITPA Link Image
Enzyme 13 HGNC ID HGNC:6176 Link Image
Enzyme 13 Chromosome Location 20
Enzyme 13 Locus 20p
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 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. 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]
  4. 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5864
Enzyme 14 Name GMP synthase [glutamine-hydrolyzing]
Enzyme 14 Synonyms
  1. Glutamine amidotransferase
  2. GMP synthetase
Enzyme 14 Gene Name GMPS
Enzyme 14 Protein Sequence >GMP synthase [glutamine-hydrolyzing] 
MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETP
AFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHK
KSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANE
SKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVL
VLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAA
HSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPE
EVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVR
ILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPH
TLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDW
ESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILR
ESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVE
VVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE
Enzyme 14 Number of Residues 693
Enzyme 14 Molecular Weight 76716
Enzyme 14 Theoretical pI 6.86
Enzyme 14 GO Classification
Function
  • ATP binding
  • GMP synthase (glutamine-hydrolyzing) activity
  • GMP synthase (glutamine-hydrolyzing) activity
  • adenyl nucleotide binding
  • binding
  • carbon-nitrogen ligase activity, with glutamine as amido-N-donor
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • molecular function unknown
  • nucleotide binding
  • purine nucleotide binding
Process
  • GMP biosynthesis
  • amino acid and derivative metabolism
  • amino acid metabolism
  • biosynthesis
  • cellular metabolism
  • glutamine family amino acid metabolism
  • glutamine metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside monophosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside monophosphate biosynthesis
Component
—
Enzyme 14 General Function Nucleotide transport and metabolism
Enzyme 14 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 14 Pathways
Enzyme 14 Reactions
  • ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 595410 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P49915 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name GUAA_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 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 14 GenBank Gene ID U10860 Link Image
Enzyme 14 GeneCard ID GMPS Link Image
Enzyme 14 GenAtlas ID GMPS Link Image
Enzyme 14 HGNC ID HGNC:4378 Link Image
Enzyme 14 Chromosome Location 3
Enzyme 14 Locus 3q24
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5893
Enzyme 15 Name Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
Enzyme 15 Synonyms
  1. Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase
  2. Diadenosine tetraphosphatase
  3. Ap4A hydrolase
  4. Ap4Aase
  5. Nucleoside diphosphate-linked moiety X motif 2
  6. Nudix motif 2
Enzyme 15 Gene Name NUDT2
Enzyme 15 Protein Sequence >Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] 
MALRACGLIIFRRCLIPKVDNNAIEFLLLQASDGIHHWTPPKGHVEPGEDDLETALRETQ
EEAGIEAGQLTIIEGFKRELNYVARNKPKTVIYWLAEVKDYDVEIRLSHEHQAYRWLGLE
EACQLAQFKEMKAALQEGHQFLCSIEA
Enzyme 15 Number of Residues 147
Enzyme 15 Molecular Weight 16829
Enzyme 15 Theoretical pI 5.06
Enzyme 15 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 15 General Function Replication, recombination and repair
Enzyme 15 Specific Function Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis
Enzyme 15 Pathways
Enzyme 15 Reactions
  • P1,P4-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 1050960 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P50583 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name AP4A_HUMAN Link Image
Enzyme 15 PDB ID 1XSC Link Image
Enzyme 15 PDB File Show
Enzyme 15 3D Structure
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >60 bp 
ATGCCAGCCCTGTTTTACAGGGAGCCCTGGAGGAGTTGGGATAGAGGCCACATTGACTGA
Enzyme 15 GenBank Gene ID U30313 Link Image
Enzyme 15 GeneCard ID NUDT2 Link Image
Enzyme 15 GenAtlas ID NUDT2 Link Image
Enzyme 15 HGNC ID HGNC:8049 Link Image
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 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]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5924
Enzyme 16 Name Adenylate kinase isoenzyme 5
Enzyme 16 Synonyms
  1. ATP-AMP transphosphorylase
Enzyme 16 Gene Name AK5
Enzyme 16 Protein Sequence >Adenylate kinase isoenzyme 5 
MGGFMEDLRKCKIIFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLI
RDIMERGDLVPSGIVLELLKEAMVASLGDTRGFLIDGYPREVKQGEEFGRRIGDPQLVIC
MDCSADTMTNRLLQRSRSSLPVDDTTKTIAKRLEAYYRASIPVIAYYETKTQLHKINAEG
TPEDVFLQLCTAIDSIIF
Enzyme 16 Number of Residues 198
Enzyme 16 Molecular Weight 22088
Enzyme 16 Theoretical pI 5.16
Enzyme 16 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenylate kinase activity
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleotide binding
  • nucleotide kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • ATP metabolism
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate metabolism
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 16 General Function Nucleotide transport and metabolism
Enzyme 16 Specific Function Active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP
Enzyme 16 Pathways
Enzyme 16 Reactions
  • ATP + AMP = 2 ADP
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 4691541 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q9Y6K8 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name KAD5_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >597 bp 
ATGGGAGGTTTCATGGAAGATTTGAGAAAGTGTAAAATTATTTTCATAATTGGTGGTCCT
GGCTCTGGCAAAGGCACACAGTGTGAAAAGCTGGTGGAAAAATATGGATTTACACATCTC
TCAACTGGCGAGCTCCTGCGTGAGGAACTGGCATCAGAATCTGAAAGAAGCAAATTGATC
AGAGACATTATGGAACGTGGAGACCTGGTGCCCTCAGGCATCGTTTTGGAGCTCCTGAAG
GAGGCCATGGTGGCCAGCCTCGGGGACACCAGGGGCTTCCTGATTGACGGCTATCCTCGG
GAGGTGAAGCAAGGGGAAGAGTTCGGACGCAGGATTGGAGACCCACAGTTGGTGATCTGT
ATGGACTGCTCGGCAGACACCATGACCAACCGCCTTCTCCAAAGGAGCCGGAGCAGCCTG
CCTGTGGACGACACCACCAAGACCATCGCCAAGCGCCTAGAAGCCTACTACCGAGCGTCC
ATCCCCGTGATCGCCTACTACGAGACAAAAACACAGCTACACAAGATAAATGCAGAGGGA
ACACCAGAGGACGTTTTTCTTCAACTCTGCACAGCTATTGACTCTATTATTTTCTGA
Enzyme 16 GenBank Gene ID AF062595 Link Image
Enzyme 16 GeneCard ID AK5 Link Image
Enzyme 16 GenAtlas ID AK5 Link Image
Enzyme 16 HGNC ID HGNC:365 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 1p31
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Van Rompay AR, Johansson M, Karlsson A: Identification of a novel human adenylate kinase. cDNA cloning, expression analysis, chromosome localization and characterization of the recombinant protein. Eur J Biochem. 1999 Apr;261(2):509-17. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5949
Enzyme 17 Name CTP synthase 1
Enzyme 17 Synonyms
  1. UTP--ammonia ligase 1
  2. CTP synthetase 1
Enzyme 17 Gene Name CTPS
Enzyme 17 Protein Sequence >CTP synthase 1 
MKYILVTGGVISGIGKGIIASSVGTILKSCGLHVTSIKIDPYINIDAGTFSPYEHGEVFV
LDDGGEVDLDLGNYERFLDIRLTKDNNLTTGKIYQYVINKERKGDYLGKTVQVVPHITDA
IQEWVMRQALIPVDEDGLEPQVCVIELGGTVGDIESMPFIEAFRQFQFKVKRENFCNIHV
SLVPQPSSTGEQKTKPTQNSVRELRGLGLSPDLVVCRCSNPLDTSVKEKISMFCHVEPEQ
VICVHDVSSIYRVPLLLEEQGVVDYFLRRLDLPIERQPRKMLMKWKEMADRYDRLLETCS
IALVGKYTKFSDSYASVIKALEHSALAINHKLEIKYIDSADLEPITSQEEPVRYHEAWQK
LCSAHGVLVPGGFGVRGTEGKIQAIAWARNQKKPFLGVCLGMQLAVVEFSRNVLGWQDAN
STEFDPTTSHPVVVDMPEHNPGQMGGTMRLGKRRTLFQTKNSVMRKLYGDADYLEERHRH
RFEVNPVWKKCLEEQGLKFVGQDVEGERMEIVELEDHPFFVGVQYHPEFLSRPIKPSPPY
FGLLLASVGRLSHYLQKGCRLSPRDTYSDRSGSSSPDSEITELKFPSINHD
Enzyme 17 Number of Residues 591
Enzyme 17 Molecular Weight 66691
Enzyme 17 Theoretical pI 6.42
Enzyme 17 GO Classification
Function
  • CTP synthase activity
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • pyrimidine nucleotide biosynthesis
  • pyrimidine nucleotide metabolism
Component
—
Enzyme 17 General Function Nucleotide transport and metabolism
Enzyme 17 Specific Function Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen
Enzyme 17 Pathways
Enzyme 17 Reactions
  • ATP + UTP + NH3 = ADP + phosphate + CTP
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 30293 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID P17812 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name PYRG1_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1776 bp 
ATGAAGTACATTCTGGTTACTGGTGGTGTTATATCAGGAATTGGAAAAGGAATCATTGCC
AGCAGTGTGGGCACAATACTCAAGTCATGTGGTTTACATGTAACTTCAATCAAAATTGAC
CCCTACATTAACATTGATGCAGGAACATTCTCTCCTTATGAGCATGGTGAGGTTTTTGTG
CTGGATGATGGTGGGGAAGTAGACCTTGACCTGGGTAACTATGAGCGGTTCCTTGACATC
CGCCTCACCAAGGACAATAATCTGACCACTGGAAAGATATACCAGTATGTCATTAACAAG
GAACGGAAAGGAGATTACTTGGGGAAAACTGTCCAAGTTGTCCCTCATATCACAGATGCA
ATCCAGGAGTGGGTGATGAGACAGGCGTTAATACCTGTAGATGAAGATGGCCTGGAACCT
CAAGTGTGTGTTATTGAGCTTGGTGGAACCGTGGGGGACATAGAAAGCATGCCCTTTATT
GAGGCCTTCCGTCAGTTCCAATTCAAGGTCAAAAGAGAGAACTTTTGTAACATCCACGTC
AGTCTAGTTCCCCAGCCAAGTTCAACAGGGGAACAGAAGACTAAACCTACCCAGAATAGT
GTTCGGGAACTTAGAGGACTTGGGCTTTCCCCAGATCTGGTTGTATGCAGGTGCTCAAAT
CCACTTGACACATCAGTGAAGGAGAAAATATCAATGTTCTGCCATGTTGAGCCTGAACAA
GTGATCTGTGTCCACGATGTCTCATCCATCTACCGAGTCCCCTTGTTGTTAGAGGAGCAA
GGGGTTGTAGATTATTTTCTTCGAAGACTTGACCTTCCTATTGAGAGGCAGCCAAGAAAA
ATGCTGATGAAATGGAAAGAGATGGCTGACAGATATGATCGCTTGCTGGAGACCTGCTCT
ATTGCCCTTGTGGCGAAATACACCGAGTTCTCAGACTCCTATGCCTCTGTCATTAAGGCT
CTGGAGCATTCTGCACTGGCCATCAACCACAAATTGGAAATCAAGTACATAGATTCTGCG
GACTTGGAGCCCATCACCTCGCAAGAAGAGCCCGTGCGCTACCACGAAGCTTGGCAGAAG
CTCTGTAGTGCTCATGGAGTGCTGGTTCCAGGAGGATTTGGTGTTCGAGGAACAGAAGGA
AAAATCCAAGCAATTGCCTGGGCTCGGAATCAGAAAAAGCCTTTTTTGGGCGTGTGCTTA
GGGATGCAGTTGGCAGTGGTTGAATTCTCAAGAAACGTGCTGGGATGGCAAGATGCCAAT
TCTACAGAGTTTGACCCTACGACCAGTCATCCCGTGGTCGTAGACATGCCAGAACACAAC
CCAGGGCAGATGGGCGGAACCATGAGGCTGGGCAAGAGGAGAACCCTGTTCCAGACCAAG
AACTCAGTCATGAGGAAACTCTATGGAGACGCAGACTACTTGGAAGAGAGGCACCGCCAC
CGATTTGAGGTGAATCCAGTCTGGAAAAAGTGTTTGGAAGAACAAGGCTTGAAGTTTGTT
GGCCAAGATGTTGAAGGAGAGAGAATGGAAATTGTGGAGTTAGAAGATCATCCCTTTTTT
GTTGGGGTTCAGTACCACCCTGAGTTCCTGTCCAGGCCTATCAAGCCCTCCCCACCATAC
TTTGGCCTCCTCCTGGCCTCTGTGGGGCGGCTCTCACATTACCTCCAGAAAGGCTGCAGG
CTCTCACCCAGGGACACCTATAGTGACAGGAGTGGAAGCAGCTCCCCTGACTCTGAAATC
ACCGAACTGAAGTTTCCATCAATAAATCATGACTGA
Enzyme 17 GenBank Gene ID X52142 Link Image
Enzyme 17 GeneCard ID CTPS Link Image
Enzyme 17 GenAtlas ID CTPS Link Image
Enzyme 17 HGNC ID HGNC:2519 Link Image
Enzyme 17 Chromosome Location 1
Enzyme 17 Locus 1p34.1
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Yamauchi M, Yamauchi N, Meuth M: Molecular cloning of the human CTP synthetase gene by functional complementation with purified human metaphase chromosomes. EMBO J. 1990 Jul;9(7):2095-9. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5967
Enzyme 18 Name Glutamate dehydrogenase 1, mitochondrial precursor
Enzyme 18 Synonyms
  1. GDH
Enzyme 18 Gene Name GLUD1
Enzyme 18 Protein Sequence >Glutamate dehydrogenase 1, mitochondrial precursor 
MYRYLGEALLLSRAGPAALGSASADSAALLGWARGQPAAAPQPGLALAARRHYSEAVADR
EDDPNFFKMVEGFFDRGASIVEDKLVEDLRTRESEEQKRNRVRGILRIIKPCNHVLSLSF
PIRRDDGSWEVIEGYRAQHSQHRTPCKGGIRYSTDVSVDEVKALASLMTYKCAVVDVPFG
GAKAGVKINPKNYTDNELEKITRRFTMELAKKGFIGPGIDVPAPDMSTGEREMSWIADTY
ASTIGHYDINAHACVTGKPISQGGIHGRISATGRGVFHGIENFINEASYMSILGMTPGFG
DKTFVVQGFGNVGLHSMRYLHRFGAKCIAVGESDGSIWNPDGIDPKELEDFKLQHGSILG
FPKAKPYEGSILEADCDILIPAASEKQLTKSNAPRVKAKIIAEGANGPTTPEADKIFLER
NIMVIPDLYLNAGGVTVSYFEWLKNLNHVSYGRLTFKYERDSNYHLLMSVQESLERKFGK
HGGTIPIVPTAEFQDRISGASEKDIVHSGLAYTMERSARQIMRTAMKYNLGLDLRTAAYV
NAIEKVFKVYNEAGVTFT
Enzyme 18 Number of Residues 558
Enzyme 18 Molecular Weight 61399
Enzyme 18 Theoretical pI 7.91
Enzyme 18 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 18 General Function Replication, recombination and repair
Enzyme 18 Specific Function May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate
Enzyme 18 Pathways
Enzyme 18 Reactions
  • L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + ammonia + NAD(P)H + H+
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-20
Enzyme 18 Transmembrane Regions Not Available
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 31707 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID P00367 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name DHE3_HUMAN Link Image
Enzyme 18 PDB ID 1L1F Link Image
Enzyme 18 PDB File Show
Enzyme 18 3D Structure
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1677 bp 
ATGTACCGCTACCTGGGCGAAGCGCTGTTGCTGTCCCGGGCCGGGCCCGCTGCCCTGGGC
TCGGCGTCCGCCGACTCGGCCGCGTTGCTGGGCTGGGCCCGGGGACAGCCCGCCGCCGCC
CCGCAGCCGGGGCTGGCATTGGCCGCCCGGCGCCACTACAGCGAGGCGGTGGCCGACCGC
GAGGACGACCCCAACTTCTTCAAGATGGTGGAGGGCTTCTTCGATCGCGGCGCCAGCATC
GTGGAGGACAAGCTGGTGGAGGACCTGAGGACCCGGGAGAGCGAGGAGCAGAAGCGGAAC
CGGGTGCGCGGCATCCTGCGGATCATCAAGCCCTGCAACCATGTGCTGAGTCTCTCCTTC
CCCATCCGGCGCGACGACGGCTCCTGGGAGGTCATCGAAGGCTACCGGGCCCAGCACAGC
CAGCACCGCACGCCCTGCAAGGGAGGTATCCGTTACAGCACTGATGTGAGTGTAGATGAA
GTAAAAGCTTTGGCTTCTCTGATGACATACAAGTGTGCAGTGGTTGATGTGCCGTTTGGG
GGTGCTAAAGCTGGTGTTAAGATCAATCCCAAGAACTATACTGATAATGAATTGGAAAAG
ATCACAAGGAGGTTCACCATGGAGCTAGCAAAAAAGGGCTTTATTGGTCCTGGCATTGAT
GTGCCTGCTCCAGACATGAGCACAGGTGAGCGGGAGATGTCCTGGATCGCTGATACCTAT
GCCAGCACCATAGGGCACTATGATATTAATGCACACGCCTGTGTTACTGGTAAACCCATC
AGCCAAGGGGGAATCCATGGACGCATCTCTGCTACTGGCCGTGGTGTCTTCCATGGGATT
GAAAATTTCATCAATGAAGCTTCTTACATGAGCATTTTAGGAATGACACCAGGGTTTGGA
GATAAAACATTTGTTGTTCAGGGATTTGGTAATGTGGGCCTACACTCTATGAGATATTTA
CATCGTTTTGGTGCTAAATGTATTGCTGTTGGTGAGTCTGATGGGAGTATATGGAATCCA
GATGGTATTGACCCAAAGGAACTGGAAGACTTCAAATTGCAACATGGGTCCATTCTGGGC
TTCCCCAAGGCAAAGCCCTATGAAGGAAGCATCTTGGAGGCCGACTGTGACATACTGATC
CCAGCTGCCAGTGAGAAGCAGTTGACCAAATCCAACGCACCCAGAGTCAAAGCCAAGATC
ATTGCTGAAGGTGCCAATGGGCCAACAACTCCAGAAGCTGACAAGATCTTCCTGGAGAGA
AACATTATGGTTATTCCAGATCTCTACTTGAATGCTGGAGGAGTGACAGTATCTTACTTT
GAGTGGCTGAAGAATCTAAATCATGTCAGCTATGGCCGTTTGACCTTCAAATATGAAAGG
GATTCTAACTACCACTTGCTCATGTCTGTTCAAGAGAGTTTAGAAAGAAAATTTGGAAAG
CATGGTGGAACTATTCCCATTGTACCCACGGCAGAGTTCCAAGACAGGATATCGGGTGCA
TCTGAGAAAGACATCGTGCACTCTGGCTTGGCATACACAATGGAGCGTTCTGCCAGGCAA
ATTATGCGCACAGCCATGAAGTATAACCTGGGATTGGACCTGAGAACAGCTGCCTATGTT
AATGCCATTGAGAAAGTCTTCAAAGTGTACAATGAAGCTGGTGTGACCTTCACATAG
Enzyme 18 GenBank Gene ID X07674 Link Image
Enzyme 18 GeneCard ID GLUD1 Link Image
Enzyme 18 GenAtlas ID GLUD1 Link Image
Enzyme 18 HGNC ID HGNC:4335 Link Image
Enzyme 18 Chromosome Location 10
Enzyme 18 Locus 10q23.3
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Nakatani Y, Banner C, von Herrath M, Schneider ME, Smith HH, Freese E: Comparison of human brain and liver glutamate dehydrogenase cDNAS. Biochem Biophys Res Commun. 1987 Dec 16;149(2):405-10. [PubMed Link Image]
  2. Amuro N, Yamaura M, Goto Y, Okazaki T: Molecular cloning and nucleotide sequence of the cDNA for human liver glutamate dehydrogenase precursor. Biochem Biophys Res Commun. 1988 May 16;152(3):1395-400. [PubMed Link Image]
  3. Nakatani Y, Schneider M, Banner C, Freese E: Complete nucleotide sequence of human glutamate dehydrogenase cDNA. Nucleic Acids Res. 1988 Jul 11;16(13):6237. [PubMed Link Image]
  4. Mavrothalassitis G, Tzimagiorgis G, Mitsialis A, Zannis V, Plaitakis A, Papamatheakis J, Moschonas N: Isolation and characterization of cDNA clones encoding human liver glutamate dehydrogenase: evidence for a small gene family. Proc Natl Acad Sci U S A. 1988 May;85(10):3494-8. [PubMed Link Image]
  5. Michaelidis TM, Tzimagiorgis G, Moschonas NK, Papamatheakis J: The human glutamate dehydrogenase gene family: gene organization and structural characterization. Genomics. 1993 Apr;16(1):150-60. [PubMed Link Image]
  6. Julliard JH, Smith EL: Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme. J Biol Chem. 1979 May 10;254(9):3427-38. [PubMed Link Image]
