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Human Metabolome Database Version 2.5

 

Showing metabocard for Calcium (HMDB00464)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-15 18:25:35
Update Date 2011-06-21 09:35:19
Accession Number HMDB00464
Secondary Accession Numbers Not Available
Common Name Calcium
Description Calcium is essential for the normal growth and maintenance of bones and teeth, and calcium requirements must be met throughout life. Requirements are greatest during periods of growth, such as childhood, during pregnancy and when breast-feeding. Long-term calcium deficiency can lead to osteoporosis, in which the bone deteriorates and there is an increased risk of fractures. Adults need between 1,000 and 1,300 mg of calcium in their daily diet. Calcium is essential for living organisms, particularly in cell physiology, and is the most common metal in many animals. Physiologically, it exists as an ion in the body. Calcium combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes. Calcium is an important component of a healthy diet. A deficit can affect bone and tooth formation, while overretention can cause kidney stones. Vitamin D is needed to absorb calcium. Dairy products, such as milk and cheese, are a well-known source of calcium. However, some individuals are allergic to dairy products and even more people, particularly those of non-European descent, are lactose-intolerant, leaving them unable to consume dairy products. Fortunately, many other good sources of calcium exist. These include: seaweeds such as kelp, wakame and hijiki; nuts and seeds (like almonds and sesame); beans; amaranth; collard greens; okra; rutabaga; broccoli; kale; and fortified products such as orange juice and soy milk. Calcium has also been found to assist in the production of lymphatic fluids.
Synonyms
  1. Ca
  2. Calcium element
Chemical IUPAC Name calcium
Chemical Formula [Ca]2+
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Inorganic
Super Class
  • Inorganic compounds
Class
  • Inorganic Ions and Gases
Sub Class
  • Metals
Family
  • Mammalian Metabolite
Species
—
Biofunction
  • Essential minerals
  • Second messenger
Application
—
Source
  • Exogenous
Average Molecular Weight 40.078
Monoisotopic Molecular Weight 39.962589
Isomeric SMILES [Ca++]
Canonical SMILES [Ca++]
KEGG Compound ID C00076 Link Image
BioCyc ID CA%2b2 Link Image
BiGG ID 33764 Link Image
Wikipedia Link Calcium Link Image
NuGOwiki Link HMDB00464 Link Image
Metagene Link HMDB00464 Link Image
METLIN ID Not Available
PubChem Compound 5460341 Link Image
PubChem Substance 8024986 Link Image
ChEBI ID 29320 Link Image
CAS Registry Number 7440-70-2
InChI Identifier InChI=1/Ca/q+2
Synthesis Reference Not Available
Melting Point (Experimental) 850 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 399 mg/mL at 25 oC [MEYLAN,WM et al. (1996)] Calculated using ALOGPS
Physiological Charge 2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.57 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Not Available
Not Available
Predicted 13C NMR Spectrum Not Available
Not Available
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • Extracellular
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location Not Available
Concentrations (Normal)
Biofluid Blood
Value 2220.0 +/- 190.0 uM
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 81-83. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 2510.0 +/- 90.0 uM
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 81-83. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 2430.0 +/- 70.0 uM
Age Adolescent:13-18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 82-85. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 2420.0 (2250.0-2590.0) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 82-85. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Blood
Value 2377.0 +/- 100.0 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Dominguez LJ, Barbagallo M, Lauretani F, Bandinelli S, Bos A, Corsi AM, Simonsick EM, Ferrucci L: Magnesium and muscle performance in older persons: the InCHIANTI study. Am J Clin Nutr. 2006 Aug;84(2):419-26. [PubMed Link Image]
Biofluid Blood
Value 2352.0 +/- 100.0 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Dominguez LJ, Barbagallo M, Lauretani F, Bandinelli S, Bos A, Corsi AM, Simonsick EM, Ferrucci L: Magnesium and muscle performance in older persons: the InCHIANTI study. Am J Clin Nutr. 2006 Aug;84(2):419-26. [PubMed Link Image]
Biofluid Blood
Value 1536 +/- 141 uM
Age Elderly:>65 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Bocca B, Forte G, Petrucci F, Pino A, Marchione F, Bomboi G, Senofonte O, Giubilei F, Alimonti A: Monitoring of chemical elements and oxidative damage in patients affected by Alzheimer's disease. Ann Ist Super Sanita. 2005;41(2):197-203. [PubMed Link Image]
Biofluid CSF
Value 1190.0 (1020.0 - 1340.0) 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 1047 +/- 520 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Mandal, R. et al. (in preparation)
Biofluid Urine
Value 391.0 +/- 125.0 umol/mmol creatinine
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 Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 299.0 +/- 99.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by Cornelius Lentner.
  • West Cadwell, N.J. : Medical education Div., Ciba-Geigy Corp.
  • Basel, Switzerland c1981-1992.
Biofluid Urine
Value 256.5 +/- 13.00 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Cappuccio FP, Rink E, Perkins-Porras L, McKay C, Hilton S, Steptoe A: Estimation of fruit and vegetable intake using a two-item dietary questionnaire: a potential tool for primary health care workers. Nutr Metab Cardiovasc Dis. 2003 Feb;13(1):12-9. [PubMed Link Image]
Biofluid Urine
Value 276.00 +/- 19.7 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Cappuccio FP, Rink E, Perkins-Porras L, McKay C, Hilton S, Steptoe A: Estimation of fruit and vegetable intake using a two-item dietary questionnaire: a potential tool for primary health care workers. Nutr Metab Cardiovasc Dis. 2003 Feb;13(1):12-9. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 1714 +/- 132 uM
Age Elderly:>65 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • Bocca B, Forte G, Petrucci F, Pino A, Marchione F, Bomboi G, Senofonte O, Giubilei F, Alimonti A: Monitoring of chemical elements and oxidative damage in patients affected by Alzheimer's disease. Ann Ist Super Sanita. 2005;41(2):197-203. [PubMed Link Image]
Biofluid Blood
Value 1637 +/- 282 uM
Age Adult:>18 yrs old
Sex Both
Condition Multiple sclerosis
Comments Not Available
References
  • Forte G, Visconti A, Santucci S, Ghazaryan A, Figa-Talamanca L, Cannoni S, Bocca B, Pino A, Violante N, Alimonti A, Salvetti M, Ristori G: Quantification of chemical elements in blood of patients affected by multiple sclerosis. Ann Ist Super Sanita. 2005;41(2):213-6. [PubMed Link Image]
Biofluid Blood
Value 1683 +/- 249 uM
Age Adult:>18 yrs old
Sex Both
Condition Parkinson's disease
Comments Not Available
References
  • Forte G, Alimonti A, Pino A, Stanzione P, Brescianini S, Brusa L, Sancesario G, Violante N, Bocca B: Metals and oxidative stress in patients with Parkinson's disease. Ann Ist Super Sanita. 2005;41(2):189-95. [PubMed Link Image]
Biofluid Blood
Value 1400.00 (1200.00-1600.00) uM
Age Adult:>18 yrs old
Sex Both
Condition Primary hypomagnesemia
Comments Not Available
References
Biofluid Blood
Value 2300.00 (2100.00-2650.00) uM
Age Adult:>18 yrs old
Sex Both
Condition Primary hypomagnesemia
Comments Not Available
References
Associated Disorders
Condition References
Alzheimer's disease
  • Bocca B, Forte G, Petrucci F, Pino A, Marchione F, Bomboi G, Senofonte O, Giubilei F, Alimonti A: Monitoring of chemical elements and oxidative damage in patients affected by Alzheimer's disease. Ann Ist Super Sanita. 2005;41(2):197-203. [PubMed Link Image]
Multiple sclerosis
  • Forte G, Visconti A, Santucci S, Ghazaryan A, Figa-Talamanca L, Cannoni S, Bocca B, Pino A, Violante N, Alimonti A, Salvetti M, Ristori G: Quantification of chemical elements in blood of patients affected by multiple sclerosis. Ann Ist Super Sanita. 2005;41(2):213-6. [PubMed Link Image]
Parkinson's disease
  • Forte G, Alimonti A, Pino A, Stanzione P, Brescianini S, Brusa L, Sancesario G, Violante N, Bocca B: Metals and oxidative stress in patients with Parkinson's disease. Ann Ist Super Sanita. 2005;41(2):189-95. [PubMed Link Image]
Primary hypomagnesemia
OMIM ID
Pathways Not Available
General References
  1. Boonen S, Vanderschueren D, Haentjens P, Lips P: Calcium and vitamin D in the prevention and treatment of osteoporosis - a clinical update. J Intern Med. 2006 Jun;259(6):539-52. [PubMed Link Image]
  2. Gennari C: Calcium and vitamin D nutrition and bone disease of the elderly. Public Health Nutr. 2001 Apr;4(2B):547-59. [PubMed Link Image]
  3. Kirchhoff P, Geibel JP: Role of calcium and other trace elements in the gastrointestinal physiology. World J Gastroenterol. 2006 May 28;12(20):3229-36. [PubMed Link Image]
  4. Gross MD: Vitamin D and calcium in the prevention of prostate and colon cancer: new approaches for the identification of needs. J Nutr. 2005 Feb;135(2):326-31. [PubMed Link Image]
  5. Wikipedia Link Image
Metabolic Enzymes
  1. Group XV phospholipase A2
  2. Calcium-dependent phospholipase A2
  3. Group IIF secretory phospholipase A2
  4. Cytosolic phospholipase A2
  5. Phospholipase A2
  6. Group XIIB secretory phospholipase A2-like protein
  7. Group 10 secretory phospholipase A2
  8. Group IIE secretory phospholipase A2
  9. Group XIIA secretory phospholipase A2
  10. 85 kDa calcium-independent phospholipase A2
  11. Phospholipase A2, membrane associated
  12. Group IID secretory phospholipase A2
  13. Ectonucleoside triphosphate diphosphohydrolase 1
  14. Soluble calcium-activated nucleotidase 1
  15. Ectonucleoside triphosphate diphosphohydrolase 3
  16. Glycerol-3-phosphate dehydrogenase, mitochondrial
  17. Glucosamine-6-phosphate isomerase 1
  18. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1
  19. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4
  20. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2
  21. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3
  22. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2
  23. Diacylglycerol kinase alpha
  24. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1
  25. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1
  26. Thyroid peroxidase
  27. Lactoperoxidase
  28. Myeloperoxidase
  29. Eosinophil peroxidase
  30. Arylsulfatase D
  31. Arylsulfatase B
  32. Arylsulfatase E
  33. Annexin A3
  34. Type I inositol-1,4,5-trisphosphate 5-phosphatase
  35. Amiloride-sensitive amine oxidase [copper-containing]
  36. Glyoxylate reductase/hydroxypyruvate reductase
  37. Membrane primary amine oxidase
  38. Retina-specific copper amine oxidase
  39. Deoxyribonuclease-1
  40. Steryl-sulfatase
  41. Cytosolic phospholipase A2 gamma
  42. Group 3 secretory phospholipase A2
  43. Platelet-activating factor acetylhydrolase IB subunit alpha
  44. Bis(5'-adenosyl)-triphosphatase
  45. Protein-glutamine gamma-glutamyltransferase E
  46. Protein-glutamine gamma-glutamyltransferase 2
  47. Protein-arginine deiminase type-6
  48. Coagulation factor XIII A chain
  49. Protein-arginine deiminase type-4
  50. Protein-arginine deiminase type-3
  51. Protein-glutamine gamma-glutamyltransferase 5
  52. Protein-glutamine gamma-glutamyltransferase 4
  53. Protein-glutamine gamma-glutamyltransferase K
  54. Protein-arginine deiminase type-2
  55. Protein-arginine deiminase type-1
  56. Protein-glutamine gamma-glutamyltransferase 6
  57. Protein-glutamine gamma-glutamyltransferase Z
  58. Adenylate cyclase type 7
  59. Adenylate cyclase type 4
  60. Adenylate cyclase type 6
  61. Adenylate cyclase type 5
  62. Adenylate cyclase type 8
  63. Adenylate cyclase type 9
  64. Adenylate cyclase type 3
  65. Adenylate cyclase type 1
  66. Fumarylacetoacetase
  67. Serine--pyruvate aminotransferase
  68. Transketolase-like protein 1
  69. Transketolase
  70. Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
  71. Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
  72. Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
  73. Ectonucleoside triphosphate diphosphohydrolase 4
  74. Ectonucleoside triphosphate diphosphohydrolase 6
  75. Ectonucleoside triphosphate diphosphohydrolase 5
  76. ADP-ribosyl cyclase 2
  77. Adenylate cyclase type 2
  78. Nitric oxide synthase, inducible
  79. Nitric oxide synthase, brain
  80. Nitric oxide synthase, endothelial
  81. Protein O-mannosyl-transferase 1
  82. Protein O-mannosyl-transferase 2
  83. 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase
  84. Arachidonate 5-lipoxygenase
  85. Inositol-trisphosphate 3-kinase B
  86. Inositol-trisphosphate 3-kinase A
  87. Polypeptide N-acetylgalactosaminyltransferase 11
  88. Polypeptide N-acetylgalactosaminyltransferase 4
  89. Polypeptide N-acetylgalactosaminyltransferase 3
  90. Probable polypeptide N-acetylgalactosaminyltransferase 8
  91. Polypeptide N-acetylgalactosaminyltransferase-like protein 2
  92. Putative polypeptide N-acetylgalactosaminyltransferase-like protein 1
  93. Polypeptide N-acetylgalactosaminyltransferase 10
  94. Polypeptide N-acetylgalactosaminyltransferase 13
  95. Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3
  96. Putative polypeptide N-acetylgalactosaminyltransferase-like protein 4
  97. N-acetylgalactosaminyltransferase 7
  98. Polypeptide N-acetylgalactosaminyltransferase 6
  99. Polypeptide N-acetylgalactosaminyltransferase 14
  100. Polypeptide N-acetylgalactosaminyltransferase 2
  101. Polypeptide N-acetylgalactosaminyltransferase 12
  102. Polypeptide N-acetylgalactosaminyltransferase 1
  103. Polypeptide N-acetylgalactosaminyltransferase 5
  104. 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
  105. Retinal guanylyl cyclase 1
  106. Retinal guanylyl cyclase 2
  107. Gamma-enolase
  108. Cyclic nucleotide-gated cation channel alpha-3
  109. Cyclic nucleotide-gated cation channel beta-3
  110. Death-associated protein kinase 2
  111. Plasma membrane calcium-transporting ATPase 3
  112. Protein kinase C alpha type
  113. Serine/threonine-protein kinase 38
  114. MAP kinase-activated protein kinase 5
  115. Plasma membrane calcium-transporting ATPase 1
  116. Myosin light chain kinase 2, skeletal/cardiac muscle
  117. Calcium/calmodulin-dependent protein kinase type 1D
  118. Plasma membrane calcium-transporting ATPase 2
  119. Serine/threonine-protein kinase 38-like
  120. Calcium-transporting ATPase type 2C member 2
  121. Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit beta
  122. Sarcoplasmic/endoplasmic reticulum calcium ATPase 3
  123. Death-associated protein kinase 1
  124. V-type proton ATPase subunit B, kidney isoform
  125. Calcium/calmodulin-dependent protein kinase type 1G
  126. V-type proton ATPase 116 kDa subunit a isoform 4
  127. Calcium/calmodulin-dependent protein kinase kinase 1
  128. Calcium/calmodulin-dependent protein kinase type 1
  129. Tyrosine-protein kinase Fyn
  130. Serine/threonine-protein kinase PLK3
  131. Calcium/calmodulin-dependent protein kinase kinase 2
  132. Plasma membrane calcium-transporting ATPase 4
  133. Serine/threonine-protein kinase DCLK1
  134. Protein kinase C beta type
  135. Protein kinase C zeta type
  136. Calcium/calmodulin-dependent protein kinase type IV
  137. Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
  138. Calcium-transporting ATPase type 2C member 1
  139. Ceramide kinase
  140. Myosin light chain kinase, smooth muscle
  141. Protein-tyrosine kinase 2-beta
  142. Protein kinase C iota type
  143. Tyrosine-protein kinase SYK
  144. Ectonucleoside triphosphate diphosphohydrolase 2
  145. Calcium/calmodulin-dependent protein kinase type II subunit delta
  146. Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
  147. Serine/threonine-protein kinase D1
  148. Protein kinase C gamma type
  149. Transient receptor potential cation channel subfamily M member 7
  150. N-sulphoglucosamine sulphohydrolase
  151. Iduronate 2-sulfatase
  152. N-acetylglucosamine-6-sulfatase
  153. Glutamate [NMDA] receptor subunit zeta-1
  154. Protein lin-7 homolog A
  155. Glutamate [NMDA] receptor subunit 3B
  156. Glutamate [NMDA] receptor subunit epsilon-1
  157. Glutamate [NMDA] receptor subunit epsilon-3
  158. Glutamate [NMDA] receptor subunit epsilon-2
  159. Glutamate [NMDA] receptor subunit epsilon-4
  160. Protein AMBP
  161. Nuclear factor of activated T-cells, cytoplasmic 2
  162. Vitamin K-dependent gamma-carboxylase
  163. UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
  164. Basement membrane-specific heparan sulfate proteoglycan core protein
  165. Vasopressin V1a receptor
  166. Coagulation factor VIII
  167. Coagulation factor IX
  168. Protein NDRG1
  169. Calcium-activated potassium channel subunit alpha-1
  170. Elastin
  171. Collagen alpha-1(I) chain
  172. Collagen alpha-2(I) chain
  173. Beta-1-syntrophin
  174. Tropomyosin alpha-4 chain
  175. Serine/threonine-protein phosphatase PP1-beta catalytic subunit
  176. Calmodulin
  177. Vitamin D3 receptor
  178. 1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial
  179. Calbindin
  180. Glutamate receptor, ionotropic kainate 2
  181. Proprotein convertase subtilisin/kexin type 6
  182. Vasopressin V1b receptor
  183. Activin receptor type-1
  184. Leukotriene B4 receptor 1
  185. Protein kinase C delta type
  186. Serine/threonine-protein kinase D3
  187. Protein kinase C theta type
  188. Protein kinase C eta type
  189. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta-2
  190. Protein kinase C epsilon type
  191. Type II inositol-1,4,5-trisphosphate 5-phosphatase
  192. Nuclear factor of activated T-cells, cytoplasmic 1
  193. Endothelial differentiation-related factor 1
  194. Calmodulin-like protein 3
  195. Protein S100-A8
  196. Laforin
  197. Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
  198. 5'-AMP-activated protein kinase catalytic subunit alpha-1
  199. 5'-AMP-activated protein kinase catalytic subunit alpha-2
  200. Histone H2A type 1-C
  201. Histone H2A type 1-J
  202. Histone H2A type 1-D
  203. Histone H2A type 2-C
  204. Prostaglandin F2-alpha receptor
  205. Oxytocin receptor
  206. Phospholipid scramblase 1
  207. Enhancer of filamentation 1
  208. P-selectin glycoprotein ligand 1
  209. Tenascin-R
  210. Voltage-dependent L-type calcium channel subunit alpha-1D
  211. Transient receptor potential cation channel subfamily M member 2
  212. Vitamin K-dependent protein C
  213. Osteocalcin
  214. Osteocalcin
  215. Coagulation factor X
  216. Growth arrest-specific protein 6
  217. Coagulation factor VII
  218. Thromboxane A2 receptor
  219. Free fatty acid receptor 3
  220. Free fatty acid receptor 2
  221. Free fatty acid receptor 1
  222. Protocadherin-8
  223. Parathyroid hormone
  224. C-reactive protein
  225. Alpha-amylase 1
  226. Pancreatic alpha-amylase
  227. Annexin A5
  228. SPARC
  229. Coagulation factor V
  230. Parathyroid hormone-related protein
  231. Matrix metalloproteinase-9
  232. Alpha-amylase 2B
  233. fMet-Leu-Phe receptor
  234. N-formyl peptide receptor 2
  235. Type-1 angiotensin II receptor
  236. N-acetylgalactosamine-6-sulfatase
  237. Metabotropic glutamate receptor 5
  238. Collagenase 3
  239. Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform
  240. Alpha-S1-casein
  241. Nucleobindin-2
  242. Metabotropic glutamate receptor 1
  243. Tubulin beta-3 chain
  244. Voltage-dependent L-type calcium channel subunit alpha-1C
  245. Transient receptor potential cation channel subfamily M member 8
  246. Transient receptor potential cation channel subfamily V member 1
  247. Calcium-binding protein p22
  248. C-X-C motif chemokine 16
  249. Homer protein homolog 2
  250. Cysteinyl leukotriene receptor 1
  251. Endothelin-1 receptor
  252. Annexin A2
  253. Protein S100-A9
  254. Extracellular sulfatase Sulf-1
  255. Perforin-1
  256. Gamma-aminobutyric acid type B receptor subunit 1
  257. Neurogenic locus notch homolog protein 1
  258. Calcium-binding mitochondrial carrier protein Aralar2
  259. Transient receptor potential cation channel subfamily V member 6
  260. Cysteinyl leukotriene receptor 2
  261. 5-hydroxytryptamine receptor 2B
  262. Prostaglandin E2 receptor EP1 subtype
  263. Pro-epidermal growth factor
  264. Delta-type opioid receptor
  265. P2Y purinoceptor 2
  266. Interstitial collagenase
  267. BCL2/adenovirus E1B 19 kDa protein-interacting protein 3
  268. Platelet-activating factor receptor
  269. Arylsulfatase H
  270. Endothelin B receptor
  271. Gastrin/cholecystokinin type B receptor
  272. Recoverin
  273. Stromelysin-1
  274. Matrix metalloproteinase-20
  275. Short transient receptor potential channel 3
  276. Cardiac phospholamban
  277. Cubilin
  278. Calretinin
  279. Mu-type opioid receptor
  280. Anthrax toxin receptor 1
  281. Mannose-binding protein C
  282. 5-hydroxytryptamine receptor 2A
  283. Pulmonary surfactant-associated protein A2
  284. S-arrestin
  285. Vitamin D 25-hydroxylase
  286. Bone morphogenetic protein 7
  287. 5-hydroxytryptamine receptor 2C
  288. Histamine H3 receptor
  289. Extracellular calcium-sensing receptor
  290. Low-density lipoprotein receptor-related protein 2
  291. Fibroblast growth factor 23
  292. Prostaglandin D2 receptor
  293. Tumor necrosis factor receptor superfamily member 11B
  294. Caldesmon
  295. Progressive ankylosis protein homolog
  296. CD209 antigen
  297. Membrane-bound transcription factor site-1 protease
  298. Calsenilin
  299. 72 kDa type IV collagenase
  300. Gonadotropin-releasing hormone receptor
  301. Heparanase
  302. Dual specificity protein phosphatase 2
  303. Asialoglycoprotein receptor 2
  304. Myosin regulatory light chain 12A
  305. Parvalbumin alpha
  306. Inositol 1,4,5-trisphosphate receptor type 1
  307. Cadherin-1
  308. Transient receptor potential cation channel subfamily V member 4
  309. Matrix metalloproteinase-14
  310. Cadherin-15
  311. C-type lectin domain family 4 member M
  312. Matrilysin
  313. P2Y purinoceptor 1
  314. Polypeptide N-acetylgalactosaminyltransferase 13
  315. Peroxiredoxin-2
  316. Sodium/calcium exchanger 1
  317. Sodium/potassium/calcium exchanger 4
  318. Sodium-dependent phosphate transport protein 2C
  319. 4F2 cell-surface antigen heavy chain
  320. Dual oxidase 2
  321. Sodium/potassium/calcium exchanger 2
  322. Solute carrier family 12 member 3
  323. Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha
  324. Sodium/potassium/calcium exchanger 1
  325. Sodium/potassium/calcium exchanger 3
  326. Calcium-binding mitochondrial carrier protein Aralar1
  327. Large neutral amino acids transporter small subunit 1
  328. Sodium/calcium exchanger 3
  329. Sodium/calcium exchanger 2
  330. Inositol-trisphosphate 3-kinase C
  331. Phospholipase A2, group XIIA, isoform CRA_b
  332. Sodium-dependent phosphate transport protein 2B
  333. CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial
  334. Hematopoietic cell signal transducer
  335. Adenylate cyclase type 10
  336. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4
  337. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta-1
  338. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1
  339. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
  340. Polypeptide N-acetylgalactosaminyltransferase 9
  341. Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC
  342. Dual oxidase 1
  343. Transketolase-like protein 2
  344. Beta-1,4-galactosyltransferase 6
  345. Sn1-specific diacylglycerol lipase alpha
  346. Sn1-specific diacylglycerol lipase beta
  347. Serine/threonine-protein kinase D2
  348. Putative inactive group IIC secretory phospholipase A2
  349. Lysophosphatidylcholine acyltransferase 1
  350. Phospholipid scramblase 2
  351. Phospholipid scramblase 3
  352. Phospholipid scramblase 4
  353. Phospholipase B1, membrane-associated
  354. Serum deprivation-response protein
  355. Lysophosphatidic acid receptor 4
  356. Membrane-associated phosphatidylinositol transfer protein 1
  357. Membrane-associated phosphatidylinositol transfer protein 2
  358. Membrane-associated phosphatidylinositol transfer protein 3
  359. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase zeta-1
  360. N-acylneuraminate-9-phosphatase
  361. UDP-glucose:glycoprotein glucosyltransferase 2
  362. Bestrophin-1
  363. Bestrophin-2
  364. Bestrophin-3
  365. Bestrophin-4
  366. Neuronal acetylcholine receptor subunit alpha-10
  367. Neuronal acetylcholine receptor subunit alpha-9
  368. Alpha-1A adrenergic receptor
  369. Alpha-1B adrenergic receptor
  370. Alpha-1D adrenergic receptor
  371. A-kinase anchor protein 7 isoforms alpha and beta
  372. A-kinase anchor protein 13
  373. Anoctamin-10
  374. Anoctamin-1
  375. Anoctamin-2
  376. Anoctamin-3
  377. Anoctamin-4
  378. Anoctamin-5
  379. Anoctamin-6
  380. Anoctamin-7
  381. Anoctamin-8
  382. Anoctamin-9
  383. Ankyrin repeat and sterile alpha motif domain-containing protein 1B
  384. Anthrax toxin receptor 2
  385. Annexin A11
  386. Annexin A13
  387. Annexin A1
  388. Annexin A4
  389. Annexin A6
  390. Annexin A7
  391. Annexin A8
  392. Arylsulfatase F
  393. Arylsulfatase G
  394. Arylsulfatase I
  395. Arylsulfatase J
  396. Arylsulfatase K
  397. Asialoglycoprotein receptor 1
  398. Sodium/potassium-transporting ATPase subunit gamma
  399. Transcriptional regulator ATRX
  400. A disintegrin and metalloproteinase with thrombospondin motifs 13
  401. Putative annexin A2-like protein
  402. Annexin A8-like protein 1
  403. Annexin A8-like protein 2
  404. Transforming growth factor-beta-induced protein ig-h3
  405. Class A basic helix-loop-helix protein 15
  406. B2 bradykinin receptor
  407. Bone morphogenetic protein 8A
  408. Bone morphogenetic protein 8B
  409. Bombesin receptor subtype-3
  410. B box and SPRY domain-containing protein
  411. Scavenger receptor cysteine-rich type 1 protein M130
  412. Complement C1q subcomponent subunit A
  413. Complement C1q subcomponent subunit B
  414. Complement C1q subcomponent subunit C
  415. Complement C1r subcomponent
  416. Complement C1s subcomponent precursor
  417. Coiled-coil and C2 domain-containing protein 1A
  418. C5a anaphylatoxin chemotactic receptor
  419. Voltage-dependent calcium channel subunit alpha-2/delta-1
  420. Voltage-dependent calcium channel subunit alpha-2/delta-2
  421. Voltage-dependent calcium channel subunit alpha-2/delta-3
  422. Voltage-dependent calcium channel subunit alpha-2/delta-4
  423. 45 kDa calcium-binding protein
  424. Calcineurin-binding protein cabin-1
  425. Calcium-binding tyrosine phosphorylation-regulated protein
  426. Voltage-dependent P/Q-type calcium channel subunit alpha-1A
  427. Voltage-dependent N-type calcium channel subunit alpha-1B
  428. Voltage-dependent R-type calcium channel subunit alpha-1E
  429. Voltage-dependent L-type calcium channel subunit alpha-1F
  430. Voltage-dependent T-type calcium channel subunit alpha-1G
  431. Voltage-dependent T-type calcium channel subunit alpha-1H
  432. Voltage-dependent T-type calcium channel subunit alpha-1I
  433. Voltage-dependent L-type calcium channel subunit alpha-1S
  434. Voltage-dependent L-type calcium channel subunit beta-1
  435. Voltage-dependent L-type calcium channel subunit beta-2
  436. Voltage-dependent L-type calcium channel subunit beta-3
  437. Voltage-dependent L-type calcium channel subunit beta-4
  438. Calcium-binding and coiled-coil domain-containing protein 1
  439. Cadherin-10
  440. Cadherin-11
  441. Cadherin-12
  442. Cadherin-13
  443. Cadherin-16
  444. Cadherin-17
  445. Cadherin-18
  446. Cadherin-19
  447. Cadherin-20
  448. Cadherin-22
  449. Cadherin-23
  450. Cadherin-24
  451. Cadherin-like protein 26
  452. Cadherin-related family member 3
  453. Cadherin-2
  454. Cadherin-3
  455. Cadherin-4
  456. Cadherin-5
  457. Cadherin-6
  458. Cadherin-7
  459. Cadherin-8
  460. Cadherin-9
  461. Cadherin-related family member 4
  462. Cell adhesion molecule 3
  463. Cell adhesion molecule 4
  464. VWFA and cache domain-containing protein 1
  465. Calcitonin
  466. Calmodulin-like protein 5
  467. Calreticulin-3
  468. Calreticulin
  469. Calumenin
  470. Calnexin
  471. Neuron-specific vesicular protein calcyon
  472. CaM kinase-like vesicle-associated protein
  473. Calcium signal-modulating cyclophilin ligand
  474. Calpain-10
  475. Calpain-11
  476. Calpain-12
  477. Calpain-13
  478. Calpain-14
  479. Calpain-1 catalytic subunit
  480. Calpain-2 catalytic subunit
  481. Calpain-3
  482. Calpain-7
  483. Calpain-8
  484. Calpain-9
  485. Calcineurin subunit B type 1
  486. Calcineurin subunit B type 2
  487. Macrophage-capping protein
  488. Calcium-dependent secretion activator 1
  489. Calcium-dependent secretion activator 2
  490. Calsequestrin-1
  491. Calsequestrin-2
  492. Calcyphosin
  493. E3 ubiquitin-protein ligase CBL
  494. E3 ubiquitin-protein ligase CBL-B
  495. Signal transduction protein CBL-C
  496. Voltage-dependent calcium channel gamma-1 subunit
  497. Voltage-dependent calcium channel gamma-2 subunit
  498. Voltage-dependent calcium channel gamma-3 subunit
  499. Voltage-dependent calcium channel gamma-4 subunit
  500. Voltage-dependent calcium channel gamma-5 subunit
  501. Voltage-dependent calcium channel gamma-6 subunit
  502. Voltage-dependent calcium channel gamma-7 subunit
  503. Voltage-dependent calcium channel gamma-8 subunit
  504. Voltage-dependent calcium channel gamma-like subunit
  505. Cholecystokinin receptor type A
  506. C-C motif chemokine 16
  507. C-C motif chemokine 28
  508. C-C chemokine receptor type 10
  509. C-C chemokine receptor type 1
  510. C-C chemokine receptor type 2
  511. C-C chemokine receptor type 3
  512. C-C chemokine receptor type 4
  513. C-C chemokine receptor type 5
  514. C-C chemokine receptor type 6
  515. C-C chemokine receptor type 9
  516. Carcinoembryonic antigen-related cell adhesion molecule 3
  517. Centrin-1
  518. Centrin-2
  519. Calcium homeostasis endoplasmic reticulum protein
  520. Cartilage intermediate layer protein 1
  521. CDGSH iron-sulfur domain-containing protein 2
  522. C-type lectin domain family 10 member A
  523. C-type lectin domain family 4 member A
  524. C-type lectin domain family 4 member C
  525. C-type lectin domain family 4 member K
  526. C-type lectin domain family 5 member A
  527. Calcium-activated chloride channel regulator 1
  528. Calcium-activated chloride channel regulator 2
  529. Calcium-activated chloride channel regulator 4
  530. Claudin-10
  531. Claudin-11
  532. Claudin-12
  533. Claudin-14
  534. Claudin-15
  535. Claudin-16
  536. Claudin-17
  537. Claudin-18
  538. Claudin-19
  539. Claudin-1
  540. Claudin-20
  541. Claudin-22
  542. Claudin-23
  543. Putative claudin-24
  544. Claudin-2
  545. Claudin-3
  546. Claudin-9
  547. Calmegin
  548. Clathrin heavy chain 1
  549. Clathrin heavy chain 2
  550. CMRF35-like molecule 9
  551. Chromogranin-A
  552. Cyclic nucleotide-gated cation channel alpha-4
  553. CB1 cannabinoid receptor-interacting protein 1
  554. Collectin-12
  555. Coactosin-like protein
  556. Copine-1
  557. Copine-3
  558. Copine-4
  559. Copine-5
  560. Copine-6
  561. Copine-7
  562. Copine-8
  563. Copine-9
  564. Calpain small subunit 1
  565. Calpain small subunit 2
  566. Cysteine-rich secretory protein 2
  567. Cornulin
  568. CREB-regulated transcription coactivator 1
  569. CREB-regulated transcription coactivator 2
  570. Calsyntenin-1
  571. Calsyntenin-2
  572. Calsyntenin-3
  573. Cation channel sperm-associated protein 1
  574. Cation channel sperm-associated protein 2
  575. Cation channel sperm-associated protein 3
  576. Cation channel sperm-associated protein 4
  577. C-X-C chemokine receptor type 1
  578. C-X-C chemokine receptor type 2
  579. C-X-C chemokine receptor type 4
  580. C-X-C motif chemokine 11
  581. C-X-C motif chemokine 13
  582. Calcyclin-binding protein
  583. Neuronal migration protein doublecortin
  584. Deleted in malignant brain tumors 1 protein
  585. Dentin matrix acidic phosphoprotein 1
  586. Dentin matrix protein 4
  587. DnaJ homolog subfamily C member 5
  588. Deoxyribonuclease gamma
  589. Double C2-like domain-containing protein alpha
  590. Double C2-like domain-containing protein beta
  591. Desmocollin-1
  592. Desmocollin-2
  593. Desmocollin-3
  594. Desmoglein-1
  595. Desmoglein-2
  596. Desmoglein-3
  597. Desmoglein-4
  598. Dentin sialophosphoprotein
  599. Eukaryotic elongation factor 2 kinase
  600. EF-hand domain-containing family member A1
  601. EF-hand domain-containing family member A2
  602. EF-hand domain-containing protein 1
  603. Chymotrypsin-like elastase family member 1
  604. Enkurin
  605. Ectonucleoside triphosphate diphosphohydrolase 7
  606. Ectonucleoside triphosphate diphosphohydrolase 8
  607. Extended synaptotagmin-1
  608. Extended synaptotagmin-2
  609. Extended synaptotagmin-3
  610. RNA-binding protein EWS
  611. Fumarylacetoacetate hydrolase domain-containing protein 2A
  612. Fumarylacetoacetate hydrolase domain-containing protein 2B
  613. Fumarylacetoacetate hydrolase domain-containing protein 1
  614. Fibulin-2
  615. Fibrillin-1
  616. Fibrillin-2
  617. Fibrillin-3
  618. F-box only protein 43
  619. Ficolin-2
  620. Alpha-2-HS-glycoprotein
  621. Peptidyl-prolyl cis-trans isomerase FKBP1A
  622. Peptidyl-prolyl cis-trans isomerase FKBP7
  623. Peptidyl-prolyl cis-trans isomerase FKBP8
  624. Feline leukemia virus subgroup C receptor-related protein 2
  625. N-formyl peptide receptor 3
  626. Extracellular matrix protein FRAS1
  627. FRAS1-related extracellular matrix protein 1
  628. FRAS1-related extracellular matrix protein 2
  629. FRAS1-related extracellular matrix protein 3
  630. Fibrous sheath CABYR-binding protein
  631. Furin
  632. Frizzled-10
  633. Frizzled-1
  634. Frizzled-2
  635. Frizzled-3
  636. Frizzled-4
  637. Frizzled-5
  638. Frizzled-6
  639. Frizzled-7
  640. Frizzled-8
  641. Frizzled-9
  642. Protein G6b
  643. Gamma-aminobutyric acid type B receptor subunit 2
  644. GC-rich sequence DNA-binding factor
  645. Gelsolin
  646. Glucagon receptor
  647. Polypeptide N-acetylgalactosaminyltransferase-like 6
  648. Putative polypeptide N-acetylgalactosaminyltransferase-like protein 5
  649. Guanine nucleotide-binding protein G(t) subunit alpha-3
  650. Putative gonadotropin-releasing hormone II receptor
  651. G-protein coupled receptor family C group 6 member A
  652. G-protein coupled receptor 6
  653. Grancalcin
  654. Glutamate receptor 2
  655. RAS guanyl-releasing protein 1
  656. RAS guanyl-releasing protein 2
  657. Gastrin-releasing peptide receptor
  658. Guanylyl cyclase-activating protein 1
  659. Guanylyl cyclase-activating protein 2
  660. Guanylyl cyclase-activating protein 3
  661. Histone H2A type 1
  662. Histone H2A type 1-A
  663. Histone H2A type 1-B/E
  664. Histone H2A type 1-H
  665. Histone H2A type 2-A
  666. Histone H2A type 2-B
  667. Histone H2A type 3
  668. Homer protein homolog 1
  669. Homer protein homolog 3
  670. Neuron-specific calcium-binding protein hippocalcin
  671. Hippocalcin-like protein 1
  672. Hippocalcin-like protein 4
  673. Inhibitor of Bruton tyrosine kinase
  674. Calpastatin
  675. Immunoglobulin superfamily member 2
  676. Immunoglobulin superfamily member 5
  677. Inversin
  678. Integrin beta-7
  679. Integrin beta-1-binding protein 2
  680. Intelectin-1
  681. Inositol 1,4,5-trisphosphate receptor type 2
  682. Inositol 1,4,5-trisphosphate receptor type 3
  683. C-Jun-amino-terminal kinase-interacting protein 1
  684. Junctional sarcoplasmic reticulum protein 1
  685. Calcium/calmodulin-dependent protein kinase type 1B
  686. Kv channel-interacting protein 1
  687. Kv channel-interacting protein 2
  688. Kv channel-interacting protein 4
  689. Calcium-activated potassium channel subunit beta-1
  690. Calcium-activated potassium channel subunit beta-2
  691. Calcium-activated potassium channel subunit beta-3
  692. Calcium-activated potassium channel subunit beta-4
  693. Small conductance calcium-activated potassium channel protein 1
  694. Small conductance calcium-activated potassium channel protein 2
  695. Small conductance calcium-activated potassium channel protein 3
  696. Intermediate conductance calcium-activated potassium channel protein 4
  697. Potassium channel subfamily T member 1
  698. Potassium channel subfamily T member 2
  699. Potassium channel subfamily U member 1
  700. KiSS-1 receptor
  701. Klotho
  702. Phosphorylase b kinase regulatory subunit alpha, liver isoform
  703. Keratinocyte proline-rich protein
  704. Lethal(2) giant larvae protein homolog 2
  705. Leukocyte-associated immunoglobulin-like receptor 1
  706. Linker for activation of T-cells family member 1
  707. Late cornified envelope protein 2A
  708. Late cornified envelope protein 2B
  709. Late cornified envelope protein 2C
  710. Late cornified envelope protein 2D
  711. Lck-interacting transmembrane adapter 1
  712. Protein lin-7 homolog B
  713. Protein lin-7 homolog C
  714. Liprin-beta-1
  715. Leukocyte immunoglobulin-like receptor subfamily B member 1
  716. Leukocyte immunoglobulin-like receptor subfamily B member 2
  717. Leukocyte immunoglobulin-like receptor subfamily B member 4
  718. Vesicular integral-membrane protein VIP36
  719. Latrophilin-1
  720. Latrophilin-2
  721. Prolow-density lipoprotein receptor-related protein 1
  722. Low-density lipoprotein receptor-related protein 5
  723. Leukotriene B4 receptor 2
  724. Mannan-binding lectin serine protease 2
  725. Multiple coagulation factor deficiency protein 2
  726. Multiple C2 and transmembrane domain-containing protein 1
  727. Multiple C2 and transmembrane domain-containing protein 2
  728. Microfibril-associated glycoprotein 4
  729. Magnesium-dependent phosphatase 1
  730. Mitochondrial intermediate peptidase
  731. Cytokine-dependent hematopoietic cell linker
  732. Myosin light chain 1/3, skeletal muscle isoform
  733. Myosin light chain 3, skeletal muscle isoform
  734. Myosin regulatory light chain 2, atrial isoform
  735. Myosin regulatory light chain 2, skeletal muscle isoform
  736. Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
  737. Stromelysin-2
  738. Stromelysin-3
  739. Macrophage metalloelastase
  740. Matrix metalloproteinase-15
  741. Matrix metalloproteinase-16
  742. Matrix metalloproteinase-17
  743. Matrix metalloproteinase-19
  744. Matrix metalloproteinase-21
  745. Matrix metalloproteinase-24
  746. Matrix metalloproteinase-25
  747. Matrix metalloproteinase-26
  748. Matrix metalloproteinase-27
  749. Matrix metalloproteinase-28
  750. Neutrophil collagenase
  751. C-type mannose receptor 2
  752. Mas-related G-protein coupled receptor member X1
  753. Myosin regulatory light chain 12B
  754. Protein MRVI1
  755. Cell surface glycoprotein MUC18
  756. Cadherin-related family member 5
  757. Myosin light chain 3
  758. Myosin light chain 4
  759. Myosin light chain 5
  760. Myosin light polypeptide 6
  761. Myosin light chain 6B
  762. Myosin regulatory light polypeptide 9
  763. Myosin regulatory light chain 10
  764. Myosin-VI
  765. Myosin-IXb
  766. NKG2D ligand 1
  767. NKG2D ligand 2
  768. NKG2D ligand 3
  769. Sodium leak channel non-selective protein
  770. Neurocalcin-delta
  771. Sodium/potassium/calcium exchanger 5
  772. Sodium/potassium/calcium exchanger 6
  773. Neuronal calcium sensor 1
  774. Neuroendocrine convertase 1
  775. Neurogranin
  776. Nuclear factor of activated T-cells, cytoplasmic 3
  777. Nuclear factor of activated T-cells, cytoplasmic 4
  778. Substance-P receptor
  779. Substance-K receptor
  780. Neuromedin-K receptor
  781. Glutamate [NMDA] receptor subunit 3A
  782. NADPH oxidase 5
  783. Neuropeptide FF receptor 1
  784. Neuropeptide FF receptor 2
  785. Neuronal pentraxin-1
  786. Neuronal pentraxin-2
  787. Pentraxin-4
  788. Neuronal pentraxin receptor
  789. Neurotensin receptor type 1
  790. Neurotensin receptor type 2
  791. Nucleobindin-1
  792. Not Available
  793. Kappa-type opioid receptor
  794. Sigma non-opioid intracellular receptor 1
  795. Otopetrin-1
  796. P2X purinoceptor 1
  797. P2Y purinoceptor 4
  798. P2Y purinoceptor 6
  799. P2Y purinoceptor 11
  800. Cytosolic phospholipase A2 delta
  801. Cytosolic phospholipase A2 epsilon
  802. Cytosolic phospholipase A2 zeta
  803. Protocadherin-11 X-linked
  804. Protocadherin-11 Y-linked
  805. Protocadherin-10
  806. Protocadherin-12
  807. Protocadherin-15
  808. Protocadherin-16
  809. Protocadherin-17
  810. Protocadherin-18
  811. Protocadherin-19
  812. Protocadherin-20
  813. Cadherin-related family member 1
  814. Protocadherin-23
  815. Protocadherin alpha-1
  816. Protocadherin alpha-2
  817. Protocadherin alpha-3
  818. Protocadherin alpha-4
  819. Protocadherin alpha-5
  820. Protocadherin alpha-6
  821. Protocadherin alpha-7
  822. Protocadherin alpha-8
  823. Protocadherin alpha-9
  824. Protocadherin alpha-10
  825. Protocadherin alpha-11
  826. Protocadherin alpha-12
  827. Protocadherin alpha-13
  828. Protocadherin beta-1
  829. Protocadherin beta-2
  830. Protocadherin beta-3
  831. Protocadherin beta-4
  832. Protocadherin beta-5
  833. Protocadherin beta-6
  834. Protocadherin beta-7
  835. Protocadherin beta-8
  836. Protocadherin beta-9
  837. Protocadherin beta-10
  838. Protocadherin beta-11
  839. Protocadherin beta-12
  840. Protocadherin beta-13
  841. Protocadherin beta-14
  842. Protocadherin beta-15
  843. Protocadherin beta-16
  844. Putative protocadherin beta-18
  845. Protocadherin alpha-C1
  846. Protocadherin alpha-C2
  847. Protocadherin gamma-A1
  848. Protocadherin gamma-A2
  849. Protocadherin gamma-A3
  850. Protocadherin gamma-A4
  851. Protocadherin gamma-A5
  852. Protocadherin gamma-A6
  853. Protocadherin gamma-A7
  854. Protocadherin gamma-A8
  855. Protocadherin gamma-A9
  856. Protocadherin gamma-A10
  857. Protocadherin gamma-A11
  858. Protocadherin gamma-A12
  859. Protocadherin gamma-B1
  860. Protocadherin gamma-B2
  861. Protocadherin gamma-B3
  862. Protocadherin gamma-B4
  863. Protocadherin gamma-B5
  864. Protocadherin gamma-B6
  865. Protocadherin gamma-B7
  866. Protocadherin gamma-C3
  867. Protocadherin gamma-C4
  868. Protocadherin gamma-C5
  869. Protocadherin-9
  870. Protein piccolo
  871. Proprotein convertase subtilisin/kexin type 7
  872. Proprotein convertase subtilisin/kexin type 9
  873. Programmed cell death 6-interacting protein
  874. Programmed cell death protein 6
  875. Prostaglandin E2 receptor EP3 subtype
  876. Astrocytic phosphoprotein PEA-15
  877. Polycystic kidney disease 2-like 1 protein
  878. Polycystin-1
  879. Polycystin-2
  880. Prokineticin receptor 1
  881. Prokineticin receptor 2
  882. Calcium-independent phospholipase A2-gamma
  883. Plastin-1
  884. Periostin
  885. Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
  886. Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
  887. Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform
  888. Serine/threonine-protein phosphatase with EF-hands 1
  889. Serine/threonine-protein phosphatase with EF-hands 2
  890. Protein phosphatase 1 regulatory subunit 1A
  891. Bone marrow proteoglycan
  892. E3 ubiquitin-protein ligase parkin
  893. Salivary acidic proline-rich phosphoprotein 1/2
  894. Presenilin-1
  895. Parathyroid hormone/parathyroid hormone-related peptide receptor
  896. Peroxidasin homolog
  897. Peroxidasin-like protein
  898. Pyroglutamylated RFamide peptide receptor
  899. Ras GTPase-activating protein 4
  900. Calcipressin-1
  901. Reticulocalbin-1
  902. Reticulocalbin-2
  903. Lithostathine-1-alpha
  904. Lithostathine-1-beta
  905. GTP-binding protein REM 1
  906. Regucalcin
  907. Ras-specific guanine nucleotide-releasing factor 2
  908. Rho GTPase-activating protein 32
  909. Regulating synaptic membrane exocytosis protein 1
  910. Repetin
  911. Ryanodine receptor 1
  912. Ryanodine receptor 2
  913. Ryanodine receptor 3
  914. Protein S100-B
  915. Protein S100-P
  916. Protein S100-Z
  917. Protein S100-A1
  918. Protein S100-A2
  919. Protein S100-A3
  920. Protein S100-A4
  921. Protein S100-A10
  922. Protein S100-A11
  923. Solute carrier family 22 member 6
  924. Sodium- and chloride-dependent transporter XTRP3
  925. Serum amyloid P-component
  926. Sarcolipin
  927. Protein transport protein Sec31A
  928. Secretogranin-2
  929. Calcium-binding mitochondrial carrier protein SCaMC-1
  930. Calcium-binding mitochondrial carrier protein SCaMC-2
  931. Calcium-binding mitochondrial carrier protein SCaMC-3
  932. Secernin-1
  933. Protein SET
  934. Pulmonary surfactant-associated protein A1
  935. Sodium/hydrogen exchanger 6
  936. SNARE-associated protein Snapin
  937. SRC kinase signaling inhibitor 1
  938. Alpha-1-syntrophin
  939. Beta-2-syntrophin
  940. Sorcin
  941. Spectrin alpha chain, brain
  942. Spectrin beta chain, brain 1
  943. Sarcalumenin
  944. Sarcoplasmic reticulum histidine-rich calcium-binding protein
  945. Somatostatin receptor type 2
  946. Translocon-associated protein subunit alpha
  947. Translocon-associated protein subunit beta
  948. Translocon-associated protein subunit delta
  949. Translocon-associated protein subunit gamma
  950. Statherin
  951. Stanniocalcin-2
  952. Stromal interaction molecule 1
  953. Striatin-3
  954. Striatin-4
  955. Syntaxin-binding protein 5
  956. Extracellular sulfatase Sulf-2
  957. Synaptic vesicle glycoprotein 2A
  958. Synaptic vesicle glycoprotein 2B
  959. Synaptic vesicle glycoprotein 2C
  960. Synapsin-3
  961. Synaptophysin
  962. Synaptotagmin-10
  963. Synaptotagmin-11
  964. Synaptotagmin-13
  965. Synaptotagmin-1
  966. Synaptotagmin-2
  967. Synaptotagmin-3
  968. Synaptotagmin-4
  969. Synaptotagmin-5
  970. Synaptotagmin-6
  971. Synaptotagmin-7
  972. Synaptotagmin-9
  973. Synaptotagmin-like protein 3
  974. Gamma-synuclein
  975. Taste receptor type 2 member 10
  976. Taste receptor type 2 member 16
  977. Taste receptor type 2 member 40
  978. Taste receptor type 2 member 3
  979. Taste receptor type 2 member 4
  980. Taste receptor type 2 member 7
  981. Taste receptor type 2 member 9
  982. Transgelin
  983. Tubulin beta-2C chain
  984. Tubulin beta-4 chain
  985. Tubulin beta chain
  986. Tubulin beta-6 chain
  987. Translationally-controlled tumor protein
  988. Tescalcin
  989. Trefoil factor 1
  990. Testican-2
  991. Tuberoinfundibular peptide of 39 residues
  992. Trimeric intracellular cation channel type A
  993. Trimeric intracellular cation channel type B
  994. Troponin C, slow skeletal and cardiac muscles
  995. Troponin C, skeletal muscle
  996. Troponin I, slow skeletal muscle
  997. Troponin I, fast skeletal muscle
  998. Troponin I, cardiac muscle
  999. Troponin T, slow skeletal muscle
  1000. Troponin T, cardiac muscle
  1001. Troponin T, fast skeletal muscle
  1002. DNA topoisomerase I, mitochondrial
  1003. Prosalusin
  1004. Protein tyrosine phosphatase type IVA 3
  1005. Two pore calcium channel protein 1
  1006. Two pore calcium channel protein 2
  1007. Tropomyosin alpha-1 chain
  1008. Tropomyosin beta chain
  1009. Tropomyosin alpha-3 chain
  1010. Thyrotropin-releasing hormone receptor
  1011. Trichohyalin
  1012. Short transient receptor potential channel 1
  1013. Short transient receptor potential channel 4
  1014. Short transient receptor potential channel 5
  1015. Short transient receptor potential channel 6
  1016. Short transient receptor potential channel 7
  1017. Transient receptor potential cation channel subfamily M member 1
  1018. Transient receptor potential cation channel subfamily M member 3
  1019. Transient receptor potential cation channel subfamily M member 4
  1020. Transient receptor potential cation channel subfamily V member 2
  1021. Transient receptor potential cation channel subfamily V member 3
  1022. Transient receptor potential cation channel subfamily V member 5
  1023. Trypsin-1
  1024. Trypsin-2
  1025. Trypsin-3
  1026. Tau-tubulin kinase 1
  1027. Alpha-taxilin
  1028. Endoplasmic reticulum resident protein 44
  1029. UBX domain-containing protein 4
  1030. UDP-glucose:glycoprotein glucosyltransferase 1
  1031. Protein unc-13 homolog A
  1032. Protein unc-13 homolog B
  1033. Protein unc-13 homolog C
  1034. Urotensin-2 receptor
  1035. Vesicle-associated membrane protein 4
  1036. Vesicle-associated membrane protein 7
  1037. Villin-1
  1038. Visinin-like protein 1
  1039. Chemokine XC receptor 1
  1040. Protein Z-dependent protease inhibitor
  1041. Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
  1042. Serine/threonine-protein phosphatase 4 catalytic subunit
  1043. Serine/threonine-protein phosphatase 5
  1044. Serine/threonine-protein phosphatase 6 catalytic subunit
  1045. Putative myosin light chain kinase 3
  1046. Protein phosphatase 1A
  1047. Protein phosphatase 1D
  1048. Protein phosphatase 1E
  1049. Protein phosphatase 1F
  1050. Protein phosphatase 1G
  1051. Protein phosphatase 1M
  1052. Ubiquitin-like domain-containing CTD phosphatase 1
  1053. Dual specificity protein phosphatase 18
  1054. PH domain leucine-rich repeat-containing protein phosphatase 2
  1055. PH domain leucine-rich repeat-containing protein phosphatase 1
  1056. Dual specificity protein phosphatase CDC14A
  1057. RNA polymerase II subunit A C-terminal domain phosphatase
  1058. Dual specificity protein phosphatase 10
  1059. Dual specificity protein phosphatase 12
  1060. Dual specificity protein phosphatase 13
  1061. Dual specificity protein phosphatase 16
  1062. Dual specificity protein phosphatase 19
  1063. Dual specificity protein phosphatase 1
  1064. Dual specificity protein phosphatase 3
  1065. Dual specificity protein phosphatase 4
  1066. Dual specificity protein phosphatase 5
  1067. Dual specificity protein phosphatase 6
  1068. Dual specificity protein phosphatase 7
  1069. Dual specificity protein phosphatase 8
  1070. Cytosolic phospholipase A2 beta
  1071. Nitric oxide synthase 2A (Inducible, hepatocytes)
  1072. UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 5 (GalNAc-T5)
  1073. UDP-N-acetyl-alpha-D-galactosamine:polypeptide N- acetylgalactosaminyltransferase-like 1 (cDNA FLJ76743, highly similar to Homo sapiens UDP-N-acetyl-alpha-D-galactosamine:polypeptide N- acetylgalactosaminyltransferase-like 1 (GALNTL1), mRNA)
  1074. Pp-GalNAc-transferase 20
  1075. Calcium/calmodulin-dependent protein kinase ID
  1076. Calcium/calmodulin-dependent protein kinase (CaM kinase) II alpha, isoform CRA_b
  1077. Calcium/calmodulin-dependent protein kinase (CaM kinase) II beta
  1078. Calcium/calmodulin-dependent protein kinase isoform A
  1079. cDNA FLJ75686, highly similar to Homo sapiens phospholipase A2, group IIA (platelets, synovial fluid) (PLA2G2A), mRNA (Phospholipase A2, group IIA (Platelets, synovial fluid), isoform CRA_a)
  1080. CDKN3 protein (Cyclin-dependent kinase inhibitor 3 (CDK2-associated dual specificity phosphatase), isoform CRA_c)
  1081. Dual specificity protein phosphatase 14
  1082. Putative uncharacterized protein DUSP15
  1083. Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta
  1084. PPM1B beta isoform variant 4
  1085. Serine/threonine-protein phosphatase
  1086. cDNA FLJ76978, highly similar to Homo sapiens protein phosphatase 2 (formerly 2A), regulatory subunit B'', alpha (PPP2R3A), transcript variant 1, mRNA (Protein phosphatase 2 (Formerly 2A), regulatory subunit B'', alpha, isoform CRA_a)
  1087. Serine/threonine protein phosphatase (EC 3.1.3.16)
  1088. Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1
  1089. Dual specificity protein phosphatase 21
  1090. Putative uncharacterized protein CDC14B
  1091. Glutamyl aminopeptidase
  1092. Bone morphogenetic protein 1
  1093. cDNA FLJ75328, highly similar to Homo sapiens ATPase, Ca++ transporting, cardiac muscle, fast twitch1 (ATP2A1), transcript variant b, mRNA
  1094. Putative uncharacterized protein DKFZp686I0955
  1095. cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
  1096. NOS1 mutant
  1097. UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 8 (GalNAc-T8)
  1098. cDNA PSEC0182 fis, clone OVARC1001636, highly similar to N-acetylgalactosaminyltransferase 7 (EC 2.4.1.-)