  7. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed Link Image]
  8. Banner C, Silverman S, Thomas JW, Lampel KA, Vitkovic L, Huie D, Wenthold RJ: Isolation of a human brain cDNA for glutamate dehydrogenase. J Neurochem. 1987 Jul;49(1):246-52. [PubMed Link Image]
  9. Tzimagiorgis G, Leversha MA, Chroniary K, Goulielmos G, Sargent CA, Ferguson-Smith M, Moschonas NK: Structure and expression analysis of a member of the human glutamate dehydrogenase (GLUD) gene family mapped to chromosome 10p11.2. Hum Genet. 1993 Jun;91(5):433-8. [PubMed Link Image]
  10. Smith TJ, Peterson PE, Schmidt T, Fang J, Stanley CA: Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation. J Mol Biol. 2001 Mar 23;307(2):707-20. [PubMed Link Image]
  11. Fang J, Hsu BY, MacMullen CM, Poncz M, Smith TJ, Stanley CA: Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations. Biochem J. 2002 Apr 1;363(Pt 1):81-7. [PubMed Link Image]
  12. Smith TJ, Schmidt T, Fang J, Wu J, Siuzdak G, Stanley CA: The structure of apo human glutamate dehydrogenase details subunit communication and allostery. J Mol Biol. 2002 May 3;318(3):765-77. [PubMed Link Image]
  13. Banerjee S, Schmidt T, Fang J, Stanley CA, Smith TJ: Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation. Biochemistry. 2003 Apr 1;42(12):3446-56. [PubMed Link Image]
  14. Meissner T, Beinbrech B, Mayatepek E: Congenital hyperinsulinism: molecular basis of a heterogeneous disease. Hum Mutat. 1999;13(5):351-61. [PubMed Link Image]
  15. Stanley CA, Lieu YK, Hsu BY, Burlina AB, Greenberg CR, Hopwood NJ, Perlman K, Rich BH, Zammarchi E, Poncz M: Hyperinsulinism and hyperammonemia in infants with regulatory mutations of the glutamate dehydrogenase gene. N Engl J Med. 1998 May 7;338(19):1352-7. [PubMed Link Image]
  16. Miki Y, Taki T, Ohura T, Kato H, Yanagisawa M, Hayashi Y: Novel missense mutations in the glutamate dehydrogenase gene in the congenital hyperinsulinism-hyperammonemia syndrome. J Pediatr. 2000 Jan;136(1):69-72. [PubMed Link Image]
  17. Santer R, Kinner M, Passarge M, Superti-Furga A, Mayatepek E, Meissner T, Schneppenheim R, Schaub J: Novel missense mutations outside the allosteric domain of glutamate dehydrogenase are prevalent in European patients with the congenital hyperinsulinism-hyperammonemia syndrome. Hum Genet. 2001 Jan;108(1):66-71. [PubMed Link Image]
  18. MacMullen C, Fang J, Hsu BY, Kelly A, de Lonlay-Debeney P, Saudubray JM, Ganguly A, Smith TJ, Stanley CA: Hyperinsulinism/hyperammonemia syndrome in children with regulatory mutations in the inhibitory guanosine triphosphate-binding domain of glutamate dehydrogenase. J Clin Endocrinol Metab. 2001 Apr;86(4):1782-7. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5977
Enzyme 19 Name Adenylate cyclase type 7
Enzyme 19 Synonyms
  1. Adenylate cyclase type VII
  2. ATP pyrophosphate-lyase 7
  3. Adenylyl cyclase 7
Enzyme 19 Gene Name ADCY7
Enzyme 19 Protein Sequence >Adenylate cyclase type 7 
MPAKGRYFLNEGEEGPDQDALYEKYQLTSQHGPLLLTLLLVAATACVALIIIAFSQGDPS
RHQAILGMAFLVLAVFAALSVLMYVECLLRRWLRALALLTWACLVALGYVLVFDAWTKAA
CAWEQVPFFLFIVFVVYTLLPFSMRGAVAVGAVSTASHLLVLGSLMGGFTTPSVRVGLQL
LANAVIFLCGNLTGAFHKHQMQDASRDLFTYTVKCIQIRRKLRIEKRQQENLLLSVLPAH
ISMGMKLAIIERLKEHGDRRCMPDNNFHSLYVKRHQNVSILYADIVGFTQLASDCSPKEL
VVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDMCQAIKQ
VREATGVDINMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEAT
LKHLDKAYEVEDGHGQQRDPYLKEMNIRTYLVIDPRSQQPPPPSQHLPRPKGDAALKMRA
SVRMTRYLESWGAARPFAHLNHRESVSSGETHVPNGRRPKSVPQRHRRTPDRSMSPKGRS
EDDSYDDEMLSAIEGLSSTRPCCSKSDDFYTFGSIFLEKGFEREYRLAPIPRARHDFACA
SLIFVCILLVHVLLMPRTAALGVSFGLVACVLGLVLGLCFATKFSRCCPARGTLCTISER
VETQPLLRLTLAVLTIGSLLTVAIINLPLMPFQVPELPVGNETGLLAASSKTRALCEPLP
YYTCSCVLGFIACSVFLRMSLEPKVVLLTVALVAYLVLFNLSPCWQWDCCGQGLGNLTKP
NGTTSGTPSCSWKDLKTMTNFYLVLFYITLLTLSRQIDYYCRLDCLWKKKFKKEHEEFET
MENVNRLLLENVLPAHVAAHFIGDKLNEDWYHQSYDCVCVMFASVPDFKVFYTECDVNKE
GLECLRLLNEIIADFDELLLKPKFSGVEKIKTIGSTYMAAAGLSVASGHENQELERQHAH
IGVMVEFSIALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVAS
RMESTGELGKIQVTEETCTILQGLGYSCECRGLINVKGKGELRTYFVCTDTAKFQGLGLN
Enzyme 19 Number of Residues 1080
Enzyme 19 Molecular Weight 120310
Enzyme 19 Theoretical pI 8.16
Enzyme 19 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cell communication
  • cellular metabolism
  • cellular process
  • cyclic nucleotide biosynthesis
  • intracellular signaling cascade
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 19 General Function Signal transduction mechanisms
Enzyme 19 Specific Function This is a membrane-bound, calcium-inhibitable adenylyl cyclase
Enzyme 19 Pathways
Enzyme 19 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • 34-54 63-83 95-117 122-142 147-167 176-196 595-615 620-640 669-688 718-737 746-773 794-814
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 40788941 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID P51828 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name ADCY7_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >3267 bp 
CGACACGCGTGCCAAGGGTGGAGGATGCCAGCCAAGGGGCGCTACTTCCTCAACGAGGGC
GAGGAGGGCCCTGACCAAGATGCGCTCTACGAGAAGTACCAGCTCACCAGCCAGCATGGG
CCGCTGCTGCTCACGCTCCTGCTGGTGGCCGCCACTGCCTGCGTGGCCCTCATCATCATT
GCCTTCAGCCAGGGGGACCCCTCCAGACACCAGGCCATTCTGGGCATGGCGTTCCTGGTG
CTGGCGGTGTTTGCGGCCCTCTCTGTGCTGATGTACGTCGAGTGTCTCCTGCGGCGCTGG
CTCAGGGCCTTGGCGCTGCTCACCTGGGCCTGCTTGGTGGCGCTGGGCTATGTGCTGGTG
TTCGACGCATGGACAAAGGCGGCCTGTGCGTGGGAGCAGGTGCCCTTCTTCCTGTTCATT
GTCTTCGTGGTGTACACACTACTGCCCTTCAGCATGCGGGGCGCTGTCGCCGTTGGGGCC
GTCTCCACTGCCTCCCACCTCCTGGTGCTCGGTTCTTTGATGGGAGGCTTCACGACACCC
AGTGTCCGGGTGGGGCTGCAGCTGCTGGCCAACGCAGTCATCTTCCTGTGTGGGAACCTG
ACAGGCGCCTTCCACAAGCACCAAATGCAGGATGCGTCCCGGGACCTCTTCACCTACACT
GTGAAGTGCATCCAGATCCGCCGGAAGCTGCGCATCGAGAAGCGCCAGCAGGAGAACCTG
CTGCTGTCAGTGCTTCCGGCCCACATCTCCATGGGCATGAAGCTGGCCATCATCGAACGG
CTCAAGGAGCATGGTGACCGTCGCTGCATGCCTGACAACAACTTCCACAGCCTCTACGTC
AAGAGGCACCAGAATGTCAGCATCCTCTATGCGGACATCGTGGGCTTCACGCAGCTGGCC
AGCGACTGTTCTCCCAAGGAGCTGGTGGTGGTGCTGAATGAGCTCTTTGGCAAGTTCGAC
CAGATCGCCAAGGCCAACGAGTGCATGCGAATCAAGATCCTCGGCGACTGCTACTACTGT
GTATCGGGCCTGCCCGTGTCGCTGCCTACCCACGCCCGGAACTGCGTGAAGATGGGGCTG
GACATGTGCCAGGCCATCAAGCAGGTGCGGGAGGCCACGGGCGTGGACATCAACATGCGT
GTGGGCATACACTCGGGGAATGTGCTGTGCGGGGTCATCGGGCTGCGCAAGTGGCAGTAT
GACGTGTGGTCCCACGACGTGTCCCTGGCCAACCGGATGGAGGCAGCCGGAGTACCCGGC
CGGGTGCACATCACGGAGGCCACGCTAAAGCACCTGGACAAGGCGTACGAGGTGGAGGAT
GGGCACGGGCAGCAGCGGGACCCCTACCTCAAGGAGATGAACATCCGCACCTACCTGGTC
ATCGACCCCCGGAGCCAGCAGCCACCCCCGCCCAGCCAACACCTCCCCAGGCCCAAGGGG
GACGCGGCCCTGAAGATGCGGGCGTCAGTGCGCATGACCCGGTACCTCGAGTCCTGGGGG
GCGGCACGGCCCTTTGCACATCTCAACCACCGTGAGAGCGTGAGCAGTGGTGAGACCCAC
GTCCCCAACGGGCGGAGGCCTAAGAGCGTTCCCCAGCGCCACCGCCGGACCCCAGACAGA
AGCATGTCCCCCAAGGGGCGGTCGGAGGATGACTCGTACGATGACGAGATGCTGTCAGCC
ATTGAGGGGCTCAGCTCCACGAGGCCCTGCTGCTCCAAGTCCGATGACTTCTACACCTTT
GGGTCCATCTTCCTGGAGAAGGGCTTTGAGCGCGAGTACCGCCTGGCACCCATCCCCCGG
GCCCGCCACGACTTTGCCTGCGCCAGCCTGATCTTCGTCTGCATCCTGCTCGTCCATGTC
CTGCTCATGCCCAGGACGGCGGCACTGGGTGTGTCCTTCGGGCTGGTGGCCTGTGTACTG
GGGCTGGTGCTGGGCCTGTGCTTTGCCACCAAGTTCTCGAGGTGCTGCCCAGCTCGGGGG
ACGCTCTGCACTATCTCTGAGAGGGTGGAGACACAGCCCCTGCTGAGGCTGACCCTGGCC
GTCCTGACCATCGGCAGCCTGCTCACTGTGGCCATCATCAACCTGCCCCTGATGCCTTTC
CAAGTTCCAGAGCTGCCTGTTGGCAATGAGACAGGCCTACTGGCCGCGAGCAGCAAGACA
AGAGCCCTGTGTGAGCCCCTCCCGTACTACACCTGCAGCTGTGTCCTGGGCTTCATCGCC
TGCTCGGTCTTCCTGAGGATGAGCCTGGAGCCAAAGGTTGTGCTGCTGACAGTGGCCCTG
GTGGCCTACCTGGTGCTCTTCAACCTCTCCCCATGCTGGCAGTGGGACTGCTGCGGCCAA
GGCCTGGGCAACCTCACCAAGCCCAACGGCACCACCAGTGGCACCCCTAGCTGTTCCTGG
AAGGACCTGAAGACCATGACCAATTTCTACCTGGTCCTGTTCTACATCACCCTGCTTACA
CTCTCCAGACAGATTGACTATTACTGCCGCTTGGACTGCCTATGGAAGAAGAAGTTCAAG
AAGGAGCACGAGGAGTTTGAGACCATGGAGAACGTGAACCGCCTTCTTCTGGAGAACGTC
CTGCCAGCCCACGTGGCTGCCCACTTTATCGGTGACAAGTTAAACGAGGACTGGTACCAT
CAGTCCTATGACTGCGTCTGTGTCATGTTTGCCTCCGTGCCGGACTTCAAAGTGTTCTAC
ACAGAGTGCGATGTCAACAAAGAAGGGCTGGAGTGCCTACGCCTGCTCAATGAGATCATT
GCCGACTTCGACGAGCTCCTACTGAAGCCCAAGTTCAGCGGCGTGGAGAAGATCAAGACC
ATCGGCAGCACGTACATGGCAGCTGCAGGGCTCAGCGTCGCCTCAGGGCACGAGAACCAG
GAGCTGGAGCGGCAGCATGCCCACATTGGTGTCATGGTGGAGTTCAGCATCGCCCTGATG
AGTAAGCTGGACGGCATCAACAGGCACTCCTTCAACTCCTTCCGCCTCCGCGTCGGCATA
AACCATGGGCCTGTGATTGCTGGAGTGATTGGGGCCCGAAAACCTCAGTATGACATCTGG
GGAAACACTGTCAATGTGGCCAGCCGAATGGAAAGCACTGGAGAACTTGGGAAAATCCAG
GTTACCGAGGAGACCTGCACCATCCTCCAGGGCCTCGGGTACTCTTGTGAATGCCGTGGC
CTGATCAACGTCAAAGGCAAAGGCGAGCTGAGGACTTACTTTGTCTGTACGGACACTGCC
AAGTTTCAGGGGCTGGGGCTGAACTGA
Enzyme 19 GenBank Gene ID D25538 Link Image
Enzyme 19 GeneCard ID ADCY7 Link Image
Enzyme 19 GenAtlas ID ADCY7 Link Image
Enzyme 19 HGNC ID HGNC:238 Link Image
Enzyme 19 Chromosome Location 16
Enzyme 19 Locus 16q12-q13
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5979
Enzyme 20 Name Adenylate cyclase type 6
Enzyme 20 Synonyms
  1. Adenylate cyclase type VI
  2. ATP pyrophosphate-lyase 6
  3. Adenylyl cyclase 6
  4. Ca(2+-inhibitable adenylyl cyclase
Enzyme 20 Gene Name ADCY6
Enzyme 20 Protein Sequence >Adenylate cyclase type 6 
MSWFSGLLVPKVDERKTAWGERNGQKRSRRRGTRAGGFCTPRYMSCLRDAEPPSPTPAGP
PRCPWQDDAFIRRGGPGKGKELGLRAVALGFEDTEVTTTAGGTAEVAPDAVPRSGRSCWR
RLVQVFQSKQFRSAKLERLYQRYFFQMNQSSLTLLMAVLVLLTAVLLAFHAAPARPQPAY
VALLACAAALFVGLMVVCNRHSFRQDSMWVVSYVVLGILAAVQVGGALAADPRSPSAGLW
CPVFFVYIAYTLLPIRMRAAVLSGLGLSTLHLILAWQLNRGDAFLWKQLGANVLLFLCTN
VIGICTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINT
KKEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHC
LRIKILGDCYYCVSGLPEARADHAHCCVEMGVDMIEAISLVREVTGVNVNMRVGIHSGRV
HCGVLGLRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYLNGDYEVEPGRGGERNA
YLKEQHIETFLILGASQKRKEEKAMLAKLQRTRANSMEGLMPRWVPDRAFSRTKDSKAFR
QMGIDDSSKDNRGTQDALNPEDEVDEFLSRAIDARSIDQLRKDHVRRFLLTFQREDLEKK
YSRKVDPRFGAYVACALLVFCFICFIQLLIFPHSTLMLGIYASIFLLLLITVLICAVYSC
GSLFPKALQRLSRSIVRSRAHSTAVGIFSVLLVFTSAIANMFTCNHTPIRSCAARMLNLT
PADITACHLQQLNYSLGLDAPLCEGTMPTCSFPEYFIGNMLLSLLASSVFLHISSIGKLA
MIFVLGLIYLVLLLLGPPATIFDNYDLLLGVHGLASSNETFDGLDCPAAGRVALKYMTPV
ILLVFALALYLHAQQVESTARLDFLWKLQATGEKEEMEELQAYNRRLLHNILPKDVAAHF
LARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIIS
EERFRQLEKIKTIGSTYMAASGLNASTYDQVGRSHITALADYAMRLMEQMKHINEHSFNN
FQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQVLAAKG
YQLECRGVVKVKGKGEMTTYFLNGGPSS
Enzyme 20 Number of Residues 1168
Enzyme 20 Molecular Weight 130617
Enzyme 20 Theoretical pI 8.27
Enzyme 20 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cell communication
  • cellular metabolism
  • cellular process
  • cyclic nucleotide biosynthesis
  • intracellular signaling cascade
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 20 General Function Signal transduction mechanisms
Enzyme 20 Specific Function Membrane-bound, calcium-inhibitable adenylyl cyclase
Enzyme 20 Pathways
Enzyme 20 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • 152-168 181-197 214-230 239-255 259-275 289-305 674-691 702-718 743-759 820-836 839-855 897-913
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 9049783 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID O43306 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name ADCY6_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >3507 bp 
ATGTCATGGTTTAGTGGCCTCCTGGTCCCTAAAGTGGATGAACGGAAAACAGCCTGGGGC
GAACGCAATGGGCAGAAGCGTTCGCGGCGCCGTGGCACTCGGGCAGGTGGCTTCTGCACG
CCCCGCTATATGAGCTGCCTCCGGGATGCAGAGCCACCCAGCCCCACCCCTGCCGGCCCC
CCTCGGTGCCCCTGGCAGGATGACGCCTTCATCCGGAGGGGCGGCCCAGGCAAGGGCAAG
GAGCTGGGGCTGCGGGCAGTGGCCCTGGGCTTCGAGGATACCGAGGTGACAACGACAGCG
GGCGGGACGGCTGAGGTGGCGCCCGACGCGGTGCCCAGGAGTGGGCGATCCTGCTGGCGC
CGTCTGGTGCAGGTGTTCCAGTCGAAGCAGTTCCGTTCGGCCAAGCTGGAGCGCCTGTAC
CAGCGGTACTTCTTCCAGATGAACCAGAGCAGCCTGACGCTGCTGATGGCGGTGCTGGTG
CTGCTCACAGCGGTGCTGCTGGCTTTCCACGCCGCACCCGCCCGCCCTCAGCCTGCCTAT
GTGGCACTGTTGGCCTGTGCCGCCGCCCTGTTCGTGGGGCTCATGGTGGTGTGTAACCGG
CATAGCTTCCGCCAGGACTCCATGTGGGTGGTGAGCTACGTGGTGCTGGGCATCCTGGCG
GCAGTGCAGGTCGGGGGCGCTCTCGCAGCAGACCCGCGCAGCCCCTCTGCGGGCCTCTGG
TGCCCTGTGTTCTTTGTCTACATCGCCTACACGCTCCTCCCCATCCGCATGCGGGCTGCC
GTCCTCAGCGGCCTGGGCCTCTCCACCTTGCATTTGATCTTGGCCTGGCAACTTAACCGT
GGTGATGCCTTCCTCTGGAAGCAGCTCGGTGCCAATGTGCTGCTGTTCCTCTGCACCAAC
GTCATTGGCATCTGCACACACTATCCAGCAGAGGTGTCTCAGCGCCAGGCCTTTCAGGAG
ACCCGCGGTTACATCCAGGCCCGGCTCCACCTGCAGCATGAGAATCGGCAGCAGGAGCGG
CTGCTGCTGTCGGTATTGCCCCAGCACGTTGCCATGGAGATGAAAGAAGACATCAACACA
AAAAAAGAAGACATGATGTTCCACAAGATCTACATACAGAAGCATGACAATGTCAGCATC
CTGTTTGCAGACATTGAGGGCTTCACCAGCCTGGCATCCCAGTGCACTGCGCAGGAGCTG
GTCATGACCCTGAATGAGCTCTTTGCCCGGTTTGACAAGCTGGCTGCGGAGAATCACTGC
CTGAGGATCAAGATCTTGGGGGACTGTTACTACTGTGTGTCAGGGCTGCCGGAGGCCCGG
GCCGACCATGCCCACTGCTGTGTGGAGATGGGGGTAGACATGATTGAGGCCATCTCGCTG
GTACGTGAGGTGACAGGTGTGAATGTGAACATGCGCGTGGGCATCCACAGCGGGCGCGTG
CACTGCGGCGTCCTTGGCTTGCGGAAATGGCAGTTCGATGTGTGGTCCAATGATGTGACC
CTGGCCAACCACATGGAGGCAGGAGGCCGGGCTGGCCGCATCCACATCACTCGGGCAACA
CTGCAGTACCTGAACGGGGACTACGAGGTGGAGCCAGGCCGTGGTGGCGAGCGCAACGCG
TACCTCAAGGAGCAGCACATTGAGACTTTCCTCATCCTGGGCGCCAGCCAGAAACGGAAA
GAGGAGAAGGCCATGCTGGCCAAGCTGCAGCGGACTCGGGCCAACTCCATGGAAGGGCTG
ATGCCGCGCTGGGTTCCTGATCGTGCCTTCTCCCGGACCAAGGACTCCAAGGCCTTCCGC
CAGATGGGCATTGATGATTCCAGCAAAGACAACCGGGGCACCCAAGATGCCCTGAACCCT
GAGGATGAGGTGGATGAGTTCCTGAGCCGTGCCATCGATGCCCGCAGCATTGATCAGCTG
CGGAAGGACCATGTGCGCCGGTTTCTGCTCACCTTCCAGAGAGAGGATCTTGAGAAGAAG
TACTCCCGGAAGGTGGATCCCCGCTTCGGAGCCTACGTTGCCTGTGCCCTGTTGGTCTTC
TGCTTCATCTGCTTCATCCAGCTTCTCATCTTCCCACACTCCACCCTGATGCTTGGGATC
TATGCCAGCATCTTCCTGCTGCTGCTAATCACCGTGCTGATCTGTGCTGTGTACTCCTGT
GGTTCTCTGTTCCCTAAGGCCCTGCAACGTCTGTCCCGCAGCATTGTCCGCTCACGGGCA
CATAGCACCGCAGTTGGCATCTTTTCCGTCCTGCTTGTGTTTACTTCTGCCATTGCCAAC
ATGTTCACCTGTAACCACACCCCCATACGGAGCTGTGCAGCCCGGATGCTGAATTTAACA
CCTGCTGACATCACTGCCTGCCACCTGCAGCAGCTCAATTACTCTCTGGGCCTGGATGCT
CCCCTGTGTGAGGGCACCATGCCCACCTGCAGCTTTCCTGAGTACTTCATCGGGAACATG
CTGCTGAGTCTCTTGGCCAGCTCTGTCTTCCTGCACATCAGCAGCATCGGGAAGTTGGCC
ATGATCTTTGTCTTGGGGCTCATCTATTTGGTGCTGCTTCTGCTGGGTCCCCCAGCCACC
ATCTTTGACAACTATGACCTACTGCTTGGCGTCCATGGCTTGGCTTCTTCCAATGAGACC
TTTGATGGGCTGGACTGTCCAGCTGCAGGGAGGGTGGCCCTCAAATATATGACCCCTGTG
ATTCTGCTGGTGTTTGCGCTGGCGCTGTATCTGCATGCTCAGCAGGTGGAGTCGACTGCC
CGCCTAGACTTCCTCTGGAAACTACAGGCAACAGGGGAGAAGGAGGAGATGGAGGAGCTA
CAGGCATACAACCGGAGGCTGCTGCATAACATTCTGCCCAAGGACGTGGCGGCCCACTTC
CTGGCCCGGGAGCGCCGCAATGATGAACTCTACTATCAGTCGTGTGAGTGTGTGGCTGTT
ATGTTTGCCTCCATTGCCAACTTCTCTGAGTTCTATGTGGAGCTGGAGGCAAACAATGAG
GGTGTCGAGTGCCTGCGGCTGCTCAACGAGATCATCGCTGACTTTGATGAGATTATCAGC
GAGGAGCGGTTCCGGCAGCTGGAAAAGATCAAGACGATTGGTAGCACCTACATGGCTGCC
TCAGGGCTGAACGCCAGCACCTACGATCAGGTGGGCCGCTCCCACATCACTGCCCTGGCT
GACTACGCCATGCGGCTCATGGAGCAGATGAAGCACATCAATGAGCACTCCTTCAACAAT
TTCCAGATGAAGATTGGGCTGAACATGGGCCCAGTCGTGGCAGGTGTCATCGGGGCTCGG
AAGCCACAGTATGACATCTGGGGGAACACAGTGAATGTCTCTAGTCGTATGGACAGCACG
GGGGTCCCCGACCGAATCCAGGTGACCACGGACCTGTACCAGGTTCTAGCTGCCAAGGGC
TACCAGCTGGAGTGTCGAGGGGTGGTCAAGGTGAAGGGCAAGGGGGAGATGACCACCTAC
TTCCTCAATGGGGGCCCCAGCAGTTAA
Enzyme 20 GenBank Gene ID AF250226 Link Image
Enzyme 20 GeneCard ID ADCY6 Link Image
Enzyme 20 GenAtlas ID ADCY6 Link Image
Enzyme 20 HGNC ID HGNC:237 Link Image
Enzyme 20 Chromosome Location 12
Enzyme 20 Locus 12q12-q13
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Wicker R, Catalan AG, Cailleux A, Starenki D, Stengel D, Sarasin A, Suarez HG: Cloning and expression of human adenylyl cyclase type VI in normal thyroid tissues. Biochim Biophys Acta. 2000 Sep 7;1493(1-2):279-83. [PubMed Link Image]
  2. Ishikawa K, Nagase T, Nakajima D, Seki N, Ohira M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1997 Oct 31;4(5):307-13. [PubMed Link Image]
  3. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5980
Enzyme 21 Name Adenylate cyclase type 5
Enzyme 21 Synonyms
  1. Adenylate cyclase type V
  2. ATP pyrophosphate-lyase 5
  3. Adenylyl cyclase 5
Enzyme 21 Gene Name ADCY5
Enzyme 21 Protein Sequence >Adenylate cyclase type 5 
MSGSKSVSPPGYAAQKTAAPAPRGGPEHRSAWGEADSRANGYPHAPGGSARGSTKKPGGA
VTPQQQQRLASRWRSDDDDDPPLSGDDPLAGGFGFSFRSKSAWQERGGDDCGRGSRRQRR
GAASGGSTRAPPAGGGGGSAAAAASAGGTEVRPRSVEVGLEERRGKGRAADELEAGAVEG
GEGSGDGGSSADSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQS
SLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGL
ACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSAL
HLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLH
SQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTS
LASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEM
GMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGK
AGRIHITKATLNYLNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAKMN
RQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFL
GRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQI
TIVPHSIFMLSFYLTCSLLLTLVVFVSVIYSCVKLFPSPLQTLSRKIVRSKMNSTLVGVF
TITLVFLAAFVNMFTCNSRDLLGCLAQEHNISASQVNACHVAESAVNYSLGDEQGFCGSP
WPNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIELIYVLIVEVPGVTLFDNADL
LVTANAIDFFNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKL
QATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANF
SEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTY
DKVGKTHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWG
NTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPL
S
Enzyme 21 Number of Residues 1261
Enzyme 21 Molecular Weight 138909
Enzyme 21 Theoretical pI 7.25
Enzyme 21 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cell communication
  • cellular metabolism
  • cellular process
  • cyclic nucleotide biosynthesis
  • intracellular signaling cascade
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 21 General Function Signal transduction mechanisms
Enzyme 21 Specific Function This is a membrane-bound, calcium-inhibitable adenylyl cyclase
Enzyme 21 Pathways
Enzyme 21 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • 196-216 242-262 268-288 299-319 325-345 349-369 374-394 770-790 792-812 836-856 910-930 935-955 984-1004
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein Not Available
Enzyme 21 UniProtKB/Swiss-Prot ID O95622 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name ADCY5_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence Not Available
Enzyme 21 GenBank Gene ID AC025571 Link Image
Enzyme 21 GeneCard ID ADCY5 Link Image
Enzyme 21 GenAtlas ID ADCY5 Link Image
Enzyme 21 HGNC ID HGNC:236 Link Image
Enzyme 21 Chromosome Location 3
Enzyme 21 Locus 3q13.2-q21
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Ludwig MG, Seuwen K: Characterization of the human adenylyl cyclase gene family: cDNA, gene structure, and tissue distribution of the nine isoforms. J Recept Signal Transduct Res. 2002 Feb-Nov;22(1-4):79-110. [PubMed Link Image]
  2. Raimundo S, Giray J, Volff JN, Schwab M, Altenbuchner J, Ratge D, Wisser H: Cloning and sequence of partial cDNAs encoding the human type V and VI adenylyl cyclases and subsequent RNA-quantification in various tissues. Clin Chim Acta. 1999 Jul;285(1-2):155-61. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5981
Enzyme 22 Name Adenylate cyclase type 8
Enzyme 22 Synonyms
  1. Adenylate cyclase type VIII
  2. ATP pyrophosphate-lyase 8
  3. Adenylyl cyclase 8
  4. Ca(2+/calmodulin- activated adenylyl cyclase
Enzyme 22 Gene Name ADCY8
Enzyme 22 Protein Sequence >Adenylate cyclase type 8 
MELSDVRCLTGSEELYTIHPTPPAGDGRSASRPQRLLWQTAVRHITEQRFIHGHRGGSGS
GSGGSGKASDPAGGGPNHHAPQLSGDSALPLYSLGPGERAHSTCGTKVFPERSGSGSASG
SGGGGDLGFLHLDCAPSNSDFFLNGGYSYRGVIFPTLRNSFKSRDLERLYQRYFLGQRRK
SEVVMNVLDVLTKLTLLVLHLSLASAPMDPLKGILLGFFTGIEVVICALVVVRKDTTSHT
YLQYSGVVTWVAMTTQILAAGLGYGLLGDGIGYVLFTLFATYSMLPLPLTWAILAGLGTS
LLQVILQVVIPRLAVISINQVVAQAVLFMCMNTAGIFISYLSDRAQRQAFLETRRCVEAR
LRLETENQRQERLVLSVLPRFVVLEMINDMTNVEDEHLQHQFHRIYIHRYENVSILFADV
KGFTNLSTTLSAQELVRMLNELFARFDRLAHEHHCLRIKILGDCYYCVSGLPEPRQDHAH
CCVEMGLSMIKTIRYVRSRTKHDVDMRIGIHSGSVLCGVLGLRKWQFDVWSWDVDIANKL
ESGGIPGRIHISKATLDCLNGDYNVEEGHGKERNEFLRKHNIETYLIKQPEDSLLSLPED
IVKESVSSSDRRNSGATFTEGSWSPELPFDNIVGKQNTLAALTRNSINLLPNHLAQALHV
QSGPEEINKRIEHTIDLRSGDKLRREHIKPFSLMFKDSSLEHKYSQMRDEVFKSNLVCAF
IVLLFITAIQSLLPSSRVMPMTIQFSILIMLHSALVLITTAEDYKCLPLILRKTCCWINE
TYLARNVIIFASILINFLGAILNILWCDFDKSIPLKNLTFNSSAVFTDICSYPEYFVFTG
VLAMVTCAVFLRLNSVLKLAVLLIMIAIYALLTETVYAGLFLRYDNLNHSGEDFLGTKEV
SLLLMAMFLLAVFYHGQQLEYTARLDFLWRVQAKEEINEMKELREHNENMLRNILPSHVA
RHFLEKDRDNEELYSQSYDAVGVMFASIPGFADFYSQTEMNNQGVECLRLLNEIIADFDE
LLGEDRFQDIEKIKTIGSTYMAVSGLSPEKQQCEDKWGHLCALADFSLALTESIQEINKH
SFNNFELRIGISHGSVVAGVIGAKKPQYDIWGKTVNLASRMDSTGVSGRIQVPEETYLIL
KDQGFAFDYRGEIYVKGISEQEGKIKTYFLLGRVQPNPFILPPRRLPGQYSLAAVVLGLV
QSLNRQRQKQLLNENNNTGIIKGHYNRRTLLSPSGTEPGAQAEGTDKSDLP
Enzyme 22 Number of Residues 1251
Enzyme 22 Molecular Weight 140124
Enzyme 22 Theoretical pI 6.99
Enzyme 22 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cell communication
  • cellular metabolism
  • cellular process
  • cyclic nucleotide biosynthesis
  • intracellular signaling cascade
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • signal transduction
Component
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
Enzyme 22 General Function Signal transduction mechanisms
Enzyme 22 Specific Function This is a membrane-bound, calcium-inhibitable adenylyl cyclase. May be involved in learning, in memory and in drug dependence
Enzyme 22 Pathways
Enzyme 22 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • 183-203 212-232 247-267 274-294 296-316 321-341 716-736 738-758 787-807 831-851 861-881 894-914
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 516263 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID P40145 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name ADCY8_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >3756 bp 
ATGGAGCTCTCCGATGTGCGCTGCCTTACAGGCAGCGAGGAACTCTACACCATCCACCCG
ACGCCCCCGGCCGGCGACGGCAGGAGCGCCTCCCGGCCGCAGCGGCTGCTGTGGCAGACG
GCGGTGCGACACATCACGGAGCAGCGCTTCATTCACGGGCACCGGGGAGGCAGCGGCAGC
GGGAGTGGAGGCTCGGGCAAAGCCTCGGACCCTGCGGGCGGCGGCCCCAACCACCACGCG
CCGCAGCTGTCAGGCGACTCGGCGCTGCCCCTCTACTCGCTGGGCCCGGGAGAGCGAGCG
CACAGCACCTGCGGCACCAAAGTCTTCCCGGAACGCAGCGGGAGCGGCAGTGCCAGCGGC
AGCGGAGGCGGGGGCGACCTGGGCTTCCTGCACCTTGACTGTGCCCCTAGCAACTCGGAT
TTCTTTCTTAATGGGGGCTATAGCTACCGAGGGGTCATTTTCCCCACCCTGCGCAACTCC
TTCAAATCTCGGGATTTGGAACGCCTCTACCAGCGCTATTTCTTGGGCCAAAGGCGCAAA
TCGGAAGTGGTGATGAACGTGCTGGACGTGCTGACCAAACTCACTCTCTTGGTCCTACAC
TTGAGCCTGGCCTCGGCCCCCATGGACCCGCTCAAGGGCATCCTGCTGGGCTTCTTCACC
GGCATTGAGGTAGTGATCTGCGCCCTGGTGGTGGTCAGGAAGGACACCACCTCCCACACG
TACCTGCAGTACAGCGGCGTGGTCACCTGGGTGGCCATGACCACCCAGATCCTGGCAGCA
GGCCTCGGCTACGGGCTCCTGGGCGACGGCATAGGCTACGTGCTCTTCACGCTCTTCGCC
ACCTACAGTATGCTGCCGCTGCCGCTCACCTGGGCCATCCTGGCCGGCCTGGGCACCTCG
CTGCTGCAGGTCATCCTCCAAGTGGTCATACCCCGGCTGGCGGTCATTTCCATCAACCAG
GTTGTGGCCCAGGCAGTGCTATTCATGTGTATGAACACAGCTGGAATCTTCATCAGTTAC
CTGTCAGACCGGGCCCAGCGCCAAGCTTTCCTGGAGACTCGGAGGTGTGTGGAGGCCAGG
CTGCGCCTGGAGACAGAGAACCAAAGACAGGAGCGGCTCGTGCTTTCTGTGCTCCCCCGG
TTTGTTGTCCTGGAAATGATCAACGACATGACCAATGTGGAAGATGAGCACCTGCAGCAC
CAGTTCCATCGGATCTACATCCATCGCTATGAGAACGTCAGTATTCTTTTTGCAGATGTT
AAAGGATTTACCAACCTCTCCACGACCTTGTCTGCTCAGGAGCTGGTCAGGATGCTCAAC
GAGCTCTTTGCCAGATTTGATCGACTGGCCCATGAGCATCACTGCCTTCGTATTAAAATC
CTGGGGGACTGCTACTACTGCGTGTCTGGACTTCCTGAGCCCCGCCAGGACCATGCCCAC
TGCTGTGTTGAAATGGGTCTCAGCATGATCAAAACCATCAGGTATGTGCGGTCAAGGACA
AAACACGATGTTGACATGAGGATTGGAATCCACTCCGGCTCGGTGCTGTGCGGTGTTTTG
GGACTACGGAAGTGGCAGTTTGATGTCTGGTCTTGGGATGTGGATATTGCAAACAAACTC
GAATCTGGAGGAATCCCCGGGAGGATTCACATTTCCAAAGCCACGCTGGACTGTCTCAAC
GGTGACTATAACGTGGAAGAGGGCCATGGTAAAGAGAGGAATGAATTCCTGAGGAAGCAT
AATATCGAAACTTACTTAATTAAGCAGCCTGAGGACAGTCTGCTGTCCTTGCCTGAAGAT
ATCGTCAAGGAGTCAGTGAGCTCCTCAGACCGGAGAAACAGTGGGGCCACATTCACTGAA
GGATCCTGGAGCCCTGAACTGCCCTTTGATAATATCGTGGGGAAACAGAATACTCTGGCT
GCCCTAACAAGAAATTCAATAAATCTGCTTCCAAACCATCTTGCACAAGCTTTGCATGTC
CAGTCTGGGCCTGAGGAAATTAACAAGAGAATAGAACATACCATCGACTTGCGGAGTGGC
GATAAATTGAGAAGAGAGCATATCAAGCCATTCTCACTGATGTTTAAAGACTCCAGCCTG
GAGCACAAGTATTCTCAAATGAGGGATGAAGTGTTCAAGTCAAACTTGGTCTGTGCATTT
ATCGTTCTTCTATTTATCACGGCAATACAAAGTTTGCTTCCTTCTTCAAGAGTGATGCCA
ATGACCATCCAGTTCTCCATTCTGATTATGCTGCACTCGGCTCTGGTCCTCATCACCACA
GCAGAGGATTATAAATGTTTGCCCCTCATCCTCCGGAAAACTTGCTGTTGGATTAATGAG
ACCTATTTGGCCCGGAACGTCATCATCTTTGCATCCATTTTGATTAATTTCCTGGGTGCC
ATCTTAAATATCCTGTGGTGTGATTTTGACAAGTCGATACCCTTGAAGAACCTGACTTTC
AATTCCTCAGCTGTGTTTACAGATATCTGCTCCTACCCAGAGTACTTTGTCTTCACGGGG
GTGTTGGCCATGGTGACCTGTGCAGTTTTCCTCCGGCTGAACTCCGTCCTGAAGCTGGCA
GTGCTGCTGATCATGATTGCCATCTATGCCCTGCTCACTGAGACCGTCTACGCAGGCCTC
TTTCTGCGTTATGACAACCTCAACCACAGTGGAGAAGATTTCCTGGGGACCAAGGAGGTA
TCACTGCTACTGATGGCCATGTTCCTCCTGGCTGTGTTCTACCATGGACAGCAGCTGGAG
TACACAGCCCGCCTGGACTTCCTTTGGCGAGTACAGGCCAAAGAGGAGATCAATGAGATG
AAGGAGCTGAGGGAACACAATGAGAACATGCTCCGGAATATCTTACCCAGCCATGTGGCC
CGCCATTTCCTAGAGAAGGACCGAGACAATGAGGAGCTGTATTCTCAATCCTATGATGCT
GTTGGGGTGATGTTTGCCTCCATCCCAGGATTTGCGGACTTTTACTCTCAGACTGAAATG
AATAACCAGGGAGTGGAATGCCTGCGCTTGCTCAATGAGATCATTGCTGACTTCGATGAG
TTGCTTGGTGAAGACCGATTTCAAGACATTGAAAAGATTAAGACCATTGGCAGCACCTAC
ATGGCCGTGTCAGGCCTGTCACCTGAAAAACAGCAATGTGAAGACAAGTGGGGACATTTG
TGTGCTCTGGCTGACTTCTCACTCGCCCTGACAGAAAGCATACAGGAGATCAACAAGCAT
TCATTCAACAATTTTGAACTCCGGATTGGCATCAGCCACGGCTCAGTGGTAGCTGGCGTT
ATCGGCGCTAAGAAACCACAGTATGACATTTGGGGCAAAACTGTGAACCTGGCAAGCCGA
ATGGACAGCACGGGGGTTAGTGGCCGGATCCAAGTCCCAGAGGAGACCTATCTCATCCTG
AAGGACCAGGGCTTTGCCTTTGATTACCGAGGGGAGATCTATGTGAAGGGTATCAGTGAA
CAGGAAGGAAAAATCAAAACGTACTTTCTTCTGGGAAGAGTCCAACCCAACCCATTCATC
TTGCCCCCAAGAAGACTGCCTGGGCAGTACTCCCTGGCCGCGGTTGTCCTGGGACTTGTC
CAGTCCCTCAATAGGCAAAGGCAGAAGCAGCTACTCAATGAGAACAACAACACAGGAATC
ATCAAGGGTCATTACAACCGGCGGACTTTGTTGTCACCCAGCGGCACAGAGCCTGGAGCC
CAGGCTGAAGGCACCGACAAATCTGATTTGCCATAA
Enzyme 22 GenBank Gene ID Z35309 Link Image
Enzyme 22 GeneCard ID ADCY8 Link Image
Enzyme 22 GenAtlas ID ADCY8 Link Image
Enzyme 22 HGNC ID HGNC:239 Link Image
Enzyme 22 Chromosome Location 8
Enzyme 22 Locus 8q24
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Defer N, Marinx O, Stengel D, Danisova A, Iourgenko V, Matsuoka I, Caput D, Hanoune J: Molecular cloning of the human type VIII adenylyl cyclase. FEBS Lett. 1994 Aug 29;351(1):109-13. [PubMed Link Image]
  2. Parma J, Stengel D, Gannage MH, Poyard M, Barouki R, Hanoune J: Sequence of a human brain adenylyl cyclase partial cDNA: evidence for a consensus cyclase specific domain. Biochem Biophys Res Commun. 1991 Aug 30;179(1):455-62. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5983
Enzyme 23 Name Adenylate cyclase type 3
Enzyme 23 Synonyms
  1. Adenylate cyclase type III
  2. ATP pyrophosphate-lyase 3
  3. Adenylyl cyclase 3
  4. AC-III
  5. AC3
  6. Adenylate cyclase, olfactive type
Enzyme 23 Gene Name ADCY3
Enzyme 23 Protein Sequence >Adenylate cyclase type 3 
MPRNQGFSEPEYSAEYSAEYSVSLPSDPDRGVGRTHEISVRNSGSCLCLPRFMRLTFVPE
SLENLYQTYFKRQRHETLLVLVVFAALFDCYVVVMCAVVFSSDKLASLAVAGIGLVLDII
LFVLCKKGLLPDRVTRRVLPYVLWLLITAQIFSYLGLNFARAHAASDTVGWQVFFVFSFF
ITLPLSLSPIVIISVVSCVVHTLVLGVTVAQQQQEELKGMQLLREILANVFLYLCAIAVG
IMSYYMADRKHRKAFLEARQSLEVKMNLEEQSQQQENLMLSILPKHVADEMLKDMKKDES
QKDQQQFNTMYMYRHENVSILFADIVGFTQLSSACSAQELVKLLNELFARFDKLAAKYHQ
LRIKILGDCYYCICGLPDYREDHAVCSILMGLAMVEAISYVREKTKTGVDMRVGVHTGTV
LGGVLGQKRWQYDVWSTDVTVANKMEAGGIPGRVHISQSTMDCLKGEFDVEPGDGGSRCD
YLEEKGIETYLIIASKPEVKKTATQNGLNGSALPNGAPASSKSSSPALIETKEPNGSAHS
SGSTSEKPEEQDAQADNPSFPNPRRRLRLQDLADRVVDASEDEHELNQLLNEALLERESA
QVVKKRNTFLLSMRFMDPEMETRYSVEKEKQSGAAFSCSCVVLLCTALVEILIDPWLMTN
YVTFMVGEILLLILTICSLAAIFPRAFPKKLVAFSTWIDRTRWARNTWAMLAIFILVMAN
VVDMLSCLQYYTGPSNATAGMETEGSCLENPKYYNYVAVLSLIATIMLVQVSHMVKLTLM
LLVAGAVATINLYAWRPVFDEYDHKRFREHDLPMVALEQMQGFNPGLNGTDRLPLVPSKY
SMTVMVFLMMLSFYYFSRHVEKLARTLFLWKIEVHDQKERVYEMRRWNEALVTNMLPEHV
ARHFLGSKKRDEELYSQTYDEIGVMFASLPNFADFYTEESINNGGIECLRFLNEIISDFD
SLLDNPKFRVITKIKTIGSTYMAASGVTPDVNTNGFASSNKEDKSERERWQHLADLADFA
LAMKDTLTNINNQSFNNFMLRIGMNKGGVLAGVIGARKPHYDIWGNTVNVASRMESTGVM
GNIQVVEETQVILREYGFRFVRRGPIFVKGKGELLTFFLKGRDKLATFPNGPSVTLPHQV
VDNS
Enzyme 23 Number of Residues 1144
Enzyme 23 Molecular Weight 128962
Enzyme 23 Theoretical pI 6.55
Enzyme 23 GO Classification
Function
  • catalytic activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cell communication
  • cellular metabolism
  • cellular process
  • cyclic nucleotide biosynthesis
  • intracellular signaling cascade
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • signal transduction
Component
—
Enzyme 23 General Function Signal transduction mechanisms
Enzyme 23 Specific Function Mediates odorant detection (possibly) via modulation of intracellular cAMP concentration
Enzyme 23 Pathways
Enzyme 23 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • 80-100 105-125 139-159 173-193 226-246 381-401 633-653 664-684 708-728 754-774 775-795 833-853
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 4104226 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID O60266 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name ADCY3_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >3435 bp 
ATGCCGAGGAACCAGGGCTTCTCCGAGCCCGAATACTCGGCCGAGTACTCAGCCGAGTAC
TCCGTCAGCCTGCCCTCCGACCCTGACCGCGGGGTGGGCCGGACCCATGAAATCTCGGTC
CGGAACTCGGGCTCCTGCCTGTGCCTGCCTCGCTTCATGCGGCTGACTTTCGTGCCGGAG
TCCTTGGAGAACCTCTACCAGACCTACTTCAAAAGGCAGCGCCACGAGACCCTGCTGGTG
CTGGTGGTCTTTGCAGCCCTCTTTGACTGCTACGTGGTGGTCATGTGTGCTGTGGTCTTC
TCCAGCGACAAGCTGGCTCCCCTCGCCGTGGCTGGAATTGGACTGGTGTTGGACATCATC
CTCTTCGTGCTCTGCAAAAAGGGGCTGCTCCCGGACCGGGTCACCCGCAGAGTGCTGCCC
TACGTGCTGTGGCTGCTCATAACCGCCCAGATCTTCTCCTACCTGGGCCTGAACTTCGCG
CGTGCCCACGCGGCTAGTGACACGGTGGGCTGGCAGGTCTTCTTTGTCTTCTCCTTCTTC
ATCACGCTGCCCCTCAGCCTCAGCCCCATCGTGATCATCTCCGTGGTCTCCTGTGTGGTG
CACACGTTGGTCCTGGGGGTCACCGTGGCCCAGCAGCAGCAGGAGGAGCTCAAGGGGATG
CAGCTGCTGCGGGAGATCCTGGCCAACGTCTTCCTCTACCTGTGCGCCATCGCTGTGGGC
ATCATGTCCTACTACATGGCTGACCGCAAGCACCGCAAGGCCTTCCTGGAGGCCCGCCAG
TCGCTGGAGGTGAAGATGAACCTGGAAGAGCAGAGCCAGCAGCAGGAGAACCTCATGCTT
TCCATCCTGCCCAAGCACGTGGCTGACGAGATGCTGAAAGACATGAAGAAAGACGAGAGC
CAGAAGGACCAGCAGCAGTTCAACACCATGTACATGTACCGTCACGAGAACGTCAGCATC
CTCTTTGCCGACATCGTGGGCTTTACCCAGCTGTCTTCTGCCTGCAGTGCCCAGGAGCTT
GTGAAGCTGCTCAACGAGCTCTTTGCCCGCTTTGACAAGCTGGCAGCTAAATACCACCAG
CTGCGGATTAAGATCCTGGGCGACTGCTACTACTGCATCTGCGGCTTGCCTGACTACCGG
GAGGACCACGCCGTCTGCTCCATCCTCATGGGGCTGGCCATGGTGGAGGCCATCTCGTAT
GTGCGGGAGAAGACCAAGACTGGGGTGGACATGCGTGTGGGGGTGCACACGGGCACCGTG
CTGGGGGGCGTCCTGGGCCAGAAGCGCTGGCAGTACGACGTGTGGTCGACTGATGTCACT
GTAGCCAACAAGATGGAGGCCGGCGGCATCCCTGGGCGCGTGCACATCTCCCAGAGCACC
ATGGACTGCCTGAAAGGGGAGTTTGATGTGGAGCCAGGCGATGGGGGCAGCCGCTGTGAT
TACCTAGAAGAGAAGGGTATTGAAACCTACCTCATCATTGCCTCCAAGCCAGAGGTGAAG
AAAACAGCCACCCAGAATGGCCTCAATGGCTCGGCCCTGCCCAATGGAGCACCAGCTTCC
TCAAAGTCCAGCTCCCCTGCCCTCATTGAGACCAAGGAGCCCAACGGGAGTGCCCACAGC
AGTGGGTCCACGTCGGAGAAGCCCGAGGAGCAGGATGCCCAGGCCGACAACCCCTCATTC
CCCAACCCACGCCGGAGGCTGCGCCTGCAGGACCTGGCTGACCGAGTGGTGGATGCCTCT
GAAGATGAGCACGAGCTCAACCAGCTGCTCAACGAGGCCCTGCTTGAGCGAGAGTCCGCC
CAAGTAGTAAAGAAGAGAAACACCTTCCTCTTGTCCATGCGGTTCATGGACCCCGAGATG
GAAACCCGCTACTCGGTGGAGAAGGAGAAGCAGAGTGGGGCTGCCTTCAGCTGCTCCTGC
GTCGTCCTGCTCTGCACGGCCCTGGTCGAGATACTCATCGACCCCTGGCTAATGACAAAC
TATGTGACCTTCATGGTGGGGGAGATTCTGCTCCTCATCCTGACCATCTGCTCCCTGGCT
GCCATCTTTCCCCGGGCCTTTCCTAAGAAGCTTGTGGCCTTCTCAACTTGGATTGACCGG
ACCCGCTGGGCCAGGAACACCTGGGCCATGCTCGCCATCTTCATCCTGGTGATGGCAAAT
GTCGTGGACATGCTCAGCTGTCTCCAGTACTACACGGGACCCAGCAATGCAACGGCAGGG
ATGGAGACGGAGGGCAGCTGCCTGGAGAACCCCAAGTATTACAACTATGTGGCCGTGCTG
TCCCTCATCGCCACCATCATGCTGGTGCAGGTCAGCCACATGGTGAAGCTCACGCTCATG
CTGCTCGTCGCAGGCGCCGTGGCCACCATCAACCTCTATGCCTGGCGTCCCGTCTTTGAT
GAATACGACCACAAGCGTTTTCGGGAGCACGACTTACCTATGGTGGCCTTAGAGCAGATG
CAAGGATTCAACCCTGGGCTCAATGGCACTGACAGGCTGCCCCTGGTGCCTTCCAAGTAC
TCTATGACGGTGATGGTGTTCCTCATGATGCTCAGCTTCTACTACTTCTCCCGCCACGTA
GAAAAACTGGCACGGACACTTTTCTTGTGGAAGATTGAGGTCCACGACCAGAAGGAACGT
GTCTATGAGATGCGACGCTGGAACGAGGCCTTGGTCACCAACATGTTGCCTGAGCACGTG
GCACGCCATTTCCTGGGGTCCAAGAAGAGAGATGAGGAGCTGTATAGCCAGACGTATGAT
GAGATTGGAGTCATGTTTGCCTCCCTGCCCAACTTTGCTGACTTCTACACAGAGGAGAGC
ATCAACAATGGTGGTATTGAGTGTCTGCGTTTCCTCAATGAAATCATCTCAGATTTTGAC
TCTCTCCTGGACAATCCCAAGTTCCGGGTGATCACCAAGATCAAAACCATTGGCAGCACG
TATATGGCGGCTTCAGGAGTCACCCCCGATGTCAACACCAATGGCTTTGCCAGCTCCAAC
AAGGAAGACAAGTCCGAGAGAGAGCGCTGGCAGCACCTGGCTGACCTGGCCGACTTCGCG
CTGGCCATGAAGGATACGCTCACCAACATCAACAACCAGTCCTTCAATAACTTCATGCTG
CGCATAGGCATGAACAAAGGCGGGGTTCTGGCTGGGGTCATCGGAGCCCGGAAACCACAC
TACGACATCTGGGGCAATACAGTCAATGTAGCCAGCAGGATGGAGTCCACGGGGGTCATG
GGCAACATTCAGGTGGTAGAAGAAACCCAAGTCATCCTCCGAGAGTACGGCTTCCGCTTT
GTGAGGCGAGGCCCCATCTTTGTGAAGGGGAAGGGGGAGCTGCTGACCTTCTTCTTGAAG
GGGCGGGATAAGCTAGCCACCTTCCCCAATGGCCCCTCTGTCACACTGCCCCACCAGGTG
GTGGACAACTCCTGA
Enzyme 23 GenBank Gene ID AF033861 Link Image
Enzyme 23 GeneCard ID ADCY3 Link Image
Enzyme 23 GenAtlas ID ADCY3 Link Image
Enzyme 23 HGNC ID HGNC:234 Link Image
Enzyme 23 Chromosome Location 2
Enzyme 23 Locus 2p24-p22
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Yang B, He B, Abdel-Halim SM, Tibell A, Brendel MD, Bretzel RG, Efendic S, Hillert J: Molecular cloning of a full-length cDNA for human type 3 adenylyl cyclase and its expression in human islets. Biochem Biophys Res Commun. 1999 Jan 27;254(3):548-51. [PubMed Link Image]
  2. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
  3. Hellevuo K, Yoshimura M, Kao M, Hoffman PL, Cooper DM, Tabakoff B: A novel adenylyl cyclase sequence cloned from the human erythroleukemia cell line. Biochem Biophys Res Commun. 1993 Apr 15;192(1):311-8. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 5984
Enzyme 24 Name Adenylate cyclase type 1
Enzyme 24 Synonyms
  1. Adenylate cyclase type I
  2. ATP pyrophosphate-lyase 1
  3. Adenylyl cyclase 1
  4. Ca(2+/calmodulin- activated adenylyl cyclase
Enzyme 24 Gene Name ADCY1
Enzyme 24 Protein Sequence >Adenylate cyclase type 1 
MAGAPRGGGGGGGGAGEPGGAERAAGTSRRRGLRACDEEFACPELEALFRGYTLRLEQAA
TLKALAVLSLLAGALALAELLGAPGPAPGLAKGSHPVHCVLFLALLVVTNVRSLQVPQLQ
QVGQLALLFSLTFALLCCPFALGGPARGSAGAAGGPATAEQGVWQLLLVTFVSYALLPVR
SLLAIGFGLVVAASHLLVTATLVPAKRPRLWRTLGANALLFVGVNMYGVFVRILTERSQR
KAFLQARSCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDFLKPPERIFHKIYIQRHD
NVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGL
TQPKTDHAHCCVEMGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWS
NDVTLANVMEAAGLPGKVHITKTTLACLNGDYEVEPGYGHERNSFLKTHNIETFFIVPSH
RRKIFPGLILSDIKPAKRMKFKTVCYLLVQLMHCRKMFKAEIPFSNVMTCEDDDKRRALR
TASEKLRNRSSFSTNVVYTTPGTRVNRYISRLLEARQTELEMADLNFFTLKYKHVEREQK
YHQLQDEYFTSAVVLTLILAALFGLVYLLIFPQSVVVLLLLVFCICFLVACVLYLHITRV
QCFPGCLTIQIRTVLCIFIVVLIYSVAQGCVVGCLPWAWSSKPNSSLVVLSSGGQRTALP
TLPCESTHHALLCCLVGTLPLAIFFRVSSLPKMILLSGLTTSYILVLELSGYTRTGGGAV
SGRSYEPIVAILLFSCALALHARQVDIRLRLDYLWAAQAEEEREDMEKVKLDNRRILFNL
LPAHVAQHFLMSNPRNMDLYYQSYSQVGVMFASIPNFNDFYIELDGNNMGVECLRLLNEI
IADFDELMEKDFYKDIEKIKTIGSTYMAAVGLAPTSGTKAKKSISSHLSTLADFAIEMFD
VLDEINYQSYNDFVLRVGINVGPVVAGVIGARRPQYDIWGNTVNVASRMDSTGVQGRIQV
TEEVHRLLRRCPYHFVCRGKVSVKGKGEMLTYFLEGRTDGNGSQIRSLGLDRKMCPFGRA
GLQGRRPPVCPMPGVSVRAGLPPHSPGQYLPSAAAGKEA
Enzyme 24 Number of Residues 1119
Enzyme 24 Molecular Weight 123442
Enzyme 24 Theoretical pI 8.49
Enzyme 24 GO Classification
Function
  • catalytic activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cell communication
  • cellular metabolism
  • cellular process
  • cyclic nucleotide biosynthesis
  • intracellular signaling cascade
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide biosynthesis
  • nucleotide metabolism
  • physiological process
  • signal transduction
Component
—
Enzyme 24 General Function Signal transduction mechanisms
Enzyme 24 Specific Function This is a calmodulin-sensitive adenylyl cyclase. May be involved in regulatory processes in the central nervous system. It may play a role in memory acquisition and learning
Enzyme 24 Pathways
Enzyme 24 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • 64-84 88-108 125-145 158-178 183-203 214-234 611-631 635-655 674-694 725-745 753-773 775-794
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 41472630 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q08828 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name ADCY1_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >314 bp 
ATGAAGGAGGACTTCCTGAAGCCCCCTGAGAGGATTTTCCACAAGATTTACATCCAGAGG
CACGACAATGTGAGCATCCTGTTTGCTGACATCGTGGGTTTCACGGGCTTGGCATCCCAG
TGCACAGCCCAGGAGCTGGTGAAACTCCTCAATGAGCTCTTCGGCAAGTTCGATGAATTA
GCCACGGAGAACCACTGTCGCCGCATCAAGATTCTCGGGGACTGCTACTACTGCGTGTCG
GGCCTCACCCAGCCCAAGACTGACCATGCCCACTGCTGTGTGGAGATGGGACTCGACATG
ATTGATACCATCAC
Enzyme 24 GenBank Gene ID AC069008 Link Image
Enzyme 24 GeneCard ID ADCY1 Link Image
Enzyme 24 GenAtlas ID ADCY1 Link Image
Enzyme 24 HGNC ID HGNC:232 Link Image
Enzyme 24 Chromosome Location 7
Enzyme 24 Locus 7p13-p12
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  2. Villacres EC, Xia Z, Bookbinder LH, Edelhoff S, Disteche CM, Storm DR: Cloning, chromosomal mapping, and expression of human fetal brain type I adenylyl cyclase. Genomics. 1993 May;16(2):473-8. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 6011
Enzyme 25 Name DNA-directed RNA polymerase III subunit D
Enzyme 25 Synonyms
  1. DNA-directed RNA polymerase III 47 kDa polypeptide
  2. RNA polymerase C subunit 4
  3. RPC4
  4. RPC53
  5. Protein BN51
Enzyme 25 Gene Name POLR3D
Enzyme 25 Protein Sequence >DNA-directed RNA polymerase III subunit D 
MSEGNAAGEPSTPGGPRPLLTGARGLIGRRPAPPLTPGRLPSIRSRDLTLGGVKKKTFTP
NIISRKIKEEPKEEVTVKKEKRERDRDRQREGHGRGRGRPEVIQSHSIFEQGPAEMMKKK
GNWDKTVDVSDMGPSHIINIKKEKRETDEETKQILRMLEKDDFLDDPGLRNDTRNMPVQL
PLAHSGWLFKEENDEPDVKPWLAGPKEEDMEVDIPAVKVKEEPRDEEEEAKMKAPPKAAR
KTPGLPKDVSVAELLRELSLTKEEELLFLQLPDTLPGQPPTQDIKPIKTEVQGEDGQVVL
IKQEKDREAKLAENACTLADLTEGQVGKLLIRKSGRVQLLLGKVTLDVTMGTACSFLQEL
VSVGLGDSRTGEMTVLGHVKHKLVCSPDFESLLDHKHR
Enzyme 25 Number of Residues 398
Enzyme 25 Molecular Weight 44396
Enzyme 25 Theoretical pI 6.97
Enzyme 25 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • RNA metabolism
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • tRNA metabolism
  • transcription
Component
—
Enzyme 25 General Function Not Available
Enzyme 25 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Enzyme 25 Pathways
Enzyme 25 Reactions
  • nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 179513 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID P05423 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name RPO3D_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >1188 bp 
ATGTCGGAAGGAAACGCCGCCGGACGCCCAGCACGGCAGGGCCCGGACCTTCTCCTGACT
GGGGCCCGGGGGTCATCGGGCGGCGGCGGCCTCCCCTCACCCCCGGCCGTTCCCTCCATC
CGTTCCAGGGACCTAACCCTCGGGGGAGTCAAGAAGAAAACCTTCACCCCAAATATCATC
AGTCGGAAGATCAAGGAAGAGCCCAAGGAAGAAGTAACTGTCAAGAAGGAGAAGCGTGAA
AGGGACAGAGACCGACAACGAGAGGGGCATGGACGAGGGCGACGCCGTCCAGAAGTGATC
CAGTCTCACTCCATCTTTGAGCAGGGCCCAGCTGAAATGATGAAGAAAAAAGGGAACTGG
GATAAGACAGTGGATGTGTCAGACATGGGACCTTCTCATATCATCAACATCAAAAAAGAG
AAGAGAGAGACAGACGAAGAAACTAAACAGATCTTGCGTATGCTGGAGAAGGACGATTTC
CTCGATGACCCCGGCCTGAGGAACGACACTCGAAATATGCCTGTGCAGCTGCCGCTGGCT
CACTCAGGATGGCTTTTTAAGGAAGAAAATGACGAACCAGATGTTAAACCTTGGCTGGCT
GGCCCCAAGGAAGAGGACATGGAGGTGGACATACCTGCTGTGAAAGTGAAAGAGGAGCCA
CGAGATGAGGAGGAAGAGGCCAAGATGAAGGCTCCTCCCAAAGCAGCCAGGAAGACTCCA
GGCCTCCCGAAGGATGTATCTGTGGCAGAGCTGCTGAGGGAGCTGAGCCTCACCAAGGAA
GAGGAACTGCTGTTTCTGCAGCTGCCAGACACCCTCCCTGGCCAGCCACCCACCCAGGAC
ATCAAGCCTATCAAGACAGAGGTGCAGGGCGAGGACGGACAGGTGGTGCTCATCAAGCAG
GAGAAAGACCGAGAAGCCAAATTGGCAGAGAATGCTTGTACCCTGGCTGACCTGACAGAG
GGTCAGGTTGGCAAGCTACTCATCCGCAAGTCTGGAAGGGTGCAACTCCTCTTGGGCAAG
GTGACTCTGGACGTGACCATGGGAACTGCCTGCTCCTTCCTGCAGGAGCTGGTGTCCGTG
GGCCTTGGAGACAGTAGGACAGGGGAGATGACAGTCCTGGGACACGTGAAGCACAAACTT
GTATGTTCCCCTGATTTTGAATCCCTCTTGGATCACAAACACCGGTAA
Enzyme 25 GenBank Gene ID M17754 Link Image
Enzyme 25 GeneCard ID POLR3D Link Image
Enzyme 25 GenAtlas ID POLR3D Link Image
Enzyme 25 HGNC ID HGNC:1080 Link Image
Enzyme 25 Chromosome Location 8
Enzyme 25 Locus 8q21
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Ittmann M, Greco A, Basilico C: Isolation of the human gene that complements a temperature-sensitive cell cycle mutation in BHK cells. Mol Cell Biol. 1987 Oct;7(10):3386-93. [PubMed Link Image]
  2. Hu P, Wu S, Sun Y, Yuan CC, Kobayashi R, Myers MP, Hernandez N: Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits. Mol Cell Biol. 2002 Nov;22(22):8044-55. [PubMed Link Image]
  3. Chong SS, Hu P, Hernandez N: Reconstitution of transcription from the human U6 small nuclear RNA promoter with eight recombinant polypeptides and a partially purified RNA polymerase III complex. J Biol Chem. 2001 Jun 8;276(23):20727-34. Epub 2001 Feb 27. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 6012
Enzyme 26 Name DNA-directed RNA polymerase II 140 kDa polypeptide
Enzyme 26 Synonyms
  1. RNA polymerase II subunit 2
  2. RPB2
Enzyme 26 Gene Name POLR2B
Enzyme 26 Protein Sequence >DNA-directed RNA polymerase II 140 kDa polypeptide 
MYDADEDMQYDEDDDEITPDLWQEACWIVISSYFDEKGLVRQQLDSFDEFIQMSVQRIVE
DAPPIDLQAEAQHASGEVEEPPRYLLKFEQIYLSKPTHWERDGAPSPMMPNEARLRNLTY
SAPLYVDITKTVIKEGEEQLQTQHQKTFIGKIPIMLRSTYCLLNGLTDRDLCELNECPLD
PGGYFIINGSEKVLIAQEKMATNTVYVFAKKDSKYAYTGECRSCLENSSRPTSTIWVSML
ARGGQGAKKSAIGQRIVATLPYIKQEVPIIIVFRALGFVSDRDILEHIIYDFEDPEMMEM
VKPSLDEAFVIQEQNVALNFIGSRGAKPGVTKEKRIKYAKEVLQKEMLPHVGVSDFCETK
KAYFLGYMVHRLLLAALGRRELDDRDHYGNKRLDLAGPLLAFLFRGMFKNLLKEVRIYAQ
KFIDRGKDFNLELAIKTRIISDGLKYSLATGNWGDQKKAHQARAGVSQVLNRLTFASTLS
HLRRLNSPIGRDGKLAKPRQLHNTLWGMVCPAETPEGHAVGLVKNLALMAYISVGSQPSP
ILEFLEEWSMENLEEISPAAIADATKIFVNGCWVGIHKDPEQLMNTLRKLRRQMDIIVSE
VSMIRDIREREIRIYTDAGRICRPLLIVEKQKLLLKKRHIDQLKEREYNNYSWQDLVASG
VVEYIDTLEEETVMLAMTPDDLQEKEVAYCSTYTHCEIHPSMILGVCASIIPFPDHNQSP
RNTYQSAMGKQAMGVYITNFHVRMDTLAHVLYYPQKPLVTTRSMEYLRFRELPAGINSIV
AIASYTGYNQEDSVIMNRSAVDRGFFRSVFYRSYKEQESKKGFDQEEVFEKPTRETCQGM
RHAIYDKLDDDGLIAPGVRVSGDDVIIGKTVTLPENEDELESTNRRYTKRDCSTFLRTSE
TGIVDQVMVTLNQEGYKFCKIRVRSVRIPQIGDKFASRHGQKGTCGIQYRQEDMPFTCEG
ITPDIIINPHAIPSRMTIGHLIECLQGKVSANKGEIGDATPFNDAVNVQKISNLLSDYGY
HLRGNEVLYNGFTGRKITSQIFIGPTYYQRLKHMVDDKIHSRARGPIQILNRQPMEGRSR
DGGLRFGEMERDCQIAHGAAQFLRERLFEASDPYQVHVCNLCGIMAIANTRTHTYECRGC
RNKTQISLVRMPYACKLLFQELMSMSIAPRMMSV
Enzyme 26 Number of Residues 1174
Enzyme 26 Molecular Weight 133898
Enzyme 26 Theoretical pI 6.87
Enzyme 26 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • transcription
Component
—
Enzyme 26 General Function Transcription
Enzyme 26 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Enzyme 26 Pathways
Enzyme 26 Reactions
  • nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 36122 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P30876 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name RPB2_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >3525 bp 
ATGTACGACGCGGATGAGGATATGCAATATGATGAGGATGATGATGAAATCACCCCGGAT
TTGTGGCAAGAAGCATGCTGGATTGTAATCAGTTCCTATTTTGACGAGAAAGGCTTGGTT
AGACAACAGCTGGATTCTTTTGATGAGTTTATTCAGATGTCTGTTCAAAGAATTGTGGAA
GACGCTCCTCCTATAGACCTACAGGCTGAAGCTCAGCATGCTAGTGGAGAAGTTGAAGAA
CCGCCACGATATTTGCTGAAGTTTGAACAAATTTATCTTTCCAAGCCTACCCATTGGGAA
AGAGATGGTGCTCCTTCACCAATGATGCCCAATGAAGCTAGATTAAGGAATCTCACGTAT
TCTGCTCCGCTTTATGTTGATATAACAAAAACAGTCATTAAAGAAGGTGAAGAACAACTT
CAGACTCAGCATCAGAAAACTTTTATAGGAAAAATTCCAATTATGTTGCGGTCAACTTAC
TGCCTTTTGAATGGCTTGACAGATCGTGATCTTTGTGAGTTAAATGAATGCCCTTTGGAT
CCTGGTGGCTATTTCATTATTAATGGATCAGAAAAGGTTCTGATTGCCCAAGAGAAAATG
GCAACAAACACAGTTTATGTGTTTGCCAAAAAGGATTCTAAATATGCCTACACAGGAGAG
TGTAGATCATGTCTTGAGAATTCTTCCCGACCCACCAGTACTATATGGGTTAGCATGCTG
GCAAGAGGAGGACAGGGTGCCAAGAAGAGTGCTATTGGTCAGCGCATTGTGGCAACTCTA
CCATATATCAAGCAAGAAGTTCCCATCATTATTGTGTTCAGAGCATTAGGTTTTGTGTCC
GACAGAGATATTTTAGAACATATTATTTATGATTTTGAAGATCCAGAGATGATGGAAATG
GTTAAACCTTCTCTCGATGAAGCTTTTGTCATCCAAGAACAGAATGTTGCACTAAATTTC
ATTGGTTCACGAGGAGCAAAGCCTGGTGTTACTAAAGAGAAAAGAATTAAATATGCAAAG
GAAGTTTTACAAAAAGAAATGCTCCCTCATGTTGGTGTCAGTGATTTTTGTGAGACCAAA
AAAGCCTATTTCTTGGGATACATGGTTCATAGGTTACTTCTGGCAGCTTTGGGTAGAAGA
GAACTAGATGACAGAGATCACTATGGAAACAAGAGATTGGATCTTGCTGGGCCGCTGCTT
GCATTCTTATTTAGAGGTATGTTTAAGAATTTGCTTAAAGAAGTGCGGATCTATGCACAG
AAATTTATTGATCGAGGAAAGGATTTTAACTTGGAGTTGGCAATTAAAACACGGATCATA
TCTGATGGCCTAAAATACTCTTTAGCTACTGGAAACTGGGGTGATCAAAAGAAAGCTCAT
CAAGCCAGAGCTGGAGTATCTCAGGTGTTAAACCGCCTGACTTTTGCGTCTACTCTTTCT
CACCTGCGTCGTTTAAATTCTCCTATTGGTAGAGACGGCAAGCTAGCAAAACCAAGACAG
TTGCATAATACGTTGTGGGGAATGGTGTGTCCTGCCGAGACCCCAGAGGGCCATGCTGTA
GGACTTGTGAAGAATTTAGCCTTGATGGCGTATATTTCAGTTGGATCTCAACCATCTCCA
ATTCTGGAATTTTTAGAAGAATGGAGTATGGAAAATTTAGAAGAAATTTCTCCTGCAGCT
ATTGCTGATGCAACCAAGATTTTTGTTAATGGCTGCTGGGTTGGAATACATAAAGATCCC
GAACAACTTATGAACACCCTAAGGAAATTGAGACGTCAGATGGACATCATTGTGTCTGAA
GTTTCTATGATCAGAGATATTCGAGAGAGGGAGATTCGGATCTATACGGATGCAGGCCGT
ATTTGTAGACCACTTCTGATTGTGGAAAAACAAAAGCTACTTTTGAAGAAGAGGCATATT
GACCAATTGAAAGAGAGAGAATATAACAACTATAGTTGGCAGGATCTTGTGGCCAGTGGG
GTAGTGGAGTATATTGATACCCTGGAAGAAGAAACAGTGATGCTTGCAATGACTCCAGAT
GATTTACAGGAGAAAGAAGTAGCTTATTGTTCCACATATACACACTGTGAGATTCATCCC
TCAATGATCCTTGGTGTCTGTGCATCTATTATTCCCTTTCCTGATCATAACCAGTCCCCT
AGAAACACATACCAGTCTGCTATGGGTAAGCAGGCTATGGGAGTTTACATCACCAACTTC
CATGTTCGCATGGACACATTGGCCCATGTTCTCTATTATCCTCAAAAGCCACTTGTGACT
ACACGGTCTATGGAATATCTACGATTTAGAGAGCTGCCAGCAGGCATCAACTCAATTGTG
GCCATTGCATCATACACTGGATATAATCAGGAAGACTCTGTTATCATGAATCGTTCAGCT
GTAGACCGCGGCTTCTTCAGGTCTGTTTTCTATCGCTCATACAAAGAACAGGAGTCTAAA
AAAGGATTTGATCAAGAAGAAGTTTTTGAGAAGCCTACACGTGAAACATGCCAGGGCATG
AGGCATGCCATTTACGACAAGCTGGATGATGATGGTTTGATAGCTCCAGGGGTTCGTGTA
TCAGGAGATGATGTTATTATAGGCAAAACAGTCACCTTGCCTGAAAATGAAGATGAATTG
GAGAGCACCAATAGACGCTATACCAAGAGAGACTGTAGCACTTTTCTCAGAACTAGTGAG
ACGGGCATTGTGGATCAGGTTATGGTAACTCTCAATCAGGAAGGATATAAATTTTGTAAA
ATAAGGGTACGCTCTGTTAGGATTCCACAGATTGGAGACAAATTTGCTAGTCGACATGGT
CAAAAGGGTACTTGTGGTATTCAGTATAGACAAGAGGATATGCCTTTCACCTGTGAAGGT
ATCACCCCTGATATCATCATCAATCCCCATGCCATCCCCTCTCGTATGACTATTGGTCAC
TTAATTGAATGCCTTCAAGGGAAGGTATCGGCTAACAAGGGTGAAATTGGTGATGCCACT
CCATTTAATGATGCTGTTAACGTGCAGAAGATTTCTAATCTTTTATCTGATTATGGCTAT
CATCTCAGAGGAAATGAGGTCCTGTACAATGGGTTCACTGGTCGAAAAATCACATCACAA
ATATTTATTGGCCCCACTTATTACCAGCGTTTGAAGCATATGGTGGATGATAAGATTCAC
TCTCGTGCTAGGGGACCTATTCAGATCCTCAATAGACAGCCCATGGAGGGTAGATCTCGT
GATGGTGGCCTGCGTTTTGGAGAAATGGAACGAGATTGTCAGATTGCCCATGGAGCAGCC
CAGTTTTTAAGGGAAAGATTGTTTGAGGCATCAGATCCATATCAGGTTCATGTTTGCAAT
CTTTGTGGAATAATGGCGATTGCCAACACCAGGACCCATACATATGAATGCAGGGGCTGC
CGCAATAAAACCCAGATTTCTTTGGTGCGAATGCCTTACGCATGCAAACTATTGTTTCAG
GAACTTATGTCTATGAGTATTGCACCGCGAATGATGAGTGTTTAG
Enzyme 26 GenBank Gene ID X63563 Link Image
Enzyme 26 GeneCard ID POLR2B Link Image
Enzyme 26 GenAtlas ID POLR2B Link Image
Enzyme 26 HGNC ID HGNC:9188 Link Image
Enzyme 26 Chromosome Location 4
Enzyme 26 Locus 4q12
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Acker J, Wintzerith M, Vigneron M, Kedinger C: Primary structure of the second largest subunit of human RNA polymerase II (or B). J Mol Biol. 1992 Aug 20;226(4):1295-9. [PubMed Link Image]
  2. Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 6014
Enzyme 27 Name DNA-directed RNA polymerase II largest subunit
Enzyme 27 Synonyms
  1. RPB1
Enzyme 27 Gene Name POLR2A
Enzyme 27 Protein Sequence >DNA-directed RNA polymerase II largest subunit 
MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDP
RQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVD
SNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKG
HGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEP
RYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAA
HVIAEDVKLLQFHVATMVDNELPGLPRAMQKSGRPLKSLKQRLKGKEGRVRGNLMGKRVD
FSARTVITPDPNLSIDQVGVPRSIAANMTFAEIVTPFNIDRLQELVRRGNSQYPGAKYII
RDNGDRIDLRFHPKPSDLHLQTGYKVERHMCDGDIVIFNRQPTLHKMSMMGHRVRILPWS
TFRLNLSVTTPYNADFDGDEMNLHLPQSLETRAEIQELAMVPRMIVTPQSNRPVMGIVQD
TLTAVRKFTKRDVFLERGEVMNLLMFLSTWDGKVPQPAILKPRPLWTGKQIFSLIIPGHI
NCIRTHSTHPDDEDSGPYKHISPGDTKVVVENGELIMGILCKKSLGTSAGSLVHISYLEM
GHDITRLFYSNIQTVINNWLLIEGHTIGIGDSIADSKTYQDIQNTIKKAKQDVIEVIEKA
HNNELEPTPGNTLRQTFENQVNRILNDARDKTGSSAQKSLSEYNNFKSMVVSGAKGSKIN
ISQVIAVVGQQNVEGKRIPFGFKHRTLPHFIKDDYGPESRGFVENSYLAGLTPTEFFFHA
MGGREGLIDTAVKTAETGYIQRRLIKSMESVMVKYDATVRNSINQVVQLRYGEDGLAGES
VEFQNLATLKPSNKAFEKKFRFDYTNERALRRTLQEDLVKDVLSNAHIQNELEREFERMR
EDREVLRVIFPTGDSKVVLPCNLLRMIWNAQKIFHINPRLPSDLHPIKVVEGVKELSKKL