  1099. cDNA FLJ42944 fis, clone BRSTN2004863, highly similar to PolypeptideN-acetylgalactosaminyltransferase 11 (EC 2.4.1.41)
  1100. Calcium/calmodulin-dependent protein kinase I, isoform CRA_a
  1101. Phospholipase A2, group VI (Cytosolic, calcium-independent) (Phospholipase A2, group VI (Cytosolic, calcium-independent), isoform CRA_a)
  1102. cDNA FLJ31512 fis, clone NT2RI1000048, highly similar to Dual specificity protein phosphatase 18 (EC 3.1.3.48)
  1103. cDNA, FLJ95698, Homo sapiens dual specificity phosphatase 4 (DUSP4), transcript variant 1, mRNA (Dual specificity phosphatase 4, isoform CRA_a)
  1104. cDNA, FLJ94996, highly similar to Homo sapiens dual specificity phosphatase 9 (DUSP9), mRNA
  1105. cDNA FLJ45992 fis, clone SKMUS2008585, highly similar to Homo sapiens dual specificity phosphatase 13 (DUSP13), transcript variant 3, mRNA
  1106. Protein phosphatase 1A isoform 1 (Protein phosphatase 1A (Formerly 2C), magnesium-dependent, alpha isoform, isoform CRA_a)
  1107. cDNA, FLJ92643, Homo sapiens protein phosphatase 1, catalytic subunit, beta isoform(PPP1CB), mRNA (Protein phosphatase 1, catalytic subunit, beta isoform, isoform CRA_a)
  1108. Serine/threonine-protein phosphatase
  1109. Serine/threonine-protein phosphatase
  1110. Protein phosphatase 1, regulatory (Inhibitor) subunit 1B (Dopamine and cAMP regulated phosphoprotein, DARPP-32), isoform CRA_b
  1111. CDC14 cell division cycle 14 homolog A (S. cerevisiae)
  1112. ATPase, Ca++ transporting, plasma membrane 4
Enzyme 1 [top]
Enzyme 1 ID 5286
Enzyme 1 Name Group XV phospholipase A2
Enzyme 1 Synonyms
  1. 1-O-acylceramide synthase
  2. ACS
  3. LCAT-like lysophospholipase
  4. LLPL
  5. Lysophospholipase 3
  6. Lysosomal phospholipase A2
  7. LPLA2
Enzyme 1 Gene Name PLA2G15
Enzyme 1 Protein Sequence >Group XV phospholipase A2 
MGLHLRPYRVGLLPDGLLFLLLLLMLLADPALPAGRHPPVVLVPGDLGNQLEAKLDKPTV
VHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNIRLVYNKTSRATQFPDGVDVRVPGFGK
TFSLEFLDPSKSSVGSYFHTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREM
IEEMYQLYGGPVVLVAHSMGNMYTLYFLQRQPQAWKDKYIRAFVSLGAPWGGVAKTLRVL
ASGDNNRIPVIGPLKIREQQRSAVSTSWLLPYNYTWSPEKVFVQTPTINYTLRDYRKFFQ
DIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDPKICFGDGD
GTVNLKSALQCQAWQSRQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP
Enzyme 1 Number of Residues 412
Enzyme 1 Molecular Weight 46657.4
Enzyme 1 Theoretical pI 6.72
Enzyme 1 GO Classification
Function
  • O-acyltransferase activity
  • acyltransferase activity
  • catalytic activity
  • phosphatidylcholine-sterol O-acyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups other than amino-acyl groups
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
—
Enzyme 1 General Function Involved in phosphatidylcholine-sterol O-acyltransferase activity
Enzyme 1 Specific Function Has transacylase and calcium-independent phospholipase A2 activity. Catalyzes the formation of 1-O-acyl-N- acetylsphingosine and the concomitant release of a lyso- phospholipid. May have weak lysophospholipase activity
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-33
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein Not Available
Enzyme 1 UniProtKB/Swiss-Prot ID Q8NCC3 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PAG15_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1239 bp 
ATGGGCCTCCACCTCCGCCCCTACCGTGTGGGGCTGCTCCCGGATGGCCTCCTGTTCCTC
TTGCTGCTGCTAATGCTGCTCGCGGACCCAGCGCTCCCGGCCGGACGTCACCCCCCAGTG
GTGCTGGTCCCTGGTGATTTGGGTAACCAACTGGAAGCCAAGCTGGACAAGCCGACAGTG
GTGCACTACCTCTGCTCCAAGAAGACCGAAAGCTACTTCACAATCTGGCTGAACCTGGAA
CTGCTGCTGCCTGTCATCATTGACTGCTGGATTGACAATATCAGGCTGGTTTACAACAAA
ACATCCAGGGCCACCCAGTTTCCTGATGGTGTGGATGTACGTGTCCCTGGCTTTGGGAAG
ACCTTCTCACTGGAGTTCCTGGACCCCAGCAAAAGCAGCGTGGGTTCCTATTTCCACACC
ATGGTGGAGAGCCTTGTGGGCTGGGGCTACACACGGGGTGAGGATGTCCGAGGGGCTCCC
TATGACTGGCGCCGAGCCCCAAATGAAAACGGGCCCTACTTCCTGGCCCTCCGCGAGATG
ATCGAGGAGATGTACCAGCTGTATGGGGGCCCCGTGGTGCTGGTTGCCCACAGTATGGGC
AACATGTACACGCTCTACTTTCTGCAGCGGCAGCCGCAGGCCTGGAAGGACAAGTATATC
CGGGCCTTCGTGTCACTGGGTGCGCCCTGGGGGGGCGTGGCCAAGACCCTGCGCGTCCTG
GCTTCAGGAGACAACAACCGGATCCCAGTCATCGGGCCCCTGAAGATCCGGGAGCAGCAG
CGGTCAGCTGTCTCCACCAGCTGGCTGCTGCCCTACAACTACACATGGTCACCTGAGAAG
GTGTTCGTGCAGACACCCACAATCAACTACACACTGCGGGACTACCGCAAGTTCTTCCAG
GACATCGGCTTTGAAGATGGCTGGCTCATGCGGCAGGACACAGAAGGGCTGGTGGAAGCC
ACGATGCCACCTGGCGTGCAGCTGCACTGCCTCTATGGCACTGGCGTCCCCACACCAGAC
TCCTTCTACTATGAGAGCTTCCCTGACCGTGACCCTAAAATCTGCTTTGGTGACGGCGAT
GGTACTGTGAACTTGAAGAGTGCCCTGCAGTGCCAGGCCTGGCAGAGCCGCCAGGAGCAC
CAAGTGTTGCTGCAGGAGCTGCCAGGCAGCGAGCACATCGAGATGCTGGCCAACGCCACC
ACCCTGGCCTATCTGAAACGTGTGCTCCTTGGGCCCTGA
Enzyme 1 GenBank Gene ID AB017494 Link Image
Enzyme 1 GeneCard ID PLA2G15 Link Image
Enzyme 1 GenAtlas ID PLA2G15 Link Image
Enzyme 1 HGNC ID HGNC:17163 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 16q22.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Taniyama Y, Shibata S, Kita S, Horikoshi K, Fuse H, Shirafuji H, Sumino Y, Fujino M: Cloning and expression of a novel lysophospholipase which structurally resembles lecithin cholesterol acyltransferase. Biochem Biophys Res Commun. 1999 Apr 2;257(1):50-6. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Zhang Z, Henzel WJ: Signal peptide prediction based on analysis of experimentally verified cleavage sites. Protein Sci. 2004 Oct;13(10):2819-24. Epub 2004 Aug 31. [PubMed Link Image]
  7. Hiraoka M, Abe A, Shayman JA: Cloning and characterization of a lysosomal phospholipase A2, 1-O-acylceramide synthase. J Biol Chem. 2002 Mar 22;277(12):10090-9. Epub 2002 Jan 14. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5287
Enzyme 2 Name Calcium-dependent phospholipase A2
Enzyme 2 Synonyms
  1. Group V phospholipase A2
  2. PLA2-10
  3. Phosphatidylcholine 2-acylhydrolase 5
Enzyme 2 Gene Name PLA2G5
Enzyme 2 Protein Sequence >Calcium-dependent phospholipase A2 
MKGLLPLAWFLACSVPAVQGGLLDLKSMIEKVTGKNALTNYGFYGCYCGWGGRGTPKDGT
DWCCWAHDHCYGRLEEKGCNIRTQSYKYRFAWGVVTCEPGPFCHVNLCACDRKLVYCLKR
NLRSYNPQYQYFPNILCS
Enzyme 2 Number of Residues 138
Enzyme 2 Molecular Weight 15674.1
Enzyme 2 Theoretical pI 8.48
Enzyme 2 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylesterase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
  • primary metabolic process
Component
—
Enzyme 2 General Function Involved in phospholipase A2 activity
Enzyme 2 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. This isozyme hydrolyzes more efficiently L-alpha-1-palmitoyl-2-oleoyl phosphatidylcholine than L-alpha-1-palmitoyl-2-arachidonyl phosphatidylcholine, L- alpha-1-palmitoyl-2-arachidonyl phosphatidylethanolamine, or L- alpha-1-stearoyl-2-arachidonyl phosphatidylinositol. May be involved in the production of lung surfactant, the remodeling or regulation of cardiac muscle
Enzyme 2 Pathways
Enzyme 2 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-20
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 10862735 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P39877 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PA2G5_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >417 bp 
ATGAAAGGCCTCCTCCCACTGGCTTGGTTCCTGGCTTGTAGTGTGCCTGCTGTGCAAGGA
GGCTTGCTGGACCTAAAATCAATGATCGAGAAGGTGACAGGGAAGAACGCCCTGACAAAC
TACGGCTTCTACGGCTGTTACTGCGGCTGGGGCGGCCGAGGAACCCCCAAGGATGGCACC
GATTGGTGCTGTTGGGCGCATGACCACTGCTATGGGCGGCTGGAGGAGAAGGGCTGCAAC
ATTCGCACACAGTCCTACAAATACAGATTCGCGTGGGGCGTGGTCACCTGCGAGCCCGGG
CCCTTCTGCCATGTGAACCTCTGTGCCTGTGACCGGAAGCTCGTCTACTGCCTCAAGAGA
AACCTACGGAGCTACAACCCACAGTACCAATACTTTCCCAACATCCTCTGCTCCTAG
Enzyme 2 GenBank Gene ID AL158172 Link Image
Enzyme 2 GeneCard ID PLA2G5 Link Image
Enzyme 2 GenAtlas ID PLA2G5 Link Image
Enzyme 2 HGNC ID HGNC:9038 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1p36-p34
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Chen J, Engle SJ, Seilhamer JJ, Tischfield JA: Cloning and recombinant expression of a novel human low molecular weight Ca(2+)-dependent phospholipase A2. J Biol Chem. 1994 Jan 28;269(4):2365-8. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5288
Enzyme 3 Name Group IIF secretory phospholipase A2
Enzyme 3 Synonyms
  1. GIIF sPLA2
  2. sPLA2-IIF
  3. Phosphatidylcholine 2-acylhydrolase 2F
Enzyme 3 Gene Name PLA2G2F
Enzyme 3 Protein Sequence >Group IIF secretory phospholipase A2 
MKKFFTVAILAGSVLSTAHGSLLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEV
DWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTEIVCSDLNKTECDKQTCMCDKNMVLC
LMNQTYREEYRGFLNVYCQGPTPNCSIYEPPPEEVTCSHQSPAPPAPP
Enzyme 3 Number of Residues 168
Enzyme 3 Molecular Weight 18658.0
Enzyme 3 Theoretical pI 4.94
Enzyme 3 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylesterase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
  • primary metabolic process
Component
—
Enzyme 3 General Function Involved in phospholipase A2 activity
Enzyme 3 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Hydrolyzes phosphatidylglycerol versus phosphatidylcholine with a 15-fold preference
Enzyme 3 Pathways
Enzyme 3 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-20
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 12276060 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q9BZM2 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name PA2GF_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >507 bp 
ATGAAGAAGTTCTTCACCGTGGCCATCCTTGCTGGCAGCGTTCTGTCCACAGCTCACGGC
AGCCTGCTCAACCTGAAGGCCATGGTGGAGGCCGTCACAGGGAGGAGCGCCATCCTGTCC
TTCGTGGGCTACGGTTGCTACTGTGGGCTGGGGGGCCGTGGCCAGCCCAAGGATGAGGTG
GACTGGTGCTGCCACGCCCACGACTGCTGCTACCAGGAACTCTTTGACCAAGGCTGTCAC
CCCTATGTGGACCACTATGATCACACCATCGAGAACAACACTGAGATAGTCTGCAGTGAC
CTCAACAAGACAGAGTGTGACAAGCAGACATGCATGTGTGACAAGAACATGGTTCTGTGC
CTCATGAACCAGACGTACCGAGAGGAGTACCGTGGCTTCCTCAATGTCTACTGCCAGGGC
CCCACGCCCAACTGCAGCATCTATGAACCGCCCCCTGAGGAGGTCACCTGCAGTCACCAA
TCCCCAGCGCCCCCCGCCCCTCCCTAG
Enzyme 3 GenBank Gene ID AF306566 Link Image
Enzyme 3 GeneCard ID PLA2G2F Link Image
Enzyme 3 GenAtlas ID PLA2G2F Link Image
Enzyme 3 HGNC ID HGNC:30040 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1p35
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Valentin E, Singer AG, Ghomashchi F, Lazdunski M, Gelb MH, Lambeau G: Cloning and recombinant expression of human group IIF-secreted phospholipase A(2). Biochem Biophys Res Commun. 2000 Dec 9;279(1):223-8. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5289
Enzyme 4 Name Cytosolic phospholipase A2
Enzyme 4 Synonyms
  1. cPLA2
  2. Phospholipase A2 group IVA
  3. Phospholipase A2
  4. Phosphatidylcholine 2-acylhydrolase
  5. Lysophospholipase
Enzyme 4 Gene Name PLA2G4A
Enzyme 4 Protein Sequence >Cytosolic phospholipase A2 
MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRT
RHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFTVSSMKVGEKKEV
PFIFNQVTEMVLEMSLEVCSCPDLRFSMALCDQEKTFRQQRKEHIRESMKKLLGPKNSEG
LHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSH
PDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIG
ETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYG
TFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSRGSTMEEE
LENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFN
TREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDV
KSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMN
KLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHFVLANINFRKYKAPGVPRETE
EEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRR
QNPSRCSVSLSNVEARRFFNKEFLSKPKA
Enzyme 4 Number of Residues 749
Enzyme 4 Molecular Weight 85210.2
Enzyme 4 Theoretical pI 5.03
Enzyme 4 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • phospholipase activity
Process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid catabolic process
  • phospholipid metabolic process
Component
—
Enzyme 4 General Function Involved in metabolic process
Enzyme 4 Specific Function Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response
Enzyme 4 Pathways
Enzyme 4 Reactions
  • 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate [RN:R07291]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID P47712 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PA24A_HUMAN Link Image
Enzyme 4 PDB ID 1CJY Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2250 bp 
ATGTCATTTATAGATCCTTACCAGCACATTATAGTGGAGCACCAGTATTCCCACAAGTTT
ACGGTAGTGGTGTTACGTGCCACCAAAGTGACAAAGGGGGCCTTTGGTGACATGCTTGAT
ACTCCAGATCCCTATGTGGAACTTTTTATCTCTACAACCCCTGACAGCAGGAAGAGAACA
AGACATTTCAATAATGACATAAACCCTGTGTGGAATGAGACCTTTGAATTTATTTTGGAT
CCTAATCAGGAAAATGTTTTGGAGATTACGTTAATGGATGCCAATTATGTCATGGATGAA
ACTCTAGGGACAGCAACATTTACTGTATCTTCTATGAAGGTGGGAGAAAAGAAAGAAGTT
CCTTTTATTTTCAACCAAGTCACTGAAATGGTTCTAGAAATGTCTCTTGAAGTTTGCTCA
TGCCCAGACCTACGATTTAGTATGGCTCTGTGTGATCAGGAGAAGACTTTCAGACAACAG
AGAAAAGAACACATAAGGGAGAGCATGAAGAAACTCTTGGGTCCAAAGAATAGTGAAGGA
TTGCATTCTGCACGTGATGTGCCTGTGGTAGCCATATTGGGTTCAGGTGGGGGTTTCCGA
GCCATGGTGGGATTCTCTGGTGTGATGAAGGCATTATACGAATCAGGAATTCTGGATTGT
GCTACCTACGTTGCTGGTCTTTCTGGCTCCACCTGGTATATGTCAACCTTGTATTCTCAC
CCTGATTTTCCAGAGAAAGGGCCAGAGGAGATTAATGAAGAACTAATGAAAAATGTTAGC
CACAATCCCCTTTTACTTCTCACACCACAGAAAGTTAAAAGATATGTTGAGTCTTTATGG
AAGAAGAAAAGCTCTGGACAACCTGTCACCTTTACTGATATCTTTGGGATGTTAATAGGA
GAAACACTAATTCATAATAGAATGAATACTACTCTGAGCAGTTTGAAGGAAAAAGTTAAT
ACTGCACAATGCCCTTTACCTCTTTTCACCTGTCTTCATGTCAAACCTGACGTTTCAGAG
CTGATGTTTGCAGATTGGGTTGAATTTAGTCCATACGAAATTGGCATGGCTAAATATGGT
ACTTTTATGGCTCCCGACTTATTTGGAAGCAAATTTTTTATGGGAACAGTCGTTAAGAAG
TATGAAGAAAACCCCTTGCATTTCTTAATGGGTGTCTGGGGCAGTGCCTTTTCCATATTG
TTCAACAGAGTTTTGGGCGTTTCTGGTTCACAAAGCAGAGGCTCCACAATGGAGGAAGAA
TTAGAAAATATTACCACAAAGCATATTGTGAGTAATGATAGCTCGGACAGTGATGATGAA
TCACACGAACCCAAAGGCACTGAAAATGAAGATGCTGGAAGTGACTATCAAAGTGATAAT
CAAGCAAGTTGGATTCATCGTATGATAATGGCCTTGGTGAGTGATTCAGCTTTATTCAAT
ACCAGAGAAGGACGTGCTGGGAAGGTACACAACTTCATGCTGGGCTTGAATCTCAATACA
TCTTATCCACTGTCTCCTTTGAGTGACTTTGCCACACAGGACTCCTTTGATGATGATGAA
CTGGATGCAGCTGTAGCAGATCCTGATGAATTTGAGCGAATATATGAGCCTCTGGATGTC
AAAAGTAAAAAGATTCATGTAGTGGACAGTGGGCTCACATTTAACCTGCCGTATCCCTTG
ATACTGAGACCTCAGAGAGGGGTTGATCTCATAATCTCCTTTGACTTTTCTGCAAGGCCA
AGTGACTCTAGTCCTCCGTTCAAGGAACTTCTACTTGCAGAAAAGTGGGCTAAAATGAAC
AAGCTCCCCTTTCCAAAGATTGATCCTTATGTGTTTGATCGGGAAGGGCTGAAGGAGTGC
TATGTCTTTAAACCCAAGAATCCTGATATGGAGAAAGATTGCCCAACCATCATCCACTTT
GTTCTGGCCAACATCAACTTCAGAAAGTACAAGGCTCCAGGTGTTCCAAGGGAAACTGAG
GAAGAGAAAGAAATCGCTGACTTTGATATTTTTGATGACCCAGAATCACCATTTTCAACC
TTCAATTTTCAATATCCAAATCAAGCATTCAAAAGACTACATGATCTTATGCACTTCAAT
ACTCTGAACAACATTGATGTGATAAAAGAAGCCATGGTTGAAAGCATTGAATATAGAAGA
CAGAATCCATCTCGTTGCTCTGTTTCCCTTAGTAATGTTGAGGCAAGAAGATTTTTCAAC
AAGGAGTTTCTAAGTAAACCCAAAGCATAG
Enzyme 4 GenBank Gene ID M72393 Link Image
Enzyme 4 GeneCard ID PLA2G4A Link Image
Enzyme 4 GenAtlas ID PLA2G4A Link Image
Enzyme 4 HGNC ID HGNC:9035 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 1q25
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Clark JD, Lin LL, Kriz RW, Ramesha CS, Sultzman LA, Lin AY, Milona N, Knopf JL: A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP. Cell. 1991 Jun 14;65(6):1043-51. [PubMed Link Image]
  2. Sharp JD, White DL, Chiou XG, Goodson T, Gamboa GC, McClure D, Burgett S, Hoskins J, Skatrud PL, Sportsman JR, et al.: Molecular cloning and expression of human Ca(2+)-sensitive cytosolic phospholipase A2. J Biol Chem. 1991 Aug 15;266(23):14850-3. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Lin LL, Wartmann M, Lin AY, Knopf JL, Seth A, Davis RJ: cPLA2 is phosphorylated and activated by MAP kinase. Cell. 1993 Jan 29;72(2):269-78. [PubMed Link Image]
  6. Sharp JD, Pickard RT, Chiou XG, Manetta JV, Kovacevic S, Miller JR, Varshavsky AD, Roberts EF, Strifler BA, Brems DN, et al.: Serine 228 is essential for catalytic activities of 85-kDa cytosolic phospholipase A2. J Biol Chem. 1994 Sep 16;269(37):23250-4. [PubMed Link Image]
  7. Borsch-Haubold AG, Bartoli F, Asselin J, Dudler T, Kramer RM, Apitz-Castro R, Watson SP, Gelb MH: Identification of the phosphorylation sites of cytosolic phospholipase A2 in agonist-stimulated human platelets and HeLa cells. J Biol Chem. 1998 Feb 20;273(8):4449-58. [PubMed Link Image]
  8. Sheridan AM, Force T, Yoon HJ, O'Leary E, Choukroun G, Taheri MR, Bonventre JV: PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production. Mol Cell Biol. 2001 Jul;21(14):4470-81. [PubMed Link Image]
  9. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  10. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  11. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  12. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  13. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  14. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  15. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  16. Perisic O, Fong S, Lynch DE, Bycroft M, Williams RL: Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2. J Biol Chem. 1998 Jan 16;273(3):1596-604. [PubMed Link Image]
  17. Xu GY, McDonagh T, Yu HA, Nalefski EA, Clark JD, Cumming DA: Solution structure and membrane interactions of the C2 domain of cytosolic phospholipase A2. J Mol Biol. 1998 Jul 17;280(3):485-500. [PubMed Link Image]
  18. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5290
Enzyme 5 Name Phospholipase A2
Enzyme 5 Synonyms
  1. Group IB phospholipase A2
  2. Phosphatidylcholine 2-acylhydrolase 1B
Enzyme 5 Gene Name PLA2G1B
Enzyme 5 Protein Sequence >Phospholipase A2 
MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPV
DELDKCCQTHDNCYDQAKKLDSCKFLLDNPYTHTYSYSCSGSAITCSSKNKECEAFICNC
DRNAAICFSKAPYNKAHKNLDTKKYCQS
Enzyme 5 Number of Residues 148
Enzyme 5 Molecular Weight 16359.5
Enzyme 5 Theoretical pI 7.91
Enzyme 5 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylesterase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
  • primary metabolic process
Component
—
Enzyme 5 General Function Involved in phospholipase A2 activity
Enzyme 5 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides
Enzyme 5 Pathways
Enzyme 5 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-15
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein Not Available
Enzyme 5 UniProtKB/Swiss-Prot ID P04054 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name PA21B_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >447 bp 
ATGAAACTCCTTGTGCTAGCTGTGCTGCTCACAGTGGCCGCCGCCGACAGCGGCATCAGC
CCTCGGGCCGTGTGGCAGTTCCGCAAAATGATCAAGTGCGTGATCCCGGGGAGTGACCCC
TTCTTGGAATACAACAACTACGGCTGCTACTGTGGCTTGGGGGGCTCAGGCACCCCCGTG
GATGAACTGGACAAGTGCTGCCAGACACATGACAACTGCTATGACCAGGCCAAGAAGCTG
GACAGCTGTAAATTTCTGCTGGACAACCCGTACACCCACACCTATTCATACTCGTGCTCT
GGCTCGGCAATCACCTGTAGCAGCAAAAACAAAGAGTGTGAGGCCTTCATTTGCAACTGC
GACCGCAACGCTGCCATCTGCTTTTCAAAAGCTCCATATAACAAGGCACACAAGAACCTG
GACACCAAGAAGTATTGTCAGAGTTGA
Enzyme 5 GenBank Gene ID M21054 Link Image
Enzyme 5 GeneCard ID PLA2G1B Link Image
Enzyme 5 GenAtlas ID PLA2G1B Link Image
Enzyme 5 HGNC ID HGNC:9030 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 12q23-q24.1
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Seilhamer JJ, Randall TL, Yamanaka M, Johnson LK: Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung. DNA. 1986 Dec;5(6):519-27. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Grataroli R, Dijkman R, Dutilh CE, van der Ouderaa F, De Haas GH, Figarella C: Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region. Eur J Biochem. 1982 Feb;122(1):111-7. [PubMed Link Image]
  6. Verheij HM, Westerman J, Sternby B, De Haas GH: The complete primary structure of phospholipase A2 from human pancreas. Biochim Biophys Acta. 1983 Sep 14;747(1-2):93-9. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5291
Enzyme 6 Name Group XIIB secretory phospholipase A2-like protein
Enzyme 6 Synonyms
  1. Group XIII secretory phospholipase A2-like protein
  2. GXIII sPLA2-like
  3. sPLA2-GXIIB
  4. GXIIB
Enzyme 6 Gene Name PLA2G12B
Enzyme 6 Protein Sequence >Group XIIB secretory phospholipase A2-like protein 
MKLASGFLVLWLSLGGGLAQSDTSPDTEESYSDWGLRHLRGSFESVNSYFDSFLELLGGK
NGVCQYRCRYGKAPMPRPGYKPQEPNGCGSYFLGLKVPESMDLGIPAMTKCCNQLDVCYD
TCGANKYRCDAKFRWCLHSICSDLKRSLGFVSKVEAACDSLVDTVFNTVWTLGCRPFMNS
QRAACICAEEEKEEL
Enzyme 6 Number of Residues 195
Enzyme 6 Molecular Weight 21658.5
Enzyme 6 Theoretical pI 5.81
Enzyme 6 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylesterase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
  • extracellular region
Enzyme 6 General Function Involved in phospholipase A2 activity
Enzyme 6 Specific Function Not known; does not seem to have catalytic activity
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-19
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 15824793 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q9BX93 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name PG12B_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >588 bp 
ATGAAGCTGGCCAGTGGCTTCTTGGTTTTGTGGCTCAGCCTTGGGGGTGGCCTGGCTCAG
AGCGACACGAGCCCTGACACGGAGGAGTCCTATTCAGACTGGGGCCTTCGGCACCTCCGG
GGAAGCTTTGAATCCGTCAATAGCTACTTCGATTCTTTTCTGGAGCTGCTGGGAGGGAAG
AATGGAGTCTGTCAGTACAGGTGCCGATATGGAAAGGCACCAATGCCCAGACCTGGCTAC
AAGCCCCAAGAGCCCAATGGCTGCGGCTCCTATTTCCTGGGTCTCAAGGTACCAGAAAGT
ATGGACTTGGGCATTCCAGCAATGACAAAGTGCTGCAACCAGCTGGATGTCTGTTATGAC
ACTTGCGGTGCCAACAAATATCGCTGTGATGCAAAATTCCGATGGTGTCTCCACTCGATC
TGCTCTGACCTTAAGCGGAGTCTGGGCTTTGTCTCCAAAGTGGAAGCAGCCTGTGATTCC
CTGGTTGACACTGTGTTCAACACCGTGTGGACCTTGGGCTGCCGCCCCTTTATGAATAGT
CAGCGGGCAGCTTGCATCTGTGCAGAGGAGGAGAAGGAAGAGTTATGA
Enzyme 6 GenBank Gene ID AF339053 Link Image
Enzyme 6 GeneCard ID PLA2G12B Link Image
Enzyme 6 GenAtlas ID PLA2G12B Link Image
Enzyme 6 HGNC ID HGNC:18555 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 10q22.1
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Rouault M, Bollinger JG, Lazdunski M, Gelb MH, Lambeau G: Novel mammalian group XII secreted phospholipase A2 lacking enzymatic activity. Biochemistry. 2003 Oct 7;42(39):11494-503. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Zhang Z, Henzel WJ: Signal peptide prediction based on analysis of experimentally verified cleavage sites. Protein Sci. 2004 Oct;13(10):2819-24. Epub 2004 Aug 31. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5292
Enzyme 7 Name Group 10 secretory phospholipase A2
Enzyme 7 Synonyms
  1. Group X secretory phospholipase A2
  2. GX sPLA2
  3. sPLA2-X
  4. Phosphatidylcholine 2-acylhydrolase 10
Enzyme 7 Gene Name PLA2G10
Enzyme 7 Protein Sequence >Group 10 secretory phospholipase A2 
MGPLPVCLPIMLLLLLPSLLLLLLLPGPGSGEASRILRVHRRGILELAGTVGCVGPRTPI
AYMKYGCFCGLGGHGQPRDAIDWCCHGHDCCYTRAEEAGCSPKTERYSWQCVNQSVLCGP
AENKCQELLCKCDQEIANCLAQTEYNLKYLFYPQFLCEPDSPKCD
Enzyme 7 Number of Residues 165
Enzyme 7 Molecular Weight 18153.0
Enzyme 7 Theoretical pI 6.46
Enzyme 7 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylesterase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
  • primary metabolic process
Component
—
Enzyme 7 General Function Involved in phospholipase A2 activity
Enzyme 7 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a powerful potency for releasing arachidonic acid from cell membrane phospholipids. Prefers phosphatidylethanolamine and phosphatidylcholine liposomes to those of phosphatidylserine
Enzyme 7 Pathways
Enzyme 7 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-31
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein Not Available
Enzyme 7 UniProtKB/Swiss-Prot ID O15496 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PA2GX_HUMAN Link Image
Enzyme 7 PDB ID 1LE7 Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >498 bp 
ATGGGGCCGCTACCTGTGTGCCTGCCAATCATGCTGCTCCTGCTACTGCCGTCGCTGCTG
CTGCTGCTGCTTCTACCTGGCCCCGGGTCCGGCGAGGCCTCCAGGATATTACGTGTGCAC
CGGCGTGGGATCCTGGAACTGGCAGGAACTGTGGGTTGTGTTGGTCCCCGAACCCCCATC
GCCTATATGAAATATGGTTGCTTTTGTGGCTTGGGAGGCCATGGCCAGCCCCGCGATGCC
ATTGACTGGTGCTGCCATGGCCACGACTGTTGTTACACTCGAGCTGAGGAGGCCGGCTGC
AGCCCCAAGACAGAGCGCTACTCCTGGCAGTGCGTCAATCAGAGCGTCCTGTGCGGACCG
GCAGAGAACAAATGCCAAGAACTGTTGTGCAAGTGTGACCAGGAGATTGCTAACTGCTTA
GCCCAAACTGAGTACAACTTAAAGTACCTCTTCTACCCCCAGTTCCTATGTGAGCCGGAC
TCGCCCAAGTGTGACTGA
Enzyme 7 GenBank Gene ID U95301 Link Image
Enzyme 7 GeneCard ID PLA2G10 Link Image
Enzyme 7 GenAtlas ID PLA2G10 Link Image
Enzyme 7 HGNC ID HGNC:9029 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 16p13.1-p12
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Cupillard L, Koumanov K, Mattei MG, Lazdunski M, Lambeau G: Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2. J Biol Chem. 1997 Jun 20;272(25):15745-52. [PubMed Link Image]
  2. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5294
Enzyme 8 Name Group IIE secretory phospholipase A2
Enzyme 8 Synonyms
  1. GIIE sPLA2
  2. sPLA2-IIE
  3. Phosphatidylcholine 2-acylhydrolase 2E
Enzyme 8 Gene Name PLA2G2E
Enzyme 8 Protein Sequence >Group IIE secretory phospholipase A2 
MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDW
CCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNL
GTYNRKYAHYPNKLCTGPTPPC
Enzyme 8 Number of Residues 142
Enzyme 8 Molecular Weight 15988.5
Enzyme 8 Theoretical pI 8.28
Enzyme 8 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylesterase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
  • primary metabolic process
Component
—
Enzyme 8 General Function Involved in phospholipase A2 activity
Enzyme 8 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a preference for arachidonic-containing phospholipids
Enzyme 8 Pathways
Enzyme 8 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-19
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein Not Available
Enzyme 8 UniProtKB/Swiss-Prot ID Q9NZK7 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name PA2GE_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >429 bp 
ATGAAATCTCCCCACGTGCTGGTGTTCCTTTGCCTCCTGGTGGCTCTGGTCACCGGGAAC
CTGGTTCAGTTTGGGGTGATGATCGAGAAGATGACAGGCAAGTCCGCCCTGCAGTACAAC
GACTATGGCTGTTACTGCGGCATCGGTGGCTCCCACTGGCCGGTGGACCAGACTGACTGG
TGCTGCCACGCCCACGACTGCTGCTACGGGCGTCTGGAGAAGCTGGGCTGTGAGCCCAAA
CTGGAAAAGTATCTTTTCTCTGTCAGCGAACGTGGCATTTTCTGCGCCGGCAGGACCACC
TGCCAGCGGCTGACCTGCGAGTGTGACAAGAGGGCTGCCCTCTGCTTTCGCCGCAACCTG
GGCACCTACAACCGCAAATATGCCCATTATCCCAACAAGCTGTGCACCGGGCCCACCCCG
CCCTGCTGA
Enzyme 8 GenBank Gene ID AF189279 Link Image
Enzyme 8 GeneCard ID PLA2G2E Link Image
Enzyme 8 GenAtlas ID PLA2G2E Link Image
Enzyme 8 HGNC ID HGNC:13414 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 1p36.13
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Suzuki N, Ishizaki J, Yokota Y, Higashino K, Ono T, Ikeda M, Fujii N, Kawamoto K, Hanasaki K: Structures, enzymatic properties, and expression of novel human and mouse secretory phospholipase A(2)s. J Biol Chem. 2000 Feb 25;275(8):5785-93. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5296
Enzyme 9 Name Group XIIA secretory phospholipase A2
Enzyme 9 Synonyms
  1. GXII sPLA2
  2. sPLA2-XII
  3. Phosphatidylcholine 2-acylhydrolase 12A
Enzyme 9 Gene Name PLA2G12A
Enzyme 9 Protein Sequence >Group XIIA secretory phospholipase A2 
MALLSRPALTLLLLLMAAVVRCQEQAQTTDWRATLKTIRNGVHKIDTYLNAALDLLGGED
GLCQYKCSDGSKPFPRYGYKPSPPNGCGSPLFGVHLNIGIPSLTKCCNQHDRCYETCGKS
KNDCDEEFQYCLSKICRDVQKTLGLTQHVQACETTVELLFDSVIHLGCKPYLDSQRAACR
CHYEEKTDL
Enzyme 9 Number of Residues 189
Enzyme 9 Molecular Weight 21067.0
Enzyme 9 Theoretical pI 7.27
Enzyme 9 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylesterase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
  • primary metabolic process
Component
  • extracellular region
Enzyme 9 General Function Involved in phospholipase A2 activity
Enzyme 9 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Does not exhibit detectable activity toward sn-2-arachidonoyl- or linoleoyl- phosphatidylcholine or -phosphatidylethanolamine
Enzyme 9 Pathways
Enzyme 9 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-22
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 12276062 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID Q9BZM1 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PG12A_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >570 bp 
ATGGCCCTGCTCTCGCGCCCCGCGCTCACCCTCCTGCTCCTCCTCATGGCCGCTGTTGTC
AGGTGCCAGGAGCAGGCCCAGACCACCGACTGGAGAGCCACCCTGAAGACCATCCGGAAC
GGCGTTCATAAGATAGACACGTACCTGAACGCCGCCTTGGACCTCCTGGGAGGCGAGGAC
GGTCTCTGCCAGTATAAATGCAGTGACGGATCTAAGCCTTTCCCACGTTATGGTTATAAA
CCCTCCCCACCGAATGGATGTGGCTCTCCACTGTTTGGTGTTCATCTTAACATTGGTATC
CCTTCCCTGACAAAGTGTTGCAACCAACACGACAGGTGCTATGAGACCTGTGGCAAAAGC
AAGAATGACTGTGATGAAGAATTCCAGTATTGCCTCTCCAAGATCTGCCGAGATGTACAG
AAAACACTAGGACTAACTCAGCATGTTCAGGCATGTGAAACAACAGTGGAGCTCTTGTTT
GACAGTGTTATACATTTAGGTTGTAAACCATATCTGGACAGCCAACGAGCCGCATGCAGG
TGTCATTATGAAGAAAAAACTGATCTTTAA
Enzyme 9 GenBank Gene ID AF306567 Link Image
Enzyme 9 GeneCard ID PLA2G12A Link Image
Enzyme 9 GenAtlas ID PLA2G12A Link Image
Enzyme 9 HGNC ID HGNC:18554 Link Image
Enzyme 9 Chromosome Location 4
Enzyme 9 Locus 4q25
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Gelb MH, Valentin E, Ghomashchi F, Lazdunski M, Lambeau G: Cloning and recombinant expression of a structurally novel human secreted phospholipase A2. J Biol Chem. 2000 Dec 22;275(51):39823-6. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Murakami M, Masuda S, Shimbara S, Bezzine S, Lazdunski M, Lambeau G, Gelb MH, Matsukura S, Kokubu F, Adachi M, Kudo I: Cellular arachidonate-releasing function of novel classes of secretory phospholipase A2s (groups III and XII). J Biol Chem. 2003 Mar 21;278(12):10657-67. Epub 2003 Jan 8. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5297
Enzyme 10 Name 85 kDa calcium-independent phospholipase A2
Enzyme 10 Synonyms
  1. CaI-PLA2
  2. iPLA2
  3. Group VI phospholipase A2
  4. GVI PLA2
Enzyme 10 Gene Name PLA2G6
Enzyme 10 Protein Sequence >85 kDa calcium-independent phospholipase A2 
MQFFGRLVNTFSGVTNLFSNPFRVKEVAVADYTSSDRVREEGQLILFQNTPNRTWDCVLV
NPRNSQSGFRLFQLELEADALVNFHQYSSQLLPFYESSPQVLHTEVLQHLTDLIRNHPSW
SVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMD
VTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLL
LCNARCNIMGPNGYPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMA
RMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK
DNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILTLLRTVGAEYCFPPIHG
VPAEQGSAAPHHPFSLERAQPPPISLNNLELQDLMHISRARKPAFILGSMRDEKRTHDHL
LCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGM
YFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPAELHLFR
NYDAPETVREPRFNQNVNLRPPAQPSDQLVWRAARSSGAAPTYFRPNGRFLDGGLLANNP
TLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAKT
VFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVN
ALWETEVYIYEHREEFQKLIQLLLSP
Enzyme 10 Number of Residues 806
Enzyme 10 Molecular Weight 89902.3
Enzyme 10 Theoretical pI 7.28
Enzyme 10 GO Classification
Function
—
Process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
Component
—
Enzyme 10 General Function Involved in metabolic process
Enzyme 10 Specific Function Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity
Enzyme 10 Pathways
Enzyme 10 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 3142700 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID O60733 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PA2G6_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >2421 bp 
ATGCAGTTCTTTGGCCGCCTGGTCAATACCTTCAGTGGCGTCACCAACTTGTTCTCTAAC
CCATTCCGGGTGAAGGAGGTGGCTGTGGCCGACTACACCTCGAGTGACCGAGTTCGGGAG
GAAGGGCAGCTGATTCTGTTCCAGAACACTCCCAACCGCACCTGGGACTGCGTCCTGGTC
AACCCCAGGAACTCACAGAGTGGATTCCGACTCTTCCAGCTGGAGTTGGAGGCTGACGCC
CTAGTGAATTTCCATCAGTATTCTTCCCAGCTGCTACCCTTCTATGAGAGCTCCCCTCAG
GTCCTGCACACTGAGGTCCTGCAGCACCTGACCGACCTCATCCGTAACCACCCCAGCTGG
TCAGTGGCCCACCTGGCTGTGGAGCTAGGGATCCGCGAGTGCTTCCATCACAGCCGTATC
ATCAGCTGTGCCAATTGCGCGGAGAACGAGGAGGGCTGCACACCCCTGCACCTGGCCTGC
CGCAAGGGTGATGGGGAGATCCTGGTGGAGCTGGTGCAGTACTGCCACACTCAGATGGAT
GTCACCGACTACAAGGGAGAGACCGTCTTCCATTATGCTGTCCAGGGTGACAATTCTCAG
GTGCTGCAGCTCCTTGGAAGGAACGCAGTGGCTGGCCTGAACCAGGTGAATAACCAAGGG
CTGACCCCGCTGCACCTGGCCTGCCAGCTGGGGAAGCAGGAGATGGTCCGCGTGCTGCTG
CTGTGCAATGCTCGGTGCAACATCATGGGCCCCAACGGCTACCCCATCCACTCGGCCATG
AAGTTCTCTCAGAAGGGGTGTGCGGAGATGATCATCAGCATGGACAGCAGCCAGATCCAC
AGCAAAGACCCCCGTTACGGAGCCAGCCCCCTCCACTGGGCCAAGAACGCAGAGATGGCC
CGCATGCTGCTGAAACGGGGCTGCAACGTGAACAGCACCAGCTCCGCGGGGAACACGGCC
CTGCACGTGGCGGTGATGCGCAACCGCTTCGACTGTGCCATAGTGCTGCTGACCCACGGG
GCCAACGCGGATGCCCGCGGAGAGCACGGCAACACCCCGCTGCACCTGGCCATGTCGAAA
GACAACGTGGAGATGATCAAGGCCCTCATCGTGTTCGGAGCAGAAGTGGACACCCCGAAT
GACTTTGGGGAGACTCCTACATTCCTAGCCTCCAAAATCGGCAGACTTGTCACCAGGAAG
GCGATCTTGACTCTGCTGAGAACCGTGGGGGCCGAATACTGCTTCCCACCCATCCACGGG
GTCCCCGCGGAGCAGGGCTCTGCAGCGCCACATCATCCCTTCTCCCTGGAAAGAGCTCAG
CCCCCACCGATCAGCCTAAACAACCTAGAACTACAGGATCTCATGCACATCTCACGGGCC
CGGAAGCCAGCGTTCATCCTGGGCTCCATGAGGGACGAGAAGCGGACCCACGACCACCTG
CTGTGCCTGGATGGAGGAGGAGTGAAAGGCCTCATCATCATCCAGCTCCTCATCGCCATC
GAGAAGGCCTCGGGTGTGGCCACCAAGGACCTGTTTGACTGGGTGGCGGGCACCAGCACT
GGAGGCATCCTGGCCCTGGCCATTCTGCACAGTAAGTCCATGGCCTACATGCGCGGCATG
TACTTTCGCATGAAGGATGAGGTGTTCCGGGGCTCCAGGCCCTACGAGTCGGGGCCCCTG
GAGGAGTTCCTGAAGCGGGAGTTTGGGGAGCACACCAAGATGACGGACGTCAGGAAACCC
AAGGTGATGCTGACAGGGACACTGTCTGACCGGCAGCCGGCTGAACTCCACCTCTTCCGG
AACTACGATGCTCCAGAAACTGTCCGGGAGCCTCGTTTCAACCAGAACGTTAACCTCAGG
CCTCCAGCTCAGCCCTCAGACCAGCTGGTGTGGCGGGCGGCCCGAAGCAGCGGGGCAGCT
CCTACTTACTTCCGACCCAATGGGCGCTTCCTGGACGGTGGGCTGCTGGCCAACAACCCC
ACGCTGGATGCCATGACCGAGATCCATGAGTACAATCAGGACCTGATCCGCAAGGGTCAG
GCCAACAAGGTGAAGAAACTCTCCATCGTTGTCTCCCTGGGGACAGGGAGGTCCCCACAA
GTGCCTGTGACCTGTGTGGATGTCTTCCGTCCCAGCAACCCCTGGGAGCTGGCCAAGACT
GTTTTTGGGGCCAAGGAACTGGGCAAGATGGTGGTGGACTGTTGCACGGATCCAGACGGG
CGGGCTGTGGACCGGGCACGGGCCTGGTGCGAGATGGTCGGCATCCAGTACTTCAGATTG
AACCCCCAGCTGGGGACGGACATCATGCTGGATGAGGTCAGTGACACAGTGCTGGTCAAC
GCCCTCTGGGAGACCGAGGTCTACATCTATGAGCACCGCGAGGAGTTCCAGAAGCTCATC
CACCTGCTGCTCTCACCCTGA
Enzyme 10 GenBank Gene ID AF064594 Link Image
Enzyme 10 GeneCard ID PLA2G6 Link Image
Enzyme 10 GenAtlas ID PLA2G6 Link Image
Enzyme 10 HGNC ID HGNC:9039 Link Image
Enzyme 10 Chromosome Location 2
Enzyme 10 Locus 22q13.1
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Larsson PK, Claesson HE, Kennedy BP: Multiple splice variants of the human calcium-independent phospholipase A2 and their effect on enzyme activity. J Biol Chem. 1998 Jan 2;273(1):207-14. [PubMed Link Image]
  2. Ma Z, Wang X, Nowatzke W, Ramanadham S, Turk J: Human pancreatic islets express mRNA species encoding two distinct catalytically active isoforms of group VI phospholipase A2 (iPLA2) that arise from an exon-skipping mechanism of alternative splicing of the transcript from the iPLA2 gene on chromosome 22q13.1. J Biol Chem. 1999 Apr 2;274(14):9607-16. [PubMed Link Image]
  3. Larsson Forsell PK, Kennedy BP, Claesson HE: The human calcium-independent phospholipase A2 gene multiple enzymes with distinct properties from a single gene. Eur J Biochem. 1999 Jun;262(2):575-85. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  7. 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]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. Malhotra A, Edelman-Novemsky I, Xu Y, Plesken H, Ma J, Schlame M, Ren M: Role of calcium-independent phospholipase A2 in the pathogenesis of Barth syndrome. Proc Natl Acad Sci U S A. 2009 Feb 17;106(7):2337-41. Epub 2009 Jan 21. [PubMed Link Image]
  10. Khateeb S, Flusser H, Ofir R, Shelef I, Narkis G, Vardi G, Shorer Z, Levy R, Galil A, Elbedour K, Birk OS: PLA2G6 mutation underlies infantile neuroaxonal dystrophy. Am J Hum Genet. 2006 Nov;79(5):942-8. Epub 2006 Sep 19. [PubMed Link Image]
  11. Morgan NV, Westaway SK, Morton JE, Gregory A, Gissen P, Sonek S, Cangul H, Coryell J, Canham N, Nardocci N, Zorzi G, Pasha S, Rodriguez D, Desguerre I, Mubaidin A, Bertini E, Trembath RC, Simonati A, Schanen C, Johnson CA, Levinson B, Woods CG, Wilmot B, Kramer P, Gitschier J, Maher ER, Hayflick SJ: PLA2G6, encoding a phospholipase A2, is mutated in neurodegenerative disorders with high brain iron. Nat Genet. 2006 Jul;38(7):752-4. Epub 2006 Jun 18. [PubMed Link Image]
  12. Paisan-Ruiz C, Bhatia KP, Li A, Hernandez D, Davis M, Wood NW, Hardy J, Houlden H, Singleton A, Schneider SA: Characterization of PLA2G6 as a locus for dystonia-parkinsonism. Ann Neurol. 2009 Jan;65(1):19-23. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5301
Enzyme 11 Name Phospholipase A2, membrane associated
Enzyme 11 Synonyms
  1. GIIC sPLA2
  2. Group IIA phospholipase A2
  3. Non-pancreatic secretory phospholipase A2
  4. NPS-PLA2
  5. Phosphatidylcholine 2-acylhydrolase 2A
Enzyme 11 Gene Name PLA2G2A
Enzyme 11 Protein Sequence >Phospholipase A2, membrane associated 
MKTLLLLAVIMIFGLLQAHGNLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDAT
DRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFAR
NKTTYNKKYQYYSNKHCRGSTPRC
Enzyme 11 Number of Residues 144
Enzyme 11 Molecular Weight 16082.5
Enzyme 11 Theoretical pI 9.51
Enzyme 11 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylesterase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
  • primary metabolic process
Component
—
Enzyme 11 General Function Involved in phospholipase A2 activity
Enzyme 11 Specific Function Thought to participate in the regulation of the phospholipid metabolism in biomembranes including eicosanoid biosynthesis. Catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides
Enzyme 11 Pathways
Enzyme 11 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-20
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein Not Available
Enzyme 11 UniProtKB/Swiss-Prot ID P14555 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name PA2GA_HUMAN Link Image
Enzyme 11 PDB ID 1DB4 Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >435 bp 
ATGAAGACCCTCCTACTGTTGGCAGTGATCATGATCTTTGGCCTACTGCAGGCCCATGGG
AATTTGGTGAATTTCCACAGAATGATCAAGTTGACGACAGGAAAGGAAGCCGCACTCAGT
TATGGCTTCTACGGCTGCCACTGTGGCGTGGGTGGCAGAGGATCCCCCAAGGATGCAACG
GATCGCTGCTGTGTCACTCATGACTGTTGCTACAAACGTCTGGAGAAACGTGGATGTGGC
ACCAAATTTCTGAGCTACAAGTTTAGCAACTCGGGGAGCAGAATCACCTGTGCAAAACAG
GACTCCTGCAGAAGTCAACTGTGTGAGTGTGATAAGGCTGCTGCCACCTGTTTTGCTAGA
AACAAGACGACCTACAATAAAAAGTACCAGTACTATTCCAATAAACACTGCAGAGGGAGC
ACCCCTCGTTGCTGA
Enzyme 11 GenBank Gene ID M22430 Link Image
Enzyme 11 GeneCard ID PLA2G2A Link Image
Enzyme 11 GenAtlas ID PLA2G2A Link Image
Enzyme 11 HGNC ID HGNC:9031 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 1p35
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Seilhamer JJ, Pruzanski W, Vadas P, Plant S, Miller JA, Kloss J, Johnson LK: Cloning and recombinant expression of phospholipase A2 present in rheumatoid arthritic synovial fluid. J Biol Chem. 1989 Apr 5;264(10):5335-8. [PubMed Link Image]
  2. Kramer RM, Hession C, Johansen B, Hayes G, McGray P, Chow EP, Tizard R, Pepinsky RB: Structure and properties of a human non-pancreatic phospholipase A2. J Biol Chem. 1989 Apr 5;264(10):5768-75. [PubMed Link Image]
  3. Kramer RM, Johansen B, Hession C, Pepinsky RB: Structure and properties of a secretable phospholipase A2 from human platelets. Adv Exp Med Biol. 1990;275:35-53. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Kanda A, Ono T, Yoshida N, Tojo H, Okamoto M: The primary structure of a membrane-associated phospholipase A2 from human spleen. Biochem Biophys Res Commun. 1989 Aug 30;163(1):42-8. [PubMed Link Image]
  8. Hara S, Kudo I, Matsuta K, Miyamoto T, Inoue K: Amino acid composition and NH2-terminal amino acid sequence of human phospholipase A2 purified from rheumatoid synovial fluid. J Biochem (Tokyo). 1988 Sep;104(3):326-8. [PubMed Link Image]
  9. Lai CY, Wada K: Phospholipase A2 from human synovial fluid: purification and structural homology to the placental enzyme. Biochem Biophys Res Commun. 1988 Dec 15;157(2):488-93. [PubMed Link Image]
  10. Minami T, Tojo H, Shinomura Y, Matsuzawa Y, Okamoto M: Purification and characterization of a phospholipase A2 from human ileal mucosa. Biochim Biophys Acta. 1993 Oct 13;1170(2):125-30. [PubMed Link Image]
  11. Wery JP, Schevitz RW, Clawson DK, Bobbitt JL, Dow ER, Gamboa G, Goodson T Jr, Hermann RB, Kramer RM, McClure DB, et al.: Structure of recombinant human rheumatoid arthritic synovial fluid phospholipase A2 at 2.2 A resolution. Nature. 1991 Jul 4;352(6330):79-82. [PubMed Link Image]
  12. Scott DL, White SP, Browning JL, Rosa JJ, Gelb MH, Sigler PB: Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate. Science. 1991 Nov 15;254(5034):1007-10. [PubMed Link Image]
  13. Schevitz RW, Bach NJ, Carlson DG, Chirgadze NY, Clawson DK, Dillard RD, Draheim SE, Hartley LW, Jones ND, Mihelich ED, et al.: Structure-based design of the first potent and selective inhibitor of human non-pancreatic secretory phospholipase A2. Nat Struct Biol. 1995 Jun;2(6):458-65. [PubMed Link Image]
  14. Kitadokoro K, Hagishita S, Sato T, Ohtani M, Miki K: Crystal structure of human secretory phospholipase A2-IIA complex with the potent indolizine inhibitor 120-1032. J Biochem (Tokyo). 1998 Apr;123(4):619-23. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5302
Enzyme 12 Name Group IID secretory phospholipase A2
Enzyme 12 Synonyms
  1. GIID sPLA2
  2. sPLA2-IID
  3. PLA2IID
  4. Phosphatidylcholine 2-acylhydrolase 2D
  5. Secretory-type PLA, stroma-associated homolog
Enzyme 12 Gene Name PLA2G2D
Enzyme 12 Protein Sequence >Group IID secretory phospholipase A2 
MELALLCGLVVMAGVIPIQGGILNLNKMVKQVTGKMPILSYWPYGCHCGLGGRGQPKDAT
DWCCQTHDCCYDHLKTQGCSIYKDYYRYNFSQGNIHCSDKGSWCEQQLCACDKEVAFCLK
RNLDTYQKRLRFYWRPHCRGQTPGC
Enzyme 12 Number of Residues 145
Enzyme 12 Molecular Weight 16546.1
Enzyme 12 Theoretical pI 8.28
Enzyme 12 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylesterase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • metal ion binding
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
  • primary metabolic process
Component
—
Enzyme 12 General Function Involved in phospholipase A2 activity
Enzyme 12 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. L-alpha-1-palmitoyl-2- linoleoyl phosphatidylethanolamine is more efficiently hydrolyzed than the other phospholipids examined
Enzyme 12 Pathways
Enzyme 12 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-20
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 5771420 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q9UNK4 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name PA2GD_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >438 bp 
ATGGAACTTGCACTGCTGTGTGGGCTGGTGGTGATGGCTGGTGTGATTCCAATCCAGGGC
GGGATCCTGAACCTGAACAAGATGGTCAAGCAAGTGACTGGGAAAATGCCCATCCTCTCC
TACTGGCCCTACGGCTGTCACTGCGGACTAGGTGGCAGAGGCCAACCCAAAGATGCCACG
GACTGGTGCTGCCAGACCCATGACTGCTGCTATGACCACCTGAAGACCCAGGGGTGCGGC
ATCTACAAGGACTATTACAGATACAACTTTTCCCAGGGGAACATCCACTGCTCTGACAAG
GGAAGCTGGTGTGAGCAGCAGCTGTGTGCCTGTGACAAGGAGGTGGCCTTCTGCCTGAAG
CGCAACCTGGACACCTACCAGAAGCGACTGCGTTTCTACTGGCGGCCCCACTGCCGGGGG
CAGACCCCTGGGTGCTAG
Enzyme 12 GenBank Gene ID AF112982 Link Image
Enzyme 12 GeneCard ID PLA2G2D Link Image
Enzyme 12 GenAtlas ID PLA2G2D Link Image
Enzyme 12 HGNC ID HGNC:9033 Link Image
Enzyme 12 Chromosome Location 1
Enzyme 12 Locus 1p36.12
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Ishizaki J, Suzuki N, Higashino K, Yokota Y, Ono T, Kawamoto K, Fujii N, Arita H, Hanasaki K: Cloning and characterization of novel mouse and human secretory phospholipase A(2)s. J Biol Chem. 1999 Aug 27;274(35):24973-9. [PubMed Link Image]
  2. Shakhov AN, Rubtsov AV, Lyakhov IG, Tumanov AV, Nedospasov SA: SPLASH (PLA2IID), a novel member of phospholipase A2 family, is associated with lymphotoxin deficiency. Genes Immun. 2000 Feb;1(3):191-9. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5313
Enzyme 13 Name Ectonucleoside triphosphate diphosphohydrolase 1
Enzyme 13 Synonyms
  1. NTPDase 1
  2. Ecto-ATP diphosphohydrolase 1
  3. Ecto-ATPDase 1
  4. Ecto-ATPase 1
  5. Ecto-apyrase
  6. Lymphoid cell activation antigen
  7. CD39 antigen
Enzyme 13 Gene Name ENTPD1
Enzyme 13 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 1 
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
Enzyme 13 Number of Residues 510
Enzyme 13 Molecular Weight 57964.1
Enzyme 13 Theoretical pI 6.29
Enzyme 13 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 13 General Function Involved in hydrolase activity
Enzyme 13 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 13 Pathways
Enzyme 13 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • 17-37 479-499
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 45580700 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P49961 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name ENTP1_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 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 13 GenBank Gene ID NM_001776.5 Link Image
Enzyme 13 GeneCard ID ENTPD1 Link Image
Enzyme 13 GenAtlas ID ENTPD1 Link Image
Enzyme 13 HGNC ID HGNC:3363 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 10q24
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Maliszewski CR, Delespesse GJ, Schoenborn MA, Armitage RJ, Fanslow WC, Nakajima T, Baker E, Sutherland GR, Poindexter K, Birks C, et al.: The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. J Immunol. 1994 Oct 15;153(8):3574-83. [PubMed Link Image]
  2. Robson SC, Kaczmarek E, Siegel JB, Candinas D, Koziak K, Millan M, Hancock WW, Bach FH: Loss of ATP diphosphohydrolase activity with endothelial cell activation. J Exp Med. 1997 Jan 6;185(1):153-63. [PubMed Link Image]
  3. Matsumoto M, Sakurai Y, Kokubo T, Yagi H, Makita K, Matsui T, Titani K, Fujimura Y, Narita N: The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II. FEBS Lett. 1999 Jun 25;453(3):335-40. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  6. Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O: Purification and properties of human placental ATP diphosphohydrolase. Eur J Biochem. 1995 Nov 15;234(1):66-74. [PubMed Link Image]
  7. Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y: Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. Int J Hematol. 1998 Oct;68(3):297-310. [PubMed Link Image]
  8. Kaczmarek E, Koziak K, Sevigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC: Identification and characterization of CD39/vascular ATP diphosphohydrolase. J Biol Chem. 1996 Dec 20;271(51):33116-22. [PubMed Link Image]
  9. Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed Link Image]
  10. Koziak K, Kaczmarek E, Kittel A, Sevigny J, Blusztajn JK, Schulte Am Esch J 2nd, Imai M, Guckelberger O, Goepfert C, Qawi I, Robson SC: Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae. J Biol Chem. 2000 Jan 21;275(3):2057-62. [PubMed Link Image]
  11. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed Link Image]
  12. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5314
Enzyme 14 Name Soluble calcium-activated nucleotidase 1
Enzyme 14 Synonyms
  1. SCAN-1
  2. Apyrase homolog
  3. Putative MAPK-activating protein PM09
  4. Putative NF-kappa-B-activating protein 107
Enzyme 14 Gene Name CANT1
Enzyme 14 Protein Sequence >Soluble calcium-activated nucleotidase 1 
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
Enzyme 14 Number of Residues 401
Enzyme 14 Molecular Weight 44839.2
Enzyme 14 Theoretical pI 5.98
Enzyme 14 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • ion binding
  • metal ion binding
  • pyrophosphatase activity
Process
—
Component
—
Enzyme 14 General Function Involved in calcium ion binding
Enzyme 14 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 14 Pathways
Enzyme 14 Reactions
  • a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • 45-62
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 229577440 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q8WVQ1 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name CANT1_HUMAN Link Image
Enzyme 14 PDB ID 1S1D Link Image
Enzyme 14 PDB File Show
Enzyme 14 3D Structure
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1206 bp 
ATGCCCGTGCAGCTGTCTGAGCACCCGGAATGGAATGAGTCTATGCACTCCCTCCGGATC
AGTGTGGGGGGCCTTCCTGTGCTGGCGTCCATGACCAAGGCCGCGGACCCCCGCTTCCGC
CCCCGCTGGAAGGTGATCCTGACGTTCTTTGTGGGTGCTGCCATCCTCTGGCTGCTCTGC
TCCCACCGCCCGGCCCCCGGCAGGCCCCCCACCCACAATGCACACAACTGGAGGCTCGGC
CAGGCGCCCGCCAACTGGTACAATGACACCTACCCCCTGTCTCCCCCACAAAGGACACCG
GCTGGGATTCGGTATCGAATCGCAGTTATCGCAGACCTGGACACAGAGTCAAGGGCCCAA
GAGGAAAACACCTGGTTCAGTTACCTGAAAAAGGGCTACCTGACCCTGTCAGACAGTGGG
GACAAGGTGGCCGTGGAATGGGACAAAGACCATGGGGTCCTGGAGTCCCACCTGGCGGAG
AAGGGGAGAGGCATGGAGCTATCCGACCTGATTGTTTTCAATGGGAAACTCTACTCCGTG
GATGACCGGACGGGGGTCGTCTACCAGATCGAAGGCAGCAAAGCCGTGCCCTGGGTGATT
CTGTCCGACGGCGACGGCACCGTGGAGAAAGGCTTCAAGGCCGAATGGCTGGCAGTGAAG
GACGAGCGTCTGTACGTGGGCGGCCTGGGCAAGGAGTGGACGACCACTACGGGTGATGTG
GTGAACGAGAACCCGGAGTGGGTGAAGGTGGTGGGCTACAAGGGCAGCGTGGACCACGAG
AACTGGGTGTCCAACTACAACGCCCTGCGGGCTGCTGCCGGCATCCAGCCGCCAGGCTAC
CTCATCCATGAGTCTGCCTGCTGGAGTGACACGCTGCAGCGCTGGTTCTTCCTGCCGCGC
CGCGCCAGCCAGGAGCGCTACAGCGAGAAGGACGACGAGCGCAAGGGCGCCAACCTGCTG
CTGAGCGCCTCCCCTGACTTCGGCGACATCGCTGTGAGCCACGTCGGGGCGGTGGTCCCC
ACTCACGGCTTCTCGTCCTTCAAGTTCATCCCCAACACCGACGACCAGATCATTGTGGCC
CTCAAATCCGAGGAGGACAGCGGCAGAGTCGCCTCCTACATCATGGCCTTCACGCTGGAC
GGGCGCTTCCTGTTGCCGGAGACCAAGATCGGAAGCGTGAAATACGAAGGCATCGAGTTC
ATTTAA
Enzyme 14 GenBank Gene ID NM_001159772.1 Link Image
Enzyme 14 GeneCard ID CANT1 Link Image
Enzyme 14 GenAtlas ID CANT1 Link Image
Enzyme 14 HGNC ID HGNC:19721 Link Image
Enzyme 14 Chromosome Location 1
Enzyme 14 Locus 17q25.3
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Smith TM, Hicks-Berger CA, Kim S, Kirley TL: Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases. Arch Biochem Biophys. 2002 Oct 1;406(1):105-15. [PubMed Link Image]
  2. Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S: Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003 May 22;22(21):3307-18. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Failer BU, Braun N, Zimmermann H: Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J Biol Chem. 2002 Oct 4;277(40):36978-86. Epub 2002 Aug 6. [PubMed Link Image]
  6. Yang M, Kirley TL: Site-directed mutagenesis of human soluble calcium-activated nucleotidase 1 (hSCAN-1): identification of residues essential for enzyme activity and the Ca(2+)-induced conformational change. Biochemistry. 2004 Jul 20;43(28):9185-94. [PubMed Link Image]
  7. Dai J, Liu J, Deng Y, Smith TM, Lu M: Structure and protein design of a human platelet function inhibitor. Cell. 2004 Mar 5;116(5):649-59. [PubMed Link Image]
  8. Huber C, Oules B, Bertoli M, Chami M, Fradin M, Alanay Y, Al-Gazali LI, Ausems MG, Bitoun P, Cavalcanti DP, Krebs A, Le Merrer M, Mortier G, Shafeghati Y, Superti-Furga A, Robertson SP, Le Goff C, Muda AO, Paterlini-Brechot P, Munnich A, Cormier-Daire V: Identification of CANT1 mutations in Desbuquois dysplasia. Am J Hum Genet. 2009 Nov;85(5):706-10. Epub 2009 Oct 22. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5318
Enzyme 15 Name Ectonucleoside triphosphate diphosphohydrolase 3
Enzyme 15 Synonyms
  1. NTPDase 3
  2. CD39 antigen-like 3
  3. Ecto-ATP diphosphohydrolase 3
  4. Ecto-ATPDase 3
  5. Ecto-ATPase 3
  6. Ecto-apyrase 3
  7. HB6
Enzyme 15 Gene Name ENTPD3
Enzyme 15 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 3 
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
Enzyme 15 Number of Residues 529
Enzyme 15 Molecular Weight 59104.8
Enzyme 15 Theoretical pI 6.40
Enzyme 15 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 15 General Function Involved in hydrolase activity
Enzyme 15 Specific Function Has a threefold preference for the hydrolysis of ATP over ADP
Enzyme 15 Pathways
Enzyme 15 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • 23-43 486-506
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 13817037 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID O75355 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name ENTP3_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1590 bp 
ATGTTCACTGTGCTGACCCGCCAACCATGTGAGCAAGCAGGCCTCAAGGCCCTCTACCGA
ACTCCAACCATCATTGCCTTGGTGGTCTTGCTTGTGAGTATTGTGGTACTTGTGAGTATC
ACTGTCATCCAGATCCACAAGCAAGAGGTCCTCCCTCCAGGACTGAAGTATGGTATTGTG
CTGGATGCCGGGTCTTCAAGAACCACAGTCTACGTGTATCAATGGCCAGCAGAAAAAGAG
AATAATACCGGAGTGGTCAGTCAAACCTTCAAATGTAGTGTGAAAGGCTCTGGAATCTCC
AGCTATGGAAATAACCCCCAAGATGTCCCCAGAGCCTTTGAGGAGTGTATGCAAAAAGTC
AAGGGGCAGGTTCCATCCCACCTCCACGGATCCACCCCCATTCACCTGGGAGCCACGGCT
GGGATGCGCTTGCTGAGGTTGCAAAATGAAACAGCAGCTAATGAAGTCCTTGAAAGCATC
CAAAGCTACTTCAAGTCCCAGCCCTTTGACTTTAGGGGTGCTCAAATCATTTCTGGGCAA
GAAGAAGGGGTATATGGATGGATTACAGCCAACTATTTAATGGGAAATTTCCTGGAGAAG
AACCTGTGGCACATGTGGGTGCACCCGCATGGAGTGGAAACCACGGGTGCCCTGGACTTA
GGTGGTGCCTCCACCCAAATATCCTTCGTGGCAGGAGAGAAGATGGATCTGAACACCAGC
GACATCATGCAGGTGTCCCTGTATGGCTACGTATACACGCTCTACACACACAGCTTCCAG
TGCTATGGCCGGAATGAGGCTGAGAAGAAGTTTCTGGCAATGCTCCTGCAGAATTCTCCT
ACCAAAAACCATCTCACCAATCCCTGTTACCCTCGGGATTATAGCATCAGCTTCACCATG
GGCCATGTATTTGATAGCCTGTGCACTGTGGACCAGAGGCCAGAAAGTTATAACCCCAAT
GATGTCATCACTTTTGAAGGAACTGGGGACCCATCTCTGTGTAAGGAGAAGGTGGCTTCC
ATATTTGACTTCAAAGCTTGCCATGATCAAGAAACCTGTTCTTTTGATGGGGTTTATCAG
CCAAAGATTAAAGGGCCATTTGTGGCTTTTGCAGGATTCTACTACACAGCCAGTGCTTTA
AATCTTTCAGGTAGCTTTTCCCTGGACACCTTCAACTCCAGCACCTGGAATTTCTGCTCA
CAGAATTGGAGTCAGCTCCCACTGCTGCTCCCCAAATTTGATGAGGTATATGCCCGCTCT
TACTGCTTCTCAGCCAACTACATCTACCACTTGTTTGTGAACGGTTACAAATTCACAGAG
GAGACTTGGCCCCAAATACACTTTGAAAAAGAAGTGGGGAATAGCAGCATAGCCTGGTCT
CTTGGCTACATGCTCAGCCTGACCAACCAGATCCCAGCTGAAAGCCCTCTGATCCGTCTG
CCCATAGAACCACCTGTCTTTGTGGGCACCCTCGCTTTCTTCACAGCGGCAGCCTTGCTG
TGTCTGGCATTTCTTGCATACCTGTGTTCAGCAACCAGAAGAAAGAGGCACTCCGAGCAT
GCCTTTGACCATGCAGTGGATTCTGACTGA
Enzyme 15 GenBank Gene ID AF034840 Link Image
Enzyme 15 GeneCard ID ENTPD3 Link Image
Enzyme 15 GenAtlas ID ENTPD3 Link Image
Enzyme 15 HGNC ID HGNC:3365 Link Image
Enzyme 15 Chromosome Location 3
Enzyme 15 Locus 3p21.3
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Chadwick BP, Frischauf AM: The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster. Genomics. 1998 Jun 15;50(3):357-67. [PubMed Link Image]
  2. Smith TM, Kirley TL: Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases1. Biochim Biophys Acta. 1998 Jul 28;1386(1):65-78. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Smith TM, Lewis Carl SA, Kirley TL: Mutagenesis of two conserved tryptophan residues of the E-type ATPases: inactivation and conversion of an ecto-apyrase to an ecto-NTPase. Biochemistry. 1999 May 4;38(18):5849-57. [PubMed Link Image]
  5. Yang F, Hicks-Berger CA, Smith TM, Kirley TL: Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: the importance of residues in the apyrase conserved regions. Biochemistry. 2001 Apr 3;40(13):3943-50. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5429
Enzyme 16 Name Glycerol-3-phosphate dehydrogenase, mitochondrial
Enzyme 16 Synonyms
  1. GPD-M
  2. GPDH-M
  3. mtGPD
Enzyme 16 Gene Name GPD2
Enzyme 16 Protein Sequence >Glycerol-3-phosphate dehydrogenase, mitochondrial 
MAFQKAVKGTILVGGGALATVLGLSQFAHYRRKQMNLAYVKAADCISEPVNREPPSREAQ
LLTLQNTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVR
YLQKAIMKLDIEQYRMVKEALHERANLLEIAPHLSAPLPIMLPVYKWWQLPYYWVGIKLY
DLVAGSNCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYG
AATANYMEVVSLLKKTDPQTGKVRVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKM
DDKDAAAICQPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTPTD
VTHHPIPSEEDINFILNEVRNYLSCDVEVRRGDVLAAWSGIRPLVTDPKSADTQSISRNH
VVDISESGLITIAGGKWTTYRSMAEDTINAAVKTHNLKAGPSRTVGLFLQGGKDWSPTLY
IRLVQDYGLESEVAQHLAATYGDKAFEVAKMASVTGKRWPIVGVRLVSEFPYIEAEVKYG
IKEYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDYKKQEQLETARKFLY
YEMGYKSRSEQLTDRSEISLLPSDIDRYKKRFHKFDADQKGFITIVDVQRVLESINVQMD
ENTLHEILNEVDLNKNGQVELNEFLQLMSAIQKGRVSGSRLAILMKTAEENLDRRVPIPV
DRSCGGL
Enzyme 16 Number of Residues 727
Enzyme 16 Molecular Weight 80852.0
Enzyme 16 Theoretical pI 7.77
Enzyme 16 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • glycerol-3-phosphate dehydrogenase activity
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, quinone or similar compound as acceptor
Process
  • alcohol metabolic process
  • alditol metabolic process
  • glycerol metabolic process
  • glycerol-3-phosphate metabolic process
  • metabolic process
  • oxidation reduction
  • polyol metabolic process
  • small molecule metabolic process
Component
  • glycerol-3-phosphate dehydrogenase complex
  • macromolecular complex
  • protein complex
Enzyme 16 General Function Involved in calcium ion binding
Enzyme 16 Specific Function sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol
Enzyme 16 Pathways
Enzyme 16 Reactions
  • sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol [RN:R00849]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 285002233 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID P43304 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name GPDM_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >2184 bp 
ATGGCATTTCAAAAGGCAGTGAAAGGGACGATTCTTGTTGGAGGAGGTGCTCTTGCAACT
GTTTTAGGACTTTCTCAGTTTGCTCATTACAGAAGGAAACAAATGAACCTGGCCTATGTT
AAAGCAGCAGACTGCATTTCAGAACCAGTTAACAGGGAGCCTCCTTCCAGAGAAGCTCAG
CTACTGACTTTGCAAAACACATCTGAATTTGATATCCTTGTTATTGGAGGAGGAGCAACA
GGAAGTGGCTGTGCGCTAGATGCTGTCACCAGAGGACTAAAAACAGCCCTTGTAGAAAGA
GATGATTTCTCATCAGGGACCAGCAGCAGAAGCACTAAATTGATCCATGGTGGTGTGAGA
TATCTGCAGAAGGCCATCATGAAGTTGGATATTGAGCAGTATAGGATGGTAAAAGAAGCC
CTTCATGAGCGTGCCAACCTGCTAGAAATTGCTCCCCATTTATCAGCTCCATTGCCTATA
ATGCTTCCAGTTTACAAGTGGTGGCAGTTACCTTACTACTGGGTAGGAATCAAGCTGTAT
GATTTGGTTGCAGGAAGCAATTGCCTAAAAAGCAGTTATGTCCTCAGCAAATCAAGAGCC
CTTGAACATTTCCCAATGCTCCAGAAGGACAAACTGGTAGGAGCAATTGTCTACTATGAC
GGACAACATAACGATGCACGGATGAACCTTGCCATTGCTCTGACTGCTGCCAGGTATGGG
GCTGCCACAGCCAATTACATGGAGGTAGTGAGCTTGCTCAAGAAGACAGACCCCCAGACA
GGGAAAGTGCGTGTGAGCGGCGCACGGTGCAAGGATGTCCTCACAGGGCAGGAATTTGAC
GTGAGAGCCAAATGTGTTATCAATGCCACGGGACCTTTCACGGACTCTGTGCGCAAAATG
GATGATAAAGACGCAGCAGCTATCTGCCAGCCAAGTGCTGGTGTCCATATTGTGATGCCT
GGTTATTACAGCCCAGAGAGCATGGGACTTCTTGACCCAGCGACCAGTGATGGGCGAGTT
ATTTTCTTCTTACCCTGGCAAAAGATGACGATCGCTGGCACTACTGATACTCCAACTGAT
GTTACACACCATCCAATTCCTTCAGAAGAAGATATCAACTTCATTTTGAATGAAGTGCGT
AATTACCTGAGTTGTGATGTTGAAGTGAGAAGAGGGGATGTCCTGGCAGCATGGAGTGGA
ATCCGTCCTCTTGTTACAGACCCCAAATCTGCAGATACTCAGTCTATCTCCCGAAATCAT
GTTGTTGATATCAGTGAGAGTGGCCTTATTACTATAGCAGGTGGAAAGTGGACAACTTAT
CGGTCTATGGCAGAAGATACCATAAATGCTGCTGTCAAAACTCATAATTTAAAAGCAGGA
CCAAGTAGAACAGTTGGGCTTTTCCTTCAAGGGGGTAAAGATTGGAGCCCCACACTCTAC
ATTAGGCTTGTGCAGGATTATGGACTTGAAAGCGAGGTGGCACAGCATCTTGCCGCCACC
TATGGTGATAAGGCCTTTGAGGTGGCCAAAATGGCAAGTGTGACTGGCAAAAGGTGGCCT
ATTGTTGGAGTACGTCTTGTGTCAGAATTTCCATATATTGAAGCAGAGGTGAAATATGGG
ATTAAGGAGTATGCCTGCACTGCTGTGGATATGATTTCACGTCGTACTCGCCTGGCCTTT
CTAAATGTCCAGGCAGCAGAGGAAGCCCTACCCAGGATTGTTGAACTGATGGGCAGGGAA
CTGAATTGGGATGATTATAAGAAGCAGGAACAACTTGAAACAGCCAGGAAGTTTCTATAT
TATGAAATGGGCTATAAATCTCGATCAGAACAGTTAACAGATCGCTCTGAAATTAGCCTA
CTGCCTTCAGACATTGACAGGTATAAGAAGAGATTTCATAAGTTTGATGCAGACCAGAAA
GGCTTTATTACCATTGTTGATGTTCAGCGTGTATTAGAGAGTATCAATGTCCAAATGGAT
GAAAATACACTCCATGAAATTCTAAATGAAGTTGATTTGAATAAAAATGGACAGGTTGAA
CTCAATGAATTTTTGCAGCTGATGAGTGCTATTCAAAAAGGAAGGGTATCTGGAAGCCGG
CTTGCTATACTAATGAAAACTGCAGAAGAGAACCTCGACAGAAGAGTTCCAATTCCAGTG
GACCGTAGTTGTGGAGGATTGTGA
Enzyme 16 GenBank Gene ID NM_000408.4 Link Image
Enzyme 16 GeneCard ID GPD2 Link Image
Enzyme 16 GenAtlas ID GPD2 Link Image
Enzyme 16 HGNC ID HGNC:4456 Link Image
Enzyme 16 Chromosome Location 2
Enzyme 16 Locus 2q24.1
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Lehn DA, Brown LJ, Simonson GD, Moran SM, MacDonald MJ: The sequence of a human mitochondrial glycerol-3-phosphate dehydrogenase-encoding cDNA. Gene. 1994 Dec 15;150(2):417-8. [PubMed Link Image]
  2. Ferrer J, Aoki M, Behn P, Nestorowicz A, Riggs A, Permutt MA: Mitochondrial glycerol-3-phosphate dehydrogenase. Cloning of an alternatively spliced human islet-cell cDNA, tissue distribution, physical mapping, and identification of a polymorphic genetic marker. Diabetes. 1996 Feb;45(2):262-6. [PubMed Link Image]
  3. Brown LJ, Stoffel M, Moran SM, Fernald AA, Lehn DA, LeBeau MM, MacDonald MJ: Structural organization and mapping of the human mitochondrial glycerol phosphate dehydrogenase-encoding gene and pseudogene. Gene. 1996 Jun 26;172(2):309-12. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  6. 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]
  7. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5443
Enzyme 17 Name Glucosamine-6-phosphate isomerase 1
Enzyme 17 Synonyms
  1. Glucosamine-6-phosphate deaminase 1
  2. GNPDA 1
  3. GlcN6P deaminase 1
  4. Oscillin
Enzyme 17 Gene Name GNPDA1
Enzyme 17 Protein Sequence >Glucosamine-6-phosphate isomerase 1 
MKLIILEHYSQASEWAAKYIRNRIIQFNPGPEKYFTLGLPTGSTPLGCYKKLIEYYKNGD
LSFKYVKTFNMDEYVGLPRDHPESYHSFMWNNFFKHIDIHPENTHILDGNAVDLQAECDA
FEEKIKAAGGIELFVGGIGPDGHIAFNEPGSSLVSRTRVKTLAMDTILANARFFDGELTK
VPTMALTVGVGTVMDAREVMILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTVFVCD
EDATLELKVKTVKYFKGLMLVHNKLVDPLYSIKEKETEKSQSSKKPYSD
Enzyme 17 Number of Residues 289
Enzyme 17 Molecular Weight 32668.3
Enzyme 17 Theoretical pI 6.91
Enzyme 17 GO Classification
Function
  • catalytic activity
  • glucosamine-6-phosphate deaminase activity
  • intramolecular oxidoreductase activity
  • intramolecular oxidoreductase activity, interconverting aldoses and ketoses
  • isomerase activity
Process
  • N-acetylglucosamine metabolic process
  • alcohol metabolic process
  • amino sugar metabolic process
  • carbohydrate metabolic process
  • glucosamine metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • primary metabolic process
  • small molecule metabolic process
Component
—
Enzyme 17 General Function Involved in carbohydrate metabolic process
Enzyme 17 Specific Function Seems to trigger calcium oscillations in mammalian eggs. These oscillations serve as the essential trigger for egg activation and early development of the embryo
Enzyme 17 Pathways
Enzyme 17 Reactions
  • D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3 [RN:R00765]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein Not Available
Enzyme 17 UniProtKB/Swiss-Prot ID P46926 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name GNPI1_HUMAN Link Image
Enzyme 17 PDB ID 1NE7 Link Image
Enzyme 17 PDB File Show
Enzyme 17 3D Structure
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >870 bp 
ATGAAGCTCATCATCCTGGAGCACTATTCTCAGGCGAGCGAGTGGGCGGCTAAATACATC
AGGAACCGTATCATCCAGTTTAACCCAGGGCCAGAGAAGTACTTCACCCTGGGGCTCCCC
ACTGGGAGTACCCCACTTGGCTGCTACAAGAAGCTGATTGAATACTATAAGAATGGGGAC
CTGTCCTTTAAATATGTGAAGACCTTCAACATGGATGAGTACGTGGGCCTTCCTCGAGAC
CACCCGGAGAGTTACCACTCCTTCATGTGGAACAACTTCTTCAAGCACATTGACATCCAC
CCAGAAAACACCCACATTCTGGATGGGAATGCAGTCGACCTACAGGCAGAATGTGATGCC
TTTGAAGAGAAGATCAAGGCTGCAGGTGGGATCGAGCTATTTGTTGGAGGCATCGGCCCT
GATGGACACATTGCCTTCAACGAGCCAGGCTCCAGTCTGGTGTCCAGGACCCGTGTGAAG
ACGCTGGCCATGGATACCATCCTGGCCAATGCTAGGTTCTTCGATGGAGAACTCACCAAG
GTGCCCACCATGGCCTTGACGGTGGGGGTGGGCACTGTCATGGATGCTAGAGAGGTGATG
ATCCTTATCACAGGTGCTCACAAGGCATTTGCTCTGTACAAGGCCATCGAGGAGGGAGTG
AACCACATGTGGACCGTGTCTGCCTTCCAGCAGCATCCCCGCACCGTGTTTGTGTGTGAC
GAGGATGCCACCTTGGAGCTGAAAGTGAAGACTGTCAAGTATTTCAAAGGTTTAATGCTT
GTTCATAACAAGTTGGTGGACCCCTTGTACAGTATCAAAGAGAAAGAAACTGAGAAAAGC
CAATCTTCGAAGAAACCATACAGCGATTAG
Enzyme 17 GenBank Gene ID AF048826 Link Image
Enzyme 17 GeneCard ID GNPDA1 Link Image
Enzyme 17 GenAtlas ID GNPDA1 Link Image
Enzyme 17 HGNC ID HGNC:4417 Link Image
Enzyme 17 Chromosome Location 5
Enzyme 17 Locus 5q21
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Wolosker H, Kline D, Bian Y, Blackshaw S, Cameron AM, Fralich TJ, Schnaar RL, Snyder SH: Molecularly cloned mammalian glucosamine-6-phosphate deaminase localizes to transporting epithelium and lacks oscillin activity. FASEB J. 1998 Jan;12(1):91-9. [PubMed Link Image]
  2. Shevchenko V, Hogben M, Ekong R, Parrington J, Lai FA: The human glucosamine-6-phosphate deaminase gene: cDNA cloning and expression, genomic organization and chromosomal localization. Gene. 1998 Aug 17;216(1):31-8. [PubMed Link Image]
  3. Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, Seki N, Kawarabayasi Y, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1994;1(5):223-9. [PubMed Link Image]
  4. Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  7. Arreola R, Valderrama B, Morante ML, Horjales E: Two mammalian glucosamine-6-phosphate deaminases: a structural and genetic study. FEBS Lett. 2003 Sep 11;551(1-3):63-70. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5454
Enzyme 18 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1
Enzyme 18 Synonyms
  1. PLC-154
  2. Phosphoinositide phospholipase C-beta-1
  3. Phospholipase C-I
  4. PLC-I
  5. Phospholipase C-beta-1
  6. PLC-beta-1
Enzyme 18 Gene Name PLCB1
Enzyme 18 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1 
MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKE
TELLDLSLVKDARCGRHAKAPKDPKLRELLDVGNIGRLEQRMITVVYGPDLVNISHLNLV
AFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSA
DRKRVETALEACSLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDNIFSEFGAKSKPYL
TVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNNSLARKGQISVDGFMRYLS
GEENGVVSPEKLDLNEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCV
ELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAFKTSPFPILLSFENHVDSPKQ
QAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKK
KLSEQASNTYSDSSSMFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEM
SNLVNYIQPVKFESFEISKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPK
GTRVDSSNYMPQLFWNAGCQMVALNFQTMDLAMQINMGMYEYNGKSGYRLKPEFMRRPDK
HFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQG
NAVNPVWEEEPIVFKKVVLPTLACLRIAVYEEGGKFIGHRILPVQAIRPGYHYICLRNER
NQPLTLPAVFVYIEVKDYVPDTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKK
EADPGETPSEAPSEARTTPAENGVNHTTTLTPKPPSQALHSQPAPGSVKAPAKTEDLIQS
VLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTDLIKEHTTKYNEIQNDYL
RRRAALEKSAKKDSKKKSEPSSPDHGSSTIEQDLAALDAEMTQKLIDLKDKQQQQLLNLR
QEQYYSEKYQKREHIKLLIQKLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKI
TEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKRQEKLVEKHKEIRQQILDEKP
KLQVELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPLSLSSDPGKVNHKTPSS
EELGGDIPGKEFDTPL
Enzyme 18 Number of Residues 1216
Enzyme 18 Molecular Weight 138565.8
Enzyme 18 Theoretical pI 6.12
Enzyme 18 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
—
Enzyme 18 General Function Involved in calcium ion binding
Enzyme 18 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes
Enzyme 18 Pathways
Enzyme 18 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 12083581 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q9NQ66 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name PLCB1_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >3651 bp 
ATGGCCGGGGCTCAACCCGGAGTGCACGCCTTGCAACTCAAGCCCGTGTGCGTGTCCGAC
AGCCTCAAGAAGGGCACCAAATTCGTCAAGTGGGATGATGACTCAACTATTGTTACTCCA
ATTATTTTGAGGACTGACCCTCAGGGATTTTTCTTTTACTGGACAGATCAAAACAAGGAG
ACAGAGCTACTGGATCTCAGCCTTGTCAAAGATGCCAGATGTGGGAGACACGCCAAAGCT
CCCAAGGACCCCAAATTACGTGAACTTTTGGATGTGGGGAACATCGGGCGCCTGGAGCAG
CGCATGATCACAGTGGTGTATGGGCCTGACCTCGTGAACATCTCCCATTTGAATCTCGTG
GCTTTCCAAGAAGAAGTGGCCAAGGAATGGACAAATGAGGTTTTCAGTTTGGCAACAAAC
CTGCTGGCCCAAAACATGTCCAGGGATGCATTTCTGGAAAAAGCCTATACTAAACTTAAG
CTGCAAGTCACTCCAGAAGGGCGTATTCCTCTCAAAAACATATATCGCTTGTTTTCAGCA
GATCGGAAGCGAGTTGAAACTGCTTTAGAGGCTTGTAGTCTTCCATCTTCAAGGAATGAT
TCAATACCTCAAGAAGATTTCACTCCAGAAGTGTACAGAGTTTTCCTCAACAACCTTTGC
CCTCGACCTGAAATTGATAACATCTTTTCAGAATTTGGTGCAAAAAGCAAACCATATCTT
ACCGTTGATCAGATGATGGATTTTATCAACCTTAAGCAGCGAGATCCTCGGCTTAATGAA
ATACTTTATCCACCTCTAAAACAAGAGCAAGTCCAAGTATTGATTGAGAAGTATGAACCC
AACAACAGCCTCGCCAGAAAAGGACAAATATCAGTGGATGGGTTCATGCGCTATCTGAGT
GGAGAAGAAAACGGAGTCGTTTCACCTGAGAAACTGGATTTGAATGAAGACATGTCTCAG
CCCCTTTCTCACTATTTCATTAATTCCTCGCACAACACCTACCTCACAGCTGGCCAACTG
GCTGGAAACTCCTCTGTTGAGATGTATCGCCAAGTGCTCCTGTCTGGTTGTCGCTGTGTG
GAGCTGGACTGCTGGAAGGGACGGACTGCAGAAGAGGAACCTGTCATCACCCATGGCTTC
ACCATGACAACTGAAATATCTTTCAAGGAAGTGATAGAAGCAATTGCGGAGTGTGCATTT
AAGACTTCACCTTTTCCAATTCTCCTTTCGTTTGAGAACCATGTGGATTCCCCAAAGCAG
CAAGCCAAGATGGCGGAGTACTGCCGACTGATCTTTGGGGATGCCCTTCTCATGGAGCCC
CTGGAAAAATATCCACTGGAATCTGGAGTTCCTCTTCCAAGCCCTATGGATTTAATGTAT
AAAATTTTGGTGAAAAATAAGAAGAAATCACACAAGTCATCAGAAGGAAGCGGCAAAAAG
AAGCTCTCAGAACAAGCCTCCAACACCTACAGTGACTCCTCCAGCATGTTCGAGCCCTCA
TCCCCAGGAGCCGGAGAAGCTGATACGGAAAGTGACGACGACGATGATGATGATGACTGT
AAAAAATCTTCAATGGATGAGGGGACTGCTGGAAGTGAGGCTATGGCCACAGAAGAAATG
TCTAATCTGGTGAACTATATTCAGCCAGTCAAGTTTGAGTCATTTGAAATTTCAAAAAAA
AGAAATAAAAGTTTTGAAATGTCTTCCTTCGTGGAAACCAAAGGACTTGAACAACTCACC
AAGTCTCCAGTGGAATTTGTAGAATATAACAAAATGCAGCTTAGCAGGATATATCCAAAA
GGAACACGTGTGGATTCATCCAACTATATGCCTCAGCTCTTCTGGAATGCAGGTTGTCAG
ATGGTGGCACTTAATTTCCAGACAATGGACCTGGCTATGCAAATAAATATGGGGATGTAT
GAATACAACGGGAAGAGTGGCTACAGATTGAAGCCAGAGTTCATGAGGAGGCCTGACAAG
CATTTTGATCCATTTACTGAAGGCATCGTAGATGGGATAGTGGCAAACACTTTGTCTGTT
AAGATTATTTCAGGTCAGTTTCTTTCTGATAAGAAAGTTGGGACTTACGTGGAAGTAGAT
ATGTTTGGTTTGCCTGTGGATACAAGGAGGAAGGCATTTAAGACCAAAACATCCCAAGGA
AATGCTGTGAATCCTGTCTGGGAAGAAGAACCTATTGTGTTCAAAAAGGTGGTTCTTCCT
ACTCTGGCCTGTTTGAGAATAGCAGTTTATGAAGAAGGAGGTAAATTCATTGGCCACCGT
ATCTTGCCAGTGCAAGCCATTCGGCCAGGCTATCACTATATCTGTCTAAGGAATGAAAGG
AACCAGCCTCTGACGCTGCCTGCTGTCTTTGTCTACATAGAAGTGAAAGACTATGTGCCA
GACACATATGCAGATGTCATCGAAGCTTTATCAAACCCAATCCGATATGTGAACCTGATG
GAACAGAGAGCTAAGCAATTGGCTGCTTTGACACTGGAAGATGAAGAAGAAGTAAAGAAA
GAGGCTGATCCTGGAGAAACACCATCAGAGGCTCCAAGTGAAGCGAGAACGACTCCAGCA
GAAAATGGGGTGAATCACACTACAACCCTGACACCCAAGCCACCCTCCCAGGCTCTCCAC
AGCCAGCCAGCTCCAGGTTCTGTAAAGGCACCTGCCAAAACAGAAGATCTTATTCAGAGT
GTCTTAACAGAAGTGGAAGCACAGACCATCGAAGAACTAAAGCAACAGAAATCGTTTGTG
AAACTTCAAAAGAAACACTACAAAGAAATGAAAGACCTGGTTAAGAGACACCACAAGAAA
ACCACTGACCTTATCAAAGAACACACTACCAAGTATAATGAAATTCAGAATGACTACTTG
AGAAGGAGAGCCGCTTTGGAAAAGTCCGCCAAAAAGGACAGTAAGAAAAAATCGGAACCC
AGCAGCCCTGATCATGGTTCATCAACGATTGAGCAAGACCTCGCTGCTCTGGATGCTGAA
ATGACCCAAAAGTTAATAGACTTGAAGGACAAACAACAGCAGCAGCTGCTTAATCTTCGG
CAAGAACAGTATTATAGTGAAAAATACCAGAAGCGAGAACATATTAAACTGCTTATTCAA
AAGTTGACGGATGTCGCAGAAGAGTGTCAGAACAATCAGTTAAAGAAGCTCAAAGAAATC
TGTGAGAAAGAAAAGAAAGAATTAAAGAAGAAAATGGATAAAAAGAGGCAGGAGAAGATA
ACAGAAGCTAAATCCAAAGACAAAAGTCAGATGGAAGAGGAGAAGACAGAGATGATCCGG
TCATATATCCAGGAAGTGGTGCAGTATATCAAGAGGCTAGAAGAAGCGCAAAGTAAACGG
CAAGAAAAACTCGTAGAGAAACACAAGGAAATACGTCAGCAGATCCTGGATGAAAAGCCC
AAGCTGCAGGTGGAGCTGGAGCAAGAATACCAAGACAAATTCAAAAGACTGCCCCTCGAG
ATTTTGGAATTCGTGCAGGAAGCCATGAAAGGAAAGATCAGTGAAGACAGCAATCACGGT
TCTGCCCCTCTCTCCCTGTCCTCAGACCCTGGAAAAGTGAACCACAAGACTCCCTCCAGT
GAGGAGCTGGGAGGAGACATCCCAGGAAAAGAATTTGATACTCCTCTGTGA
Enzyme 18 GenBank Gene ID NM_015192.2 Link Image
Enzyme 18 GeneCard ID PLCB1 Link Image
Enzyme 18 GenAtlas ID PLCB1 Link Image
Enzyme 18 HGNC ID HGNC:15917 Link Image
Enzyme 18 Chromosome Location 2
Enzyme 18 Locus 20p12
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Caricasole A, Sala C, Roncarati R, Formenti E, Terstappen GC: Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1). Biochim Biophys Acta. 2000 Dec 15;1517(1):63-72. [PubMed Link Image]
  2. Peruzzi D, Calabrese G, Faenza I, Manzoli L, Matteucci A, Gianfrancesco F, Billi AM, Stuppia L, Palka G, Cocco L: Identification and chromosomal localisation by fluorescence in situ hybridisation of human gene of phosphoinositide-specific phospholipase C beta(1). Biochim Biophys Acta. 2000 Apr 12;1484(2-3):175-82. [PubMed Link Image]
  3. 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]
  4. 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]
  5. 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]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  8. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  9. Tabellini G, Bortul R, Santi S, Riccio M, Baldini G, Cappellini A, Billi AM, Berezney R, Ruggeri A, Cocco L, Martelli AM: Diacylglycerol kinase-theta is localized in the speckle domains of the nucleus. Exp Cell Res. 2003 Jul 1;287(1):143-54. [PubMed Link Image]
  10. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed Link Image]
  11. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  12. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5455
Enzyme 19 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4
Enzyme 19 Synonyms
  1. Phosphoinositide phospholipase C-beta-4
  2. Phospholipase C-beta-4
  3. PLC-beta-4
Enzyme 19 Gene Name PLCB4
Enzyme 19 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4 
MAKPYEFNWQKEVPSFLQEGAVFDRYEEESFVFEPNCLFKVDEFGFFLTWRSEGKEGQVL
ECSLINSIRSGAIPKDPKILAALEAVGKSENDLEGRIVCVCSGTDLVNISFTYMVAENPE
VTKQWVEGLRSIIHNFRANNVSPMTCLKKHWMKLAFMTNTNGKIPVRSITRTFASGKTEK
VIFQALKELGLPSGKNDEIEPTAFSYEKFYELTQKICPRTDIEDLFKKINGDKTDYLTVD
QLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDE
NAPVFLDRLELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELD
CWDGKGEDQEPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKM
SKYCEDLFGDLLLKQALESHPLEPGRALPSPNDLKRKILIKNKRLKPEVEKKQLEALRSM
MEAGESASPANILEDDNEEEIESADQEEEAHPEFKFGNELSADDLGHKEAVANSVKKGLV
TVEDEQAWMASYKYVGATTNIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVG
LGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQL
NQGKFEYNGSCGYLLKPDFMRRPDRTFDPFSETPVDGVIAATCSVQVISGQFLSDKKIGT
YVEVDMYGLPTDTIRKEFRTRMVMNNGLNPVYNEESFVFRKVILPDLAVLRIAVYDDNNK
LIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNIVLKTYVPDGFGDIVDALSDPKK
FLSITEKRADQMRAMGIETSDIADVPSDTSKNDKKGKANTAKANVTPQSSSELRPTTTAA
LASGVEAKKGIELIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKLHCTQ
VDKIVAQYDKEKSTHEKILEKAMKKKGGSNCLEMKKETEIKIQTLTSDHKSKVKEIVAQH
TKEWSEMINTHSAEEQEIRDLHLSQQCELLKKLLINAHEQQTQQLKLSHDRESKEMRAHQ
AKISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQ
LEHLEFLEKQNEQAKEMQQMVKLEAEMDRRPATVV
Enzyme 19 Number of Residues 1175
Enzyme 19 Molecular Weight 134462.6
Enzyme 19 Theoretical pI 6.90
Enzyme 19 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
—
Enzyme 19 General Function Involved in calcium ion binding
Enzyme 19 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This form has a role in retina signal transduction
Enzyme 19 Pathways
Enzyme 19 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 57284038 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q15147 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name PLCB4_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >3528 bp 
ATGGCCAAACCTTATGAATTTAACTGGCAGAAGGAAGTTCCCTCCTTTTTGCAAGAAGGA
GCAGTTTTTGACAGATACGAGGAGGAATCCTTTGTGTTTGAACCCAACTGCCTCTTCAAA
GTGGATGAGTTTGGCTTCTTTCTGACATGGAGAAGTGAAGGCAAGGAAGGACAGGTGCTA
GAATGCTCCCTCATCAACAGTATTCGGTCGGGAGCCATACCAAAGGATCCCAAAATCTTG
GCTGCTCTTGAAGCTGTTGGAAAATCAGAAAATGATCTGGAAGGGCGGATAGTTTGTGTC
TGCAGTGGCACAGATCTAGTGAACATTAGTTTTACCTACATGGTGGCTGAAAATCCAGAA
GTAACTAAGCAATGGGTAGAAGGCCTGAGATCAATCATACACAACTTCAGGGCCAACAAC
GTCAGTCCAATGACATGCCTCAAGAAACACTGGATGAAATTGGCATTTATGACCAACACA
AATGGTAAAATTCCAGTTAGGAGTATTACTAGAACATTTGCATCGGGAAAAACAGAAAAG
GTGATCTTTCAAGCACTCAAGGAGTTAGGTCTTCCCAGTGGAAAGAATGATGAAATTGAG
CCCACAGCATTTTCTTATGAAAAGTTCTATGAACTGACACAAAAGATTTGTCCTCGGACA
GATATAGAAGATCTTTTCAAAAAAATCAATGGAGACAAAACTGATTATTTAACGGTAGAC
CAATTAGTGAGCTTTCTAAATGAACATCAACGAGATCCTCGATTGAATGAAATTTTATTT
CCATTTTATGATGCCAAAAGGGCAATGCAGATCATTGAGATGTATGAACCTGATGAAGAT
TTGAAGAAAAAAGGCCTTATATCAAGTGATGGGTTTTGCAGATATCTGATGTCAGATGAA
AACGCCCCAGTCTTCCTAGATCGTTTAGAACTTTACCAAGAAATGGACCATCCTCTGGCT
CACTACTTCATCAGTTCTTCCCATAACACTTATCTCACTGGCAGACAGTTCGGCGGGAAG
TCTTCGGTAGAAATGTACAGACAGGTTCTCCTGGCTGGTTGCAGATGTGTTGAACTTGAC
TGCTGGGATGGAAAAGGTGAAGACCAAGAACCAATAATAACTCATGGAAAAGCAATGTGT
ACAGATATCCTTTTTAAGGATGTAATTCAAGCCATCAAGGAAACTGCATTTGTCACATCA
GAATATCCTGTAATTCTCTCCTTTGAAAATCACTGCAGCAAATATCAACAGTACAAGATG
TCCAAATATTGCGAAGATCTATTTGGGGATCTCCTGTTGAAACAAGCACTTGAATCACAT
CCACTTGAACCAGGCAGGGCTTTGCCATCCCCCAATGACCTCAAAAGAAAAATACTCATA
AAAAACAAGCGGCTGAAACCTGAAGTTGAAAAAAAACAGCTGGAAGCTTTGAGAAGCATG
ATGGAAGCTGGAGAATCTGCCTCCCCAGCAAACATCTTAGAGGACGATAATGAAGAGGAG
ATCGAAAGTGCTGACCAAGAGGAGGAAGCTCACCCCGAATTCAAATTTGGAAATGAACTT
TCTGCTGATGACTTGGGTCACAAGGAAGCTGTTGCAAATAGCGTCAAGAAGGGCCTGGTC
ACTGTAGAAGATGAGCAGGCGTGGATGGCATCTTATAAATATGTAGGTGCTACCACTAAT
ATCCATCCATATTTGTCCACAATGATCAACTACGCCCAGCCTGTAAAGTTTCAAGGTTTC
CATGTGGCAGAAGAACGCAATATTCATTATAACATGTCTTCTTTTAATGAATCAGTCGGT
CTTGGCTACTTGAAGACACATGCAATTGAATTTGTCAATTATAACAAACGGCAAATGAGT
CGCATTTACCCCAAGGGAGGCCGAGTCGATTCCAGTAATTACATGCCTCAGATTTTCTGG
AACGCTGGCTGCCAGATGGTTTCACTGAACTATCAAACCCCAGATTTAGCGATGCAATTG
AATCAGGGAAAATTTGAGTATAATGGATCGTGCGGGTACCTTCTCAAACCAGATTTCATG
AGGCGGCCTGATCGAACATTTGACCCCTTCTCTGAAACTCCTGTTGATGGTGTTATTGCA
GCCACTTGCTCAGTGCAGGTTATATCAGGTCAATTCTTATCAGATAAGAAAATTGGCACC
TACGTAGAGGTGGATATGTATGGGTTGCCCACTGACACCATACGTAAGGAATTCCGAACT
CGCATGGTTATGAATAATGGACTCAATCCAGTTTACAATGAAGAGTCATTTGTATTTCGG
AAGGTGATCCTGCCGGACCTGGCTGTCTTGAGAATAGCTGTGTATGATGATAACAACAAG
CTGATTGGCCAGAGGATCCTCCCGCTTGATGGCCTCCAAGCCGGATATCGACACATTTCC
CTTCGAAATGAGGGAAATAAACCATTATCACTACCAACAATTTTCTGCAATATTGTTCTT
AAAACATATGTGCCTGATGGATTTGGAGATATCGTGGATGCTTTATCAGATCCAAAGAAA
TTTCTCTCAATTACAGAAAAGAGAGCAGACCAAATGAGAGCTATGGGCATTGAAACTAGT
GACATAGCCGACGTGCCCAGTGACACTTCCAAAAATGACAAGAAAGGAAAGGCCAACACC
GCCAAAGCAAATGTGACCCCTCAGAGTAGCTCTGAGCTCAGACCAACCACCACGGCTGCC
CTGGCCTCTGGTGTGGAAGCCAAGAAAGGTATTGAACTTATCCCTCAAGTAAGGATAGAA
GACTTAAAGCAGATGAAGGCTTACTTGAAGCATTTAAAGAAACAGCAGAAGGAGCTAAAT
TCTTTAAAGAAGAAACATGCAAAGGAACACAGTACCATGCAGAAGTTACACTGCACGCAA
GTTGACAAAATTGTGGCACAGTATGACAAAGAGAAGTCGACTCATGAGAAAATCCTAGAG
AAGGCAATGAAGAAGAAGGGGGGAAGTAATTGTCTCGAAATGAAAAAAGAAACAGAAATC
AAAATTCAGACGCTGACATCAGATCACAAATCTAAGGTCAAAGAGATTGTAGCACAGCAC
ACAAAGGAATGGTCAGAAATGATCAATACCCACAGTGCTGAGGAGCAAGAAATCCGAGAC
CTGCACCTCAGCCAGCAGTGTGAGCTGCTGAAAAAGCTACTCATCAATGCCCACGAGCAG
CAAACCCAGCAGCTGAAACTGTCCCATGACAGGGAAAGCAAGGAAATGCGAGCACACCAG
GCTAAGATTTCTATGGAAAATAGCAAAGCCATCAGCCAAGATAAATCTATCAAGAATAAA
GCAGAACGGGAAAGGCGAGTCAGGGAGTTAAACAGCAGCAACACTAAAAAGTTTCTGGAA
GAAAGAAAGAGACTTGCCATGAAGCAGTCCAAAGAAATGGATCAGTTGAAAAAAGTCCAG
CTTGAACATCTAGAATTCCTAGAGAAACAGAATGAGCAGGCGAAGGAGATGCAGCAGATG
GTGAAATTGGAAGCCGAGATGGACCGCAGACCAGCAACAGTAGTATGA
Enzyme 19 GenBank Gene ID AL023805 Link Image
Enzyme 19 GeneCard ID PLCB4 Link Image
Enzyme 19 GenAtlas ID PLCB4 Link Image
Enzyme 19 HGNC ID HGNC:9059 Link Image
Enzyme 19 Chromosome Location 2
Enzyme 19 Locus 20p12
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Alvarez RA, Ghalayini AJ, Xu P, Hardcastle A, Bhattacharya S, Rao PN, Pettenati MJ, Anderson RE, Baehr W: cDNA sequence and gene locus of the human retinal phosphoinositide-specific phospholipase-C beta 4 (PLCB4). Genomics. 1995 Sep 1;29(1):53-61. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  5. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5456
Enzyme 20 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2
Enzyme 20 Synonyms
  1. Phosphoinositide phospholipase C-beta-2
  2. Phospholipase C-beta-2
  3. PLC-beta-2
Enzyme 20 Gene Name PLCB2
Enzyme 20 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2 
MSLLNPVLLPPKVKAYLSQGERFIKWDDETTVASPVILRVDPKGYYLYWTYQSKEMEFLD
ITSIRDTRFGKFAKMPKSQKLRDVFNMDFPDNSFLLKTLTVVSGPDMVDLTFHNFVSYKE
NVGKAWAEDVLALVKHPLTANASRSTFLDKILVKLKMQLNSEGKIPVKNFFQMFPADRKR
VEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSYHAKAKPYMTKEH
LTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPEN
SVLAQDKLLLHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDC
WKGKPPDEEPIITHGFTMTTDIFFKEAIEAIAESAFKTSPYPIILSFENHVDSPRQQAKM
AEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKNQFSGPTSSSKDTGGE
AEGSSPPSAPAGEGTVWAGEEGTELEEEEVEEEEEEESGNLDEEEIKKMQSDEGTAGLEV
TAYEEMSSLVNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQM
SRIYPKGTRMDSSNYMPQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEF
MRRPDKQFNPFSVDRIDVVVATTLSITVISGQFLSERSVRTYVEVELFGLPGDPKRRYRT
KLSPSTNSINPVWKEEPFVFEKILMPELASLRVAVMEEGNKFLGHRIIPINALNSGYHHL
CLHSESNMPLTMPALFIFLEMKDYIPGAWADLTVALANPIKFFSAHDTKSVKLKEAMGGL
PEKPFPLASPVASQVNGALAPTSNGSPAARAGAREEAMKEAAEPRTASLEELRELKGVVK
LQRRHEKELRELERRGARRWEELLQRGAAQLAELGPPGVGGVGACKLGPGKGSRKKRSLP
REESAGAAPGEGPEGVDGRVRELKDRLELELLRQGEEQYECVLKRKEQHVAEQISKMMEL
AREKQAAELKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREINNSHI
QEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEARMKGLEAEVKE
SVRACLRTCFPSEAKDKPERACECPPELCEQDPLIAKADAQESRL
Enzyme 20 Number of Residues 1185
Enzyme 20 Molecular Weight 134023.2
Enzyme 20 Theoretical pI 6.21
Enzyme 20 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
—
Enzyme 20 General Function Involved in calcium ion binding
Enzyme 20 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes
Enzyme 20 Pathways
Enzyme 20 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 95147333 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q00722 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name PLCB2_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >3558 bp 
ATGTCTCTGCTCAACCCTGTCCTGCTGCCCCCCAAGGTGAAGGCCTATCTGAGCCAAGGG
GAGCGCTTCATCAAATGGGATGATGAAACTACAGTTGCCTCTCCAGTTATCCTCCGTGTG
GATCCTAAGGGCTACTACTTATACTGGACGTATCAAAGTAAGGAGATGGAGTTTCTGGAT
ATCACCAGCATCCGGGATACTCGCTTTGGGAAGTTTGCCAAGATGCCCAAGAGCCAGAAG
CTCCGGGACGTCTTCAACATGGACTTTCCTGATAACAGTTTCCTGCTGAAGACACTCACG
GTGGTGTCCGGCCCGGACATGGTGGACCTCACCTTCCACAACTTCGTCTCCTACAAGGAG
AACGTGGGCAAGGCCTGGGCTGAGGACGTACTGGCCCTAGTCAAACATCCGCTGACGGCC
AACGCCTCCCGCAGCACCTTCCTGGACAAGATCCTTGTGAAGCTCAAGATGCAGCTCAAC
TCTGAAGGGAAGATTCCGGTGAAGAACTTTTTCCAGATGTTTCCTGCTGACCGCAAGCGG
GTGGAAGCTGCTCTCAGTGCCTGCCACCTCCCCAAAGGCAAAAATGACGCCATCAATCCT
GAGGACTTCCCAGAACCTGTCTACAAGAGTTTCCTCATGAGCCTCTGTCCTCGGCCAGAA
ATAGATGAGATCTTCACTTCTTACCATGCTAAGGCCAAACCCTACATGACGAAGGAGCAC
CTGACCAAATTCATCAACCAGAAACAGCGGGACTCCCGGCTTAACTCCCTGCTGTTCCCG
CCAGCACGGCCTGACCAGGTGCAGGGCCTCATCGACAAGTATGAGCCCAGTGGCATCAAT
GCACAGAGGGGCCAGCTGTCACCTGAAGGCATGGTCTGGTTTCTCTGTGGGCCAGAGAAC
AGCGTGCTGGCCCAGGACAAGCTGCTGCTCCACCACGACATGACGCAGCCACTCAATCAT
TACTTCATCAACTCGTCCCACAACACCTACCTGACAGCCGGCCAGTTCTCAGGCCTCTCC
TCGGCTGAGATGTACCGCCAGGTGCTGCTCTCTGGCTGCCGTTGCGTGGAGCTAGACTGC
TGGAAGGGGAAACCCCCTGACGAGGAGCCCATTATCACCCATGGCTTCACCATGACCACA
GACATCTTCTTCAAAGAAGCAATTGAGGCTATTGCAGAAAGCGCCTTTAAGACCTCCCCC
TATCCCATCATCCTGTCGTTTGAGAACCATGTGGACTCACCCCGCCAGCAGGCTAAGATG
GCTGAGTATTGCCGGACGATCTTTGGGGATATGCTGCTCACAGAGCCCCTGGAAAAGTTC
CCACTAAAACCAGGTGTCCCCCTGCCCAGCCCTGAGGATCTCAGGGGCAAGATCCTCATC
AAGAACAAGAAGAACCAGTTTTCTGGCCCCACCTCCTCCAGTAAGGATACTGGTGGGGAG
GCTGAGGGCAGCAGCCCACCCAGTGCCCCTGCAGGTGAGGGCACAGTGTGGGCTGGCGAG
GAAGGGACTGAGCTGGAGGAGGAGGAGGTGGAAGAGGAAGAGGAGGAGGAGTCAGGAAAC
CTGGATGAAGAAGAGATTAAGAAGATGCAGTCGGATGAGGGCACAGCGGGCCTGGAAGTG
ACGGCTTATGAGGAGATGTCCAGCCTAGTCAATTACATCCAGCCCACCAAGTTCGTCTCC
TTTGAGTTCTCTGCCCAAAAGAACCGAAGTTATGTCATCTCGTCCTTCACAGAGCTCAAG
GCATATGACCTGCTCTCCAAGGCCTCGGTGCAGTTTGTGGACTACAACAAGCGCCAGATG
AGCCGCATTTACCCCAAGGGAACCCGCATGGACTCCTCCAACTACATGCCCCAGATGTTC
TGGAATGCTGGATGCCAGATGGTTGCCCTCAACTTCCAGACGATGGACTTGCCCATGCAG
CAGAACATGGCAGTATTTGAGTTCAACGGGCAGAGCGGCTACCTCCTCAAGCATGAGTTC
ATGCGCCGGCCGGACAAGCAGTTCAACCCCTTCTCAGTGGACCGCATCGACGTGGTGGTG
GCCACCACCCTTTCCATTACGGTGATCTCTGGGCAGTTCCTGTCAGAACGCAGCGTGCGC
ACCTATGTAGAAGTGGAGCTGTTTGGCCTTCCTGGGGACCCCAAGAGGCGCTATCGAACT
AAGCTGTCACCCAGTACTAACTCCATCAATCCTGTCTGGAAGGAGGAGCCCTTTGTCTTT
GAGAAGATCTTGATGCCTGAGCTGGCCTCCCTCAGAGTGGCTGTGATGGAGGAAGGCAAC
AAGTTTCTTGGACACCGCATCATCCCCATCAATGCCCTAAATTCTGGGTACCACCACCTG
TGCCTGCACAGTGAGAGCAACATGCCCCTCACCATGCCTGCGCTCTTCATCTTCCTGGAG
ATGAAGGACTACATACCTGGTGCTTGGGCAGATCTCACTGTGGCCCTCGCCAACCCCATT
AAGTTCTTCAGTGCCCATGACACGAAGTCTGTGAAGCTCAAGGAGGCCATGGGAGGTCTG
CCTGAGAAGCCCTTCCCACTGGCGAGTCCAGTTGCCAGCCAGGTCAATGGGGCGTTGGCC
CCAACGAGCAATGGGTCACCAGCAGCCAGGGCCGGGGCCAGGGAAGAGGCTATGAAAGAA
GCTGCGGAGCCGCGGACCGCCAGCCTGGAGGAGCTCCGGGAGCTAAAGGGCGTGGTGAAG
CTGCAGCGGCGGCACGAGAAGGAGCTGCGAGAGTTGGAGCGGCGCGGAGCGCGGCGCTGG
GAGGAGCTGCTGCAGCGGGGCGCGGCGCAGCTGGCGGAGCTCGGGCCACCGGGCGTGGGG
GGCGTCGGGGCCTGCAAGCTCGGTCCCGGCAAGGGCTCTCGCAAGAAGAGGAGCCTGCCC
CGCGAGGAGAGCGCCGGAGCCGCGCCGGGCGAGGGCCCTGAGGGCGTGGACGGGCGCGTG
CGGGAGCTGAAAGACAGGCTGGAGCTGGAGCTGCTGCGGCAGGGCGAGGAGCAGTACGAG
TGCGTTCTGAAGCGCAAGGAGCAGCACGTGGCCGAGCAAATCTCCAAAATGATGGAGCTG
GCCAGAGAGAAACAGGCGGCAGAGCTGAAGGCCCTGAAGGAGACGTCGGAGAACGACACC
AAAGAGATGAAGAAAAAGCTGGAGACAAAGAGACTGGAGCGGATCCAGGGCATGACCAAA
GTCACCACAGACAAGATGGCCCAGGAGAGGTTGAAGAGAGAGATTAACAACTCCCACATC
CAGGAAGTAGTGCAGGTGATCAAGCAGATGACGGAGAACTTGGAGAGGCACCAGGAGAAG
CTGGAGGAGAAGCAGGCGGCTTGCCTGGAACAGATACGGGAGATGGAAAAGCAGTTCCAG
AAGGAGGCGCTGGCAGAGTACGAGGCCAGGATGAAGGGTCTGGAGGCAGAGGTGAAGGAG
TCGGTGAGGGCCTGCCTCAGGACCTGCTTTCCCTCCGAGGCCAAGGACAAGCCTGAGAGG
GCCTGCGAGTGCCCCCCAGAGCTGTGTGAGCAGGACCCACTCATAGCAAAGGCAGATGCC
CAGGAGAGCCGCCTCTGA
Enzyme 20 GenBank Gene ID NM_004573.2 Link Image
Enzyme 20 GeneCard ID PLCB2 Link Image
Enzyme 20 GenAtlas ID PLCB2 Link Image
Enzyme 20 HGNC ID HGNC:9055 Link Image
Enzyme 20 Chromosome Location 1
Enzyme 20 Locus 15q15
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Park D, Jhon DY, Kriz R, Knopf J, Rhee SG: Cloning, sequencing, expression, and Gq-independent activation of phospholipase C-beta 2. J Biol Chem. 1992 Aug 15;267(23):16048-55. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed Link Image]
  4. Jezyk MR, Snyder JT, Gershberg S, Worthylake DK, Harden TK, Sondek J: Crystal structure of Rac1 bound to its effector phospholipase C-beta2. Nat Struct Mol Biol. 2006 Dec;13(12):1135-40. Epub 2006 Nov 19. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5460
Enzyme 21 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3
Enzyme 21 Synonyms
  1. Phosphoinositide phospholipase C-beta-3
  2. Phospholipase C-beta-3
  3. PLC-beta-3
Enzyme 21 Gene Name PLCB3
Enzyme 21 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3 
MAGAQPGVHALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNME
VDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLNF
MAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMFS
ADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPY
LTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYL
GGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRC
VELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSAK
QQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPDS
AGRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLGD
EGLNRGPYVLGPADREDEEEDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEPV
KFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYM
PQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIV
DGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEP
FDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLI
YTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAALIGESEAQAGQETCQDTQSQQL
GSQPSSNPTPSPLDASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPTPLDELRGH
KALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRPGALGGAADVED
TKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQF
KRLKEMNEREKKELQKILDRKRHNSISEAKMRDKHKKEAELTEINRRHITESVNSIRRLE
EAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRRSLLGEMPEGLG
DGPLVACASNGHAPGSSGHLSGADSESQEENTQL
Enzyme 21 Number of Residues 1234
Enzyme 21 Molecular Weight 138797.7
Enzyme 21 Theoretical pI 5.66
Enzyme 21 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
—
Enzyme 21 General Function Involved in calcium ion binding
Enzyme 21 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes
Enzyme 21 Pathways
Enzyme 21 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 148745659 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q01970 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name PLCB3_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >3705 bp 
ATGGCGGGCGCCCAGCCCGGCGTCCACGCGCTGCAGTTGGAGCCGCCCACCGTGGTGGAG
ACCCTGCGGCGCGGGAGTAAGTTCATCAAATGGGACGAGGAGACCTCCAGTCGGAACCTG
GTGACCCTGCGTGTGGACCCCAATGGCTTCTTCTTGTACTGGACGGGCCCCAACATGGAG
GTGGACACACTGGACATCAGTTCCATCAGGGACACACGGACAGGCCGGTACGCCCGCCTG
CCCAAGGACCCCAAGATCCGGGAAGTTCTGGGCTTTGGGGGTCCCGATGCCCGGCTGGAG
GAGAAGCTGATGACGGTGGTGTCTGGGCCAGACCCGGTGAACACAGTGTTCTTGAACTTC
ATGGCCGTGCAGGATGACACAGCCAAGGTCTGGTCTGAGGAGCTATTCAAGCTGGCTATG
AACATCCTGGCTCAGAACGCCTCCCGGAACACCTTCCTGCGCAAAGCATACACGAAGCTG
AAGCTGCAGGTGAACCAGGATGGTCGGATCCCCGTCAAGAACATCCTGAAGATGTTCTCA
GCAGACAAGAAGCGGGTGGAGACTGCGCTGGAATCCTGTGGCCTCAAATTCAACCGGAGT
GAGTCCATCCGGCCTGATGAGTTTTCCTTGGAAATCTTTGAGCGGTTCCTGAACAAGCTG
TGTCTGCGGCCGGACATTGACAAGATCCTGCTGGAGATAGGCGCCAAGGGCAAGCCATAC
CTGACGCTGGAGCAGCTCATGGACTTCATCAACCAGAAGCAACGCGACCCGAGACTCAAC
GAAGTGCTGTACCCGCCCCTGCGGCCCTCCCAGGCCCGGCTGCTCATCGAAAAGTATGAG
CCCAACCAGCAGTTTCTGGAGCGAGACCAGATGTCCATGGAGGGCTTTAGCCGCTACCTG
GGAGGCGAGGAGAATGGCATCCTGCCCCTGGAAGCCCTGGATCTGAGCACGGACATGACC
CAGCCACTGAGTGCCTACTTCATCAACTCCTCGCATAACACCTATCTCACTGCGGGGCAG
CTGGCTGGGACCTCGTCGGTGGAGATGTACCGCCAGGCACTACTATGGGGCTGCCGCTGC
GTGGAGCTGGACGTGTGGAAGGGACGGCCGCCTGAGGAGGAACCCTTCATTACCCACGGC
TTCACCATGACCACAGAGGTGCCTCTGCGCGACGTGCTGGAGGCCATTGCCGAGACTGCC
TTCAAGACCTCGCCCTACCCCGTCATCCTCTCCTTCGAGAACCATGTGGACTCGGCAAAG
CAACAGGCAAAGATGGCTGAGTACTGCCGCTCCATCTTTGGAGACGCGCTACTCATCGAG
CCTCTGGACAAGTACCCGCTGGCCCCAGGCGTTCCCCTGCCCAGCCCCCAGGACCTGATG
GGCCGTATCCTGGTGAAGAACAAGAAGCGGCACCGACCCAGCGCAGGTGGCCCAGACAGC
GCCGGGCGCAAGCGGCCCCTGGAGCAGAGCAATTCTGCCCTGAGCGAGAGCTCCGCGGCC
ACCGAGCCCTCCTCCCCGCAGCTGGGGTCTCCCAGCTCTGACAGCTGCCCAGGCCTGAGC
AATGGGGAGGAGGTAGGGCTTGAGAAGCCCAGCCTGGAGCCTCAGAAGTCTCTGGGTGAC
GAGGGCCTGAACCGAGGCCCCTATGTTCTTGGACCTGCTGACCGTGAGGATGAGGAGGAA
GATGAGGAAGAGGAGGAACAGACAGACCCCAAAAAGCCAACTACAGATGAGGGCACAGCC
AGCAGCGAGGTGAATGCCACTGAGGAGATGTCCACGCTTGTCAACTACATCGAACCTGTC
AAGTTCAAGTCCTTTGAGGCTGCTCGAAAGAGGAACAAATGCTTCGAGATGTCGTCCTTT
GTGGAGACCAAGGCCATGGAGCAACTGACCAAGAGCCCCATGGAGTTTGTGGAATACAAC
AAGCAGCAGCTCAGCCGCATCTACCCCAAGGGCACCCGCGTGGACTCCTCCAACTACATG
CCCCAGCTCTTCTGGAACGTAGGGTGCCAGCTTGTTGCGCTCAACTTCCAGACCCTCGAT
GTGGCGATGCAGCTCAACGCGGGCGTTTTTGAGTACAACGGGCGCAGCGGGTACCTGCTC
AAGCCGGAGTTCATGCGGCGGCCGGACAAGTCCTTCGACCCCTTCACTGAGGTCATCGTG
GATGGCATCGTGGCCAATGCCTTGCGGGTCAAGGTGATCTCAGGGCAGTTCCTGTCCGAC
AGGAAGGTGGGCATCTACGTGGAGGTGGACATGTTTGGCCTCCCTGTTGATACGCGGCGC
AAGTACCGCACCCGGACCTCTCAGGGGAACTCGTTCAACCCCGTGTGGGACGAAGAGCCC
TTCGACTTCCCCAAGGTGGTGCTGCCCACGCTGGCTTCACTTCGCATTGCAGCCTTTGAG
GAGGGGGGTAAATTCGTAGGGCACCGGATCCTGCCTGTCTCTGCCATCCGCTCCGGATAC
CACTACGTCTGCCTGCGGAACGAGGCCAACCAACCGCTGTGCCTGCCGGCCCTGCTCATC
TACACCGAAGCCTCGGACTACATTCCTGACGACCACCAGGACTATGCGGAGGCCCTGATC
AACCCCATTAAGCACGTCAGCCTGATGGACCAGAGGGCCCGGCAGCTGGCCGCCCTCATT
GGGGAGAGTGAGGCTCAGGCTGGCCAAGAGACGTGCCAGGACACCCAGTCTCAGCAGCTG
GGGTCTCAGCCGTCCTCAAACCCCACCCCCAGCCCACTGGATGCCTCCCCCCGCCGGCCC
CCTGGCCCCACCACCTCCCCTGCCAGCACCTCCCTCAGCAGCCCAGGGCAGCGTGATGAT
CTCATCGCCAGCATCCTCTCAGAGGTGGCCCCCACCCCGCTGGATGAGCTCCGAGGTCAC
AAGGCTCTGGTCAAGCTCCGGAGCCGGCAAGAGCGAGACCTGCGGGAGCTGCGCAAGAAG
CATCAGCGGAAGGCAGTCACCCTCACCCGCCGCCTGCTGGATGGCCTGGCTCAGGCACAG
GCTGAGGGCAGGTGCCGGCTGCGGCCAGGTGCCCTAGGTGGGGCCGCTGATGTGGAGGAC
ACGAAGGAGGGGGAGGACGAGGCAAAGCGGTATCAGGAGTTCCAGAACAGACAGGTGCAG
AGCCTGCTGGAGCTGCGGGAGGCCCAGGTGGACGCAGAGGCCCAGCGGAGGCTGGAACAC
CTGAGACAGGCTCTGCAGCGGCTCAGGGAGGTCGTCCTTGATGCAAACACAACTCAGTTC
AAGAGGCTGAAAGAGATGAACGAGAGGGAGAAGAAGGAGCTGCAGAAGATCCTGGACAGA
AAGCGCCATAACAGCATCTCGGAGGCCAAGATGAGGGACAAGCATAAGAAGGAGGCGGAA
CTGACGGAGATTAACCGTCGGCACATCACTGAGTCAGTCAACTCCATCCGTCGGCTGGAG
GAGGCCCAGAAGCAGCGGCATGACCGTCTTGTGGCTGGGCAGCAGCAGGTCCTGCAACAG
CTGGCAGAAGAGGAGCCCAAGCTGCTGGCCCAGCTGGCCCAGGAGTGTCAGGAGCAGCGG
GCGAGGCTCCCCCAGGAGATCCGCCGGAGCCTGCTGGGCGAGATGCCAGAGGGGCTGGGG
GACGGGCCTCTGGTGGCCTGTGCCAGCAACGGTCACGCACCCGGGAGCAGCGGGCACCTG
TCGGGCGCTGACTCGGAGAGCCAGGAGGAGAACACGCAGCTCTGA
Enzyme 21 GenBank Gene ID BC142681 Link Image
Enzyme 21 GeneCard ID PLCB3 Link Image
Enzyme 21 GenAtlas ID PLCB3 Link Image
Enzyme 21 HGNC ID HGNC:9056 Link Image
Enzyme 21 Chromosome Location 1
Enzyme 21 Locus 11q13
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Mazuruk K, Schoen TJ, Chader GJ, Rodriguez IR: Structural organization and expression of the human phosphatidylinositol-specific phospholipase C beta-3 gene. Biochem Biophys Res Commun. 1995 Jul 6;212(1):190-5. [PubMed Link Image]
  2. Lagercrantz J, Carson E, Phelan C, Grimmond S, Rosen A, Dare E, Nordenskjold M, Hayward NK, Larsson C, Weber G: Genomic organization and complete cDNA sequence of the human phosphoinositide-specific phospholipase C beta 3 gene (PLCB3). Genomics. 1995 Apr 10;26(3):467-72. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Carozzi AJ, Kriz RW, Webster C, Parker PJ: Identification, purification and characterization of a novel phosphatidylinositol-specific phospholipase C, a third member of the beta subfamily. Eur J Biochem. 1992 Dec 1;210(2):521-9. [PubMed Link Image]
  5. Oh YS, Jo NW, Choi JW, Kim HS, Seo SW, Kang KO, Hwang JI, Heo K, Kim SH, Kim YH, Kim IH, Kim JH, Banno Y, Ryu SH, Suh PG: NHERF2 specifically interacts with LPA2 receptor and defines the specificity and efficiency of receptor-mediated phospholipase C-beta3 activation. Mol Cell Biol. 2004 Jun;24(11):5069-79. [PubMed Link Image]
  6. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  7. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5462
Enzyme 22 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2
Enzyme 22 Synonyms
  1. Phosphoinositide phospholipase C-gamma-2
  2. Phospholipase C-IV
  3. PLC-IV
  4. Phospholipase C-gamma-2
  5. PLC-gamma-2
Enzyme 22 Gene Name PLCG2
Enzyme 22 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2 
MSTTVNVDSLAEYEKSQIKRALELGTVMTVFSFRKSTPERRTVQVIMETRQVAWSKTADK
IEGFLDIMEIKEIRPGKNSKDFERAKAVRQKEDCCFTILYGTQFVLSTLSLAADSKEDAV
NWLSGLKILHQEAMNASTPTIIESWLRKQIYSVDQTRRNSISLRELKTILPLINFKVSSA
KFLKDKFVEIGAHKDELSFEQFHLFYKKLMFEQQKSILDEFKKDSSVFILGNTDRPDASA
VYLHDFQRFLIHEQQEHWAQDLNKVRERMTKFIDDTMRETAEPFLFVDEFLTYLFSRENS
IWDEKYDAVDMQDMNNPLSHYWISSSHNTYLTGDQLRSESSPEAYIRCLRMGCRCIELDC
WDGPDGKPVIYHGWTRTTKIKFDDVVQAIKDHAFVTSSFPVILSIEEHCSVEQQRHMAKA
FKEVFGDLLLTKPTEASADQLPSPSQLREKIIIKHKKLGPRGDVDVNMEDKKDEHKQQGE
LYMWDSIDQKWTRHYCAIADAKLSFSDDIEQTMEEEVPQDIPPTELHFGEKWFHKKVEKR
TSAEKLLQEYCMETGGKDGTFLVRESETFPNDYTLSFWRSGRVQHCRIRSTMEGGTLKYY
LTDNLTFSSIYALIQHYRETHLRCAEFELRLTDPVPNPNPHESKPWYYDSLSRGEAEDML
MRIPRDGAFLIRKREGSDSYAITFRARGKVKHCRINRDGRHFVLGTSAYFESLVELVSYY
EKHSLYRKMRLRYPVTPELLERYNMERDINSLYDVSRMYVDPSEINPSMPQRTVKALYDY
KAKRSDELSFCRGALIHNVSKEPGGWWKGDYGTRIQQYFPSNYVEDISTADFEELEKQII
EDNPLGSLCRGILDLNTYNVVKAPQGKNQKSFVFILEPKQQGDPPVEFATDRVEELFEWF
QSIREITWKIDTKENNMKYWEKNQSIAIELSDLVVYCKPTSKTKDNLENPDFREIRSFVE
TKADSIIRQKPVDLLKYNQKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALNFQTADKY
MQMNHALFSLNGRTGYVLQPESMRTEKYDPMPPESQRKILMTLTVKVLGARHLPKLGRSI
ACPFVEVEICGAEYDNNKFKTTVVNDNGLSPIWAPTQEKVTFEIYDPNLAFLRFVVYEED
MFSDPNFLAHATYPIKAVKSGFRSVPLKNGYSEDIELASLLVFCEMRPVLESEEELYSSC
RQLRRRQEELNNQLFLYDTHQNLRNANRDALVKEFSVNENQLQLYQEKCNKRLREKRVSN
SKFYS
Enzyme 22 Number of Residues 1265
Enzyme 22 Molecular Weight 147868.7
Enzyme 22 Theoretical pI 6.60
Enzyme 22 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • molecular transducer activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • protein binding
  • signal transducer activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid catabolic process
  • phospholipid metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
—
Enzyme 22 General Function Involved in phosphoinositide phospholipase C activity
Enzyme 22 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling
Enzyme 22 Pathways
Enzyme 22 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 117320537 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID P16885 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name PLCG2_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >3798 bp 
ATGTCCACCACGGTCAATGTAGATTCCCTTGCGGAATATGAGAAGAGCCAGATCAAGAGA
GCCCTGGAGCTGGGGACGGTGATGACTGTGTTCAGCTTCCGCAAGTCCACCCCCGAGCGG
AGAACCGTCCAGGTGATCATGGAGACGCGGCAGGTGGCCTGGAGCAAGACCGCCGACAAG
ATCGAGGGCTTCTTGGATATCATGGAAATAAAAGAAATCCGCCCAGGGAAGAACTCCAAA
GATTTCGAGCGAGCAAAAGCAGTTCGCCAGAAAGAAGACTGCTGCTTCACCATCCTATAT
GGCACTCAGTTCGTCCTCAGCACGCTCAGCTTGGCAGCTGACTCTAAAGAGGATGCAGTT
AACTGGCTCTCTGGCTTGAAAATCTTACACCAGGAAGCGATGAATGCGTCCACGCCCACC
ATTATCGAGAGTTGGCTGAGAAAGCAGATATATTCTGTGGATCAAACCAGAAGAAACAGC
ATCAGTCTCCGAGAGTTGAAGACCATCTTGCCCCTGATCAACTTTAAAGTGAGCAGTGCC
AAGTTCCTTAAAGATAAGTTTGTGGAAATAGGAGCACACAAAGATGAGCTCAGCTTTGAA
CAGTTCCATCTCTTCTATAAAAAACTTATGTTTGAACAGCAAAAATCGATTCTCGATGAA
TTCAAAAAGGATTCGTCCGTGTTCATCCTGGGGAACACTGACAGGCCGGATGCCTCTGCT
GTTTACCTGCATGACTTCCAGAGGTTTCTCATACATGAACAGCAGGAGCATTGGGCTCAG
GATCTGAACAAAGTCCGTGAGCGGATGACAAAGTTCATTGATGACACCATGCGTGAAACT
GCTGAGCCTTTCTTGTTTGTGGATGAGTTCCTCACGTACCTGTTTTCACGAGAAAACAGC
ATCTGGGATGAGAAGTATGACGCGGTGGACATGCAGGACATGAACAACCCCCTGTCTCAT
TACTGGATCTCCTCGTCACATAACACGTACCTTACAGGTGACCAGCTGCGGAGCGAGTCG
TCCCCAGAAGCTTACATCCGCTGCCTGCGCATGGGCTGTCGCTGCATTGAACTGGACTGC
TGGGACGGGCCCGATGGGAAGCCGGTCATCTACCATGGCTGGACGCGGACTACCAAGATC
AAGTTTGACGACGTCGTGCAGGCCATCAAAGACCACGCCTTTGTTACCTCGAGCTTCCCA
GTGATCCTGTCCATCGAGGAGCACTGCAGCGTGGAGCAACAGCGTCACATGGCCAAGGCC
TTCAAGGAAGTATTTGGCGACCTGCTGTTGACGAAGCCCACGGAGGCCAGTGCTGACCAG
CTGCCCTCGCCCAGCCAGCTGCGGGAGAAGATCATCATCAAGCATAAGAAGCTGGGCCCC
CGAGGCGATGTGGATGTCAACATGGAGGACAAGAAGGACGAACACAAGCAACAGGGGGAG
CTGTACATGTGGGATTCCATTGACCAGAAATGGACTCGGCACTACTGCGCCATTGCCGAT
GCCAAGCTGTCCTTCAGTGATGACATTGAACAGACTATGGAGGAGGAAGTGCCCCAGGAT
ATACCCCCTACAGAACTACATTTTGGGGAGAAATGGTTCCACAAGAAGGTGGAGAAGAGG
ACGAGTGCCGAGAAGTTGCTGCAGGAATACTGCATGGAGACGGGGGGCAAGGATGGCACC
TTCCTGGTTCGGGAGAGCGAGACCTTCCCCAATGACTACACCCTGTCCTTCTGGCGGTCA
GGCCGGGTCCAGCACTGCCGGATCCGCTCCACCATGGAGGGCGGGACCCTGAAATACTAC
TTGACTGACAACCTCACCTTCAGCAGCATCTATGCCCTCATCCAGCACTACCGCGAGACG
CACCTGCGCTGCGCCGAGTTCGAGCTGCGGCTCACGGACCCTGTGCCCAACCCCAACCCC
CACGAGTCCAAGCCGTGGTACTATGACAGCCTGAGCCGCGGAGAGGCAGAGGACATGCTG
ATGAGGATTCCCCGGGACGGGGCCTTCCTGATCCGGAAGCGAGAGGGGAGCGACTCCTAT
GCCATCACCTTCAGGGCTAGGGGCAAGGTAAAGCATTGTCGCATCAACCGGGACGGCCGG
CACTTTGTGCTGGGGACCTCCGCCTATTTTGAGAGTCTGGTGGAGCTCGTCAGTTACTAC
GAGAAGCATTCACTCTACCGAAAGATGAGACTGCGCTACCCCGTGACCCCCGAGCTCCTG
GAGCGCTACAATATGGAAAGAGATATAAACTCCCTCTACGACGTCAGCAGAATGTATGTG
GATCCCAGTGAAATCAATCCGTCCATGCCTCAGAGAACCGTGAAAGCTCTGTATGACTAC
AAAGCCAAGCGAAGCGATGAGCTGAGCTTCTGCCGTGGTGCCCTCATCCACAATGTCTCC
AAGGAGCCCGGGGGCTGGTGGAAAGGAGACTATGGAACCAGGATCCAGCAGTACTTCCCA
TCCAACTACGTCGAGGACATCTCAACTGCAGACTTCGAGGAGCTAGAAAAGCAGATTATT
GAAGACAATCCCTTAGGGTCTCTTTGCAGAGGAATATTGGACCTCAATACCTATAACGTC
GTGAAAGCCCCTCAGGGAAAAAACCAGAAGTCCTTTGTCTTCATCCTGGAGCCCAAGCAG
CAGGGCGATCCTCCGGTGGAGTTTGCCACAGACAGGGTGGAGGAGCTCTTTGAGTGGTTT
CAGAGCATCCGAGAGATCACCTGGAAGATTGACACCAAGGAGAACAACATGAAGTACTGG
GAGAAGAACCAGTCCATCGCCATCGAGCTCTCTGACCTGGTTGTCTACTGCAAACCAACC
AGCAAAACCAAGGACAACTTAGAAAATCCTGACTTCCGAGAAATCCGCTCCTTTGTGGAG
ACGAAGGCTGACAGCATCATCAGACAGAAGCCCGTCGACCTCCTGAAGTACAATCAAAAG
GGCCTGACCCGCGTCTACCCAAAGGGACAAAGAGTTGACTCTTCAAACTACGACCCCTTC
CGCCTCTGGCTGTGCGGTTCTCAGATGGTGGCACTCAATTTCCAGACGGCAGATAAGTAC
ATGCAGATGAATCACGCATTGTTTTCTCTCAATGGGCGCACGGGCTACGTTCTGCAGCCT
GAGAGCATGAGGACAGAGAAATATGACCCGATGCCACCCGAGTCCCAGAGGAAGATCCTG
ATGACGCTGACAGTCAAGGTTCTCGGTGCTCGCCATCTCCCCAAACTTGGACGAAGTATT
GCCTGTCCCTTTGTAGAAGTGGAGATCTGTGGAGCCGAGTATGACAACAACAAGTTCAAG
ACGACGGTTGTGAATGATAATGGCCTCAGCCCTATCTGGGCTCCAACACAGGAGAAGGTG
ACATTTGAAATTTATGACCCAAACCTGGCATTTCTGCGCTTTGTGGTTTATGAAGAAGAT
ATGTTCAGCGATCCCAACTTTCTTGCTCATGCCACTTACCCCATTAAAGCAGTCAAATCA
GGATTCAGGTCCGTTCCTCTGAAGAATGGGTACAGCGAGGACATAGAGCTGGCTTCCCTC
CTGGTTTTCTGTGAGATGCGGCCAGTCCTGGAGAGCGAAGAGGAACTTTACTCCTCCTGT
CGCCAGCTGAGGAGGCGGCAAGAAGAACTGAACAACCAGCTCTTTCTGTATGACACACAC
CAGAACTTGCGCAATGCCAACCGGGATGCCCTGGTTAAAGAGTTCAGTGTTAATGAGAAC
CAGCTCCAGCTGTACCAGGAGAAATGCAACAAGAGGTTAAGAGAGAAGAGAGTCAGCAAC
AGCAAGTTTTACTCATAG
Enzyme 22 GenBank Gene ID NM_002661.2 Link Image
Enzyme 22 GeneCard ID PLCG2 Link Image
Enzyme 22 GenAtlas ID PLCG2 Link Image
Enzyme 22 HGNC ID HGNC:9066 Link Image
Enzyme 22 Chromosome Location 1
Enzyme 22 Locus 16q24.1
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Ohta S, Matsui A, Nazawa Y, Kagawa Y: Complete cDNA encoding a putative phospholipase C from transformed human lymphocytes. FEBS Lett. 1988 Dec 19;242(1):31-5. [PubMed Link Image]
  2. Kemmer D, Podowski RM, Arenillas D, Lim J, Hodges E, Roth P, Sonnhammer EL, Hoog C, Wasserman WW: NovelFam3000--uncharacterized human protein domains conserved across model organisms. BMC Genomics. 2006 Mar 13;7:48. [PubMed Link Image]
  3. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Ozdener F, Dangelmaier C, Ashby B, Kunapuli SP, Daniel JL: Activation of phospholipase Cgamma2 by tyrosine phosphorylation. Mol Pharmacol. 2002 Sep;62(3):672-9. [PubMed Link Image]
  6. Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC: Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. Anal Chem. 2004 May 15;76(10):2763-72. [PubMed Link Image]
  7. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  8. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5465
Enzyme 23 Name Diacylglycerol kinase alpha
Enzyme 23 Synonyms
  1. DAG kinase alpha
  2. 80 kDa diacylglycerol kinase
  3. Diglyceride kinase alpha
  4. DGK-alpha
Enzyme 23 Gene Name DGKA
Enzyme 23 Protein Sequence >Diacylglycerol kinase alpha 
MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAKYVQGDAIGYEGFQQFLKIY
LEVDNVPRHLSLALFQSFETGHCLNETNVTKDVVCLNDVSCYFSLLEGGRPEDKLEFTFK
LYDTDRNGILDSSEVDKIILQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSQAEW
VRAGATTVPLLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKY
TVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLTGLHC
VWCHLEIHDDCLQAVGHECDCGLLRDHILPPSSIYPSVLASGPDRKNSKTSQKTMDDLNL
STSEALRIDPVPNTHPLLVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRL
FKDVPDSRILVCGGDGTVGWILETIDKANLPVLPPVAVLPLGTGNDLARCLRWGGGYEGQ
NLAKILKDLEMSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIM
REKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVL
NIPSMHGGSNLWGDTRRPHGDIYGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLE
GAIEMGQIYTKLKNAGRRLAKCSEITFHTTKTLPMQIDGEPWMQTPCTIKITHKNQMPML
MGPPPRSTNFFGFLS
Enzyme 23 Number of Residues 735
Enzyme 23 Molecular Weight 82629.5
Enzyme 23 Theoretical pI 6.71
Enzyme 23 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • diacylglycerol kinase activity
  • ion binding
  • kinase activity
  • metal ion binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
  • cell surface receptor linked signaling pathway
  • intracellular signaling pathway
  • signaling
  • signaling pathway
Component
—
Enzyme 23 General Function Involved in diacylglycerol kinase activity
Enzyme 23 Specific Function Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity
Enzyme 23 Pathways
Enzyme 23 Reactions
  • ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 30823 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID P23743 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name DGKA_HUMAN Link Image
Enzyme 23 PDB ID 1TUZ Link Image
Enzyme 23 PDB File Show
Enzyme 23 3D Structure
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >2208 bp 
ATGGCCAAGGAGAGGGGCCTAATAAGCCCCAGTGATTTTGCCCAGCTGCAAAAATACATG
GAATACTCCACCAAAAAGGTCAGTGATGTCCTAAAGCTCTTCGAGGATGGCGAGATGGCT
AAATATGTCCAAGGAGATGCCATTGGGTACGAGGGATTCCAGCAATTCCTGAAAATCTAT
CTCGAAGTGGATAATGTTCCCAGACACCTAAGCCTGGCACTGTTTCAATCCTTTGAGACT
GGTCACTGCTTAAATGAGACAAATGTGACAAAAGATGTGGTGTGTCTCAATGATGTTTCC
TGCTACTTTTCCCTTCTGGAGGGTGGTCGGCCAGAAGACAAGTTAGAATTCACCTTCAAG
CTGTACGACACGGACAGAAATGGGATCCTGGACAGCTCAGAAGTGGACAAAATTATCCTA
CAGATGATGCGAGTGGCTGAATACCTGGATTGGGATGTGTCTGAGCTGAGGCCGATTCTT
CAGGAGATGATGAAAGAGATTGACTATGATGGCAGTGGCTCTGTCTCTCAAGCTGAGTGG
GTCCGGGCTGGGGCCACCACCGTGCCACTGCTAGTGCTGCTGGGTCTGGAGATGACTCTG
AAGGACGACGGACAGCACATGTGGAGGCCCAAGAGGTTCCCCAGACCAGTCTACTGCAAT
CTGTGCGAGTCAAGCATTGGTCTTGGCAAACAGGGACTGAGCTGTAACCTCTGTAAGTAC
ACTGTTCACGACCAGTGTGCCATGAAAGCCCTGCCTTGTGAAGTCAGCACCTATGCCAAG
TCTCGGAAGGACATTGGTGTCCAATCACATGTGTGGGTGCGAGGAGGCTGTGAGTCCGGG
CGCTGCGACCGCTGTCAGAAAAAGATCCGGATCTACCACAGTCTGACCGGGCTGCATTGT
GTATGGTGCCACCTAGAGATCCACGATGACTGCCTGCAAGCGGTGGGCCATGAGTGTGAC
TGTGGGCTGCTCCGGGATCACATCCTGCCTCCATCTTCCATCTATCCCAGTGTCCTGGCC
TCTGGACCGGATCGTAAAAATAGCAAAACAAGCCAGAAGACCATGGATGATTTAAATTTG
AGCACCTCTGAGGCTCTGCGGATTGACCCTGTTCCTAACACCCACCCACTTCTCGTCTTT
GTCAATCCTAAGAGTGGCGGGAAGCAGGGGCAGAGGGTGCTCTGGAAGTTCCAGTATATA
TTAAACCCTCGACAGGTGTTCAACCTCCTAAAGGATGGTCCTGAGATAGGGCTCCGATTA
TTCAAGGATGTTCCTGATAGCCGGATTTTGGTGTGTGGTGGAGACGGCACAGTAGGCTGG
ATTCTAGAGACCATTGACAAAGCTAACTTGCCAGTTTTGCCTCCTGTTGCTGTGTTGCCC
CTGGGTACTGGAAATGATCTGGCTCGATGCCTAAGATGGGGAGGAGGTTATGAAGGACAG
AATCTGGCAAAGATCCTCAAGGATTTAGAGATGAGTAAAGTGGTACATATGGATCGATGG
TCTGTGGAGGTGATACCTCAACAAACTGAAGAAAAAAGTGACCCAGTCCCCTTTCAAATC
ATCAATAACTACTTCTCTATTGGCGTGGATGCCTCTATTGCTCATCGATTCCACATCATG
CGAGAGAAATATCCGGAGAAGTTCAACAGCAGAATGAAGAACAAGCTATGGTACTTCGAA
TTTGCCACATCTGAATCCATCTTCTCAACATGCAAAAAGCTGGAGGAGTCTTTGACAGTT
GAGATCTGTGGGAAACCGCTGGATCTGAGCAACCTGTCCCTAGAAGGCATCGCAGTGCTA
AACATCCCTAGCATGCATGGTGGCTCCAACCTCTGGGGTGATACCAGGAGACCCCATGGG
GATATCTATGGGATCAACCAGGCCTTAGGTGCTACAGCTAAAGTCATCACCGACCCTGAT
ATCCTGAAAACCTGTGTACCAGACCTAAGTGACAAGAGACTGGAAGTGGTTGGGCTGGAG
GGTGCAATTGAGATGGGCCAAATCTATACCAAGCTCAAGAATGCTGGACGTCGGCTGGCC
AAGTGCTCTGAGATCACCTTCCACACCACAAAAACCCTTCCCATGCAAATTGACGTAGAA
CCCTGGATGCAGACGCCCTGTACAATCAAGATCACCCACAAGAACCAGATGCCCATGCTC
ATGGGCCCACCCCCCCGCTCCACCAATTTCTTTGGCTTCTTGAGCTAA
Enzyme 23 GenBank Gene ID X62535 Link Image
Enzyme 23 GeneCard ID DGKA Link Image
Enzyme 23 GenAtlas ID DGKA Link Image
Enzyme 23 HGNC ID HGNC:2849 Link Image
Enzyme 23 Chromosome Location 1
Enzyme 23 Locus 12q13.3
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Schaap D, de Widt J, van der Wal J, Vandekerckhove J, van Damme J, Gussow D, Ploegh HL, van Blitterswijk WJ, van der Bend RL: Purification, cDNA-cloning and expression of human diacylglycerol kinase. FEBS Lett. 1990 Nov 26;275(1-2):151-8. [PubMed Link Image]
  2. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Hart TC, Champagne C, Zhou J, Van Dyke TE: Assignment of the gene for diacylglycerol kinase (DAGK) to human chromosome 12. Mamm Genome. 1994 Feb;5(2):123-4. [PubMed Link Image]
  5. Hart TC, Zhou J, Champagne C, Van Dyke TE, Rao PN, Pettenati MJ: Assignment of the human diacylglycerol kinase gene (DAGK) to 12q13.3 using fluorescence in situ hybridization analysis. Genomics. 1994 Jul 1;22(1):246-7. [PubMed Link Image]
  6. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  7. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  8. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 5476
Enzyme 24 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1
Enzyme 24 Synonyms
  1. PLC-148
  2. Phosphoinositide phospholipase C-gamma-1
  3. Phospholipase C-II
  4. PLC-II
  5. Phospholipase C-gamma-1
  6. PLC-gamma-1
Enzyme 24 Gene Name PLCG1
Enzyme 24 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1 
MAGAASPCANGCGPGAPSDAEVLHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQI
TWSRGADKIEGAIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTL
SLQATSEDEVNMWIKGLTWLMEDTLQAPTPLQIERWLRKQFYSVDRNREDRISAKDLKNM