VIVNGDDPLSRQAQENATLLFNIHLRSTLCSRRMAEEFRLSGEAFDWLLGEIESKFNQAI
AHPGEMVGALAAQSLGEPATQMTLNTFHYAGVSAKNVTLGVPRLKELINISKKPKTPSLT
VFLLGQSARDAERAKDILCRLEHTTLRKVTANTAIYYDPNPQSTVVAEDQEWVNVYYEMP
DFDVARISPWLLRVELDRKHMTDRKLTMEQIAEKINAGFGDDLNCIFNDDNAEKLVLRIR
IMNSDENKMQEEEEVVDKMDDDVFLRCIESNMLTDMTLQGIEQISKVYMHLPQTDNKKKI
IITEDGEFKALQEWILETDGVSLMRVLSEKDVDPVRTTSNDIVEIFTVLGIEAVRKALER
ELYHVISFDGSYVNYRHLALLCDTMTCRGHLMAITRHGVNRQDTGPLMKCSFEETVDVLM
EAAAHGESDPMKGVSENIMLGQLAPAGTGCFDLLLDAEKCKYGMEIPTNIPGLGAAGPTG
MFFGSAPSPMGGISPAMTPWNQGATPAYGAWSPSVGSGMTPGAAGFSPSAASDASGFSPG
YSPAWSPTPGSPGSPGPSSPYIPSPGGAMSPSYSPTSPAYEPRSPGGYTPQSPSYSPTSP
SYSPTSPSYSPTSPNYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSP
TSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPS
YSPTSPNYSPTSPNYTPTSPSYSPTSPSYSPTSPNYTPTSPNYSPTSPSYSPTSPSYSPT
SPSYSPSSPRYTPQSPTYTPSSPSYSPSSPSYSPTSPKYTPTSPSYSPSSPEYTPTSPKY
SPTSPKYSPTSPKYSPTSPTYSPTTPKYSPTSPTYSPTSPVYTPTSPKYSPTSPTYSPTS
PKYSPTSPTYSPTSPKGSTYSPTSPGYSPTSPTYSLTSPAISPDDSDEEN
Enzyme 27 Number of Residues 1970
Enzyme 27 Molecular Weight 217208
Enzyme 27 Theoretical pI 7.38
Enzyme 27 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • transcription
  • transcription from RNA polymerase II promoter
  • transcription, DNA-dependent
Component
  • DNA-directed RNA polymerase II, core complex
  • RNA polymerase complex
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
  • protein complex
Enzyme 27 General Function Transcription
Enzyme 27 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Enzyme 27 Pathways
Enzyme 27 Reactions
  • nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 36124 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID P24928 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name RPB1_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >5913 bp 
ATGCACGGGGGTGGCCCCCCCTCGGGGGACAGCGCATGCCCGCTGCGCACCATCAAGAGA
GTCCAGTTCGGAGTCCTGAGTCCGGATGAACTGAAGCGAATGTCTGTGACGGAGGGTGGC
ATCAAATACCCAGAGACGACTGAGGGAGGCCGCCCCAAGCTTGGGGGGCTGATGGACCCG
AGGCAGGGGGTGATTGAGCGGACTGGCCGCTGCCAAACATGTGCAGGAAACATGACAGAG
TGTCCTGGCCACTTTGGCCACATTGAACTGGCCAAGCCTGTGTTTCACGTGGGCTTCCTG
GTGAAGACAATGAAAGTTTTGCGCTGTGTCTGCTTCTTCTGCTCCAAACTGCTTGTGGAC
TCTAACAACCCAAAGATCAAGGATATCCTGGCTAAGTCCAAGGGACAGCCCAAGAAGCGG
CTCACACATGTCTACGACCTTTGCAAGGGCAAAAACATATGCGAGGGTGGGGAGGAGATG
GACAACAAGTTCGGTGTGGAACAACCTGAGGGTGACGAGGATCTGACCAAAGAAAAGGGC
CATGGTGGCTGTGGGCGGTACCAGCCCAGGATCCGGCGTTCTGGCCTAGAGCTGTATGCG
GAATGGAAGCACGTTAATGAGGACTCTCAGGAGAAGAAGATCCTGCTGAGTCCAGAGCGA
GTGCATGAGATCTTCAAACGCATCTCAGATGAGGAGTGTTTTGTGCTGGGCATGGAGCCC
CGCTATGCACGGCCAGAGTGGATGATTGTCACAGTGCTGCCTGTGCCCCCGCTCTCCGTG
CGGCCTGCTGTTGTGATGCAGGGCTCTGCCCGTAACCAGGATGACCTGACTCACAAACTG
GCTGACATCGTGAAGATCAACAATCAGCTGCGGCGCAATGAGCAGAACGGCGCAGCGGCC
CATGTCATTGCAGAGGATGTGAAGCTCCTCCAGTTCCATGTGGCCACCATGGTGGACAAT
GAGCTGCCTGGCTTGCCCCGTGCCATGCAGAAGTCTGGGCGTCCCCTCAAGTCCCTGAAG
CAGCGGTTGAAGGGCAAGGAAGGCCGGGTGCGAGGGAACCTGATGGGCAAAAGAGTGGAC
TTCTCGGCCCGTACTGTCATCACCCCCGACCCCAACCTCTCCATTGACCAGGTTGGCGTG
CCCCGCTCCATTGCTGCCAACATGACCTTTGCGGAGATTGTCACCCCCTTCAACATTGAC
AGACTTCAAGAACTAGTGCGCAGGGGGAACAGTCAGTACCCAGGCGCCAAGTACATCATC
CGAGACAATGGTGATCGCATTGACTTGCGTTTCCACCCCAAGCCCAGTGACCTTCACCTG
CAGACCGGCTATAAGGTGGAACGGCACATGTGTGATGGGGACATTGTTATCTTCAACCGG
CAGCCAACTCTGCACAAAATGTCCATGATGGGGCATCGGGTCCGCATTCTCCCATGGTCT
ACCTTTCGCTTGAATCTTAGCGTGACAACTCCGTACAATGCAGACTTTGACGGGGATGAG
ATGAACTTGCACCTGCCACAGTCTCTGGAGACGCGAGCAGAGATCCAGGAGCTGGCCATG
GTTCCTCGCATGATTGTCACCCCCCAGAGCAATCGGCCTGTCATGGGTATTGTGCAGGAC
ACACTCACAGCAGTGCGCAAATTCACCAAGAGAGACGTCTTCCTGGAGCGGGGTGAAGTG
ATGAACCTCCTGATGTTCCTGTCGACGTGGGATGGGAAGGTCCCACAGCCGGCCATCCTA
AAGCCCCGGCCCCTGTGGACAGGCAAGCAAATCTTCTCCCTCATCATACCTGGTCACATC
AATTGTATCCGTACCCACAGCACCCATCCCGATGATGAAGACAGTGGCCCTTACAAGCAC
ATCTCTCCTGGGGACACCAAGGTGGTGGTGGAGAATGGGGAGCTGATCATGGGCATCCTG
TGTAAGAAGTCTCTGGGCACGTCAGCTGGCTCCCTGGTCCACATCTCCTACCTAGAGATG
GGTCATGACATCACTCGCCTCTTCTACTCCAACATTCAGACTGTCATTAACAACTGGCTC
CTCATCGAGGGTCATACTATTGGCATTGGGGACTCCATTGCTGATTCTAAGACTTACCAG
GACATTCAGAACACTATTAAGAAGGCCAAGCAGGACGTAATAGAGGTCATCGAGAAGGCA
CACAACAATGAGCTGGAGCCCACCCCAGGGAACACTCTGCGGCAGACGTTTGAGAATCAG
GTGAACCGCATTCTTAACGATGCCCGAGACAAGACTGGCTCCTCTGCTCAGAAATCCCTG
TCTGAATACAACAACTTCAAGTCTATGGTCGTGTCCGGAGCTAAAGGTTCCAAGATTAAC
ATCTCCCAGGTCATTGCTGTCGTTGGACAGCAGAACGTCGAGGGCAAGCGGATTCCATTT
GGCTTCAAGCACCGGACTCTGCCTCACTTCATCAAGGATGACTACGGGCCTGAGAGCCGT
GGCTTTGTGGAGAACTCCTACCTAGCCGGCCTCACACCCACTGAGTTCTTTTTCCACGCC
ATGGGGGGTCGTGAGGGGCTCATTGACACGGCTGTCAAGACTGCTGAGACTGGATACATC
CAGCGGCGGCTGATCAAGTCCATGGAGTCAGTGATGGTGAAGTACGACGCGACTGTGCGG
AACTCCATCAACCAGGTGGTGCAGCTGCGCTACGGCGAAGACGGCCTGGCAGGCGAGAGC
GTTGAGTTCCAGAACCTGGCTACGCTTAAGCCTTCCAACAAGGCTTTTGAGAAGAAGTTC
CGCTTTGATTATACCAATGAGAGGGCCCTGCGGCGCACTCTGCAGGAGGACCTGGTGAAG
GACGTGCTGAGCAACGCACACATCCAGAACGAGTTGGAGCGGGAATTTGAGCGGATGCGG
GAGGATCGGGAGGTGCTCAGGGTCATCTTCCCAACTGGAGACAGCAAGGTCGTCCTCCCC
TGTAACCTGCTGCGGATGATCTGGAATGCTCAGAAAATCTTCCACATCAACCCACGCCTT
CCCTCCGACCTGCACCCCATCAAAGTGGTGGAGGGAGTCAAGGAATTGAGCAAGAAGCTG
GTGATTGTGAATGGGGATGACCCACTAAGTCGACAGGCCCAGGAAAATGCCACGCTGCTC
TTCAACATCCACCTGCGGTCCACGTTGTGTTCCCGCCGCATGGCAGAGGAGTTTCGGCTC
AGTGGGGAGGCCTTCGACTGGCTGCTTGGGGAGATTGAGTCCAAGTTCAACCAAGCCATT
GCGCATCCCGGGGAAATGGTGGGGGCTCTGGCTGCGCAGTCCCTTGGAGAACCTGCCACC
CAGATGACCTTGAATACCTTCCACTATGCTGGTGTGTCTGCCAAGAATGTGACGCTGGGT
GTGCCCCGACTTAAGGAGCTCATCAACATTTCCAAGAAGCCAAAGACTCCTTCGCTTACT
GTCTTCCTGTTGGGCCAGTCCGCTCGAGATGCTGAGAGAGCCAAGGATATTCTGTGCCGT
CTGGAGCATACAACGTTGAGGAAGGTGACTGCCAACACAGCCATCTACTATGACCCCAAC
CCCCAGAGCACGGTGGTGGCAGAGGATCAGGAATGGGTGAATGTCTACTATGAAATGCCT
GACTTTGATGTGGCCCGAATCTCCCCCTGGCTGTTGCGGGTGGAGCTGGATCGGAAGCAC
ATGACTGACCGGAAGCTCACCATGGAGCAGATTGCTGAAAAGATCAATGCTGGTTTTGGT
GACGACTTGAACTGCATCTTTAATGATGACAATGCAGAGAAGCTGGTGCTCCGTATTCGC
ATCATGAACAGCGATGAGAACAAGATGCAAGAGGAGGAAGAGGTGGTGGACAAGATGGAT
GATGATGTCTTCCTGCGCTGCATCGAGTCCAACATGCTGACAGATATGACCCTGCAGGGC
ATCGAGCAGATCAGCAAGGTGTACATGCACTTGCCACAGACAGACAACAAGAAGAAGATC
ATCATCACGGAGGATGGGGAATTCAAGGCCCTGCAGGAGTGGATCCTGGAGACGGACGGC
GTGAGCTTGATGCGGGTGCTGAGTGAGAAGGACGTGGACCCCGTACGCACCACGTCCAAT
GACATTGTGGAGATCTTCACGGTGCTGGGCATTGAAGCCGTGCGGAAGGCCCTGGAGCGG
GAGCTGTACCACGTCATCTCCTTTGATGGCTCCTATGTCAATTACCGACACTTGGCTCTC
TTGTGTGATACCATGACCTGTCGTGGCCACTTGATGGCCATCACCCGACACGGAGTCAAC
CGCCAGGACACAGGACCACTCATGAAGTGTTCCTTTGAGGAAACGGTGGACGTGCTTATG
GAAGCAGCCGCACACGGTGAGAGTGACCCCATGAAGGGGGTCTCTGAGAATATCATGCTG
GGCCAGCTGGCTCCGGCCGGCACTGGCTGCTTTGACCTCCTGCTTGATGCAGAGAAGTGC
AAGTATGGCATGGAGATCCCCACCAATATCCCCGGCCTGGGGGCTGCTGGACCCACCGGC
ATGTTCTTTGGTTCAGCACCCAGTCCCATGGGTGGAATCTCTCCTGCCATGACACCTTGG
AACCAGGGTGCAACCCCTGCCTATGGCGCCTGGTCCCCCAGTGTTGGGAGTGGAATGACC
CCAGGGGCAGCCGGTTTCTCTCCCAGTGCTGCGTCAGATGCCAGCGGCTTCAGCCCAGGT
TACTCCCCTGCCTGGTCTCCCACACCGGGCTCCCCGGGGTCCCCAGGTCCCTCAAGCCCC
TACATCCCTTCACCAGGTGGCGCCATGTCTCCCAGCTACTCGCCAACGTCACCTGCCTAC
GAGCCCCGCTCTCCTGGGGGCTACACACCCCAGAGTCCCTCTTATTCCCCCACTTCACCC
TCCTACTCCCCTACCTCTCCATCCTATTCTCCAACCAGTCCCAACTATAGTCCCACATCA
CCCAGCTATTCGCCAACGTCACCCAGCTACTCACCGACCTCTCCCAGCTACTCACCCACC
TCTCCCAGCTACTCGCCCACCTCTCCCAGCTATTCGCCCACCTCTCCCAGCTACTCACCC
ACTTCCCCTAGCTATTCGCCCACTTCCCCTAGCTACTCGCCAACGTCTCCCAGCTACTCG
CCGACATCTCCCAGCTACTCGCCAACTTCACCCAGCTATTCTCCCACTTCTCCCAGCTAC
TCACCTACCTCTCCAAGCTATTCACCCACCTCCCCCAGCTACTCACCCACTTCCCCAAGT
TACTCACCCACCAGCCCGAACTATTCTCCAACCAGTCCCAATTACACCCCAACATCACCC
AGCTACAGCCCGACATCACCCAGCTATTCCCCTACTAGTCCCAACTACACACCTACCAGC
CCTAACTACAGCCCAACCTCTCCAAGCTACTCTCCAACATCACCCAGCTATTCCCCGACC
TCACCAAGTTACTCCCCTTCCAGCCCACGATACACACCACAGTCTCCAACCTATACCCCA
AGCTCACCCAGCTACAGCCCCAGTTCGCCCAGCTACAGCCCAACCTCACCCAAGTACACC
CCAACCAGTCCTTCTTATAGTCCCAGCTCCCCAGAGTATACCCCAACCTCTCCCAAGTAC
TCACCTACCAGTCCCAAATATTCACCCACCTCTCCCAAGTACTCGCCTACCAGTCCCACC
TATTCACCCACCACCCCAAAATACTCCCCAACATCTCCTACTTATTCCCCAACCTCTCCA
GTCTACACCCCAACCTCTCCCAAGTACTCACCTACTAGCCCCACTTACTCGCCCACTTCC
CCCAAGTACTCGCCCACCAGCCCCACCTACTCGCCCACCTCCCCCAAAGGCTCAACCTAC
TCTCCCACTTCCCCTGGTTACTCGCCCACCAGCCCCACCTACAGTCTCACAAGCCCGGCT
ATCAGCCCGGATGACAGTGACGAGGAGAACTGA
Enzyme 27 GenBank Gene ID X63564 Link Image
Enzyme 27 GeneCard ID POLR2A Link Image
Enzyme 27 GenAtlas ID POLR2A Link Image
Enzyme 27 HGNC ID HGNC:9187 Link Image
Enzyme 27 Chromosome Location 17
Enzyme 27 Locus 17p13.1
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Wintzerith M, Acker J, Vicaire S, Vigneron M, Kedinger C: Complete sequence of the human RNA polymerase II largest subunit. Nucleic Acids Res. 1992 Feb 25;20(4):910. [PubMed Link Image]
  2. Mita K, Tsuji H, Morimyo M, Takahashi E, Nenoi M, Ichimura S, Yamauchi M, Hongo E, Hayashi A: The human gene encoding the largest subunit of RNA polymerase II. Gene. 1995 Jul 4;159(2):285-6. [PubMed Link Image]
  3. Nayler O, Stratling W, Bourquin JP, Stagljar I, Lindemann L, Jasper H, Hartmann AM, Fackelmayer FO, Ullrich A, Stamm S: SAF-B protein couples transcription and pre-mRNA splicing to SAR/MAR elements. Nucleic Acids Res. 1998 Aug 1;26(15):3542-9. [PubMed Link Image]
  4. Allen M, Friedler A, Schon O, Bycroft M: The structure of an FF domain from human HYPA/FBP11. J Mol Biol. 2002 Oct 25;323(3):411-6. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 6017
Enzyme 28 Name DNA-directed RNA polymerase, mitochondrial precursor
Enzyme 28 Synonyms
  1. MtRPOL
Enzyme 28 Gene Name POLRMT
Enzyme 28 Protein Sequence >DNA-directed RNA polymerase, mitochondrial precursor 
MSALCWGRGAAGLKRALRPCGRPGLPGKEGTAGGVCGPRRSSSASPQEQDQDRRKDWGHV
ELLEVLQARVRQLQAESVSEVVVNRVDVARLPECGSGDGSLQPPRKVQMGAKDATPVPCG
RWAKILEKDKRTQQMRMQRLKAKLQMPFQSGEFKALTRRLQVEPRLLSKQMAGCLEDCTR
QAPESPWEEQLARLLQEAPGKLSLDVEQAPSGQHSQAQLSGQQQRLLAFFKCCLLTDQLP
LAHHLLVVHHGQRQKRKLLTLDMYNAVMLGWARQGAFKELVYVLFMVKDAGLTPDLLSYA
AALQCMGRQDQDAGTIERCLEQMSQEGLKLQALFTAVLLSEEDRATVLKAVHKVKPTFSL
PPQLPPPVNTSKLLRDVYAKDGRVSYPKLHLPLKTLQCLFEKQLHMELASRVCVVSVEKP
TLPSKEVKHARKTLKTLRDQWEKALCRALRETKNRLEREVYEGRFSLYPFLCLLDEREVV
RMLLQVLQALPAQGESFTTLARELSARTFSRHVVQRQRVSGQVQALQNHYRKYLCLLASD
AEVPEPCLPRQYWEELGAPEALREQPWPLPVQMELGKLLAEMLVQATQMPCSLDKPHRSS
RLVPVLYHVYSFRNVQQIGILKPHPAYVQLLEKAAEPTLTFEAVDVPMLCPPLPWTSPHS
GAFLLSPTKLMRTVEGATQHQELLETCPPTALHGALDALTQLGNCAWRVNGRVLDLVLQL
FQAKGCPQLGVPAPPSEAPQPPEAHLPHSAAPARKAELRRELAHCQKVAREMHSLRAEAL
YRLSLAQHLRDRVFWLPHNMDFRGRTYPCPPHFNHLGSDVARALLEFAQGRPLGPHGLDW
LKIHLVNLTGLKKREPLRKRLAFAEEVMDDILDSADQPLTGRKWWMGAEEPWQTLACCME
VANAVRASDPAAYVSHLPVHQDGSCNGLQHYAALGRDSVGAASVNLEPSDVPQDVYSGVA
AQVEVFRRQDAQRGMRVAQVLEGFITRKVVKQTVMTVVYGVTRYGGRLQIEKRLRELSDF
PQEFVWEASHYLVRQVFKSLQEMFSGTRAIQHWLTESARLISHMGSVVEWVTPLGVPVIQ
PYRLDSKVKQIGGGIQSITYTHNGDISRKPNTRKQKNGFPPNFIHSLDSSHMMLTALHCY
RKGLTFVSVHDCYWTHAADVSVMNQVCREQFVRLHSEPILQDLSRFLVKRFCSEPQKILE
ASQLKETLQAVPKPGAFDLEQVKRSTYFFS
Enzyme 28 Number of Residues 1230
Enzyme 28 Molecular Weight 138622
Enzyme 28 Theoretical pI 9.25
Enzyme 28 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • transcription
Component
—
Enzyme 28 General Function Not Available
Enzyme 28 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Enzyme 28 Pathways
Enzyme 28 Reactions
  • nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 2114396 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID O00411 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name RPOM_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >3693 bp 
ATGTCGGCACTTTGCTGGGGCCGCGGAGCGGCGGGGCTCAAACGAGCCCTACGGCCTTGC
GGCCGCCCGGGACTCCCCGGCAAAGAAGGGACCGCCGGTGGCGTCTGCGGCCCCAGGAGG
AGCTCGTCCGCCAGCCCCCAGGAGCAAGACCAAGACCGCAGGAAGGACTGGGGCCACGTG
GAGCTGCTGGAGGTGCTCCAGGCGCGGGTGCGGCAGCTGCAGGCTGAGAGCGTGTCGGAG
GTGGTGGTGAACAGGGTGGATGTGGCGCGGCTCCCAGAATGTGGCAGTGGAGATGGTAGC
CTCCAGCCACCCAGGAAGGTCCAGATGGGGGCCAAGGATGCCACCCCGGTGCCCTGTGGC
CGCTGGGCAAAGATACTGGAGAAGGATAAGCGGACCCAGCAGATGCGTATGCAGCGGTTG
AAGGCGAAGCTGCAGATGCCATTCCAGAGCGGGGAGTTCAAGGCGCTGACCAGGCGCCTG
CAGGTGGAGCCCCGGCTCCTGAGCAAGCAGATGGCCGGGTGCCTGGAGGACTGCACGCGC
CAGGCCCCCGAGAGCCCCTGGGAGGAGCAGCTGGCCCGGCTGCTGCAGGAGGCCCCTGGG
AAGCTGAGCCTCGATGTGGAGCAGGCCCCGTCGGGGCAGCACTCGCAGGCCCAGCTCTCA
GGTCAGCAGCAGAGGCTCCTGGCCTTCTTCAAGTGCTGCCTGCTCACTGACCAGCTGCCC
CTCGCCCACCACCTGCTGGTCGTCCACCACGGCCAGCGGCAGAAGCGGAAGCTGCTCACG
CTGGACATGTACAACGCCGTGATGCTTGGCTGGGCGCGGCAGGGTGCTTTCAAGGAGCTG
GTATATGTGTTATTCATGGTGAAGGATGCCGGCTTGACCCCGGACCTGCTGTCCTATGCG
GCTGCCCTCCAGTGCATGGGGAGGCAGGACCAGGACGCCGGGACCATCGAAAGGTGTCTG
GAACAGATGAGCCAGGAGGGGCTGAAGCTGCAGGCACTCTTCACCGCCGTTCTGCTGTCT
GAGGAGGATCGGGCCACTGTTCTGAAGGCCGTGCACAAGGTGAAGCCCACCTTCAGCCTC
CCGCCGCAGCTGCCGCCCCCGGTCAACACCTCCAAGCTGCTCAGGGACGTGTATGCCAAG
GATGGGCGTGTGTCCTACCCGAAGCTGCACCTGCCCTTGAAGACCCTGCAGTGCTTCTTT
GAGAAGCAGCTCCACATGGAGCTGGCCAGCAGGGTGTGCGTGGTGTCCGTGGAGAAGCCC
ACGTTGCCAAGCAAGGAGGTCAAGCACGCGCGGAAGACCCTGAAGACCCTGCGGGACCAA
TGGGAGAAAGCACTGTGCCGGGCGCTGCGGGAGACCAAGAACCGCCTAGAGCGCGAGGTG
TACGAGGGCCGGTTCTCACTTTACCCCTTCCTGTGCCTGCTGGACGAGCGCGAGGTGGTG
CGGATGCTCCTGCAGGTCCTGCAGGCGCTGCCCGCCCAAGGTGAGTCCTTCACCACCCTG
GCCCGGGAGCTGAGTGCGCGCACTTTCAGCCGGCACGTGGTGCAGAGGCAGCGGGTCAGT
GGCCAGGTGCAGGCGCTGCAGAACCACTACAGGAAGTACCTCTGCTTGCTGGCCTCCGAC
GCCGAGGTGCCCGAGCCCTGCCTGCCGCGGCAGTACTGGGAGGAGCTGGGGGCGCCCGAG
GCCCTGCGGGAGCAGCCCTGGCCCCTGCCAGTGCAGATGGAGCTGGGCAAGCTGCTGGCG
GAGATGCTGGTGCAGGCTACGCAGATGCCATGCAGCCTGGACAAGCCGCATCGTTCCTCT
CGGCTTGTCCCCGTGCTCTACCACGTGTATTCCTTCCGCAACGTCCAGCAAATCGGCATC
CTGAAGCCGCACCCGGCCTACGTGCAGCTGCTGGAGAAGGCCGCGGAACCCACGCTGACC
TTCGAGGCGGTGGATGTACCCATGCTTTGCCCCCCGCTGCCCTGGACATCGCCGCACTCT
GGTGCTTTCCTGCTCAGCCCCACCAAGCTGATGCGCACGGTGGAAGGCGCCACGCAACAC
CAGGAGCTGCTGGAAACCTGCCCACCCACCGCGCTGCATGGCGCACTGGACGCCCTCACC
CAACTGGGCAACTGCGCCTGGCGCGTCAACGGGCGCGTGCTGGACCTGGTGCTGCAGCTC
TTCCAGGCCAAGGGCTGCCCCCAGCTAGGCGTGCCGGCCCCGCCCTCCGAGGCGCCCCAG
CCGCCCGAGGCCCACCTGCCGCACAGCGCCGCGCCCGCCCGCAAGGCCGAGCTGCGCCGT
GAGCTGGCGCACTGCCAGAAGGTGGCCCGGGAGATGCACAGCCTGCGGGCGGAGGCGCTG
TACCGCCTCTCGCTGGCGCAGCACCTGCGGGACCGCGTCTTCTGGCTGCCGCACAACATG
GACTTCCGCGGCCGCACCTACCCCTGCCCGCCGCACTTCAACCACCTGGGCAGCGACGTG
GCGCGGGCCCTGCTGGAGTTCGCCCAGGGCCGCCCGCTCGGCCCGCACGGCCTGGATTGG
CTCAAGATCCACCTGGTCAATCTCACGGGGTTGAAGAAGCGGGAGCCGCTGCGGAAGCGC
CTGGCCTTTGCGGAGGAGGTGATGGATGACATCCTGGACTCCGCGGACCAACCCTTGACG
GGCCGAAAGTGGTGGATGGGCGCGGAGGAACCCTGGCAGACGCTGGCCTGCTGTATGGAG
GTGGCGAACGCTGTGCGCGCCTCCGACCCTGCCGCCTATGTCTCCCACCTCCCCGTCCAT
CAGGACGGCTCTTGCAACGGCCTGCAGCATTATGCTGCTCTGGGCCGCGACAGCGTGGGC
GCCGCCTCCGTCAACCTGGAGCCCTCGGATGTGCCGCAGGACGTGTACAGCGGCGTGGCC
GCGCAGGTGGAGGTGTTCCGTAGGCAGGACGCCCAGCGGGGCATGCGGGTGGCACAGGTG
CTGGAAAGTTTCATCACCCGCAAGGTGGTGAAGCAGACGGTGATGACGGTGGTGTACGGG
GTCACGCGCTATGGCGGGCGCCTGCAGATTGAGAAGCGCCTCCGGGAGCTGAGCGACTTT
CCCCAGGAGTTCGTGTGGGAGGCCTCTCACTATCTCGTACGCCAGGTCTTCAAGAGTCTA
CAGGAGATGTTCTCGGGGACCCGGGCCATCCAGCACTGGCTGACCGAGAGTGCCCGCCTC
ATCTCCCACATGGGCTCTGTGGTGGAGTGGGTCACACCCCTGGGCGTCCCCGTCATCCAG
CCGTATCGCCTGGACTCCAAGGTCAAGCAAATAGGAGGTGGAATTCAGAGCATCACCTAC
ACCCACAACGGAGACATCAGCCGAAAGCCCAACACACGTAAGCAGAAGAACGGCTTCCCG
CCCAACTTCATCCACTCGCTGGACTCCTCCCACATGATGCTCACCGCCCTGCACTGCTAC
AGGAAGGGCCTGACCTTCGTCTCTGTGCACGACTGTTACTGGACTCACGCAGCTGATGTC
TCCGTCATGAACCAGGTGTGCCGGGAGCAGTTTGTCCGCTTGCACAGCGAGCCCATCCTG
CAGGACCTGTCCAGATTCCTGGTCAAGCGGTTCTGCTCTGAGCCCCAGAAGATCTTGGAG
GCCAGCCAGCTGAAGGAGACACTGCAGGCGGTGCCCAAGCCAGGGGCCTTCGACCTGGAG
CAGGTGAAGCGTTCCACCTACTTCTTCAGCTGA
Enzyme 28 GenBank Gene ID U75370 Link Image
Enzyme 28 GeneCard ID POLRMT Link Image
Enzyme 28 GenAtlas ID POLRMT Link Image
Enzyme 28 HGNC ID HGNC:9200 Link Image
Enzyme 28 Chromosome Location 19
Enzyme 28 Locus 19p13.3
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Tiranti V, Savoia A, Forti F, D'Apolito MF, Centra M, Rocchi M, Zeviani M: Identification of the gene encoding the human mitochondrial RNA polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence Tags database. Hum Mol Genet. 1997 Apr;6(4):615-25. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 6018
Enzyme 29 Name DNA-directed RNA polymerase I 135 kDa polypeptide
Enzyme 29 Synonyms
  1. RNA polymerase I subunit 2
  2. RPA135
Enzyme 29 Gene Name POLR1B
Enzyme 29 Protein Sequence >DNA-directed RNA polymerase I 135 kDa polypeptide 
MDPGSRWRNLPSGPSLKHLTDPSYGIPREQQKAALQELTRAHVESFNYAVHEGLGLAVQA
IPPFEFAFKDERISFTILDAVISPPTVPKGTICKEANVYPAECRGRRSTYRGKLTADINW