LSQVNYRVPNMRFLRERLTDLEQRSGDITYGQFAQLYRSLMYSAQKTMDLPFLEASTLRA
GERPELCRVSLPEFQQFLLDYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDEFVT
FLFSKENSVWNSQLDAVCPDTMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMG
CRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLHTIKEHAFVASEYPVILSIEDHCSIA
QQRNMAQYFKKVLGDTLLTKPVEISADGLPSPNQLKRKILIKHKKLAEGSAYEEVPTSMM
YSENDISNSIKNGILYLEDPVNHEWYPHYFVLTSSKIYYSEETSSDQGNEDEEEPKEVSS
STELHSNEKWFHGKLGAGRDGRHIAERLLTEYCIETGAPDGSFLVRESETFVGDYTLSFW
RNGKVQHCRIHSRQDAGTPKFFLTDNLVFDSLYDLITHYQQVPLRCNEFEMRLSEPVPQT
NAHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQE
GQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEEALEKIGTAEPDYGALYEGRNP
GFYVEANPMPTFKCAVKALFDYKAQREDELTFIKSAIIQNVEKQEGGWWRGDYGGKKQLW
FPSNYVEEMVNPVALEPEREHLDENSPLGDLLRGVLDVPACQIAIRPEGKNNRLFVFSIS
MASVAHWSLDVAADSQEELQDWVKKIREVAQTADARLTEGKIMERRKKIALELSELVVYC
RPVPFDEEKIGTERACYRDMSSFPETKAEKYVNKAKGKKFLQYNRLQLSRIYPKGQRLDS
SNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMTGRHCGYVLQPSTMRDEAFDPFDKS
SLRGLEPCAISIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSTKQKTEFVVDNGLNPVW
PAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQATFPVKGLKTGYRAVPLKNNYSEDL
ELASLLIKIDIFPAKENGDLSPFSGTSLRERGSDASGQLFHGRAREGSFESRYQQPFEDF
RISQEHLADHFDSRERRAPRRTRVNGDNRL
Enzyme 24 Number of Residues 1290
Enzyme 24 Molecular Weight 148530.8
Enzyme 24 Theoretical pI 5.91
Enzyme 24 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • molecular transducer activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
  • protein binding
  • signal transducer activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid catabolic process
  • phospholipid metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
—
Enzyme 24 General Function Involved in calcium ion binding
Enzyme 24 Specific Function PLC-gamma is a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase
Enzyme 24 Pathways
Enzyme 24 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 3336979 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID P19174 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name PLCG1_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >3873 bp 
ATGGCGGGCGCCGCGTCCCCTTGCGCCAACGGCTGCGGGCCCGGCGCGCCCTCGGACGCC
GAGGTGCTGCACCTCTGCCGCAGCCTCGAGGTGGGCACCGTCATGACTTTGTTCTACTCC
AAGAAGTCGCAGCGACCCGAGCGGAAGACCTTCCAGGTCAAGCTGGAGACGCGCCAGATC
ACGTGGAGCCGGGGCGCCGACAAGATCGAGGGGGCCATTGACATTCGTGAAATTAAGGAG
ATCCGCCCAGGGAAGACCTCACGGGACTTTGATCGCTATCAAGAGGACCCAGCTTTCCGG
CCGGACCAGTCACATTGCTTTGTCATTCTCTATGGAATGGAATTTCGCCTGAAAACGCTG
AGCCTGCAAGCCACATCTGAGGATGAAGTGAACATGTGGATCAAGGGCTTAACTTGGCTG
ATGGAGGATACATTGCAGGCACCCACACCCCTGCAGATTGAGAGGTGGCTCCGGAAGCAG
TTTTACTCAGTGGATCGGAATCGTGAGGATCGTATATCAGCCAAGGACCTGAAGAACATG
CTGTCCCAGGTCAACTACCGGGTCCCCAACATGCGCTTCCTCCGAGAGCGGCTGACGGAC
CTGGAGCAGCGCAGCGGGGACATCACCTACGGGCAGTTTGCTCAGCTGTACCGCAGCCTC
ATGTACAGCGCCCAGAAGACGATGGACCTCCCCTTCTTGGAAGCCAGTACTCTGAGGGCT
GGGGAGCGGCCGGAGCTTTGCCGAGTGTCCCTTCCTGAGTTCCAGCAGTTCCTTCTTGAC
TACCAGGGGGAGCTGTGGGCTGTTGATCGCCTCCAGGTGCAGGAGTTCATGCTCAGCTTC
CTCCGAGACCCCTTACGAGAGATCGAGGAGCCATACTTCTTCCTGGATGAGTTTGTCACC
TTCCTGTTCTCCAAAGAGAACAGTGTGTGGAACTCGCAGCTGGATGCAGTATGCCCGGAC
ACCATGAACAACCCTCTTTCCCACTACTGGATCTCCTCCTCGCACAACACGTACCTGACC
GGGGACCAGTTCTCCAGTGAGTCCTCCTTGGAAGCCTATGCTCGCTGCCTGCGGATGGGC
TGTCGCTGCATTGAGTTGGACTGCTGGGACGGCCCGGATGGGATGCCAGTTATTTACCAT
GGGCACACCCTTACCACCAAGATCAAGTTCTCAGATGTCCTGCACACCATCAAGGAGCAT
GCCTTTGTGGCCTCAGAGTACCCAGTCATCCTGTCCATTGAGGACCACTGCAGCATTGCC
CAGCAGAGAAACATGGCCCAATACTTCAAGAAGGTGCTGGGGGACACACTCCTCACCAAG
CCCGTGGAGATCTCTGCCGACGGGCTCCCCTCACCCAACCAGCTTAAGAGGAAGATCCTC
ATCAAGCACAAGAAGCTGGCTGAGGGCAGTGCCTACGAGGAGGTGCCTACATCCATGATG
TACTCTGAGAACGACATCAGCAACTCTATCAAGAATGGCATCCTCTACCTGGAGGACCCT
GTGAACCACGAATGGTATCCCCACTACTTTGTTCTGACCAGCAGCAAGATCTACTACTCT
GAGGAGACCAGCAGTGACCAGGGCAACGAGGATGAGGAGGAGCCCAAGGAGGTCAGCAGC
AGCACAGAGCTGCACTCCAATGAGAAGTGGTTCCATGGGAAGCTAGGGGCAGGGCGTGAC
GGGCGTCACATCGCTGAGCGCCTGCTTACTGAGTACTGCATCGAGACCGGAGCCCCTGAC
GGCTCCTTCCTCGTGCGAGAGAGTGAGACCTTCGTGGGCGACTACACGCTCTCTTTCTGG
CGGAACGGGAAAGTCCAGCACTGCCGTATCCACTCCCGGCAAGATGCTGGGACCCCCAAG
TTCTTCTTGACAGACAACCTCGTCTTTGACTCCCTCTATGACCTCATCACGCACTACCAG
CAGGTGCCCCTGCGCTGTAATGAGTTTGAGATGCGACTTTCAGAGCCTGTCCCACAGACC
AACGCCCACGAGAGCAAAGAGTGGTACCACGCGAGCCTGACCAGAGCACAGGCTGAGCAC
ATGCTAATGCGCGTCCCTCGTGATGGGGCCTTCCTGGTGCGGAAGCGGAATGAACCCAAC
TCATATGCCATCTCTTTCCGGGCTGAGGGCAAGATCAAGCATTGCCGTGTCCAGCAAGAG
GGCCAGACAGTGATGCTAGGGAACTCGGAGTTCGACAGCCTTGTTGACCTCATCAGCTAC
TATGAGAAACACCCGCTATACCGCAAGATGAAGCTGCGCTATCCCATCAACGAGGAGGCA
CTGGAGAAGATTGGCACAGCTGAGCCTGACTACGGGGCCCTGTATGAGGGACGCAACCCT
GGCTTCTATGTAGAGGCAAACCCTATGCCAACTTTCAAGTGTGCAGTCAAAGCCCTCTTT
GACTACAAGGCCCAGAGGGAGGACGAGCTGACCTTCATCAAGAGCGCCATCATCCAGAAT
GTGGAGAAGCAAGAGGGAGGCTGGTGGCGAGGGGACTACGGAGGGAAGAAGCAGCTGTGG
TTCCCATCAAACTACGTGGAAGAGATGGTCAACCCCGTGGCCCTGGAGCCGGAGAGGGAG
CACTTGGACGAGAACAGCCCCCTAGGGGACTTGCTGCGGGGGGTCTTGGATGTGCCGGCT
TGTCAGATTGCCATCCGTCCTGAGGGCAAGAACAACCGGCTCTTCGTCTTCTCCATCAGC
ATGGCGTCGGTGGCCCACTGGTCCCTGGATGTTGCTGCCGACTCACAGGAGGAGCTGCAG
GACTGGGTGAAAAAGATCCGTGAAGTGGCCCAGACAGCAGACGCCAGGCTCACTGAAGGG
AAGATAATGGAACGGAGGAAGAAGATTGCCCTGGAGCTCTCTGAACTTGTCGTCTACTGC
CGGCCTGTTCCCTTTGATGAAGAGAAGATTGGCACAGAACGTGCTTGCTACCGGGACATG
TCATCCTTCCCGGAAACCAAGGCTGAGAAATACGTGAACAAGGCCAAAGGCAAGAAGTTC
CTTCAGTACAATCGACTGCAGCTCTCCCGCATCTACCCCAAGGGCCAGCGACTGGATTCC
TCCAACTACGATCCTTTGCCCATGTGGATCTGTGGCAGTCAGCTTGTGGCCCTCAACTTC
CAGACCCCTGACAAGCCTATGCAGATGAACCAGGCCCTCTTCATGACGGGCAGGCACTGT
GGCTACGTGCTGCAGCCAAGCACCATGCGGGATGAGGCCTTCGACCCCTTTGACAAGAGC
AGCCTCCGCGGGCTGGAGCCATGTGCCATCTCTATTGAGGTGCTGGGGGCCCGACATCTG
CCAAAGAATGGCCGAGGCATTGTGTGTCCTTTTGTGGAGATTGAGGTGGCTGGAGCTGAG
TATGACAGCACCAAGCAGAAGACAGAGTTTGTGGTGGACAATGGACTCAACCCTGTATGG
CCAGCCAAGCCCTTCCACTTCCAGATCAGTAACCCTGAATTTGCCTTTCTGCGCTTCGTG
GTGTATGAGGAAGACATGTTTAGTGACCAGAATTTCCTGGCTCAGGCTACTTTCCCAGTA
AAAGGCCTGAAGACAGGATACAGAGCAGTGCCTTTGAAGAACAACTACAGTGAGGACCTG
GAGTTGGCCTCCCTGCTGATCAAGATTGACATTTTCCCTGCCAAGGAGAATGGTGACCTC
AGTCCCTTCAGTGGTACGTCCCTGCGGGAGCGGGGCTCAGATGCCTCAGGCCAGCTGTTT
CATGGCCGAGCCCGGGAAGGCTCCTTTGAATCCCGCTACCAGCAGCCGTTTGAGGACTTC
CGCATCTCCCAGGAGCATCTCGCAGACCATTTTGACAGTCGAGAACGAAGGGCCCCAAGA
AGGACTCGGGTCAATGGAGACAACCGCCTCTAG
Enzyme 24 GenBank Gene ID AL022394 Link Image
Enzyme 24 GeneCard ID PLCG1 Link Image
Enzyme 24 GenAtlas ID PLCG1 Link Image
Enzyme 24 HGNC ID HGNC:9065 Link Image
Enzyme 24 Chromosome Location 2
Enzyme 24 Locus 20q12-q13.1
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Burgess WH, Dionne CA, Kaplow J, Mudd R, Friesel R, Zilberstein A, Schlessinger J, Jaye M: Characterization and cDNA cloning of phospholipase C-gamma, a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase. Mol Cell Biol. 1990 Sep;10(9):4770-7. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Zhang W, Sloan-Lancaster J, Kitchen J, Trible RP, Samelson LE: LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell. 1998 Jan 9;92(1):83-92. [PubMed Link Image]
  5. Lindholm CK, Gylfe E, Zhang W, Samelson LE, Welsh M: Requirement of the Src homology 2 domain protein Shb for T cell receptor-dependent activation of the interleukin-2 gene nuclear factor for activation of T cells element in Jurkat T cells. J Biol Chem. 1999 Sep 24;274(39):28050-7. [PubMed Link Image]
  6. Felschow DM, Civin CI, Hoehn GT: Characterization of the tyrosine kinase Tnk1 and its binding with phospholipase C-gamma1. Biochem Biophys Res Commun. 2000 Jun 24;273(1):294-301. [PubMed Link Image]
  7. Korkaya H, Jameel S, Gupta D, Tyagi S, Kumar R, Zafrullah M, Mazumdar M, Lal SK, Xiaofang L, Sehgal D, Das SR, Sahal D: The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK. J Biol Chem. 2001 Nov 9;276(45):42389-400. Epub 2001 Aug 22. [PubMed Link Image]
  8. Rebhun JF, Chen H, Quilliam LA: Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral. J Biol Chem. 2000 May 5;275(18):13406-10. [PubMed Link Image]
  9. Taguchi T, Kiyokawa N, Takenouch H, Matsui J, Tang WR, Nakajima H, Suzuki K, Shiozawa Y, Saito M, Katagiri YU, Takahashi T, Karasuyama H, Matsuo Y, Okita H, Fujimoto J: Deficiency of BLNK hampers PLC-gamma2 phosphorylation and Ca2+ influx induced by the pre-B-cell receptor in human pre-B cells. Immunology. 2004 Aug;112(4):575-82. [PubMed Link Image]
  10. Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM: Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics. 2005 Sep;4(9):1240-50. Epub 2005 Jun 11. [PubMed Link Image]
  11. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  12. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  13. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  14. Wolf-Yadlin A, Hautaniemi S, Lauffenburger DA, White FM: Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5860-5. Epub 2007 Mar 26. [PubMed Link Image]
  15. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed Link Image]
  16. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  17. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  18. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  19. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  20. Kohda D, Hatanaka H, Odaka M, Mandiyan V, Ullrich A, Schlessinger J, Inagaki F: Solution structure of the SH3 domain of phospholipase C-gamma. Cell. 1993 Mar 26;72(6):953-60. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 5479
Enzyme 25 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1
Enzyme 25 Synonyms
  1. Phosphoinositide phospholipase C-delta-1
  2. Phospholipase C-III
  3. PLC-III
  4. Phospholipase C-delta-1
  5. PLC-delta-1
Enzyme 25 Gene Name PLCD1
Enzyme 25 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1 
MDSGRDFLTLHGLQDDEDLQALLKGSQLLKVKSSSWRRERFYKLQEDCKTIWQESRKVMR
TPESQLFSIEDIQEVRMGHRTEGLEKFARDVPEDRCFSIVFKDQRNTLDLIAPSPADAQH
WVLGLHKIIHHSGSMDQRQKLQHWIHSCLRKADKNKDNKMSFKELQNFLKELNIQVDDSY
ARKIFRECDHSQTDSLEDEEIEAFYKMLTQRVEIDRTFAEAAGSGETLSVDQLVTFLQHQ
QREEAAGPALALSLIERYEPSETAKAQRQMTKDGFLMYLLSADGSAFSLAHRRVYQDMGQ
PLSHYLVSSSHNTYLLEDQLAGPSSTEAYIRALCKGCRCLELDCWDGPNQEPIIYHGYTF
TSKILFCDVLRAIRDYAFKASPYPVILSLENHCTLEQQRVMARHLHAILGPMLLNRPLDG
VTNSLPSPEQLKGKILLKGKKLGGLLPPGGEGGPEATVVSDEDEAAEMEDEAVRSRVQHK
PKEDKLRLAQELSDMVIYCKSVHFGGFSSPGTPGQAFYEMASFSENRALRLLQESGNGFV
RHNVGHLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYQGRFQDNGACG
YVLKPAFLRDPNGTFNPRALAQGPWWARKRLNIRVISGQQLPKVNKNKNSIVDPKVTVEI
HGVSRDVASRQTAVITNNGFNPWWDTEFAFEVVVPDLALIRFLVEDYDASSKNDFIGQST
IPLNSLKQGYRHVHLMSKNGDQHPSATLFVKISLQD
Enzyme 25 Number of Residues 756
Enzyme 25 Molecular Weight 85664.3
Enzyme 25 Theoretical pI 6.68
Enzyme 25 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • metal ion binding
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • biological regulation
  • intracellular signaling pathway
  • lipid metabolic process
  • metabolic process
  • primary metabolic process
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
  • signaling
  • signaling pathway
Component
—
Enzyme 25 General Function Involved in calcium ion binding
Enzyme 25 Specific Function The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. Essential for trophoblast and placental development
Enzyme 25 Pathways
Enzyme 25 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 37572274 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID P51178 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name PLCD1_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >2271 bp 
ATGGACTCGGGCCGGGACTTCCTGACCCTGCACGGCCTACAGGATGATGAGGATCTACAG
GCGCTGCTGAAGGGCAGCCAGCTCCTGAAGGTGAAGTCCAGCTCATGGAGGAGAGAGCGC
TTCTACAAGTTGCAGGAGGACTGCAAGACCATCTGGCAGGAGTCCCGCAAGGTCATGCGG
ACCCCGGAGTCCCAGCTGTTCTCCATCGAGGACATTCAGGAGGTGCGAATGGGGCACCGC
ACGGAGGGTCTGGAGAAGTTCGCCCGTGATGTGCCCGAGGACCGCTGCTTCTCCATTGTC
TTCAAGGACCAGCGCAATACACTAGACCTCATCGCCCCATCGCCAGCTGATGCCCAGCAC
TGGGTGCTGGGGCTGCACAAGATCATCCACCACTCAGGCTCCATGGACCAGCGTCAGAAG
CTACAGCACTGGATTCACTCCTGCTTGCGAAAAGCTGACAAAAACAAGGACAACAAGATG
AGCTTCAAGGAGCTGCAGAACTTCCTGAAGGAGCTCAACATCCAGGTGGACGACAGCTAT
GCCCGGAAGATCTTCAGGGAGTGTGACCACTCCCAGACAGACTCCCTGGAGGACGAGGAG
ATTGAGGCCTTCTACAAGATGCTGACCCAGCGGGTGGAGATCGACCGCACCTTCGCCGAG
GCCGCGGGCTCAGGGGAGACTCTGTCGGTGGATCAGTTAGTGACGTTCCTGCAGCACCAG
CAGCGGGAGGAGGCGGCAGGGCCTGCGCTGGCCCTCTCCCTCATTGAGCGCTACGAGCCC
AGCGAGACTGCCAAGGCGCAGCGGCAGATGACCAAGGACGGCTTCCTCATGTACTTACTG
TCGGCTGACGGCAGCGCCTTCAGCCTGGCACACCGCCGTGTCTACCAGGACATGGGCCAG
CCACTTAGCCACTACCTGGTGTCCTCTTCACACAACACCTACCTGCTGGAGGACCAGCTA
GCCGGGCCCAGCAGCACTGAAGCCTACATCCGGGCACTGTGCAAAGGCTGCCGATGCCTG
GAGCTTGACTGCTGGGACGGGCCCAACCAGGAACCAATCATCTACCACGGCTATACTTTC
ACTTCCAAGATCCTCTTCTGCGATGTGCTCAGGGCCATCCGGGACTATGCCTTCAAGGCG
TCCCCCTACCCTGTCATCCTATCCCTGGAGAACCACTGCACACTGGAGCAGCAGCGCGTG
ATGGCGCGGCACCTGCATGCCATCCTGGGCCCCATGCTGTTGAACCGACCACTGGATGGG
GTCACCAACAGCCTGCCCTCCCCTGAGCAACTGAAGGGGAAGATCCTGCTGAAGGGGAAG
AAGCTCGGGGGGCTCCTGCCCCCTGGAGGGGAGGGTGGCCCTGAGGCCACTGTGGTGTCA
GACGAAGACGAGGCTGCTGAGATGGAGGATGAGGCAGTGAGGAGCCGTGTGCAGCACAAG
CCCAAGGAGGACAAGCTCAGGCTAGCACAGGAGCTCTCTGACATGGTCATTTACTGCAAG
AGTGTCCACTTTGGGGGCTTCTCCAGTCCTGGCACCCCTGGACAGGCCTTCTACGAGATG
GCGTCCTTCTCTGAGAACCGTGCCCTTCGACTGCTCCAAGAATCAGGAAACGGCTTTGTC
CGCCACAACGTGGGGCACCTGAGCAGAATCTACCCGGCTGGATGGAGAACAGACTCCTCC
AACTACAGCCCCGTGGAGATGTGGAATGGGGGCTGCCAGATCGTGGCCCTGAATTTCCAG
ACACCTGGGCCAGAGATGGACGTGTACCAGGGCCGCTTCCAGGACAACGGGGCCTGTGGG
TACGTGCTGAAGCCCGCCTTCCTGCGAGACCCCAACGGCACCTTTAACCCCCGCGCCCTG
GCTCAGGGGCCCTGGTGGGCACGGAAGCGGCTCAACATCAGGGTCATTTCGGGGCAGCAG
CTGCCAAAAGTCAACAAGAATAAGAATTCAATTGTGGACCCCAAAGTGACAGTGGAGATC
CATGGCGTGAGCCGGGACGTGGCCAGCCGCCAGACTGCTGTCATCACCAACAATGGTTTC
AACCCATGGTGGGACACGGAGTTTGCGTTTGAGGTAGTTGTGCCTGACCTTGCCCTCATC
CGCTTCTTGGTGGAAGATTATGATGCCTCCTCCAAGAATGACTTCATTGGCCAGAGTACC
ATCCCCTTGAACAGCCTCAAGCAAGGATACCGCCATGTCCACCTCATGTCTAAGAACGGG
GACCAGCATCCATCAGCCACCCTCTTTGTGAAGATCTCCCTCCAGGACTAG
Enzyme 25 GenBank Gene ID BC050382 Link Image
Enzyme 25 GeneCard ID PLCD1 Link Image
Enzyme 25 GenAtlas ID PLCD1 Link Image
Enzyme 25 HGNC ID HGNC:9060 Link Image
Enzyme 25 Chromosome Location 3
Enzyme 25 Locus 3p22-p21.3
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Cheng HF, Jiang MJ, Chen CL, Liu SM, Wong LP, Lomasney JW, King K: Cloning and identification of amino acid residues of human phospholipase C delta 1 essential for catalysis. J Biol Chem. 1995 Mar 10;270(10):5495-505. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 5508
Enzyme 26 Name Thyroid peroxidase
Enzyme 26 Synonyms
  1. TPO
Enzyme 26 Gene Name TPO
Enzyme 26 Protein Sequence >Thyroid peroxidase 
MRALAVLSVTLVMACTEAFFPFISRGKELLWGKPEESRVSSVLEESKRLVDTAMYATMQR
NLKKRGILSPAQLLSFSKLPEPTSGVIARAAEIMETSIQAMKRKVNLKTQQSQHPTDALS
EDLLSIIANMSGCLPYMLPPKCPNTCLANKYRPITGACNNRDHPRWGASNTALARWLPPV
YEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHD
IAFTPQSTSKAAFGGGADCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGD
QGALFGNLSTANPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAEGLLRVHARLRDSG
RAYLPFVPPRAPAACAPEPGIPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAA
LKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPT
VSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIR
GLLARPAKLQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGL
PRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQ
MKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFES
CDSITGMNLEAWRETFPQDDKCGFPESVENGDFVHCEESGRRVLVYSCRHGYELQGREQL
TCTQEGWDFQPPLCKDVNECADGAHPPCHASARCRNTKGGFQCLCADPYELGDDGRTCVD
SGRLPRVTWISMSLAALLIGGFAGLTSTVICRWTRTGTKSTLPISETGGGTPELRCGKHQ
AVGTSPQRAAAQDSEQESAGMEGRDTHRLPRAL
Enzyme 26 Number of Residues 933
Enzyme 26 Molecular Weight 102961.6
Enzyme 26 Theoretical pI 6.75
Enzyme 26 GO Classification
Function
  • antioxidant activity
  • binding
  • calcium ion binding
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • peroxidase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
—
Enzyme 26 General Function Involved in calcium ion binding
Enzyme 26 Specific Function Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4)
Enzyme 26 Pathways
Enzyme 26 Reactions
  • 2 iodide + H2O2 + 2 H+ = diiodine + 2 H2O [RN:R02810]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • 1-14
Enzyme 26 Transmembrane Regions
  • 847-871
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 339867 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P07202 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name PERT_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >2802 bp 
ATGAGAGCGCTCGCTGTGCTGTCTGTCACGCTGGTTATGGCCTGCACAGAAGCCTTCTTC
CCCTTCATCTCGAGAGGGAAAGAACTCCTTTGGGGAAAGCCTGAGGAGTCTCGTGTCTCT
AGCGTCTTGGAGGAAAGCAAGCGCCTGGTGGACACCGCCATGTACGCCACGATGCAGAGA
AACCTCAAGAAAAGAGGAATCCTTTCTCCAGCTCAGCTTCTGTCTTTTTCCAAACTTCCT
GAGCCAACAAGCGGAGTGATTGCCCGAGCAGCAGAGATAATGGAAACATCAATACAAGCG
ATGAAAAGAAAAGTCAACCTGAAAACTCAACAATCACAGCATCCAACGGATGCTTTATCA
GAAGATCTGCTGAGCATCATTGCAAACATGTCTGGATGTCTCCCTTACATGCTGCCCCCA
AAATGCCCAAACACTTGCCTGGCGAACAAATACAGGCCCATCACAGGAGCTTGCAACAAC
AGAGACCACCCCAGATGGGGCGCCTCCAACACGGCCCTGGCACGATGGCTCCCTCCAGTC
TATGAGGACGGCTTCAGTCAGCCCCGAGGCTGGAACCCCGGCTTCTTGTACAACGGGTTC
CCACTGCCCCCGGTCCGGGAGGTGACAAGACATGTCATTCAAGTTTCAAATGAGGTTGTC
ACAGATGATGACCGCTATTCTGACCTCCTGATGGCATGGGGACAATACATCGACCACGAC
ATCGCGTTCACACCACAGAGCACCAGCAAAGCTGCCTTCGGGGGAGGGGCTGACTGCCAG
ATGACTTGTGAGAACCAAAACCCATGTTTTCCCATACAACTCCCGGAGGAGGCCCGGCCG
GCCGCGGGCACCGCCTGTCTGCCCTTCTACCGCTCTTCGGCCGCCTGCGGCACCGGGGAC
CAAGGCGCGCTCTTTGGGAACCTGTCCACGGCCAACCCGCGGCAGCAGATGAACGGGTTG
ACCTCGTTCCTGGACGCGTCCACCGTGTATGGCAGCTCCCCGGCCCTAGAGAGGCAGCTG
CGGAACTGGACCAGTGCCGAAGGGCTGCTCCGCGTCCACGCGCGCCTCCGGGACTCCGGC
CGCGCCTACCTGCCCTTCGTGCCGCCACGGCGGCCTGCGGCCTGTGCGCCCGAGCCCGGC
ATCCCCGGAGAGACCCGCGGGCCCTGCTTCCTGGCCGGAGACGGCCGCGCCAGCGAGGTC
CCCTCCCTGACGGCACTGCACACGCTGTGGCTGCGCGAGCACAACCGCCTGGCCGCGGCG
CTCAAGGCCCTCAATGCGCACTGGAGCGCGGACGCCGTGTACCAGGAGGCGCGCAAGGTC
GTGGGCGCTCTGCACCAGATCATCACCCTGAGGGATTACATCCCCAGGATCCTGGGACCC
GAGGCCTTCCAGCAGTACGTGGGTCCCTATGAAGGCTATGACTCCACCGCCAACCCCACT
GTGTCCAACGTGTTCTCCACAGCCGCCTTCCGCTTCGGCCATGCCACGATCCACCCGCTG
GTGAGGAGGCTGGACGCCAGCTTCCAGGAGCACCCCGACCTGCCCGGGCTGTGGCTGCAC
CAGGCTTTCTTCAGCCCATGGACATTACTCCGTGGAGGTGGTTTGGACCCACTAATACGA
GGCCTTCTTGCAAGACCAGCCAAACTGCAGGTGCAGGATCAGCTGATGAACGAGGAGCTG
ACGGAAAGGCTCTTTGTGCTGTCCAATTCCAGCACCTTGGATCTGGCGTCCATCAACCTG
CAGAGGGGCCGGGACCACGGGCTGCCAGGTTACAATGAGTGGAGGGAGTTCTGCGGCCTG
CCTCGCCTGGAGACCCCCGCTGACCTGAGCACAGCCATCGCCAGCAGGAGCGTGGCCGAC
AAGATCCTGGACTTGTACAAGCATCCTGACAACATCGATGTCTGGCTGGGAGGCTTAGCT
GAAAACTTCCTCCCCAGGGCTCGGACAGGGCCCCTGTTTGCCTGTCTCATTGGGAAGCAG
ATGAAGGCTCTGCGGGATGGTGACTGGTTTTGGTGGGAGAACAGCCACGTCTTCACGGAT
GCACAGAGGCGTGAGCTGGAGAAGCACTCCCTGTCTCGGGTCATCTGTGACAACACTGGC
CTCACCAGGGTGCCCATGGATGCCTTCCAAGTCGGCAAATTCCCTGAAGACTTTGAGTCT
TGTGACAGCATCCCTGGCATGAACCTGGAGGCCTGGAGGGAAACCTTTCCTCAAGACGAC
AAGTGTGGCTTCCCAGAGAGCGTGGAGAATGGGGACTTTGTGCACTGTGAGGAGTCTGGG
AGGCGCGTGCTGGTGTATTCCTGCCGGCACGGGTATGAGCTCCAAGGCCGGGAGCAGCTC
ACTTGCACCCAGGAAGGATGGGATTTCCAGCCTCCCCTCTGCAAAGATGTGAACGAGTGT
GCAGACGGTGCCCACCCCCCCTGCCACGCCTCTGCGAGGTGCAGAAACACCAAAGGCGGC
TTCCAGTGTCTCTGCGCGGACCCCTACGAGTTAGGAGACGATGGGAGAACCTGCGTAGAC
TCCGGGAGGCTCCCTCGGGCGACTTGGATCTCCATGTCGCTGGCTGCTCTGCTGATCGGA
GGCTTCGCAGGTCTCACCTCGACGGTGATTTGCAGGTGGACACGCACTGGCACTAAATCC
ACACTGCCCATCTCGGAGACAGGCGGAGGAACTCCCGAGCTGAGATGCGGAAAGCACCAG
GCCGTAGGGACCTCACCGCAGCGGGCCGCAGCTCAGGACTCGGAGCAGGAGAGTGCTGGG
ATGGAAGGCCGGGATACTCACAGGCTGCCGAGAGCCCTCTGA
Enzyme 26 GenBank Gene ID J02969 Link Image
Enzyme 26 GeneCard ID TPO Link Image
Enzyme 26 GenAtlas ID TPO Link Image
Enzyme 26 HGNC ID HGNC:12015 Link Image
Enzyme 26 Chromosome Location 2
Enzyme 26 Locus 2p25
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Kimura S, Kotani T, McBride OW, Umeki K, Hirai K, Nakayama T, Ohtaki S: Human thyroid peroxidase: complete cDNA and protein sequence, chromosome mapping, and identification of two alternately spliced mRNAs. Proc Natl Acad Sci U S A. 1987 Aug;84(16):5555-9. [PubMed Link Image]
  2. Libert F, Ruel J, Ludgate M, Swillens S, Alexander N, Vassart G, Dinsart C: Complete nucleotide sequence of the human thyroperoxidase-microsomal antigen cDNA. Nucleic Acids Res. 1987 Aug 25;15(16):6735. [PubMed Link Image]
  3. Kimura S, Hong YS, Kotani T, Ohtaki S, Kikkawa F: Structure of the human thyroid peroxidase gene: comparison and relationship to the human myeloperoxidase gene. Biochemistry. 1989 May 16;28(10):4481-9. [PubMed Link Image]
  4. Barnett PS, Banga JP, Watkins J, Huang GC, Gluckman DR, Page MJ, McGregor AM: Nucleotide sequence of the alternatively spliced human thyroid peroxidase cDNA, TPO-2. Nucleic Acids Res. 1990 Feb 11;18(3):670. [PubMed Link Image]
  5. Ferrand M, Le Fourn V, Franc JL: Increasing diversity of human thyroperoxidase generated by alternative splicing. Characterized by molecular cloning of new transcripts with single- and multispliced mRNAs. J Biol Chem. 2003 Feb 7;278(6):3793-800. Epub 2002 Nov 25. [PubMed Link Image]
  6. Seto P, Hirayu H, Magnusson RP, Gestautas J, Portmann L, DeGroot LJ, Rapoport B: Isolation of a complementary DNA clone for thyroid microsomal antigen. Homology with the gene for thyroid peroxidase. J Clin Invest. 1987 Oct;80(4):1205-8. [PubMed Link Image]
  7. Zanelli E, Henry M, Charvet B, Malthiery Y: Evidence for an alternate splicing in the thyroperoxidase messenger from patients with Graves' disease. Biochem Biophys Res Commun. 1990 Jul 31;170(2):735-41. [PubMed Link Image]
  8. Wang D, De Deken X, Milenkovic M, Song Y, Pirson I, Dumont JE, Miot F: Identification of a novel partner of duox: EFP1, a thioredoxin-related protein. J Biol Chem. 2005 Jan 28;280(4):3096-103. Epub 2004 Nov 22. [PubMed Link Image]
  9. Bikker H, Vulsma T, Baas F, de Vijlder JJ: Identification of five novel inactivating mutations in the human thyroid peroxidase gene by denaturing gradient gel electrophoresis. Hum Mutat. 1995;6(1):9-16. [PubMed Link Image]
  10. Bikker H, Baas F, De Vijlder JJ: Molecular analysis of mutated thyroid peroxidase detected in patients with total iodide organification defects. J Clin Endocrinol Metab. 1997 Feb;82(2):649-53. [PubMed Link Image]
  11. Santos CL, Bikker H, Rego KG, Nascimento AC, Tambascia M, De Vijlder JJ, Medeiros-Neto G: A novel mutation in the TPO gene in goitrous hypothyroid patients with iodide organification defect. Clin Endocrinol (Oxf). 1999 Aug;51(2):165-72. [PubMed Link Image]
  12. Pannain S, Weiss RE, Jackson CE, Dian D, Beck JC, Sheffield VC, Cox N, Refetoff S: Two different mutations in the thyroid peroxidase gene of a large inbred Amish kindred: power and limits of homozygosity mapping. J Clin Endocrinol Metab. 1999 Mar;84(3):1061-71. [PubMed Link Image]
  13. Kotani T, Umeki K, Yamamoto I, Maesaka H, Tachibana K, Ohtaki S: A novel mutation in the human thyroid peroxidase gene resulting in a total iodide organification defect. J Endocrinol. 1999 Feb;160(2):267-73. [PubMed Link Image]
  14. Bakker B, Bikker H, Vulsma T, de Randamie JS, Wiedijk BM, De Vijlder JJ: Two decades of screening for congenital hypothyroidism in The Netherlands: TPO gene mutations in total iodide organification defects (an update). J Clin Endocrinol Metab. 2000 Oct;85(10):3708-12. [PubMed Link Image]
  15. Ambrugger P, Stoeva I, Biebermann H, Torresani T, Leitner C, Gruters A: Novel mutations of the thyroid peroxidase gene in patients with permanent congenital hypothyroidism. Eur J Endocrinol. 2001 Jul;145(1):19-24. [PubMed Link Image]
  16. Umeki K, Kotani T, Kawano J, Suganuma T, Yamamoto I, Aratake Y, Furujo M, Ichiba Y: Two novel missense mutations in the thyroid peroxidase gene, R665W and G771R, result in a localization defect and cause congenital hypothyroidism. Eur J Endocrinol. 2002 Apr;146(4):491-8. [PubMed Link Image]
  17. Niu DM, Hwang B, Chu YK, Liao CJ, Wang PL, Lin CY: High prevalence of a novel mutation (2268 insT) of the thyroid peroxidase gene in Taiwanese patients with total iodide organification defect, and evidence for a founder effect. J Clin Endocrinol Metab. 2002 Sep;87(9):4208-12. [PubMed Link Image]
  18. Wu JY, Shu SG, Yang CF, Lee CC, Tsai FJ: Mutation analysis of thyroid peroxidase gene in Chinese patients with total iodide organification defect: identification of five novel mutations. J Endocrinol. 2002 Mar;172(3):627-35. [PubMed Link Image]
  19. Calaciura F, Miscio G, Coco A, Leonardi D, Cisternino C, Regalbuto C, Bozzali M, Maiorana R, Ranieri A, Carta A, Buscema M, Trischitta V, Sava L, Tassi V: Genetics of specific phenotypes of congenital hypothyroidism: a population-based approach. Thyroid. 2002 Nov;12(11):945-51. [PubMed Link Image]
  20. Kotani T, Umeki K, Kawano J, Suganuma T, Hishinuma A, Ieiri T, Harada S: Partial iodide organification defect caused by a novel mutation of the thyroid peroxidase gene in three siblings. Clin Endocrinol (Oxf). 2003 Aug;59(2):198-206. [PubMed Link Image]
  21. Rivolta CM, Esperante SA, Gruneiro-Papendieck L, Chiesa A, Moya CM, Domene S, Varela V, Targovnik HM: Five novel inactivating mutations in the thyroid peroxidase gene responsible for congenital goiter and iodide organification defect. Hum Mutat. 2003 Sep;22(3):259. [PubMed Link Image]
  22. Fugazzola L, Cerutti N, Mannavola D, Vannucchi G, Fallini C, Persani L, Beck-Peccoz P: Monoallelic expression of mutant thyroid peroxidase allele causing total iodide organification defect. J Clin Endocrinol Metab. 2003 Jul;88(7):3264-71. [PubMed Link Image]
  23. Tajima T, Tsubaki J, Fujieda K: Two novel mutations in the thyroid peroxidase gene with goitrous hypothyroidism. Endocr J. 2005 Oct;52(5):643-5. [PubMed Link Image]
  24. Pfarr N, Borck G, Turk A, Napiontek U, Keilmann A, Muller-Forell W, Kopp P, Pohlenz J: Goitrous congenital hypothyroidism and hearing impairment associated with mutations in the TPO and SLC26A4/PDS genes. J Clin Endocrinol Metab. 2006 Jul;91(7):2678-81. Epub 2006 May 9. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 5511
Enzyme 27 Name Lactoperoxidase
Enzyme 27 Synonyms
  1. LPO
  2. Salivary peroxidase
  3. SPO
Enzyme 27 Gene Name LPO
Enzyme 27 Protein Sequence >Lactoperoxidase 
MRVLLHLPALLASLILLQAAASTTRAQTTRTSAISDTVSQAKVQVNKAFLDSRTRLKTAM
SSETPTSRQLSEYLKHAKGRTRTAIRNGQVWEESLKRLRQKASLTNVTDPSLDLTSLSLE
VGCGAPAPVVRCDPCSPYRTITGDCNNRRKPALGAANRALARWLPAEYEDGLSLPFGWTP
GKTRNGFPLPLAREVSNKIVGYLNEEGVLDQNRSLLFMQWGQIVDHDLDFAPDTELGSSE
YSKAQCDEYCIQGDNCFPIMFPPNDPKAGTQGKCMPFFRAGFVCPTPPYKSLAREQINAL
TSFLDASFVYSSEPSLASRLRNLSSPLGLMAVNQEVSDHGLPYLPYDSKKPSPCEFINTT
ARVPCFLAGDSRASEHILLATSHTLFLREHNRLARELKRLNPQWDGEKLYQEARKILGAF
VQIITFRDYLPILLGDHMQKWIPPYQGYSESVDPRISNVFTFAFRFGHLEVPSSMFRLDE
NYQPWGPEPELPLHTLFFNTWRMVKDGGIDPLVRGLLAKKSKLMKQNKMMTGELRNKLFQ
PTHRIHGFDLAAINTQRCRDHGQPGYNSWRAFCDLSQPQTLEELNTVLKSKMLAKKLLGL
YGTPDNIDIWIGAIAEPLVERGRVGPLLACLLGKQFQQIRDGDRFWWENPGVFTNEQKDS
LQKMSFSRLVCDNTRITKVPRDPFWANSYPYDFVDCSAIDKLDLSPWASVKN
Enzyme 27 Number of Residues 712
Enzyme 27 Molecular Weight 80287.1
Enzyme 27 Theoretical pI 8.76
Enzyme 27 GO Classification
Function
  • antioxidant activity
  • binding
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • peroxidase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
—
Enzyme 27 General Function Involved in peroxidase activity
Enzyme 27 Specific Function May contribute to airway host defense against infection
Enzyme 27 Pathways
Enzyme 27 Reactions
  • donor + H2O2 = oxidized donor + 2 H2O [RN:R03532]
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • 1-26
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein Not Available
Enzyme 27 UniProtKB/Swiss-Prot ID P22079 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name PERL_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >2139 bp 
ATGAGGGTCCTTCTCCATCTCCCAGCCCTCCTGGCTTCCCTCATCTTGCTTCAGGCTGCA
GCATCTACCACAAGAGCGCAGACTACCAGAACCTCTGCCATCTCCGATACTGTGAGTCAG
GCCAAGGTCCAAGTCAACAAGGCCTTCCTGGACTCCCGAACCAGGCTGAAGACCGCCATG
AGCTCTGAGACTCCCACCAGCCGACAGCTCTCAGAATACCTCAAGCATGCCAAAGGCCGG
ACGCGCACAGCCATCCGCAATGGACAGGTGTGGGAGGAGTCTTTAAAGAGACTGAGGCAG
AAGGCATCCTTGACCAATGTCACAGATCCCAGCCTGGACTTGACTTCACTGTCTCTGGAG
GTGGGCTGTGGTGCTCCTGCTCCCGTGGTGAGATGCGACCCGTGCAGCCCTTACCGCACC
ATTACGGGAGACTGCAATAACAGGAGGAAGCCTGCGCTGGGCGCCGCCAACAGGGCTCTG
GCGCGCTGGCTGCCCGCGGAGTACGAGGACGGGCTCTCCCTGCCCTTCGGCTGGACGCCG
GGGAAGACGCGCAACGGCTTCCCTCTCCCGCTGGCCCGGGAGGTATCTAACAAGATTGTT
GGCTATCTGAATGAGGAGGGTGTTCTGGACCAAAACAGGTCCCTGCTCTTCATGCAGTGG
GGTCAGATTGTGGATCATGACCTGGACTTTGCCCCTGACACCGAGCTGGGGAGTAGCGAG
TACTCCAAAGCCCAGTGTGATGAGTACTGTATCCAGGGAGACAACTGCTTCCCCATCATG
TTCCCACCCAATGACCCCAAGGCGGGGACTCAAGGGAAATGCATGCCTTTCTTCCGAGCT
GGGTTCGTCTGCCCCACTCCACCCTACAAGTCCCTGGCCCGAGAGCAGATCAACGCTCTG
ACCTCCTTCCTGGATGCCAGCTTTGTGTACAGCTCCGAGCCAAGCCTGGCCAGCCGCCTC
CGCAACCTCAGCAGCCCCCTGGGCCTCATGGCTGTCAACCAGGAGGTCTCAGACCATGGA
CTACCCTACCTGCCCTATGACAGCAAGAAGCCAAGCCCCTGTGAGTTCATCAACACCACT
GCCCGTGTGCCCTGCTTCCTGGCAGGAGATTCTCGAGCCTCAGAGCATATTCTGCTGGCC
ACATCCCACACCCTCTTTCTCCGCGAGCATAACCGGCTGGCCAGAGAACTAAAGAGACTC
AACCCTCAGTGGGATGGAGAGAAGCTCTACCAGGAAGCCCGGAAAATCCTGGGAGCCTTC
GTGCAGATTATCACCTTTAGGGACTACCTACCCATTTTGCTAGGTGACCACATGCAGAAG
TGGATACCCCCATATCAAGGCTACAGTGAATCTGTGGATCCCAGAATTTCCAATGTCTTC
ACCTTCGCCTTCCGCTTTGGCCACTTGGAGGTCCCCTCTAGTATGTTCCGCCTGGATGAG
AATTATCAGCCATGGGGGCCAGAACCAGAACTCCCCCTCCACACCCTCTTCTTCAACACT
TGGAGGATGGTCAAAGATGGTGGAATTGATCCTCTGGTGCGGGGCCTGCTGGCCAAGAAA
TCCAAGCTGATGAAACAGAATAAAATGATGACTGGAGAGCTGCGCAACAAGCTTTTCCAG
CCAACTCACAGGATCCATGGCTTTGACCTGGCTGCCATCAACACACAGCGTTGCCGGGAC
CATGGGCAACCTGGGTACAATTCCTGGAGAGCCTTCTGTGACCTCTCACAGCCGCAGACA
CTAGAGGAGTTGAACACAGTGCTGAAGAGCAAGATGCTGGCCAAGAAGTTACTGGGTCTC
TACGGGACCCCTGACAACATCGACATCTGGATAGGGGCCATTGCTGAGCCGCTGGTGGAA
AGGGGTCGGGTGGGGCCTCTCCTGGCCTGCCTCTTGGGCAAGCAGTTCCAGCAGATCCGT
GATGGAGACAGGTTCTGGTGGGAAAACCCTGGGGTCTTCACGAACGAGCAGAAGGACTCT
CTACAGAAAATGTCCTTCTCACGCCTTGTCTGTGACAACACCCGCATCACCAAGGTCCCA
CGGGACCCATTCTGGGCCAACAGCTACCCCTATGACTTCGTGGATTGCTCAGCCATCGAC
AAGCTGGACCTGTCACCCTGGGCCTCAGTGAAGAATTAG
Enzyme 27 GenBank Gene ID U39573 Link Image
Enzyme 27 GeneCard ID LPO Link Image
Enzyme 27 GenAtlas ID LPO Link Image
Enzyme 27 HGNC ID HGNC:6678 Link Image
Enzyme 27 Chromosome Location 1
Enzyme 27 Locus 17q23.1
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Kiser C, Caterina CK, Engler JA, Rahemtulla B, Rahemtulla F: Cloning and sequence analysis of the human salivary peroxidase-encoding cDNA. Gene. 1996 Sep 16;173(2):261-4. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Dull TJ, Uyeda C, Strosberg AD, Nedwin G, Seilhamer JJ: Molecular cloning of cDNAs encoding bovine and human lactoperoxidase. DNA Cell Biol. 1990 Sep;9(7):499-509. [PubMed Link Image]
  4. Wijkstrom-Frei C, El-Chemaly S, Ali-Rachedi R, Gerson C, Cobas MA, Forteza R, Salathe M, Conner GE: Lactoperoxidase and human airway host defense. Am J Respir Cell Mol Biol. 2003 Aug;29(2):206-12. Epub 2003 Mar 6. [PubMed Link Image]
  5. Ramachandran P, Boontheung P, Xie Y, Sondej M, Wong DT, Loo JA: Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry. J Proteome Res. 2006 Jun;5(6):1493-503. [PubMed Link Image]
  6. Picariello G, Ferranti P, Mamone G, Roepstorff P, Addeo F: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics. 2008 Sep;8(18):3833-47. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 5514
Enzyme 28 Name Myeloperoxidase
Enzyme 28 Synonyms
  1. MPO
  2. 89 kDa myeloperoxidase
  3. 84 kDa myeloperoxidase
  4. Myeloperoxidase light chain
  5. Myeloperoxidase heavy chain
Enzyme 28 Gene Name MPO
Enzyme 28 Protein Sequence >Myeloperoxidase 
MGVPFFSSLRCMVDLGPCWAGGLTAEMKLLLALAGLLAILATPQPSEGAAPAVLGEVDTS
LVLSSMEEAKQLVDKAYKERRESIKQRLRSGSASPMELLSYFKQPVAATRTAVRAADYLH
VALDLLERKLRSLWRRPFNVTDVLTPAQLNVLSKSSGCAYQDVGVTCPEQDKYRTITGMC
NNRRSPTLGASNRAFVRWLPAEYEDGFSLPYGWTPGVKRNGFPVALARAVSNEIVRFPTD
QLTPDQERSLMFMQWGQLLDHDLDFTPEPAARASFVTGVNCETSCVQQPPCFPLKIPPND
PRIKNQADCIPFFRSCPACPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNMSNQL
GLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLL
REHNRLATELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPTYR
SYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLSRVFFASWRVVLE
GGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYN
AWRRFCGLPQPETVGQLGTVLRNLKLARKLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPL
LACIIGTQFRKLRDGDRFWWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMS
NSYPRDFVNCSTLPALNLASWREAS
Enzyme 28 Number of Residues 745
Enzyme 28 Molecular Weight 83867.7
Enzyme 28 Theoretical pI 9.14
Enzyme 28 GO Classification
Function
  • antioxidant activity
  • binding
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • peroxidase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
—
Enzyme 28 General Function Involved in peroxidase activity
Enzyme 28 Specific Function Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity
Enzyme 28 Pathways
Enzyme 28 Reactions
  • donor + H2O2 = oxidized donor + 2 H2O [RN:R03532]
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • 1-48
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 189040 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID P05164 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name PERM_HUMAN Link Image
Enzyme 28 PDB ID 1MYP Link Image
Enzyme 28 PDB File Show
Enzyme 28 3D Structure
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >2238 bp 
ATGGGGGTTCCCTTCTTCTCTTCTCTCAGATGCATGGTGGACTTAGGACCTTGCTGGGCT
GGGGGTCTCACTGCAGAGATGAAGCTGCTTCTGGCCCTAGCAGGGCTCCTGGCCATTCTG
GCCACGCCCCAGCCCTCTGAAGGTGCTGCTCCAGCTGTCCTGGGGGAGGTGGACACCTCG
TTGGTGCTGAGCTCCATGGAGGAGGCCAAGCAGCTGGTGGACAAGGCCTACAAGGAGCGG
CGGGAAAGCATCAAGCAGCGGCTTCGCAGCGGCTCAGCCAGCCCCATGGAACTCCTATCC
TACTTCAAGCAGCCGGTGGCAGCCACCAGGACGGCGGTGAGGGCCGCTGACTACCTGCAC
GTGGCTCTAGACCTGCTGGAGAGGAAGCTGCGGTCCCTGTGGCGAAGGCCATTCAATGTC
ACTGATGTGCTGACGCCCGCCCAGCTGAATGTGTTGTCCAAGTCAAGCGGCTGCGCCTAC
CAGGACGTGGGGGTGACTTGCCCGGAGCAGGACAAATACCGCACCATCACCGGGATGTGC
AACAACAGACGCAGCCCCACGCTGGGGGCCTCCAACCGTGCCTTTGTGCGCTGGCTGCCG
GCGGAGTATGAGGACGGCTTCTCTCTTCCCTACGGCTGGACGCCCGGGGTCAAGCGCAAC
GGCTTCCCGGTGGCTCTGGCTCGCGCGGTCTCCAACGAGATCGTGCGCTTCCCCACTGAT
CAGCTGACTCCGGACCAGGAGCGCTCACTCATGTTCATGCAATGGGGCCAGCTGTTGGAC
CACGACCTCGACTTCACCCCTGAGCCGGCCGCCCGGGCCTCCTTCGTCACTGGCGTCAAC
TGCGAGACCAGCTGCGTTCAGCAGCCGCCCTGCTTCCCGCTCAAGATCCCGCCCAATGAC
CCCCGCATCAAGAACCAAGCCGACTGCATCCCGTTCTTCCGCTCCTGCCCGGCTTGCCCC
GGGAGCAACATCACCATCCGCAACCAGATCAACGCGCTCACTTCCTTCGTGGACGCCAGC
ATGGTGTACGGCAGCGAGGAGCCCCTGGCCAGGAACCTGCGCAACATGTCCAACCAGCTG
GGGCTGCTGGCCGTCAACCAGCGCTTCCAAGACAACGGCCGGGCCCTGCTGCCCTTTGAC
AACCTGCACGATGACCCCTGTCTCCTCACCAACCGCTCAGCGCGCATCCCCTGCTTCCTG
GCAGGGGACACCCGTTCCAGTGAGATGCCCGAGCTCACCTCCATGCACACCCTCTTACTT
CGGGAGCACAACCGGCTGGCCACAGAGCTCAAGAGCCTGAACCCTAGGTGGGATGGGGAG
AGGCTCTACCAGGAAGCCCGGAAGATCGTGGGGGCCATGGTCCAGATCATCACTTACCGG
GACTACCTGCCCCTGGTGCTGGGGCCAACGGCCATGAGGAAGTACCTGCCCACGTACCGT
TCCTACAATGACTCAGTGGACCCACGCATCGCCAACGTCTTCACCAATGCCTTCCGCTAC
GGCCACACCCTCATCCAACCCTTCATGTTCCGCCTGGACAATCGGTACCAGCCCATGGAA
CCCAACCCCCGTGTCCCCCTCAGCAGGGTCTTTTTTGCCTCCTGGAGGGTCGTGCTGGAA
GGTGGCATTGACCCCATCCTCCGGGGCCTCATGGCCACCCCTGCCAAGCTGAATCGTCAG
AACCAAATTGCAGTGGATGAGATCCGGGAGCGATTGTTTGAGCAGGTCATGAGGATTGGG
CTGGACCTGCCTGCTCTGAACATGCAGCGCAGCAGGGACCACGGCCTCCCAGGATACAAT
GCCTGGAGGCGCTTCTGTGGGCTCCCGCAGCCTGAAACTGTGGGCCAGCTGGGCACGGTG
CTGAGGAACCTGAAATTGGCGAGGAAACTGATGGAGCAGTATGGCACGCCCAACAACATC
GACATCTGGATGGGCGGCGTGTCCGAGCCTCTGAAGCGCAAAGGCCGCGTGGGCCCACTC
CTCGCCTGCATCATCGGTACCCAGTTCAGGAAGCTCCGGGATGGTGATCGGTTTTGGTGG
GAGAACGAGGGTGTGTTCAGCATGCAGCAGCGACAGGCCCTGGCCCAGATCTCATTGCCC
CGGATCATCTGCGACAACACAGGCATCACCACCGTGTCTAAGAACAACATCTTCATGTCC
AACTCATATCCCCGGGACTTTGTCAACTGCAGTACACTTCCTGCATTGAACCTGGCTTCC
TGGAGGGAAGCCTCCTAG
Enzyme 28 GenBank Gene ID J02694 Link Image
Enzyme 28 GeneCard ID MPO Link Image
Enzyme 28 GenAtlas ID MPO Link Image
Enzyme 28 HGNC ID HGNC:7218 Link Image
Enzyme 28 Chromosome Location 1
Enzyme 28 Locus 17q23.1
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Morishita K, Kubota N, Asano S, Kaziro Y, Nagata S: Molecular cloning and characterization of cDNA for human myeloperoxidase. J Biol Chem. 1987 Mar 15;262(8):3844-51. [PubMed Link Image]
  2. Morishita K, Tsuchiya M, Asano S, Kaziro Y, Nagata S: Chromosomal gene structure of human myeloperoxidase and regulation of its expression by granulocyte colony-stimulating factor. J Biol Chem. 1987 Nov 5;262(31):15208-13. [PubMed Link Image]
  3. Seto P, Hirayu H, Magnusson RP, Gestautas J, Portmann L, DeGroot LJ, Rapoport B: Isolation of a complementary DNA clone for thyroid microsomal antigen. Homology with the gene for thyroid peroxidase. J Clin Invest. 1987 Oct;80(4):1205-8. [PubMed Link Image]
  4. Johnson KR, Nauseef WM, Care A, Wheelock MJ, Shane S, Hudson S, Koeffler HP, Selsted M, Miller C, Rovera G: Characterization of cDNA clones for human myeloperoxidase: predicted amino acid sequence and evidence for multiple mRNA species. Nucleic Acids Res. 1987 Mar 11;15(5):2013-28. [PubMed Link Image]
  5. Hashinaka K, Nishio C, Hur SJ, Sakiyama F, Tsunasawa S, Yamada M: Multiple species of myeloperoxidase messenger RNAs produced by alternative splicing and differential polyadenylation. Biochemistry. 1988 Aug 9;27(16):5906-14. [PubMed Link Image]
  6. Johnson K, Gemperlein I, Hudson S, Shane S, Rovera G: Complete nucleotide sequence of the human myeloperoxidase gene. Nucleic Acids Res. 1989 Oct 11;17(19):7985-6. [PubMed Link Image]
  7. Hosokawa Y, Kawaguchi R, Hikiji K, Yamada M, Suzuki K, Nakagawa T, Yoshihara T, Yamaguchi K: Cloning and characterization of four types of cDNA encoding myeloperoxidase from human monocytic leukemia cell line, SKM-1. Leukemia. 1993 Mar;7(3):441-5. [PubMed Link Image]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. Yamada M, Hur SJ, Toda H: Isolation and characterization of extracellular myeloperoxidase precursor in HL-60 cell cultures. Biochem Biophys Res Commun. 1990 Jan 30;166(2):852-9. [PubMed Link Image]
  10. Taylor KL, Pohl J, Kinkade JM Jr: Unique autolytic cleavage of human myeloperoxidase. Implications for the involvement of active site MET409. J Biol Chem. 1992 Dec 15;267(35):25282-8. [PubMed Link Image]
  11. Yamada M, Yoshida M, Hashinaka K: Identification of transcriptional cis-elements in introns 7 and 9 of the myeloperoxidase gene. J Biol Chem. 1993 Jun 25;268(18):13479-85. [PubMed Link Image]
  12. Yamada M, Hur SJ, Hashinaka K, Tsuneoka K, Saeki T, Nishio C, Sakiyama F, Tsunasawa S: Isolation and characterization of a cDNA coding for human myeloperoxidase. Arch Biochem Biophys. 1987 May 15;255(1):147-55. [PubMed Link Image]
  13. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  14. Ramachandran P, Boontheung P, Xie Y, Sondej M, Wong DT, Loo JA: Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry. J Proteome Res. 2006 Jun;5(6):1493-503. [PubMed Link Image]
  15. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  16. Fiedler TJ, Davey CA, Fenna RE: X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution. J Biol Chem. 2000 Apr 21;275(16):11964-71. [PubMed Link Image]
  17. Fenna R, Zeng J, Davey C: Structure of the green heme in myeloperoxidase. Arch Biochem Biophys. 1995 Jan 10;316(1):653-6. [PubMed Link Image]
  18. Blair-Johnson M, Fiedler T, Fenna R: Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution. Biochemistry. 2001 Nov 20;40(46):13990-7. [PubMed Link Image]
  19. Kizaki M, Miller CW, Selsted ME, Koeffler HP: Myeloperoxidase (MPO) gene mutation in hereditary MPO deficiency. Blood. 1994 Apr 1;83(7):1935-40. [PubMed Link Image]
  20. Nauseef WM, Brigham S, Cogley M: Hereditary myeloperoxidase deficiency due to a missense mutation of arginine 569 to tryptophan. J Biol Chem. 1994 Jan 14;269(2):1212-6. [PubMed Link Image]
  21. Nauseef WM, Cogley M, McCormick S: Effect of the R569W missense mutation on the biosynthesis of myeloperoxidase. J Biol Chem. 1996 Apr 19;271(16):9546-9. [PubMed Link Image]
  22. DeLeo FR, Goedken M, McCormick SJ, Nauseef WM: A novel form of hereditary myeloperoxidase deficiency linked to endoplasmic reticulum/proteasome degradation. J Clin Invest. 1998 Jun 15;101(12):2900-9. [PubMed Link Image]
  23. Romano M, Dri P, Dadalt L, Patriarca P, Baralle FE: Biochemical and molecular characterization of hereditary myeloperoxidase deficiency. Blood. 1997 Nov 15;90(10):4126-34. [PubMed Link Image]
  24. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 5517
Enzyme 29 Name Eosinophil peroxidase
Enzyme 29 Synonyms
  1. EPO
  2. Eosinophil peroxidase light chain
  3. Eosinophil peroxidase heavy chain
Enzyme 29 Gene Name EPX
Enzyme 29 Protein Sequence >Eosinophil peroxidase 
MHLLPALAGVLATLVLAQPCEGTDPASPGAVETSVLRDCIAEAKLLVDAAYNWTQKSIKQ
RLRSGSASPMDLLSYFKQPVAATRTVVRAADYMHVALGLLEEKLQPQRSGPFNVTDVLTE
PQLRLLSQASGCALRDQAERCSDKYRTITGRCNNKRRPLLGASNQALARWLPAEYEDGLS
LPFGWTPSRRRNGFLLPLVRAVSNQIVRFPNERLTSDRGRALMFMQWGQFIDHDLDFSPE
SPARVAFTAGVDCERTCAQLPPCFPIKIPPNDPRIKNQRDCIPFFRSAPSCPQNKNRVRN
QINALTSFVDASMVYGSEVSLSLRLRNRTNYLGLLAINQRFQDNGRALLPFDNLHDDPCL
LTNRSARIPCFLAGDTRSTETPKLAAMHTLFMREHNRLATELRRLNPRWNGDKLYNEARK
IMGAMVQIITYRDFLPLVLGKARARRTLGHYRGYCSNVDPRVANVFTLAFRFGHTMLQPF
MFRLDSQYRASAPNSHVPLSSAFFASWRIVYEGGIDPILRGLMATPAKLNRQDAMLVDEL
RDRLFRQVRRIGLDLAALNMQRSRDHGLPGYNAWRRFCGLSQPRNLAQLSRVLKNQDLAR
KFLNLYGTPDNIDIWIGAIAEPLLPGARVGPLLACLFENQFRRARDGDRFWWQKRGVFTK
RQRKALSRISLSRIICDNTGITTVSRDIFRANIYPRGFVNCSRIPRLNLSAWRGT
Enzyme 29 Number of Residues 715
Enzyme 29 Molecular Weight 81039.5
Enzyme 29 Theoretical pI 10.81
Enzyme 29 GO Classification
Function
  • antioxidant activity
  • binding
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • peroxidase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
  • response to oxidative stress
  • response to stimulus
  • response to stress
Component
—
Enzyme 29 General Function Involved in peroxidase activity
Enzyme 29 Specific Function Mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils. Shows significant inhibitory activity towards Mycobacterium tuberculosis H37Rv by inducing bacterial fragmentation and lysis
Enzyme 29 Pathways
Enzyme 29 Reactions
  • donor + H2O2 = oxidized donor + 2 H2O [RN:R03532]
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • 1-17
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 66268791 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID P11678 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name PERE_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >2148 bp 
ATGCATCTGCTCCCAGCCCTGGCAGGGGTCCTGGCCACACTCGTCCTCGCCCAGCCCTGT
GAGGGCACTGACCCAGCCTCCCCTGGGGCAGTGGAGACCTCGGTCCTGCGAGACTGCATA
GCAGAGGCCAAGTTGCTGGTGGATGCTGCCTACAATTGGACCCAGAAGAGCATCAAGCAG
CGGCTTCGCAGCGGTTCAGCCAGCCCCATGGACCTCCTGTCCTACTTCAAACAACCGGTA
GCAGCCACCAGGACAGTTGTTCGGGCCGCAGATTATATGCATGTGGCTTTGGGGCTGCTT
GAAGAGAAGTTACAACCCCAGCGGTCCGGACCCTTCAATGTCACTGATGTGCTAACAGAA
CCACAGCTGCGGCTGCTGTCCCAGGCCAGTGGCTGTGCTCTCCGGGACCAGGCCGAGCGC
TGCAGCGACAAGTACCGCACCATCACTGGACGGTGCAACAACAAGAGGAGACCCTTGCTA
GGGGCCTCCAACCAGGCTCTGGCTCGCTGGCTGCCCGCCGAGTATGAGGATGGGCTGTCG
CTCCCCTTCGGCTGGACCCCCAGCAGGAGGCGCAATGGCTTCCTTCTCCCTCTTGTCCGG
GCTGTCTCCAACCAGATTGTGCGCTTCCCCAATGAGAGACTGACCTCCGACCGTGGCCGA
GCCCTCATGTTCATGCAGTGGGGCCAGTTCATTGACCATGACCTGGACTTCTCCCCGGAG
TCCCCGGCCAGAGTGGCCTTCACTGCAGGCGTTGACTGTGAGAGGACCTGCGCCCAGCTG
CCCCCCTGCTTTCCCATCAAGATCCCACCCAATGACCCCCGCATCAAGAACCAGCGTGAC
TGCATCCCTTTCTTCCGCTCGGCACCCTCATGCCCCCAAAACAAGAACAGAGTCCGCAAC
CAGATCAACGCGCTCACCTCCTTTGTGGACGCCAGCATGGTGTATGGCAGTGAGGTCTCC
CTCTCGCTGCGGCTCCGCAACCGGACCAACTACCTGGGGCTGCTGGCCATCAACCAGCGC
TTTCAAGACAACGGCCGGGCCCTGCTGCCCTTCGACAACCTGCACGATGACCCCTGTCTC
CTCACCAACCGCTCGGCGCGCATCCCCTGCTTCCTGGCAGGTGACACCCGATCAACGGAA
ACCCCCAAACTGGCAGCCATGCACACCCTCTTTATGCGAGAGCACAACCGGCTGGCCACC
GAGCTGAGACGCCTGAATCCCCGGTGGAATGGAGACAAACTGTACAATGAGGCTCGGAAG
ATCATGGGGGCCATGGTCCAGATCATCACCTACCGAGACTTTCTGCCCCTGGTTCTGGGC
AAGGCCCGGGCCAGGAGAACCCTGGGGCACTACAGGGGGTACTGCTCCAATGTGGACCCA
CGGGTGGCCAATGTCTTCACCCTGGCCTTCCGCTTTGGCCACACAATGCTCCAGCCCTTC
ATGTTCCGCTTGGACAGTCAGTACCGGGCCTCCGCACCCAACTCGCATGTCCCACTTAGC
TCTGCCTTCTTTGCCAGCTGGCGGATCGTGTATGAAGGGGGCATCGACCCCATCCTCCGG
GGCCTCATGGCCACCCCTGCCAAGCTGAACCGTCAGGATGCCATGTTAGTGGATGAGCTC
CGGGACCGGCTGTTTCGGCAAGTGAGGAGGATTGGGCTGGACCTGGCAGCTCTCAACATG
CAACGAAGCCGGGACCACGGCCTTCCAGGGTACAATGCTTGGAGGCGCTTCTGTGGGCTC
TCCCAGCCCCGGAATTTGGCACAGCTTAGCCGGGTGCTGAAAAACCAGGACTTGGCAAGG
AAGTTCCTGAATTTGTATGGAACACCTGACAACATTGACATCTGGATTGGGGCCATCGCT
GAGCCTCTTTTGCCGGGGGCTCGAGTGGGGCCTCTTCTGGCTTGTCTGTTCGAGAACCAG
TTCAGAAGAGCCCGAGACGGAGACAGGTTCTGGTGGCAGAAACGAGGTGTTTTCACCAAA
AGACAGCGCAAGGCCCTGAGCAGAATTTCCTTGTCTCGAATTATATGTGACAATACCGGT
ATCACCACGGTTTCAAGGGACATCTTCAGAGCCAACATCTACCCTCGGGGCTTTGTGAAC
TGCAGCCGTATCCCCAGGTTGAACCTATCAGCCTGGCGAGGGACATGA
Enzyme 29 GenBank Gene ID DQ054598 Link Image
Enzyme 29 GeneCard ID EPX Link Image
Enzyme 29 GenAtlas ID EPX Link Image
Enzyme 29 HGNC ID HGNC:3423 Link Image
Enzyme 29 Chromosome Location 1
Enzyme 29 Locus 17q23.1
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Sakamaki K, Tomonaga M, Tsukui K, Nagata S: Molecular cloning and characterization of a chromosomal gene for human eosinophil peroxidase. J Biol Chem. 1989 Oct 5;264(28):16828-36. [PubMed Link Image]
  2. Ten RM, Pease LR, McKean DJ, Bell MP, Gleich GJ: Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family. J Exp Med. 1989 May 1;169(5):1757-69. [PubMed Link Image]
  3. Oxvig C, Thomsen AR, Overgaard MT, Sorensen ES, Hojrup P, Bjerrum MJ, Gleich GJ, Sottrup-Jensen L: Biochemical evidence for heme linkage through esters with Asp-93 and Glu-241 in human eosinophil peroxidase. The ester with Asp-93 is only partially formed in vivo. J Biol Chem. 1999 Jun 11;274(24):16953-8. [PubMed Link Image]
  4. Borelli V, Vita F, Shankar S, Soranzo MR, Banfi E, Scialino G, Brochetta C, Zabucchi G: Human eosinophil peroxidase induces surface alteration, killing, and lysis of Mycobacterium tuberculosis. Infect Immun. 2003 Feb;71(2):605-13. [PubMed Link Image]
  5. Ulrich M, Petre A, Youhnovski N, Promm F, Schirle M, Schumm M, Pero RS, Doyle A, Checkel J, Kita H, Thiyagarajan N, Acharya KR, Schmid-Grendelmeier P, Simon HU, Schwarz H, Tsutsui M, Shimokawa H, Bellon G, Lee JJ, Przybylski M, Doring G: Post-translational tyrosine nitration of eosinophil granule toxins mediated by eosinophil peroxidase. J Biol Chem. 2008 Oct 17;283(42):28629-40. Epub 2008 Aug 11. [PubMed Link Image]
  6. Romano M, Patriarca P, Melo C, Baralle FE, Dri P: Hereditary eosinophil peroxidase deficiency: immunochemical and spectroscopic studies and evidence for a compound heterozygosity of the defect. Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12496-500. [PubMed Link Image]
  7. Nakamura H, Miyagawa K, Ogino K, Endo T, Imai T, Ozasa K, Motohashi Y, Matsuzaki I, Sasahara S, Hatta K, Eboshida A: High contribution contrast between the genes of eosinophil peroxidase and IL-4 receptor alpha-chain in Japanese cedar pollinosis. J Allergy Clin Immunol. 2003 Dec;112(6):1127-31. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 5551
Enzyme 30 Name Arylsulfatase D
Enzyme 30 Synonyms
  1. ASD
Enzyme 30 Gene Name ARSD
Enzyme 30 Protein Sequence >Arylsulfatase D 
MRSAARRGRAAPAARDSLPVLLFLCLLLKTCEPKTANAFKPNILLIMADDLGTGDLGCYG
NNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRALQWNA
GSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHHPLNHGFDYFYGMPFTL
TNDCDPGRPPEVDAALRAQLWGYTQFLALGILTLAAGQTCGFFSVSARAVTGMAGVGCLF
FISWYSSFGFVRRWNCILMRNHDVTEQPMVLEKTASLMLKEAVSYIERHKHGPFLLFLSL
LHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYFTSDHGGH
LEARDGHSQLGGWNGIYKGGKGMGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPT
VVQLVGGEVPQDRVIDGHSLVPLLQGAEARSAHEFLFHYCGQHLHAARWHQKDSGSVWKV
HYTTPQFHPEGAGACYGRGVCPCSGEGVTHHRPPLLFDLSRDPSEARPLTPDSEPLYHAV
IARVGAAVSEHRQTLSPVPQQFSMSNILWKPWLQPCCGHFPFCSCHEDGDGTP
Enzyme 30 Number of Residues 593
Enzyme 30 Molecular Weight 64859.3
Enzyme 30 Theoretical pI 7.24
Enzyme 30 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • sulfuric ester hydrolase activity
Process
  • metabolic process
Component
—
Enzyme 30 General Function Involved in catalytic activity
Enzyme 30 Specific Function Not Available
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions Not Available
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • 1-33
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 791002 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID P51689 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name ARSD_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >1782 bp 
ATGCGATCCGCCGCGCGGAGGGGACGCGCCGCGCCCGCCGCCAGGGACTCTTTGCCGGTG
CTACTGTTTTTATGCTTGCTTCTGAAGACGTGTGAACCTAAAACTGCAAATGCCTTTAAA
CCAAATATCCTACTGATCATGGCGGATGATCTAGGCACTGGGGATCTCGGTTGCTACGGG
AACAATACACTGAGAACGCCGAATATTGACCAGCTTGCAGAGGAAGGTGTGAGGCTCACT
CAGCACCTGGCGGCCGCCCCGCTCTGCACCCCAAGCCGAGCTGCATTCCTCACAGGGAGA
CATTCCTTCAGATCAGGCATGGACGCCAGCAATGGATACCGGGCCCTTCAGTGGAACGCA
GGCTCAGGTGGACTCCCTGAGAACGAAACCACTTTTGCAAGAATCTTGCAGCAGCATGGC
TATGCAACCGGCCTCATAGGAAAATGGCACCAGGGTGTGAATTGTGCATCCCGCGGGGAT
CACTGCCACCACCCCCTGAACCACGGATTTGACTATTTCTACGGCATGCCCTTCACGCTC
ACAAACGACTGTGACCCAGGCAGGCCCCCCGAAGTGGACGCCGCCCTGAGGGCGCAGCTC
TGGGGTTACACCCAGTTCCTGGCGCTGGGGATTCTCACCCTGGCTGCCGGCCAGACCTGC
GGTTTCTTCTCTGTCTCCGCGAGAGCAGTCACCGGCATGGCCGGCGTGGGCTGCCTGTTT
TTCATCTCTTGGTACTCCTCCTTCGGGTTTGTGCGACGCTGGAACTGTATCCTGATGAGA
AACCATGACGTCACGGAGCAACCCATGGTTCTGGAGAAAACAGCGAGTCTTATGCTAAAG
GAAGCTGTTTCCTATATTGAAAGACACAAGCATGGGCCATTTCTCCTCTTCCTTTCTTTG
CTGCATGTGCACATTCCCCTTGTGACCACGAGTGCATTCCTGGGGAAAAGTCAGCATGGC
TTATATGGTGATAATGTGGAGGAGATGGACTGGCTCATAGGTAAGGTTCTTAATGCCATC
GAAGACAATGGTTTAAAGAACTCAACATTCACGTATTTCACCTCTGACCATGGAGGACAT
TTAGAGGCAAGAGATGGACACAGCCAGTTAGGGGGATGGAACGGAATTTACAAAGGTGGG
AAGGGCATGGGAGGATGGGAAGGTGGGATCCGAGTGCCCGGGATCTTCCACTGGCCGGGG
GTGCTCCCGGCCGGCCGAGTGATTGGAGAGCCCACGAGCCTGATGGACGTGTTCCCTACT
GTGGTCCAGCTGGTGGGTGGCGAGGTGCCCCAGGACAGGGTGATTGATGGCCACAGCCTG
GTACCCTTGCTGCAGGGAGCTGAGGCACGCTCGGCACATGAGTTCCTGTTTCATTACTGT
GGGCAGCATCTTCACGCAGCACGCTGGCACCAGAAGGACAGTGGAAGCGTCTGGAAGGTT
CATTACACGACCCCGCAGTTCCACCCCGAGGAGCGGGGCCTGCTAACGGCCGAGGCGTCT
GCCCATGCTGAATGGGGAGGCGTGACCCATCACAGACCCCCTTTGCTCTTTGACCTCTCC
AGGGACCCCTCCGAGGCACGGCCCCTGACCCCCGACTCCGAGCCCCTGTACCACGCCGTG
ATAGCAAGGGTAGGTGCCGCGGTGTCGGAGCATCGGCAGACCCTGAGTCCTGTGCCCCAG
CAGTTTTCCATGAGCAACATCCTGTGGAAGCCGTGGCTGCAGCCGTGCTGCGGACATTTC
CCGTTCTGTTCATGCCACGAGGATGGGGATGGCACCCCCTGA
Enzyme 30 GenBank Gene ID X83572 Link Image
Enzyme 30 GeneCard ID ARSD Link Image
Enzyme 30 GenAtlas ID ARSD Link Image
Enzyme 30 HGNC ID HGNC:717 Link Image
Enzyme 30 Chromosome Location Not Available
Enzyme 30 Locus Not Available
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Franco B, Meroni G, Parenti G, Levilliers J, Bernard L, Gebbia M, Cox L, Maroteaux P, Sheffield L, Rappold GA, et al.: A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy. Cell. 1995 Apr 7;81(1):15-25. [PubMed Link Image]
  2. Urbitsch P, Salzer MJ, Hirschmann P, Vogt PH: Arylsulfatase D gene in Xp22.3 encodes two protein isoforms. DNA Cell Biol. 2000 Dec;19(12):765-73. [PubMed Link Image]
  3. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 5557
Enzyme 31 Name Arylsulfatase B
Enzyme 31 Synonyms
  1. ASB
  2. N-acetylgalactosamine-4-sulfatase
  3. G4S
Enzyme 31 Gene Name ARSB
Enzyme 31 Protein Sequence >Arylsulfatase B 
MGPRGAASLPRGPGPRRLLLPVVLPLLLLLLLAPPGSGAGASRPPHLVFLLADDLGWNDV
GFHGSRIRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPS
CVPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYSHER
CTLIDALNVTRCALDFRDGEEVATGYKNMYSTNIFTKRAIALITNHPPEKPLFLYLALQS
VHEPLQVPEEYLKPYDFIQDKNRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTD
NGGQTLAGGNNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELIHISDWLPTLVKL
ARGHTNGTKPLDGFDVWKTISEGSPSPRIELLHNIDPNFVDSSPCPRNSMAPAKDDSSLP
EYSAFNTSVHAAIRHGNWKLLTGYPGCGYWFPPPSQYNVSEIPSSDPPTKTLWLFDIDRD
PEERHDLSREYPHIVTKLLSRLQFYHKHSVPVYFPAQDPRCDPKATGVWGPWM
Enzyme 31 Number of Residues 533
Enzyme 31 Molecular Weight 59686.7
Enzyme 31 Theoretical pI 8.31
Enzyme 31 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • sulfuric ester hydrolase activity
Process
  • metabolic process
Component
—
Enzyme 31 General Function Involved in catalytic activity
Enzyme 31 Specific Function Hydrolysis of the 4-sulfate groups of the N- acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate
Enzyme 31 Pathways
Enzyme 31 Reactions
  • Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate [RN:R07823] ALL_REAC R07823(G)
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • 1-36
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 179077 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID P15848 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name ARSB_HUMAN Link Image
Enzyme 31 PDB ID 1FSU Link Image
Enzyme 31 PDB File Show
Enzyme 31 3D Structure
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >1602 bp 
ATGGGTCCGCGCGGCGCGGCGAGCTTGCCCCGAGGCCCCGGACCTCGGCGGCTGCTCCTC
CCCGTCGTCCTCCCGCTGCTGCTGCTGCTGTTGTTGGCGCCGCCGGGCTCGGGCGCCGGG
GCCAGCCGGCCGCCCCACCTGGTCTTCTTGCTGGCAGACGACCTAGGCTGGAACGACGTC
GGCTTCCACGGCTCCCGCATCCGCACGCCGCACCTGGACGCGCTGGCGGCCGGCGGGGTG
CTCCTGGACAACTACTACACGCAGCCGCTGTGCACGCCGTCGCGGAGCCAGCTGCTCACT
GGCCGCTACCAGATCCGTACAGGTTTACAGCACCAAATAATCTGGCCCTGTCAGCCCAGC
TGTGTTCCTCTGGATGAAAAACTCCTGCCCCAGCTCCTAAAAGAAGCAGGTTATACTACC
CATATGGTCGGAAAATGGCACCTGGGAATGTACCGGAAAGAATGCCTTCCAACCCGCCGA
GGATTTGATACCTACTTTGGATATCTCCTGGGTAGTGAAGATTATTATTCCCATGAACGC
TGTACATTAATTGACGCTCTGAATGTCACACGATGTGCTCTTGATTTTCGAGATGGCGAA
GAAGTTGCAACAGGATATAAAAATATGTATTCAACAAACATATTCACCAAAAGGGCTATA
GCCCTCATAACTAACCATCCACCAGAGAAGCCTCTGTTTCTCTACCTTGCTCTCCAGTCT
GTGCATGAGCCCCTTCAGGTCCCTGAGGAATACTTGAAGCCATATGACTTTATCCAAGAC
AAGAACAGGCATCACTATGCAGGAATGGTGTCCCTTATGGATGAAGCAGTAGGAAATGTC
ACTGCAGCTTTAAAAAGCAGTGGGCTCTGGAACAACACGGTGTTCATCTTTTCTACAGAT
AACGGAGGGCAGACTTTGGCAGGGGGTAATAACTGGCCCCTTCGAGGAAGAAAATGGAGC
CTGTGGGAAGGAGGCGTCCGAGGGGTGGGCTTTGTGGCAAGCCCCTTGCTGAAGCAGAAG
GGCGTGAAGAACCGGGAGCTCATCCACATCTCTGACTGGCTGCCAACACTCGTGAAGCTG
GCCAGGGGACACACCAATGGCACAAAGCCTCTGGATGGCTTCGACGTGTGGAAAACCATC
AGTGAAGGAAGCCCATCCCCCAGAATTGAGCTGCTGCATAATATTGACCCAAACTTCGTG
GACTCTTCACCGTGTCCCAGGAACAGCATGGCTCCAGCAAAGGATGACTCTTCTCTTCCA
GAATATTCAGCCTTTAACACATCTGTCCATGCTGCAATTAGACATGGAAATTGGAAACTC
CTCACGGGCTACCCAGGCTGTGGTTACTGGTTCCCTCCACCGTCTCAATACAATGTTTCT
GAGATACCCTCATCAGACCCACCAACCAAGACCCTCTGGCTCTTTGATATTGATCGGGAC
CCTGAAGAAAGACATGACCTGTCCAGAGAATATCCTCACATCGTCACAAAGCTCCTGTCC
CGCCTACAGTTCTACCATAAACACTCAGTCCCCGTGTACTTCCCTGCACAGGACCCCCGC
TGTGATCCCAAGGCCACTGGGGTGTGGGGCCCTTGGATGTAG
Enzyme 31 GenBank Gene ID J05225 Link Image
Enzyme 31 GeneCard ID ARSB Link Image
Enzyme 31 GenAtlas ID ARSB Link Image
Enzyme 31 HGNC ID HGNC:714 Link Image
Enzyme 31 Chromosome Location 5
Enzyme 31 Locus 5q11-q13
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Peters C, Schmidt B, Rommerskirch W, Rupp K, Zuhlsdorf M, Vingron M, Meyer HE, Pohlmann R, von Figura K: Phylogenetic conservation of arylsulfatases. cDNA cloning and expression of human arylsulfatase B. J Biol Chem. 1990 Feb 25;265(6):3374-81. [PubMed Link Image]
  2. Schuchman EH, Jackson CE, Desnick RJ: Human arylsulfatase B: MOPAC cloning, nucleotide sequence of a full-length cDNA, and regions of amino acid identity with arylsulfatases A and C. Genomics. 1990 Jan;6(1):149-58. [PubMed Link Image]
  3. Modaressi S, Rupp K, von Figura K, Peters C: Structure of the human arylsulfatase B gene. Biol Chem Hoppe Seyler. 1993 May;374(5):327-35. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Litjens T, Morris CP, Gibson GJ, Beckmann KR, Hopwood JJ: Human N-acetylgalactosamine-4-sulphatase: protein maturation and isolation of genomic clones. Biochem Int. 1991 May;24(2):209-15. [PubMed Link Image]
  6. Kobayashi T, Honke K, Jin T, Gasa S, Miyazaki T, Makita A: Components and proteolytic processing sites of arylsulfatase B from human placenta. Biochim Biophys Acta. 1992 Oct 20;1159(3):243-7. [PubMed Link Image]
  7. Schmidt B, Selmer T, Ingendoh A, von Figura K: A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell. 1995 Jul 28;82(2):271-8. [PubMed Link Image]
  8. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  9. Bond CS, Clements PR, Ashby SJ, Collyer CA, Harrop SJ, Hopwood JJ, Guss JM: Structure of a human lysosomal sulfatase. Structure. 1997 Feb 15;5(2):277-89. [PubMed Link Image]
  10. Wicker G, Prill V, Brooks D, Gibson G, Hopwood J, von Figura K, Peters C: Mucopolysaccharidosis VI (Maroteaux-Lamy syndrome). An intermediate clinical phenotype caused by substitution of valine for glycine at position 137 of arylsulfatase B. J Biol Chem. 1991 Nov 15;266(32):21386-91. [PubMed Link Image]
  11. Jin WD, Jackson CE, Desnick RJ, Schuchman EH: Mucopolysaccharidosis type VI: identification of three mutations in the arylsulfatase B gene of patients with the severe and mild phenotypes provides molecular evidence for genetic heterogeneity. Am J Hum Genet. 1992 Apr;50(4):795-800. [PubMed Link Image]
  12. Isbrandt D, Arlt G, Brooks DA, Hopwood JJ, von Figura K, Peters C: Mucopolysaccharidosis VI (Maroteaux-Lamy syndrome): six unique arylsulfatase B gene alleles causing variable disease phenotypes. Am J Hum Genet. 1994 Mar;54(3):454-63. [PubMed Link Image]
  13. Voskoboeva E, Isbrandt D, von Figura K, Krasnopolskaya X, Peters C: Four novel mutant alleles of the arylsulfatase B gene in two patients with intermediate form of mucopolysaccharidosis VI (Maroteaux-Lamy syndrome). Hum Genet. 1994 Mar;93(3):259-64. [PubMed Link Image]
  14. Simonaro CM, Schuchman EH: N-acetylgalactosamine-4-sulfatase: identification of four new mutations within the conserved sulfatase region causing mucopolysaccharidosis type VI. Biochim Biophys Acta. 1995 Dec 12;1272(3):129-32. [PubMed Link Image]
  15. Litjens T, Brooks DA, Peters C, Gibson GJ, Hopwood JJ: Identification, expression, and biochemical characterization of N-acetylgalactosamine-4-sulfatase mutations and relationship with clinical phenotype in MPS-VI patients. Am J Hum Genet. 1996 Jun;58(6):1127-34. [PubMed Link Image]
  16. Villani GR, Balzano N, Di Natale P: Two novel mutations of the arylsulfatase B gene in two Italian patients with severe form of mucopolysaccharidosis. Mutations in brief no. 127. Online. Hum Mutat. 1998;11(5):410. [PubMed Link Image]
  17. Wang DG, Fan JB, Siao CJ, Berno A, Young P, Sapolsky R, Ghandour G, Perkins N, Winchester E, Spencer J, Kruglyak L, Stein L, Hsie L, Topaloglou T, Hubbell E, Robinson E, Mittmann M, Morris MS, Shen N, Kilburn D, Rioux J, Nusbaum C, Rozen S, Hudson TJ, Lipshutz R, Chee M, Lander ES: Large-scale identification, mapping, and genotyping of single-nucleotide polymorphisms in the human genome. Science. 1998 May 15;280(5366):1077-82. [PubMed Link Image]
  18. Villani GR, Balzano N, Vitale D, Saviano M, Pavone V, Di Natale P: Maroteaux-lamy syndrome: five novel mutations and their structural localization. Biochim Biophys Acta. 1999 Feb 24;1453(2):185-92. [PubMed Link Image]
  19. Wu JY, Yang CF, Lee CC, Chang JG, Tsai FJ: A novel mutation (Q239R) identified in a Taiwan Chinese patient with type VI mucopolysaccharidosis (Maroteaux-Lamy syndrome). Hum Mutat. 2000 Apr;15(4):389-90. [PubMed Link Image]
  20. Yang CF, Wu JY, Lin SP, Tsai FJ: Mucopolysaccharidosis type VI: Report of two Taiwanese patients and identification of one novel mutation. J Formos Med Assoc. 2001 Dec;100(12):820-3. [PubMed Link Image]
  21. Karageorgos L, Harmatz P, Simon J, Pollard A, Clements PR, Brooks DA, Hopwood JJ: Mutational analysis of mucopolysaccharidosis type VI patients undergoing a trial of enzyme replacement therapy. Hum Mutat. 2004 Mar;23(3):229-33. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 5560
Enzyme 32 Name Arylsulfatase E
Enzyme 32 Synonyms
  1. ASE
Enzyme 32 Gene Name ARSE
Enzyme 32 Protein Sequence >Arylsulfatase E 
MLHLHHSCLCFRSWLPAMLAVLLSLAPSASSDISASRPNILLLMADDLGIGDIGCYGNNT
MRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTGASG
GLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDHFYGMPFSLMGD
CARWELSEKRVNLEQKLNFLFQVLALVALTLVAGKLTHLIPVSWMPVIWSALSAVLLLAS
SYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLILQEVASFLKRNKHGPFLLFVSFLHV
HIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLEN
QLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVR
LAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFV
TPVFQPEGAGACYGRKVCPCFGEKVVHHDPPLLFDLSRDPSETHILTPASEPVFYQVMER
VQQAVWEHQRTLSPVPLQLDRLGNIWRPWLQPCCGPFPLCWCLREDDPQ
Enzyme 32 Number of Residues 589
Enzyme 32 Molecular Weight 65668.4
Enzyme 32 Theoretical pI 6.96
Enzyme 32 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • sulfuric ester hydrolase activity
Process
  • metabolic process
Component
—
Enzyme 32 General Function Involved in catalytic activity
Enzyme 32 Specific Function May be essential for the correct composition of cartilage and bone matrix during development. Has no activity toward steroid sulfates
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions Not Available
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • 1-31
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 62897927 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID P51690 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name ARSE_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >1770 bp 
ATGTTACATCTGCACCATTCTTGTTTGTGTTTCAGGAGCTGGCTGCCAGCGATGCTCGCT
GTACTGCTAAGTTTGGCACCATCAGCTTCCAGCGACATTTCCGCCTCCCGACCGAACATC
CTTCTTCTGATGGCGGACGACCTTGGCATTGGGGACATTGGCTGCTATGGCAACAACACC
ATGAGGACTCCGAATATTGACCGCCTTGCAGAGGACGGCGTGAAGCTGACCCAACACATC
TCTGCCGCATCTTTGTGCACCCCAAGCAGAGCCGCCTTCCTCACGGGCAGATACCCTGTG
CGATCAGGGATGGTTTCCAGCATTGGTTACCGTGTTCTTCAGTGGACCGGAGCATCTGGA
GGTCTTCCAACAAATGAGACAACTTTTGCAAAAATACTGAAAGAGAAAGGCTATGCCACT
GGACTCATTGGAAAATGGCATCTGGGTCTCAACTGTGAGTCAGCCAGTGATCATTGCCAC
CACCCTCTCCATCACGGCTTTGACCATTTCTACGGAATGCCTTTCTCCTTGATGGGTGAT
TGCGCCCGCTGGGAACTCTCAGAGAAGCGTGTCAACCTGGAACAAAAACTCAACTTCCTC
TTCCAAGTCCTGGCCTTGGTTGCCCTCACACTGGTAGCAGGGAAGCTCACACACCTGATA
CCCGTCTCGTGGATGCCGGTCATCTGGTCAGCCCTTTCGGCCGTCCTCCTCCTCGCAAGC
TCCTATTTTGTGGGTGCTCTGATTGTCCATGCCGATTGCTTTCTGATGAGAAACCACACC
ATCACGGAGCAGCCCATGTGCTTCCAAAGAACGACACCCCTTATTCTGCAGGAGGTTGCG
TCCTTTCTCAAAAGGAATAAGCATGGGCCTTTCCTCCTCTTTGTTTCCTTTCTACACGTT
CACATCCCTCTTATCACTATGGAGAACTTCCTCGGGAAGAGTCTCCACGGGCTGTATGGG
GACAACGTAGAGGAGATGGACTGGATGGTAGGACGGATCCTTGACACTTTGGACGTGGAG
GGTTTGAGCAACAGCACCCTCATTTATTTTACGTCGGATCACGGCGGTTCCCTAGAGAAT
CAACTTGGAAACACCCAGTATGGTGGCTGGAATGGAATTTATAAAGGTGGGAAGGGCATG
GGAGGATGGGAAGGTGGGATCCGCGTGCCCGGGATCTTCCGCTGGCCCGGGGTGCTCCCG
GCCGGCCGAGTGATTGGCGAGCCCACGAGTCTGATGGACGTGTTCCCCACCGTGGTCCGG
CTGGCGGGCAGCGAGGTGCCCCAGGACAGAGTGATTGACGGCCAAGACCTTCTGCCCTTG
CTCCTGGGGACAGCCCAACACTCAGACCACGAGTTCCTGATGCATTATTGTGAGAGGTTT
CTGCACGCAGCCAGGTGGCATCAACGGGACAGAGGAACAATGTGGAAAGTCCACTTTGTG
ACGCCTGTGTTCCAGCCAGAGGGAGCCGGTGCCTGCTATGGAAGAAAGGTCTGCCCGTGC
TTTGGGGAAAAAGTAGTCCACCACGATCCACCTTTGCTCTTTGACCTCTCAAGAGACCCT
TCTGAGACCCACATCCTCACACCAGCCTCAGAGCCCGTGTTCTATCAGGTGATGGAACGA
GTCCAGCAGGCGGTGTGGGAACACCAGCGGACACTCAGCCCAGTTCCTCTGCAGCTGGAC
AGGCTGGGCAATATCTGGAGACCGTGGCTGCAGCCCTGCTGTGGCCCGTTCCCCCTCTGC
TGGTGCCTTAGGGAAGATGACCCACAATAA
Enzyme 32 GenBank Gene ID AK223183 Link Image
Enzyme 32 GeneCard ID ARSE Link Image
Enzyme 32 GenAtlas ID ARSE Link Image
Enzyme 32 HGNC ID HGNC:719 Link Image
Enzyme 32 Chromosome Location Not Available
Enzyme 32 Locus Not Available
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Franco B, Meroni G, Parenti G, Levilliers J, Bernard L, Gebbia M, Cox L, Maroteaux P, Sheffield L, Rappold GA, et al.: A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy. Cell. 1995 Apr 7;81(1):15-25. [PubMed Link Image]
  2. Daniele A, Parenti G, d'Addio M, Andria G, Ballabio A, Meroni G: Biochemical characterization of arylsulfatase E and functional analysis of mutations found in patients with X-linked chondrodysplasia punctata. Am J Hum Genet. 1998 Mar;62(3):562-72. [PubMed Link Image]
  3. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  4. Parenti G, Buttitta P, Meroni G, Franco B, Bernard L, Rizzolo MG, Brunetti-Pierri N, Ballabio A, Andria G: X-linked recessive chondrodysplasia punctata due to a new point mutation of the ARSE gene. Am J Med Genet. 1997 Dec 12;73(2):139-43. [PubMed Link Image]
  5. Brunetti-Pierri N, Andreucci MV, Tuzzi R, Vega GR, Gray G, McKeown C, Ballabio A, Andria G, Meroni G, Parenti G: X-linked recessive chondrodysplasia punctata: spectrum of arylsulfatase E gene mutations and expanded clinical variability. Am J Med Genet A. 2003 Mar 1;117A(2):164-8. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 5562
Enzyme 33 Name Annexin A3
Enzyme 33 Synonyms
  1. 35-alpha calcimedin
  2. Annexin III
  3. Annexin-3
  4. Inositol 1,2-cyclic phosphate 2-phosphohydrolase
  5. Lipocortin III
  6. Placental anticoagulant protein III
  7. PAP-III
Enzyme 33 Gene Name ANXA3
Enzyme 33 Protein Sequence >Annexin A3 
MASIWVGHRGTVRDYPDFSPSVDAEAIQKAIRGIGTDEKMLISILTERSNAQRQLIVKEY
QAAYGKELKDDLKGDLSGHFEHLMVALVTPPAVFDAKQLKKSMKGAGTNEDALIEILTTR
TSRQMKDISQAYYTVYKKSLGDDISSETSGDFRKALLTLADGRRDESLKVDEHLAKQDAQ
ILYKAGENRWGTDEDKFTEILCLRSFPQLKLTFDEYRNISQKDIVDSIKGELSGHFEDLL
LAIVNCVRNTPAFLAERLHRALKGIGTDEFTLNRIMVSRSEIDLLDIRTEFKKHYGYSLY
SAIKSDTSGDYEITLLKICGGDD
Enzyme 33 Number of Residues 323
Enzyme 33 Molecular Weight 36374.8
Enzyme 33 Theoretical pI 5.71
Enzyme 33 GO Classification
Function
  • binding
  • calcium ion binding
  • calcium-dependent phospholipid binding
  • cation binding
  • enzyme inhibitor activity
  • enzyme regulator activity
  • ion binding
  • lipase inhibitor activity
  • lipid binding
  • metal ion binding
  • phospholipase inhibitor activity
  • phospholipid binding
Process
—
Component
—
Enzyme 33 General Function Involved in calcium ion binding
Enzyme 33 Specific Function Inhibitor of phospholipase A2, also possesses anti- coagulant properties. Also cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate
Enzyme 33 Pathways Not Available
Enzyme 33 Reactions Not Available
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein Not Available
Enzyme 33 UniProtKB/Swiss-Prot ID P12429 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name ANXA3_HUMAN Link Image
Enzyme 33 PDB ID 1AII Link Image
Enzyme 33 PDB File Show
Enzyme 33 3D Structure
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >972 bp 
ATGGCATCTATCTGGGTTGGACACCGAGGAACAGTAAGAGATTATCCAGACTTTAGCCCA
TCAGTGGATGCTGAAGCTATTCAGAAAGCAATCAGAGGAATTGGAACTGATGAGAAAATG
CTCATCAGCATTCTGACTGAGAGGTCAAATGCACAGCGGCAGCTGATTGTTAAGGAATAT
CAAGCAGCATATGGAAAGGAGCTGAAAGATGACTTGAAGGGTGATCTCTCTGGCCACTTT
GAGCATCTCATGGTGGCCCTAGTGACTCCACCAGCAGTCTTTGATGCAAAGCAGCTAAAG
AAATCCATGAAGGGCGCGGGAACAAACGAAGATGCCTTGATTGAAATCTTAACTACCAGG
ACAAGCAGGCAAATGAAGGATATCTCTCAAGCCTATTATACAGTATACAAGAAGAGTCTT
GGAGATGACATTAGTTCCGAAACATCTGGTGACTTCCGGAAAGCTCTGTTGACTTTGGCA
GATGGCAGAAGAGATGAAAGTCTGAAAGTGGATGAGCATCTGGCCAAACAAGATGCCCAG
ATTCTCTATAAAGCTGGTGAGAACAGATGGGGCACGGATGAAGACAAATTCACTGAGATC
CTGTGTTTAAGGAGCTTTCCTCAATTAAAACTAACATTTGATGAATACAGAAATATCAGC
CAAAAGGACATTGTGGACAGCATAAAAGGAGAATTATCTGGGCATTTTGAAGACTTACTG
TTGGCCATAGTTAATTGTGTGAGGAACACGCCGGCCTTTTTAGCCGAAAGACTGCATCGA
GCCTTGAAGGGTATTGGAACTGATGAGTTTACTCTGAACCGAATAATGGTGTCCAGATCA
GAAATTGACCTTTTGGACATTCGAACAGAGTTCAAGAAGCATTATGGCTATTCCCTATAT
TCAGCAATTAAATCGGATACTTCTGGAGACTATGAAATCACACTCTTAAAAATCTGTGGT
GGAGATGACTGA
Enzyme 33 GenBank Gene ID M20560 Link Image
Enzyme 33 GeneCard ID ANXA3 Link Image
Enzyme 33 GenAtlas ID ANXA3 Link Image
Enzyme 33 HGNC ID HGNC:541 Link Image
Enzyme 33 Chromosome Location 4
Enzyme 33 Locus 4q21.21
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Pepinsky RB, Tizard R, Mattaliano RJ, Sinclair LK, Miller GT, Browning JL, Chow EP, Burne C, Huang KS, Pratt D, et al.: Five distinct calcium and phospholipid binding proteins share homology with lipocortin I. J Biol Chem. 1988 Aug 5;263(22):10799-811. [PubMed Link Image]
  2. Tait JF, Frankenberry DA, Miao CH, Killary AM, Adler DA, Disteche CM: Chromosomal localization of the human annexin III (ANX3) gene. Genomics. 1991 Jun;10(2):441-8. [PubMed Link Image]
  3. Tait JF, Smith C, Xu L, Cookson BT: Structure and polymorphisms of the human annexin III (ANX3) gene. Genomics. 1993 Oct;18(1):79-86. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  7. Ross TS, Tait JF, Majerus PW: Identity of inositol 1,2-cyclic phosphate 2-phosphohydrolase with lipocortin III. Science. 1990 May 4;248(4955):605-7. [PubMed Link Image]
  8. Tait JF, Sakata M, McMullen BA, Miao CH, Funakoshi T, Hendrickson LE, Fujikawa K: Placental anticoagulant proteins: isolation and comparative characterization four members of the lipocortin family. Biochemistry. 1988 Aug 23;27(17):6268-76. [PubMed Link Image]
  9. Ernst JD, Hoye E, Blackwood RA, Jaye D: Purification and characterization of an abundant cytosolic protein from human neutrophils that promotes Ca2(+)-dependent aggregation of isolated specific granules. J Clin Invest. 1990 Apr;85(4):1065-71. [PubMed Link Image]
  10. Favier-Perron B, Lewit-Bentley A, Russo-Marie F: The high-resolution crystal structure of human annexin III shows subtle differences with annexin V. Biochemistry. 1996 Feb 13;35(6):1740-4. [PubMed Link Image]
  11. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 5597
Enzyme 34 Name Type I inositol-1,4,5-trisphosphate 5-phosphatase
Enzyme 34 Synonyms
  1. 5PTase
Enzyme 34 Gene Name INPP5A
Enzyme 34 Protein Sequence >Type I inositol-1,4,5-trisphosphate 5-phosphatase 
MAGKAAAPGTAVLLVTANVGSLFDDPENLQKNWLREFYQVVHTHKPHFMALHCQEFGGKN
YEASMSHVDKFVKELLSSDAMKEYNRARVYLDENYKSQEHFTALGSFYFLHESLKNIYQF
DFKAKKYRKVAGKEIYSDTLESTPMLEKEKFPQDYFPECKWSRKGFIRTRWCIADCAFDL
VNIHLFHDASNLVAWETSPSVYSGIRHKALGYVLDRIIDQRFEKVSYFVFGDFNFRLDSK
SVVETLCTKATMQTVRAADTNEVVKLIFRESDNDRKVMLQLEKKLFDYFNQEVFRDNNGT
ALLEFDKELSVFKDRLYELDISFPPSYPYSEDARQGEQYMNTRCPAWCDRILMSPSAKEL
VLRSESEEKVVTYDHIGPNVCMGDHKPVFLAFRIMPGAGKPHAHVHKCCVVQ
Enzyme 34 Number of Residues 412
Enzyme 34 Molecular Weight 47819.2
Enzyme 34 Theoretical pI 7.04
Enzyme 34 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphatase activity
  • phosphatase activity
  • phosphoric ester hydrolase activity
Process
—
Component
—
Enzyme 34 General Function Involved in inositol or phosphatidylinositol phosphatase activity
Enzyme 34 Specific Function Major isoenzyme hydrolyzing the calcium-mobilizing second messenger Ins(1,4,5)P3, this is a signal-terminating reaction
Enzyme 34 Pathways
Enzyme 34 Reactions
  • (1) D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate [RN:R03394]
  • (2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate [RN:R03430]
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 57209040 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q14642 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name I5P1_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >1239 bp 
ATGGCGGGGAAGGCGGCCGCCCCGGGCACCGCGGTGCTGCTGGTCACGGCCAACGTGGGC
TCGCTCTTCGACGACCCAGAAAACCTGCAGAAGAACTGGCTTCGGGAATTTTACCAGGTC
GTGCACACACACAAGCCGCACTTCATGGCCTTGCACTGTCAGGAGTTTGGAGGGAAGAAC
TACGAGGCCTCCATGTCCCACGTGGACAAGTTCGTCAAAGAACTATTGTCGAGTGATGCG
ATGAAAGAATATAACAGGGCTCGAGTCTACCTGGATGAAAACTACAAATCCCAGGAGCAC
TTCACGGCACTAGGAAGCTTTTATTTTCTTCATGAGTCCTTAAAAAACATCTACCAGTTT
GACTTTAAAGCTAAGAAGTATAGAAAGGTCGCTGGCAAAGAGATCTACTCGGATACCTTA
GAGAGCACGCCCATGCTGGAGAAGGAGAAGTTTCCGCAGGACTACTTCCCCGAGTGCAAA
TGGTCAAGAAAAGGCTTCATCCGGACGAGGTGGTGCATTGCAGACTGTGCCTTTGACTTG
GTGAATATCCATCTTTTCCATGATGCTTCCAATCTGGTCGCCTGGGAAACAAGCCCTTCC
GTGTACTCGGGAATCCGGCACAAGGCACTGGGCTACGTGCTGGACAGAATCATTGATCAG
CGATTCGAGAAGGTTTCCTACTTTGTATTTGGTGATTTCAACTTCCGGCTGGATTCCAAG
TCCGTCGTGGAGACGCTCTGCACAAAAGCCACCATGCAGACGGTCCGGGCCGCCGACACC
AATGAAGTGGTGAAGCTCATATTTCGTGAGTCGGACAACGACCGGAAGGTTATGCTCCAG
TTAGAAAAGAAACTCTTCGACTACTTCAACCAGGAGGTTTTCCGAGACAACAACGGCACC
GCGCTCTTGGAGTTTGACAAGGAGTTGTCTGTCTTTAAGGACAGACTGTATGAACTGGAC
ATCTCGTTCCCTCCCAGCTACCCGTACAGTGAGGACGCCCGCCAGGGTGAGCAGTACATG
AACACCCGGTGCCCAGCCTGGTGTGACCGCATCCTCATGTCCCCGTCTGCCAAGGAGCTG
GTGCTGCGGTCGGAGAGCGAGGAGAAGGTTGTCACCTATGACCACATTGGGCCCAACGTC
TGCATGGGAGACCACAAGCCCGTGTTCCTGGCCTTCCGAATCATGCCCGGGGCAGGTAAA
CCTCATGCCCATGTGCACAAGTGTTGTGTCGTGCAGTGA
Enzyme 34 GenBank Gene ID AL356603 Link Image
Enzyme 34 GeneCard ID INPP5A Link Image
Enzyme 34 GenAtlas ID INPP5A Link Image
Enzyme 34 HGNC ID HGNC:6076 Link Image
Enzyme 34 Chromosome Location 1
Enzyme 34 Locus 10q26.3
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. De Smedt F, Verjans B, Mailleux P, Erneux C: Cloning and expression of human brain type I inositol 1,4,5-trisphosphate 5-phosphatase. High levels of mRNA in cerebellar Purkinje cells. FEBS Lett. 1994 Jun 20;347(1):69-72. [PubMed Link Image]
  2. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Laxminarayan KM, Chan BK, Tetaz T, Bird PI, Mitchell CA: Characterization of a cDNA encoding the 43-kDa membrane-associated inositol-polyphosphate 5-phosphatase. J Biol Chem. 1994 Jun 24;269(25):17305-10. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 5627
Enzyme 35 Name Amiloride-sensitive amine oxidase [copper-containing]
Enzyme 35 Synonyms
  1. DAO
  2. Diamine oxidase
  3. Amiloride-binding protein
  4. ABP
  5. Histaminase
  6. Kidney amine oxidase
  7. KAO
Enzyme 35 Gene Name ABP1
Enzyme 35 Protein Sequence >Amiloride-sensitive amine oxidase [copper-containing] 
MPALGWAVAAILMLQTAMAEPSPGTLPRKAGVFSDLSNQELKAVHSFLWSKKELRLQPSS
TTTMAKNTVFLIEMLLPKKYHVLRFLDKGERHPVREARAVIFFGDQEHPNVTEFAVGPLP
GPCYMRALSPRPGYQSSWASRPISTAEYALLYHTLQEATKPLHQFFLNTTGFSFQDCHDR
CLAFTDVAPRGVASGQRRSWLIIQRYVEGYFLHPTGLELLVDHGSTDAGHWAVEQVWYNG
KFYGSPEELARKYADGEVDVVVLEDPLPGGKGHDSTEEPPLFSSHKPRGDFPSPIHVSGP
RLVQPHGPRFRLEGNAVLYGGWSFAFRLRSSSGLQVLNVHFGGERIAYEVSVQEAVALYG
GHTPAGMQTKYLDVGWGLGSVTHELAPGIDCPETATFLDTFHYYDADDPVHYPRALCLFE
MPTGVPLRRHFNSNFKGGFNFYAGLKGQVLVLRTTSTVYNYDYIWDFIFYPNGVMEAKMH
ATGYVHATFYTPEGLRHGTRLHTHLIGNIHTHLVHYRVDLDVAGTKNSFQTLQMKLENIT
NPWSPRHRVVQPTLEQTQYSWERQAAFRFKRKLPKYLLFTSPQENPWGHKRTYRLQIHSM
ADQVLPPGWQEEQAITWARYPLAVTKYRESELCSSSIYHQNDPWHPPVVFEQFLHNNENI
ENEDLVAWVTVGFLHIPHSEDIPNTATPGNSVGFLLRPFNFFPEDPSLASRDTVIVWPRD
NGPNYVQRWIPEDRDCSMPPPFSYNGTYRPV
Enzyme 35 Number of Residues 751
Enzyme 35 Molecular Weight 85377.1
Enzyme 35 Theoretical pI 7.10
Enzyme 35 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • cofactor binding
  • copper ion binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
  • primary amine oxidase activity
  • quinone binding
  • transition metal ion binding
Process
  • amine metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
Component
—
Enzyme 35 General Function Involved in copper ion binding
Enzyme 35 Specific Function Catalyzes the degradation of compounds such as putrescine, histamine, spermine, and spermidine, substances involved in allergic and immune responses, cell proliferation, tissue differentiation, tumor formation, and possibly apoptosis. Placental DAO is thought to play a role in the regulation of the female reproductive function
Enzyme 35 Pathways
Enzyme 35 Reactions
  • histamine + H2O + O2 = (imidazol-4-yl)acetaldehyde + NH3 + H2O2 [RN:R02150]
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • 1-19
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 73486661 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID P19801 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name ABP1_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >2256 bp 
ATGCCGGCCCTGGGCTGGGCCGTGGCTGCCATCCTGATGCTGCAGACGGCCATGGCGGAG
CCCTCCCCGGGGACTCTGCCCAGGAAGGCAGGGGTGTTTTCAGACCTAAGCAACCAAGAG
CTGAAGGCAGTGCACAGCTTCCTCTGGTCCAAGAAGGAGCTGAGGCTGCAGCCCTCCAGT
ACCACCACCATGGCCAAGAACACCGTGTTTCTCATCGAGATGCTGCTGCCCAAGAAGTAC
CATGTGCTGAGGTTTCTGGATAAAGGTGAAAGGCATCCTGTGCGGGAAGCCCGTGCCGTC
ATCTTCTTTGGTGACCAGGAGCATCCCAATGTCACCGAGTTTGCTGTGGGGCCCCTGCCA
GGGCCCTGCTACATGCGAGCACTGTCCCCCAGGCCTGGGTACCAGTCCTCCTGGGCATCG
AGGCCCATCTCCACAGCAGAGTATGCCCTCCTCTACCACACCCTGCAGGAAGCCACCAAG
CCCCTGCATCAGTTCTTCCTCAATACCACAGGCTTCTCATTCCAAGACTGCCATGACAGA
TGCCTGGCCTTCACCGATGTGGCCCCCCGGGGTGTGGCTTCTGGCCAGCGCCGCAGTTGG
CTTATCATACAGCGCTATGTAGAAGGCTACTTTCTGCACCCCACTGGGCTGGAGCTCCTC
GTGGATCATGGGAGCACAGATGCTGGGCACTGGGCCGTGGAGCAGGTGTGGTACAACGGG
AAGTTCTATGGGAGCCCAGAGGAACTGGCTCGGAAGTATGCAGATGGAGAGGTGGACGTG
GTGGTCCTGGAGGACCCGCTGCCTGGGGGCAAGGGGCATGACAGCACAGAGGAGCCGCCC
CTCTTCTCCTCCCACAAGCCCCGCGGGGACTTCCCCAGCCCCATCCATGTGAGCGGCCCC
CGCTTGGTCCAGCCCCACGGCCCTCGCTTCAGGCTGGAGGGCAACGCTGTGCTCTACGGC
GGCTGGAGCTTTGCCTTCCGGCTGCGCTCCTCCTCCGGGCTGCAGGTCCTGAACGTGCAC
TTCGGCGGAGAGCGCATTGCCTATGAGGTCAGCGTGCAAGAGGCAGTGGCGCTGTATGGA
GGACACACACCTGCAGGCATGCAGACCAAGTACCTCGATGTCGGCTGGGGCCTGGGCAGC
GTCACTCATGAGTTAGCCCCCGGCATCGACTGCCCGGAGACCGCCACCTTCCTGGACACT
TTCCACTACTATGATGCCGATGACCCGGTCCATTATCCCCGAGCCCTCTGCCTCTTTGAA
ATGCCCACAGGGGTGCCCCTTCGGCGGCACTTTAATTCCAACTTTAAAGGTGGCTTCAAC
TTCTATGCGGGGCTGAAGGGCCAGGTGCTGGTGCTGCGGACAACTTCAACTGTCTACAAT
TATGATTACATTTGGGACTTTATCTTCTACCCCAACGGGGTGATGGAGGCCAAGATGCAT
GCCACTGGCTACGTCCACGCCACCTTCTACACCCCCGAGGGGCTGCGCCACGGCACTCGC
CTGCACACCCACCTGATTGGCAACATACACACTCACTTGGTGCACTACCGCGTAGACCTG
GATGTGGCAGGCACCAAGAACAGCTTCCAGACACTGCAGATGAAGCTAGAAAACATCACC
AACCCCTGGAGCCCAAGACACCGCGTGGTCCAGCCAACTCTGGAGCAGACGCAGTACTCC
TGGGAGCGCCAGGCGGCCTTCCGCTTCAAAAGGAAGCTGCCTAAGTACCTGCTCTTTACC
AGCCCCCAGGAGAACCCCTGGGGCCACAAGCGCACGTACCGCCTGCAGATCCACTCCATG
GCCGACCAGGTGCTGCCCCCAGGCTGGCAGGAGGAGCAGGCCATCACCTGGGCAAGGTAC
CCCCTGGCAGTGACCAAGTACCGGGAGTCGGAGCTGTGCAGCAGCAGCATCTACCACCAG
AACGACCCCTGGCACCCGCCCGTGGTCTTTGAGCAGTTTCTTCACAACAACGAGAACATT
GAAAATGAGGACCTGGTGGCCTGGGTGACGGTGGGCTTCCTGCACATCCCCCACTCAGAG
GACATTCCCAACACAGCCACACCTGGGAACTCCGTGGGCTTCCTGCTCCGGCCATTCAAC
TTCTTCCCAGAGGACCCCTCCCTGGCATCCAGAGACACTGTGATCGTGTGGCCTCGGGAC
AACGGCCCCAACTACGTCCAGCGCTGGATCCCTGAGGACAGGGACTGCTCGATGCCTCCC
CCTTTTAGCTACAATGGGACCTATAGACCTGTGTGA
Enzyme 35 GenBank Gene ID NM_001091.2 Link Image
Enzyme 35 GeneCard ID ABP1 Link Image
Enzyme 35 GenAtlas ID ABP1 Link Image
Enzyme 35 HGNC ID HGNC:80 Link Image
Enzyme 35 Chromosome Location 7
Enzyme 35 Locus 7q34-q36
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Barbry P, Champe M, Chassande O, Munemitsu S, Champigny G, Lingueglia E, Maes P, Frelin C, Tartar A, Ullrich A, et al.: Human kidney amiloride-binding protein: cDNA structure and functional expression. Proc Natl Acad Sci U S A. 1990 Oct;87(19):7347-51. [PubMed Link Image]
  2. Chassande O, Renard S, Barbry P, Lazdunski M: The human gene for diamine oxidase, an amiloride binding protein. Molecular cloning, sequencing, and characterization of the promoter. J Biol Chem. 1994 May 20;269(20):14484-9. [PubMed Link Image]
  3. Zhang X, Kim J, McIntire WS: cDNA sequences of variant forms of human placenta diamine oxidase. Biochem Genet. 1995 Aug;33(7-8):261-8. [PubMed Link Image]
  4. 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]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Novotny WF, Chassande O, Baker M, Lazdunski M, Barbry P: Diamine oxidase is the amiloride-binding protein and is inhibited by amiloride analogues. J Biol Chem. 1994 Apr 1;269(13):9921-5. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 5628
Enzyme 36 Name Glyoxylate reductase/hydroxypyruvate reductase
Enzyme 36 Synonyms Not Available
Enzyme 36 Gene Name GRHPR
Enzyme 36 Protein Sequence >Glyoxylate reductase/hydroxypyruvate reductase 
MRPVRLMKVFVTRRIPAEGRVALARAADCEVEQWDSDEPIPAKELERGVAGAHGLLCLLS
DHVDKRILDAAGANLKVISTMSVGIDHLALDEIKKRGIRVGYTPDVLTDTTAELAVSLLL
TTCRRLPEAIEEVKNGGWTSWKPLWLCGYGLTQSTVGIIGLGRIGQAIARRLKPFGVQRF
LYTGRQPRPEEAAEFQAEFVSTPELAAQSDFIVVACSLTPATEGLCNKDFFQKMKETAVF
INISRGDVVNQDDLYQALASGKIAAAGLDVTSPEPLPTNHPLLTLKNCVILPHIGSATHR
TRNTMSLLAANNLLAGLRGEPMPSELKL
Enzyme 36 Number of Residues 328
Enzyme 36 Molecular Weight 35667.9
Enzyme 36 Theoretical pI 7.44
Enzyme 36 GO Classification
Function
  • NAD or NADH binding
  • binding
  • catalytic activity
  • cofactor binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • metabolic process
Component
—
Enzyme 36 General Function Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Enzyme 36 Specific Function Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate
Enzyme 36 Pathways
Enzyme 36 Reactions
  • D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H + H+ [RN:R01388 R01392]
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 6002730 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q9UBQ7 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name GRHPR_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >987 bp 
ATGAGACCGGTGCGACTCATGAAGGTGTTCGTCACCCGCAGGATACCCGCCGAGGGTAGG
GTCGCGCTCGCCCGGGCGGCAGACTGTGAGGTGGAGCAGTGGGACTCGGATGAGCCCATC
CCTGCCAAGGAGCTAGAGCGAGGTGTGGCGGGGGCCCACGGCCTGCTCTGCCTCCTCTCC
GACCACGTGGACAAGAGGATCCTGGATGCTGCAGGGGCCAATCTCAAAGTCATCAGCACC
ATGTCTGTGGGCATCGACCACTTGGCTTTGGATGAAATCAAGAAGCGTGGGATCCGAGTT
GGCTACACCCCAGATGTCCTGACAGATACCACCGCCGAACTCGCAGTCTCCCTGCTACTT
ACCACCTGCCGCCGGTTGCCGGAGGCCATCGAGGAAGTGAAGAATGGTGGCTGGACCTCG
TGGAAGCCCCTCTGGCTGTGTGGCTATGGACTCACGCAGAGCACTGTCGGCATCATCGGG
CTGGGGCGCATAGGCCAGGCCATTGCTCGGCGTCTGAAACCATTCGGTGTCCAGAGATTT
CTGTACACAGGGCGCCAGCCCAGGCCTGAGGAAGCAGCAGAATTCCAGGCAGAGTTTGTG
TCTACCCCTGAGCTGGCTGCCCAATCTGATTTCATCGTCGTGGCCTGCTCCTTAACACCT
GCAACCGAGGGACTCTGCAACAAGGACTTCTTCCAGAAGATGAAGGAAACAGCTGTGTTC
ATCAACATCAGCAGGGGCGACGTCGTAAACCAGGACGACCTGTACCAGGCCTTGGCCAGT
GGTAAGATTGCAGCTGCTGGACTGGATGTGACGAGCCCAGAACCACTGCCTACAAACCAC
CCTCTCCTGACCCTGAAGAACTGTGTGATTCTGCCCCACATTGGCAGTGCCACCCACAGA
ACCCGCAACACCATGTCCTTGTTGGCAGCTAACAACTTGCTGGCTGGCCTGAGAGGGGAG
CCGATGCCTAGTGAACTCAAGCTGTAG
Enzyme 36 GenBank Gene ID AF134895 Link Image
Enzyme 36 GeneCard ID GRHPR Link Image
Enzyme 36 GenAtlas ID GRHPR Link Image
Enzyme 36 HGNC ID HGNC:4570 Link Image
Enzyme 36 Chromosome Location 9
Enzyme 36 Locus 9q12
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Rumsby G, Cregeen DP: Identification and expression of a cDNA for human hydroxypyruvate/glyoxylate reductase. Biochim Biophys Acta. 1999 Sep 3;1446(3):383-8. [PubMed Link Image]
  2. Cramer SD, Ferree PM, Lin K, Milliner DS, Holmes RP: The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type II. Hum Mol Genet. 1999 Oct;8(11):2063-9. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Huang T, Yang W, Pereira AC, Craigen WJ, Shih VE: Cloning and characterization of a putative human d-2-hydroxyacid dehydrogenase in chromosome 9q. Biochem Biophys Res Commun. 2000 Feb 16;268(2):298-301. [PubMed Link Image]
  5. Booth MP, Conners R, Rumsby G, Brady RL: Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase. J Mol Biol. 2006 Jun 30;360(1):178-89. Epub 2006 May 22. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 5630
Enzyme 37 Name Membrane primary amine oxidase
Enzyme 37 Synonyms
  1. Copper amine oxidase
  2. HPAO
  3. Semicarbazide-sensitive amine oxidase
  4. SSAO
  5. Vascular adhesion protein 1
  6. VAP-1
Enzyme 37 Gene Name AOC3
Enzyme 37 Protein Sequence >Membrane primary amine oxidase 
MNQKTILVLLILAVITIFALVCVLLVGRGGDGGEPSQLPHCPSVSPSAQPWTHPGQSQLF
ADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPP
AREALAIVFFGRQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLFQEYLDID
QMIFNRELPQASGLLHHCCFYKHRGRNLVTMTTAPRGLQSGDRATWFGLYYNISGAGFFL
HHVGLELLVNHKALDPARWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSW
SLKSPVPPGPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVRFQGERLV
YEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVDCPYLATYVDWHFLLESQ
APKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFGGLAETVLVVRSMSTLLNYDYVWDTVFH
PSGAIEIRFYATGYISSAFLFGATGKYGNQVSEHTLGTVHTHSAHFKVDLDVAGLENWVW
AEDMVFVPMAVPWSPEHQLQRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHP
RGYRIQMLSFAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDPWAPTVDF
SDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYNFFDEDPSFYSA
DSIYFRGDQDAGACEVNPLACLPQAAACAPDLPAFSHGGFSHN
Enzyme 37 Number of Residues 763
Enzyme 37 Molecular Weight 84621.3
Enzyme 37 Theoretical pI 6.51
Enzyme 37 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • cofactor binding
  • copper ion binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
  • primary amine oxidase activity
  • quinone binding
  • transition metal ion binding
Process
  • amine metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
Component
—
Enzyme 37 General Function Involved in copper ion binding
Enzyme 37 Specific Function Cell adhesion protein that participates in lymphocyte recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin- independent fashion. Has a monoamine oxidase activity. May play a role in adipogenesis
Enzyme 37 Pathways
Enzyme 37 Reactions
  • RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2 [RN:R01853]
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • 6-26
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein Not Available
Enzyme 37 UniProtKB/Swiss-Prot ID Q16853 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name AOC3_HUMAN Link Image
Enzyme 37 PDB ID 1PU4 Link Image
Enzyme 37 PDB File Show
Enzyme 37 3D Structure
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >2292 bp 
ATGAACCAGAAGACAATCCTCGTGCTCCTCATTCTGGCCGTCATCACCATCTTTGCCTTG
GTTTGTGTCCTGCTGGTGGGCAGGGGTGGAGATGGGGGTGAACCCAGCCAGCTTCCCCAT
TGCCCCTCTGTATCTCCCAGTGCCCAGCCTTGGACACACCCTGGCCAGAGCCAGCTGTTT
GCAGACCTGAGCCGAGAGGAGCTGACGGCTGTGATGCGCTTTCTGACCCAGCGGCTGGGG
CCAGGGCTGGTGGATGCAGCCCAGGCCCGGCCCTCGGACAACTGTGTCTTCTCAGTGGAG
TTGCAGCTGCCTCCCAAGGCTGCAGCCCTGGCTCACTTGGACAGGGGGAGCCCCCCACCT
GCCCGGGAGGCACTGGCCATCGTCTTCTTTGGCAGGCAACCCCAGCCCAACGTGAGTGAG
CTGGTGGTGGGGCCACTGCCTCACCCCTCCTACATGCGGGACGTGACTGTGGAGCGTCAT
GGAGGCCCCCTGCCCTATCACCGACGCCCCGTGCTGTTCCAAGAGTACCTGGACATAGAC
CAGATGATCTTCAACAGAGAGCTGCCCCAGGCTTCTGGGCTTCTCCACCACTGTTGCTTC
TACAAGCACCGGGGACGGAACCTGGTGACAATGACCACGGCTCCCCGTGGTCTGCAATCA
GGGGACCGGGCCACCTGGTTTGGCCTCTACTACAACATCTCGGGCGCTGGGTTCTTCCTG
CACCACGTGGGCTTGGAGCTGCTAGTGAACCACAAGGCCCTTGACCCTGCCCGCTGGACT
ATCCAGAAGGTGTTCTATCAAGGCCGCTACTACGACAGCCTGGCCCAGCTGGAGGCCCAG
TTTGAGGCCGGCCTGGTGAATGTGGTGCTGATCCCAGACAATGGCACAGGTGGGTCCTGG
TCCCTGAAGTCCCCTGTGCCCCCGGGTCCAGCTCCCCCTCTACAGTTCTATCCCCAAGGC
CCCCGCTTCAGTGTCCAGGGAAGTCGAGTGGCCTCCTCACTGTGGACTTTCTCCTTTGGC
CTCGGAGCATTCAGTGGCCCAAGGATCTTTGACGTTCGCTTCCAAGGAGAAAGACTAGTT
TATGAGATAAGCCTCCAAGAGGCCTTGGCCATCTATGGTGGAAATTCCCCAGCAGCAATG
ACGACCCGCTATGTGGATGGAGGCTTTGGCATGGGCAAGTACACCACGCCCCTGACCCGT
GGGGTGGACTGCCCCTACTTGGCCACCTACGTGGACTGGCACTTCCTTTTGGAGTCCCAG
GCCCCCAAGACAATACGTGATGCCTTTTGTGTGTTTGAACAGAACCAGGGCCTCCCCCTG
CGGCGACACCACTCAGATCTCTACTCGCACTACTTTGGGGGTCTTGCGGAAACGGTGCTG
GTCGTCAGATCTATGTCCACCTTGCTCAACTATGACTATGTGTGGGATACGGTCTTCCAC
CCCAGTGGGGCCATAGAAATACGATTCTATGCCACGGGCTACATCAGCTCGGCATTCCTC
TTTGGTGCTACTGGGAAGTACGGGAACCAAGTGTCAGAGCACACCCTGGGCACGGTCCAC
ACCCACAGCGCCCACTTCAAGGTGGATCTGGATGTAGCAGGACTGGAGAACTGGGTCTGG
GCCGAGGATATGGTCTTTGTCCCCATGGCTGTGCCCTGGAGCCCTGAGCACCAGCTGCAG
AGGCTGCAGGTGACCCGGAAGCTGCTGGAGATGGAGGAGCAGGCCGCCTTCCTCGTGGGA
AGCGCCACCCCTCGCTACCTGTACCTGGCCAGCAACCACAGCAACAAGTGGGGTCACCCC
CGGGGCTACCGCATCCAGATGCTCAGCTTTGCTGGAGAGCCGCTGCCCCAAAACAGCTCC
ATGGCGAGAGGCTTCAGCTGGGAGAGGTACCAGCTGGCTGTGACCCAGCGGAAGGAGGAG
GAGCCCAGTAGCAGCAGCGTTTTCAATCAGAATGACCCTTGGGCCCCCACTGTGGATTTC
AGTGACTTCATCAACAATGAGACCATTGCTGGAAAGGATTTGGTGGCCTGGGTGACAGCT
GGTTTTCTGCATATCCCACATGCAGAGGACATTCCTAACACAGTGACTGTGGGGAACGGC
GTGGGCTTCTTCCTCCGACCCTATAACTTCTTTGACGAAGACCCCTCCTTCTACTCTGCC
GACTCCATCTACTTCCGAGGGGACCAGGATGCTGGGGCCTGCGAGGTCAACCCCCTAGCT
TGCCTGCCCCAGGCTGCTGCCTGTGCCCCCGACCTCCCTGCCTTCTCCCACGGGGGCTTC
TCTCACAACTAG
Enzyme 37 GenBank Gene ID U39447 Link Image
Enzyme 37 GeneCard ID AOC3 Link Image
Enzyme 37 GenAtlas ID AOC3 Link Image
Enzyme 37 HGNC ID HGNC:550 Link Image
Enzyme 37 Chromosome Location 1
Enzyme 37 Locus 17q21
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Zhang X, McIntire WS: Cloning and sequencing of a copper-containing, topa quinone-containing monoamine oxidase from human placenta. Gene. 1996 Nov 14;179(2):279-86. [PubMed Link Image]
  2. Smith DJ, Salmi M, Bono P, Hellman J, Leu T, Jalkanen S: Cloning of vascular adhesion protein 1 reveals a novel multifunctional adhesion molecule. J Exp Med. 1998 Jul 6;188(1):17-27. [PubMed Link Image]
  3. Zhang Q, Mashima Y, Noda S, Imamura Y, Kudoh J, Shimizu N, Nishiyama T, Umeda S, Oguchi Y, Tanaka Y, Iwata T: Characterization of AOC2 gene encoding a copper-binding amine oxidase expressed specifically in retina. Gene. 2003 Oct 30;318:45-53. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed Link Image]
  7. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  8. Bour S, Daviaud D, Gres S, Lefort C, Prevot D, Zorzano A, Wabitsch M, Saulnier-Blache JS, Valet P, Carpene C: Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and monoamine oxidase in human adipocytes. Biochimie. 2007 Aug;89(8):916-25. Epub 2007 Feb 24. [PubMed Link Image]
  9. Kaitaniemi S, Elovaara H, Gron K, Kidron H, Liukkonen J, Salminen T, Salmi M, Jalkanen S, Elima K: The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase. Cell Mol Life Sci. 2009 Aug;66(16):2743-57. Epub 2009 Jul 9. [PubMed Link Image]
  10. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  11. Airenne TT, Nymalm Y, Kidron H, Smith DJ, Pihlavisto M, Salmi M, Jalkanen S, Johnson MS, Salminen TA: Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications. Protein Sci. 2005 Aug;14(8):1964-74. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 5631
Enzyme 38 Name Retina-specific copper amine oxidase
Enzyme 38 Synonyms
  1. RAO
  2. Amine oxidase [copper-containing]
  3. Semicarbazide-sensitive amine oxidase
  4. SSAO
Enzyme 38 Gene Name AOC2
Enzyme 38 Protein Sequence >Retina-specific copper amine oxidase 
MHLKIVLAFLALSLITIFALAYVLLTSPGGSSQPPHCPSVSHRAQPWPHPGQSQLFADLS
REELTAVMRFLTQRLGPGLVDAAQAQPSDNCIFSVELQLPPKAAALAHLDRGSPPPAREA
LAIVLFGGQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLRAEFTQMWRHLK
EVELPKAPIFLSSTFNYNGSTLAAVHATPRGLRSGDRATWMALYHNISGVGLFLHPVGLE
LLLDHRALDPAHWTVQQVFYLGHYYADLGQLEREFKSGRLEVVRVPLPPPNGASSLRSRN
SPGPLPPLQFSPQGSQYSVQGNLVVSSLWSFTFGHGVFSGLRIFDVRFQGERIAYEVSVQ
ECVSIYGADSPKTMLTRYLDSSFGLGRNSRGLVRGVDCPYQATMVDIHILVGKGAVQLLP
GAVCVFEEAQGLPLRRHHNYLQNHFYGGLASSALVVRSVSSVGNYDYIWDFVLYPNGALE
GRVHATGYINTAFLKGGEEGLLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDV
VFKPVAAPWNPEHWLQRPQLTRQVLGKEDLTAFSLGSPLPRYLYLASNQTNAWGHQRGYR
IQIHSPLGIHIPLESDMERALSWGRYQLVVTQRKEEESQSSSIYHQNDIWTPTVTFADFI
NNETLLGEDLVAWVTASFLHIPHAEDIPNTVTLGNRVGFLLRPYNFFDEDPSIFSPGSVY
FEKGQDAGLCSINPVACLPDLAACVPDLPPFSYHGF
Enzyme 38 Number of Residues 756
Enzyme 38 Molecular Weight 83672.7
Enzyme 38 Theoretical pI 7.03
Enzyme 38 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • cofactor binding
  • copper ion binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH2 group of donors
  • oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
  • primary amine oxidase activity
  • quinone binding
  • transition metal ion binding
Process
  • amine metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • oxidation reduction
Component
—
Enzyme 38 General Function Involved in copper ion binding
Enzyme 38 Specific Function Has a monoamine oxidase activity with substrate specificity for 2-phenylethylamine and tryptamine. May play a role in adipogenesis. May be a critical modulator of signal transmission in retina
Enzyme 38 Pathways
Enzyme 38 Reactions
  • RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2 [RN:R01853]
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • 1-32
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 3510335 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID O75106 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name AOC2_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >2271 bp 
ATGCATCTCAAGATAGTCCTGGCGTTCCTGGCACTGTCCCTCATTACCATCTTTGCCCTG
GCCTATGTTTTGCTGACCAGCCCAGGTGGTTCCAGCCAGCCTCCCCACTGCCCCTCTGTA
TCCCATAGGGCCCAGCCCTGGCCACACCCTGGCCAGAGCCAGCTGTTTGCAGACCTGAGC
CGAGAGGAGTTGACAGCTGTGATGCGCTTTCTGACCCAGCGGCTGGGGCCAGGGCTGGTG
GACGCAGCCCAGGCTCAGCCCTCGGACAACTGCATCTTCTCAGTGGAGCTGCAGCTGCCC
CCCAAGGCTGCAGCCCTGGCCCACCTGGACAGGGGGAGCCCCCCACCTGCCCGGGAGGCA
CTGGCCATCGTCCTCTTTGGTGGACAACCCCAACCCAATGTGAGTGAGCTGGTGGTGGGG
CCGCTGCCTCACCCCTCGTACATGCGGGATGTGACTGTGGAGCGTCACGGCGGGCCCCTG
CCCTATCACCGTCGCCCGGTGCTGAGAGCTGAGTTTACACAGATGTGGAGGCATCTGAAA
GATGTGGAGCTACCCAAGGCACCCATCTTCCTGTCGTCCACCTTCAACTACAATGGCTCT
ACCCTGGCAGCTGTGCATGCCACCCCTCGGGGCTTGCGCTCAAGGGAACGAACTACCTGG
ATGGCCCTCTACCATAACATCTCAGGGGTTGGTCTTTTCCTTCACCCCGTGGGGCTGGAG
CTACTACTGGACCACAGGGCCCTGGACCCTGCCCACTGGACTGTCCAGCAGGTCTTCTAC
CTTGGGCACTACTATGCAGACTTGGGCCAGTTGGAACGGGAGTTTAAGTCTGGCCGGTTG
GAAGTGGTTAGAGTCCCTCTACCTCCACCAAATGGAGCTTCATCCCTGAGGTCTCGGAAC
TCTCCAGGTCCTCTTCCCCCTCTTCAGTTCTCGCCCCAGGGTTCCCAGTACAGTGTGCAA
GGAAACCTGGTGGTATCCTCCCTCTGGTCATTTACCTTTGGCCATGGGGTGTTCAGCGGC
CTGAGGATTTTTGATGTTCGGTTCCAGGGTGAGCGAATAGCCTATGAAGTCAGTGTCCAG
GAGTGTGTATCTATCTATGGTGCCGATTCACCCAAGACGATGCTGACTCGCTATTTGGAT
AGCAGCTTTGGACTCGGCCGTAACAGCCGAGGCTTGGTGCGGGGAGTGGACTGCCCCTAT
CAAGCCACGATGGTGGACATCCATATATTAGTGGGCAAAGGGGCAGTCCAGCTGCTTCCA
GGGGCTGTGTGTGTATTTGAGGAAGCCCAGGGACTGCCCCTTCGAAGGCACCACAATTAC
CTTCAAAATCATTTCTATGGTGGTTTGGCCAGCTCAGCCCTTGTGGTCAGGTCTGTGTCA
TCTGTGGGCAACTATGACTACATTTGGGACTTTGTGTTGTACCCAAATGGGGCACTTGAA
GGGCGGGTCCATGCCACGGGTTATATCAACACAGCTTTCCTGAAAGGGGGAGAGGAGGGC
CTCCTCTTTGGGAACCGTGTGGGGGAAAGAGTGCTGGGAACGGTGCACACACATGCCTTC
CACTTCAAGCTGGACCTGGATGTGGCAGGGCTGAAAAACTGGGTGGTAGCTGAAGACGTG
GTGTTTAAACCTGTGGCTGCCCCCTGGAACCCGGAGCACTGGCTACAGCGCCCACAGCTG
ACTCGGCAGGTCCTGGGAAAGGAGGACCTGACAGCTTTTTCCTTGGGAAGCCCCCTACCC
CGCTACCTCTACCTGGCTAGCAACCAGACTAATGCGTGGGGTCACCAGCGCGGGTACCGA
ATCCAGATCCACAGCCCCCTTGGCATACAAATACCCCTGGAGAGTGACATGGAGAGGGCC
CTCAGCTGGGGGAGATACCAGCTTGTGGTGACCCAGAGAAAGGAGGAGGAGTCACAGAGC
AGTAGCATCTATCACCAGAATGACATCTGGACACCCACAGTTACCTTTGCTGACTTCATC
AACAATGAAACCCTCTTAGGAGAGGATCTGGTGGCTTGGGTCACAGCCAGCTTCCTGCAC
ATTCCCCATGCCGAGGACATCCCAAACACAGTGACTCTGGGGAACAGAGTTGGCTTCTTG
CTCCGACCCTATAACTTCTTTGATGAGGACCCCTCCATCTTCTCCCCTGGCAGTGTGTAC
TTTGAGAAGGGCCAGGATGCTGGGCTCTGCAGCATCAATCCTGTGGCCTGCCTCCCCGAC
CTGGCAGCCTGTGTCCCGGACTTACCCCCTTTCTCTTACCACGGCTTCTAG
Enzyme 38 GenBank Gene ID AB012943 Link Image
Enzyme 38 GeneCard ID AOC2 Link Image
Enzyme 38 GenAtlas ID AOC2 Link Image
Enzyme 38 HGNC ID HGNC:549 Link Image
Enzyme 38 Chromosome Location 1
Enzyme 38 Locus 17q21
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Imamura Y, Kubota R, Wang Y, Asakawa S, Kudoh J, Mashima Y, Oguchi Y, Shimizu N: Human retina-specific amine oxidase (RAO): cDNA cloning, tissue expression, and chromosomal mapping. Genomics. 1997 Mar 1;40(2):277-83. [PubMed Link Image]
  2. Imamura Y, Noda S, Mashima Y, Kudoh J, Oguchi Y, Shimizu N: Human retina-specific amine oxidase: genomic structure of the gene (AOC2), alternatively spliced variant, and mRNA expression in retina. Genomics. 1998 Jul 15;51(2):293-8. [PubMed Link Image]
  3. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Heniquez A, Meissonnier G, Visentin V, Prevot D, Carpene C: High expression of semicarbazide-sensitive amine oxidase genes AOC2 and AOC3, but not the diamine oxidase gene AOC1 in human adipocytes. Inflamm Res. 2003 Apr;52 Suppl 1:S74-5. [PubMed Link Image]
  6. Bour S, Daviaud D, Gres S, Lefort C, Prevot D, Zorzano A, Wabitsch M, Saulnier-Blache JS, Valet P, Carpene C: Adipogenesis-related increase of semicarbazide-sensitive amine oxidase and monoamine oxidase in human adipocytes. Biochimie. 2007 Aug;89(8):916-25. Epub 2007 Feb 24. [PubMed Link Image]
  7. Kaitaniemi S, Elovaara H, Gron K, Kidron H, Liukkonen J, Salminen T, Salmi M, Jalkanen S, Elima K: The unique substrate specificity of human AOC2, a semicarbazide-sensitive amine oxidase. Cell Mol Life Sci. 2009 Aug;66(16):2743-57. Epub 2009 Jul 9. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 5693
Enzyme 39 Name Deoxyribonuclease-1
Enzyme 39 Synonyms
  1. Deoxyribonuclease I
  2. DNase I
  3. Dornase alfa
Enzyme 39 Gene Name DNASE1
Enzyme 39 Protein Sequence >Deoxyribonuclease-1 
MRGMKLLGALLALAALLQGAVSLKIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQ
EVRDSHLTAVGKLLDNLNQDAPDTYHYVVSEPLGRNSYKERYLFVYRPDQVSAVDSYYYD
DGCEPCGNDTFNREPAIVRFFSRFTEVREFAIVPLHAAPGDAVAEIDALYDVYLDVQEKW
GLEDVMLMGDFNAGCSYVRPSQWSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRIVVAG
MLLRGAVVPDSALPFNFQAAYGLSDQLAQAISDHYPVEVMLK
Enzyme 39 Number of Residues 282
Enzyme 39 Molecular Weight 31433.4
Enzyme 39 Theoretical pI 4.49
Enzyme 39 GO Classification
Function
  • catalytic activity
  • deoxyribonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
Process
  • DNA catabolic process
  • DNA metabolic process
  • cellular macromolecule metabolic process
  • macromolecule metabolic process
  • metabolic process
Component
—
Enzyme 39 General Function Involved in deoxyribonuclease activity
Enzyme 39 Specific Function Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization
Enzyme 39 Pathways Not Available
Enzyme 39 Reactions
  • Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • 1-22
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein Not Available
Enzyme 39 UniProtKB/Swiss-Prot ID P24855 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name DNAS1_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >849 bp 
ATGAGGGGCATGAAGCTGCTGGGGGCGCTGCTGGCACTGGCGGCCCTACTGCAGGGGGCC
GTGTCCCTGAAGATCGCAGCCTTCAACATCCAGACATTTGGGGAGACCAAGATGTCCAAT
GCCACCCTCGTCAGCTACATTGTGCAGATCCTGAGCCGCTATGACATCGCCCTGGTCCAG
GAGGTCAGAGACAGCCACCTGACTGCCGTGGGGAAGCTGCTGGACAACCTCAATCAGGAT
GCACCAGACACCTATCACTACGTGGTCAGTGAGCCACTGGGACGGAACAGCTATAAGGAG
CGCTACCTGTTCGTGTACAGGCCTGACCAGGTGTCTGCGGTGGACAGCTACTACTACGAT
GATGGCTGCGAGCCCTGCGGGAACGACACCTTCAACCGAGAGCCAGCCATTGTCAGGTTC
TTCTCCCGGTTCACAGAGGTCAGGGAGTTTGCCATTGTTCCCCTGCATGCGGCCCCGGGG
GACGCAGTAGCCGAGATCGACGCTCTCTATGACGTCTACCTGGATGTCCAAGAGAAATGG
GGCTTGGAGGACGTCATGTTGATGGGCGACTTCAATGCGGGCTGCAGCTATGTGAGACCC
TCCCAGTGGTCATCCATCCGCCTGTGGACAAGCCCCACCTTCCAGTGGCTGATCCCCGAC
AGCGCTGACACCACAGCTACACCCACGCACTGTGCCTATGACAGGATCGTGGTTGCAGGG
ATGCTGCTCCGAGGCGCCGTTGTTCCCGACTCGGCTCTTCCCTTTAACTTCCAGGCTGCC
TATGGCCTGAGTGACCAACTGGCCCAAGCCATCAGTGACCACTATCCAGTGGAGGTGATG
CTGAAGTGA
Enzyme 39 GenBank Gene ID M55983 Link Image
Enzyme 39 GeneCard ID DNASE1 Link Image
Enzyme 39 GenAtlas ID DNASE1 Link Image
Enzyme 39 HGNC ID HGNC:2956 Link Image
Enzyme 39 Chromosome Location 1
Enzyme 39 Locus 16p13.3
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Shak S, Capon DJ, Hellmiss R, Marsters SA, Baker CL: Recombinant human DNase I reduces the viscosity of cystic fibrosis sputum. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9188-92. [PubMed Link Image]
  2. Yasuda T, Kishi K, Yanagawa Y, Yoshida A: Structure of the human deoxyribonuclease I (DNase I) gene: identification of the nucleotide substitution that generates its classical genetic polymorphism. Ann Hum Genet. 1995 Jan;59(Pt 1):1-15. [PubMed Link Image]
  3. Oliveri M, Daga A, Cantoni C, Lunardi C, Millo R, Puccetti A: DNase I mediates internucleosomal DNA degradation in human cells undergoing drug-induced apoptosis. Eur J Immunol. 2001 Mar;31(3):743-51. [PubMed Link Image]
  4. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Rosenstreich DL, Tu JH, Kinkade PR, Maurer-Fogy I, Kahn J, Barton RW, Farina PR: A human urine-derived interleukin 1 inhibitor. Homology with deoxyribonuclease I. J Exp Med. 1988 Nov 1;168(5):1767-79. [PubMed Link Image]
  7. Yasuda T, Awazu S, Sato W, Iida R, Tanaka Y, Kishi K: Human genetically polymorphic deoxyribonuclease: purification, characterization, and multiplicity of urine deoxyribonuclease I. J Biochem (Tokyo). 1990 Sep;108(3):393-8. [PubMed Link Image]
  8. Yasuda T, Nadano D, Takeshita H, Tenjo E, Kishi K: Molecular analysis of the third allele of human deoxyribonuclease I polymorphism. Ann Hum Genet. 1995 Apr;59(Pt 2):139-47. [PubMed Link Image]
  9. Yasuda T, Nadano D, Takeshita H, Tenjo E, Sawazaki K, Ootani M, Kishi K: The molecular basis for genetic polymorphism of human deoxyribonuclease I: identification of the nucleotide substitution that generates the fourth allele. FEBS Lett. 1995 Feb 13;359(2-3):211-4. [PubMed Link Image]
  10. Iida R, Yasuda T, Aoyama M, Tsubota E, Kobayashi M, Yuasa I, Matsuki T, Kishi K: The fifth allele of the human deoxyribonuclease I (DNase I) polymorphism. Electrophoresis. 1997 Oct;18(11):1936-9. [PubMed Link Image]
  11. Yasuda T, Takeshita H, Iida R, Kogure S, Kishi K: A new allele, DNASE1*6, of human deoxyribonuclease I polymorphism encodes an Arg to Cys substitution responsible for its instability. Biochem Biophys Res Commun. 1999 Jun 24;260(1):280-3. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 5740
Enzyme 40 Name Steryl-sulfatase
Enzyme 40 Synonyms
  1. Arylsulfatase C
  2. ASC
  3. Steroid sulfatase
  4. Steryl-sulfate sulfohydrolase
Enzyme 40 Gene Name STS
Enzyme 40 Protein Sequence >Steryl-sulfatase 
MPLRKMKIPFLLLFFLWEAESHAASRPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLAS
GGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTGVFLFTASSGGLPTDEITFAK
LLKDQGYSTALIGKWHLGMSCHSKTDFCHHPLHHGFNYFYGISLTNLRDCKPGEGSVFTT
GFKRLVFLPLQIVGVTLLTLAALNCLGLLHVPLGVFFSLLFLAALILTLFLGFLHYFRPL
NCFMMRNYEIIQQPMSYDNLTQRLTVEAAQFIQRNTETPFLLVLSYLHVHTALFSSKDFA
GKSQHGVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFTSDQGAHVEEVSSKGEIHGGS
NGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDRI
IDGRDLMPLLEGKSQRSDHEFLFHYCNAYLNAVRWHPQNSTSIWKAFFFTPNFNPVGSNG
CFATHVCFCFGSYVTHHDPPLLFDISKDPRERNPLTPASEPRFYEILKVMQEAADRHTQT
LPEVPDQFSWNNFLWKPWLQLCCPSTGLSCQCDREKQDKRLSR
Enzyme 40 Number of Residues 583
Enzyme 40 Molecular Weight 65491.7
Enzyme 40 Theoretical pI 7.71
Enzyme 40 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • sulfuric ester hydrolase activity
Process
  • metabolic process
Component
—
Enzyme 40 General Function Involved in catalytic activity
Enzyme 40 Specific Function Conversion of sulfated steroid precursors to estrogens during pregnancy
Enzyme 40 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 40 Reactions
  • 3beta-hydroxyandrost-5-en-17-one 3-sulfate + H2O = 3beta-hydroxyandrost-5-en-17-one + sulfate [RN:R03404]
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • 1-21
Enzyme 40 Transmembrane Regions
  • 185-208 213-234
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 338565 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID P08842 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name STS_HUMAN Link Image
Enzyme 40 PDB ID 1P49 Link Image
Enzyme 40 PDB File Show
Enzyme 40 3D Structure
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >1752 bp 
ATGCCTTTAAGGAAGATGAAGATCCCTTTCCTCCTACTGTTCTTTCTGTGGGAAGCCGAG
AGCCACGCAGCATCAAGGCCGAACATCATCCTGGTGATGGCTGACGACCTCGGCATTGGA
GATCCTGGGTGCTATGGGAACAAAACTATCAGGACTCCCAATATCGACCGGTTGGCCAGT
GGGGGAGTGAAACTCACTCAGCACCTGGCAGCATCACCGCTGTGCACACCAAGCAGGGCA
GCCTTCATGACTGGCCGGTACCCTGTCCGATCAGGAATGGCATCTTGGTCCCGCACTGGA
GTTTTCCTCTTCACAGCCTCTTCGGGAGGACTTCCCACCGATGAGATTACCTTTGCTAAG
CTTCTGAAGGATCAAGGTTATTCAACAGCACTGATAGGGAAATGGCACCTTGGGATGAGC
TGTCACAGCAAGACTGACTTCTGTCACCACCCTTTACATCACGGCTTCAATTATTTCTAT
GGGATCTCTTTGACCAATCTGAGAGACTGCAAGCCCGGAGAGGGCAGTGTCTTCACCACG
GGCTTCAAGAGGCTGGTCTTCCTCCCCCTGCAGATCGTCGGGGTCACCCTCCTTACCCTT
GCTGCACTCAATTGTCTGGGGCTACTCCACGTGCCTCTAGGCGTTTTTTTCAGCCTTCTC
TTCCTAGCAGCCCTAATCCTGACCCTTTTCTTGGGCTTCCTTCATTACTTCCGGCCCCTG
AACTGCTTCATGATGAGGAACTACGAGATCATTCAGCAGCCCATGTCCTATGACAATCTC
ACCCAGAGGCTAACGGTGGAGGCGGCCCAGTTCATACAGCGGAACACTGAGACTCCGTTC
CTGCTTGTCTTGTCCTACCTCCACGTGCACACAGCCCTGTTCTCCAGCAAAGACTTTGCT
GGCAAAAGTCAACACGGAGTCTACGGGGATGCTGTTGAGGAAATGGACTGGAGTGTGGGG
CAGATCTTGAACCTTCTGGATGAGCTGAGATTGGCTAATGATACCCTCATCTACTTCACA
TCGGACCAGGGAGCACATGTAGAGGAGGTGTCTTCCAAAGGAGAAATTCATGGCGGAAGT
AATGGGATCTATAAAGGAGGAAAAGCAAACAACTGGGAAGGAGGTATCCGGGTTCCAGGC
ATCCTTCGTTGGCCCAGGGTGATACAGGCTGGCCAGAAGATTGATGAGCCCACTAGCAAC
ATGGACATATTTCCTACAGTAGCCAAGCTGGCTGGAGCTCCCTTGCCTGAGGACAGGATC
ATTGATGGACGTGATCTGATGCCCCTGCTTGAAGGAAAAAGCCAACGCTCCGATCATGAG
TTTCTCTTCCATTACTGCAACGCCTACTTAAATGCTGTGCGCTGGCACCCTCAGAACAGC
ACATCCATCTGGAAGGCCTTTTTCTTCACCCCCAACTTCAACCCCGTGGGTTCCAACGGA
TGCTTTGCCACACACGTGTGCTTCTGTTTCGGGAGTTATGTCACCCATCACGACCCACCT
TTACTCTTTGATATTTCCAAAGATCCCAGAGAGAGAAACCCACTAACTCCAGCATCCGAG
CCCCGGTTTTATGAAATCCTCAAAGTCATGCAGGAAGCTGCGGACAGACACACCCAGACC
CTGCCAGAGGTGCCCGATCAGTTTTCATGGAACAACTTTCTTTGGAAGCCCTGGCTTCAG
CTGTGCTGTCCTTCCACCGGCCTGTCTTGCCAGTGTGATAGAGAAAAACAGGATAAGAGA
CTGAGCCGCTAG
Enzyme 40 GenBank Gene ID J04964 Link Image
Enzyme 40 GeneCard ID STS Link Image
Enzyme 40 GenAtlas ID STS Link Image
Enzyme 40 HGNC ID HGNC:11425 Link Image
Enzyme 40 Chromosome Location Not Available
Enzyme 40 Locus Not Available
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Stein C, Hille A, Seidel J, Rijnbout S, Waheed A, Schmidt B, Geuze H, von Figura K: Cloning and expression of human steroid-sulfatase. Membrane topology, glycosylation, and subcellular distribution in BHK-21 cells. J Biol Chem. 1989 Aug 15;264(23):13865-72. [PubMed Link Image]
  2. Yen PH, Allen E, Marsh B, Mohandas T, Wang N, Taggart RT, Shapiro LJ: Cloning and expression of steroid sulfatase cDNA and the frequent occurrence of deletions in STS deficiency: implications for X-Y interchange. Cell. 1987 May 22;49(4):443-54. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Yen PH, Marsh B, Allen E, Tsai SP, Ellison J, Connolly L, Neiswanger K, Shapiro LJ: The human X-linked steroid sulfatase gene and a Y-encoded pseudogene: evidence for an inversion of the Y chromosome during primate evolution. Cell. 1988 Dec 23;55(6):1123-35. [PubMed Link Image]
  6. Kawano J, Kotani T, Ohtaki S, Minamino N, Matsuo H, Oinuma T, Aikawa E: Characterization of rat and human steroid sulfatases. Biochim Biophys Acta. 1989 Aug 31;997(3):199-205. [PubMed Link Image]
  7. Hernandez-Guzman FG, Higashiyama T, Pangborn W, Osawa Y, Ghosh D: Structure of human estrone sulfatase suggests functional roles of membrane association. J Biol Chem. 2003 Jun 20;278(25):22989-97. Epub 2003 Mar 25. [PubMed Link Image]
  8. Basler E, Grompe M, Parenti G, Yates J, Ballabio A: Identification of point mutations in the steroid sulfatase gene of three patients with X-linked ichthyosis. Am J Hum Genet. 1992 Mar;50(3):483-91. [PubMed Link Image]
  9. Alperin ES, Shapiro LJ: Characterization of point mutations in patients with X-linked ichthyosis. Effects on the structure and function of the steroid sulfatase protein. J Biol Chem. 1997 Aug 15;272(33):20756-63. [PubMed Link Image]
  10. Sugawara T, Shimizu H, Hoshi N, Fujimoto Y, Nakajima A, Fujimoto S: PCR diagnosis of X-linked ichthyosis: identification of a novel mutation (E560P) of the steroid sulfatase gene. Hum Mutat. 2000 Mar;15(3):296. [PubMed Link Image]
  11. Oyama N, Satoh M, Iwatsuki K, Kaneko F: Novel point mutations in the steroid sulfatase gene in patients with X-linked ichthyosis: transfection analysis using the mutated genes. J Invest Dermatol. 2000 Jun;114(6):1195-9. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 5778