AVNGISKGIIKQFLGYVPIMVKSKLCNLRNLPPQALIEHHEEAEEMGGYFIINGIEKVIR
MLIMPRRNFPIAMIRPKWKTRGPGYTQYGVSMHCVREEHSAVNMNLHYLENGTVMLNFIY
RKELFFLPLGFALKALVSFSDYQIFQELIKGKEDDSFLRNSVSQMLRIVMEEGCSTQKQV
LNYLGECFRVKLNVPDWYPNEQAAEFLFNQCICIHLKSNTEKFYMLCLMTRKLFALAKGE
CMEDNPDSLVNQEVLTPGQLFLMFLKEKLEGWLVSIKIAFDKKAQKTSVSMNTDNLMRIF
TMGIDLTKPFEYLFATGNLRSKTGLGLLQDSGLCVVADKLNFIRYLSHFRCVHRGADFAK
MRTTTVRRLLPESWGFLCPVHTPDGEPCGLMNHLTAVCEVVTQFVYTASIPALLCNLGVT
PIDGAPHRSYSECYPVLLDGVMVGWVDKDLAPGIADSLRHFKVLREKRIPPWMEVVLIPM
TGKPSLYPGLFLFTTPCRLVRPVQNLALGKEELIGTMEQIFMNVAIFEDEVFAGVTTHQE
LFPHSLLSVIANFIPFSDHNQSPRNMYQCQMGKQTMGFPLLTYQDRSDNKLYRLQTPQSP
LVRPSMYDYYDMDNYPIGTNAIVAVISYTGYDMEDAMIVNKASWERGFAHGSVYKSEFID
LSEKIKQGDSSLVFGIKPGDPRVLQKLDDDGLPFIGAKLQYGDPYYSYLNLNTGESFVMY
YKSKENCVVDNIKVCSNDTGSGKFKCVCITMRVPRNPTIGDKFASRHGQKGILSRLWPAE
DMPFTESGMVPDILFNPHGFPSRMTIGMLIESMAGKSAALHGLCHDATPFIFSEENSALE
YFGEMLKAAGYNFYGTERLYSGISGLELEADIFIGVVYYQRLRHMVSDKFQVRTTGARDR
VTNQPIGGRNVQGGIRFGEMERDALLAHGTSFLLHDRLFNCSDRSVAHVCVKCGSLLSPL
LEKPPPSWSAMRNRKYNCTLCSRSDTIDTVSVPYVFRYFVAELAAMNIKVKLDVV
Enzyme 29 Number of Residues 1135
Enzyme 29 Molecular Weight 128231
Enzyme 29 Theoretical pI 7.88
Enzyme 29 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • transcription
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 29 General Function Transcription
Enzyme 29 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. RNA polymerase I is essentially used to transcribe ribosomal DNA units
Enzyme 29 Pathways
Enzyme 29 Reactions
  • nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 10433976 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID Q9H9Y6 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name RPA2_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >3240 bp 
ATGGATCCTGGCAGCCGGTGGCGGAACCTGCCCAGCGGGCCTAGCCTAAAGCACTTGACT
GACCCCTCTTATGGAATCCCGCGGGAACAGCAAAAGGCAGCGTTGCAGGAGCTGACGCGG
GCGCACGTGGAGTCCTTCAACTACGCTGTGCACGAGGGTCTCGGCCTCGCGGTGCAGGCT
GATATCAACTGGGCAGTGAATGGAATCTCAAAAGGAATCATTAAGCAGTTTCTTGGCTAC
GTTCCCATCATGGTGAAATCCAAGCTTTGCAACTTACGTAACCTTCCCCCACAAGCCCTC
ATTGAGCACCATGAGGAGGCAGAGGAAATGGGGGGCTATTTTATAATCAATGGCATTGAA
AAAGTCATCCGAATGTTGATTATGCCTCGGAGAAATTTTCCCATTGCAATGATAAGACCA
AAATGGAAAACCAGAGGGCCTGGTTATACTCAGTATGGAGTTTCAATGCACTGTGTGAGG
GAAGAACATTCCGCTGTCAATATGAACCTCCACTACTTGGAAAATGGCACAGTTATGTTG
AACTTTATTTACCGAAAAGAACTGTTCTTTCGTCCTTTGGGATTTGCACTTAAGGCACTT
GTCAGCTTTTCTGATTATCAGATCTTTCAGGAGCTCATCAAAGGAAAAGAGGATGATTCT
TTCCTTAGGAACTCTGTTTCTCAGATGTTAAGGATTGTAATGGAAGAGGGTTGTTTGACA
CAAAAACAGGTCCTTAACTACCTAGGTGAATGCTTCAGAGTAAAACTCAATGTTCCTGAC
TGGTACCCAAATGAGCAAGCTGCGGAGTTCCTGTTTAACCAGTGCATCTGTATCCACTTG
AAATCCAATACTGAAAAGTTTTATATGCTTTGTCTCATGACGCGAAAGCTCTTTGCTTTA
GCCAAAGGAGAGTGCATGGAGGACAATCCTGATAGTTTGGTGAACCAGGAAGTCCTCACA
CCGGGTCAGCTCTTCCTTATGTTCCTGAAGGAAAAACTGGAAGGTTGGTTAGTGTCTATT
AAAATAGCTTTTGATAAGAAGGCTCAGAAGACCAGTGTTTCCATGAACACTGACAATTTG
ATGAGGATTTTTACAATGGGCATAGACCTTACAAAACCATTTGAATACCTTTTTGCTACT
GGGAATCTGCGTTCTAAAACAGGTCTTGGCCTCCTACAAGATTCTGGACTTTGTGTTGTG
GCTGACAAGCTGAACTTCATACGCTACCTCTCCCATTTCCGCTGCGTGCACAGAGGGGCT
GATTTTGCCAAGATGAGGACCACCACAGTACGCAGGCTGCTGCCAGAGTCCTGGGGCTTC
CTTTGTCCCGTGCATACCCCAGACGGGGAGCCCTGTGGCCTGATGAACCACCTAACTGCC
GTATGTGAGGTTGTCACACAGTTTGTGTATACGGCATCTATTCCAGCTTTACTGTGCAAC
TTGGGGGTCACTCCCATTGATGGAGCTCCCCACCGATCATACAGTGAGTGCTACCCTGTC
CTGCTGGACGGTGTCATGGTTGGCTGGGTGGATAAGGATCTTGCTCCAGGCATCGCAGAT
TCTCTTCGTCATTTTAAGGTGTTGAGAGAGAAAAGAATTCCTCCCTGGATGGAAGTGGTC
CTTATACCCATGACAGGAAAACCAAGTCTGTACCCAGGATTGTTCCTTTTTACCACTCCT
TGTAGACTGGTACGGCCTGTGCAGAACTTAGCATTGGGCAAAGAAGAGCTAATTGGAACT
ATGGAACAGATCTTCATGAATGTCGCTATCTTTGAGGATGAAGTTTTTGCTGGAGTTACC
ACACACCAGGAACTCTTTCCACACAGCCTGCTGAGTGTGATTGCCAACTTCATCCCTTTC
TCTGATCACAACCAGAGTCCACGGAACATGTACCAATGCCAGATGGGTAAGCAAACTATG
GGCTTTCCACTTCTCACTTATCAAGACCGATCGGATAACAAACTGTATCGTCTTCAGACT
CCTCAGAGTCCCTTGGTGAGACCCTCCATGTATGATTATTATGACATGGATAACTATCCA
ATTGGGACCAATGCCATCGTTGCTGTGATTTCTTACACTGGCTATGATATGGAAGATGCC
ATGATTGTGAATAAGGCCTCTTGGGAACGAGGCTTTGCCCATGGAAGTGTCTACAAGTCT
GAGTTCATAGACCTCTCTGAAAAAATTAAACAAGGAGATAGTAGCCTGGTGTTTGGCATC
AAACCTGGTGACCCACGCGTTCTGCAGAAGTTAGATGACGATGGATTGCCGTTTATAGGA
GCAAAACTGCAGTACGGAGATCCGTATTACAGCTACCTCAACCTCAACACCGGGGAAAGT
TTTGTGATGTACTATAAGAGTAAAGAAAATTGTGTTGTGGATAACATCAAAGTGTGCAGT
AATGACACTGGGAGTGGAAAATTCAAGTGTGTTCGCATCACTATGAGAGTGCCTCGGAAC
CCAACTATCGGAGATAAATTTGCCAGTCGCCATGGGCGGAAGGGCATTTTAAGCAGATTG
TGGCCGGCTGAGGACATGCCTTTTACTGAGAGTGGGATGGTCCCAGACATTCTGTTCAAT
CCCCATGGTTTTCCATCCCGCATGACCATTGGGATGTTAATTGAGAGTATGGCCGGGAAG
TCTGCAGCTTTGCATGGTCTCTGCCATGATGCTACACCCTTCATCTTCTCAGAGGAGAAC
TCGGCCTTAGAATACTTTGGTGAGATGTTAAAGGCTGCTGGCTACAATTTCTATGGCACC
GAGAGGTTATATAGTGGCATCAGTGGGCTAGAACTGGAAGCAGACATCTTCATAGGAGTG
GTTTATTATCAGCGCTTACGCCATATGGTCTCAGACAAATTTCAAGTAAGGACAACTGGA
GCCCGAGACAGAGTCACCAACCAGCCTATTGGGGGAAGAAATGTCCAGGGTGGAATCCGT
TTTGGGGAGATGGAACGGGATGCGCTTTTAGCTCATGGTACATCTTTTCTCCTTCATGAC
CGCCTCTTCAACTGCTCAGATCGGTCGGTAGCCCATGTGTGTGTGAAGTGTGGCAGTTTA
CTCTCTCCACTGTTGGAGAAGCCACCCCCTTCTTGGTCTGCCATGCGCAACAGAAAATAC
AACTGTACTCTGTGTAGTCGCAGTGACACTATCGATACTGTTTCTGTGCCTTATGTTTTT
CGGTATTTTGTAGCTGAACTGGCAGCTATGAACATCAAAGTGAAACTGGATGTTGTTTAA
Enzyme 29 GenBank Gene ID AK022533 Link Image
Enzyme 29 GeneCard ID POLR1B Link Image
Enzyme 29 GenAtlas ID POLR1B Link Image
Enzyme 29 HGNC ID HGNC:20454 Link Image
Enzyme 29 Chromosome Location 2
Enzyme 29 Locus 2q13
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References Not Available
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 6027
Enzyme 30 Name DNA-directed RNA polymerase III subunit 127.6 kDa polypeptide
Enzyme 30 Synonyms
  1. RNA polymerase III subunit 2
  2. RPC2
Enzyme 30 Gene Name POLR3B
Enzyme 30 Protein Sequence >DNA-directed RNA polymerase III subunit 127.6 kDa polypeptide 
MDVLAEEFGNLTPEQLAAPIPTVEEKWRLLPAFLKVKGLVKQHIDSFNYFINVEIKKIMK
ANEKVTSDADPMWYLKYLNIYVGLPDVEESFNVTRPVSPHECRLRDMTYSAPITVDIEYT
RGSQRIIRNALPIGRMPIMLRSSNCVLTGKTPAEFAKLNECPLDPGGYFIVKGVEKVILI
QEQLSKNRIIVEADRKGAVGASVTSSTHEKKSRTNMAVKQGRFYLRHNTLSEDIPIVIIF
KAMGVESDQEIVQMIGTEEHVMAAFGPSLEECQKAQIFTQMQALKYIGNKVRRQRMWGGG
PKKTKIEEARELLASTILTHVPVKEFNFRAKCIYTAVMVRRVILAQGDNKVDDRDYYGNK
RLELAGQLLSLLFEDLFKKFNSEMKKIADQVIPKQRAAQFDVVKHMRQDQITNGMVNAIS
TGNWSLKRFKMDRQGVTQVLSRLSYISALGMMTRISSQFEKTRKVSGPRSLQPSQWGMLC
PSDTPEGEACGLVKNLALMTHITTDMEDGPIVKLASNLGVEDVNLLCGEELSYPNVFLVF
LNGNILGVIRDHKKLVNTFRLMRRAGYINEFVSISTNLTDRCVYISSDGGRLCRPYIIVK
KQKPAVTNKHMEELAQGYRNFEDFLHESLVEYLDVNEENDCNIALYEHTINKDTTHLEIE
PFTLLGVCAGLIPYPHHNQSPRNTYQCAMGKQAMGTIGYNQRNRIDTLMYLLAYPQKPMV
KTKTIELIEFEKLPAGQNATVAVMSYSGYDIEDALVLNKASLDRGFGRCLVYKNAKCTLK
RYTNQTFDKVMGPMLDAATRKPIWRHEILDADGICSPGEKVENKQVLVNKSMPTVTQIPL
EGSNVPQQPQYKDVPITYKGATDSYIEKVMISSNAEDAFLIKMLLRQTRRPEIGDKFSSR
HGQKGVCGLIVPQEDMPFCDSGICPDIIMNPHGFPSRMTVGKLIELLAGKAGVLDGRFHY
GTAFGGSKVKDVCEDLVRHGYNYLGKDYVTSGITGEPLEAYIYFGPVYYQKLKHMVLDKM
HARARGPRAVLTRQPTEGRSRDGGLRLGEMERDCLIGYGASMLLLERLMISSDAFEVDVC
GQCGLLGYSGWCHYCKSSCHVSSLRIPYACKLLFQELQSMNIIPRLKLSKYNE
Enzyme 30 Number of Residues 1133
Enzyme 30 Molecular Weight 127787
Enzyme 30 Theoretical pI 8.64
Enzyme 30 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • transcription
Component
—
Enzyme 30 General Function Transcription
Enzyme 30 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Enzyme 30 Pathways
Enzyme 30 Reactions
  • nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 24429617 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID Q9NW08 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name RPC2_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >3402 bp 
ATGGACGTGCTAGCGGAGGAGTTTGGGAACCTGACTCCGGAGCAGCTGGCGGCGCCGATC
CCGACTGTAGAGGAAAAATGGAGGCTGCTTCCAGCATTTTTAAAGGTGAAAGGCCTTGTG
AAACAGCATATAGATTCATTTAACTATTTCATTAATGTAGAGATAAAGAAGATAATGAAA
GCCAATGAAAAGGTTACAAGTGACGCTGACCCTATGTGGTACTTAAAATATCTTAATATC
TATGTTGGGCTTCCTGATGTTGAAGAAAGCTTCAATGTAACTAGACCAGTGTCCCCTCAT
GAGTGCCGTTTGAGAGACATGACATACTCTGCCCCTATTACAGTGGATATTGAATATACC
CGAGGCAGCCAGAGGATCATCCGCAATGCCTTACCTATCGGCAGAATGCCCATAATGCTA
CGTAGTTCAAACTGTGTTCTTACAGGAAAAACGCCAGCAGAATTTGCCAAACTGAACGAA
TGTCCCTTAGATCCAGGTGGCTACTTCATTGTTAAAGGAGTAGAAAAAGTTATTCTTATC
CAAGAGCAGCTGTCTAAGAACAGGATCATCGTGGAGGCTGATAGAAAAGGGGCTGTTGGA
GCTTCAGTTACCAGCTCTACCCATGAGAAAAAAAGCAGAACCAATATGGCTGTGAAACAA
GGACGATTTTATTTGAGGCATAATACTTTGTCAGAAGATATACCCATTGTCATCATATTT
AAGGCCATGGGTGTTGAGAGTGACCAGGAAATTGTGCAGATGATTGGAACAGCGGAGCAC
GTGATGGCTGCATTTGGGCCCAGTCTGGAAGAGTGCCAGAAAGCTCAGATTTTCACACAG
ATGCAGGCATTAAAATATATAGGGAACAAAGTAAGAAGGCAAAGGATGTGGGGAGGTGGA
CCAAAGAAAACCAAAATAGAAGAAGCAAGAGAGCTCCTGGCTTCCACCATTCTGACCCAT
GTCCCAGTTAAGGAATTCAATTTCCGAGCCAAATGTATCTATACTGCAGTGATGGTGCGA
AGAGTTATTCTGGCCCAAGGAGATAATAAAGTTGACGACAGAGATTATTATGGTAACAAG
CGACTGGAATTGGCAGGACAGCTTTTATCTCTTCTTTTTGAAGACTTGTTCAAAAAATTT
AATTCTGAAATGAAAAAGATTGCCGACCAGGTGATTCCTAAGCAAAGAGCAGCCCAGTTT
GATGTTGTCAAACACATGCGCCAAGACCAGATCACCAATGGCATGGTGAATGCTATTTCT
ACCGGAAATTGGTCTTTAAAGAGATTTAAAATGGACCGCCAGGGTGTAACCCAAGTGCTG
TCTCGCTTGTCATATATATCCGCACTGGGCATGATGACAAGAATCTCTTCCCAGTTTGAA
AAAACGAGAAAAGTGAGTGGTCCTCGCTCCCTCCAGCCATCTCAGTGGGGAATGCTGTGT
CCTTCGGACACTCCTGAAGGAGAGGCATGTGGTTTGGTTAAAAACTTGGCCCTTATGACA
CACATCACAACTGATATGGAAGATGGACCCATTGTTAAATTAGCCAGTAACTTGGGAGTA
GAAGATGTGAATTTATTATGTGGGGAAGAGCTCTCTTACCCAAATGTGTTTCTTGTCTTT
CTTAATGGTAACATCTTAGGTGTCATTCGAGACCACAAAAAGCTAGTGAATACATTTCGA
CTCATGAGAAGAGCAGGATATATCAATGAATTTGTTTCCATCTCAACAAATCTTACAGAT
CGATGTGTCTATATTTCTTCTGATGGGGGAAGGCTATGCAGACCCTACATAATTGTCAAG
AAACAGAAGCCAGCAGTCACAAATAAACATATGGAAGAGCTGGCCCAAGGGTACAGGAAT
TTTGAAGATTTCTTACATGAGAGTCTGGTTGAATATTTAGATGTGAATGAAGAAAATGAT
TGTAACATTGCACTGTACGAACACACAATTAATAAAGACACCACCCACTTGGAGATTGAA
CCCTTCACTCTTCTCGGCGTGTGTGCTGGACTTATCCCATACCCTCACCATAACCAGTCA
CCGAGAAACACTTATCAGTGTGCCATGGGGAAACAAGCCATGGGTACTATAGGATACAAC
CAGCGAAACAGAATTGATACTCTCATGTATCTACTAGCATATCCACAAAAACCCATGGTT
AAGACAAAAACCATTGAATTGATAGAATTTGAGAAACTGCCAGCTGGACAGAATGCAACA
GTTGCTGTGATGAGCTATAGTGGCTATGATATTGAAGATGCTCTTGTTTTAAACAAGGCC
TCTTTAGACAGAGGCTTTGGGCGTTGCCTTGTATATAAAAATGCTAAATGTACGTTGAAA
CGATACACCAATCAGACTTTTGATAAAGTGATGGGGCCCATGTTGGATGCTGCTACAAGG
AAACCTATCTGGCGACATGAAATCTTAGATGCAGATGGTATTTGTTCTCCAGGTGAGAAA
GTAGAAAACAAACAAGTGCTTGTAAATAAGTCCATGCCCACAGTGACTCAGATTCCTTTG
GAAGGAAGTAATGTACCACAGCAACCACAGTACAAAGATGTACCCATAACCTACAAAGGA
GCAACAGACTCATATATTGAAAAAGTGATGATATCTTCAAATGCTGAAGATGCTTTTCTG
ATCAAAATGCTGCTGAGACAGACAAGGCGTCCAGAAATTGGAGACAAATTCAGCAGTCGT
CATGGGCAAAAAGGTGTTTGTGGCTTGATCGTCCCCCAGGAAGACATGCCATTTTGTGAT
TCTGGCATCTGTCCGGACATCATCATGAACCCACACGGCTTCCCATCACGAATGACGGTG
GGGAAGCTCATTGAGCTGCTGGCTGGCAAGGCCGGTGTGCTGGACGGCAGATTCCACTAC
GGCACTGCGTTTGGAGGCAGTAAAGTGAAGGATGTGTGTGAGGACCTCGTTCGCCATGGT
TATAACTACTTGGGGAAAGACTATGTTACATCCGGCATCACAGGTGAGCCCTTAGAAGCA
TACATCTATTTTGGCCCCGTGTACTATCAGAAGCTGAAACACATGGTGCTAGATAAAATG
CATGCCCGGGCCCGGGGCCCACGAGCCGTCCTTACCAGGCAACCCACTGAAGGACGGTCT
CGTGATGGTGGCTTGCGTCTCGGGGAAATGGAACGTGACTGTTTAATCGGTTATGGAGCC
AGTATGCTTTTGCTAGAGAGACTAATGATTTCAAGTGATGCCTTTGAGGTTGATGTCTGT
GGGCAGTGTGGACTTCTGGGGTATTCTGGCTGGTGCCATTACTGCAAGTCATCCTGCCAC
GTGTCTTCCCTCCGTATTCCGTATGCCTGCAAGCTGCTCTTCCAGGAACTACAGTCTATG
AACATCATCCCCAGGTTAAAACTGTCCAAGTACAATGAATGA
Enzyme 30 GenBank Gene ID AY092084 Link Image
Enzyme 30 GeneCard ID POLR3B Link Image
Enzyme 30 GenAtlas ID POLR3B Link Image
Enzyme 30 HGNC ID HGNC:30348 Link Image
Enzyme 30 Chromosome Location 12
Enzyme 30 Locus 12q23.3
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Hu P, Wu S, Sun Y, Yuan CC, Kobayashi R, Myers MP, Hernandez N: Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits. Mol Cell Biol. 2002 Nov;22(22):8044-55. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 6031
Enzyme 31 Name DNA-directed RNA polymerase I-associated factor 53 kDa subunit
Enzyme 31 Synonyms
  1. RNA polymerase I polypeptide E
  2. RNA polymerase I- associated factor 1
Enzyme 31 Gene Name POLR1E
Enzyme 31 Protein Sequence >DNA-directed RNA polymerase I-associated factor 53 kDa subunit 
MYQASAVSLLPRDIPSCHSPSPGFSHLPTSSSQLAPDLLQFPLGQDPSFLAIPILTLPPS
DSLVPPYIVWYIVWPSALISFLGCTLTVQFSNGKLQSPGNMRFTLYENKDSTNPRKRNQR
ILAAETDRLSYVGNNFGTGALKCNTLCRHFVGILNKTSGQMEVYDAELFNMQPLFSDVSV
ESELALESQTKTYREKMDSCIEAFGTTKQKRALNTRRMNRVGNESLNRAVAKAAETIIDT
KGVTALVSDAIHNDLQDDSLYLPPCYDDAAKPEDVYKFEDLLSPAEYEALQSPSEAFRNV
TSEEILKMIEENSHCTFVIEALKSLPSDVESRDRQARCIWFLDTLIKFRAHRVVKRKSAL
GPGVPHIINTKLLKHFTCLTYNNGRLRNLISDSMKAKITAYVIILALHIHDFQIDLTVLQ
RDLKLSEKRMMEIAKAMRLKISKRRVSVAAGSEEDHKLGTLSLPLPPAQTSDRLAKRRKI
T
Enzyme 31 Number of Residues 481
Enzyme 31 Molecular Weight 53963
Enzyme 31 Theoretical pI 8.74
Enzyme 31 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • binding
  • catalytic activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • transcription
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 31 General Function Not Available
Enzyme 31 Specific Function Required for the initiation of transcription by the DNA- dependent RNA polymerase I holoenzyme. This complex catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Enzyme 31 Pathways
Enzyme 31 Reactions
  • nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 10435392 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q9GZS1 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name RPF53_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >1260 bp 
ATGGCGGCGGAGGTGTTGCCGAGTGCGAGGTGGCAGTATTGTGGGGCGCCCGACGGGAGC
CAGAGAGCTGTACTGGTCCAGTTCTCCAACGGGAAGCTACAGAGTCCAGGCAACATGCGC
TTTACCTTGTATGAGAACAAAGATTCCACCAACCCCAGGAAGAGGAATCAACGGATCCTG
GCAGCTGAAACAGATAGGCTCTCCTATGTGGGAAACAATTTTGGGACTGGAGCCCTCAAA
TGCAACACTTTGTGCAGGCACTTTGTGGGAATTTTGAACAAGACCTCTGGCCAAATGGAA
GTATATGATGCTGAATTGTTCAACATGCAGCCACTATTTTCAGATGTATCAGTTGAGAGT
GAACTGGCGCTAGAGAGTCAGACCAAAACTTACAGAGAAAAGATGGATTCTTGTATTGAA
GCCTTTGGTACCACCAAACAGAAGCGAGCTCTGAACACCAGGAGAATGAACAGAGTTGGC
AATGAATCTTTGAATCGTGCAGTGGCTAAAGCTGCAGAGACTATCATTGATACGAAGGGT
GTGACTGCTCTGGTCAGCGATGCTATCCACAATGACTTGCAAGATGACTCCCTCTACCTT
CCTCCCTGCTATGATGATGCAGCCAAGCCTGAAGACGTGTATAAATTTGAAGATCTTCTT
TCCCCTGCGGAGTATGAAGCTCTTCAGAGCCCATCTGAAGCTTTCAGGAACGTCACGTCA
GAAGAAATACTGAAGATGATTGAGGAGAACAGCCATTGCACCTTTGTCATAGAAGCGTTG
AAGTCTTTGCCATCAGATGTGGAGAGCCGAGACCGCCAGGCCCGATGCATATGGTTTCTG
GATACCCTCATCAAATTTCGAGCTCATAGGGTAGTTAAGCGGAAAAGTGCTCTGGGACCT
GGAGTTCCCCACATCATCAACACCAAACTGCTGAAGCACTTTACTTGCTTGACCTACAAC
AATGGCAGATTACGGAACTTAATTTCGGATTCTATGAAGGCGAAGATTACTGCATATGTG
ATCATACTTGCCTTGCACATACATGACTTCCAAATTGACCTGACAGTGTTACAGAGGGAC
TTGAAGCTCAGTGAGAAAAGGATGATGGAGATAGCCAAAGCCATGAGGCTGAAGATCTCC
AAAAGAAGGGTGTCTGTGGCCGCCGGCAGTGAAGAAGATCACAAACTGGGCACCCTGTCC
CTCCCGCTGCCTCCAGCCCAGACCTCAGACCGCCTGGCAAAGCGGAGGAAGATTACCTAG
Enzyme 31 GenBank Gene ID AK023452 Link Image
Enzyme 31 GeneCard ID POLR1E Link Image
Enzyme 31 GenAtlas ID POLR1E Link Image
Enzyme 31 HGNC ID HGNC:17631 Link Image
Enzyme 31 Chromosome Location 9
Enzyme 31 Locus 9p13.2
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Scherl A, Coute Y, Deon C, Calle A, Kindbeiter K, Sanchez JC, Greco A, Hochstrasser D, Diaz JJ: Functional proteomic analysis of human nucleolus. Mol Biol Cell. 2002 Nov;13(11):4100-9. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 6035
Enzyme 32 Name DNA-directed RNA polymerase III subunit 22.9 kDa polypeptide
Enzyme 32 Synonyms
  1. RPC8
Enzyme 32 Gene Name POLR3H
Enzyme 32 Protein Sequence >DNA-directed RNA polymerase III subunit 22.9 kDa polypeptide 
MFVLVEMVDTVRIPPWQFERKLNDSIAEELNKKLANKVVYNVGLCICLFDITKLEDAYVF
PGDGASHTKVHFRCVVFHPFLDEILIGKIKGCSPEGVHVSLGFFDDILIPPESLQQPAKF
DEAEQVWVWEYETEEGAHDLYMDTGEEIRFRVVDESFVDTSPTGPSSADATTSSEELPKK
EAPYTLVGSISEPGLGLLSWWTSN
Enzyme 32 Number of Residues 204
Enzyme 32 Molecular Weight 22918
Enzyme 32 Theoretical pI 4.21
Enzyme 32 GO Classification
Function
  • DNA-directed RNA polymerase activity
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • transcription
Component
—
Enzyme 32 General Function Transcription
Enzyme 32 Specific Function DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates
Enzyme 32 Pathways
Enzyme 32 Reactions
  • nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 24429623 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID Q9Y535 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name RPC8_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >615 bp 
ATGTTCGTCCTGGTGGAAATGGTGGACACCGTCCGGATCCCCCCTTGGCAGTTTGAGAGG
AAGCTCAACGACTCCATTGCCGAGGAGCTGAACAAGAAGTTGGCCAACAAGGTCGTGTAC
AACGTGGGACTCTGCATTTGTCTGTTTGATATCACCAAACTGGAGGATGCCTATGTATTC
CCTGGGGATGGCGCATCACACACCAAAGTCCATTTTCGCTGCGTGGTGTTTCATCCATTC
CTAGATGAGATTCTCATTGGGAAGATCAAAGGCTGCAGCCCAGAAGGAGTGCACGTCTCT
CTAGGCTTCTTCGATGACATTCTCATCCCCCCAGAGTCACTGCAGCAGCCAGCCAAGTTC
GACGAAGCGGAGCAGGTGTGGGTGTGGGAGTACGAGACGGAGGAAGGAGCACACGACCTC
TACATGGACACCGGCGAGGAGATCCGCTTCCGGGTGGTGGACGAGAGCTTTGTTGACACG
TCCCCCACAGGGCCCAGCTCAGCAGATGCCACCACTTCCAGTGAGGAGCTGCCAAAGAAG
GAGGCTCCGTACACGCTTGTGGGATCCATCAGTGAGCCAGGCCTGGGCCTTCTCTCCTGG
TGGACCAGCAACTAG
Enzyme 32 GenBank Gene ID AY092087 Link Image
Enzyme 32 GeneCard ID POLR3H Link Image
Enzyme 32 GenAtlas ID POLR3H Link Image
Enzyme 32 HGNC ID HGNC:30349 Link Image
Enzyme 32 Chromosome Location 22
Enzyme 32 Locus 22q13.2
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Hu P, Wu S, Sun Y, Yuan CC, Kobayashi R, Myers MP, Hernandez N: Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits. Mol Cell Biol. 2002 Nov;22(22):8044-55. [PubMed Link Image]
  2. Hirosawa M, Nagase T, Murahashi Y, Kikuno R, Ohara O: Identification of novel transcribed sequences on human chromosome 22 by expressed sequence tag mapping. DNA Res. 2001 Feb 28;8(1):1-9. [PubMed Link Image]
  3. 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]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 6036
Enzyme 33 Name DNA-directed RNA polymerases III 12.5 kDa polypeptide
Enzyme 33 Synonyms
  1. RNA polymerase III subunit K
  2. RNA polymerase III C11 subunit
  3. HsC11p
  4. hRPC11
Enzyme 33 Gene Name POLR3K
Enzyme 33 Protein Sequence >DNA-directed RNA polymerases III 12.5 kDa polypeptide 
MLLFCPGCGNGLIVEEGQRCHRFSCNTCPYVHNITRKVTNRKYPKLKEVDDVLGGAAAWE
NVDSTAESCPKCEHPRAYFMQLQTRSADEPMTTFYKCCNAQCGHRWRD
Enzyme 33 Number of Residues 108
Enzyme 33 Molecular Weight 12336
Enzyme 33 Theoretical pI 7.89
Enzyme 33 GO Classification
Function
  • DNA binding
  • DNA-directed RNA polymerase activity
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • nucleic acid binding
  • nucleotidyltransferase activity
  • transcription factor activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transition metal ion binding
  • zinc ion binding
Process
  • RNA elongation
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • regulation of biological process
  • regulation of cellular metabolism
  • regulation of metabolism
  • regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • regulation of physiological process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
  • transcription
  • transcription, DNA-dependent
Component
—
Enzyme 33 General Function Transcription
Enzyme 33 Specific Function Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Enzyme 33 Pathways
Enzyme 33 Reactions
  • nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 4877775 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q9Y2Y1 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name RPC11_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >327 bp 
ATGCTGCTGTTCTGCCCCGGCTGCGGGAACGGGCTGATCGTGGAGGAGGGACAACGCTGC
CACCGCTTCGCCTGCAACACGTGCCCCTACGTGCACAACATCACCCGCAAGGTAACAAAT
CGGAAGTACCCAAAACTGAAAGAAGTGGATGATGTGCTTGGTGGAGCAGCTGCCTGGGAG
AATGTTGACTCTACTGCAGAGTCGTGTCCCAAATGCGAACATCCTCGTGCTTACTTCATG
CAGCTTCAGACCCGCTCTGCAGATGAGCCGATGACCACCTTCTACAAGTGCTGCAATGCT
CAGTGTGGACACCGCTGGAGGGATTAG
Enzyme 33 GenBank Gene ID AF126531 Link Image
Enzyme 33 GeneCard ID POLR3K Link Image
Enzyme 33 GenAtlas ID POLR3K Link Image
Enzyme 33 HGNC ID HGNC:14121 Link Image
Enzyme 33 Chromosome Location 16
Enzyme 33 Locus 16p13.3
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Chedin S, Riva M, Schultz P, Sentenac A, Carles C: The RNA cleavage activity of RNA polymerase III is mediated by an essential TFIIS-like subunit and is important for transcription termination. Genes Dev. 1998 Dec 15;12(24):3857-71. [PubMed Link Image]
  2. Spakovskii GV, Lebedenko EN: [Molecular identification and characteristics of hRPC11, the smallest specific subunit of human RNA polymerase III] Bioorg Khim. 1998 Nov;24(11):877-80. [PubMed Link Image]
  3. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 6041
Enzyme 34 Name Pyruvate kinase isozymes R/L
Enzyme 34 Synonyms
  1. R-type/L-type pyruvate kinase
  2. Red cell/liver pyruvate kinase
  3. Pyruvate kinase 1
Enzyme 34 Gene Name PKLR
Enzyme 34 Protein Sequence >Pyruvate kinase isozymes R/L 
MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQ
LPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFS
HGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKG
SQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQV
ENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAA
LGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRC
NLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKM
QHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRS
AQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESG
KLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
Enzyme 34 Number of Residues 574
Enzyme 34 Molecular Weight 61831
Enzyme 34 Theoretical pI 7.83
Enzyme 34 GO Classification
Function
  • catalytic activity
  • kinase activity
  • pyruvate kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 34 General Function Carbohydrate transport and metabolism
Enzyme 34 Specific Function ATP + pyruvate = ADP + phosphoenolpyruvate
Enzyme 34 Pathways
Enzyme 34 Reactions
  • ATP + pyruvate = ADP + phosphoenolpyruvate
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 3327365 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID P30613 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name KPYR_HUMAN Link Image
Enzyme 34 PDB ID 1LIU Link Image
Enzyme 34 PDB File Show
Enzyme 34 3D Structure
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >1725 bp 
ATGTCGATCCAGGAGAACATATCATCCCTGCAGCTTCGGTCATGGGTCTCTAAGTCCCAA
AGAGACTTAGCAAAGTCCATCCTGATTGGGGCTCCAGGAGGGCCAGCGGGGTATCTGCGG
CGGGCCAGTGTGGCCCAACTGACCCAGGAGCTGGGCACTGCCTTCTTCCAGCAGCAGCAG
CTGCCAGCTGCTATGGCAGACACCTTCCTGGAACACCTCTGCCTACTGGACATTGACTCC
GAGCCCGTGGCTGCTCGCAGTACCAGCATCATTGCCACCATCGGGCCAGCATCTCGCTCC
GTGGAGCGCCTCAAGGAGATGATCAAGGCCGGGATGAACATTGCGCGACTCAACTTCTCC
CACGGCTCCCACGAGTACCATGCTGAGTCCATCGCCAACGTCCGGGAGGCGGTGGAGAGC
TTTGCAGGTTCCCCACTCAGCTACCGGCCCGTGGCCATCGCCCTGGACACCAAGGGACCG
GAGATCCGCACTGGGATCCTGCAGGGGGGTCCAGAGTCGGAAGTGGAGCTGGTGAAGGGC
TCCCAGGTGCTGGTGACTGTGGACCCCGCGTTCCGGACGCGGGGGAACGCGAACACCGTG
TGGGTGGACTACCCCAATATTGTCCGGGTCGTGCCGGTGGGGGGCCGCATCTACATTGAC
GACGGGCTCATCTCCCTAGTGGTCCAGAAAATCGGCCCAGAGGGACTGGTGACCCAAGTG
GAGAACGGCGGCGTCCTGGGCAGCCGGAAGGGCGTGAACTTGCCAGGGGCCCAGGTGGAC
TTGCCCGGGCTGTCCGAGCAGGACGTCCGAGACCTGCGCTTCGGGGTGGAGCATGGGGTG
GACATCGTCTTTGCCTCCTTTGTGCGGAAAGCCAGCGACGTGGCTGCCGTCAGGGCTGCT
CTGGGTCCGGAAGGACACGGCATCAAGATCATCAGCAAAATTGAGAACCACGAAGGCGTG
AAGAGGTTTGATGAAATCCTGGAGGTGAGCGACGGCATCATGGTGGCACGGGGGGACCTA
GGCATCGAGATCCCAGCAGAGAAGGTTTTCCTGGCTCAGAAGATGATGATTGGGCGCTGC
AACTTGGCGGGCAAGCCTGTTGTCTGTGCCACACAGATGCTGGAGAGCATGATTACCAAG
CCCCGGCCAACGAGGGCAGAGACAAGCGATGTCGCCAATGCTGTGCTGGATGGGGCTGAC
TGCATCATGCTGTCAGGGGAGACTGCCAAGGGCAACTTCCCTGTGGAAGCGGTGAAGATG
CAGCATGCGATTGCCCGGGAGGCAGAGGCCGCAGTGTACCACCGGCAGCTGTTTGAGGAG
CTACGTCGGGCAGCGCCACTAAGCCGTGATCCCACTGAGGTCACCGCCATTGGTGCTGTG
GAGGCTGCCTTCAAGTGCTGTGCTGCTGCCATCATTGTGCTGACCACAACTGGCCGCTCA
GCCCAGCTTCTGTCTCGGTACCGACCTCGGGCAGCAGTCATTGCTGTCACCCGCTCTGCC
CAGGCTGCCCGCCAGGTCCACTTATGCCGAGGAGTCTTCCCCTTGCTTTACCGTGAACCT
CCAGAAGCCATCTGGGCAGATGATGTAGATCGCCGGGTGCAATTTGGCATTGAAAGTGGA
AAGCTCCGTGGCTTCCTCCGTGTTGGAGACCTGGTGATTGTGGTGACAGGCTGGCGACCT
GGCTCCGGCTACACCAACATCATGAGGGTGCTAAGCATATCCTGA
Enzyme 34 GenBank Gene ID AB015983 Link Image
Enzyme 34 GeneCard ID PKLR Link Image
Enzyme 34 GenAtlas ID PKLR Link Image
Enzyme 34 HGNC ID HGNC:9020 Link Image
Enzyme 34 Chromosome Location 1
Enzyme 34 Locus 1q21
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Kanno H, Fujii H, Hirono A, Miwa S: cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384----Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia. Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):8218-21. [PubMed Link Image]
  2. Tani K, Fujii H, Nagata S, Miwa S: Human liver type pyruvate kinase: complete amino acid sequence and the expression in mammalian cells. Proc Natl Acad Sci U S A. 1988 Mar;85(6):1792-5. [PubMed Link Image]
  3. Tani K, Fujii H, Tsutsumi H, Sukegawa J, Toyoshima K, Yoshida MC, Noguchi T, Tanaka T, Miwa S: Human liver type pyruvate kinase: cDNA cloning and chromosomal assignment. Biochem Biophys Res Commun. 1987 Mar 13;143(2):431-8. [PubMed Link Image]
  4. Kanno H, Fujii H, Tsujino G, Miwa S: Molecular basis of impaired pyruvate kinase isozyme conversion in erythroid cells: a single amino acid substitution near the active site and decreased mRNA content of the R-type PK. Biochem Biophys Res Commun. 1993 Apr 15;192(1):46-52. [PubMed Link Image]
  5. Beutler E, Baronciani L: Mutations in pyruvate kinase. Hum Mutat. 1996;7(1):1-6. [PubMed Link Image]
  6. Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase. Blood Cells Mol Dis. 1996;22(1):85-9. [PubMed Link Image]
  7. Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (1st update). Blood Cells Mol Dis. 1996;22(3):259-64. [PubMed Link Image]
  8. Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (2nd update). Blood Cells Mol Dis. 1998 Sep;24(3):273-9. [PubMed Link Image]
  9. Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (Third update). Blood Cells Mol Dis. 2000 Feb;26(1):47-53. [PubMed Link Image]
  10. Neubauer B, Lakomek M, Winkler H, Parke M, Hofferbert S, Schroter W: Point mutations in the L-type pyruvate kinase gene of two children with hemolytic anemia caused by pyruvate kinase deficiency. Blood. 1991 May 1;77(9):1871-5. [PubMed Link Image]
  11. Kanno H, Fujii H, Hirono A, Omine M, Miwa S: Identical point mutations of the R-type pyruvate kinase (PK) cDNA found in unrelated PK variants associated with hereditary hemolytic anemia. Blood. 1992 Mar 1;79(5):1347-50. [PubMed Link Image]
  12. Kanno H, Fujii H, Miwa S: Low substrate affinity of pyruvate kinase variant (PK Sapporo) caused by a single amino acid substitution (426 Arg-->Gln) associated with hereditary hemolytic anemia. Blood. 1993 May 1;81(9):2439-41. [PubMed Link Image]
  13. Baronciani L, Beutler E: Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia. Proc Natl Acad Sci U S A. 1993 May 1;90(9):4324-7. [PubMed Link Image]
  14. Kanno H, Ballas SK, Miwa S, Fujii H, Bowman HS: Molecular abnormality of erythrocyte pyruvate kinase deficiency in the Amish. Blood. 1994 Apr 15;83(8):2311-6. [PubMed Link Image]
  15. Lenzner C, Nurnberg P, Thiele BJ, Reis A, Brabec V, Sakalova A, Jacobasch G: Mutations in the pyruvate kinase L gene in patients with hereditary hemolytic anemia. Blood. 1994 May 15;83(10):2817-22. [PubMed Link Image]
  16. Baronciani L, Beutler E: Molecular study of pyruvate kinase deficient patients with hereditary nonspherocytic hemolytic anemia. J Clin Invest. 1995 Apr;95(4):1702-9. [PubMed Link Image]
  17. Beutler E, Westwood B, van Zwieten R, Roos D: G-->T transition at cDNA nt 110 (K37Q) in the PKLR (pyruvate kinase) gene is the molecular basis of a case of hereditary increase of red blood cell ATP. Hum Mutat. 1997;9(3):282-5. [PubMed Link Image]
  18. Zarza R, Alvarez R, Pujades A, Nomdedeu B, Carrera A, Estella J, Remacha A, Sanchez JM, Morey M, Cortes T, Perez Lungmus G, Bureo E, Vives Corrons JL: Molecular characterization of the PK-LR gene in pyruvate kinase deficient Spanish patients. Red Cell Pathology Group of the Spanish Society of Haematology (AEHH). Br J Haematol. 1998 Nov;103(2):377-82. [PubMed Link Image]
  19. Cohen-Solal M, Prehu C, Wajcman H, Poyart C, Bardakdjian-Michau J, Kister J, Prome D, Valentin C, Bachir D, Galacteros F: A new sickle cell disease phenotype associating Hb S trait, severe pyruvate kinase deficiency (PK Conakry), and an alpha2 globin gene variant (Hb Conakry). Br J Haematol. 1998 Dec;103(4):950-6. [PubMed Link Image]
  20. Pastore L, Della Morte R, Frisso G, Alfinito F, Vitale D, Calise RM, Ferraro F, Zagari A, Rotoli B, Salvatore F: Novel mutations and structural implications in R-type pyruvate kinase-deficient patients from Southern Italy. Hum Mutat. 1998;11(2):127-34. [PubMed Link Image]
  21. Zanella A, Bianchi P, Fermo E, Iurlo A, Zappa M, Vercellati C, Boschetti C, Baronciani L, Cotton F: Molecular characterization of the PK-LR gene in sixteen pyruvate kinase-deficient patients. Br J Haematol. 2001 Apr;113(1):43-8. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 6159
Enzyme 35 Name Ectonucleoside triphosphate diphosphohydrolase 4
Enzyme 35 Synonyms
  1. NTPDase 4
  2. Uridine-diphosphatase
  3. UDPase
  4. Lysosomal apyrase-like protein of 70 kDa
Enzyme 35 Gene Name ENTPD4
Enzyme 35 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 4 
MGRIGISCLFPASWHFSISPVGCPRILNTNLRQIMVISVLAAAVSLLYFSVVIIRNKYGR
LTRDKKFQRYLARVTDIEATDTNNPNVNYGIVVDCGSSGSRVFVYCWPRHNGNPHDLLDI
RQMRDKNRKPVVMKIKPGISEFATSPEKVSDYISPLLNFAAEHVPRAKHKETPLYILCTA
GMRILPESQQKAILEDLLTDIPVHFDFLFSDSHAEVISGKQEGVYAWIGINFVLGRFEHI
EDDDEAVVEVNIPGSESSEAIVRKRTAGILDMGGVSTQIAYEVPKTVSFASSQQEEVAKN
LLAEFNLGCDVHQTEHVYRVYVATFLGFGGNAARQRYEDRIFANTIQKNRLLGKQTGLTP
DMPYLDPCLPLDIKDEIQQNGQTIYLRGTGDFDLCRETIQPFMNKTNETQTSLNGVYQPP
IHFQNSEFYGFSEFYYCTEDVLRMGGDYNAAKFTKAAKDYCATKWSILRERFDRGLYASH
ADLHRLKYQCFKSAWMFEVFHRGFSFPVNYKSLKTALQVYDKEVQWTLGAILYRTRFLPL
RDIQQEAFRASHTHWRGVSFVYNHYLFSGCFLVVLLAILLYLLRLRRIHRRTPRSSSAAA
LWMEEGLPAQNAPGTL
Enzyme 35 Number of Residues 616
Enzyme 35 Molecular Weight 70256
Enzyme 35 Theoretical pI 8.39
Enzyme 35 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 35 General Function Not Available
Enzyme 35 Specific Function Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent. The order of activity with different substrates is UDP >> GDP = CDP = TDP, AMP, ADP, ATP and UMP are not substrates. Preferred substrates for isoform 2 are CTP, UDP, CDP, GTP and GDP, while isoform 1 utilizes UTP and TTP
Enzyme 35 Pathways
Enzyme 35 Reactions
  • A nucleoside diphosphate + H2O = a nucleotide + phosphate
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • 34-54 560-580
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 3153211 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID Q9Y227 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name ENTP4_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >1830 bp 
ATGGGGAGGATTGGCATCTCCTGTCTTTTTCCTGCTTCTTGGCATTTTAGCATATCTCCA
GTAGGGTGTCCTCGAATTCTGAATACCAATTTACGCCAAATTATGGTCATTAGTGTCCTG
GCTGCTGCTGCTGTTTCACTTTTATATTTTTCTGTTGTCATAATCCGAAATAAGTATGGG
CGACTAACCAGAGACAAGAAATTTCAAAGGTACCTGGCACGAGTTACCGACATTGAAGCT
ACAGACACCAATAACCCCAATGTGAACTATGGGATCGTGGTGGACTGTGGTAGCAGTGGG
TCTCGAGTATTTGTTTACTGCTGGCCAAGGCATAATGGCAATCCACATGATCTGTTGGAT
ATCAGGCAAATGAGGGATAAAAACCGAAAGCCAGTGGTCATGAAGATAAAACCGGGCATT
TCAGAATTTGCTACCTCTCCAGAGAAAGTCAGTGATTACATTTCTCCACTTTTGAACTTT
GCTGCAGAGCATGTGCCACGGGCAAAACACAAAGAGACACCTCTCTACATTCTCTGCACG
GCTGGAATGAGAATCCTCCCCGAAAGCCAGCAGAAAGCTATTCTGGAAGACCTTCTGACC
GATATCCCCGTGCACTTTGACTTTCTGTTTTCTGACTCTCATGCAGAAGTAATTTCTGGG
AAACAAGAAGGTGTGTATGCTTGGATTGGCATTAATTTTGTCCTTGGACGATTTGAGCAT
ATTGAAGATGATGATGAGGCCGTTGTGGAAGTTAACATTCCTGGAAGTGAAAGCAGCGAA
GCCATTGTCCGTAAAAGGACAGCGGGCATTCTCGACATGGGCGGCGTGTCGACTCAGATA
GCGTACGAAGTCCCCAAAACTGAAGAAGTAGCTAAAAACTTGTTAGCTGAATTTAACTTG
GGATGTGATGTTCACCAAACTGAGCATGTGTATCGAGTCTATGTGGCCACGTTTCTTGGG
TTTGGTGGCAATGCTGCTCGACAGAGATACGAAGACAGAATATTTGCCAACACCATTCAA
AAGAACAGGCTCCTGGGTAAACAGACTGGTCTGACTCCTGATATGCCGTACTTGGACCCC
TGCCTACCCCTAGACATTAAAGATGAAATCCAGCAAAATGGACAAACCATATACCTACGA