Enzyme 41 Name Cytosolic phospholipase A2 gamma
Enzyme 41 Synonyms
  1. cPLA2-gamma
  2. Phospholipase A2 group IVC
Enzyme 41 Gene Name PLA2G4C
Enzyme 41 Protein Sequence >Cytosolic phospholipase A2 gamma 
MGSSEVSIIPGLQKEEKAAVERRRLHVLKALKKLRIEADEAPVVAVLGSGGGLRAHIACL
GVLSEMKEQGLLDAVTYLAGVSGSTWAISSLYTNDGDMEALEADLKHRFTRQEWDLAKSL
QKTIQAARSENYSLTDFWAYMVISKQTRELPESHLSNMKKPVEEGTLPYPIFAAIDNDLQ
PSWQEARAPETWFEFTPHHAGFPALGAFVSITHFGSKFKKGRLVRTHPERDLTFLRGLWG
SALGNTEVIREYIFDQLRNLTLKGLWRRAVANAKSIGHLIFARLLRLQESSQGEHPPPED
EGGEPEHTWLTEMLENWTRTSLEKQEQPHEDPERKGSLSNLMDFVKKTGICASKWEWGTT
HNFLYKHGGIRDKIMSSRKHLHLVDAGLAINTPFPLVLPPTREVHLILSFDFSAGDPFET
IRATTDYCRRHKIPFPQVEEAELDLWSKAPASCYILKGETGPVVMHFPLFNIDACGGDIE
AWSDTYDTFKLADTYTLDVVVLLLALAKKNVRENKKKILRELMNVAGLYYPKDSARSCCL
A
Enzyme 41 Number of Residues 541
Enzyme 41 Molecular Weight 60948.1
Enzyme 41 Theoretical pI 6.93
Enzyme 41 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • phospholipase activity
Process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid catabolic process
  • phospholipid metabolic process
Component
—
Enzyme 41 General Function Involved in metabolic process
Enzyme 41 Specific Function Has a preference for arachidonic acid at the sn-2 position of phosphatidylcholine as compared with palmitic acid
Enzyme 41 Pathways
Enzyme 41 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 226693354 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID Q9UP65 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name PA24C_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >1626 bp 
ATGGGAAGCTCTGAAGTTTCCATAATTCCTGGGCTCCAGAAAGAAGAAAAGGCGGCCGTG
GAGAGACGAAGACTTCATGTGCTGAAAGCTCTGAAGAAGCTAAGGATTGAGGCTGATGAG
GCCCCAGTTGTTGCTGTGCTGGGCTCAGGCGGAGGACTGCGGGCTCACATTGCCTGCCTT
GGGGTCCTGAGTGAGATGAAAGAACAGGGCCTGTTGGATGCCGTCACGTACCTCGCAGGG
GTCTCTGGATCCACTTGGGCAATATCTTCTCTCTACACCAATGATGGTGACATGGAAGCT
CTCGAGGCTGACCTGAAACATCGATTTACCCGACAGGAGTGGGACTTGGCTAAGAGCCTA
CAGAAAACCATCCAAGCAGCGAGGTCTGAGAATTACTCTCTGACCGACTTCTGGGCCTAC
ATGGTTATCTCTAAGCAAACCAGAGAACTGCCGGAGTCTCATTTGTCCAATATGAAGAAG
CCCGTGGAAGAAGGGACACTACCCTACCCAATATTTGCAGCCATTGACAATGACCTGCAA
CCTTCCTGGCAGGAGGCAAGAGCACCAGAGACCTGGTTCGAGTTCACCCCTCACCACGCT
GGCTTCTCTGCACTGGGGGCCTTTGTTTCCATAACCCACTTCGGAAGCAAATTCAAGAAG
GGAAGACTGGTCAGAACTCACCCTGAGAGAGACCTGACTTTCCTGAGAGGTTTATGGGGA
AGTGCTCTTGGTAACACTGAAGTCATTAGGGAATACATTTTTGACCAGTTAAGGAATCTG
ACCCTGAAAGGTTTATGGAGAAGGGCTGTTGCTAATGCTAAAAGCATTGGACACCTTATT
TTTGCCCGATTACTGAGGCTGCAAGAAAGTTCACAAGGGGAACATCCTCCCCCAGAAGAT
GAAGGCGGTGAGCCTGAACACACCTGGCTGACTGAGATGCTCGAGAATTGGACCAGGACC
TCCCTGGAAAAGCAGGAGCAGCCCCATGAGGACCCCGAAAGGAAAGGCTCACTCAGTAAC
TTGATGGATTTTGTGAAGAAAACAGGCATTTGCGCTTCAAAGTGGGAATGGGGGACCACT
CACAACTTCCTGTACAAACACGGTGGCATCCGGGACAAGATAATGAGCAGCCGGAAGCAC
CTCCACCTGGTGGATGCTGGTTTAGCCATCAACACTCCCTTCCCACTCGTGCTGCCCCCG
ACGCGGGAGGTTCACCTCATCCTCTCCTTCGACTTCAGTGCCGGAGATCCTTTCGAGACC
ATCCGGGCTACCACTGACTACTGCCGCCGCCACAAGATCCCCTTTCCCCAAGTAGAAGAG
GCTGAGCTGGATTTGTGGTCCAAGGCCCCCGCCAGCTGCTACATCCTGAAAGGAGAAACT
GGACCAGTGGTGATGCATTTTCCCCTGTTCAACATAGATGCCTGTGGAGGTGATATTGAG
GCATGGAGTGACACATACGACACATTCAAGCTTGCTGACACCTACACTCTAGATGTGGTG
GTGCTACTCTTGGCATTAGCCAAGAAGAATGTCAGGGAAAACAAGAAGAAGATCCTTAGA
GAGTTGATGAACGTGGCCGGGCTCTACTACCCGAAGGATAGTGCCCGAAGTTGCTGCTTG
GCATAG
Enzyme 41 GenBank Gene ID NM_003706.2 Link Image
Enzyme 41 GeneCard ID PLA2G4C Link Image
Enzyme 41 GenAtlas ID PLA2G4C Link Image
Enzyme 41 HGNC ID HGNC:9037 Link Image
Enzyme 41 Chromosome Location 1
Enzyme 41 Locus 19q13.3
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Underwood KW, Song C, Kriz RW, Chang XJ, Knopf JL, Lin LL: A novel calcium-independent phospholipase A2, cPLA2-gamma, that is prenylated and contains homology to cPLA2. J Biol Chem. 1998 Aug 21;273(34):21926-32. [PubMed Link Image]
  2. Pickard RT, Strifler BA, Kramer RM, Sharp JD: Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2. J Biol Chem. 1999 Mar 26;274(13):8823-31. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  6. Jenkins CM, Han X, Yang J, Mancuso DJ, Sims HF, Muslin AJ, Gross RW: Purification of recombinant human cPLA2 gamma and identification of C-terminal farnesylation, proteolytic processing, and carboxymethylation by MALDI-TOF-TOF analysis. Biochemistry. 2003 Oct 14;42(40):11798-807. [PubMed Link Image]
  7. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 5783
Enzyme 42 Name Group 3 secretory phospholipase A2
Enzyme 42 Synonyms
  1. Group III secretory phospholipase A2
  2. GIII sPLA2
  3. sPLA2-III
  4. Phosphatidylcholine 2-acylhydrolase 3
Enzyme 42 Gene Name PLA2G3
Enzyme 42 Protein Sequence >Group 3 secretory phospholipase A2 
MGVQAGLFGMLGFLGVALGGSPALRWYRTSCHLTKAVPGNPLGYLSFLAKDAQGLALIHA
RWDAHRRLQACSWEDEPELTAAYGALCAHETAWGSFIHTPGPELQRALATLQSQWEACRA
LEESPAGARKKRAAGQSGVPGGGHQREKRGWTMPGTLWCGVGDSAGNSSELGVFQGPDLC
CREHDRCPQNISPLQYNYGIRNYRFHTISHCDCDTRFQQCLQNQHDSISDIVGVAFFNVL
EIPCFVLEEQEACVAWYWWGGCRMYGTVPLARLQPRTFYNASWSSRATSPTPSSRSPAPP
KPRQKQHLRKGPPHQKGSKRPSKANTTALQDPMVSPRLDVAPTGLQGPQGGLKPQGARWV
CRSFRRHLDQCEHQIGPREIEFQLLNSAQEPLFHCNCTRRLARFLRLHSPPEVTNMLWEL
LGTTCFKLAPPLDCVEGKNCSRDPRAIRVSARHLRRLQQRRHQLQDKGTDERQPWPSEPL
RGPMSFYNQCLQLTQAARRPDRQQKSWSQ
Enzyme 42 Number of Residues 509
Enzyme 42 Molecular Weight 57150.5
Enzyme 42 Theoretical pI 9.23
Enzyme 42 GO Classification
Function
  • carboxylesterase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phospholipase A2 activity
Process
  • lipid catabolic process
  • lipid metabolic process
  • metabolic process
  • organophosphate metabolic process
  • phospholipid metabolic process
  • primary metabolic process
Component
—
Enzyme 42 General Function Involved in phospholipase A2 activity
Enzyme 42 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Shows an 11-fold preference for phosphatidylglycerol over phosphatidylcholine (PC). Preferential cleavage:1-palmitoyl-2-linoleoyl- phosphatidylethanolamine (PE) > 1-palmitoyl-2-linoleoyl-PC > 1- palmitoyl-2-arachidonoyl-PC > 1-palmitoyl-2-arachidonoyl-PE
Enzyme 42 Pathways
Enzyme 42 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • 1-19
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 142976884 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID Q9NZ20 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name PA2G3_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >1530 bp 
ATGGGGGTTCAGGCAGGGCTGTTTGGGATGCTGGGCTTCCTGGGGGTGGCCCTGGGGGGC
TCCCCTGCCCTCCGCTGGTACAGGACCTCCTGCCACTTGACCAAGGCCGTCCCTGGCAAC
CCACTGGGGTACCTGAGCTTCCTGGCCAAGGATGCTCAGGGACTGGCCCTGATCCATGCC
CGCTGGGATGCGCATAGGAGGCTGCAGTCATGTAGCTGGGAGGATGAGCCGGAGCTCACC
GCAGCCTACGGTGCTCTCTGTGCTCATGAGACTGCCTGGGGCTCCTTCATCCACACCCCC
GGACCCGAGCTGCAGAGAGCACTGGCCACTCTTCAGAGTCAGTGGGAGGCATGCCGAGCG
CTTGAGGAGAGTCCAGCAGGGGCCAGGAAGAAGCGAGCAGCAGGGCAGAGTGGAGTCCCT
GGTGGAGGGCACCAGCGAGAGAAGAGAGGATGGACCATGCCTGGCACACTGTGGTGTGGA
GTTGGAGATTCTGCTGGGAACTCCTCGGAGCTGGGGGTCTTCCAGGGACCTGATCTCTGT
TGCCGGGAACATGACCGCTGCCCACAGAACATCTCACCCTTGCAGTACAACTATGGCATC
CGAAACTACCGATTCCACACCATCTCCCACTGTGACTGTGACACCAGGTTTCAGCAATGC
CTACAGAATCAGCACGACTCCATCTCGGACATCGTGGGCGTGGCCTTCTTCAACGTGCTG
GAGATCCCCTGCTTTGTGCTGGAGGAGCAGGAGGCGTGTGTGGCGTGGTACTGGTGGGGC
GGGTGTAGGATGTACGGCACAGTGCCCCTCGCTCGCCTGCAGCCCAGGACCTTCTACAAT
GCCTCCTGGAGCTCCCGGGCCACCTCCCCAACTCCCAGCTCCCGGAGCCCAGCCCCTCCC
AAGCCTCGACAGAAGCAGCACCTTCGGAAGGGGCCACCACATCAGAAAGGGTCCAAGCGC
CCCAGCAAAGCCAACACCACAGCCCTCCAGGACCCTATGGTCTCTCCCAGGCTTGATGTG
GCCCCCACAGGCCTCCAGGGCCCACAGGGTGGCCTAAAACCTCAGGGTGCCCGCTGGGTC
TGCCGCAGCTTCCGCCGCCACCTGGACCAGTGTGAGCACCAGATTGGGCCCCGGGAAATC
GAGTTCCAGCTGCTCAACAGCGCCCAAGAGCCCCTCTTCCACTGCAACTGCACGCGCCGT
CTGGCACGCTTCCTGAGGCTCCACAGCCCACCCGAGGTTACCAACATGCTTTGGGAGCTG
CTGGGCACAACCTGCTTCAAGCTGGCCCCTCCACTGGACTGTGTGGAAGGCAAAAACTGT
TCCAGAGACCCTAGGGCCATCAGGGTGTCAGCCCGGCACTTGCGGAGGCTTCAGCAGAGG
CGACACCAGCTCCAGGATAAAGGCACAGATGAGAGGCAGCCATGGCCTTCAGAGCCCCTG
AGAGGCCCCATGTCATTCTACAACCAGTGCCTGCAGCTAACCCAGGCAGCCAGGAGACCC
GACAGGCAGCAGAAGTCCTGGAGCCAGTGA
Enzyme 42 GenBank Gene ID NM_015715.3 Link Image
Enzyme 42 GeneCard ID PLA2G3 Link Image
Enzyme 42 GenAtlas ID PLA2G3 Link Image
Enzyme 42 HGNC ID HGNC:17934 Link Image
Enzyme 42 Chromosome Location 2
Enzyme 42 Locus 22q12.2
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Valentin E, Ghomashchi F, Gelb MH, Lazdunski M, Lambeau G: Novel human secreted phospholipase A(2) with homology to the group III bee venom enzyme. J Biol Chem. 2000 Mar 17;275(11):7492-6. [PubMed Link Image]
  2. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Murakami M, Masuda S, Shimbara S, Bezzine S, Lazdunski M, Lambeau G, Gelb MH, Matsukura S, Kokubu F, Adachi M, Kudo I: Cellular arachidonate-releasing function of novel classes of secretory phospholipase A2s (groups III and XII). J Biol Chem. 2003 Mar 21;278(12):10657-67. Epub 2003 Jan 8. [PubMed Link Image]
  5. Murakami M, Masuda S, Shimbara S, Ishikawa Y, Ishii T, Kudo I: Cellular distribution, post-translational modification, and tumorigenic potential of human group III secreted phospholipase A(2). J Biol Chem. 2005 Jul 1;280(26):24987-98. Epub 2005 Apr 29. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 5828
Enzyme 43 Name Platelet-activating factor acetylhydrolase IB subunit alpha
Enzyme 43 Synonyms
  1. Lissencephaly-1 protein
  2. LIS-1
  3. PAF acetylhydrolase 45 kDa subunit
  4. PAF-AH 45 kDa subunit
  5. PAF-AH alpha
  6. PAFAH alpha
Enzyme 43 Gene Name PAFAH1B1
Enzyme 43 Protein Sequence >Platelet-activating factor acetylhydrolase IB subunit alpha 
MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDVNEELDKKYAGLLEKKWTSVIR
LQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVF
SVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQ
GFECIRTMHGHDHNVSSVAIMPNGDHIVSASRDKTIKMWEVQTGYCVKTFTGHREWVRMV
RPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSE
TKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDK
TLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR
Enzyme 43 Number of Residues 410
Enzyme 43 Molecular Weight 46637.7
Enzyme 43 Theoretical pI 7.40
Enzyme 43 GO Classification Not Available
Enzyme 43 General Function Involved in dynactin binding
Enzyme 43 Specific Function Required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. Non-catalytic subunit of an acetylhydrolase complex which inactivates platelet- activating factor (PAF) by removing the acetyl group at the SN-2 position. Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing
Enzyme 43 Pathways Not Available
Enzyme 43 Reactions Not Available
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein Not Available
Enzyme 43 UniProtKB/Swiss-Prot ID P43034 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name LIS1_HUMAN Link Image
Enzyme 43 PDB ID 1UUJ Link Image
Enzyme 43 PDB File Show
Enzyme 43 3D Structure
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >1233 bp 
ATGGTGCTGTCCCAGAGACAACGAGATGAACTAAATCGAGCTATAGCAGATTATCTTCGT
TCAAATGGCTATGAAGAGGCATATTCAGTTTTTAAAAAGGAAGCTGAATTAGATGTGAAT
GAAGAATTAGATAAAAAGTATGCTGGTCTTTTGGAAAAAAAATGGACATCTGTTATTAGA
TTACAAAAGAAGGTTATGGAATTAGAATCAAAGCTAAATGAAGCAAAAGAAGAATTTACG
TCAGGTGGACCTCTTGGTCAGAAACGAGACCCAAAAGAATGGATTCCCCGTCCGCCAGAA
AAATATGCATTGAGTGGTCACAGGAGTCCAGTCACTCGAGTCATTTTCCATCCTGTGTTC
AGTGTTATGGTCTCTGCTTCAGAGGATGCTACAATTAAGGTGTGGGATTATGAGACTGGA
GATTTTGAACGAACTCTTAAAGGACATACAGACTCTGTACAGGACATTTCATTCGACCAC
AGCGGCAAGCTTCTGGCTTCCTGTTCTGCAGATATGACCATTAAACTATGGGATTTTCAG
GGCTTTGAATGCATCAGAACCATGCACGGCCATGACCACAATGTTTCTTCAGTAGCCATC
ATGCCCAATGGAGATCATATAGTGTCTGCCTCAAGGGATAAAACTATAAAAATGTGGGAA
GTGCAAACTGGCTACTGTGTGAAGACATTCACAGGACACAGAGAATGGGTACGTATGGTA
CGGCCAAATCAAGATGGCACTCTGATAGCCAGCTGTTCCAATGACCAGACTGTGCGTGTA
TGGGTCGTAGCAACAAAGGAATGCAAGGCTGAGCTCCGAGAGCATGAGCATGTGGTAGAA
TGCATTTCCTGGGCTCCAGAAAGCTCATATTCCTCCATCTCTGAAGCAACAGGATCTGAG
ACTAAAAAAAGTGGTAAACCTGGGCCATTCTTGCTGTCTGGATCCAGAGACAAGACTATT
AAGATGTGGGATGTCAGTACTGGCATGTGCCTTATGACCCTCGTGGGTCATGATAACTGG
GTACGTGGAGTTCTGTTCCATTCTGGGGGGAAGTTTATTTTGAGTTGTGCTGATGACAAG
ACCCTACGCGTATGGGATTACAAGAACAAGCGATGCATGAAGACCCTCAATGCGCATGAA
CACTTTGTTACCTCCTTGGATTTCCACAAGACGGCACCCTATGTCGTCACTGGCAGCGTA
GATCAAACAGTAAAAGTGTGGGAGTGCCGTTGA
Enzyme 43 GenBank Gene ID L13385 Link Image
Enzyme 43 GeneCard ID PAFAH1B1 Link Image
Enzyme 43 GenAtlas ID PAFAH1B1 Link Image
Enzyme 43 HGNC ID HGNC:8574 Link Image
Enzyme 43 Chromosome Location 1
Enzyme 43 Locus 17p13.3
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Reiner O, Carrozzo R, Shen Y, Wehnert M, Faustinella F, Dobyns WB, Caskey CT, Ledbetter DH: Isolation of a Miller-Dieker lissencephaly gene containing G protein beta-subunit-like repeats. Nature. 1993 Aug 19;364(6439):717-21. [PubMed Link Image]
  2. Lo Nigro C, Chong CS, Smith AC, Dobyns WB, Carrozzo R, Ledbetter DH: Point mutations and an intragenic deletion in LIS1, the lissencephaly causative gene in isolated lissencephaly sequence and Miller-Dieker syndrome. Hum Mol Genet. 1997 Feb;6(2):157-64. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Caspi M, Atlas R, Kantor A, Sapir T, Reiner O: Interaction between LIS1 and doublecortin, two lissencephaly gene products. Hum Mol Genet. 2000 Sep 22;9(15):2205-13. [PubMed Link Image]
  7. Feng Y, Olson EC, Stukenberg PT, Flanagan LA, Kirschner MW, Walsh CA: LIS1 regulates CNS lamination by interacting with mNudE, a central component of the centrosome. Neuron. 2000 Dec;28(3):665-79. [PubMed Link Image]
  8. Tai CY, Dujardin DL, Faulkner NE, Vallee RB: Role of dynein, dynactin, and CLIP-170 interactions in LIS1 kinetochore function. J Cell Biol. 2002 Mar 18;156(6):959-68. Epub 2002 Mar 11. [PubMed Link Image]
  9. Coquelle FM, Caspi M, Cordelieres FP, Dompierre JP, Dujardin DL, Koifman C, Martin P, Hoogenraad CC, Akhmanova A, Galjart N, De Mey JR, Reiner O: LIS1, CLIP-170's key to the dynein/dynactin pathway. Mol Cell Biol. 2002 May;22(9):3089-102. [PubMed Link Image]
  10. Yan X, Li F, Liang Y, Shen Y, Zhao X, Huang Q, Zhu X: Human Nudel and NudE as regulators of cytoplasmic dynein in poleward protein transport along the mitotic spindle. Mol Cell Biol. 2003 Feb;23(4):1239-50. [PubMed Link Image]
  11. Liang Y, Yu W, Li Y, Yang Z, Yan X, Huang Q, Zhu X: Nudel functions in membrane traffic mainly through association with Lis1 and cytoplasmic dynein. J Cell Biol. 2004 Feb 16;164(4):557-66. [PubMed Link Image]
  12. Tanaka T, Serneo FF, Higgins C, Gambello MJ, Wynshaw-Boris A, Gleeson JG: Lis1 and doublecortin function with dynein to mediate coupling of the nucleus to the centrosome in neuronal migration. J Cell Biol. 2004 Jun 7;165(5):709-21. Epub 2004 Jun 1. [PubMed Link Image]
  13. Brandon NJ, Handford EJ, Schurov I, Rain JC, Pelling M, Duran-Jimeniz B, Camargo LM, Oliver KR, Beher D, Shearman MS, Whiting PJ: Disrupted in Schizophrenia 1 and Nudel form a neurodevelopmentally regulated protein complex: implications for schizophrenia and other major neurological disorders. Mol Cell Neurosci. 2004 Jan;25(1):42-55. [PubMed Link Image]
  14. Tang LY, Deng N, Wang LS, Dai J, Wang ZL, Jiang XS, Li SJ, Li L, Sheng QH, Wu DQ, Li L, Zeng R: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction. Mol Cell Proteomics. 2007 Nov;6(11):1952-67. Epub 2007 Aug 12. [PubMed Link Image]
  15. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  16. Pilz DT, Kuc J, Matsumoto N, Bodurtha J, Bernadi B, Tassinari CA, Dobyns WB, Ledbetter DH: Subcortical band heterotopia in rare affected males can be caused by missense mutations in DCX (XLIS) or LIS1. Hum Mol Genet. 1999 Sep;8(9):1757-60. [PubMed Link Image]
  17. Leventer RJ, Cardoso C, Ledbetter DH, Dobyns WB: LIS1 missense mutations cause milder lissencephaly phenotypes including a child with normal IQ. Neurology. 2001 Aug 14;57(3):416-22. [PubMed Link Image]
  18. Sicca F, Kelemen A, Genton P, Das S, Mei D, Moro F, Dobyns WB, Guerrini R: Mosaic mutations of the LIS1 gene cause subcortical band heterotopia. Neurology. 2003 Oct 28;61(8):1042-6. [PubMed Link Image]
  19. Torres FR, Montenegro MA, Marques-De-Faria AP, Guerreiro MM, Cendes F, Lopes-Cendes I: Mutation screening in a cohort of patients with lissencephaly and subcortical band heterotopia. Neurology. 2004 Mar 9;62(5):799-802. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 5887
Enzyme 44 Name Bis(5'-adenosyl)-triphosphatase
Enzyme 44 Synonyms
  1. AP3A hydrolase
  2. AP3Aase
  3. Diadenosine 5',5'''-P1,P3-triphosphate hydrolase
  4. Dinucleosidetriphosphatase
  5. Fragile histidine triad protein
Enzyme 44 Gene Name FHIT
Enzyme 44 Protein Sequence >Bis(5'-adenosyl)-triphosphatase 
MSFRFGQHLIKPSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQ
TTQRVGTVVEKHFHGTSLTFSMQDGPEAGQTVKHVHVHVLPRKAGDFHRNDSIYEELQKH
DKEDFPASWRSEEEMAAEAAALRVYFQ
Enzyme 44 Number of Residues 147
Enzyme 44 Molecular Weight 16858.1
Enzyme 44 Theoretical pI 7.09
Enzyme 44 GO Classification
Function
  • catalytic activity
Process
—
Component
—
Enzyme 44 General Function Involved in catalytic activity
Enzyme 44 Specific Function Cleaves A-5'-PPP-5'A to yield AMP and ADP. Possible tumor suppressor for specific tissues
Enzyme 44 Pathways
Enzyme 44 Reactions
  • P1,P3-bis(5'-adenosyl) triphosphate + H2O = ADP + AMP [RN:R00187]
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 261278358 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID P49789 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name FHIT_HUMAN Link Image
Enzyme 44 PDB ID 1FHI Link Image
Enzyme 44 PDB File Show
Enzyme 44 3D Structure
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence >444 bp 
ATGTCGTTCAGATTTGGCCAACATCTCATCAAGCCCTCTGTAGTGTTTCTCAAAACAGAA
CTGTCCTTCGCTCTTGTGAATAGGAAACCTGTGGTACCAGGACATGTCCTTGTGTGCCCG
CTGCGGCCAGTGGAGCGCTTCCATGACCTGCGTCCTGATGAAGTGGCCGATTTGTTTCAG
ACGACCCAGAGAGTCGGGACAGTGGTGGAAAAACATTTCCATGGGACCTCTCTCACCTTT
TCCATGCAGGATGGCCCCGAAGCCGGACAGACTGTGAAGCACGTTCACGTCCATGTTCTT
CCCAGGAAGGCTGGAGACTTTCACAGGAATGACAGCATCTATGAGGAGCTCCAGAAACAT
GACAAGGAGGACTTTCCTGCCTCTTGGAGATCAGAGGAGGAAATGGCAGCAGAAGCCGCA
GCTCTGCGGGTCTACTTTCAGTGA
Enzyme 44 GenBank Gene ID NM_001166243.1 Link Image
Enzyme 44 GeneCard ID FHIT Link Image
Enzyme 44 GenAtlas ID FHIT Link Image
Enzyme 44 HGNC ID HGNC:3701 Link Image
Enzyme 44 Chromosome Location 3
Enzyme 44 Locus 3p14.2
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References
  1. Ohta M, Inoue H, Cotticelli MG, Kastury K, Baffa R, Palazzo J, Siprashvili Z, Mori M, McCue P, Druck T, Croce CM, Huebner K: The FHIT gene, spanning the chromosome 3p14.2 fragile site and renal carcinoma-associated t(3;8) breakpoint, is abnormal in digestive tract cancers. Cell. 1996 Feb 23;84(4):587-97. [PubMed Link Image]
  2. Druck T, Hadaczek P, Fu TB, Ohta M, Siprashvili Z, Baffa R, Negrini M, Kastury K, Veronese ML, Rosen D, Rothstein J, McCue P, Cotticelli MG, Inoue H, Croce CM, Huebner K: Structure and expression of the human FHIT gene in normal and tumor cells. Cancer Res. 1997 Feb 1;57(3):504-12. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Barnes LD, Garrison PN, Siprashvili Z, Guranowski A, Robinson AK, Ingram SW, Croce CM, Ohta M, Huebner K: Fhit, a putative tumor suppressor in humans, is a dinucleoside 5',5"'-P1,P3-triphosphate hydrolase. Biochemistry. 1996 Sep 10;35(36):11529-35. [PubMed Link Image]
  5. Huang K, Arabshahi A, Wei Y, Frey PA: The mechanism of action of the fragile histidine triad, Fhit: isolation of a covalent adenylyl enzyme and chemical rescue of H96G-Fhit. Biochemistry. 2004 Jun 15;43(23):7637-42. [PubMed Link Image]
  6. Pekarsky Y, Garrison PN, Palamarchuk A, Zanesi N, Aqeilan RI, Huebner K, Barnes LD, Croce CM: Fhit is a physiological target of the protein kinase Src. Proc Natl Acad Sci U S A. 2004 Mar 16;101(11):3775-9. Epub 2004 Mar 8. [PubMed Link Image]
  7. Lima CD, D'Amico KL, Naday I, Rosenbaum G, Westbrook EM, Hendrickson WA: MAD analysis of FHIT, a putative human tumor suppressor from the HIT protein family. Structure. 1997 Jun 15;5(6):763-74. [PubMed Link Image]
  8. Lima CD, Klein MG, Hendrickson WA: Structure-based analysis of catalysis and substrate definition in the HIT protein family. Science. 1997 Oct 10;278(5336):286-90. [PubMed Link Image]
  9. Pace HC, Garrison PN, Robinson AK, Barnes LD, Draganescu A, Rosler A, Blackburn GM, Siprashvili Z, Croce CM, Huebner K, Brenner C: Genetic, biochemical, and crystallographic characterization of Fhit-substrate complexes as the active signaling form of Fhit. Proc Natl Acad Sci U S A. 1998 May 12;95(10):5484-9. [PubMed Link Image]
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 5938
Enzyme 45 Name Protein-glutamine gamma-glutamyltransferase E
Enzyme 45 Synonyms
  1. Transglutaminase E
  2. TG(E)
  3. TGE
  4. TGase E
  5. Transglutaminase-3
  6. TGase-3
  7. Protein-glutamine gamma-glutamyltransferase E 50 kDa non-catalytic chain
  8. Protein-glutamine gamma-glutamyltransferase E 27 kDa catalytic chain
Enzyme 45 Gene Name TGM3
Enzyme 45 Protein Sequence >Protein-glutamine gamma-glutamyltransferase E 
MAALGVQSINWQTAFNRQAHHTDKFSSQELILRRGQNFQVLMIMNKGLGSNERLEFIVST
GPYPSESAMTKAVFPLSNGSSGGWSAVLQASNGNTLTISISSPASAPIGRYTMALQIFSQ
GGISSVKLGTFILLFNPWLNVDSVFMGNHAEREEYVQEDAGIIFVGSTNRIGMIGWNFGQ
FEEDILSICLSILDRSLNFRRDAATDVASRNDPKYVGRVLSAMINSNDDNGVLAGNWSGT
YTGGRDPRSWNGSVEILKNWKKSGFSPVRYGQCWVFAGTLNTALRSLGIPSRVITNFNSA
HDTDRNLSVDVYYDPMGNPLDKGSDSVWNFHVWNEGWFVRSDLGPSYGGWQVLDATPQER
SQGVFQCGPASVIGVREGDVQLNFDMPFIFAEVNADRITWLYDNTTGKQWKNSVNSHTIG
RYISTKAVGSNARMDVTDKYKYPEGSDQERQVFQKALGKLKPNTPFAATSSMGLETEEQE
PSIIGKLKVAGMLAVGKEVNLVLLLKNLSRDTKTVTVNMTAWTIIYNGTLVHEVWKDSAT
MSLDPEEEAEHPIKISYAQYEKYLKSDNMIRITAVCKVPDESEVVVERDIILDNPTLTLE
VLNEARVRKPVNVQMLFSNPLDEPVRDCVLMVEGSGLLLGNLKIDVPTLGPKEGSRVRFD
ILPSRSGTKQLLADFSCNKFPAIKAMLSIDVAE
Enzyme 45 Number of Residues 693
Enzyme 45 Molecular Weight 76631.3
Enzyme 45 Theoretical pI 5.60
Enzyme 45 GO Classification
Function
  • catalytic activity
  • protein-glutamine gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptide cross-linking
  • post-translational protein modification
  • protein modification process
Component
—
Enzyme 45 General Function Involved in protein-glutamine gamma-glutamyltransferase activity
Enzyme 45 Specific Function Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. It is responsible for the later stages of cell envelope formation in the epidermis and the hair follicle
Enzyme 45 Pathways Not Available
Enzyme 45 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3 [RN:R03983]
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 307504 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID Q08188 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name TGM3_HUMAN Link Image
Enzyme 45 PDB ID 1SGX Link Image
Enzyme 45 PDB File Show
Enzyme 45 3D Structure
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >2082 bp 
ATGGCTGCTCTAGGAGTCCAGAGTATCAACTGGCAGAAGGCCTTCAACCGACAAGCGCAT
CACACAGACAAGTTCTCCAGCCAGGAGCTCATCTTGCGGAGAGGCCAAAACTTCCAGGTC
TTAATGATCATGAACAAAGGCCTTGGCTCTAACGAAAGACTGGAGTTCATTGACACCACA
GGGCCTTACCCCTCAGAGTCGGCCATGACGAAGGCTGTGTTTCCACTCTCCAATGGCAGT
AGTGGTGGCTGGAGTGCGGTGCTTCAGGCCAGCAATGGCAATACTCTGACTATCAGCATC
TCCAGTCCTGCCAGCGCACCCATAGGACGGTACACAATGGCCCTCCAGATCTTCTCCCAG
GGCGGCATCTCCTCTGTGAAACTTGGGACGTTCATACTGCTTTTTAACCCCTGGCTGAAT
GTGGATAGCGTCTTTATGGGTAACCATGCTGAGAGAGAAGAGTATGTTCAGGAAGATGCC
GGCATCATCTTTGTGGGAAGCACAAACCGAATTGGCATGATTGGCTGGAACTTTGGACAG
TTTGAAGAAGACATTCTCAGCATCTGCCTCTCAATCTTGGATAGGAGTCTGAATTTCCGC
CGTGACGCTGCTACTGATGTGGCCAGCAGAAATGACCCCAAATACGTTGGCCGGGTGCTG
AGTGCCATGATCAATAGCAATGATGACAATGGTGTGCTTGCTGGGAATTGGAGCGGCACT
TACACCGGTGGCCGGGACCCAAGGAGCTGGGACGGCAGCGTGGAGATCCTCAAAAATTGG
AAAAAATCTGGCTTCAGCCCAGTCCGATATGGCCAGTGCTGGGTCTTTGCTGGGACCCTC
AACACAGCGCTGCGGTCTTTGGGGATTCCTTCCCGGGTGATCACCAACTTCAACTCAGCT
CATGACACAGACCGAAATCTCAGTGTGGATGTGTACTACGACCCCATGGGAAACCCCCTG
GACAAGGGTAGTGATAGCGTATGGAATTTCCATGTCTGGAATGAAGGCTGGTTTGTGAGG
TCTGACCTGGGCCCCCCGTACGGTGGATGGCAGGTGTTGGATGCTACCCCGCAGGAAAGA
AGCCAAGGGGTGTTCCAGTGCGGCCCCGCTTCGGTCATTGGTGTTCGAGAGGGTGATGTG
CAGCTGAACTTCGACATGCCCTTTATCTTCGCGGAGGTTAATGCCGACCGCATCACCTGG
CTGTACGACAACACCACTGGCAAACAGTGGAAGAATTCCGTGAACAGTCACACCATTGGC
AGGTACATCAGCACCAAGGCGGTGGGCAGCAATGCTCGCATGGACGTCACGGACAAGTAC
AAGTACCCAGAAGGCTCTGACCAGGAAAGACAAGTGTTCCAAAAGGCTTTGGGGAAACTT
AAACCCAACACGCCATTTGCCGCGACGTCTTCGATGGGTTTGGAAACAGAGGAACAGGAG
CCCAGCATCATCGGGAAGCTGAAGGTCGCTGGCATGCTGGCAGTAGGCAAAGAAGTCAAC
CTGGTCCTACTGCTCAAAAACCTGAGCAGGGATACGAAGACAGTGACAGTGAACATGACA
GCCTGGACCATCATCTACAACGGCACGCTTGTACATGAAGTGTGGAAGGACTCTGCCACA
ATGTCCCTGGACCCTGAGGAAGAGGCAGAACATCCCATAAAGATCTCGTACGCTCAGTAT
GAGAGGTACCTGAAGTCAGACAACATGATCCGGATCACAGCGGTGTGCAAGGTCCCAGAT
GAGTCTGAGGTGGTGGTGGAGCGGGACATCATCCTGGACAACCCCACCTTGACCCTGGAG
GTGCTGAACGAGGCTCGTGTGCGGAAGCCTGTGAACGTGCAGATGCTCTTCTCCAATCCA
CTGGATGAGCCGGTGAGGGACTGCGTGCTGATGGTGGAGGGAAGCGGCCTGCTGTTGGGT
AACCTGAAGATCGACGTGCCGACCCTAGGGCCCAAGGAGCGGTCCCGGGTCCGTTTTGAT
ATCCTGCCCTCCCGGAGTGGCACCAAGCAACTGCTCGCCGACTTCTCCTGCAACAAGTTC
CCTGCAATCAAGGCCATGTTGTCCATCGACGTAGCCGAATGA
Enzyme 45 GenBank Gene ID L10386 Link Image
Enzyme 45 GeneCard ID TGM3 Link Image
Enzyme 45 GenAtlas ID TGM3 Link Image
Enzyme 45 HGNC ID HGNC:11779 Link Image
Enzyme 45 Chromosome Location 2
Enzyme 45 Locus 20q11.2
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References
  1. Kim IG, Gorman JJ, Park SC, Chung SI, Steinert PM: The deduced sequence of the novel protransglutaminase E (TGase3) of human and mouse. J Biol Chem. 1993 Jun 15;268(17):12682-90. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 5940
Enzyme 46 Name Protein-glutamine gamma-glutamyltransferase 2
Enzyme 46 Synonyms
  1. Tissue transglutaminase
  2. Transglutaminase C
  3. TG(C)
  4. TGC
  5. TGase C
  6. Transglutaminase H
  7. TGase H
  8. Transglutaminase-2
  9. TGase-2
Enzyme 46 Gene Name TGM2
Enzyme 46 Protein Sequence >Protein-glutamine gamma-glutamyltransferase 2 
MAEELVLERCDLELETNGRDHHTADLCREKLVVRRGQPFWLTLHFEGRNYEASVDSLTFS
VVTGPAPSQEAGTKARFPLRDAVEEGDWTATVVDQQDCTLSLQLTTPANAPIGLYRLSLE
ASTGYQGSSFVLGHFILLFNAWCPADAVYLDSEEERQEYVLTQQGFIYQGSAKFIKNIPW
NFGQFEDGILDICLILLDVNPKFLKNAGRDCSRRSSPVYVGRVVSGMVNCNDDQGVLLGR
WDNNYGDGVSPMSWIGSVDILRRWKNHGCQRVKYGQCWVFAAVACTVLRCLGIPTRVVTN
YNSAHDQNSNLLIEYFRNEFGEIQGDKSEMIWNFHCWVESWMTRPDLQPGYEGWQALDPT
PQEKSEGTYCCGPVPVRAIKEGDLSTKYDAPFVFAEVNADVVDWIQQDDGSVHKSINRSL
IVGLKISTKSVGRDEREDITHTYKYPEGSSEEREAFTRANHLNKLAEKEETGMAMRIRVG
QSMNMGSDFDVFAHITNNTAEEYVCRLLLCARTVSYNGILGPECGTKYLLNLNLEPFSEK
SVPLCILYEKYRDCLTESNLIKVRALLVEPVINSYLLAERDLYLENPEIKIRILGEPKQK
RKLVAEVSLQNPLPVALEGCTFTVEGAGLTEEQKTVEIPDPVEAGEEVKVRMDLLPLHMG
LHKLVVNFESDKLKAVKGFRNVIIGPA
Enzyme 46 Number of Residues 687
Enzyme 46 Molecular Weight 77328.2
Enzyme 46 Theoretical pI 4.86
Enzyme 46 GO Classification
Function
  • catalytic activity
  • protein-glutamine gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptide cross-linking
  • post-translational protein modification
  • protein modification process
Component
—
Enzyme 46 General Function Involved in protein-glutamine gamma-glutamyltransferase activity
Enzyme 46 Specific Function Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3 [RN:R03983]
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 158256860 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID P21980 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name TGM2_HUMAN Link Image
Enzyme 46 PDB ID 1KV3 Link Image
Enzyme 46 PDB File Show
Enzyme 46 3D Structure
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >2064 bp 
ATGGCCGAGGAGCTGGTCTTAGAGAGGTGTGATCTGGAGCTGGAGACCAATGGCCGAGAC
CACCACACGGCCGACCTGTGCCGGGAGAAGCTGGTGGTGCGACGGGGCCAGCCCTTCTGG
CTGACCCTGCACTTTGAGGGCCGCAACTACGAGGCCAGTGTAGACAGTCTCACCTTCAGT
GTCGTGACCGGCCCAGCCCCTAGCCAGGAGGCCGGGACCAAGGCCCGTTTTCCACTAAGA
GATGCTGTGGAGGAGGGTGACTGGACAGCCACCGTGGTGGACCAGCAAGACTGCACCCTC
TCGCTGCAGCTCACCACCCCGGCCAACGCCCCCATCGGCCTGTATCGCCTCAGCCTGGAG
GCCTCCACTGGCTACCAGGGATCCAGCTTTGTGCTGGGCCACTTCATTTTGCTCTTCAAC
GCCTGGTGCCCAGCGGATGCTGTGTACCTGGACTCGGAAGAGGAGCGGCAGGAGTATGTC
CTCACCCAGCAGGGCTTTATCTACCAGGGCTCGGCCAAGTTCATCAAGAACATACCTTGG
AATTTTGGGCAGTTTGAAGATGGGATCCTAGACATCTGCCTGATCCTTCTAGATGTCAAC
CCCAAGTTCCTGAAGAACGCCGGCCGTGACTGCTCCCGCCGCAGCAGCCCCGTCTACGTG
GGCCGGGTGGTGAGTGGCATGGTCAACTGCAACGATGACCAGGGTGTGCTGCTGGGACGC
TGGGACAACAACTACGGGGACGGCGTCAGCCCCATGTCCTGGATCGGCAGCGTGGACATC
CTGCGGCGCTGGAAGAACCACGGCTGCCAGCGCGTCAAGTATGGCCAGTGCTGGGTCTTC
GCCGCCGTGGCCTGCACAGTGCTGAGGTGCCTGGGCATCCCTACCCGCGTCGTGACCAAC
TACAACTCGGCCCATGACCAGAACAGCAACCTTCTCATCGAGTACTTCCGCAATGAGTTT
GGGGAGATCCAGGGTGACAAGAGCGAGATGATCTGGAACTTCCACTGCTGGGTGGAGTCG
TGGATGACCAGGCCGGACCTGCAGCCGGGGTACGAGGGCTGGCAGGCCCTGGACCCAACG
CCCCAGGAGAAGAGCGAAGGGACGTACTGCTGTGGCCCAGTTCCAGTTCGTGCCATCAAG
GAGGGCGACCTGAGCACCAAGTACGATGCGCCCTTTGTCTTTGCGGAGGTCAATGCCGAC
GTGGTAGACTGGATCCAGCAGGACGATGGGTCTGTGCACAAATCCATCAACCGTTCCCTG
ATCGTTGGGCTGAAGATCAGCACTAAGAGCGTGGGCCGAGACGAGCGGGAGGATATCACC
CACACCTACAAATACCCAGAGGGGTCCTCAGAGGAGAGGGAGGCCTTCACAAGGGCGAAC
CACCTGAACAAACTGGCCGAGAAGGAGGAGACAGGGATGGCCATGCGGATCCGTGTGGGC
CAGAGCATGAACATGGGCAGTGACTTTGACGTCTTTGCCCACATCACCAACAACACCGCT
GAGGAGTACGTCTGCCGCCTCCTGCTCTGTGCCCGCACCGTCAGCTACAATGGGATCTTG
GGGCCCGAGTGTGGCACCAAGTACCTGCTCAACCTCAACCTGGAGCCTTTCTCTGAGAAG
AGCGTTCCTCTTTGCATCCTCTATGAGAAATACCGTGACTGCCTTACGGAGTCCAACCTC
ATCAAGGTGCGGGCCCTCCTCGTGGAGCCAGTTATCAACAGCTACCTGCTGGCTGAGAGG
GACCTCTACCTGGAGAATCCAGAAATCAAGATCCGGATCCTTGGGGAGCCCAAGCAGAAA
CGCAAGCTGGTGGCTGAGGTGTCCCTGCAGAACCCGCTCCCTGTGGCCCTGGAAGGCTGC
ACCTTCACTGTGGAGGGGGCCGGCCTGACTGAGGAGCAGAAGACGGTGGAGATCCCAGAC
CCCGTGGAGGCAGGGGAGGAAGTTAAGGTGAGAATGGACCTGCTGCCGCTCCACATGGGC
CTCCACAAGCTGGTGGTGAACTTCGAGAGCGACAAGCTGAAGGCTGTGAAGGGCTTCCGG
AATGTCATCATTGGCCCCGCCTAA
Enzyme 46 GenBank Gene ID AK291714 Link Image
Enzyme 46 GeneCard ID TGM2 Link Image
Enzyme 46 GenAtlas ID TGM2 Link Image
Enzyme 46 HGNC ID HGNC:11778 Link Image
Enzyme 46 Chromosome Location 2
Enzyme 46 Locus 20q12
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Gentile V, Saydak M, Chiocca EA, Akande O, Birckbichler PJ, Lee KN, Stein JP, Davies PJ: Isolation and characterization of cDNA clones to mouse macrophage and human endothelial cell tissue transglutaminases. J Biol Chem. 1991 Jan 5;266(1):478-83. [PubMed Link Image]
  2. Fraij BM, Birckbichler PJ, Patterson MK Jr, Lee KN, Gonzales RA: A retinoic acid-inducible mRNA from human erythroleukemia cells encodes a novel tissue transglutaminase homologue. J Biol Chem. 1992 Nov 5;267(31):22616-23. [PubMed Link Image]
  3. Fraij BM, Gonzales RA: A third human tissue transglutaminase homologue as a result of alternative gene transcripts. Biochim Biophys Acta. 1996 Apr 10;1306(1):63-74. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Deloukas P, 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]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  8. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  9. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  10. Pinkas DM, Strop P, Brunger AT, Khosla C: Transglutaminase 2 undergoes a large conformational change upon activation. PLoS Biol. 2007 Dec;5(12):e327. [PubMed Link Image]
  11. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
  12. Porzio O, Massa O, Cunsolo V, Colombo C, Malaponti M, Bertuzzi F, Hansen T, Johansen A, Pedersen O, Meschi F, Terrinoni A, Melino G, Federici M, Decarlo N, Menicagli M, Campani D, Marchetti P, Ferdaoussi M, Froguel P, Federici G, Vaxillaire M, Barbetti F: Missense mutations in the TGM2 gene encoding transglutaminase 2 are found in patients with early-onset type 2 diabetes. Mutation in brief no. 982. Online. Hum Mutat. 2007 Nov;28(11):1150. [PubMed Link Image]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 5941
Enzyme 47 Name Protein-arginine deiminase type-6
Enzyme 47 Synonyms
  1. Peptidylarginine deiminase VI
  2. Protein-arginine deiminase type VI
Enzyme 47 Gene Name PADI6
Enzyme 47 Protein Sequence >Protein-arginine deiminase type-6 
MSFQSIIHLSLDSPVHAVCVLGTEICLDLSGCAPQKCQCFTIHGSGRVLIDVANTVISEK
EDATIWWPLSDPTYATVKMTSPSPSVDADKVSVTYYGPNEDAPVGTAVLYLTGIEVSLEV
DIYRNGQVEMSSDKQAKKKWIWGPSGWGAILLVNCNPADVGQQLEDKKTKKVIFSEEITN
LSQMTLNVQGPSCILKKYRLVLHTSKEESKKARVYWPQKDNSSTFELVLGPDQHAYTLAL
LGNHLKETFYVEAIAFPSAEFSGLISYSVSLVEESQDPSIPETVLYKDTVVFRVAPCVFI
PCTQVPLEVYLCRELQLQGFVDTVTKLSEKSNSQVASVYEDPNRLGRWLQDEMAFCYTQA
PHKTTSLILDTPQAADLDEFPMKYSLSPGIGYMIQDTEDHKVASMDSIGNLMVSPPVKVQ
GKEYPLGRVLIGSSFYPSAEGRAMSKTLRDFLYAQQVQAPVELYSDWLMTGHVDEFMCFI
PTDDKNEGKKGFLLLLASPSACYKLFREKQKEGYGDALLFDELRADQLLSNGREAKTIDQ
LLADESLKKQNEYVEKCIHLNRDILKTELGLVEQDIIEIPQLFCLEKLTNIPSDQQPKRS
FARPYFPDLLRMIVMGKNLGIPKPFGPQIKGTCCLEEKICCLLEPLGFKCTFINDFDCYL
TEVGDICACANIRRVPFAFKWWKMVP
Enzyme 47 Number of Residues 686
Enzyme 47 Molecular Weight 76896.8
Enzyme 47 Theoretical pI 4.90
Enzyme 47 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • ion binding
  • metal ion binding
  • protein-arginine deiminase activity
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptidyl-amino acid modification
  • peptidyl-arginine modification
  • peptidyl-citrulline biosynthetic process from peptidyl-arginine
  • protein modification process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 47 General Function Involved in protein-arginine deiminase activity
Enzyme 47 Specific Function Catalyzes the deimination of arginine residues of proteins. May be involved in cytoskeletal reorganization in the egg and early embryo
Enzyme 47 Pathways Not Available
Enzyme 47 Reactions
  • protein L-arginine + H2O = protein L-citrulline + NH3 [RN:R02621]
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 117414158 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID Q6TGC4 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name PADI6_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence >2085 bp 
ATGGTCAGCGTGGAGGGCCGAGCCATGTCCTTCCAGAGTATCATCCACCTGTCCCTGGAC
AGCCCTGTCCATGCCGTTTGTGTGTTGGGCACAGAAATCTGCTTGGATCTCAGCGGGTGT
GCCCCCCAGAAGTGCCAGTGCTTCACCATCCATGGCTCTGGGAGGGTCTTGATCGATGTG
GCCAACACGGTGATTTCTGAGAAGGAGGACGCCACCATCTGGTGGCCCCTGTCTGATCCC
ACGTACGCCACAGTGAAGATGACATCGCCCAGCCCTTCCGTGGATGCGGATAAGGTCTCG
GTCACATACTATGGGCCCAACGAGGATGCCCCCGTGGGCACAGCTGTGCTGTACCTCACT
GGCATTGAGGTCTCTCTAGAGGTAGACATCTACCGCAATGGGCAAGTTGAGATGTCAAGT
GACAAACAGGCTAAGAAAAAATGGATCTGGGGTCCCAGCGGTTGGGGTGCCATCCTGCTT
GTGAATTGCAACCCTGCTGATGTGGGCCAGCAACTTGAGGACAAGAAAACCAAGAAAGTG
ATCTTTTCAGAGGAAATAACGAATCTGTCCCAGATGACTCTGAATGTCCAAGGCCCCAGC
TGTATCTTAAAGAAATATCGGCTAGTCCTCCATACCTCCAAGGAAGAGTCGAAGAAGGCG
AGAGTCTACTGGCCCCAAAAAGACAACTCCAGTACCTTTGAGTTGGTGCTGGGGCCCGAC
CAGCACGCCTATACCTTGGCCCTCCTCGGGAACCACTTGAAGGAGACTTTCTACGTTGAA
GCTATAGCATTCCCATCTGCCGAATTCTCAGGCCTCATCTCCTACTCTGTGTCCCTGGTG
GAGGAGTCTCAAGACCCGTCAATTCCAGAGACTGTGCTGTACAAAGACACGGTGGTGTTC
CGGGTGGCTCCCTGTGTCTTCATTCCCTGTACCCAGGTGCCTCTGGAGGTTTACCTGTGC
AGGGAGCTGCAGCTGCAGGGTTTTGTGGACACAGTGACGAAGCTGAGTGAGAAGAGCAAC
AGCCAGGTGGCATCTGTCTATGAGGACCCCAACCGCCTGGGCAGGTGGCTCCAGGATGAG
ATGGCCTTCTGCTACACCCAGGCTCCCCACAAGACAACGTCCTTGATCCTCGACACACCT
CAGGCCGCCGATCTCGATGAGTTCCCCATGAAGTACTCACTGAGCCCTGGTATTGGCTAC
ATGATCCAGGACACTGAGGACCATAAAGTGGCCAGCATGGATTCCATTGGGAACCTGATG
GTGTCCCCACCTGTCAAGGTCCAAGGGAAAGAGTACCCGCTGGGCAGAGTCCTCATTGGC
AGCAGCTTTTACCCCAGCGCAGAGGGCCGGGCCATGAGTAAGACCCTCCGAGACTTCCTC
TATGCCCAGCAGGTCCAAGCGCCGGTGGAGCTCTACTCAGATTGGCTAATGACTGGCCAC
GTGGATGAGTTCATGTGCTTCATCCCCACAGATGACAAGAATGAGGGCAAAAAGGGCTTC
CTGCTGCTCCTGGCCAGCCCCAGTGCCTGCTATAAACTGTTCCGAGAGAAACAGAAGGAA
GGCTATGGCGACGCTCTTCTGTTTGATGAGCTTAGAGCAGATCAGCTCCTGTCTAATGGA
AGGGAAGCCAAAACCATCGACCAACTTCTGGCTGATGAAAGCCTGAAGAAGCAGAATGAA
TACGTGGAGAAGTGCATTCACCTGAACCGTGACATCCTGAAGACGGAGCTGGGCCTGGTG
GAACAGGACATCATCGAGATTCCCCAGCTGTTCTGCTTGGAGAAGCTGACTAACATCCCC
TCTGACCAGCAGCCCAAGAGGTCCTTTGCGAGGCCATACTTCCCTGACCTGTTGCGGATG
ATTGTGATGGGCAAGAACCTGGGGATCCCCAAGCCTTTTGGGCCCCAAATCAAGGGGACC
TGCTGCCTGGAAGAAAAGATTTGCTGCTTGCTGGAGCCCCTGGGCTTCAAGTGCACCTTC
ATCAATGACTTTGACTGTTACCTGACAGAGGTCGGAGACATCTGTGCCTGTGCCAACATC
CGCCGGGTGCCCTTTGCCTTCAAATGGTGGAAGATGGTACCTTAG
Enzyme 47 GenBank Gene ID Not Available
Enzyme 47 GeneCard ID PADI6 Link Image
Enzyme 47 GenAtlas ID PADI6 Link Image
Enzyme 47 HGNC ID HGNC:20449 Link Image
Enzyme 47 Chromosome Location 1
Enzyme 47 Locus 1p36.13
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References
  1. Chavanas S, Mechin MC, Takahara H, Kawada A, Nachat R, Serre G, Simon M: Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6. Gene. 2004 Apr 14;330:19-27. [PubMed Link Image]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 5945
Enzyme 48 Name Coagulation factor XIII A chain
Enzyme 48 Synonyms
  1. Coagulation factor XIIIa
  2. Protein-glutamine gamma-glutamyltransferase A chain
  3. Transglutaminase A chain
Enzyme 48 Gene Name F13A1
Enzyme 48 Protein Sequence >Coagulation factor XIII A chain 
MSETSRTAFGGRRAVPPNNSNAAEDDLPTVELQGVVPRGVNLQEFLNVTSVHLFKERWDT
NKVDHHTDKYENNKLIVRRGQSFYVQIDFSRPYDPRRDLFRVEYVIGRYPQENKGTYIPV
PIVSELQSGKWGAKIVMREDRSVRLSIQSSPKCIVGKFRMYVAVWTPYGVLRTSRNPETD
TYILFNPWCEDDAVYLDNEKEREEYVLNDIGVIFYGEVNDIKTRSWSYGQFEDGILDTCL
YVMDRAQMDLSGRGNPIKVSRVGSAMVNAKDDEGVLVGSWDNIYAYGVPPSAWTGSVDIL
LEYRSSENPVRYGQCWVFAGVFNTFLRCLGIPARIVTNYFSAHDNDANLQMDIFLEEDGN
VNSKLTKDSVWNYHCWNEAWMTRPDLPVGFGGWQAVDSTPQENSDGMYRCGPASVQAIKH
GHVCFQFDAPFVFAEVNSDLIYITAKKDGTHVVENVDATHIGKLIVTKQIGGDGMMDITD
TYKFQEGQEEERLALETALMYGAKKPLNTEGVMKSRSNVDMDFEVENAVLGKDFKLSITF
RNNSHNRYTITAYLSANITFYTGVPKAEFKKETFDVTLEPLSFKKEAVLIQAGEYMGQLL
EQASLHFFVTARINETRDVLAKQKSTVLTIPEIIIKVRGTQVVGSDMTVTVQFTNPLKET
LRNVWVHLDGPGVTRPMKKMFREIRPNSTVQWEEVCRPWVSGHRKLIASMSSDSLRHVYG
ELDVQIQRRPSM
Enzyme 48 Number of Residues 732
Enzyme 48 Molecular Weight 83266.8
Enzyme 48 Theoretical pI 5.95
Enzyme 48 GO Classification
Function
  • catalytic activity
  • protein-glutamine gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptide cross-linking
  • post-translational protein modification
  • protein modification process
Component
—
Enzyme 48 General Function Involved in protein-glutamine gamma-glutamyltransferase activity
Enzyme 48 Specific Function Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl- epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin
Enzyme 48 Pathways Not Available
Enzyme 48 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3 [RN:R03983]
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 119395709 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID P00488 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name F13A_HUMAN Link Image
Enzyme 48 PDB ID 1FIE Link Image
Enzyme 48 PDB File Show
Enzyme 48 3D Structure
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence >2199 bp 
ATGTCAGAAACTTCCAGGACCGCCTTTGGAGGCAGAAGAGCAGTTCCACCCAATAACTCT
AATGCAGCGGAAGATGACCTGCCCACAGTGGAGCTTCAGGGCGTGGTGCCCCGGGGCGTC
AACCTGCAAGAGTTTCTTAATGTCACGAGCGTTCACCTGTTCAAGGAGAGATGGGACACT
AACAAGGTGGACCACCACACTGACAAGTATGAAAACAACAAGCTGATTGTCCGCAGAGGG
CAGTCTTTCTATGTGCAGATTGACTTCAGTCGTCCATATGACCCCAGAAGGGATCTCTTC
AGGGTGGAATACGTCATTGGTCGCTACCCACAGGAGAACAAGGGAACCTACATCCCAGTG
CCTATAGTCTCAGAGTTACAAAGTGGAAAGTGGGGGGCCAAGATTGTCATGAGAGAGGAC
AGGTCTGTGCGGCTGTCCATCCAGTCTTCCCCCAAATGTATTGTGGGGAAATTCCGCATG
TATGTTGCTGTCTGGACTCCCTATGGCGTACTTCGAACCAGTCGAAACCCAGAAACAGAC
ACGTACATTCTCTTCAATCCTTGGTGTGAAGATGATGCTGTGTATCTGGACAATGAGAAA
GAAAGAGAAGAGTATGTCCTGAATGACATCGGGGTAATTTTTTATGGAGAGGTCAATGAC
ATCAAGACCAGAAGCTGGAGCTATGGTCAGTTTGAAGATGGCATCCTGGACACTTGCCTG
TATGTGATGGACAGAGCACAAATGGACCTCTCTGGAAGAGGGAATCCCATCAAAGTCAGC
CGTGTGGGGTCTGCAATGGTGAATGCCAAAGATGACGAAGGTGTCCTCGTTGGATCCTGG
GACAATATCTATGCCTATGGCGTCCCCCCATCGGCCTGGACTGGAAGCGTTGACATTCTA
TTGGAATACCGGAGCTCTGAGAATCCAGTCCGGTATGGCCAATGCTGGGTTTTTGCTGGT
GTCTTTAACACATTTTTACGATGCCTTGGAATACCAGCAAGAATTGTTACCAATTATTTC
TCTGCCCATGATAATGATGCCAATTTGCAAATGGACATCTTCCTGGAAGAAGATGGGAAC
GTGAATTCCAAACTCACCAAGGATTCAGTGTGGAACTACCACTGCTGGAATGAAGCATGG
ATGACAAGGCCTGACCTTCCTGTTGGATTTGGAGGCTGGCAAGCTGTGGACAGCACCCCC
CAGGAAAATAGCGATGGCATGTATCGGTGTGGCCCCGCCTCGGTTCAAGCCATCAAGCAC
GGCCATGTCTGCTTCCAATTTGATGCACCTTTTGTTTTTGCAGAGGTCAACAGCGACCTC
ATTTACATTACAGCTAAGAAAGATGGCACTCATGTGGTGGAAAATGTGGATGCCACCCAC
ATTGGGAAATTAATTGTGACCAAACAAATTGGAGGAGATGGCATGATGGATATTACTGAT
ACTTACAAATTCCAAGAAGGTCAAGAAGAAGAGAGATTGGCCCTAGAAACTGCCCTGATG
TACGGAGCTAAAAAGCCCCTCAACACAGAAGGTGTCATGAAATCAAGGTCCAACGTTGAC
ATGGACTTTGAAGTGGAAAATGCTGTGCTGGGAAAAGACTTCAAGCTCTCCATCACCTTC
CGGAACAACAGCCACAACCGTTACACCATCACAGCTTATCTCTCAGCCAACATCACCTTC
TACACCGGGGTCCCGAAGGCAGAATTCAAGAAGGAGACGTTCGACGTGACGCTGGAGCCC
TTGTCCTTCAAGAAAGAGGCGGTGCTGATCCAAGCCGGCGAGTACATGGGTCAGCTGCTG
GAACAAGCGTCCCTGCACTTCTTTGTCACAGCTCGCATCAATGAGACCAGGGATGTTCTG
GCCAAGCAAAAGTCCACCGTGCTAACCATCCCTGAGATCATCATCAAGGTCCGTGGCACT
CAGGTAGTTGGTTCTGACATGACTGTGACAGTTGAGTTTACCAATCCTTTAAAAGAAACC
CTGCGAAATGTCTGGGTACACCTGGATGGTCCTGGAGTAACAAGACCAATGAAGAAGATG
TTCCGTGAAATCCGGCCCAACTCCACCGTGCAGTGGGAAGAAGTGTGCCGGCCCTGGGTC
TCTGGGCATCGGAAGCTGATAGCCAGCATGAGCAGTGACTCCCTGAGACATGTGTATGGC
GAGCTGGACGTGCAGATTCAAAGACGACCTTCCATGTGA
Enzyme 48 GenBank Gene ID NM_000129.3 Link Image
Enzyme 48 GeneCard ID F13A1 Link Image
Enzyme 48 GenAtlas ID F13A1 Link Image
Enzyme 48 HGNC ID HGNC:3531 Link Image
Enzyme 48 Chromosome Location 6
Enzyme 48 Locus 6p25.3-p24.3
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References
  1. Ichinose A, Hendrickson LE, Fujikawa K, Davie EW: Amino acid sequence of the a subunit of human factor XIII. Biochemistry. 1986 Nov 4;25(22):6900-6. [PubMed Link Image]
  2. Grundmann U, Amann E, Zettlmeissl G, Kupper HA: Characterization of cDNA coding for human factor XIIIa. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8024-8. [PubMed Link Image]
  3. Ichinose A, Davie EW: Characterization of the gene for the a subunit of human factor XIII (plasma transglutaminase), a blood coagulation factor. Proc Natl Acad Sci U S A. 1988 Aug;85(16):5829-33. [PubMed Link Image]
  4. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Takahashi N, Takahashi Y, Putnam FW: Primary structure of blood coagulation factor XIIIa (fibrinoligase, transglutaminase) from human placenta. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8019-23. [PubMed Link Image]
  7. Takagi T, Doolittle RF: Amino acid sequence studies on factor XIII and the peptide released during its activation by thrombin. Biochemistry. 1974 Feb 12;13(4):750-6. [PubMed Link Image]
  8. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  9. Yee VC, Pedersen LC, Le Trong I, Bishop PD, Stenkamp RE, Teller DC: Three-dimensional structure of a transglutaminase: human blood coagulation factor XIII. Proc Natl Acad Sci U S A. 1994 Jul 19;91(15):7296-300. [PubMed Link Image]
  10. Yee VC, Pedersen LC, Bishop PD, Stenkamp RE, Teller DC: Structural evidence that the activation peptide is not released upon thrombin cleavage of factor XIII. Thromb Res. 1995 Jun 1;78(5):389-97. [PubMed Link Image]
  11. Weiss MS, Metzner HJ, Hilgenfeld R: Two non-proline cis peptide bonds may be important for factor XIII function. FEBS Lett. 1998 Feb 27;423(3):291-6. [PubMed Link Image]
  12. Fox BA, Yee VC, Pedersen LC, Le Trong I, Bishop PD, Stenkamp RE, Teller DC: Identification of the calcium binding site and a novel ytterbium site in blood coagulation factor XIII by x-ray crystallography. J Biol Chem. 1999 Feb 19;274(8):4917-23. [PubMed Link Image]
  13. Suzuki K, Iwata M, Ito S, Matsui K, Uchida A, Mizoi Y: Molecular basis for subtypic differences of the "a" subunit of coagulation factor XIII with description of the genesis of the subtypes. Hum Genet. 1994 Aug;94(2):129-35. [PubMed Link Image]
  14. Board P, Coggan M, Miloszewski K: Identification of a point mutation in factor XIII A subunit deficiency. Blood. 1992 Aug 15;80(4):937-41. [PubMed Link Image]
  15. Kangsadalampai S, Board PG: The Val34Leu polymorphism in the A subunit of coagulation factor XIII contributes to the large normal range in activity and demonstrates that the activation peptide plays a role in catalytic activity. Blood. 1998 Oct 15;92(8):2766-70. [PubMed Link Image]
  16. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 5946
Enzyme 49 Name Protein-arginine deiminase type-4
Enzyme 49 Synonyms
  1. HL-60 PAD
  2. Peptidylarginine deiminase IV
  3. Protein-arginine deiminase type IV
Enzyme 49 Gene Name PADI4
Enzyme 49 Protein Sequence >Protein-arginine deiminase type-4 
MAQGTLIRVTPEQPTHAVCVLGTLTQLDICSSAPEDCTSFSINASPGVVVDIAHGPPAKK
KSTGSSTWPLDPGVEVTLTMKVASGSTGDQKVQISYYGPKTPPVKALLYLTGVEISLCAD
ITRTGKVKPTRAVKDQRTWTWGPCGQGAILLVNCDRDNLESSAMDCEDDEVLDSEDLQDM
SLMTLSTKTPKDFFTNHTLVLHVARSEMDKVRVFQATRGKLSSKCSVVLGPKWPSHYLMV
PGGKHNMDFYVEALAFPDTDFPGLITLTISLLDTSNLELPEAVVFQDSVVFRVAPWIMTP
NTQPPQEVYACSIFENEDFLKSVTTLAMKAKCKLTICPEEENMDDQWMQDEMEIGYIQAP
HKTLPVVFDSPRNRGLKEFPIKRVMGPDFGYVTRGPQTGGISGLDSFGNLEVSPPVTVRG
KEYPLGRILFGDSCYPSNDSRQMHQALQDFLSAQQVQAPVKLYSDWLSVGHVDEFLSFVP
APDRKGFRLLLASPRSCYKLFQEQQNEGHGEALLFEGIKKKKQQKIKNILSNKTLREHNS
FVERCIDWNRELLKRELGLAESDIIDIPQLFKLKEFSKAEAFFPNMVNMLVLGKHLGIPK
PFGPVINGRCCLEEKVCSLLEPLGLQCTFINDFFTYHIRHGEVHCGTNVRRKPFSFKWWN
MVP
Enzyme 49 Number of Residues 663
Enzyme 49 Molecular Weight 74078.6
Enzyme 49 Theoretical pI 6.56
Enzyme 49 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • ion binding
  • metal ion binding
  • protein-arginine deiminase activity
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptidyl-amino acid modification
  • peptidyl-arginine modification
  • peptidyl-citrulline biosynthetic process from peptidyl-arginine
  • protein modification process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 49 General Function Involved in protein-arginine deiminase activity
Enzyme 49 Specific Function Catalyzes the citrullination/deimination of arginine residues of proteins. Citrullinates histone H3 at 'Arg-8' and/or 'Arg-17' and histone H4 at 'Arg-3', which prevents their methylation by CARM1 and HRMT1L2/PRMT1 and represses transcription. Citrullinates EP300/P300 at 'Arg-2142', which favors its interaction with NCOA2/GRIP1
Enzyme 49 Pathways Not Available
Enzyme 49 Reactions
  • protein L-arginine + H2O = protein L-citrulline + NH3 [RN:R02621]
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • None
Enzyme 49 Transmembrane Regions
  • None
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 5913971 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID Q9UM07 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name PADI4_HUMAN Link Image
Enzyme 49 PDB ID 1WD8 Link Image
Enzyme 49 PDB File Show
Enzyme 49 3D Structure
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >1992 bp 
ATGGCCCAGGGGACATTGATCCGTGTGACCCCAGAGCAGCCCACCCATGCCGTGTGTGTG
CTGGGCACCTTGACTCAGCTTGACATCTGCAGCTCTGCCCCTGAGGACTGCACGTCCTTC
AGCATCAACGCCTCCCCAGGGGTGGTCGTGGATATTGCCCACAGCCCTCCAGCCAAGAAG
AAATCCACAGGTTCCTCCACATGGCCCCTGGACCCTGGGGTAGAGGTGACCCTGACGATG
AAAGCGGCCAGTGGTAGCACAGGCGACCAGAAGGTTCAGATTTCATACTACGGACCCAAG
ACTCCACCAGTCAAAGCTCTACTCTACCTCACCGCGGTGGAAATCTCCCTGTGCGCAGAC
ATCACCCGCACCGGCAAAGTGAAGCCAACCAGAGCTGTGAAAGATCAGAGGACCTGGACC
TGGGGCCCTTGTGGACAGGGTGCCATCCTGCTGGTGAACTGTGACAGAGACAATCTCGAA
TCTTCTGCCATGGACTGCGAGGATGATGAAGTGCTTGACAGCGAAGACCTGCAGGACATG
TCGCTGATGACCCTGAGCACGAAGACCCCCAAGGACTTCTTCACAAACCATACACTGGTG
CTCCACGTGGCCAGGTCTGAGATGGACAAAGTGAGGGTGTTTCAGGCCACACGGGGCAAA
CTGTCCTCCAAGTGCAGCGTAGTCTTGGGTCCCAAGTGGCCCTCTCACTACCTGATGGTC
CCCGGTGGAAAGCACAACATGGACTTCTACGTGGAGGCCCTCGCTTTCCCGGACACCGAC
TTCCCGGGGCTCATTACCCTCACCATCTCCCTGCTGGACACGTCCAACCTGGAGCTCCCC
GAGGCTGTGGTGTTCCAAGACAGCGTGGTCTTCCGCGTGGCGCCCTGGATCATGACCCCC
AACACCCAGCCCCCGCAGGAGGTGTACGCGTGCAGTATTTTTGAAAATGAGGACTTCCTG
AAGTCAGTGACTACTCTGGCCATGAAAGCCAAGTGCAAGCTGACCATCTGCCCTGAGGAG
GAGAACATGGATGACCAGTGGATGCAGGATGAAATGGAGATCGGCTACATCCAAGCCCCA
CACAAAACGCTGCCCGTGGTCTTCGACTCTCCAAGGAACAGAGGCCTGAAGGAGTTTCCC
ATCAAACGAGTGATGGGTCCAGATTTTGGCTATGTAACTCGAGGGCCCCAAACAGGGGGT
ATCAGTGGACTGGACTCCTTTGGGAACCTGGAAGTGAGCCCCCCAGTCACAGTCAGGGGC
AAGGAATACCCGCTGGGCAGGATTCTCTTCGGGGACAGCTGTTATCCCAGCAATGACAGC
CGGCAGATGCACCAGGCCCTGCAGGACTTCCTCAGTGCCCAGCAGGTGCAGGCCCCTGTG
AAGCTCTATTCTGACTGGCTGTCCGTGGGCCACGTGGACGAGTTCCTGAGCTTTGTGCCA
GCACCCGACAGGAAGGGCTTCCGGCTGCTCCTGGCCAGCCCCAGGTCCTGCTACAAACTG
TTCCAGGAGCAGCAGAATGAGGGCCACGGGGAGGCCCTGCTGTTCGAAGGGATCAAGAAA
AAAAAACAGCAGAAAATAAAGAACATTCTGTCAAACAAGACATTGAGAGAACATAATTCA
TTTGTGGAGAGATGCATCGACTGGAACCGCGAGCTGCTGAAGCGGGAGCTGGGCCTGGCC
GAGAGTGACATCATTGACATCCCGCAGCTCTTCAAGCTCAAAGAGTTCTCTAAGGCGGAA
GCTTTTTTCCCCAACATGGTGAACATGCTGGTGCTAGGGAAGCACCTGGGCATCCCCAAG
CCCTTCGGGCCCGTCATCAACGGCCGCTGCTGCCTGGAGGAGAAGGTGTGTTCCCTGCTG
GAGCCACTGGGCCTCCAGTGCACCTTCATCAACGACTTCTTCACCTACCACATCAGGCAT
GGGGAGGTGCACTGCGGCACCAACGTGCGCAGAAAGCCCTTCTCCTTCAAGTGGTGGAAC
ATGGTGCCCTGA
Enzyme 49 GenBank Gene ID AB017919 Link Image
Enzyme 49 GeneCard ID PADI4 Link Image
Enzyme 49 GenAtlas ID PADI4 Link Image
Enzyme 49 HGNC ID HGNC:18368 Link Image
Enzyme 49 Chromosome Location 1
Enzyme 49 Locus 1p36.13
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References
  1. Nakashima K, Hagiwara T, Ishigami A, Nagata S, Asaga H, Kuramoto M, Senshu T, Yamada M: Molecular characterization of peptidylarginine deiminase in HL-60 cells induced by retinoic acid and 1alpha,25-dihydroxyvitamin D(3). J Biol Chem. 1999 Sep 24;274(39):27786-92. [PubMed Link Image]
  2. Chavanas S, Mechin MC, Takahara H, Kawada A, Nachat R, Serre G, Simon M: Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6. Gene. 2004 Apr 14;330:19-27. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Asaga H, Nakashima K, Senshu T, Ishigami A, Yamada M: Immunocytochemical localization of peptidylarginine deiminase in human eosinophils and neutrophils. J Leukoc Biol. 2001 Jul;70(1):46-51. [PubMed Link Image]
  6. Suzuki A, Yamada R, Chang X, Tokuhiro S, Sawada T, Suzuki M, Nagasaki M, Nakayama-Hamada M, Kawaida R, Ono M, Ohtsuki M, Furukawa H, Yoshino S, Yukioka M, Tohma S, Matsubara T, Wakitani S, Teshima R, Nishioka Y, Sekine A, Iida A, Takahashi A, Tsunoda T, Nakamura Y, Yamamoto K: Functional haplotypes of PADI4, encoding citrullinating enzyme peptidylarginine deiminase 4, are associated with rheumatoid arthritis. Nat Genet. 2003 Aug;34(4):395-402. [PubMed Link Image]
  7. Cuthbert GL, Daujat S, Snowden AW, Erdjument-Bromage H, Hagiwara T, Yamada M, Schneider R, Gregory PD, Tempst P, Bannister AJ, Kouzarides T: Histone deimination antagonizes arginine methylation. Cell. 2004 Sep 3;118(5):545-53. [PubMed Link Image]
  8. Wang Y, Wysocka J, Sayegh J, Lee YH, Perlin JR, Leonelli L, Sonbuchner LS, McDonald CH, Cook RG, Dou Y, Roeder RG, Clarke S, Stallcup MR, Allis CD, Coonrod SA: Human PAD4 regulates histone arginine methylation levels via demethylimination. Science. 2004 Oct 8;306(5694):279-83. Epub 2004 Sep 2. [PubMed Link Image]
  9. Nakayama-Hamada M, Suzuki A, Kubota K, Takazawa T, Ohsaka M, Kawaida R, Ono M, Kasuya A, Furukawa H, Yamada R, Yamamoto K: Comparison of enzymatic properties between hPADI2 and hPADI4. Biochem Biophys Res Commun. 2005 Feb 4;327(1):192-200. [PubMed Link Image]
  10. Lee YH, Coonrod SA, Kraus WL, Jelinek MA, Stallcup MR: Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination. Proc Natl Acad Sci U S A. 2005 Mar 8;102(10):3611-6. Epub 2005 Feb 24. [PubMed Link Image]
  11. Arita K, Hashimoto H, Shimizu T, Nakashima K, Yamada M, Sato M: Structural basis for Ca(2+)-induced activation of human PAD4. Nat Struct Mol Biol. 2004 Aug;11(8):777-83. Epub 2004 Jul 11. [PubMed Link Image]
  12. Hoppe B, Heymann GA, Tolou F, Kiesewetter H, Doerner T, Salama A: High variability of peptidylarginine deiminase 4 (PADI4) in a healthy white population: characterization of six new variants of PADI4 exons 2-4 by a novel haplotype-specific sequencing-based approach. J Mol Med. 2004 Nov;82(11):762-7. Epub 2004 Aug 25. [PubMed Link Image]
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 5950
Enzyme 50 Name Protein-arginine deiminase type-3
Enzyme 50 Synonyms
  1. Peptidylarginine deiminase III
  2. Protein-arginine deiminase type III
Enzyme 50 Gene Name PADI3
Enzyme 50 Protein Sequence >Protein-arginine deiminase type-3 
MSLQRIVRVSLEHPTSAVCVAGVETLVDIYGSVPEGTEMFEVYGTPGVDIYISPNMERGR
ERADTRRWRFDATLEIIVVMNSPSNDLNDSHVQISYHSSHEPLPLAYAVLYLTCVDISLD
CDLNCEGRQDRNFVDKRQWVWGPSGYGGILLVNCDRDDPSCDVQDNCDQHVHCLQDLEDM
SVMVLRTQGPAALFDDHKLVLHTSSYDAKRAQVFHICGPEDVCEAYRHVLGQDKVSYEVP
RLHGDEERFFVEGLSFPDAGFTGLISFHVTLLDDSNEDFSASPIFTDTVVFRVAPWIMTP
STLPPLEVYVCRVRNNTCFVDAVAELARKAGCKLTICPQAENRNDRWIQDEMELGYVQAP
HKTLPVVFDSPRNGELQDFPYKRILGPDFGYVTREPRDRSVSGLDSFGNLEVSPPVVANG
KEYPLGRILIGGNLPGSSGRRVTQVVRDFLHAQKVQPPVELFVDWLAVGHVDEFLSFVPA
PDGKGFRMLLASPGACFKLFQEKQKCGHGRALLFQGVVDDEQVKTISINQVLSNKDLINY
NKFVQSCIDWNREVLKRELGLAECDIIDIPQLFKTERKKATAFFPDLVNMLVLGKHLGIP
KPFGPIINGCCCLEEKVRSLLEPLGLHCTFIDDFTPYHMLHGEVHCGTNVCRKPFSFKWW
NMVP
Enzyme 50 Number of Residues 664
Enzyme 50 Molecular Weight 74742.7
Enzyme 50 Theoretical pI 5.22
Enzyme 50 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • ion binding
  • metal ion binding
  • protein-arginine deiminase activity
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptidyl-amino acid modification
  • peptidyl-arginine modification
  • peptidyl-citrulline biosynthetic process from peptidyl-arginine
  • protein modification process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 50 General Function Involved in protein-arginine deiminase activity
Enzyme 50 Specific Function Catalyzes the deimination of arginine residues of proteins
Enzyme 50 Pathways Not Available
Enzyme 50 Reactions
  • protein L-arginine + H2O = protein L-citrulline + NH3 [RN:R02621]
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • None
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 6172379 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID Q9ULW8 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name PADI3_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence >1995 bp 
ATGTCGCTGCAGAGAATCGTGCGTGTGTCCCTGGAGCATCCCACCAGCGCGGTGTGTGTG
GCTGGCGTGGAGACCCTCGTGGACATTTATGGGTCAGTGCCTGAGGGCACAGAAATGTTT
GAGGTCTATGGGACGCCTGGCGTGGACATCTACATCTCTCCCAACATGGAGAGGGGCCGG
GAGCGTGCAGACACCAGGCGGTGGCGCTTTGACGCGACTTTGGAGATCATCGTGGTCATG
AACTCCCCCAGCAATGACCTCAACGACAGCCATGTTCAGATTTCCTACCACTCCAGCCAT
GAGCCTCTGCCCCTAGCCTATGCGGTGCTCTACCTCACCTGTGTTGACATCTCTCTGGAT
TGCGACCTGAACTGTGAGGGAAGGCAGGACAGGAACTTTGTAGACAAGCGGCAGTGGGTC
TGGGGGCCCAGTGGGTATGGCGGCATCTTGCTGGTGAACTGTGACCGTGATGATCCGAGC
TGTGATGTCCAGGACAATTGTGACCAGCACGTGCACTGCCTGCAAGACCTGGAAGACATG
TCTGTCATGGTCCTGCGGACGCAGGGCCCTGCAGCCCTCTTTGATGACCACAAACTTGTC
CTCCATACCTCCAGCTATGATGCCAAACGGGCACAGGTCTTCCACATCTGCGGTCCTGAG
GATGTGTGTGAGGCCTATAGGCATGTGCTGGGCCAAGATAAGGTGTCCTATGAGGTACCC
CGCTTGCATGGGGATGAGGAGCGCTTCTTCGTGGAAGGCCTGTCCTTCCCTGATGCCGGC
TTCACAGGACTCATCTCCTTCCATGTCACTCTGCTGGACGACTCCAACGAGGATTTCTCG
GCATCCCCTATCTTCACTGACACTGTGGTGTTCCGAGTGGCACCCTGGATCATGACGCCC
AGCACTCTGCCACCCCTAGAGGTGTATGTGTGCCGTGTGAGGAACAACACGTGTTTTGTG
GATGCGGTGGCAGAGCTGGCCAGGAAGGCCGGCTGCAAGCTGACCATCTGCCCACAGGCC
GAGAACCGCAACGACCGCTGGATCCAGGATGAGATGGAGCTGGGCTACGTTCAGGCGCCG
CACAAGACCCTCCCGGTGGTCTTTGACTCCCCAAGGAATGGGGAACTGCAGGATTTCCCT
TACAAAAGAATCCTGGGTCCAGATTTTGGTTACGTGACTCGGGAACCACGCGACAGGTCT
GTGAGTGGCCTGGACTCCTTTGGGAACCTGGAGGTCAGCCCTCCAGTGGTGGCCAATGGG
AAAGAGTACCCCCTGGGGAGGATCCTCATTGGGGGCAACCTGCCTGGGTCAAGTGGCCGC
AGGGTCACCCAGGTGGTGCGGGACTTCCTCCATGCCCAGAAGGTGCAGCCCCCCGTGGAG
CTCTTTGTGGACTGGTTGGCCGTGGGCCATGTGGATGAGTTTCTGAGCTTTGTCCCTGTC
CCCGATGGGAAGGGCTTCCGGATGCTCCTGGCCAGCCCTGGGGCCTGCTTCAAGCTCTTC
CAGGAAAAGCAGAAGTGTGGCCACGGGAGGGCCCTCCTGTTCCAGGGGGTTGTTGATGAT
GAGCAGGTCAAGACCATCTCCATCAACCAGGTGCTCTCCAATAAAGACCTCATCAACTAC
AATAAGTTTGTGCAGAGCTGCATCGACTGGAACCGTGAGGTGCTGAAGCGGGAGCTGGGC
CTGGCAGAGTGTGACATCATTGACATCCCACAGCTCTTCAAGACCGAGAGGAAAAAAGCA
ACGGCCTTCTTCCCTGACTTGGTGAACATGCTGGTGCTGGGGAAGCACCTGGGCATCCCC
AAGCCCTTTGGGCCCATCATCAATGGCTGCTGCTGCCTGGAGGAGAAGGTGCGGTCCCTG
CTGGAGCCTCTGGGCCTCCACTGCACCTTCATTGATGACTTCACTCCATACCACATGCTG
CATGGGGAGGTGCACTGTGGCACCAATGTGTGCAGAAAGCCCTTCTCTTTCAAGTGGTGG
AACATGGTGCCCTGA
Enzyme 50 GenBank Gene ID AB026831 Link Image
Enzyme 50 GeneCard ID PADI3 Link Image
Enzyme 50 GenAtlas ID PADI3 Link Image
Enzyme 50 HGNC ID HGNC:18337 Link Image
Enzyme 50 Chromosome Location 1
Enzyme 50 Locus 1p36.13
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 General References
  1. Kanno T, Kawada A, Yamanouchi J, Yosida-Noro C, Yoshiki A, Shiraiwa M, Kusakabe M, Manabe M, Tezuka T, Takahara H: Human peptidylarginine deiminase type III: molecular cloning and nucleotide sequence of the cDNA, properties of the recombinant enzyme, and immunohistochemical localization in human skin. J Invest Dermatol. 2000 Nov;115(5):813-23. [PubMed Link Image]
  2. Chavanas S, Mechin MC, Takahara H, Kawada A, Nachat R, Serre G, Simon M: Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6. Gene. 2004 Apr 14;330:19-27. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 5952
Enzyme 51 Name Protein-glutamine gamma-glutamyltransferase 5
Enzyme 51 Synonyms
  1. Transglutaminase X
  2. TG(X)
  3. TGX
  4. TGase X
  5. Transglutaminase-5
  6. TGase-5
Enzyme 51 Gene Name TGM5
Enzyme 51 Protein Sequence >Protein-glutamine gamma-glutamyltransferase 5 
MAQGLEVALTDLQSSRNNVRHHTEEITVDHLLVRRGQAFNLTLYFRNRSFQPGLDNIIFV
VETGPLPDLALGTRAVFSLARHHSPSPWIAWLETNGATSTEVSLCAPPTAAVGRYLLKIH
IDSFQGSVTAYQLGEFILLFNPWCPEDAVYLDSEPQRQEYVMNDYGFIYQGSKNWIRPCP
WNYGQFEDKIIDICLKLLDKSLHFQTDPATDCALRGSPVYVSRVVCAMINSNDDNGVLNG
NWSENYTDGANPAEWTGSVAILKQWNATGCQPVRYGQCWVFAAVMCTVMRCLGIPTRVIT
NFDSGHDTDGNLIIDEYYDNTGRILGNKKKDTIWNFHVWNECWMARKDLPPAYGGWQVLD
ATPQEMSNGVYCCGPASVRAIKEGEVDLNYDTPFVFSMVNADCMSWLVQGGKEQKLHQDT
SSVGNFISTKSIQSDERDDITENYKYEEGSLQERQVFLKALQKLKARSFHGSQRGAELQP
SRPTSLSQDSPRSLHTPSLRPSDVVQVSLKFKLLDPPNMGQDICFVLLALNMSSQFKDLK
VNLSAQSLLHDGSPLSPFWQDTAFITLSPKEAKTYPCKISYSQYSQYLSTDKLIRISALG
EEKSSPEKILVNKIITLSYPSITINVLGAAVVNQPLSIQVIFSNPLSEQVEDCVLTVEGS
GLFKKQQKVFLGVLKPQHQASIILETVPFKSGQRQIQANMRSNKFKDIKGYRNVYVDFAL
Enzyme 51 Number of Residues 720
Enzyme 51 Molecular Weight 80777.1
Enzyme 51 Theoretical pI 6.39
Enzyme 51 GO Classification
Function
  • catalytic activity
  • protein-glutamine gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptide cross-linking
  • post-translational protein modification
  • protein modification process
Component
—
Enzyme 51 General Function Involved in protein-glutamine gamma-glutamyltransferase activity
Enzyme 51 Specific Function Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Contributes to the formation of the cornified cell envelope of keratinocytes
Enzyme 51 Pathways Not Available
Enzyme 51 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3 [RN:R03983]
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • None
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 2895530 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID O43548 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name TGM5_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence >2163 bp 
ATGGCCCAAGGGCTAGAAGTGGCCCTCACAGACCTCCAGAGCTCCAGAAATAATGTGCGG
CACCACACGGAGGAGATCACTGTGGACCACCTGCTTGTTCGCCGGGGCCAGGCCTTCAAC
CTCACCCTGTACTTCAGGAACCGGAGCTTCCAGCCAGGCCTGGACAACATCATCTTCGTG
GTTGAAACTGGACCGCTGTCAGACCTGGCCTTGGGGACTCGGGCTGTGTTCAGCCTGGCA
CGCCATCACAGCCCCAGCCCCTGGATTGCCTGGCTGGAGACCAATGGGGCCACCTCCACA
GAGGTGAGCTTGTGCGCTCCTCCCACGGCGGCCGTGGGTCGGTACCTCTTGAAAATCCAC
ATCGACTCCTTCCAGGGGTCTGTGACGGCCTACCAGCTAGGGGAGTTCATCCTGCTTTTC
AATCCCTGGTGCCCAGAGGATGCTGTCTACTTGGACAGTGAACCCCAGAGGCAGGAGTAT
GTCATGAATGATTATGGCTTCATCTACCAAGGCAGCAAGAACTGGATCCGCCCATGTCCC
TGGAACTATGGACAGTTTGAAGACAAAATCATAGACATCTGCCTGAAGCTGCTAGACAAG
AGCCTGCACTTCCAGACTGACCCAGCCACAGACTGTGCTCTGCGGGGAAGCCCCGTCTAC
GTCAGCAGAGTGGTGTGTGCCATGATCAACAGCAATGATGATAATGGGGTGCTCAATGGA
AACTGGAGTGAGAATTACACAGACGGCGCCAACCCTGCGGAGTGGACGGGCAGCGTGGCC
ATCCTGAAGCAGTGGAACGCCACAGGCTGCCAGCCCGTGCGCTACGGGCAATGCTGGGTC
TTTGCTGCCGTCATGTGCACAGTGATGAGGTGTCTGGGGATCCCTACCCGTGTGATCACC
AACTTCGACTCTGGCCACGATACAGATGGAAACCTGATCATAGATGAGTATTATGACAAC
ACAGGCAGGATTTTGGGGAATAAGAAGAAGGATACTATCTGGAACTTCCATGTCTGGAAT
GAGTGCTGGATGGCCCGGAAGGATCTGCCCCCTGCATATGGAGGCTGGCAGGTGCTGGAC
GCCACACCTCAGGAGATGAGCAACGGCGTCTACTGCTGTGGCCCTGCCTCTGTCAGAGCC
ATCAAAGAAGGAGAAGTGGACCTGAACTATGACACGCCCTTTGTGTTTTCGATGGTGAAT
GCTGACTGCATGTCCTGGCTCGTCCAGGGAGGGAAGGAGCAGAAGCTTCACCAGGACACG
AGTTCTGTTGGCAATTTTATCAGCACAAAGAGCATCCAGAGTGACGAGCGGGATGACATC
ACAGAGAACTACAAGTATGAAGAAGGATCCCTCCAGGAGAGGCAGGTGTTTCTGAAGGCT
CTGCAGAAGCTGAAGGCTAGAAGCTTCCATGGCTCCCAAAGAGGAGCAGAGTTGCAACCT
TCCAGGCCCACATCACTGAGCCAGGACAGCCCTCGGAGCCTGCATACACCTTCCCTTCGA
CCCAGTGATGTGGTGCAAGTCTCCCTGAAATTCAAGCTGCTCGACCCGCCCAACATGGGC
CAGGATATATGCTTTGTCCTGCTGGCCCTCAACATGTCCTCCCAGTTCAAGGACCTCAAA
GTGAACCTGAGTGCCCAGTCTCTGCTGCACGATGGCAGCCCCCTGTCCCCATTCTGGCAG
GACACAGCGTTCATCACACTCTCTCCTAAAGAAGCAAAGACCTACCCCTGCAAAATCTCC
TATTCCCAGTACAGCCAGTACCTGTCAACAGACAAGCTGATCCGCATCAGTGCCCTGGGT
GAAGAGAAAAGCAGTCCTGAGAAAATCCTGGTGAACAAGATCATCACCTTATCTTATCCA
AGCATCACGATTAATGTTCTAGGAGCAGCCGTTGTGAACCAGCCACTCTCCATACAGGTG
ATATTTTCAAACCCCCTCTCGGAGCAGGTTGAGGACTGTGTGCTGACTGTGGAAGGAAGT
GGCCTCTTCAAGAAACAGCAGAAAGTCTTCCTTGGAGTCCTCAAACCCCAACACCAAGCA
AGCATCATTCTGGAGACCGTCCCCTTCAAGAGTGGACAAAGGCAGATCCAAGCTAATATG
AGAAGCAACAAGTTTAAGGACATTAAGGGTTACAGGAATGTTTATGTAGACTTTGCATTA
TAA
Enzyme 51 GenBank Gene ID AF035960 Link Image
Enzyme 51 GeneCard ID TGM5 Link Image
Enzyme 51 GenAtlas ID TGM5 Link Image
Enzyme 51 HGNC ID HGNC:11781 Link Image
Enzyme 51 Chromosome Location 1
Enzyme 51 Locus 15q15.2
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 General References
  1. Aeschlimann D, Koeller MK, Allen-Hoffmann BL, Mosher DF: Isolation of a cDNA encoding a novel member of the transglutaminase gene family from human keratinocytes. Detection and identification of transglutaminase gene products based on reverse transcription-polymerase chain reaction with degenerate primers. J Biol Chem. 1998 Feb 6;273(6):3452-60. [PubMed Link Image]
  2. Grenard P, Bates MK, Aeschlimann D: Evolution of transglutaminase genes: identification of a transglutaminase gene cluster on human chromosome 15q15. Structure of the gene encoding transglutaminase X and a novel gene family member, transglutaminase Z. J Biol Chem. 2001 Aug 31;276(35):33066-78. Epub 2001 Jun 4. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Rufini A, Vilbois F, Paradisi A, Oddi S, Tartaglione R, Leta A, Bagetta G, Guerrieri P, Finazzi-Agro' A, Melino G, Candi E: Transglutaminase 5 is acetylated at the N-terminal end. Amino Acids. 2004 Jul;26(4):425-30. Epub 2004 Jun 17. [PubMed Link Image]
  5. Cassidy AJ, van Steensel MA, Steijlen PM, van Geel M, van der Velden J, Morley SM, Terrinoni A, Melino G, Candi E, McLean WH: A homozygous missense mutation in TGM5 abolishes epidermal transglutaminase 5 activity and causes acral peeling skin syndrome. Am J Hum Genet. 2005 Dec;77(6):909-17. Epub 2005 Oct 11. [PubMed Link Image]
Enzyme 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 5954
Enzyme 52 Name Protein-glutamine gamma-glutamyltransferase 4
Enzyme 52 Synonyms
  1. Fibrinoligase
  2. Prostate transglutaminase
  3. Prostate-specific transglutaminase
  4. Transglutaminase P
  5. TG(P)
  6. TGP
  7. TGase P
  8. Transglutaminase-4
  9. TGase-4
Enzyme 52 Gene Name TGM4
Enzyme 52 Protein Sequence >Protein-glutamine gamma-glutamyltransferase 4 
MMDASKELQVLHIDFLNQDNAVSHHTWEFQTSSPVFRRGQVFHLRLVLNQPLQSYHQLKL
EFSTGPNPSIAKHTLVVLDPRTPSDHYNWQATLQNESGKEVTVAVTSSPNAILGKYQLNV
KTGNHILKSEENILYLLFNPWCKEDMVFMPDEDERKEYILNDTGCHYVGAARSIKCKPWN
FGQFEKNVLDCCISLLTESSLKPTDRRDPVLVCRAMCAMMSFEKGQGVLIGNWTGDYEGG
TAPYKWTGSAPILQQYYNTKQAVCFGQCWVFAGILTTVLRALGIPARSVTGFDSAHDTER
NLTVDTYVNENGEKITSMTHDSVWNFHVWTDAWMKRPDLPKGYDGWQAVDATPQERSQGV
FCCGPSPLTAIRKGDIFIVYDTRFVFSEVNGDRLIWLVKMVNGQEELHVISMETTSIGKN
ISTKAVGQDRRRDITYEYKYPEGSSEERQVMDHAFLLLSSEREHRRPVKENFLHMSVQSD
DVLLGNSVNFTVILKRKTAALQNVNILGSFELQLYTGKKMAKLCDLNKTSQIQGQVSEVT
LTLDSKTYINSLAILDDEPVIRGFIIAEIVESKEIMASEVFTSFQYPEFSIELPNTGRIG
QLLVCNCIFKNTLAIPLTDVKFSLESLGISSLQTSDHGTVQPGETIQSQIKCTPIKTGPK
KFIVKLSSKQVKEINAQKIVLITK
Enzyme 52 Number of Residues 684
Enzyme 52 Molecular Weight 77144.6
Enzyme 52 Theoretical pI 6.75
Enzyme 52 GO Classification
Function
  • catalytic activity
  • protein-glutamine gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptide cross-linking
  • post-translational protein modification
  • protein modification process
Component
—
Enzyme 52 General Function Involved in protein-glutamine gamma-glutamyltransferase activity
Enzyme 52 Specific Function Associated with the mammalian reproductive process. Catalyzes the cross-linking of proteins and the conjugation of polyamines to specific proteins in the seminal tract
Enzyme 52 Pathways Not Available
Enzyme 52 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3 [RN:R03983]
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • None
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein Not Available
Enzyme 52 UniProtKB/Swiss-Prot ID P49221 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name TGM4_HUMAN Link Image
Enzyme 52 PDB ID Not Available
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence >2055 bp 
ATGATGGATGCATCAAAAGAGCTGCAAGTTCTCCACATTGACTTCTTGAATCAGGACAAC
GCCGTTTCTCACCACACATGGGAGTTCCAAACGAGCAGTCCTGTGTTCCGGCGAGGACAG
GTGTTTCACCTGCGGCTGGTGCTGAACCAGCCCCTACAATCCTACCACCAACTGAAACTG
GAATTCAGCACAGGGCCGAATCCTAGCATCGCCAAACACACCCTGGTGGTGCTCGACCCG
AGGACGCCCTCAGACCACTACAACTGGCAGGCAACCCTTCAAAATGAGTCTGGCAAAGAG
GTCACAGTGGCTGTCACCAGTTCCCCCAATGCCATCCTGGGCAAGTACCAACTAAACGTG
AAAACTGGAAACCACATCCTTAAGTCTGAAGAAAACATCCTATACCTTCTCTTCAACCCA
TGGTGTAAAGAGGACATGGTTTTCATGCCTGATGAGGACGAGCGCAAAGAGTACATCCTC
AATGACACGGGCTGCCATTACGTGGGGGCTGCCAGAAGTATCAAATGCAAACCCTGGAAC
TTTGGTCAGTTTGAGAAAAATGTCCTGGACTGCTGCATTTCCCTGCTGACTGAGAGCTCC
CTCAAGCCCACAGATAGGAGGGACCCCGTGCTGGTGTGCAGGGCCATGTGTGCTATGATG
AGCTTTGAGAAAGGCCAGGGCGTGCTCATTGGGAATTGGACTGGGGACTACGAAGGTGGC
ACAGCCCCATACAAGTGGACAGGCAGTGCCCCGATCCTGCAGCAGTACTACAACACGAAG
CAGGCTGTGTGCTTTGGCCAGTGCTGGGTGTTTGCTGGGATCCTGACTACAGTGCTGAGA
GCGTTGGGCATCCCAGCACGCAGTGTGACAGGCTTCGATTCAGCTCACGACACAGAAAGG
AACCTCACGGTGGACACCTATGTGAATGAGAATGGCGAGAAAATCACCAGTATGACCCAC
GACTCTGTCTGGAATTTCCATGTGTGGACGGATGCCTGGATGAAGCGACCGGATCTGCCC
AAGGGCTACGACGGCTGGCAGGCTGTGGACGCAACGCCGCAGGAGCGAAGCCAGGGTGTC
TTCTGCTGTGGGCCATCACCACTGACCGCCATCCGCAAAGGTGACATCTTTATTGTCTAT
GACACCAGATTCGTCTTCTCAGAAGTGAATGGTGACAGGCTCATCTGGTTGGTGAAGATG
GTGAATGGGCAGGAGGAGTTACACGTAATTTCAATGGAGACCACAAGCATCGGGAAAAAC
ATCAGCACCAAGGCAGTGGGCCAAGACAGGCGGAGAGATATCACCTATGAGTACAAGTAT
CCAGAAGGCTCCTCTGAGGAGAGGCAGGTCATGGATCATGCCTTCCTCCTTCTCAGTTCT
GAGAGGGAGCACAGACGACCTGTAAAAGAGAACTTTCTTCACATGTCGGTACAATCAGAT
GATGTGCTGCTGGGAAACTCTGTTAATTTCACCGTGATTCTTAAAAGGAAGACCGCTGCC
CTACAGAATGTCAACATCTTGGGCTCCTTTGAACTACAGTTGTACACTGGCAAGAAGATG
GCAAAACTGTGTGACCTCAATAAGACCTCGCAGATCCAAGGTCAAGTATCAGAAGTGACT
CTGACCTTGGACTCCAAGACCTACATCAACAGCCTGGCTATATTAGATGATGAGCCAGTT
ATCAGAGGTTTCATCATTGCGGAAATTGTGGAGTCTAAGGAAATCATGGCCTCTGAAGTA
TTCACGTCTTTCCAGTACCCTGAGTTCTCTATAGAGTTGCCTAACACAGGCAGAATTGGC
CAGCTACTTGTCTGCAATTGTATCTTCAAGAATACCCTGGCCATCCCTTTGACTGACGTC
AAGTTCTCTTTGGAAAGCCTGGGCATCTCCTCACTACAGACCTCTGACCATGGGACGGTG
CAGCCTGGTGAGACCATCCAATCCCAAATAAAATGCACCCCAATAAAAACTGGACCCAAG
AAATTTATCGTCAAGTTAAGTTCCAAACAAGTGAAAGAGATTAATGCTCAGAAGATTGTT
CTCATCACCAAGTAG
Enzyme 52 GenBank Gene ID L34840 Link Image
Enzyme 52 GeneCard ID TGM4 Link Image
Enzyme 52 GenAtlas ID TGM4 Link Image
Enzyme 52 HGNC ID HGNC:11780 Link Image
Enzyme 52 Chromosome Location 3
Enzyme 52 Locus 3p22-p21.33
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 General References
  1. Grant FJ, Taylor DA, Sheppard PO, Mathewes SL, Lint W, Vanaja E, Bishop PD, O'Hara PJ: Molecular cloning and characterization of a novel transglutaminase cDNA from a human prostate cDNA library. Biochem Biophys Res Commun. 1994 Sep 15;203(2):1117-23. [PubMed Link Image]
  2. Dubbink HJ, Verkaik NS, Faber PW, Trapman J, Schroder FH, Romijn JC: Tissue specific and androgen-regulated expression of human prostate-specific transglutaminase. Biochem J. 1996 May 1;315 ( Pt 3):901-8. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 5955
Enzyme 53 Name Protein-glutamine gamma-glutamyltransferase K
Enzyme 53 Synonyms
  1. Epidermal TGase
  2. Transglutaminase K
  3. TG(K)
  4. TGK
  5. TGase K
  6. Transglutaminase-1
  7. TGase-1
Enzyme 53 Gene Name TGM1
Enzyme 53 Protein Sequence >Protein-glutamine gamma-glutamyltransferase K 
MMDGPRSDVGRWGGNPLQPPTTPSPEPEPEPDGRSRRGGGRSFWARCCGCCSCRNAADDD
WGPEPSDSRGRGSSSGTRRPGSRGSDSRRPVSRGSGVNAAGDGTIREGMLVVNGVDLLSS
RSDQNRREHHTDEYEYDELIVRRGQPFHMLLLLSRTYESSDRITLELLIGNNPEVGKGTH
VIIPVGKGGSGGWKAQVVKASGQNLNLRVHTSPNAIIGKFQFTVRTQSDAGEFQLPFDPR
NEIYILFNPWCPEDIVYVDHEDWRQEYVLNESGRIYYGTEAQIGERTWNYGQFDHGVLDA
CLYILDRRGMPYGGRGDPVNVSRVISAMVNSLDDNGVLIGNWSGDYSRGTNPSAWVGSVE
ILLSYLRTGYSVPYGQCWVFAGVTTTVLRCLGLATRTVTNFNSAHDTDTSLTMDIYFDEN
MKPLEHLNHDSVWNFHVWNDCWMKRPDLPSGFDGWQVVDATPQETSSGIFCCGPCSVESI
KNGLVYMKYDTPFIFAEVNSDKVYWQRQDDGSFKIVYVEEKAIGTLIVTKAISSNMREDI
TYLYKHPEGSDAERKAVETAAAHGSKPNVYANRGSAEDVAMQVEAQDAVMGQDLMVSVML
INHSSSRRTVKLHLYLSVTFYTGVSGTIFKETKKEVELAPGASDRVTMPVAYKEYRPHLV
DQGAMLLNVSGHVKESGQVLAKQHTFRLRTPDLSLTLLGAAVVGQECEVQIVFKNPLPVT
LTNVVFRLEGSGLQRPKILNVGDIGGNETVTLRQSFVPVRPGPRQLIASLDSPQLSQVHG
VIQVDVAPAPGDGGFFSDAGGDSHLGETIPMASRGGA
Enzyme 53 Number of Residues 817
Enzyme 53 Molecular Weight 89786.1
Enzyme 53 Theoretical pI 5.92
Enzyme 53 GO Classification
Function
  • catalytic activity
  • protein-glutamine gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptide cross-linking
  • post-translational protein modification
  • protein modification process
Component
—
Enzyme 53 General Function Involved in protein-glutamine gamma-glutamyltransferase activity
Enzyme 53 Specific Function Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Responsible for cross- linking epidermal proteins during formation of the stratum corneum
Enzyme 53 Pathways Not Available
Enzyme 53 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3 [RN:R03983]
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • None
Enzyme 53 Transmembrane Regions
  • None
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein Not Available
Enzyme 53 UniProtKB/Swiss-Prot ID P22735 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name TGM1_HUMAN Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence >2454 bp 
ATGATGGATGGGCCACGTTCCGATGTGGGCCGTTGGGGTGGCAACCCCTTGCAGCCCCCT
ACCACGCCATCTCCAGAGCCAGAGCCAGAGCCAGACGGACGCTCTCGCAGAGGAGGAGGC
CGTTCCTTCTGGGCTCGCTGCTGTGGCTGCTGTTCATGCCGAAATGCGGCAGATGACGAC
TGGGGACCTGAACCCTCTGACTCCAGGGGTCGAGGGTCCAGCTCTGGCACTCGAAGACCT
GGCTCCCGGGGCTCAGACTCCCGCCGGCCTGTATCCCGGGGCAGCGGTGTCAATGCAGCT
GGAGATGGCACCATCCGAGAGGGCATGCTAGTAGTGAACGGTGTGGACTTGCTGAGCTCG
CGCTCGGACCAGAACCGCCGAGAGCACCACACAGACGAGTATGAGTACGACGAGCTGATA
GTGCGCCGCGGGCAGCCTTTCCATATGCTCCTCCTCCTGTCCCGGACCTATGAATCCTCT
GATCGCATCACCCTTGAGTTACTCATCGGAAACAACCCCGAGGTGGGCAAGGGCACGCAC
GTGATCATCCCAGTGGGCAAGGGGGGCAGTGGAGGCTGGAAAGCCCAGGTGGTCAAGGCC
AGTGGGCAGAATCTGAACCTGCGGGTCCACACTTCCCCCAACGCCATCATCGGCAAGTTT
CAGTTCACAGTCCGCACACAATCAGACGCTGGGGAGTTCCAGTTGCCCTTTGACCCCCGC
AATGAGATCTACATCCTCTTCAACCCCTGGTGCCCAGAGGACATTGTGTACGTGGACCAT
GAGGATTGGCGGCAGGAGTATGTTCTTAATGAGTCTGGGAGAATTTACTACGGGACCGAA
GCACAGATTGGTGAGCGGACCTGGAACTACGGCCAGTTTGACCACGGGGTGCTGGATGCC
TGCTTATACATCCTGGACCGGCGGGGGATGCCATATGGAGGCCGTGGAGACCCAGTCAAT
GTCTCCCGGGTCATCTCTGCCATGGTGAACTCCCTGGATGACAATGGAGTCCTGATTGGG
AACTGGTCTGGTGATTACTCCCGAGGCACCAACCCATCAGCGTGGGTGGGCAGCGTGGAG
ATCCTGCTTAGCTACCTACGCACGGGATATTCCGTCCCCTATGGCCAGTGCTGGGTCTTT
GCTGGAGTGACCACCACAGTGCTGCGCTGCCTGGGTCTGGCCACCCGTACTGTCACCAAC
TTCAACTCCGCCCACGACACAGACACATCCCTTACCATGGACATCTACTTCGACGAGAAC
ATGAAGCCCCTGGAGCACCTGAACCATGATTCTGTCTGGAACTTCCATGTGTGGAACGAC
TGCTGGATGAAGAGGCCGGATCTGCCCTCGGGCTTTGATGGGTGGCAGGTGGTGGATGCC
ACACCCCAAGAGACTAGCAGTGGCATCTTCTGCTGCGGCCCCTGCTCTGTGGAGTCCATC
AAGAATGGCCTGGTCTACATGAAGTACGACACGCCTTTCATTTTTGCTGAGGTGAATAGT
GACAAGGTGTACTGGCAGCGGCAGGATGATGGCAGCTTCAAGATTGTTTATGTGGAGGAG
AAGGCCATCGGCACACTCATTGTCACAAAGGCCATCAGCTCCAACATGCGGGAGGACATC
ACCTACCTCTATAAGCACCCAGAAGGCTCAGACGCAGAGCGGAAGGCAGTAGAGACAGCA
GCAGCCCACGGCAGCAAACCCAATGTGTATGCCAACCGGGGCTCAGCGGAGGATGTGGCC
ATGCAGGTGGAGGCACAGGACGCGGTGATGGGGCAGGATCTGATGGTCTCTGTGATGCTG
ATCAATCACAGCAGCAGCCGCCGCACAGTGAAACTGCACCTCTACCTCTCAGTCACTTTC
TATACTGGTGTCAGTGGTACCATCTTCAAGGAGACCAAGAAGGAAGTGGAGCTGGCACCA
GGGGCCTCGGACCGTGTGACCATGCCAGTGGCCTACAAGGAATACCGGCCCCATCTTGTG
GACCAGGGGGCCATGCTGCTCAATGTCTCAGGCCACGTCAAGGAGAGCGGGCAGGTGCTG
GCCAAGCAGCACACCTTCCGTCTGCGCACCCCAGACCTCTCCCTCACGTTACTGGGAGCA
GCAGTGGTTGGCCAGGAGTGTGAAGTACAGATTGTCTTCAAGAACCCCCTTCCCGTCACC
CTCACCAATGTCGTCTTCCGGCTCGAAGGCTCTGGGTTACAGAGGCCCAAGATCCTCAAC
GTTGGGGACATTGGAGGCAATGAAACAGTGACACTGCGCCAGTCGTTTGTGCCTGTGCGA
CCAGGCCCCCGCCAGCTCATTGCCAGCTTGGACAGCCCACAGCTCTCCCAGGTGCACGGT
GTCATCCAGGTGGATGTGGCCCCAGCCCCTGGGGATGGGGGCTTCTTCTCAGACGCTGGA
GGTGACAGTCACTTAGGAGAGACCATCCCTATGGCATCTCGAGGTGGAGCTTAG
Enzyme 53 GenBank Gene ID M55183 Link Image
Enzyme 53 GeneCard ID TGM1 Link Image
Enzyme 53 GenAtlas ID TGM1 Link Image
Enzyme 53 HGNC ID HGNC:11777 Link Image
Enzyme 53 Chromosome Location 1
Enzyme 53 Locus 14q11.2
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 General References
  1. Phillips MA, Stewart BE, Qin Q, Chakravarty R, Floyd EE, Jetten AM, Rice RH: Primary structure of keratinocyte transglutaminase. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9333-7. [PubMed Link Image]
  2. Yamanishi K, Liew FM, Konishi K, Yasuno H, Doi H, Hirano J, Fukushima S: Molecular cloning of human epidermal transglutaminase cDNA from keratinocytes in culture. Biochem Biophys Res Commun. 1991 Mar 29;175(3):906-13. [PubMed Link Image]
  3. Kim HC, Idler WW, Kim IG, Han JH, Chung SI, Steinert PM: The complete amino acid sequence of the human transglutaminase K enzyme deduced from the nucleic acid sequences of cDNA clones. J Biol Chem. 1991 Jan 5;266(1):536-9. [PubMed Link Image]
  4. Phillips MA, Stewart BE, Rice RH: Genomic structure of keratinocyte transglutaminase. Recruitment of new exon for modified function. J Biol Chem. 1992 Feb 5;267(4):2282-6. [PubMed Link Image]
  5. Kim IG, McBride OW, Wang M, Kim SY, Idler WW, Steinert PM: Structure and organization of the human transglutaminase 1 gene. J Biol Chem. 1992 Apr 15;267(11):7710-7. [PubMed Link Image]
  6. Yamanishi K, Inazawa J, Liew FM, Nonomura K, Ariyama T, Yasuno H, Abe T, Doi H, Hirano J, Fukushima S: Structure of the gene for human transglutaminase 1. J Biol Chem. 1992 Sep 5;267(25):17858-63. [PubMed Link Image]
  7. Polakowska RR, Eickbush T, Falciano V, Razvi F, Goldsmith LA: Organization and evolution of the human epidermal keratinocyte transglutaminase I gene. Proc Natl Acad Sci U S A. 1992 May 15;89(10):4476-80. [PubMed Link Image]
  8. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  9. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  10. Polakowska R, Herting E, Goldsmith LA: Isolation of cDNA for human epidermal type I transglutaminase. J Invest Dermatol. 1991 Feb;96(2):285-8. [PubMed Link Image]
  11. Schroeder WT, Thacher SM, Stewart-Galetka S, Annarella M, Chema D, Siciliano MJ, Davies PJ, Tang HY, Sowa BA, Duvic M: Type I keratinocyte transglutaminase: expression in human skin and psoriasis. J Invest Dermatol. 1992 Jul;99(1):27-34. [PubMed Link Image]
  12. Herman ML, Farasat S, Steinbach PJ, Wei MH, Toure O, Fleckman P, Blake P, Bale SJ, Toro JR: Transglutaminase-1 gene mutations in autosomal recessive congenital ichthyosis: summary of mutations (including 23 novel) and modeling of TGase-1. Hum Mutat. 2009 Apr;30(4):537-47. [PubMed Link Image]
  13. Huber M, Rettler I, Bernasconi K, Frenk E, Lavrijsen SP, Ponec M, Bon A, Lautenschlager S, Schorderet DF, Hohl D: Mutations of keratinocyte transglutaminase in lamellar ichthyosis. Science. 1995 Jan 27;267(5197):525-8. [PubMed Link Image]
  14. Russell LJ, DiGiovanna JJ, Rogers GR, Steinert PM, Hashem N, Compton JG, Bale SJ: Mutations in the gene for transglutaminase 1 in autosomal recessive lamellar ichthyosis. Nat Genet. 1995 Mar;9(3):279-83. [PubMed Link Image]
  15. Laiho E, Ignatius J, Mikkola H, Yee VC, Teller DC, Niemi KM, Saarialho-Kere U, Kere J, Palotie A: Transglutaminase 1 mutations in autosomal recessive congenital ichthyosis: private and recurrent mutations in an isolated population. Am J Hum Genet. 1997 Sep;61(3):529-38. [PubMed Link Image]
  16. Akiyama M, Takizawa Y, Kokaji T, Shimizu H: Novel mutations of TGM1 in a child with congenital ichthyosiform erythroderma. Br J Dermatol. 2001 Feb;144(2):401-7. [PubMed Link Image]
  17. Yang JM, Ahn KS, Cho MO, Yoneda K, Lee CH, Lee JH, Lee ES, Candi E, Melino G, Ahvazi B, Steinert PM: Novel mutations of the transglutaminase 1 gene in lamellar ichthyosis. J Invest Dermatol. 2001 Aug;117(2):214-8. [PubMed Link Image]
Enzyme 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 5957
Enzyme 54 Name Protein-arginine deiminase type-2
Enzyme 54 Synonyms
  1. PAD-H19
  2. Peptidylarginine deiminase II
  3. Protein-arginine deiminase type II
Enzyme 54 Gene Name PADI2
Enzyme 54 Protein Sequence >Protein-arginine deiminase type-2 
MLRERTVRLQYGSRVEAVYVLGTYLWTDVYSAAPAGAQTFSLKHSEHVWVEVVRDGEAEE
VATNGKQRWLLSPSTTLRVTMSQASTEASSDKVTVNYYDEEGSIPIDQAGLFLTAIEISL
DVDADRDGVVEKNNPKKASWTWGPEGQGAILLVNCDRETPWLPKEDCRDEKVYSKEDLKD
MSQMILRTKGPDRLPAGYEIVLYISMSDSDKVGVFYVENPFFGQRYIHILGRRKLYHVVK
YTGGSAELLFFVEGLCFPDEGFSGLVSIHVSLLEYMAQDIPLTPIFTDTVIFRIAPWIMT
PNILPPVSVFVCCMKDNYLFLKEVKNLVEKTNCELKVCFQYLNRGDRWIQDEIEFGYIEA
PHKGFPVVLDSPRDGNLKDFPVKELLGPDFGYVTREPLFESVTSLDSFGNLEVSPPVTVN
GKTYPLGRILIGSSFPLSGGRRMTKVVRDFLKAQQVQAPVELYSDWLTVGHVDEFMSFVP
IPGTKKFLLLMASTSACYKLFREKQKDGHGEAIMFKGLGGMSSKRITINKILSNESLVQE
NLYFQRCLDWNRDILKKELGLTEQDIIDLPALFKMDEDHRARAFFPNMVNMIVLDKDLGI
PKPFGPQVEEECCLEMHVRGLLEPLGLECTFIDDISAYHKFLGEVHCGTNVRRKPFTFKW
WHMVP
Enzyme 54 Number of Residues 665
Enzyme 54 Molecular Weight 75563.3
Enzyme 54 Theoretical pI 5.28
Enzyme 54 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • ion binding
  • metal ion binding
  • protein-arginine deiminase activity
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptidyl-amino acid modification
  • peptidyl-arginine modification
  • peptidyl-citrulline biosynthetic process from peptidyl-arginine
  • protein modification process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 54 General Function Involved in protein-arginine deiminase activity
Enzyme 54 Specific Function Catalyzes the deimination of arginine residues of proteins
Enzyme 54 Pathways Not Available
Enzyme 54 Reactions
  • protein L-arginine + H2O = protein L-citrulline + NH3 [RN:R02621]
Enzyme 54 Pfam Domain Function
Enzyme 54 Signals
  • None
Enzyme 54 Transmembrane Regions
  • None
Enzyme 54 Essentiality Not Available
Enzyme 54 GenBank ID Protein 122939159 Link Image
Enzyme 54 UniProtKB/Swiss-Prot ID Q9Y2J8 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name PADI2_HUMAN Link Image
Enzyme 54 PDB ID Not Available
Enzyme 54 Cellular Location Not Available
Enzyme 54 Gene Sequence >1998 bp 
ATGCTGCGCGAGCGGACCGTGCGGCTGCAGTACGGGAGCCGCGTGGAGGCGGTGTACGTG
CTGGGCACCTACCTCTGGACCGATGTCTACAGCGCGGCCCCAGCCGGGGCCCAAACCTTC
AGCCTGAAGCACTCGGAACACGTGTGGGTGGAGGTGGTGCGTGATGGGGAGGCTGAGGAG
GTGGCCACCAATGGCAAGCAGCGCTGGCTTCTCTCGCCCAGCACCACCCTGCGGGTCACC
ATGAGCCAGGCGAGCACCGAGGCCAGCAGTGACAAGGTCACCGTCAACTACTATGACGAG
GAAGGGAGCATTCCCATCGACCAGGCGGGGCTCTTCCTCACAGCCATTGAGATCTCCCTG
GATGTGGACGCAGACCGGGATGGTGTGGTGGAGAAGAACAACCCAAAGAAGGCATCCTGG
ACCTGGGGCCCCGAGGGCCAGGGGGCCATCCTGCTGGTGAACTGTGACCGAGAGACACCC
TGGTTGCCCAAGGAGGACTGCCGTGATGAGAAGGTCTACAGCAAGGAAGATCTCAAGGAC
ATGTCCCAGATGATCCTGCGGACCAAAGGCCCCGACCGCCTCCCCGCCGGATACGAGATA
GTTCTGTACATTTCCATGTCAGACTCAGACAAAGTGGGCGTGTTCTACGTGGAGAACCCG
TTCTTCGGCCAACGCTATATCCACATCCTGGGCCGGCGGAAGCTCTACCATGTGGTCAAG
TACACGGGTGGCTCCGCGGAGCTGCTGTTCTTCGTGGAAGGCCTCTGTTTCCCCGACGAG
GGCTTCTCAGGCCTGGTCTCCATCCATGTCAGCCTGCTGGAGTACATGGCCCAGGACATT
CCCCTGACTCCCATCTTCACGGACACCGTGATATTCCGGATTGCTCCGTGGATCATGACC
CCCAACATCCTGCCTCCCGTGTCGGTGTTTGTGTGCTGCATGAAGGATAATTACCTGTTC
CTGAAAGAGGTGAAGAACCTTGTGGAGAAAACCAACTGTGAGCTGAAGGTCTGCTTCCAG
TACCTAAACCGAGGCGATCGCTGGATCCAGGATGAAATTGAGTTTGGCTACATCGAGGCC
CCCCATAAAGGCTTCCCCGTGGTGCTGGACTCTCCCCGAGATGGAAACCTAAAGGACTTC
CCTGTGAAGGAGCTCCTGGGCCCAGATTTTGGCTACGTGACCCGGGAGCCCCTCTTTGAG
TCTGTCACCAGCCTTGACTCATTTGGAAACCTGGAGGTCAGTCCCCCAGTGACCGTGAAC
GGCAAGACATACCCGCTTGGCCGCATCCTCATCGGGAGCAGCTTTCCTCTGTCTGGTGGT
CGGAGGATGACCAAGGTGGTGCGTGACTTCCTGAAGGCCCAGCAGGTGCAGGCGCCCGTG
GAGCTCTACTCAGACTGGCTGACTGTGGGCCACGTGGATGAGTTCATGTCCTTTGTCCCC
ATCCCCGGCACAAAGAAATTCCTGCTACTCATGGCCAGCACCTCGGCCTGCTACAAGCTC
TTCCGAGAGAAGCAGAAGGACGGCCATGGAGAGGCCATCATGTTCAAAGGCTTGGGTGGG
ATGAGCAGCAAGCGAATCACCATCAACAAGATTCTGTCCAACGAGAGCCTTGTGCAGGAG
AACCTGTACTTCCAGCGCTGCCTAGACTGGAACCGTGACATCCTCAAGAAGGAGCTGGGA
CTGACAGAGCAGGACATCATTGACCTGCCCGCTCTGTTCAAGATGGACGAGGACCACCGT
GCCAGAGCCTTCTTCCCAAACATGGTGAACATGATCGTGCTGGACAAGGACCTGGGCATC
CCCAAGCCATTCGGGCCACAGGTTGAGGAGGAATGCTGCCTGGAGATGCACGTGCGTGGC
CTCCTGGAGCCCCTGGGCCTCGAATGCACCTTCATCGACGACATTTCTGCCTACCACAAA
TTTCTGGGGGAAGTCCACTGTGGCACCAACGTCCGCAGGAAGCCCTTCACCTTCAAGTGG
TGGCACATGGTGCCCTGA
Enzyme 54 GenBank Gene ID NM_007365.2 Link Image
Enzyme 54 GeneCard ID PADI2 Link Image
Enzyme 54 GenAtlas ID PADI2 Link Image
Enzyme 54 HGNC ID HGNC:18341 Link Image
Enzyme 54 Chromosome Location 1
Enzyme 54 Locus 1p36.13
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 General References
  1. Ishigami A, Ohsawa T, Asaga H, Akiyama K, Kuramoto M, Maruyama N: Human peptidylarginine deiminase type II: molecular cloning, gene organization, and expression in human skin. Arch Biochem Biophys. 2002 Nov 1;407(1):25-31. [PubMed Link Image]
  2. Chavanas S, Mechin MC, Takahara H, Kawada A, Nachat R, Serre G, Simon M: Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6. Gene. 2004 Apr 14;330:19-27. [PubMed Link Image]
  3. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Feb 26;6(1):63-70. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
Enzyme 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 5960
Enzyme 55 Name Protein-arginine deiminase type-1
Enzyme 55 Synonyms
  1. Peptidylarginine deiminase I
  2. Protein-arginine deiminase type I
Enzyme 55 Gene Name PADI1
Enzyme 55 Protein Sequence >Protein-arginine deiminase type-1 
MAPKRVVQLSLKMPTHAVCVVGVEAHVDIHSDVPKGANSFRVSGSSGVEVFMVYNRTRVK
EPIGKARWPLDTDADMVVSVGTASKELKDFKVRVSYFGEQEDQALGRSVLYLTGVDISLE
VDTGRTGKVKRSQGDKKTWRWGPEGYGAILLVNCDRDNHRSAEPDLTHSWLMSLADLQDM
SPMLLSCNGPDKLFDSHKLVLNVPFSDSKRVRVFCARGGNSLSDYKQVLGPQCLSYEVER
QPGEQEIKFYVEGLTFPDADFLGLVSLSVSLVDPGTLPEVTLFTDTVGFRMAPWIMTPNT
QPPEELYVCRVMDTHGSNEKFLEDMSYLTLKANCKLTICPQVENRNDRWIQDEMEFGYIE
APHKSFPVVFDSPRNRGLKDFPYKRILGPDFGYVTREIPLPGPSSLDSFGNLDVSPPVTV
GGTEYPLGRILIGSSFPKSGGRQMARAVRNFLKAQQVQAPVELYSDWLSVGHVDEFLTFV
PTSDQKGFRLLLASPSACLKLFQEKKEEGYGEAAQFDGLKHQAKRSINEMLADRHLQRDN
LHAQKCIDWNRNVLKRELGLAESDIVDIPQLFFLKNFYAEAFFPDMVNMVVLGKYLGIPK
PYGPIINGRCCLEEKVQSLLEPLGLHCIFIDDYLSYHELQGEIHCGTNVRRKPFPFKWWN
MVP
Enzyme 55 Number of Residues 663
Enzyme 55 Molecular Weight 74665.0
Enzyme 55 Theoretical pI 6.46
Enzyme 55 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
  • ion binding
  • metal ion binding
  • protein-arginine deiminase activity
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptidyl-amino acid modification
  • peptidyl-arginine modification
  • peptidyl-citrulline biosynthetic process from peptidyl-arginine
  • protein modification process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 55 General Function Involved in protein-arginine deiminase activity
Enzyme 55 Specific Function Catalyzes the deimination of arginine residues of proteins
Enzyme 55 Pathways Not Available
Enzyme 55 Reactions
  • protein L-arginine + H2O = protein L-citrulline + NH3 [RN:R02621]
Enzyme 55 Pfam Domain Function
Enzyme 55 Signals
  • None
Enzyme 55 Transmembrane Regions
  • None
Enzyme 55 Essentiality Not Available
Enzyme 55 GenBank ID Protein 6116899 Link Image
Enzyme 55 UniProtKB/Swiss-Prot ID Q9ULC6 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name PADI1_HUMAN Link Image
Enzyme 55 PDB ID Not Available
Enzyme 55 Cellular Location Not Available
Enzyme 55 Gene Sequence >1992 bp 
ATGGCCCCAAAGAGAGTTGTGCAGCTGTCCCTGAAGATGCCTACCCATGCCGTGTGTGTG
GTGGGAGTCGAGGCACATGTGGACATTCACAGTGATGTGCCCAAGGGTGCCAACAGCTTC
AGGGTCTCTGGAAGCTCCGGGGTGGAGGTCTTCATGGTCTACAACCGCACACGTGTGAAA
GAGCCCATAGGCAAGGCCCGTTGGCCGCTAGACACTGATGCAGACATGGTCGTATCTGTG
GGCACAGCCAGTAAGGAATTAAAGGACTTCAAGGTGAGGGTCTCCTACTTTGGGGAGCAG
GAAGACCAAGCTCTGGGCCGCAGCGTGCTTTACCTCACTGGCGTCGATATTTCCCTTGAG
GTTGACACAGGCCGCACAGGCAAGGTGAAGAGGAGCCAAGGGGACAAGAAAACCTGGCGC
TGGGGCCCTGAGGGCTATGGGGCTATCTTGCTGGTGAACTGTGACCGGGACAATCACAGG
TCCGCGGAGCCTGACCTCACCCACAGCTGGCTGATGTCGCTGGCTGACCTGCAGGACATG
TCCCCAATGCTGCTGAGCTGCAATGGCCCCGACAAGCTCTTCGACAGCCACAAGCTTGTC
TTGAACGTGCCCTTTTCTGATTCCAAAAGAGTGAGGGTCTTCTGTGCCAGGGGTGGGAAT
TCTCTCTCGGACTACAAACAGGTGCTGGGGCCCCAGTGTCTGTCCTATGAAGTTGAGCGA
CAGCCAGGGGAGCAGGAGATCAAGTTCTATGTGGAGGGGCTGACCTTCCCCGATGCCGAT
TTCCTAGGGCTGGTTTCCCTCAGTGTCAGCCTGGTGGACCCGGGGACCCTGCCCGAGGTG
ACCCTCTTCACAGACACTGTGGGCTTCCGCATGGCCCCCTGGATCATGACGCCCAACACT
CAGCCTCCTGAGGAGCTGTATGTGTGCAGAGTGATGGACACTCATGGCTCCAATGAGAAA
TTCCTGGAGGACATGTCTTATCTGACATTGAAAGCCAACTGCAAGCTGACCATCTGCCCT
CAAGTTGAAAATCGAAATGACCGCTGGATCCAGGACGAGATGGAGTTTGGCTACATCGAG
GCCCCTCACAAATCCTTCCCCGTGGTCTTTGACTCCCCCAGGAACAGGGGCCTGAAAGAT
TTCCCCTATAAGAGGATCCTGGGTCCTGACTTTGGATATGTTACCCGGGAGATCCCGCTC
CCTGGTCCCTCCAGCCTTGACTCCTTCGGCAACCTGGACGTCAGCCCGCCCGTCACGGGG
GGCGGCACGGAATACCCCCTGGGCCGGATCCTCATCGGGAGCAGCTTCCCCAAGTCCGGT
GGGCGGCAGATGGCCAGGGCAGTGCGGAACTTCCTGAAGGCACAGCAGGTGCAGGCACCC
GTGGAGCTCTACTCGGACTGGCTCTCTGTGGGCCATGTGGACGAGTTTCTGACCTTTGTG
CCTACCTCTGACCAGAAGGGCTTCCGGCTGCTCCTGGCTAGCCCCAGCGCTTGCCCCAAA
CTCTTCCAAGAGAAGAAAGAAGAGGGTTATGGGGAGGCAGCCCAGTTTGATGGGTTAAAA
CACCAGGCAAAAAGAAGCATTAATGAGATGCTGGCAGACAGACACCTCCAGAGAGACAAT
CTTCATGCACAGAAATGCATTGACTGGAACCGTAATGTGCTGAAGCGGGAGCTGGGCCTG
GCAGAGAGTGACATCGTGGACATTCCCCAGCTCTTCTTCCTGAAAAACTTCTACGCGGAA
GCCTTCTTCCCAGACATGGTTAACATGGTGGTCTTAGGCAAGTACCTGGGCATCCCCAAG
CCCTACGGGCCCATCATCAATGGCCGCTGCTGCCTGGAGGAGAAGGTGCAGTCCCTGCTG
GAGCCTCTGGGCCTGCACTGCATCTTCATTGATGACTACTTGTCCTACCACGAGCTGCAG
GGGGAGATCCACTGTGGCACCAACGTGCGCAGGAAGCCCTTTCCCTTCAAATGGTGGAAC
ATGGTGCCCTGA
Enzyme 55 GenBank Gene ID AB033768 Link Image
Enzyme 55 GeneCard ID PADI1 Link Image
Enzyme 55 GenAtlas ID PADI1 Link Image
Enzyme 55 HGNC ID HGNC:18367 Link Image
Enzyme 55 Chromosome Location 1
Enzyme 55 Locus 1p36.13
Enzyme 55 SNPs SNPJam Report Link Image
Enzyme 55 General References
  1. Guerrin M, Ishigami A, Mechin MC, Nachat R, Valmary S, Sebbag M, Simon M, Senshu T, Serre G: cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I. Biochem J. 2003 Feb 15;370(Pt 1):167-74. [PubMed Link Image]
  2. Chavanas S, Mechin MC, Takahara H, Kawada A, Nachat R, Serre G, Simon M: Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6. Gene. 2004 Apr 14;330:19-27. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 55 Metabolite References Not Available
Enzyme 56 [top]
Enzyme 56 ID 5964
Enzyme 56 Name Protein-glutamine gamma-glutamyltransferase 6
Enzyme 56 Synonyms
  1. Transglutaminase Y
  2. TGase Y
  3. Transglutaminase-3-like
  4. TGase-3-like
  5. Transglutaminase-6
  6. TGase-6
Enzyme 56 Gene Name TGM6
Enzyme 56 Protein Sequence >Protein-glutamine gamma-glutamyltransferase 6 
MAGIRVTKVDWQRSRNGAAHHTQEYPCPELVVRRGQSFSLTLELSRALDCEEILIFTMET
GPRASEALHTKAVFQTSELERGEGWTAAREAQMEKTLTVSLASPPSAVIGRYLLSIRLSS
HRKHSNRRLGEFVLLFNPWCAEDDVFLASEEERQEYVLSDSGIIFRGVEKHIRAQGWNYG
QFEEDILNICLSILDRSPGHQNNPATDVSCRHNPIYVTRVISAMVNSNNDRGVVQGQWQG
KYGGGTSPLHWRGSVAILQKWLKGRYKPVKYGQCWVFAGVLCTVLRCLGIATRVVSNFNS
AHDTDQNLSVDKYVDSFGRTLEDLTEDSMWNFHVWNESWFARQDLGPSYNGWQVLDATPQ
EESEGVFRCGPASVTAIREGDVHLAHDGPFVFAEVNADYITWLWHEDESRERVYSNTKKI
GRCISTKAVGSDSRVDITDLYKYPEGSRKERQVYSKAVNRLFGVEASGRRIWIRRAGGRC
LWRDDLLEPATKPSIAGKFKVLEPPMLGHDLRLALCLANLTSRAQRVRVNLSGATILYTR
KPVAEILHESHAVRLGPQEEKRIPITISYSKYKEDLTEDKKILLAAMCLVTKGEKLLVEK
DITLEDFITIKVLGPAMVGVAVTVEVTVVNPLIERVKDCALMVEGSGLLQEQLSIDVPTL
EPQERASVQFDITPSKSGPRQLQVDLVSPHFPDIKGFVIVHVATAK
Enzyme 56 Number of Residues 706
Enzyme 56 Molecular Weight 79311.7
Enzyme 56 Theoretical pI 7.26
Enzyme 56 GO Classification
Function
  • catalytic activity
  • protein-glutamine gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptide cross-linking
  • post-translational protein modification
  • protein modification process
Component
—
Enzyme 56 General Function Involved in protein-glutamine gamma-glutamyltransferase activity
Enzyme 56 Specific Function Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins
Enzyme 56 Pathways Not Available
Enzyme 56 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3 [RN:R03983]
Enzyme 56 Pfam Domain Function
Enzyme 56 Signals
  • None
Enzyme 56 Transmembrane Regions
  • None
Enzyme 56 Essentiality Not Available
Enzyme 56 GenBank ID Protein 33331030 Link Image
Enzyme 56 UniProtKB/Swiss-Prot ID O95932 Link Image
Enzyme 56 UniProtKB/Swiss-Prot Entry Name TGM3L_HUMAN Link Image
Enzyme 56 PDB ID Not Available
Enzyme 56 Cellular Location Not Available
Enzyme 56 Gene Sequence >2121 bp 
ATGGCAGGGATCAGAGTCACCAAGGTGGACTGGCAGCGGTCGAGGAATGGCGCTGCCCAC
CACACCCAGGAGTACCCCTGCCCTGAGCTGGTGGTTCGCAGGGGCCAGTCGTTCAGCCTC
ACGCTGGAGCTGAGCAGAGCCCTGGACTGTGAGGAGATCCTCATCTTCACGGTGGAGACA
GGACCCCGGGCTTCTGAGGCCCTCCACACCAAAGCTGTGTTCCAGACATCGGAGCTGGAG
CGGGGTGAGGGCTGGACAGCAGCAAGGGAGGCTCAGATGGAGAAAACTCTGACCGTCAGT
CTCGCCAGCCCTCCCAGTGCTGTCATTGGCCGCTACCTGCTGAGCATCAGGCTTTCCTCT
CACCGCAAACACAGCAACCGGAGGCTGGGCGAGTTTGTTCTCCTTTTCAACCCATGGTGT
GCAGAGGACGATGTGTTTCTGGCCTCAGAGGAGGAGAGACAGGAGTACGTGCTCAGCGAC
AGCGGCATCATCTTCCGAGGCGTGGAGAAGCACATACGAGCCCAGGGCTGGAACTACGGG
CAGTTTGAGGAGGACATCCTGAACATCTGCCTCTCCATCCTGGATCGAAGCCCCGGTCAC
CAAAACAACCCAGCCACCGACGTGTCCTGCCGCCACAACCCCATCTACGTCACCAGGGTC
ATCAGTGCCATGGTGAACAGCAACAACGACCGAGGTGTGGTGCAAGGACAGTGGCAGGGC
AAGTACGGCGGCGGCACCAGCCCGCTGCACTGGCGCGGCAGCGTGGCCATTCTGCAGAAG
TGGCTCAAGGGCAGGTACAAGCCAGTCAAGTACGGCCAGTGCTGGGTCTTCGCCGGAGTC
CTGTGCACAGTCCTCAGGTGCTTGGGGATAGCCACACGGGTCGTGTCCAACTTCAACTCA
GCCCACGACACAGACCAGAACCTGAGTGTGGACAAATACGTGGACTCCTTCGGGCGGACC
CTGGAGGACCTGACAGAAGACAGCATGTGGAATTTCCATGTCTGGAATGAGAGCTGGTTT
GCCCGGCAGGACCTAGGCCCCTCTTACAATGGCTGGCAGGTTCTGGATGCCACCCCCCAG
GAGGAGAGTGAAGGTGTGTTCCGGTGCGGCCCAGCCTCAGTCACCGCCATCCGCGAGGGT
GATGTGCACCTGGCTCACGATGGCCCCTTCGTGTTTGCGGAGGTCAACGCCGACTACATC
ACCTGGCTGTGGCACGAGGATGAGAGCCGGGAGCGTGTATACTCAAACACGAAGAAGATT
GGGAGATGCATCAGCACCAAGGCGGTGGGCAGTGACTCCCGCGTGGACATCACTGACCTC
TACAAGTATCCGGAAGGGTCCCGGAAAGAGAGGCAGGTGTACAGCAAGGCGGTGAACAGG
CTGTTCGGCGTGGAAGCCTCTGGAAGGAGAATCTGGATCCGCAGGGCTGGGGGTCGCTGT
CTCTGGCGTGACGACCTCCTGGAGCCTGCCACCAAGCCCAGCATCGCTGGCAAGTTCAAG
GTGCTAGAGCCTCCCATGCTGGGCCACGACCTGAGACTGGCCCTGTGCTTGGCCAACCTC
ACCTCCCGGGCCCAGCGGGTGAGGGTCAACCTGAGCGGTGCCACCATCCTCTATACCCGC
AAGCCAGTGGCAGAGATCCTGCATGAATCCCACGCCGTGAGGCTGGGGCCGCAAGAAGAG
AAGAGAATCCCAATTACAATATCTTACTCTAAGTATAAAGAAGACCTGACAGAGGACAAG
AAGATCCTGTTGGCTGCCATGTGCCTTGTCACCAAAGGAGAGAAGCTTCTGGTGGAGAAG
GACATTACTCTAGAGGACTTCATCACCATCAAGGTTCTGGGCCCAGCCATGGTGGGAGTG
GCAGTTACAGTGGAAGTGACAGTAGTCAACCCCCTCATAGAGAGAGTGAAGGACTGTGCG
CTGATGGTGGAGGGCAGCGGCCTTCTCCAGGAACAGCTCAGCATCGACGTGCCTACCCTG
GAGCCTCAGGAGAGGGCCTCAGTCCAGTTTGACATCACCCCCTCCAAAAGTGGCCCAAGG
CAGCTGCAGGTGGACCTTGTAAGCCCTCACTTCCCGGACATCAAGGGCTTTGTGATCGTC
CATGTGGCCACTGCCAAGTGA
Enzyme 56 GenBank Gene ID AF540969 Link Image
Enzyme 56 GeneCard ID TGM6 Link Image
Enzyme 56 GenAtlas ID TGM6 Link Image
Enzyme 56 HGNC ID HGNC:16255 Link Image
Enzyme 56 Chromosome Location 2
Enzyme 56 Locus 20p13
Enzyme 56 SNPs SNPJam Report Link Image
Enzyme 56 General References
  1. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
Enzyme 56 Metabolite References Not Available
Enzyme 57 [top]
Enzyme 57 ID 5966
Enzyme 57 Name Protein-glutamine gamma-glutamyltransferase Z
Enzyme 57 Synonyms
  1. Transglutaminase Z
  2. TG(Z)
  3. TGZ
  4. TGase Z
  5. Transglutaminase-7
  6. TGase-7
Enzyme 57 Gene Name TGM7
Enzyme 57 Protein Sequence >Protein-glutamine gamma-glutamyltransferase Z 
MDQVATLRLESVDLQSSRNNKEHHTQEMGVKRLTVRRGQPFYLRLSFSRPFQSQNDHITF
VAETGPKPSELLGTRATFFLTRVQPGNVWSASDFTIDSNSLQVSLFTPANAVIGHYTLKI
EISQGQGHSVTYPLGTFILLFNPWSPEDDVYLPSEILLQEYIMRDYGFVYKGHERFITSW
PWNYGQFEEDIIDICFEILNKSLYHLKNPAKDCSQRNDVVYVCRVVSAMINSNDDNGVLQ
GNWGEDYSKGVSPLEWKGSVAILQQWSARGGQPVKYGQCWVFASVMCTVMRCLGVPTRVV
SNFRSAHNVDRNLTIDTYYDRNAEMLSTQKRDKIWNFHVWNECWMIRKDLPPGYNGWQVL
DPTPQQTSSGLFCCGPASVKAIREGDVHLAYDTPFVYAEVNADEVIWLLGDGQAQEILAH
NTSSIGKEISTKMVGSDQRQSITSSYKYPEGSPEERAVFMKASRKMLGPQRASLPFLDLL
ESGGLRDQPAQLQLHLARIPEWGQDLQLLLRIQRVPDSTHPRGPIGLVVRFCAQALLHGG
GTQKPFWRHTVRMNLDFGKETQWPLLLPYSNYRNKLTDEKLIRVSGIAEVEETGRSMLVL
KDICLEPPHLSIEVSERAEVGKALRVHVTLTNTLMVALSSCTMVLEGSGLINGQIAKDLG
TLVAGHTLQIQLDLYPTKAGPRQLQVLISSNEVKEIKGYKDIFVTVAGAP
Enzyme 57 Number of Residues 710
Enzyme 57 Molecular Weight 79940.6
Enzyme 57 Theoretical pI 7.00
Enzyme 57 GO Classification
Function
  • catalytic activity
  • protein-glutamine gamma-glutamyltransferase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring amino-acyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • peptide cross-linking
  • post-translational protein modification
  • protein modification process
Component
—
Enzyme 57 General Function Involved in protein-glutamine gamma-glutamyltransferase activity
Enzyme 57 Specific Function Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins
Enzyme 57 Pathways Not Available
Enzyme 57 Reactions
  • protein glutamine + alkylamine = protein N5-alkylglutamine + NH3 [RN:R03983]
Enzyme 57 Pfam Domain Function
Enzyme 57 Signals
  • None
Enzyme 57 Transmembrane Regions
  • None
Enzyme 57 Essentiality Not Available
Enzyme 57 GenBank ID Protein 15425755 Link Image
Enzyme 57 UniProtKB/Swiss-Prot ID Q96PF1 Link Image
Enzyme 57 UniProtKB/Swiss-Prot Entry Name TGM7_HUMAN Link Image
Enzyme 57 PDB ID Not Available
Enzyme 57 Cellular Location Not Available
Enzyme 57 Gene Sequence >2133 bp 
ATGGATCAGGTGGCAACCTTGCGGCTTGAGTCTGTCGACCTGCAGAGCTCCAGGAACAAC
AAGGAGCACCACACGCAGGAGATGGGCGTCAAGCGGCTCACTGTGCGCCGCGGCCAGCCC
TTCTACCTCCGGCTGAGCTTCAGCCGACCCTTCCAGTCCCAGAACGACCACATCACCTTT
GTGGCTGAGACCGGACCCAAGCCGTCAGAGCTGCTGGGGACCCGAGCCACATTCTTCCTC
ACCCGGGTCCAGCCCGGGAATGTCTGGAGCGCTTCTGATTTCACCATTGACTCCAACTCT
CTCCAAGTTTCCCTTTTCACACCAGCCAATGCAGTTATTGGCCATTACACTCTGAAAATA
GAGATCTCTCAGGGCCAAGGTCACAGTGTGACTTACCCGCTGGGAACTTTCATCCTACTT
TTTAACCCTTGGAGTCCAGAGGACGACGTCTACCTGCCAAGTGAAATACTGCTGCAGGAG
TATATCATGCGAGATTATGGCTTTGTTTACAAGGGTCATGAAAGATTCATCACCTCCTGG
CCCTGGAACTACGGGCAGTTTGAAGAGGACATCATAGACATCTGCTTTGAGATCCTGAAC
AAGAGCCTGTATCACTTAAAGAACCCGGCCAAAGACTGTTCCCAGCGGAACGACGTGGTG
TATGTGTGCAGGGTGGTGAGTGCCATGATCAACAGCAACGATGACAATGGCGTGCTGCAG
GGGAACTGGGGCGAGGACTACTCCAAAGGGGTCAGTCCTCTGGAGTGGAAGGGCAGTGTG
GCCATCCTACAGCAGTGGTCAGCCAGGGGCGGGCAGCCTGTGAAGTACGGACAGTGCTGG
GTCTTCGCCTCTGTTATGTGCACCGTAATGAGATGCTTAGGTGTTCCAACCCGTGTTGTT
TCCAATTTCCGTTCCGCGCACAACGTGGATAGGAACTTGACCATCGATACGTACTATGAC
CGAAATGCCGAGATGCTGTCAACTCAGAAACGAGACAAAATATGGAACTTCCACGTCTGG
AATGAGTGCTGGATGATCCGGAAAGATCTCCCACCAGGATACAACGGGTGGCAGGTTCTG
GACCCCACTCCCCAGCAGACCAGCAGTGGGCTGTTCTGCTGTGGCCCTGCCTCTGTGAAG
GCCATCAGGGAAGGGGATGTCCACCTGGCCTATGACACCCCTTTTGTGTATGCCGAGGTG
AACGCCGATGAAGTCATTTGGCTCCTTGGGGATGGCCAGGCCCAGGAAATCCTGGCCCAC
AACACCAGTTCCATCGGGAAGGAGATCAGCACTAAGATGGTGGGGTCAGACCAGCGCCAG
AGCATCACCAGCTCCTACAAGTACCCAGAAGGATCCCCTGAGGAGAGAGCTGTCTTCATG
AAGGCTTCTCGGAAAATGCTGGGCCCCCAAAGAGCTTCTTTGCCCTTCCTGGATCTCCTG
GAGTCTGGGGGTCTTAGGGATCAGCCAGCGCAGCTGCAGCTTCACCTGGCCAGGATACCC
GAGTGGGGCCAGGACCTGCAGCTGCTGCTGCGTATCCAGAGGGTGCCAGACAGCACCCAC
CCTCGGGGGCCCATCGGACTGGTGGTGCGCTTCTGTGCACAGGCCCTGCTGCATGGGGGT
GGTACCCAGAAGCCCTTCTGGAGGCACACAGTGCGGATGAACCTGGACTTTGGGAAGGAG
ACACAGTGGCCGCTCCTCCTGCCCTACAGCAATTACAGAAACAAGCTAACGGACGAAAAG
CTCATCCGCGTGTCTGGCATCGCGGAGGTTGAAGAGACAGGGAGGTCCATGCTGGTCCTA
AAAGATATCTGTCTGGAGCCTCCCCACTTGTCTATTGAGGTGTCTGAGAGGGCTGAGGTG
GGCAAGGCGCTGAGAGTCCATGTCACCCTCACCAACACCTTAATGGTGGCTCTGAGCAGC
TGCACGATGGTGCTGGAAGGAAGCGGCCTCATCAATGGGCAGATAGCAAAGGACCTTGGG
ACTCTGGTGGCCGGACACACCCTCCAAATTCAACTGGACCTCTACCCGACCAAAGCTGGA
CCCCGCCAGCTCCAGGTTCTCATCAGCAGCAACGAGGTCAAGGAGATCAAAGGCTACAAG
GACATATTCGTCACTGTGGCTGGGGCTCCCTGA
Enzyme 57 GenBank Gene ID AF363393 Link Image
Enzyme 57 GeneCard ID TGM7 Link Image
Enzyme 57 GenAtlas ID TGM7 Link Image
Enzyme 57 HGNC ID HGNC:30790 Link Image
Enzyme 57 Chromosome Location 1
Enzyme 57 Locus 15q15.2
Enzyme 57 SNPs SNPJam Report Link Image
Enzyme 57 General References
  1. Grenard P, Bates MK, Aeschlimann D: Evolution of transglutaminase genes: identification of a transglutaminase gene cluster on human chromosome 15q15. Structure of the gene encoding transglutaminase X and a novel gene family member, transglutaminase Z. J Biol Chem. 2001 Aug 31;276(35):33066-78. Epub 2001 Jun 4. [PubMed Link Image]
Enzyme 57 Metabolite References Not Available
Enzyme 58 [top]
Enzyme 58 ID 5977
Enzyme 58 Name Adenylate cyclase type 7
Enzyme 58 Synonyms
  1. ATP pyrophosphate-lyase 7
  2. Adenylate cyclase type VII
  3. Adenylyl cyclase 7
Enzyme 58 Gene Name ADCY7
Enzyme 58 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 58 Number of Residues 1080
Enzyme 58 Molecular Weight 120307.2
Enzyme 58 Theoretical pI 8.16
Enzyme 58 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 58 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 58 Specific Function This is a membrane-bound, calcium-inhibitable adenylyl cyclase
Enzyme 58 Pathways
Enzyme 58 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 58 Pfam Domain Function
Enzyme 58 Signals
  • None
Enzyme 58 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 58 Essentiality Not Available
Enzyme 58 GenBank ID Protein 116496681 Link Image
Enzyme 58 UniProtKB/Swiss-Prot ID P51828 Link Image
Enzyme 58 UniProtKB/Swiss-Prot Entry Name ADCY7_HUMAN Link Image
Enzyme 58 PDB ID Not Available
Enzyme 58 Cellular Location Not Available
Enzyme 58 Gene Sequence >3243 bp 
ATGCCAGCCAAGGGGCGCTACTTCCTCAACGAGGGCGAGGAGGGCCCTGACCAAGATGCG
CTCTACGAGAAGTACCAGCTCACCAGCCAGCATGGGCCGCTGCTGCTCACGCTCCTGCTG
GTGGCCGCCACTGCCTGCGTGGCCCTCATCATCATTGCCTTCAGCCAGGGGGACCCCTCC
AGACACCAGGCCATTCTGGGCATGGCGTTCCTGGTGCTGGCGGTGTTTGCGGCCCTCTCT
GTGCTGATGTACGTCGAGTGTCTCCTGCGGCGCTGGCTCAGGGCCTTGGCGCTGCTCACC
TGGGCCTGCTTGGTGGCGCTGGGCTATGTGCTGGTGTTCGACGCATGGACAAAGGCGGCC
TGTGCGTGGGAGCAGGTGCCCTTCTTCCTGTTCATTGTCTTCGTGGTGTACACACTACTG
CCCTTCAGCATGCGGGGCGCTGTCGCCGTTGGGGCCGTCTCCACTGCCTCCCACCTCCTG
GTGCTCGGTTCTTTGATGGGAGGCTTCACGACACCCAGTGTCCGGGTGGGGCTGCAGCTG
CTGGCCAACGCAGTCATCTTCCTGTGTGGGAACCTGACAGGCGCCTTCCACAAGCACCAA
ATGCAGGATGCGTCCCGGGACCTCTTCACCTACACTGTGAAGTGCATCCAGATCCGCCGG
AAGCTGCGCATCGAGAAGCGCCAGCAGGAGAACCTGCTGCTGTCAGTGCTTCCGGCCCAC
ATCTCCATGGGCATGAAGCTGGCCATCATCGAACGGCTCAAGGAGCATGGTGACCGTCGC
TGCATGCCTGACAACAACTTCCACAGCCTCTACGTCAAGAGGCACCAGAATGTCAGCATC
CTCTATGCGGACATCGTGGGCTTCACGCAGCTGGCCAGCGACTGTTCTCCCAAGGAGCTG
GTGGTGGTGCTGAATGAGCTCTTTGGCAAGTTCGACCAGATCGCCAAGGCCAACGAGTGC
ATGCGAATCAAGATCCTCGGCGACTGCTACTACTGTGTATCGGGCCTGCCCGTGTCGCTG
CCTACCCACGCCCGGAACTGCGTGAAGATGGGGCTGGACATGTGCCAGGCCATCAAGCAG
GTGCGGGAGGCCACGGGCGTGGACATCAACATGCGTGTGGGCATACACTCGGGGAATGTG
CTGTGCGGGGTCATCGGGCTGCGCAAGTGGCAGTATGACGTGTGGTCCCACGACGTGTCC
CTGGCCAACCGGATGGAGGCAGCCGGAGTACCCGGCCGGGTGCACATCACGGAGGCCACG
CTAAAGCACCTGGACAAGGCGTACGAGGTGGAGGATGGGCACGGGCAGCAGCGGGACCCC
TACCTCAAGGAGATGAACATCCGCACCTACCTGGTCATCGACCCCCGGAGCCAGCAGCCA
CCCCCGCCCAGCCAACACCTCCCCAGGCCCAAGGGGGACGCGGCCCTGAAGATGCGGGCG
TCAGTGCGCATGACCCGGTACCTCGAGTCCTGGGGGGCGGCACGGCCCTTTGCACATCTC
AACCACCGTGAGAGCGTGAGCAGTGGTGAGACCCACGTCCCCAACGGGCGGAGGCCTAAG
AGCGTTCCCCAGCGCCACCGCCGGACCCCAGACAGAAGCATGTCCCCCAAGGGGCGGTCG
GAGGATGACTCGTACGATGACGAGATGCTGTCAGCCATTGAGGGGCTCAGCTCCACGAGG
CCCTGCTGCTCCAAGTCCGATGACTTCTACACCTTTGGGTCCATCTTCCTGGAGAAGGGC
TTTGAGCGCGAGTACCGCCTGGCACCCATCCCCCGGGCCCGCCACGACTTTGCCTGCGCC
AGCCTGATCTTCGTCTGCATCCTGCTCGTCCATGTCCTGCTCATGCCCAGGACGGCGGCA
CTGGGTGTGTCCTTCGGGCTGGTGGCCTGTGTACTGGGGCTGGTGCTGGGCCTGTGCTTT
GCCACCAAGTTCTCGAGGTGCTGCCCAGCTCGGGGGACGCTCTGCACTATCTCTGAGAGG
GTGGAGACACAGCCCCTGCTGAGGCTGACCCTGGCCGTCCTGACCATCGGCAGCCTGCTC
ACTGTGGCCATCATCAACCTGCCCCTGATGCCTTTCCAAGTTCCAGAGCTGCCTGTTGGC
AATGAGACAGGCCTACTGGCCGCGAGCAGCAAGACAAGAGCCCTGTGTGAGCCCCTCCCG
TACTACACCTGCAGCTGTGTCCTGGGCTTCATCGCCTGCTCGGTCTTCCTGAGGATGAGC
CTGGAGCCAAAGGTTGTGCTGCTGACAGTGGCCCTGGTGGCCTACCTGGTGCTCTTCAAC
CTCTCCCCATGCTGGCAGTGGGACTGCTGCGGCCAAGGCCTGGGCAACCTCACCAAGCCC
AACGGCACCACCAGTGGCACCCCTAGCTGTTCCTGGAAGGACCTGAAGACCATGACCAAT
TTCTACCTGGTCCTGTTCTACATCACCCTGCTTACACTCTCCAGACAGATTGACTATTAC
TGCCGCTTGGACTGCCTATGGAAGAAGAAGTTCAAGAAGGAGCACGAGGAGTTTGAGACC
ATGGAGAACGTGAACCGCCTTCTTCTGGAGAACGTCCTGCCAGCCCACGTGGCTGCCCAC
TTTATCGGTGACAAGTTAAACGAGGACTGGTACCATCAGTCCTATGACTGCGTCTGTGTC
ATGTTTGCCTCCGTGCCGGACTTCAAAGTGTTCTACACAGAGTGCGATGTCAACAAAGAA
GGGCTGGAGTGCCTACGCCTGCTCAATGAGATCATTGCCGACTTCGACGAGCTCCTACTG
AAGCCCAAGTTCAGCGGCGTGGAGAAGATCAAGACCATCGGCAGCACGTACATGGCAGCT
GCAGGGCTCAGCGTCGCCTCAGGGCACGAGAACCAGGAGCTGGAGCGGCAGCATGCCCAC
ATTGGTGTCATGGTGGAGTTCAGCATCGCCCTGATGAGTAAGCTGGACGGCATCAACAGG
CACTCCTTCAACTCCTTCCGCCTCCGCGTCGGCATAAACCATGGGCCTGTGATTGCTGGA
GTGATTGGGGCCCGAAAACCTCAGTATGACATCTGGGGAAACACTGTCAATGTGGCCAGC
CGAATGGAAAGCACTGGAGAACTTGGGAAAATCCAGGTTACCGAGGAGACCTGCACCATC
CTCCAGGGCCTCGGGTACTCTTGTGAATGCCGTGGCCTGATCAACGTCAAAGGCAAAGGC
GAGCTGAGGACTTACTTTGTCTGTACGGACACTGCCAAGTTTCAGGGGCTGGGGCTGAAC
TGA
Enzyme 58 GenBank Gene ID BC126271 Link Image
Enzyme 58 GeneCard ID ADCY7 Link Image
Enzyme 58 GenAtlas ID ADCY7 Link Image
Enzyme 58 HGNC ID HGNC:238 Link Image
Enzyme 58 Chromosome Location 1
Enzyme 58 Locus 16q12.1
Enzyme 58 SNPs SNPJam Report Link Image
Enzyme 58 General References
  1. Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 58 Metabolite References Not Available
Enzyme 59 [top]
Enzyme 59 ID 5978
Enzyme 59 Name Adenylate cyclase type 4
Enzyme 59 Synonyms
  1. ATP pyrophosphate-lyase 4
  2. Adenylate cyclase type IV
  3. Adenylyl cyclase 4
Enzyme 59 Gene Name ADCY4
Enzyme 59 Protein Sequence >Adenylate cyclase type 4 
MARLFSPRPPPSEDLFYETYYSLSQQYPLLLLLLGIVLCALAALLAVAWASGRELTSDPS
FLTTVLCALGGFSLLLGLASREQRLQRWTRPLSGLVWVALLALGHAFLFTGGVVSAWDQV
SYFLFVIFTAYAMLPLGMRDAAVAGLASSLSHLLVLGLYLGPQPDSRPALLPQLAANAVL
FLCGNVAGVYHKALMERALRATFREALSSLHSRRRLDTEKKHQEHLLLSILPAYLAREMK
AEIMARLQAGQGSRPESTNNFHSLYVKRHQGVSVLYADIVGFTRLASECSPKELVLMLNE
LFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRAIRKLRAATG
VDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAG
AYAVEDAGMEHRDPYLRELGEPTYLVIDPRAEEEDEKGTAGGLLSSLEGLKMRPSLLMTR
YLESWGAAKPFAHLSHGDSPVSTSTPLPEKTLASFSTQWSLDRSRTPRGLDDELDTGDAK
FFQVIEQLNSQKQWKQSKDFNPLTLYFREKEMEKEYRLSAIPAFKYYEACTFLVFLSNFI
IQMLVTNRPPALAITYSITFLLFLLILFVCFSEDLMRCVLKGPKMLHWLPALSGLVATRP
GLRIALGTATILLVFAMAITSLFFFPTSSDCPFQAPNVSSMISNLSWELPGSLPLISVPY
SMHCCTLGFLSCSLFLHMSFELKLLLLLLWLAASCSLFLHSHAWLSECLIVRLYLGPLDS
RPGVLKEPKLMGAISFFIFFFTLLVLARQNEYYCRLDFLWKKKLRQEREETETMENLTRL
LLENVLPAHVAPQFIGQNRRNEDLYHQSYECVCVLFASVPDFKEFYSESNINHEGLECLR
LLNEIIADFDELLSKPKFSGVEKIKTIGSTYMAATGLNATSGQDAQQDAERSCSHLGTMV
EFAVALGSKLDVINKHSFNNFRLRVGLNHGPVVAGVIGAQKPQYDIWGNTVNVASRMEST
GVLGKIQVTEETAWALQSLGYTCYSRGVIKVKGKGQLCTYFLNTDLTRTGPPSATLG
Enzyme 59 Number of Residues 1077
Enzyme 59 Molecular Weight 119792.9
Enzyme 59 Theoretical pI 7.50
Enzyme 59 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 59 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 59 Specific Function This is a membrane-bound, calmodulin-insensitive adenylyl cyclase
Enzyme 59 Pathways
Enzyme 59 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 59 Pfam Domain Function
Enzyme 59 Signals
  • None
Enzyme 59 Transmembrane Regions
  • 29-50 61-80 94-117 120-138 141-162 170-190 586-607 611-633 664-687 715-736 744-764 791-807
Enzyme 59 Essentiality Not Available
Enzyme 59 GenBank ID Protein 22212709 Link Image
Enzyme 59 UniProtKB/Swiss-Prot ID Q8NFM4 Link Image
Enzyme 59 UniProtKB/Swiss-Prot Entry Name ADCY4_HUMAN Link Image
Enzyme 59 PDB ID Not Available
Enzyme 59 Cellular Location Not Available
Enzyme 59 Gene Sequence >3234 bp 
ATGGCCCGCCTCTTCAGCCCCCGGCCGCCCCCCAGCGAAGACCTCTTCTACGAGACCTAC
TACAGCCTGAGCCAGCAGTACCCGCTGCTGCTGCTGCTGCTGGGGATCGTGCTCTGTGCG
CTCGCGGCGCTGCTCGCAGTGGCCTGGGCCAGCGGCAGGGAGCTGACCTCAGACCCGAGC
TTCCTGACCACTGTGCTGTGCGCGCTGGGCGGCTTCTCGCTGCTGCTGGGCCTCGCTTCC
CGGGAGCAGCGACTGCAGCGCTGGACGCGTCCCCTGTCCGGCTTGGTATGGGTCGCGCTG
CTAGCGCTAGGCCACGCCTTCCTGTTCACCGGGGGCGTGGTGAGCGCCTGGGACCAGGTG
TCCTATTTTCTCTTCGTCATCTTCACGGCGTATGCCATGCTGCCCTTGGGCATGCGGGAC
GCCGCCGTCGCGGGCCTCGCCTCCTCACTCTCGCATCTGCTGGTCCTCGGGCTGTATCTT
GGGCCACAGCCGGACTCACGGCCTGCACTGCTGCCGCAGTTGGCAGCAAACGCAGTGCTG
TTCCTGTGCGGGAACGTGGCAGGAGTGTACCACAAGGCGCTGATGGAGCGCGCCCTGCGG
GCCACGTTCCGGGAGGCACTCAGCTCCCTGCACTCACGCCGGCGGCTGGACACCGAGAAG
AAGCACCAGGAACACCTTCTCTTGTCCATCCTTCCTGCCTACCTGGCCCGAGAGATGAAG
GCAGAGATCATGGCACGGCTGCAGGCAGGACAGGGGTCACGGCCAGAGAGCACTAACAAT
TTCCACAGCCTCTATGTCAAGAGGCACCAGGGAGTCAGCGTGCTGTATGCTGACATCGTG
GGCTTCACGCGGCTGGCCAGCGAGTGTTCCCCTAAGGAGCTGGTGCTCATGCTCAATGAG
CTCTTTGGCAAGTTCGACCAGATTGCCAAGGAGCATGAATGCATGCGGATCAAGATCCTG
GGGGACTGTTACTACTGTGTCTCTGGGCTGCCACTCTCACTGCCAGACCATGCCATCAAC
TGCGTGCGCATGGGCCTGGACATGTGCCGGGCCATCAGGAAACTGCGGGCAGCCACTGGC
GTGGACATCAACATGCGTGTGGGCGTGCACTCAGGCAGCGTACTGTGTGGAGTCATCGGG
CTGCAGAAGTGGCAGTACGACGTTTGGTCACATGATGTCACACTGGCTAACCACATGGAG
GCAGGCGGTGTACCAGGGCGAGTGCACATCACAGGGGCTACCCTGGCCCTGCTGGCAGGG
GCTTATGCTGTGGAGGACGCAGGCATGGAGCATCGGGACCCCTACCTTCGGGAGCTAGGG
GAGCCTACCTATCTGGTCATCGATCCACGGGCAGAGGAGGAGGATGAGAAGGGCACTGCA
GGAGGCTTGCTGTCCTCGCTTGAGGGCCTCAAGATGCGTCCATCACTGCTGATGACCCGT
TACCTGGAGTCCTGGGGCGCAGCCAAGCCTTTTGCCCACCTGAGCCACGGAGACAGCCCT
GTGTCCACCTCCACCCCTCTCCCGGAGAAGACCCTGGCTTCCTTCAGCACCCAGTGGAGC
CTGGATCGGAGCCGTACCCCCCGGGGACTAGATGATGAACTGGACACCGGGGATGCCAAG
TTCTTCCAGGTCATTGAGCAGCTCAACTCGCAGAAACAGTGGAAGCAGTCGAAGGACTTC
AACCCACTGACACTGTACTTCAGAGAGAAGGAGATGGAGAAAGAGTACCGACTCTCTGCA
ATCCCCGCCTTCAAATACTATGAAGCCTGCACCTTCCTGGTTTTTCTCTCCAACTTCATC
ATCCAGATGCTAGTGACAAACAGGCCCCCAGCTCTGGCCATCACGTATAGCATCACCTTC
CTCCTCTTCCTCCTCATCCTTTTTGTCTGCTTCTCAGAGGACCTGATGAGGTGTGTCCTG
AAAGGCCCCAAGATGCTGCACTGGCTGCCTGCACTGTCTGGCCTGGTGGCCACACGACCA
GGACTGAGAATAGCCTTGGGCACCGCCACCATCCTCCTTGTCTTTGCCATGGCCATTACC
AGCCTGTTCTTCTTCCCAACATCATCAGACTGCCCTTTCCAAGCTCCCAATGTGTCCTCC
ATGATTTCCAACCTCTCCTGGGAGCTCCCTGGGTCTCTGCCTCTCATCAGTGTCCCATAC
TCCATGCACTGCTGCACGCTGGGCTTCCTCTCCTGCTCCCTCTTTCTGCACATGAGCTTC
GAGCTGAAGCTGCTGCTGCTCCTGCTGTGGCTGGCGGCATCCTGCTCCCTCTTCCTGCAC
TCCCATGCCTGGCTGTCGGAATGCCTCATCGTCCGCCTCTATCTGGGCCCCTTGGACTCC
AGGCCCGGAGTGCTGAAGGAGCCCAAACTGATGGGTGCTATCTCCTTCTTCATCTTCTTC
TTCACCCTCCTTGTCCTGGCTCGCCAGAATGAGTACTACTGCCGCCTGGACTTCCTGTGG
AAGAAGAAGCTGAGGCAGGAGAGGGAGGAGACAGAGACGATGGAGAACCTGACTCGGCTG
CTCTTGGAGAACGTGCTCCCTGCACACGTGGCCCCCCAGTTCATTGGCCAGAACCGGCGC
AACGAGGATCTCTACCACCAGTCCTATGAATGCGTTTGTGTCCTCTTCGCCTCAGTCCCA
GACTTCAAGGAGTTCTACTCTGAATCCAACATCAATCATGAGGGCCTAGAGTGTCTGAGG
CTGCTCAATGAGATAATTGCTGATTTTGATGAGCTGCTCTCCAAGCCCAAGTTCAGTGGG
GTGGAGAAGATCAAGACCATCGGCAGCACCTACATGGCAGCCACAGGCTTAAATGCCACC
TCTGGACAGGATGCACAACAGGATGCTGAACGGAGCTGCAGCCACCTTGGCACTATGGTG
GAATTTGCCGTGGCCCTGGGGTCTAAGCTGGACGTCATCAACAAGCATTCATTCAACAAC
TTCCGCCTGCGAGTGGGGTTGAACCATGGACCCGTAGTAGCTGGAGTTATTGGGGCCCAG
AAGCCGCAATATGACATTTGGGGCAACACAGTGAACGTGGCCAGCCGCATGGAGAGTACA