GGGACTGGAGACTTTGACCTGTGTCGAGAGACTATCCAGCCTTTCATGAATAAAACAAAC
GAGACCCAGACTTCCCTCAATGGGGTCTACCAGCCCCCAATTCACTTCCAGAACAGTGAA
TTCTATGGCTTCTCCGAATTCTACTACTGCACCGAGGATGTGTTACGAATGGGGGGAGAC
TACAATGCTGCTAAATTTACTAAAGCTGCAAAGGATTACTGTGCAACAAAGTGGTCCATT
TTGCGGGAACGCTTTGACCGAGGACTGTACGCCTCTCATGCTGACCTCCACAGGCTTAAG
TATCAGTGCTTCAAATCGGCCTGGATGTTTGAGGTGTTTCATAGGGGCTTTTCGTTTCCT
GTCAACTATAAAAGCTTAAAGACTGCCTTGCAAGTTTACGACAAGGAGGTTCAGTGGACC
CTTGGAGCCATCCTCTACAGGACCCGCTTTCTACCATTAAGAGACATCCAGCAGGAGGCC
TTCCGAGCCAGTCACACCCACTGGCGGGGCGTTTCCTTTGTCTACAACCACTACCTGTTC
TCTGGCTGCTTCCTGGTGGTGCTGCTGGCCATCCTGCTGTACCTGCTGCGGCTGCGGCGC
ATCCACAGGCGCACTCCCCGGAGCAGCTCGGCCGCCGCCCTCTGGATGGAGGAGGGCCTT
CCCGCCCAGAATGCCCCAGGGACCTTGTGA
Enzyme 35 GenBank Gene ID AF016032 Link Image
Enzyme 35 GeneCard ID ENTPD4 Link Image
Enzyme 35 GenAtlas ID ENTPD4 Link Image
Enzyme 35 HGNC ID HGNC:14573 Link Image
Enzyme 35 Chromosome Location 8
Enzyme 35 Locus 8p21.3
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Wang TF, Guidotti G: Golgi localization and functional expression of human uridine diphosphatase. J Biol Chem. 1998 May 1;273(18):11392-9. [PubMed Link Image]
  2. Biederbick A, Rose S, Elsasser HP: A human intracellular apyrase-like protein, LALP70, localizes to lysosomal/autophagic vacuoles. J Cell Sci. 1999 Aug;112 ( Pt 15):2473-84. [PubMed Link Image]
  3. Biederbick A, Kosan C, Kunz J, Elsasser HP: First apyrase splice variants have different enzymatic properties. J Biol Chem. 2000 Jun 23;275(25):19018-24. [PubMed Link Image]
  4. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 6162
Enzyme 36 Name Adenylosuccinate synthetase isozyme 2
Enzyme 36 Synonyms
  1. Adenylosuccinate synthetase, acidic isozyme
  2. IMP--aspartate ligase 2
  3. AdSS 2
  4. AMPSase 2
Enzyme 36 Gene Name ADSS
Enzyme 36 Protein Sequence >Adenylosuccinate synthetase isozyme 2 
MAFAETYPAASSLPNGDCGRPRARPGGNRVTVVLGAQWGDEGKGKVVDLLAQDADIVCRC
QGGNNAGHTVVVDSVEYDFHLLPSGIINPNVTAFIGNGVVIHLPGLFEEAEKNVQKGKGL
EGWEKRLIISDRAHIVFDFHQAADGIQEQQRQEQAGKNLGTTKKGIGPVYSSKAARSGLR
MCDLVSDFDGFSERFKVLANQYKSIYPTLEIDIEGELQKLKGYMEKIKPMVRDGVYFLYE
ALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGMPPQNVGEVYGVVKAY
TTRVGIGAFPTEQDNEIGELLQTRGREFGVTTGRKRRCGWLDLVLLKYAHMINGFTALAL
TKLDILDMFTEIKVGVAYKLDGEIIPHIPANQEVLNKVEVQYKTLPGWNTDISNARAFKE
LPVNAQNYVRFIEDELQIPVKWIGVGKSRESMIQLF
Enzyme 36 Number of Residues 456
Enzyme 36 Molecular Weight 50098
Enzyme 36 Theoretical pI 6.52
Enzyme 36 GO Classification
Function
  • GTP binding
  • adenylosuccinate synthase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleotide binding
  • purine nucleotide binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
Component
—
Enzyme 36 General Function Nucleotide transport and metabolism
Enzyme 36 Specific Function Plays an important role in the de novo pathway of purine nucleotide biosynthesis
Enzyme 36 Pathways
Enzyme 36 Reactions
  • GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 415849 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID P30520 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name PURA2_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >1368 bp 
ATGGCGTTCGCCGAGACCTACCCGGCGGCATCCTCCCTGCCCAACGGCGATTGCGGCCGC
CCCAGGGCGGCCGGAGGAAACCGGGTGACGGTGGTGCTCGGTGCGCAGTGGGGCGACGAA
GGCAAAGGGAAGGTGGTGGACCTGCTGGCGCAGGACGCCGACATCGTGTGCCGCTGCCAG
GGAGGAAATAATGCTGGCCATACAGTTGTTGTGGATTCTGTGGAATATGATTTTCATCTC
TTACCCAGTGGAATAATTAATCCAAATGTCACTGCATTCATTGGAAATGGTGTGGTAATT
CATCTACCTGGATTGTTTGAAGAAGCAGAGAAAAATGTTCAAAAAGGAAAAGGACTAGAA
GGCTGGGAAAAAAGGCTTATTATATCTGACAGAGCTCATATTGTATTTGATTTTCATCAA
GCAGCTGATGGTATCCAGGAACAACAGAGACAAGAACAAGCAGGAAAAAATTTGGGTACA
ACAAAAAAGGGCATTGGCCCAGTTTATTCGTCCAAAGCTGCTCGGAGTGGACTCAGGATG
TGCGACCTTGTTTCTGACTTTGATGGCTTCTCTGAGAGGTTTAAAGTTCTAGCTAACCAA
TACAAATCTATATACCCCACTTTGGAAATAGACATTGAAGGTGAATTACAAAAACTCAAG
GGTTATATGGAAAAGATTAAACCAATGGTGAGAGATGGAGTTTATTTTCTATATGAGGCC
CTACATGGACCACCAAAGAAAATCTTGGTAGAAGGTGCAAATGCAGCACTATTAGATATT
GATTTTGGGACTTACCCTTTTGTAACCTCTTCAAATTGTACTGTTGGAGGTGTTTGTACT
GGTTTGGGTATGCCACCTCAAAATGTTGGAGAAGTGTATGGAGTTGTGAAAGCTTATACA
ACTAGAGTTGGTATTGGTGCCTTTCCTACAGAGCAAGACAATGAAATTGGAGAATTATTA
CAAACAAGGGGTAGAGAGTTTGGTGTAACTACTGGAAGGAAAAGAAGATGTGGCTGGTTG
GACCTCGTTTTGCTCAAATATGCTCATATGATCAATGGATTTACTGCGTTGGCACTTACC
AAGTTGGATATTTTGGACATGTTTACGGAAATCAAAGTTGGAGTTGCTTACAAGTTAGAT
GGTGAAATCATACCTCATATCCCAGCAAACCAAGAAGTCTTAAATAAAGTTGAAGTTCAA
TATAAGACTCTCCCAGGATGGAACACAGACATATCAAATGCAAGGGCGTTTAAAGAACTA
CCTGTTAATGCACAAAACTATGTTCGATTTATTGAAGATGAGCTTCAAATTCCAGTTAAG
TGGATTGGTGTTGGTAAATCCAGAGAATCTATGATTCAACTCTTTTAA
Enzyme 36 GenBank Gene ID X66503 Link Image
Enzyme 36 GeneCard ID ADSS Link Image
Enzyme 36 GenAtlas ID ADSS Link Image
Enzyme 36 HGNC ID HGNC:292 Link Image
Enzyme 36 Chromosome Location 1
Enzyme 36 Locus 1cen-q12
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Powell SM, Zalkin H, Dixon JE: Cloning and characterization of the cDNA encoding human adenylosuccinate synthetase. FEBS Lett. 1992 May 25;303(1):4-10. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 6166
Enzyme 37 Name Adenylosuccinate synthetase isozyme 1
Enzyme 37 Synonyms
  1. IMP--aspartate ligase 1
  2. AdSS 1
  3. AMPSase 1
Enzyme 37 Gene Name ADSSL1
Enzyme 37 Protein Sequence >Adenylosuccinate synthetase isozyme 1 
MSGTRASNDRPPGAGGVKRGRLQQEAAATGSRVTVVLGAQWGDEGKGKVVDLLATDADII
SRCQGGNNAGHTVVVDGKEYDFHLLPSGIINTKAVSFIGNGVVIHLPGLFEEAEKNEKKG
LKDWEKRLIISDRAHLVFDFHQAVDGLQEVQRQAQEGKNIGTTKKGIGPTYSSKAARTGL
RICDLLSDFDEFSSRFKNLAHQHQSMFPTLEIDIEGQLKRLKGFAERIRPMVRDGVYFMY
EALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDVYGVVKA
YTTRVGIGAFPTEQINEIGGLLQTRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALA
LTKLDILDVLGEVKVGVSYKLNGKRIPYFPANQEMLQKVEVEYETLPGWKADTTGARRWE
DLPPQAQNYIRFVENHVGVAVKWVGVGKSRESMIQLF
Enzyme 37 Number of Residues 457
Enzyme 37 Molecular Weight 50209
Enzyme 37 Theoretical pI 8.85
Enzyme 37 GO Classification
Function
  • GTP binding
  • adenylosuccinate synthase activity
  • binding
  • catalytic activity
  • guanyl nucleotide binding
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleotide binding
  • purine nucleotide binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
Component
—
Enzyme 37 General Function Nucleotide transport and metabolism
Enzyme 37 Specific Function Plays an important role in the de novo pathway of purine nucleotide biosynthesis
Enzyme 37 Pathways
Enzyme 37 Reactions
  • GTP + IMP + L-aspartate = GDP + phosphate + N6-(1,2-dicarboxyethyl)-AMP
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • None
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 21303413 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q8N142 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name PURA1_HUMAN Link Image
Enzyme 37 PDB ID 1MF1 Link Image
Enzyme 37 PDB File Show
Enzyme 37 3D Structure
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >1374 bp 
ATGTCGGGGACCCGAGCCTCCAACGACCGGCCCCCCGGCGCAGGCGGCGTCAAGCGGGGG
CGGCTGCAGCAGGAGGCGGCGGCGACCGGCTCCCGCGTGACGGTGGTGCTGGGCGCGCAG
TGGGGGGACGAGGGCAAAGGCAAGGTGGTGGACCTGCTGGCCACGGACGCCGACATCATC
AGCCGCTGCCAGGGGGGCAACAACGCCGGCCACACGGTGGTGGTGGATGGGAAAGAGTAC
GACTTCCACCTGCTGCCCAGCGGCATCATCAACACCAAGGCCGTGTCCTTCATTGGCAAC
GGGGTGGTCATCCACTTGCCAGGCTTGTTTGAGGAAGCAGAGAAGAATGAAAAGAAAGGC
CTGAAGGACTGGGAGAAGAGGCTCATCATCTCTGACAGAGCCCACCTTGTGTTTGATTTT
CACCAGGCTGTCGACGGACTTCAGGAAGTGCAGCGCCAGGCACAAGAGGGGAAGAATATA
GGCACCACCAAGAAGGGAATCGGACCAACCTACTCTTCCAAAGCTGCCCGGACAGGCCTC
CGCATCTGCGACCTCCTGTCAGATTTTGATGAGTTTTCCTCCAGATTCAAGAACCTGGCC
CACCAGCACCAGTCGATGTTCCCCACCCTGGAAATAGACATTGAAGGCCAACTCAAAAGG
CTCAAGGGCTTTGCTGAGCGGATCAGACCCATGGTCCGAGATGGTGTTTACTTTATGTAT
GAGGCACTCCACGGCCCCCCCAAGAAGATCCTGGTGGAGGGTGCCAACGCCGCCCTCCTC
GACATTGACTTCGGGACCTACCCCTTTGTGACTTCATCCAACTGCACCGTGGGCGGTGTG
TGCACGGGCCTGGGCATCCCCCCGCAGAACATAGGTGACGTGTATGGCGTGGTGAAAGCC
TATACCACACGTGTGGGCATCGGGGCCTTCCCCACCGAGCAGATCAACGAGATTGGAGGC
CTGCTGCAGACCCGCGGCCACGAGTGGGGAGTGACCACAGGCAGGAAGAGGCGCTGCGGC
TGGCTCGACCTGATGATTCTAAGATATGCTCACATGGTCAACGGATTCACTGCGCTGGCC
CTGACGAAGCTGGACATCCTGGACGTACTGGGTGAGGTTAAAGTCGGTGTCTCATACAAG
CTGAACGGGAAAAGGATTCCCTATTTCCCAGCTAACCAGGAGATGCTTCAGAAGGTCGAA
GTTGAGTATGAAACGCTGCCTGGGTGGAAAGCAGACACCACAGGCGCCAGGAGGTGGGAG
GACCTGCCCCCACAGGCCCAGAACTACATCCGCTTTGTGGAGAATCACGTGGGAGTCGCA
GTCAAATGGGTTGGTGTTGGCAAGTCAAGAGAGTCGATGATCCAGCTGTTTTAG
Enzyme 37 GenBank Gene ID AY037159 Link Image
Enzyme 37 GeneCard ID ADSSL1 Link Image
Enzyme 37 GenAtlas ID ADSSL1 Link Image
Enzyme 37 HGNC ID HGNC:20093 Link Image
Enzyme 37 Chromosome Location 14
Enzyme 37 Locus 14q32.33
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References Not Available
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 6171
Enzyme 38 Name Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial precursor
Enzyme 38 Synonyms
  1. Succinyl-CoA synthetase subunit alpha
  2. SCS- alpha
Enzyme 38 Gene Name SUCLG1
Enzyme 38 Protein Sequence >Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial precursor 
MVSGSSGLAAARLLSRSFLLPQNGIRHCSYTASRQHLYVDKNTKIICQGFTGKQGTFHSQ
QALEYGTKLVGGTTPGKGGQTHLGLPVFNTVKEAKEQTGATASVIYVPPPFAAAAINEAI
EAEIPLVVCITEGIPQQDMVRVKHKLLRQEKTRLIGPNCPGVINPGECKIGIMPGHIHKK
GRIGIVSRSGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFIDCLEIFLNDSATEGII
LIGEIGGNAEENAAEFLKQHNSGPNSKPVVSFIAGLTAPPGRRMGHAGAIIAGGKGGAKE
KISALQSAGVVVSMSPAQLGTTIYKEFEKRKML
Enzyme 38 Number of Residues 333
Enzyme 38 Molecular Weight 35048
Enzyme 38 Theoretical pI 9.24
Enzyme 38 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 38 General Function Energy production and conversion
Enzyme 38 Specific Function GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
Enzyme 38 Pathways
Enzyme 38 Reactions
  • GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • 1-19
Enzyme 38 Transmembrane Regions Not Available
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 9409794 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID P53597 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name SUCA_HUMAN Link Image
Enzyme 38 PDB ID 1EUC Link Image
Enzyme 38 PDB File Show
Enzyme 38 3D Structure
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >1002 bp 
ATGGTCTCCGGCAGCAGCGGCCTCGCCGCCGCCCGTCTCCTGTCGCGCAGCTTCCTCCTG
CCGCAGAATGGAATTCGGCATTGTTCCTACACAGCTTCTCGGCAACATCTCTATGTTGAT
AAAAATACAAAGATTATTTGCCAGGGTTTCACTGGCAAACAGGGCACCTTTCACAGCCAG
CAGGCATTGGAATATGGCACCAAACTCGTTGGAGGAACACTCCCAGGGAAAGGAGGCCAG
ACACATCTGGGCTTACCTGTCTTTAATACTGTGAAGGAGGCCAAAGAACAGACAGGAGCA
ACGGCTTCTGTCATTTATGTTCCTCCGCCTTTTGCTGCTGCTGCCATTAATGAAGCTATT
GAGGCAGAAATTCCCTTGGTTGTGTGTATCACTGAAGGAATTCCCCAGCAGGACATGGTA
CGAGTCAAGCACAAACTGCTGCGCCAGGAAAAGACAAGGCTAATTGGGCCCAACTGCCCT
GGAGTCATCAATCCTGGAGAATGTAAAATTGGGATCATGCCTGGCCATATTCACAAAAAA
GGAAGGATTGGCATTGTGTCCAGATCTGGCACCCTGACTTATGAAGCAGTTCACCAAACA
ACGCAAGTTGGATTGGGGCAGTCTTTGTGCGTTGGCATTGGAGGTGATCCTTTTAATGGA
ACAGATTTTATTGACTGCCTCGAAATCTTTTTGAACGATTCTGCCACAGAAGGCATCATA
TTGATTGGTGAAATTGGTGGTAATGCAGAAGAGAATGCTGCAGAATTTTTGAAGCAACAT
AATTCAGGTCCAAATTCCAAGCCTGTAGTGTCCTTCATTGCTGGTTTAACTGCTCCTCCT
GGGAGAAGAATGGGTCATGCCGGGGCAATTATTGCTGGAGGAAAAGGTGGAGCTAAAGAG
AAGATCTCTGCCCTTCAGAGTGCAGGAGTTGTGGTCAGTATGTCTCCTGCACAGCTGGGA
ACCACGATCTACAAGGAATTTGAAAAGAGGAAGATGCTATGA
Enzyme 38 GenBank Gene ID AF104921 Link Image
Enzyme 38 GeneCard ID SUCLG1 Link Image
Enzyme 38 GenAtlas ID SUCLG1 Link Image
Enzyme 38 HGNC ID HGNC:11449 Link Image
Enzyme 38 Chromosome Location 2
Enzyme 38 Locus 2p11.2
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. James M, Man NT, Edwards YH, Morris GE: The molecular basis for cross-reaction of an anti-dystrophin antibody with alpha-actinin. Biochim Biophys Acta. 1997 Apr 12;1360(2):169-76. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 6172
Enzyme 39 Name Phosphoenolpyruvate carboxykinase [GTP], mitochondrial precursor
Enzyme 39 Synonyms
  1. Phosphoenolpyruvate carboxylase
  2. PEPCK-M
Enzyme 39 Gene Name PCK2
Enzyme 39 Protein Sequence >Phosphoenolpyruvate carboxykinase [GTP], mitochondrial precursor 
MAALYRPGLRLNWHGLSPLGWPSCRSIQTLRVLSGDLGQLPTGIRDFVEHSARLCQPEGI
HICDGTEAENTATLTLLEQQGLIRKLPKYNNCWLARTDPKDVARVESKTVIVTPSQRDTV
PLPPGGARGQLGNWMSPADFQRAVDERFPGCMQGRTMYVLPFSMGPVGSPLSRIGVQLTD
SAYVVASMRIMTRLGTPVLQALGDGDFVKCLHSVGQPLTGQGEPVSQWPCNPEKTLIGHV
PDQREIISFGSGYGGNSLLGKKCFALRIASRLARDEGWLAEHMLILGITSPAGKKALCAA
AFPSACGKTNLAMMRPALPGWKVECVGDDIAWMRFDSEGRLRAINPENGFFGVAPGTSAT
TNPNAMATIQSNTIFTNVAETSDGGVYWEGIDQPLPPGVTVTSWLGKPWKPGDKEPCAHP
NSRFCAPARQCPIMDPAWEAPEGVPIDAIIFGGRRPKGVPLVYEAFNWRHGVFVGRAMRS
ESTAAAEHKGKIIMHDPFAMRPFFGYNFGHYLEHWLSMEGRKGAQLPRIFHVNWFRRDEA
GHFLWPGFGENARVLDWICRRLEGEDSARETPIGLVPKEGALDLSGLRAIDTTQLFSLPK
DFWEQEVRDIRSYLTEQVNQDLPKEVLAELEALERRVHKM
Enzyme 39 Number of Residues 640
Enzyme 39 Molecular Weight 70638
Enzyme 39 Theoretical pI 7.65
Enzyme 39 GO Classification
Function
  • GTP binding
  • binding
  • carbon-carbon lyase activity
  • carboxy-lyase activity
  • catalytic activity
  • guanyl nucleotide binding
  • lyase activity
  • nucleotide binding
  • phosphoenolpyruvate carboxykinase activity
  • purine nucleotide binding
Process
  • alcohol metabolism
  • cellular metabolism
  • gluconeogenesis
  • glucose metabolism
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 39 General Function Energy production and conversion
Enzyme 39 Specific Function GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO(2)
Enzyme 39 Pathways
Enzyme 39 Reactions
  • GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 1403050 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID Q16822 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name PPCKM_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >1923 bp 
ATGGCCGCATTGTACCGCCCTGGCCTGCGGCTTAACTGGCATGGGCTGAGCCCCTTGGGC
TGGCCATCATGCCGTAGCATCCAGACCCTGCGAGTGCTTAGTGGAGATCTGGGCCAGCTT
CCCACTGGCATTCGAGATTTTGTAGAGCACAGTGCCCGCCTGTGCCAACCAGAGGGCATC
CACATCTGTGATGGAACTGAGGCTGAGAATACTGCCACACTGACCCTGCTGGAGCAGCAG
GGCCTCATCCGAAAGCTCCCCAAGTACAATAACTGCTGGCTGGCCCGCACAGACCCCAAG
GATGTGGCACGAGTAGAGAGCAAGACGGTGATTGTAACTCCTTCTCAGCGGGACACGGTA
CCACTCCCGCCTGGTGGGGCCTGTGGGCAGCTGGGCAACTGGATGTCCCCAGCTGATTTC
CAGCGAGCTGTGGATGAGAGGTTTCCAGGCTGCATGCAGGGCCGCACCATGTATGTGCTT
CCATTCAGCATGGGTCCTGTGGGCTCCCCGCTGTCCCGCATCGGGGTGCAGCTCACTGAC
TCAGCCTATGTGGTGGCAAGCATGCGTATTATGACCCGACTGGGGACACCTGTGCTTCAG
GCCCTGGGAGATGGTGACTTTGTCAAGTGTCTGCACTCCGTGGGCCAGCCCCTGACAGGA
CAAGGGGAGCCAGTGAGCCAGTGGCCGTGCAACCCAGAGAAAACCCTGATTGGCCACGTG
CCCGACCAGCGGGAGATCATCTCCTTCGGCAGCGGCTATGGTGGCAACTCCCTGCTGGGC
AAGAAGTGCTTTGCCCTACGCATCGCCTCTCGGCTGGCCCGGGATGAGGGCTGGCTGGCA
GAGCACATGCTGATCCTGGGCATCACCAGCCCTGCAGGGAAGAAGGCGCTATGTGCAGCC
GCCTTCCCTAGTGCCTGTGGCAAGACCAACCTGGCTATGATGCGGCCTGCACTGCCAGGC
TGGAAAGTGGAGTGTGTGGGGGATGATATTGCTTGGATGAGGTTTGACAGTGAAGGTCGA
CTCCGGGCCATCAACCCTGAGAACGGCTTCTTTGGGGTTGCCCCTGGTACCTCTGCCACC
ACCAATCCCAACGCCATGGCTACAATCCAGAGTAACACTATTTTTACCAATGTGGCTGAG
ACCAGTGATGGTGGCGTGTACTGGGAGGGCATTGACCAGCCTCTTCCACCTGGTGTTACT
GTGACCTCCTGGCTGGGCAAACCCTGGAAACCTGGTGACAAGGAGCCCTGTGCACATCCC
AACTCTCGATTTTGTGCCCCGGCTCGCCAGTGCCCCATCATGGACCCAGCCTGGGAGGCC
CCAGAGGGTGTCCCCATTGACGCCATCATCTTTGGTGGCCGCAGACCCAAAGGGGTACCC
CTGGTATACGAGGCCTTCAACTGGCGTCATGGGGTGTTTGTGGGCAGAGCCATGCGCTCT
GAGTCCACTGCTGCAGCAGAACACAAAGGGAAGATCATCATGCACGACCCATTTGCCATG
CGGCCCTTTTTTGGCTACAACTTCGGGCACTACCTGGAACACTGGCTGAGCATGGAAGGG
CGCAAGGGGGCCCAGCTGCCCCGTATCTTCCATGTCAACTGGTTCCGGCGTGACGAGGCA
GGGCACTTCCTGTGGCCAGGCTTTGGGGAGAATGCTCGGGTGCTAGACTGGATCTGCCGG
CGGTTAGAGGGGGAGGACAGTGCCCGAGAGACACCCATTGGGCTGGTGCCAAAGGAAGGA
GCCTTGGATCTCAGCGGCCTCAGAGCTATAGACACCACTCAGCTGTTCTCCCTCCCCAAG
GACTTCTGGGAACAGGAGGTTCGTGACATTCGGAGCTACCTGACAGAGCAGGTCAACCAG
GATCTGCCCAAAGAGGTGTTGGCTGAGCTTGAGGCCCTGGAGAGACGTGTGCACAAAATG
TGA
Enzyme 39 GenBank Gene ID X92720 Link Image
Enzyme 39 GeneCard ID PCK2 Link Image
Enzyme 39 GenAtlas ID PCK2 Link Image
Enzyme 39 HGNC ID HGNC:8725 Link Image
Enzyme 39 Chromosome Location 14
Enzyme 39 Locus 14q12
Enzyme 39 SNPs SNPJam Repo