GGAGTCCTTGGCAAAATCCAAGTGACTGAGGAGACAGCATGGGCCCTACAGTCCCTGGGC
TACACCTGCTACAGCCGGGGTGTCATCAAGGTGAAAGGCAAAGGGCAGCTCTGCACCTAC
TTCCTGAACACAGACTTGACACGAACTGGACCTCCTTCAGCTACCCTAGGCTGA
Enzyme 59 GenBank Gene ID AF497516 Link Image
Enzyme 59 GeneCard ID ADCY4 Link Image
Enzyme 59 GenAtlas ID ADCY4 Link Image
Enzyme 59 HGNC ID HGNC:235 Link Image
Enzyme 59 Chromosome Location 1
Enzyme 59 Locus 14q12
Enzyme 59 SNPs SNPJam Report Link Image
Enzyme 59 General References
  1. Ludwig MG, Seuwen K: Characterization of the human adenylyl cyclase gene family: cDNA, gene structure, and tissue distribution of the nine isoforms. J Recept Signal Transduct Res. 2002 Feb-Nov;22(1-4):79-110. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 59 Metabolite References Not Available
Enzyme 60 [top]
Enzyme 60 ID 5979
Enzyme 60 Name Adenylate cyclase type 6
Enzyme 60 Synonyms
  1. ATP pyrophosphate-lyase 6
  2. Adenylate cyclase type VI
  3. Adenylyl cyclase 6
  4. Ca(2+)-inhibitable adenylyl cyclase
Enzyme 60 Gene Name ADCY6
Enzyme 60 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 60 Number of Residues 1168
Enzyme 60 Molecular Weight 130614.1
Enzyme 60 Theoretical pI 8.27
Enzyme 60 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 60 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 60 Specific Function Membrane-bound, calcium-inhibitable adenylyl cyclase
Enzyme 60 Pathways
Enzyme 60 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 60 Pfam Domain Function
Enzyme 60 Signals
  • None
Enzyme 60 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 60 Essentiality Not Available
Enzyme 60 GenBank ID Protein Not Available
Enzyme 60 UniProtKB/Swiss-Prot ID O43306 Link Image
Enzyme 60 UniProtKB/Swiss-Prot Entry Name ADCY6_HUMAN Link Image
Enzyme 60 PDB ID 1U0H Link Image
Enzyme 60 PDB File Show
Enzyme 60 3D Structure
Enzyme 60 Cellular Location Not Available
Enzyme 60 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 60 GenBank Gene ID AF250226 Link Image
Enzyme 60 GeneCard ID ADCY6 Link Image
Enzyme 60 GenAtlas ID ADCY6 Link Image
Enzyme 60 HGNC ID HGNC:237 Link Image
Enzyme 60 Chromosome Location 1
Enzyme 60 Locus 12q12-q13
Enzyme 60 SNPs SNPJam Report Link Image
Enzyme 60 General References
  1. Wicker R, Catalan AG, Cailleux A, Starenki D, Stengel D, Sarasin A, Suarez HG: Cloning and expression of human adenylyl cyclase type VI in normal thyroid tissues. Biochim Biophys Acta. 2000 Sep 7;1493(1-2):279-83. [PubMed Link Image]
  2. Ishikawa K, Nagase T, Nakajima D, Seki N, Ohira M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1997 Oct 31;4(5):307-13. [PubMed Link Image]
  3. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Hellevuo K, Yoshimura M, Kao M, Hoffman PL, Cooper DM, Tabakoff B: A novel adenylyl cyclase sequence cloned from the human erythroleukemia cell line. Biochem Biophys Res Commun. 1993 Apr 15;192(1):311-8. [PubMed Link Image]
  6. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  7. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 60 Metabolite References Not Available
Enzyme 61 [top]
Enzyme 61 ID 5980
Enzyme 61 Name Adenylate cyclase type 5
Enzyme 61 Synonyms
  1. ATP pyrophosphate-lyase 5
  2. Adenylate cyclase type V
  3. Adenylyl cyclase 5
Enzyme 61 Gene Name ADCY5
Enzyme 61 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 61 Number of Residues 1261
Enzyme 61 Molecular Weight 138906.4
Enzyme 61 Theoretical pI 7.25
Enzyme 61 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 61 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 61 Specific Function This is a membrane-bound, calcium-inhibitable adenylyl cyclase
Enzyme 61 Pathways
Enzyme 61 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 61 Pfam Domain Function
Enzyme 61 Signals
  • None
Enzyme 61 Transmembrane Regions
  • 196-216 242-262 268-288 299-319 325-345 374-394 770-790 792-812 836-856 910-930 935-955 984-1004
Enzyme 61 Essentiality Not Available
Enzyme 61 GenBank ID Protein 34486092 Link Image
Enzyme 61 UniProtKB/Swiss-Prot ID O95622 Link Image
Enzyme 61 UniProtKB/Swiss-Prot Entry Name ADCY5_HUMAN Link Image
Enzyme 61 PDB ID 1U0H Link Image
Enzyme 61 PDB File Show
Enzyme 61 3D Structure
Enzyme 61 Cellular Location Not Available
Enzyme 61 Gene Sequence >3786 bp 
ATGTCCGGCTCCAAAAGCGTGAGCCCCCCGGGCTACGCGGCGCAGAAGACTGCGGCGCCG
GCGCCCCGGGGAGGCCCCGAACACCGCTCTGCGTGGGGCGAGGCCGATTCCCGCGCGAAT
GGCTACCCCCATGCCCCCGGGGGCTCTGCCCGCGGCTCCACCAAGAAACCCGGGGGGGCG
GTGACCCCGCAGCAGCAGCAGCGCCTGGCCAGCCGCTGGCGCAGCGACGACGACGACGAT
CCTCCGCTGAGCGGTGACGACCCCCTGGCCGGGGGCTTCGGCTTCAGCTTCCGCTCCAAG
TCCGCCTGGCAGGAGCGCGGCGGCGACGACTGCGGTCGCGGCAGCCGCCGGCAGCGGCGG
GGCGCGGCCAGCGGGGGCAGCACCCGGGCGCCCCCTGCGGGCGGCGGCGGCGGCTCGGCG
GCGGCGGCTGCCTCGGCGGGCGGGACGGAGGTGCGCCCTCGCTCGGTGGAGGTGGGTCTG
GAGGAGCGGCGGGGCAAGGGGCGCGCGGCCGACGAGCTGGAGGCCGGCGCCGTCGAGGGC
GGCGAGGGGTCCGGGGATGGCGGCAGCTCGGCGGACTCGGGCTCGGGCGCGGGGCCCGGC
GCGGTGCTGTCCCTGGGCGCCTGCTGCCTGGCGTTGCTGCAGATATTCCGCTCCAAGAAG
TTCCCGTCGGACAAACTGGAGCGGCTGTACCAGCGCTACTTCTTCCGCCTGAACCAGAGC
AGCCTCACCATGCTCATGGCCGTGCTGGTGCTCGTGTGCCTGGTCATGTTGGCCTTCCAC
GCGGCGCGGCCCCCGCTCCAGCTGCCCTACCTGGCCGTGCTGGCGGCCGCCGTCGGCGTG
ATCCTCATCATGGCTGTGCTTTGCAACCGCGCCGCCTTCCACCAGGACCACATGGGCCTG
GCCTGCTATGCGCTCATCGCCGTGGTGCTGGCCGTCCAGGTGGTGGGCCTGCTGCTGCCG
CAGCCACGCAGCGCCTCTGAGGGCATCTGGTGGACCGTGTTCTTCATCTACACCATCTAC
ACGCTGCTGCCCGTGCGCATGCGGGCCGCAGTGCTCAGCGGGGTGCTCCTGTCCGCCCTC
CACCTGGCCATCGCCCTGCGCACCAACGCCCAGGACCAGTTCCTGCTGAAGCAGCTTGTC
TCCAATGTTCTCATTTTCTCCTGCACCAACATCGTGGGTGTCTGCACCCACTATCCGGCT
GAGGTCTCCCAGAGACAGGCTTTCCAGGAGACCCGAGAGTGCATCCAGGCGCGGCTCCAC
TCGCAGCGGGAGAACCAGCAGCAGGAACGGCTCCTGCTGTCTGTCCTTCCCCGTCATGTT
GCCATGGAGATGAAAGCAGACATCAACGCCAAGCAGGAGGATATGATGTTCCATAAGATT
TACATCCAGAAACATGACAACGTGAGCATCCTGTTTGCTGACATCGAGGGCTTCACCAGC
CTGGCGTCCCAGTGCACTGCACAGGAACTGGTCATGACCCTCAACGAGCTCTTCGCCCGC
TTTGACAAGCTGGCCGCAGAGAATCACTGTTTACGTATTAAGATCCTTGGGGATTGTTAT
TACTGCGTCTCGGGGCTGCCTGAAGCAAGGGCTGACCACGCCCACTGCTGTGTGGAGATG
GGCATGGACATGATCGAGGCCATCTCGTTGGTCCGGGAGGTGACAGGGGTGAACGTGAAC
ATGCGTGTGGGAATTCACAGCGGGCGAGTACACTGCGGTGTCCTTGGTCTCAGGAAGTGG
CAGTTCGACGTCTGGTCTAACGATGTCACGCTAGCCAACCACATGGAGGCTGGCGGCAAG
GCAGGACGCATCCACATCACCAAGGCTACACTCAACTACCTGAATGGGGACTACGAGGTG
GAGCCAGGCTGTGGGGGCGAGCGCAACGCCTACCTCAAGGAGCACAGTATCGAGACCTTC
CTCATCCTGCGCTGCACCCAGAAGCGGAAAGAAGAGAAGGCCATGATCGCCAAGATGAAC
CGCCAGAGAACCAACTCCATCGGGCACAACCCACCACACTGGGGGGCTGAGCGCCCCTTC
TACAACCACCTGGGTGGCAACCAGGTGTCCAAGGAGATGAAGCGGATGGGCTTTGAAGAC
CCCAAGGACAAGAACGCCCAGGAGAGTGCGAACCCTGAGGATGAAGTGGATGAGTTTCTG
GGCCGTGCCATTGACGCCAGGAGCATTGATAGGCTTCGGTCTGAGCACGTCCGCAAGTTC
CTCCTGACCTTCAGGGAGCCTGACTTAGAGAAGAAGTACTCCAAGCAGGTAGACGACCGA
TTTGGTGCCTATGTGGCGTGTGCCTCGCTCGTCTTCCTCTTCATCTGCTTTGTCCAGATC
ACCATCGTGCCCCACTCCATATTCATGCTCAGCTTCTACCTGACCTGTTCCCTGCTGCTG
ACCTTGGTGGTGTTTGTGTCTGTGATCTACTCCTGCGTAAAGCTCTTCCCCTCCCCACTG
CAGACCCTCTCCAGGAAGATCGTGCGGTCCAAGATGAACAGCACCCTGGTTGGGGTGTTC
ACCATCACCCTGGTGTTCCTGGCGGCTTTTGTCAACATGTTCACGTGCAACTCCAGGGAC
CTGCTGGGCTGCTTGGCACAGGAGCACAACATCAGCGCGAGCCAGGTCAACGCGTGTCAC
GTGGCGGAGTCGGCCGTCAACTACAGCCTGGGCGATGAGCAGGGCTTCTGTGGCAGCCCC
TGGCCCAACTGCAACTTCCCCGAGTACTTCACCTACAGCGTGCTGCTCAGCCTGCTGGCC
TGCTCCGTGTTCCTGCAGATCAGCTGCATCGGGAAGCTGGTGCTCATGCTGGCCATCGAG
CTCATCTACGTGCTCATCGTGGAGGTGCCAGGTGTCACGCTCTTCGACAACGCCGACCTG
CTGGTCACCGCCAACGCCATAGACTTCTTCAACAACGGGACCTCCCAGTGCCCTGAGCAT
GCAACCAAGGTGGCATTGAAGGTGGTGACGCCCATCATCATCTCAGTCTTTGTGCTGGCC
CTGTACCTGCACGCCCAGCAGGTGGAGTCCACTGCCCGCCTCGACTTCCTCTGGAAACTG
CAGGCCACAGAGGAGAAAGAGGAGATGGAGGAGCTGCAGGCCTACAACCGGCGGCTGCTG
CACAACATCCTGCCCAAGGACGTGGCCGCTCACTTCCTGGCCCGCGAGCGGCGCAATGAT
GAGCTCTACTATCAGTCCTGTGAGTGTGTGGCGGTCATGTTCGCCTCCATCGCCAACTTC
TCCGAGTTCTACGTTGAGCTGGAGGCCAACAACGAGGGTGTCGAGTGCCTGCGGCTACTC
AATGAGATCATCGCTGACTTTGATGAGATCATCAGCGAGGATCGGTTCCGGCAGCTGGAG
AAGATCAAGACCATCGGCAGCACCTACATGGCTGCCTCCGGCCTCAACGACTCTACCTAC
GACAAGGTGGGCAAGACCCACATCAAGGCACTGGCCGACTTTGCCATGAAGCTGATGGAC
CAGATGAAGTACATCAATGAGCACTCCTTCAACAACTTCCAGATGAAGATCGGGCTCAAC
ATCGGCCCCGTGGTGGCCGGGGTGATAGGGGCACGAAAGCCTCAGTACGACATCTGGGGC
AATACCGTGAACGTGGCCAGCCGCATGGACAGCACCGGTGTACCCGACCGCATCCAGGTC
ACCACAGACATGTACCAGGTGCTGGCTGCCAACACGTACCAGCTGGAGTGCCGGGGCGTG
GTCAAGGTCAAGGGCAAAGGCGAGATGATGACCTACTTCCTCAATGGAGGGCCCCCGCTC
AGTTAG
Enzyme 61 GenBank Gene ID NM_183357.1 Link Image
Enzyme 61 GeneCard ID ADCY5 Link Image
Enzyme 61 GenAtlas ID ADCY5 Link Image
Enzyme 61 HGNC ID HGNC:236 Link Image
Enzyme 61 Chromosome Location 3
Enzyme 61 Locus 3q13.2-q21
Enzyme 61 SNPs SNPJam Report Link Image
Enzyme 61 General References
  1. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  2. Ludwig MG, Seuwen K: Characterization of the human adenylyl cyclase gene family: cDNA, gene structure, and tissue distribution of the nine isoforms. J Recept Signal Transduct Res. 2002 Feb-Nov;22(1-4):79-110. [PubMed Link Image]
  3. Raimundo S, Giray J, Volff JN, Schwab M, Altenbuchner J, Ratge D, Wisser H: Cloning and sequence of partial cDNAs encoding the human type V and VI adenylyl cyclases and subsequent RNA-quantification in various tissues. Clin Chim Acta. 1999 Jul;285(1-2):155-61. [PubMed Link Image]
Enzyme 61 Metabolite References Not Available
Enzyme 62 [top]
Enzyme 62 ID 5981
Enzyme 62 Name Adenylate cyclase type 8
Enzyme 62 Synonyms
  1. ATP pyrophosphate-lyase 8
  2. Adenylate cyclase type VIII
  3. Adenylyl cyclase 8
  4. Ca(2+)/calmodulin-activated adenylyl cyclase
Enzyme 62 Gene Name ADCY8
Enzyme 62 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 62 Number of Residues 1251
Enzyme 62 Molecular Weight 140120.8
Enzyme 62 Theoretical pI 6.99
Enzyme 62 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 62 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 62 Specific Function This is a membrane-bound, calcium-stimulable adenylyl cyclase. May be involved in learning, in memory and in drug dependence
Enzyme 62 Pathways
Enzyme 62 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 62 Pfam Domain Function
Enzyme 62 Signals
  • None
Enzyme 62 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 62 Essentiality Not Available
Enzyme 62 GenBank ID Protein 516263 Link Image
Enzyme 62 UniProtKB/Swiss-Prot ID P40145 Link Image
Enzyme 62 UniProtKB/Swiss-Prot Entry Name ADCY8_HUMAN Link Image
Enzyme 62 PDB ID Not Available
Enzyme 62 Cellular Location Not Available
Enzyme 62 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 62 GenBank Gene ID Z35309 Link Image
Enzyme 62 GeneCard ID ADCY8 Link Image
Enzyme 62 GenAtlas ID ADCY8 Link Image
Enzyme 62 HGNC ID HGNC:239 Link Image
Enzyme 62 Chromosome Location 8
Enzyme 62 Locus 8q24
Enzyme 62 SNPs SNPJam Report Link Image
Enzyme 62 General References
  1. Defer N, Marinx O, Stengel D, Danisova A, Iourgenko V, Matsuoka I, Caput D, Hanoune J: Molecular cloning of the human type VIII adenylyl cyclase. FEBS Lett. 1994 Aug 29;351(1):109-13. [PubMed Link Image]
  2. Parma J, Stengel D, Gannage MH, Poyard M, Barouki R, Hanoune J: Sequence of a human brain adenylyl cyclase partial cDNA: evidence for a consensus cyclase specific domain. Biochem Biophys Res Commun. 1991 Aug 30;179(1):455-62. [PubMed Link Image]
  3. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 62 Metabolite References Not Available
Enzyme 63 [top]
Enzyme 63 ID 5982
Enzyme 63 Name Adenylate cyclase type 9
Enzyme 63 Synonyms
  1. ATP pyrophosphate-lyase 9
  2. Adenylate cyclase type IX
  3. Adenylyl cyclase 9
Enzyme 63 Gene Name ADCY9
Enzyme 63 Protein Sequence >Adenylate cyclase type 9 
MASPPHQQLLHHHSTEVSCDSSGDSNSVRVKINPKQLSSNSHPKHCKYSISSSCSSSGDS
GGVPRRVGGGGRLRRQKKLPQLFERASSRWWDPKFDSVNLEEACLERCFPQTQRRFRYAL
FYIGFACLLWSIYFAVHMRSRLIVMVAPALCFLLVCVGFFLFTFTKLYARHYAWTSLALT
LLVFALTLAAQFQVLTPVSGRGDSSNLTATARPTDTCLSQVGSFSMCIEVLFLLYTVMHL
PLYLSLCLGVAYSVLFETFGYHFRDEACFPSPGAGALHWELLSRGLLHGCIHAIGVHLFV
MSQVRSRSTFLKVGQSIMHGKDLEVEKALKERMIHSVMPRIIADDLMKQGDEESENSVKR
HATSSPKNRKKKSSIQKAPIAFRPFKMQQIEEVSILFADIVGFTKMSANKSAHALVGLLN
DLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPRADHAYCCIEMGLGMIKAIEQFCQEK
KEMVNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLD
DRYEMEDGKVIERLGQSVVADQLKGLKTYLISGQRAKESRCSCAEALLSGFEVIDGSQVS
SGPRGQGTASSGNVSDLAQTVKTFDNLKTCPSCGITFAPKSEAGAEGGAPQNGCQDEHKN
STKASGGPNPKTQNGLLSPPQEEKLTNSQTSLCEILQEKGRWAGVSLDQSALLPLRFKNI
REKTDAHFVDVIKEDSLMKDYFFKPPINQFSLNFLDQELERSYRTSYQEEVIKNSPVKTF
ASPTFSSLLDVFLSTTVFLTLSTTCFLKYEAATVPPPPAALAVFSAALLLEVLSLAVSIR
MVFFLEDVMACTKRLLEWIAGWLPRHCIGAILVSLPALAVYSHVTSEYETNIHFPVFTGS
AALIAVVHYCNFCQLSSWMRSSLATVVGAGPLLLLYVSLCPDSSVLTSPLDAVQNFSSER
NPCNSSVPRDLRRPASLIGQEVVLVFFLLLLLVWFLNREFEVSYRLHYHGDVEADLHRTK
IQSMRDQADWLLRNIIPYHVAEQLKVSQTYSKNHDSGGVIFASIVNFSEFYEENYEGGKE
CYRVLNELIGDFDELLSKPDYSSIEKIKTIGATYMAASGLNTAQAQDGSHPQEHLQILFE
FAKEMMRVVDDFNNNMLWFNFKLRVGFNHGPLTAGVIGTTKLLYDIWGDTVNIASRMDTT
GVECRIQVSEESYRVLSKMGYDFDYRGTVNVKGKGQMKTYLYPKCTDHRVIPQHQLSISP
DIRVQVDGSIGRSPTDEIANLVPSVQYVDKTSLGSDSSTQAKDAHLSPKRPWKEPVKAEE
RGRFGKAIEKDDCDETGIEEANELTKLNVSKSV
Enzyme 63 Number of Residues 1353
Enzyme 63 Molecular Weight 150699.4
Enzyme 63 Theoretical pI 7.35
Enzyme 63 GO Classification
Function
  • catalytic activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
—
Enzyme 63 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 63 Specific Function May play a fundamental role in situations where fine interplay between intracellular calcium and cAMP determines the cellular function. May be a physiologically relevant docking site for calcineurin
Enzyme 63 Pathways
Enzyme 63 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 63 Pfam Domain Function
Enzyme 63 Signals
  • None
Enzyme 63 Transmembrane Regions
  • 118-138 142-162 172-192 216-235 242-259 281-301 787-807 819-839 868-888 892-912 921-941 976-996
Enzyme 63 Essentiality Not Available
Enzyme 63 GenBank ID Protein 50959205 Link Image
Enzyme 63 UniProtKB/Swiss-Prot ID O60503 Link Image
Enzyme 63 UniProtKB/Swiss-Prot Entry Name ADCY9_HUMAN Link Image
Enzyme 63 PDB ID Not Available
Enzyme 63 Cellular Location Not Available
Enzyme 63 Gene Sequence >4062 bp 
ATGGCTTCCCCACCCCACCAGCAGCTGCTGCATCACCACAGCACCGAGGTGAGCTGCGAC
TCCAGCGGGGACAGCAACAGCGTGCGCGTCAAGATCAACCCCAAGCAGCTGTCCTCCAAC
AGCCACCCCAAGCACTGCAAATACAGCATCTCCTCTAGCTGCAGCAGCTCTGGGGACTCC
GGGGGCGTCCCCCGGCGAGTGGGCGGCGGAGGCCGGCTGCGCAGGCAGAAGAAGCTGCCC
CAGCTGTTCGAGAGGGCCTCCAGCCGCTGGTGGGACCCCAAGTTCGACTCGGTGAACCTG
GAGGAGGCCTGCCTGGAGCGCTGCTTCCCGCAGACCCAGCGCCGGTTCCGGTATGCGCTC
TTCTACATCGGCTTCGCCTGCCTTCTGTGGAGCATCTATTTTGCGGTCCACATGAGATCC
AGACTGATCGTCATGGTCGCCCCCGCGCTGTGCTTCCTCCTGGTGTGTGTGGGCTTCTTT
CTGTTTACCTTCACCAAGCTGTACGCCCGGCATTACGCGTGGACCTCGCTGGCTCTCACC
CTGCTGGTGTTCGCCCTGACCCTGGCTGCGCAGTTCCAGGTCTTGACGCCTGTCTCAGGA
CGCGGCGACAGCTCCAACCTTACGGCCACAGCCCGGCCCACAGATACTTGCTTATCTCAA
GTGGGGAGCTTCTCCATGTGCATCGAAGTGCTCTTTTTGCTCTATACCGTCATGCACTTA
CCTTTGTACCTGAGTTTGTGTCTGGGGGTGGCCTACTCTGTCCTTTTCGAGACCTTTGGC
TACCATTTCCGGGATGAAGCCTGCTTCCCCTCGCCCGGAGCCGGGGCCCTGCACTGGGAG
CTGCTGAGCAGGGGGCTGCTCCACGGCTGCATCCACGCCATCGGGGTCCACCTGTTCGTC
ATGTCCCAGGTGAGGTCCAGGAGCACCTTCCTCAAGGTGGGGCAATCCATTATGCACGGG
AAGGACCTGGAAGTGGAAAAAGCCCTCAAAGAGAGGATGATTCATTCCGTGATGCCAAGA
ATCATAGCCGATGACTTAATGAAGCAGGGAGATGAGGAGAGTGAGAATTCTGTCAAGAGG
CATGCCACCTCGAGCCCCAAGAACAGGAAGAAAAAGTCTTCCATCCAAAAAGCTCCTATA
GCCTTCCGCCCTTTTAAGATGCAGCAGATCGAAGAAGTCAGTATTTTATTTGCAGATATC
GTGGGCTTCACCAAGATGAGTGCCAACAAGTCTGCCCACGCCCTGGTGGGTCTCCTGAAC
GATCTGTTCGGTCGCTTCGACCGCCTGTGTGAGGAGACCAAGTGTGAGAAAATCAGCACC
CTGGGAGACTGTTACTACTGCGTGGCGGGCTGTCCCGAGCCCCGGGCCGACCATGCCTAC
TGCTGCATCGAGATGGGCCTGGGCATGATCAAGGCCATCGAGCAGTTCTGCCAGGAGAAG
AAGGAGATGGTGAACATGAGAGTCGGGGTGCACACGGGCACCGTCCTTTGCGGCATCCTG
GGCATGAGGAGGTTTAAATTTGACGTGTGGTCCAACGATGTGAACCTGGCCAATCTCATG
GAGCAGCTGGGAGTGGCCGGCAAAGTTCACATTTCTGAGGCCACCGCAAAATACTTAGAT
GACCGGTACGAAATGGAAGATGGGAAAGTTATTGAACGGCTGGGCCAGAGCGTGGTTGCT
GACCAGTTGAAAGGTTTGAAGACATACCTGATATCGGGTCAGAGAGCCAAGGAGTCTCGC
TGCAGCTGTGCAGAGGCCTTGCTTTCTGGCTTTGAGGTCATTGACGGCTCACAGGTGTCC
TCAGGCCCTAGGGGACAGGGGACAGCGTCATCAGGGAATGTCAGTGACTTGGCGCAGACT
GTCAAAACCTTTGATAACCTTAAGACCTGCCCTTCGTGCGGAATCACATTTGCTCCCAAA
TCTGAAGCCGGCGCCGAGGGAGGAGCACCTCAAAACGGCTGCCAAGACGAGCATAAAAAC
AGCACCAAGGCTTCTGGAGGACCTAATCCCAAAACTCAGAACGGGCTCCTCAGCCCTCCC
CAAGAGGAGAAGCTCACCAACAGTCAGACTTCTCTGTGTGAGATCTTGCAGGAGAAGGGA
AGGTGGGCAGGGGTGAGCCTGGACCAGTCGGCTCTCCTTCCGCTGAGGTTCAAGAACATC
CGGGAGAAAACGGACGCCCACTTTGTGGACGTTATCAAAGAAGACAGCCTGATGAAAGAT
TACTTTTTTAAGCCGCCCATTAATCAGTTCAGCCTGAACTTCCTGGATCAGGAGCTGGAG
CGATCCTACAGGACCAGCTATCAGGAAGAGGTCATAAAGAACTCCCCCGTGAAGACGTTT
GCTAGTCCCACCTTCAGCTCCCTCCTGGATGTGTTTCTGTCGACCACAGTGTTTCTGACG
CTGTCCACCACCTGCTTCCTGAAGTACGAGGCGGCCACCGTGCCTCCCCCGCCCGCCGCC
CTGGCGGTCTTCAGTGCAGCCCTGCTGCTGGAGGTGCTGTCCCTCGCGGTGTCCATCAGG
ATGGTGTTCTTCCTGGAGGACGTCATGGCCTGCACCAAGCGCCTGCTGGAGTGGATCGCC
GGCTGGCTACCACGTCACTGCATCGGGGCCATCCTGGTGTCGCTTCCCGCACTGGCCGTC
TACTCCCATGTCACCTCCGAATATGAGACCAACATACACTTCCCAGTGTTCACAGGCTCG
GCCGCGCTGATTGCCGTCGTGCACTACTGTAACTTCTGCCAGCTCAGCTCCTGGATGAGG
TCCTCCCTCGCCACCGTCGTGGGGGCCGGGCCGCTGCTCCTGCTCTACGTCTCCCTGTGC
CCAGACAGTTCTGTATTAACTTCGCCCCTTGACGCAGTACAGAATTTCAGTTCCGAGAGG
AACCCGTGCAATAGTTCGGTGCCGCGTGACCTCCGGCGGCCCGCCAGCCTCATCGGCCAG
GAGGTGGTTCTCGTCTTCTTTCTCCTGCTCTTGTTGGTCTGGTTCCTGAATCGCGAATTT
GAAGTCAGCTACCGCCTCCACTACCACGGAGACGTGGAAGCGGATCTTCACCGCACCAAG
ATCCAGAGCATGCGGGACCAGGCAGACTGGCTGCTGAGGAACATCATCCCCTACCACGTG
GCTGAGCAGCTGAAGGTGTCCCAGACCTACTCCAAGAACCATGACAGCGGAGGGGTGATC
TTCGCCAGCATCGTCAACTTCAGCGAGTTCTACGAGGAGAACTACGAGGGCGGCAAGGAG
TGCTACCGGGTCCTCAACGAGCTCATCGGGGACTTTGACGAGCTCCTAAGCAAGCCGGAC
TACAGCAGCATCGAGAAGATCAAGACCATCGGAGCCACGTACATGGCGGCGTCAGGGCTG
AACACCGCGCAGGCCCAGGACGGCAGCCACCCGCAGGAGCACCTGCAGATCCTGTTCGAG
TTCGCCAAGGAGATGATGCGCGTGGTGGACGACTTCAACAACAACATGCTGTGGTTCAAC
TTCAAGCTCCGCGTCGGCTTCAACCATGGGCCCCTCACGGCCGGGGTCATCGGCACCACC
AAGCTGCTGTACGACATCTGGGGAGACACCGTCAACATCGCCAGCAGGATGGACACCACC
GGCGTGGAGTGCCGCATCCAGGTGAGCGAAGAGAGCTACCGCGTCTTGAGCAAGATGGGC
TATGACTTCGACTACAGAGGGACCGTGAATGTCAAGGGGAAAGGCCAGATGAAGACCTAC
CTGTACCCAAAGTGCACGGATCACAGGGTCATCCCACAGCACCAGCTGTCCATCTCCCCA
GACATCCGCGTCCAGGTGGATGGCAGCATCGGACGGTCTCCCACAGACGAGATTGCCAAC
CTGGTGCCTTCTGTCCAGTATGTGGACAAGACATCTCTGGGTTCTGACAGCAGCACGCAG
GCCAAGGATGCCCACCTGTCCCCCAAGAGACCGTGGAAGGAGCCCGTCAAAGCCGAAGAA
AGGGGTCGATTTGGCAAAGCCATAGAGAAAGACGACTGTGACGAAACAGGAATAGAAGAA
GCCAACGAACTCACCAAGCTCAACGTTTCAAAGAGTGTGTGA
Enzyme 63 GenBank Gene ID NM_001116.3 Link Image
Enzyme 63 GeneCard ID ADCY9 Link Image
Enzyme 63 GenAtlas ID ADCY9 Link Image
Enzyme 63 HGNC ID HGNC:240 Link Image
Enzyme 63 Chromosome Location 1
Enzyme 63 Locus 16p13.3
Enzyme 63 SNPs SNPJam Report Link Image
Enzyme 63 General References
  1. Hacker BM, Tomlinson JE, Wayman GA, Sultana R, Chan G, Villacres E, Disteche C, Storm DR: Cloning, chromosomal mapping, and regulatory properties of the human type 9 adenylyl cyclase (ADCY9). Genomics. 1998 May 15;50(1):97-104. [PubMed Link Image]
  2. Small KM, Brown KM, Theiss CT, Seman CA, Weiss ST, Liggett SB: An Ile to Met polymorphism in the catalytic domain of adenylyl cyclase type 9 confers reduced beta2-adrenergic receptor stimulation. Pharmacogenetics. 2003 Sep;13(9):535-41. [PubMed Link Image]
  3. Tantisira KG, Small KM, Litonjua AA, Weiss ST, Liggett SB: Molecular properties and pharmacogenetics of a polymorphism of adenylyl cyclase type 9 in asthma: interaction between beta-agonist and corticosteroid pathways. Hum Mol Genet. 2005 Jun 15;14(12):1671-7. Epub 2005 May 6. [PubMed Link Image]
  4. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
  5. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 63 Metabolite References Not Available
Enzyme 64 [top]
Enzyme 64 ID 5983
Enzyme 64 Name Adenylate cyclase type 3
Enzyme 64 Synonyms
  1. ATP pyrophosphate-lyase 3
  2. Adenylate cyclase type III
  3. AC-III
  4. Adenylate cyclase, olfactive type
  5. Adenylyl cyclase 3
  6. AC3
Enzyme 64 Gene Name ADCY3
Enzyme 64 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 64 Number of Residues 1144
Enzyme 64 Molecular Weight 128958.9
Enzyme 64 Theoretical pI 6.55
Enzyme 64 GO Classification
Function
  • catalytic activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
—
Enzyme 64 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 64 Specific Function Mediates odorant detection (possibly) via modulation of intracellular cAMP concentration
Enzyme 64 Pathways
Enzyme 64 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 64 Pfam Domain Function
Enzyme 64 Signals
  • None
Enzyme 64 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 64 Essentiality Not Available
Enzyme 64 GenBank ID Protein 148536830 Link Image
Enzyme 64 UniProtKB/Swiss-Prot ID O60266 Link Image
Enzyme 64 UniProtKB/Swiss-Prot Entry Name ADCY3_HUMAN Link Image
Enzyme 64 PDB ID Not Available
Enzyme 64 Cellular Location Not Available
Enzyme 64 Gene Sequence >3435 bp 
ATGCCGAGGAACCAGGGCTTCTCCGAGCCCGAATACTCGGCCGAGTACTCAGCCGAGTAC
TCCGTCAGCCTGCCCTCCGACCCTGACCGCGGGGTGGGCCGGACCCATGAAATCTCGGTC
CGGAACTCGGGCTCCTGCCTGTGCCTGCCTCGCTTCATGCGGCTGACTTTCGTGCCGGAG
TCCTTGGAGAACCTCTACCAGACCTACTTCAAAAGGCAGCGCCACGAGACCCTGCTGGTG
CTGGTGGTCTTTGCAGCCCTCTTTGACTGCTACGTGGTGGTCATGTGTGCTGTGGTCTTC
TCCAGCGACAAGCTGGCTTCCCTCGCCGTGGCTGGAATTGGACTGGTGTTGGACATCATC
CTCTTCGTGCTCTGCAAAAAGGGGCTGCTCCCGGACCGGGTCACCCGCAGAGTGCTGCCC
TACGTGCTGTGGCTGCTCATAACCGCCCAGATCTTCTCCTACCTGGGCCTGAACTTCGCG
CGTGCCCACGCGGCTAGTGACACGGTGGGCTGGCAGGTCTTCTTTGTCTTCTCCTTCTTC
ATCACGCTGCCCCTCAGCCTCAGCCCCATCGTGATCATCTCCGTGGTCTCCTGTGTGGTG
CACACGTTGGTCCTGGGGGTCACCGTGGCCCAGCAGCAGCAGGAGGAGCTCAAGGGGATG
CAGCTGCTGCGGGAGATCCTGGCCAACGTCTTCCTCTACCTGTGCGCCATCGCTGTGGGC
ATCATGTCCTACTACATGGCTGACCGCAAGCACCGCAAGGCCTTCCTGGAGGCCCGCCAG
TCGCTGGAGGTGAAGATGAACCTGGAAGAGCAGAGCCAGCAGCAGGAGAACCTCATGCTT
TCCATCCTGCCCAAGCACGTGGCTGACGAGATGCTGAAAGACATGAAGAAAGACGAGAGC
CAGAAGGACCAGCAGCAGTTCAACACCATGTACATGTACCGTCACGAGAACGTCAGCATC
CTCTTTGCCGACATCGTGGGCTTTACCCAGCTGTCTTCTGCCTGCAGTGCCCAGGAGCTT
GTGAAGCTGCTCAACGAGCTCTTTGCCCGCTTTGACAAGCTGGCAGCTAAATACCACCAG
CTGCGGATTAAGATCCTGGGCGACTGCTACTACTGCATCTGCGGCTTGCCCGACTACCGG
GAGGACCACGCCGTCTGCTCCATCCTCATGGGGCTGGCCATGGTGGAGGCCATCTCGTAT
GTGCGGGAGAAGACCAAGACTGGGGTGGACATGCGTGTGGGGGTGCACACGGGCACCGTG
CTGGGGGGCGTCCTGGGCCAGAAGCGCTGGCAGTACGACGTGTGGTCGACTGATGTCACT
GTAGCCAACAAGATGGAGGCCGGCGGCATCCCTGGGCGCGTGCACATCTCCCAGAGCACC
ATGGACTGCCTGAAAGGGGAGTTTGATGTGGAGCCAGGCGATGGGGGCAGCCGCTGTGAT
TACCTAGAAGAGAAGGGTATTGAAACCTACCTCATCATTGCCTCCAAGCCAGAGGTGAAG
AAAACAGCCACCCAGAATGGCCTCAATGGCTCGGCCCTGCCCAATGGAGCACCAGCTTCC
TCAAAGTCCAGCTCCCCTGCCCTCATTGAGACCAAGGAGCCCAACGGGAGTGCCCACAGC
AGTGGGTCCACGTCGGAGAAGCCCGAGGAGCAGGATGCCCAGGCCGACAACCCCTCATTC
CCCAACCCACGCCGGAGGCTGCGCCTGCAGGACCTGGCTGACCGAGTGGTGGATGCCTCT
GAAGATGAGCACGAGCTCAACCAGCTGCTCAACGAGGCCCTGCTTGAGCGAGAGTCCGCC
CAAGTAGTAAAGAAGAGAAACACCTTCCTCTTGTCCATGCGGTTCATGGACCCCGAGATG
GAAACCCGCTACTCGGTGGAGAAGGAGAAGCAGAGTGGGGCTGCCTTCAGCTGCTCCTGC
GTCGTCCTGCTCTGCACGGCCCTGGTCGAGATACTCATCGACCCCTGGCTAATGACAAAC
TATGTGACCTTCATGGTGGGGGAGATTCTGCTCCTCATCCTGACCATCTGCTCCCTGGCT
GCCATCTTTCCCCGGGCCTTTCCTAAGAAGCTTGTGGCCTTCTCAACTTGGATTGACCGG
ACCCGCTGGGCCAGGAACACCTGGGCCATGCTCGCCATCTTCATCCTGGTGATGGCAAAT
GTCGTGGACATGCTCAGCTGTCTCCAGTACTACACGGGACCCAGCAATGCAACGGCAGGG
ATGGAAACGGAGGGCAGCTGCCTGGAGAACCCCAAGTATTACAACTATGTGGCCGTGCTG
TCCCTCATCGCCACCATCATGCTGGTGCAGGTCAGCCACATGGTGAAGCTCACGCTCATG
CTGCTCGTCGCAGGCGCCGTGGCCACCATCAACCTCTATGCCTGGCGTCCCGTCTTTGAT
GAATACGACCACAAGCGTTTTCGGGAGCACGACTTACCTATGGTGGCCTTAGAGCAGATG
CAAGGATTCAACCCTGGGCTCAATGGCACTGACAGGCTGCCCCTGGTGCCTTCCAAGTAC
TCTATGACGGTGATGGTGTTCCTCATGATGCTCAGCTTCTACTACTTCTCCCGCCACGTA
GAAAAACTGGCACGGACACTTTTCTTGTGGAAGATTGAGGTCCACGACCAGAAGGAACGT
GTCTATGAGATGCGACGCTGGAACGAGGCCTTGGTCACCAACATGTTGCCTGAGCACGTG
GCACGCCATTTCCTGGGGTCCAAGAAGAGAGATGAGGAGCTGTATAGCCAGACGTATGAT
GAGATTGGAGTCATGTTTGCCTCCCTGCCCAACTTTGCTGACTTCTACACAGAGGAGAGC
ATCAACAATGGTGGTATTGAGTGTCTGCGTTTCCTCAATGAAATCATCTCAGATTTTGAC
TCTCTCCTGGACAATCCCAAGTTCCGGGTGATCACCAAGATCAAAACCATTGGCAGCACG
TATATGGCGGCTTCAGGAGTCACCCCCGATGTCAACACCAATGGCTTTGCCAGCTCCAAC
AAGGAAGACAAGTCCGAGAGAGAGCGCTGGCAGCACCTGGCTGACCTGGCCGACTTCGCG
CTGGCCATGAAGGATACGCTCACCAACATCAACAACCAGTCCTTCAATAACTTCATGCTG
CGCATAGGCATGAACAAAGGCGGGGTTCTGGCTGGGGTCATCGGAGCCCGGAAACCACAC
TACGACATCTGGGGCAATACAGTCAATGTAGCCAGCAGGATGGAGTCCACGGGGGTCATG
GGCAACATTCAGGTGGTAGAAGAAACCCAAGTCATCCTCCGAGAGTACGGCTTCCGCTTT
GTGAGGCGAGGCCCCATCTTTGTGAAGGGGAAGGGGGAGCTGCTGACCTTCTTCTTGAAG
GGGCGGGATAAGCTAGCCACCTTCCCCAATGGCCCCTCTGTCACACTGCCCCACCAGGTG
GTGGACAACTCCTGA
Enzyme 64 GenBank Gene ID NM_004036.3 Link Image
Enzyme 64 GeneCard ID ADCY3 Link Image
Enzyme 64 GenAtlas ID ADCY3 Link Image
Enzyme 64 HGNC ID HGNC:234 Link Image
Enzyme 64 Chromosome Location 2
Enzyme 64 Locus 2p23.3
Enzyme 64 SNPs SNPJam Report Link Image
Enzyme 64 General References
  1. Yang B, He B, Abdel-Halim SM, Tibell A, Brendel MD, Bretzel RG, Efendic S, Hillert J: Molecular cloning of a full-length cDNA for human type 3 adenylyl cyclase and its expression in human islets. Biochem Biophys Res Commun. 1999 Jan 27;254(3):548-51. [PubMed Link Image]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
  5. Hellevuo K, Yoshimura M, Kao M, Hoffman PL, Cooper DM, Tabakoff B: A novel adenylyl cyclase sequence cloned from the human erythroleukemia cell line. Biochem Biophys Res Commun. 1993 Apr 15;192(1):311-8. [PubMed Link Image]
Enzyme 64 Metabolite References Not Available
Enzyme 65 [top]
Enzyme 65 ID 5984
Enzyme 65 Name Adenylate cyclase type 1
Enzyme 65 Synonyms
  1. ATP pyrophosphate-lyase 1
  2. Adenylate cyclase type I
  3. Adenylyl cyclase 1
  4. Ca(2+)/calmodulin-activated adenylyl cyclase
Enzyme 65 Gene Name ADCY1
Enzyme 65 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 65 Number of Residues 1119
Enzyme 65 Molecular Weight 123438.8
Enzyme 65 Theoretical pI 8.49
Enzyme 65 GO Classification
Function
  • catalytic activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
—
Enzyme 65 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 65 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 65 Pathways
Enzyme 65 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 65 Pfam Domain Function
Enzyme 65 Signals
  • None
Enzyme 65 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 65 Essentiality Not Available
Enzyme 65 GenBank ID Protein 31083193 Link Image
Enzyme 65 UniProtKB/Swiss-Prot ID Q08828 Link Image
Enzyme 65 UniProtKB/Swiss-Prot Entry Name ADCY1_HUMAN Link Image
Enzyme 65 PDB ID Not Available
Enzyme 65 Cellular Location Not Available
Enzyme 65 Gene Sequence >3360 bp 
ATGGCGGGGGCGCCGCGCGGCGGAGGCGGCGGCGGAGGCGGCGCGGGCGAGCCCGGGGGC
GCCGAGCGGGCGGCCGGGACAAGCCGCCGGCGCGGGCTCCGGGCGTGCGACGAGGAGTTC
GCTTGCCCAGAGCTGGAGGCGCTGTTCCGCGGCTACACGCTGCGGCTGGAGCAGGCGGCC
ACGCTGAAGGCGCTGGCCGTTCTCAGCCTGCTGGCGGGCGCGCTGGCGCTGGCCGAGCTG
CTGGGCGCGCCGGGGCCCGCGCCCGGCCTGGCCAAGGGCTCACACCCGGTGCACTGCGTC
CTCTTCCTGGCGCTGCTCGTGGTAACCAACGTCCGGTCCCTGCAGGTGCCCCAGCTGCAG
CAGGTCGGCCAGCTGGCGCTGCTCTTCAGCCTCACCTTCGCGCTGCTCTGCTGTCCTTTC
GCGCTGGGCGGCCCCGCCCGGGGTTCCGCCGGGGCCGCTGGGGGGCCAGCGACCGCCGAA
CAAGGGGTTTGGCAGCTCCTTTTGGTCACCTTCGTGTCCTATGCCTTGCTGCCCGTGCGC
AGCCTGCTGGCCATAGGCTTTGGGCTCGTGGTGGCTGCGTCGCACTTGCTGGTCACAGCC
ACCTTGGTCCCCGCCAAGCGCCCACGTCTCTGGAGGACGCTCGGTGCCAATGCCTTGCTC
TTCGTCGGTGTGAACATGTATGGGGTCTTTGTGCGGATTCTGACTGAGCGTTCACAGAGG
AAGGCGTTCCTGCAGGCCCGGAGCTGCATTGAGGACCGACTGAGGCTGGAGGATGAGAAC
GAGAAGCAGGAGCGGCTCCTCATGAGCCTCCTGCCCCGGAACGTTGCCATGGAGATGAAG
GAGGACTTCCTGAAGCCCCCTGAGAGGATTTTCCACAAGATTTACATCCAGAGGCACGAC
AATGTGAGCATCCTGTTTGCTGACATCGTGGGTTTCACGGGCTTGGCATCCCAGTGCACA
GCCCAGGAGCTGGTGAAACTCCTCAATGAGCTCTTCGGCAAGTTCGATGAATTAGCCACG
GAGAACCACTGTCGCCGCATCAAGATTCTCGGGGACTGCTACTACTGCGTGTCGGGCCTC
ACCCAGCCCAAGACTGACCATGCCCACTGCTGTGTGGAGATGGGACTCGACATGATTGAT
ACCATCACATCTGTGGCTGAAGCCACCGAGGTGGATCTGAACATGCGTGTGGGTCTGCAC
ACGGGCAGGGTCCTCTGTGGTGTCCTGGGCTTGCGCAAGTGGCAGTACGACGTGTGGTCC
AATGATGTGACCTTGGCCAATGTCATGGAAGCCGCTGGCCTGCCAGGGAAGGTTCATATC
ACAAAGACGACCCTAGCGTGCTTGAATGGGGACTACGAGGTAGAACCGGGTTACGGACAT
GAGAGGAACAGTTTCTTGAAAACTCATAACATCGAAACCTTTTTTATTGTGCCATCCCAT
CGCCGAAAGATATTTCCAGGCCTGATTCTCTCAGATATAAAACCGGCCAAAAGGATGAAG
TTCAAGACTGTCTGCTACCTGCTGGTGCAGCTCATGCACTGCCGGAAAATGTTCAAGGCC
GAGATCCCCTTCTCCAATGTCATGACCTGCGAGGACGATGACAAGCGGAGGGCATTAAGA
ACAGCCTCGGAAAAACTCAGAAACCGCTCATCTTTTTCTACCAACGTTGTCTACACCACC
CCGGGCACTCGCGTCAACAGGTACATCAGCCGCCTCTTAGAAGCCCGCCAGACAGAGCTG
GAGATGGCAGACCTGAACTTCTTTACCCTGAAGTACAAACATGTCGAACGGGAGCAAAAG
TACCACCAGCTTCAGGACGAGTATTTCACCAGCGCCGTTGTCCTCACCCTCATCCTGGCT
GCCTTATTTGGCCTTGTCTACCTTCTAATATTCCCACAGAGTGTGGTCGTCCTGCTCCTG
CTAGTATTCTGCATCTGCTTCCTGGTGGCCTGTGTCCTGTACCTGCACATCACCCGGGTC
CAGTGTTTTCCAGGGTGCCTGACGATTCAGATTCGCACTGTCCTGTGTATTTTCATAGTG
GTCTTAATCTACTCAGTAGCCCAAGGTTGTGTGGTGGGCTGCCTGCCTTGGGCCTGGAGC
TCCAAGCCCAACAGTTCCCTGGTGGTCCTTTCGTCTGGGGGCCAGCGCACAGCCCTGCCC
ACCCTGCCCTGCGAGTCTACACACCATGCCCTGCTCTGCTGCCTGGTGGGCACCCTCCCG
CTAGCCATATTTTTCCGGGTGTCCTCCTTGCCAAAAATGATCCTGCTCTCCGGGCTCACC
ACGTCCTACATCCTCGTTCTGGAGCTCAGCGGATACACCAGGACTGGGGGTGGTGCCGTC
TCCGGGCGCAGCTACGAGCCGATTGTGGCCATCCTGCTCTTCTCCTGTGCGCTGGCCCTG
CATGCCAGGCAGGTGGACATCAGGCTGAGGCTGGACTACCTCTGGGCCGCACAGGCAGAG
GAGGAGCGAGAGGACATGGAGAAGGTGAAGCTGGACAACAGGCGCATCCTCTTCAACCTC
CTGCCGGCCCACGTCGCCCAGCACTTCCTCATGTCCAACCCTCGGAACATGGACCTCTAC
TACCAGTCCTACTCCCAGGTGGGCGTCATGTTTGCCTCCATCCCCAACTTCAATGACTTC
TACATCGAGCTGGACGGCAACAACATGGGGGTGGAGTGTCTGCGGCTTCTCAACGAGATC
ATCGCCGACTTTGACGAGCTCATGGAAAAAGACTTTTACAAGGACATAGAGAAGATCAAG
ACCATCGGGAGCACCTACATGGCCGCTGTGGGGCTAGCGCCCACCTCGGGGACCAAGGCT
AAGAAGTCCATCTCCTCCCACCTGAGCACGCTGGCGGACTTTGCCATTGAGATGTTTGAC
GTTCTGGATGAAATCAACTACCAGTCTTACAACGACTTTGTCCTCCGAGTTGGCATCAAT
GTTGGCCCTGTGGTGGCTGGAGTGATTGGCGCTCGCAGGCCCCAGTACGACATCTGGGGA
AACACAGTCAACGTGGCCAGTCGGATGGATAGCACAGGGGTCCAGGGCAGAATCCAGGTG
ACTGAGGAAGTCCACCGGCTGCTGAGAAGGTGCCCCTACCACTTTGTGTGCCGAGGCAAA
GTCAGTGTCAAGGGCAAAGGCGAGATGTTGACATACTTTCTAGAAGGCAGGACTGATGGA
AACGGCTCCCAAATCAGGTCCCTGGGCTTGGATCGGAAAATGTGTCCATTTGGGAGAGCT
GGCCTTCAGGGCAGACGTCCCCCCGTGTGCCCCATGCCTGGCGTCTCAGTCAGGGCTGGG
CTCCCTCCACACTCCCCAGGCCAGTACCTGCCCTCTGCAGCAGCTGGGAAGGAGGCTTAG
Enzyme 65 GenBank Gene ID NM_021116.2 Link Image
Enzyme 65 GeneCard ID ADCY1 Link Image
Enzyme 65 GenAtlas ID ADCY1 Link Image
Enzyme 65 HGNC ID HGNC:232 Link Image
Enzyme 65 Chromosome Location 7
Enzyme 65 Locus 7p13-p12
Enzyme 65 SNPs SNPJam Report Link Image
Enzyme 65 General References
  1. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  2. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  3. Villacres EC, Xia Z, Bookbinder LH, Edelhoff S, Disteche CM, Storm DR: Cloning, chromosomal mapping, and expression of human fetal brain type I adenylyl cyclase. Genomics. 1993 May;16(2):473-8. [PubMed Link Image]
Enzyme 65 Metabolite References Not Available
Enzyme 66 [top]
Enzyme 66 ID 5986
Enzyme 66 Name Fumarylacetoacetase
Enzyme 66 Synonyms
  1. FAA
  2. Beta-diketonase
  3. Fumarylacetoacetate hydrolase
Enzyme 66 Gene Name FAH
Enzyme 66 Protein Sequence >Fumarylacetoacetase 
MSFIPVAEDSDFPIHNLPYGVFSTRGDPRPRIGVAIGDQILDLSIIKHLFTGPVLSKHQD
VFNQPTLNSFMGLGQAAWKEARVFLQNLLSVSQARLRDDTELRKCAFISQASATMHLPAT
IGDYTDFYSSRQHATNVGIMFRDKENALMPNWLHLPVGYHGRASSVVVSGTPIRRPMGQM
KPDDSKPPVYGACKLLDMELEMAFFVGPGNRLGEPIPISKAHEHIFGMVLMNDWSARDIQ
KWEYVPLGPFLGKSFGTTVSPWVVPMDALMPFAVPNPKQDPRPLPYLCHDEPYTFDINLS
VNLKGEGMSQAATICKSNFKYMYWTMLQQLTHHSVNGCNLRPGDLLASGTISGPEPENFG
SMLELSWKGTKPIDLGNGQTRKFLLDGDEVIITGYCQGDGYRIGFGQCAGKVLPALLPS
Enzyme 66 Number of Residues 419
Enzyme 66 Molecular Weight 46374.0
Enzyme 66 Theoretical pI 6.94
Enzyme 66 GO Classification
Function
  • catalytic activity
  • fumarylacetoacetase activity
  • hydrolase activity
  • hydrolase activity, acting on acid carbon-carbon bonds
  • hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
Process
  • aromatic amino acid family metabolic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid metabolic process
  • cellular metabolic process
  • metabolic process
Component
—
Enzyme 66 General Function Involved in fumarylacetoacetase activity
Enzyme 66 Specific Function 4-fumarylacetoacetate + H(2)O = acetoacetate + fumarate
Enzyme 66 Pathways
Enzyme 66 Reactions
  • 4-fumarylacetoacetate + H2O = acetoacetate + fumarate [RN:R01364]
Enzyme 66 Pfam Domain Function
Enzyme 66 Signals
  • None
Enzyme 66 Transmembrane Regions
  • None
Enzyme 66 Essentiality Not Available
Enzyme 66 GenBank ID Protein 182393 Link Image
Enzyme 66 UniProtKB/Swiss-Prot ID P16930 Link Image
Enzyme 66 UniProtKB/Swiss-Prot Entry Name FAAA_HUMAN Link Image
Enzyme 66 PDB ID 1QQJ Link Image
Enzyme 66 PDB File Show
Enzyme 66 3D Structure
Enzyme 66 Cellular Location Not Available
Enzyme 66 Gene Sequence >1260 bp 
ATGTCCTTCATCCCGGTGGCCGAGGATTCCGACTTCCCCATCCACAACCTGCCCTACGGC
GTCTTCTCGACCAGAGGCGACCCAAGACCGAGGATAGGTGTGGCCATTGGCGACCAGATC
CTGGACCTCAGCATCATCAAGCACCTCTTTACTGGTCCTGTCCTCTCCAAACACCAGGAT
GTCTTCAATCAGCCTACACTCAACAGCTTCATGGGCCTGGGTCAGGCTGCCTGGAAGGAG
GCGAGAGTGTTCTTGCAGAACTTGCTGTCTGTGAGCCAAGCCAGGCTCAGAGATGACACC
GAACTTCGGAAGTGTGCATTCATCTCCCAGGCTTCTGCCACGATGCACCTTCCAGCCACC
ATAGGAGACTACACAGACTTCTATTCCTCTCGGCAGCATGCTACCAACGTCGGAATCATG
TTCAGGGACAAGGAGAATGCGTTGATGCCAAATTGGCTGCACTTACCAGTGGGCTACCAT
GGCCGTGCCTCCTCTGTCGTGGTGTCTGGCACCCCAATCCGAAGGCCCATGGGACAGATG
AAACCTGATGACTCTAAGCCTCCCGTATATGGTGCCTGCAAGCTCTTGGACATGGAGCTG
GAAATGGCTTTTTTTGTAGGCCCTGGAAACAGATTGGGAGAGCCGATCCCCATTTCCAAG
GCCCATGAGCACATTTTTGGAATGGTCCTTATGAACGACTGGAGTGCACGAGACATTCAG
AAGTGGGAGTATGTCCCTCTCGGGCCATTCCTTGGGAAGAGTTTTGGGACCACTGTCTCT
CCGTGGGTGGTGCCCATGGATGCTCTCATGCCCTTTGCTGTGCCCAACCCGAAGCAGGAC
CCCAGGCCCCTGCCGTATCTGTGCCATGACGAGCCCTACACATTTGACATCAACCTCTCT
GTTAACCTGAAAGGAGAAGGAATGAGCCAGGCGGCTACCATATGCAAGTCCAATTTTAAG
TACATGTACTGGACGATGCTGCAGCAGCTCACTCACCACTCTGTCAACGGCTGCAACCTG
CGGCCGGGGGACCTCCTGGCTTCTGGGACCATCAGCGGGCCGGAGCCAGAAAACTTCGGC
TCCATGTTGGAACTGTCGTGGAAGGGAACGAAGCCCATAGACCTGGGGAATGGTCAGACC
AGGAAGTTTCTGCTGGACGGGGATGAAGTCATCATAACAGGGTACTGCCAGGGGGATGGT
TACCGCATCGGCTTTGGCCAGTGTGCTGGAAAAGTGCTGCCTGCTCTCCTGCCATCATGA
Enzyme 66 GenBank Gene ID M55150 Link Image
Enzyme 66 GeneCard ID FAH Link Image
Enzyme 66 GenAtlas ID FAH Link Image
Enzyme 66 HGNC ID HGNC:3579 Link Image
Enzyme 66 Chromosome Location 1
Enzyme 66 Locus 15q23-q25
Enzyme 66 SNPs SNPJam Report Link Image
Enzyme 66 General References
  1. Phaneuf D, Labelle Y, Berube D, Arden K, Cavenee W, Gagne R, Tanguay RM: Cloning and expression of the cDNA encoding human fumarylacetoacetate hydrolase, the enzyme deficient in hereditary tyrosinemia: assignment of the gene to chromosome 15. Am J Hum Genet. 1991 Mar;48(3):525-35. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Agsteribbe E, van Faassen H, Hartog MV, Reversma T, Taanman JW, Pannekoek H, Evers RF, Welling GM, Berger R: Nucleotide sequence of cDNA encoding human fumarylacetoacetase. Nucleic Acids Res. 1990 Apr 11;18(7):1887. [PubMed Link Image]
  5. Bergeron A, D'Astous M, Timm DE, Tanguay RM: Structural and functional analysis of missense mutations in fumarylacetoacetate hydrolase, the gene deficient in hereditary tyrosinemia type 1. J Biol Chem. 2001 May 4;276(18):15225-31. Epub 2001 Jan 22. [PubMed Link Image]
  6. St-Louis M, Tanguay RM: Mutations in the fumarylacetoacetate hydrolase gene causing hereditary tyrosinemia type I: overview. Hum Mutat. 1997;9(4):291-9. [PubMed Link Image]
  7. Phaneuf D, Lambert M, Laframboise R, Mitchell G, Lettre F, Tanguay RM: Type 1 hereditary tyrosinemia. Evidence for molecular heterogeneity and identification of a causal mutation in a French Canadian patient. J Clin Invest. 1992 Oct;90(4):1185-92. [PubMed Link Image]
  8. Labelle Y, Phaneuf D, Leclerc B, Tanguay RM: Characterization of the human fumarylacetoacetate hydrolase gene and identification of a missense mutation abolishing enzymatic activity. Hum Mol Genet. 1993 Jul;2(7):941-6. [PubMed Link Image]
  9. Grompe M, al-Dhalimy M: Mutations of the fumarylacetoacetate hydrolase gene in four patients with tyrosinemia, type I. Hum Mutat. 1993;2(2):85-93. [PubMed Link Image]
  10. Rootwelt H, Berger R, Gray G, Kelly DA, Coskun T, Kvittingen EA: Novel splice, missense, and nonsense mutations in the fumarylacetoacetase gene causing tyrosinemia type 1. Am J Hum Genet. 1994 Oct;55(4):653-8. [PubMed Link Image]
  11. Rootwelt H, Brodtkorb E, Kvittingen EA: Identification of a frequent pseudodeficiency mutation in the fumarylacetoacetase gene, with implications for diagnosis of tyrosinemia type I. Am J Hum Genet. 1994 Dec;55(6):1122-7. [PubMed Link Image]
  12. Rootwelt H, Chou J, Gahl WA, Berger R, Coskun T, Brodtkorb E, Kvittingen EA: Two missense mutations causing tyrosinemia type 1 with presence and absence of immunoreactive fumarylacetoacetase. Hum Genet. 1994 Jun;93(6):615-9. [PubMed Link Image]
  13. St-Louis M, Poudrier J, Phaneuf D, Leclerc B, Laframboise R, Tanguay RM: Two novel mutations involved in hereditary tyrosinemia type I. Hum Mol Genet. 1995 Feb;4(2):319-20. [PubMed Link Image]
  14. Hahn SH, Krasnewich D, Brantly M, Kvittingen EA, Gahl WA: Heterozygosity for an exon 12 splicing mutation and a W234G missense mutation in an American child with chronic tyrosinemia type 1. Hum Mutat. 1995;6(1):66-73. [PubMed Link Image]
  15. Ploos van Amstel JK, Bergman AJ, van Beurden EA, Roijers JF, Peelen T, van den Berg IE, Poll-The BT, Kvittingen EA, Berger R: Hereditary tyrosinemia type 1: novel missense, nonsense and splice consensus mutations in the human fumarylacetoacetate hydrolase gene; variability of the genotype-phenotype relationship. Hum Genet. 1996 Jan;97(1):51-9. [PubMed Link Image]
  16. Bergman AJ, van den Berg IE, Brink W, Poll-The BT, Ploos van Amstel JK, Berger R: Spectrum of mutations in the fumarylacetoacetate hydrolase gene of tyrosinemia type 1 patients in northwestern Europe and Mediterranean countries. Hum Mutat. 1998;12(1):19-26. [PubMed Link Image]
Enzyme 66 Metabolite References Not Available
Enzyme 67 [top]
Enzyme 67 ID 6069
Enzyme 67 Name Serine--pyruvate aminotransferase
Enzyme 67 Synonyms
  1. SPT
  2. Alanine--glyoxylate aminotransferase
  3. AGT
Enzyme 67 Gene Name AGXT
Enzyme 67 Protein Sequence >Serine--pyruvate aminotransferase 
MASHKLLVTPPKALLKPLSIPNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEI
KEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVGANGIWGQRAVDIGERIG
ARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLL
LVDSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSF
YLDIKWLANFWGCDDQPRMYHHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHG
RLQALGLQLFVKDPALRLPTVTTVAVPAGYDWRDIVSYVIDHFDIEIMGGLGPSTGKVLR
IGLLGCNATRENVDRVTEALRAALQHCPKKKL
Enzyme 67 Number of Residues 392
Enzyme 67 Molecular Weight 43009.5
Enzyme 67 Theoretical pI 8.55
Enzyme 67 GO Classification
Function
—
Process
  • metabolic process
Component
—
Enzyme 67 General Function Involved in metabolic process
Enzyme 67 Specific Function L-serine + pyruvate = 3-hydroxypyruvate + L- alanine
Enzyme 67 Pathways
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
Enzyme 67 Reactions
  • L-serine + pyruvate = 3-hydroxypyruvate + L-alanine [RN:R00585]
Enzyme 67 Pfam Domain Function
Enzyme 67 Signals
  • None
Enzyme 67 Transmembrane Regions
  • None
Enzyme 67 Essentiality Not Available
Enzyme 67 GenBank ID Protein 36582 Link Image
Enzyme 67 UniProtKB/Swiss-Prot ID P21549 Link Image
Enzyme 67 UniProtKB/Swiss-Prot Entry Name SPYA_HUMAN Link Image
Enzyme 67 PDB ID 1H0C Link Image
Enzyme 67 PDB File Show
Enzyme 67 3D Structure
Enzyme 67 Cellular Location Not Available
Enzyme 67 Gene Sequence >1179 bp 
ATGGCCTCTCACAAGCTGCTGGTGACCCCCCCCAAGGCCCTGCTCAAGCCCCTCTCCATC
CCCAACCAGCTCCTGCTGGGGCCTGGTCCTTCCAACCTGCCTCCTCGCATCATGGCAGCC
GGGGGGCTGCAGATGATCGGGTCCATGAGCAAGGATATGTACCAGATCATGGACGAGATC
AAGGAAGGCATCCAGTACGTGTTCCAGACCAGGAACCCACTCACACTGGTCATCTCTGGC
TCGGGACACTGTGCCCTGGAGGCCGCCCTGGTCAATGTGCTGGAGCCTGGGGACTCCTTC
CTGGTTGGGGCCAATGGCATTTGGGGGCAGCGAGCCGTGGACATCGGGGAGCGCATAGGA
GCCCGAGTGCACCCGATGACCAAGGACCCTGGAGGCCACTACACACTGCAGGAGGTGGAG
GAGGGCCTGGCCCAGCACAAGCCAGTGCTGCTGTTCTTAACCCACGGGGAGTCGTCCACC
GGCGTGCTGCAGCCCCTTGATGGCTTCGGGGAACTCTGCCACAGGTACAAGTGCCTGCTC
CTGGTGGATTCGGTGGCATCCCTGGGCGGGACCCCCCTTTACATGGACCGGCAAGGCATC
GACATCCTGTACTCGGGCTCCCAGAAGGCCCTGAACGCCCCTCCAGGGACCTCGCTCATC
TCCTTCAGTGACAAGGCCAAAAAGAAGATGTACTCCCGCAAGACGAAGCCCTTCTCCTTC
TACCTGGACATCAAGTGGCTGGCCAACTTCTGGGGCTGTGACGACCAGCCCAGGATGTAC
CATCACACAATCCCCGTCATCAGCCTGTACAGCCTGAGAGAGAGCCTGGCCCTCATTGCG
GAACAGGGCCTGGAGAACAGCTGGCGCCAGCACCGCGAGGCCGCGGCGTATCTGCATGGG
CGCCTGCAGGCACTGGGGCTGCAGCTCTTCGTGAAGGACCCGGCGCTCCGGCTTCCCACA
GTCACCACTGTGGCTGTACCCGCTGGCTATGACTGGAGAGACATCGTCAGCTACGTCATA
GACCACTTCGACATTGAGATCATGGGTGGCCTTGGGCCCTCCACGGGGAAGGTGCTGCGG
ATCGGCCTGCTGGGCTGCAATGCCACCCGCGAGAATGTGGACCGCGTGACGGAGGCCCTG
AGGGCGGCCCTGCAGCACTGCCCCAAGAAGAAGCTGTGA
Enzyme 67 GenBank Gene ID X56092 Link Image
Enzyme 67 GeneCard ID AGXT Link Image
Enzyme 67 GenAtlas ID AGXT Link Image
Enzyme 67 HGNC ID HGNC:341 Link Image
Enzyme 67 Chromosome Location 2
Enzyme 67 Locus 2q37.3
Enzyme 67 SNPs SNPJam Report Link Image
Enzyme 67 General References
  1. Nishiyama K, Berstein G, Oda T, Ichiyama A: Cloning and nucleotide sequence of cDNA encoding human liver serine-pyruvate aminotransferase. Eur J Biochem. 1990 Nov 26;194(1):9-18. [PubMed Link Image]
  2. Purdue PE, Takada Y, Danpure CJ: Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1. J Cell Biol. 1990 Dec;111(6 Pt 1):2341-51. [PubMed Link Image]
  3. Takada Y, Kaneko N, Esumi H, Purdue PE, Danpure CJ: Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon. Biochem J. 1990 Jun 1;268(2):517-20. [PubMed Link Image]
  4. Purdue PE, Lumb MJ, Fox M, Griffo G, Hamon-Benais C, Povey S, Danpure CJ: Characterization and chromosomal mapping of a genomic clone encoding human alanine:glyoxylate aminotransferase. Genomics. 1991 May;10(1):34-42. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Zhang X, Roe SM, Hou Y, Bartlam M, Rao Z, Pearl LH, Danpure CJ: Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1. J Mol Biol. 2003 Aug 15;331(3):643-52. [PubMed Link Image]
  9. Nishiyama K, Funai T, Katafuchi R, Hattori F, Onoyama K, Ichiyama A: Primary hyperoxaluria type I due to a point mutation of T to C in the coding region of the serine:pyruvate aminotransferase gene. Biochem Biophys Res Commun. 1991 May 15;176(3):1093-9. [PubMed Link Image]
  10. Purdue PE, Lumb MJ, Allsop J, Minatogawa Y, Danpure CJ: A glycine-to-glutamate substitution abolishes alanine:glyoxylate aminotransferase catalytic activity in a subset of patients with primary hyperoxaluria type 1. Genomics. 1992 May;13(1):215-8. [PubMed Link Image]
  11. Minatogawa Y, Tone S, Allsop J, Purdue PE, Takada Y, Danpur CJ, Kido R: A serine-to-phenylalanine substitution leads to loss of alanine:glyoxylate aminotransferase catalytic activity and immunoreactivity in a patient with primary hyperoxaluria type 1. Hum Mol Genet. 1992 Nov;1(8):643-4. [PubMed Link Image]
  12. Danpure CJ, Purdue PE, Fryer P, Griffiths S, Allsop J, Lumb MJ, Guttridge KM, Jennings PR, Scheinman JI, Mauer SM, et al.: Enzymological and mutational analysis of a complex primary hyperoxaluria type 1 phenotype involving alanine:glyoxylate aminotransferase peroxisome-to-mitochondrion mistargeting and intraperoxisomal aggregation. Am J Hum Genet. 1993 Aug;53(2):417-32. [PubMed Link Image]
  13. Danpure CJ: Primary hyperoxaluria type 1 and peroxisome-to-mitochondrion mistargeting of alanine:glyoxylate aminotransferase. Biochimie. 1993;75(3-4):309-15. [PubMed Link Image]
  14. von Schnakenburg C, Rumsby G: Primary hyperoxaluria type 1: a cluster of new mutations in exon 7 of the AGXT gene. J Med Genet. 1997 Jun;34(6):489-92. [PubMed Link Image]
  15. von Schnakenburg C, Rumsby G: Identification of new mutations in primary hyperoxaluria type 1 (PH1). J Nephrol. 1998 Mar-Apr;11 Suppl 1:15-7. [PubMed Link Image]
  16. Amoroso A, Pirulli D, Puzzer D, Ferri L, Crovella S, Ferrettini C, Marangella M, Mazzola G, Florian F: Gene symbol: AGXT. Disease: primary hyperoxaluria type I. Hum Genet. 1999 May;104(5):441. [PubMed Link Image]
  17. Pirulli D, Puzzer D, Ferri L, Crovella S, Amoroso A, Ferrettini C, Marangella M, Mazzola G, Florian F: Molecular analysis of hyperoxaluria type 1 in Italian patients reveals eight new mutations in the alanine: glyoxylate aminotransferase gene. Hum Genet. 1999 Jun;104(6):523-5. [PubMed Link Image]
  18. Rinat C, Wanders RJ, Drukker A, Halle D, Frishberg Y: Primary hyperoxaluria type I: a model for multiple mutations in a monogenic disease within a distinct ethnic group. J Am Soc Nephrol. 1999 Nov;10(11):2352-8. [PubMed Link Image]
  19. Basmaison O, Rolland MO, Cochat P, Bozon D: Identification of 5 novel mutations in the AGXT gene. Hum Mutat. 2000 Jun;15(6):577. [PubMed Link Image]
  20. Lumb MJ, Danpure CJ: Functional synergism between the most common polymorphism in human alanine:glyoxylate aminotransferase and four of the most common disease-causing mutations. J Biol Chem. 2000 Nov 17;275(46):36415-22. [PubMed Link Image]
  21. Coulter-Mackie MB, Tung A, Henderson HE, Toone JR, Applegarth DA: The AGT gene in Africa: a distinctive minor allele haplotype, a polymorphism (V326I), and a novel PH1 mutation (A112D) in Black Africans. Mol Genet Metab. 2003 Jan;78(1):44-50. [PubMed Link Image]
  22. Santana A, Salido E, Torres A, Shapiro LJ: Primary hyperoxaluria type 1 in the Canary Islands: a conformational disease due to I244T mutation in the P11L-containing alanine:glyoxylate aminotransferase. Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):7277-82. Epub 2003 May 30. [PubMed Link Image]
  23. van Woerden CS, Groothoff JW, Wijburg FA, Annink C, Wanders RJ, Waterham HR: Clinical implications of mutation analysis in primary hyperoxaluria type 1. Kidney Int. 2004 Aug;66(2):746-52. [PubMed Link Image]
  24. Monico CG, Olson JB, Milliner DS: Implications of genotype and enzyme phenotype in pyridoxine response of patients with type I primary hyperoxaluria. Am J Nephrol. 2005 Mar-Apr;25(2):183-8. Epub 2005 Apr 21. [PubMed Link Image]
  25. Frishberg Y, Rinat C, Shalata A, Khatib I, Feinstein S, Becker-Cohen R, Weismann I, Wanders RJ, Rumsby G, Roels F, Mandel H: Intra-familial clinical heterogeneity: absence of genotype-phenotype correlation in primary hyperoxaluria type 1 in Israel. Am J Nephrol. 2005 May-Jun;25(3):269-75. Epub 2005 Jun 15. [PubMed Link Image]
  26. Coulter-Mackie MB, Lian Q, Applegarth D, Toone J: The major allele of the alanine:glyoxylate aminotransferase gene: nine novel mutations and polymorphisms associated with primary hyperoxaluria type 1. Mol Genet Metab. 2005 Sep-Oct;86(1-2):172-8. Epub 2005 Jun 15. [PubMed Link Image]
Enzyme 67 Metabolite References Not Available
Enzyme 68 [top]
Enzyme 68 ID 6080
Enzyme 68 Name Transketolase-like protein 1
Enzyme 68 Synonyms
  1. Transketolase 2
  2. TK 2
  3. Transketolase-related protein
Enzyme 68 Gene Name TKTL1
Enzyme 68 Protein Sequence >Transketolase-like protein 1 
MADAEARAEFPEEARPDRGTLQVLQDMASRLRIHSIRATCSTSSGHPTSCSSSSEIMSVL
FFYIMRYKQSDPENPDNDRFVLAKRLSFVDVATGWLGQGLGVACGMAYTGKYFDRASYRV
FCLMSDGESSEGSVWEAMAFASYYSLDNLVAIFDVNRLGHSGALPAEHCINIYQRRCEAF
GWNTYVVDGRDVEALCQVFWQASQVKHKPTAVVAKTFKGRGTPSIEDAESWHAKPMPRER
ADAIIKLIESQIQTSRNLDPQPPIEDSPEVNITDVRMTSPPDYRVGDKIATRKACGLALA
KLGYANNRVVVLDGDTRYSTFSEIFNKEYPERFIECFMAEQNMVSVALGCASRGRTIAFA
STFAAFLTRAFDHIRIGGLAESNINIIGSHCGVSVGDDGASQMALEDIAMFRTIPKCTIF
YPTDAVSTEHAVALAANAKGMCFIRTTRPETMVIYTPQERFEIGQAKVLRHCVSDKVTVI
GAGITVYEALAAADELSKQDIFIRVIDLFTIKPLDVATIVSSAKATEGRIITVEDHYPQG
GIGEAVCAAVSMDPDIQVHSLAVSGVPQSGKSEELLDMYGISARHIIVAVKCMLLN
Enzyme 68 Number of Residues 596
Enzyme 68 Molecular Weight 65332.7
Enzyme 68 Theoretical pI 5.65
Enzyme 68 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
—
Enzyme 68 General Function Involved in catalytic activity
Enzyme 68 Specific Function Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate
Enzyme 68 Pathways
Enzyme 68 Reactions
  • sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate [RN:R01641]
Enzyme 68 Pfam Domain Function
Enzyme 68 Signals
  • None
Enzyme 68 Transmembrane Regions
  • None
Enzyme 68 Essentiality Not Available
Enzyme 68 GenBank ID Protein 158257954 Link Image
Enzyme 68 UniProtKB/Swiss-Prot ID P51854 Link Image
Enzyme 68 UniProtKB/Swiss-Prot Entry Name TKTL1_HUMAN Link Image
Enzyme 68 PDB ID Not Available
Enzyme 68 Cellular Location Not Available
Enzyme 68 Gene Sequence >1791 bp 
ATGGCGGATGCTGAGGCGAGGGCTGAGTTCCCGGAGGAGGCCAGACCTGACAGGGGCACC
TTGCAGGTGTTGCAAGATATGGCCAGCCGCTTGCGAATCCATTCCATCAGGGCCACATGC
TCCACGAGCTCCGGCCACCCTACATCATGTAGCAGTTCTTCTGAGATCATGTCTGTGCTG
TTCTTCTACATCATGAGGTACAAGCAGTCAGATCCAGAGAATCCGGACAACGACCGATTT
GTCCTCGCAAAGAGACTGTCGTTTGTGGATGTGGCAACAGGATGGCTCGGACAAGGACTG
GGAGTTGCATGTGGAATGGCATATACTGGCAAGTACTTCGACAGGGCCAGCTACCGGGTG
TTCTGCCTCATGAGTGATGGCGAGTCCTCAGAAGGCTCTGTCTGGGAGGCAATGGCCTTT
GCTTCCTACTACAGTCTGGACAATCTTGTGGCAATCTTTGATGTGAACCGCCTGGGACAC
AGTGGTGCATTGCCCGCCGAGCACTGCATAAACATCTATCAGAGGCGCTGCGAAGCCTTT
GGGTGGAACACTTATGTGGTGGACGGCCGGGACGTGGAGGCACTGTGCCAGGTATTCTGG
CAGGCTTCTCAGGTGAAGCACAAGCCCACTGCTGTGGTGGCCAAGACCTTCAAGGGCCGG
GGCACCCCAAGTATTGAGGATGCAGAAAGTTGGCATGCAAAGCCAATGCCGAGAGAAAGA
GCAGATGCCATTATCAAATTAATTGAGAGCCAGATACAGACCAGCAGGAATCTTGACCCA
CAGCCCCCCATTGAGGACTCACCTGAAGTCAACATCACAGATGTAAGGATGACCTCTCCA
CCTGATTACAGAGTTGGTGACAAGATAGCTACTCGGAAAGCATGCGGTCTGGCTCTGGCT
AAGCTGGGCTACGCGAACAACAGAGTCGTTGTGCTGGATGGTGACACCAGGTACTCTACT
TTCTCTGAGATATTCAACAAGGAGTACCCTGAGCGCTTCATCGAGTGCTTTATGGCTGAA
CAAAACATGGTGAGCGTGGCTCTGGGCTGTGCCTCCCGTGGACGGACCATTGCTTTTGCT
AGCACCTTTGCTGCCTTTCTGACTCGAGCATTTGATCACATCCGGATAGGAGGCCTCGCT
GAGAGCAACATCAACATTATTGGTTCCCACTGTGGGGTATCTGTTGGTGACGATGGTGCT
TCCCAGATGGCCCTGGAGGATATAGCCATGTTCCGAACCATTCCCAAGTGCACGATCTTC
TACCCAACTGATGCCGTCTCCACGGAGCATGCTGTTGCTCTGGCAGCCAATGCCAAGGGG
ATGTGCTTCATTCGGACCACCCGACCAGAAACTATGGTTATTTACACCCCACAAGAACGC
TTTGAGATCGGACAGGCCAAGGTCCTCCGCCACTGTGTCAGTGACAAGGTCACAGTTATT
GGAGCTGGAATTACTGTGTATGAAGCCTTAGCAGCTGCTGATGAGCTTTCGAAACAAGAT
ATTTTTATCCGTGTCATCGACCTGTTTACCATTAAACCTCTGGATGTCGCCACCATCGTC
TCCAGTGCAAAAGCCACAGAGGGCCGGATCATTACAGTGGAGGATCACTACCCGCAAGGT
GGCATCGGGGAAGCTGTCTGCGCAGCCGTCTCCATGGATCCTGACATTCAGGTTCATTCG
CTGGCAGTGTCGGGAGTGCCCCAGAGTGGGAAGTCCGAGGAATTGCTGGATATGTATGGA
ATTAGTGCCAGACATATCATAGTGGCCGTGAAATGCATGTTGCTGAACTAA
Enzyme 68 GenBank Gene ID AK292261 Link Image
Enzyme 68 GeneCard ID TKTL1 Link Image
Enzyme 68 GenAtlas ID TKTL1 Link Image
Enzyme 68 HGNC ID HGNC:11835 Link Image
Enzyme 68 Chromosome Location Not Available
Enzyme 68 Locus Not Available
Enzyme 68 SNPs SNPJam Report Link Image
Enzyme 68 General References
  1. Coy JF, Dubel S, Kioschis P, Thomas K, Micklem G, Delius H, Poustka A: Molecular cloning of tissue-specific transcripts of a transketolase-related gene: implications for the evolution of new vertebrate genes. Genomics. 1996 Mar 15;32(3):309-16. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Coy JF, Dressler D, Wilde J, Schubert P: Mutations in the transketolase-like gene TKTL1: clinical implications for neurodegenerative diseases, diabetes and cancer. Clin Lab. 2005;51(5-6):257-73. [PubMed Link Image]
  6. Langbein S, Zerilli M, Zur Hausen A, Staiger W, Rensch-Boschert K, Lukan N, Popa J, Ternullo MP, Steidler A, Weiss C, Grobholz R, Willeke F, Alken P, Stassi G, Schubert P, Coy JF: Expression of transketolase TKTL1 predicts colon and urothelial cancer patient survival: Warburg effect reinterpreted. Br J Cancer. 2006 Feb 27;94(4):578-85. [PubMed Link Image]
  7. Staiger WI, Coy JF, Grobholz R, Hofheinz RD, Lukan N, Post S, Schwarzbach MH, Willeke F: Expression of the mutated transketolase TKTL1, a molecular marker in gastric cancer. Oncol Rep. 2006 Oct;16(4):657-61. [PubMed Link Image]
Enzyme 68 Metabolite References Not Available
Enzyme 69 [top]
Enzyme 69 ID 6085
Enzyme 69 Name Transketolase
Enzyme 69 Synonyms
  1. TK
Enzyme 69 Gene Name TKT
Enzyme 69 Protein Sequence >Transketolase 
MESYHKPDQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKS
QDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLAEAELLNLRKISSDLDGHPVPKQAFTDV
ATGSLGQGLGAACGMAYTGKYFDKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDNLVA
ILDINRLGQSDPAPLQHQMDIYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKHQPTAIIA
KTFKGRGITGVEDKESWHGKPLPKNMAEQIIQEIYSQIQSKKKILATPPQEDAPSVDIAN
IRMPSLPSYKVGDKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFI
ECYIAEQNMVSIAVGCATRNRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVS
IGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFIRTSRPENAII
YNNNEDFQVGQAKVVLKSKDDQVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPL
DRKLILDSARATKGRILTVEDHYYEGGIGEAVSSAVVGEPGITVTHLAVNRVPRSGKPAE
LLKMFGIDRDAIAQAVRGLITKA
Enzyme 69 Number of Residues 623
Enzyme 69 Molecular Weight 67876.9
Enzyme 69 Theoretical pI 7.73
Enzyme 69 GO Classification
Function
  • catalytic activity
Process
  • metabolic process
Component
—
Enzyme 69 General Function Involved in catalytic activity
Enzyme 69 Specific Function Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate
Enzyme 69 Pathways
Enzyme 69 Reactions
  • sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate [RN:R01641]
Enzyme 69 Pfam Domain Function
Enzyme 69 Signals
  • None
Enzyme 69 Transmembrane Regions
  • None
Enzyme 69 Essentiality Not Available
Enzyme 69 GenBank ID Protein 158259931 Link Image
Enzyme 69 UniProtKB/Swiss-Prot ID P29401 Link Image
Enzyme 69 UniProtKB/Swiss-Prot Entry Name TKT_HUMAN Link Image
Enzyme 69 PDB ID Not Available
Enzyme 69 Cellular Location Not Available
Enzyme 69 Gene Sequence >1872 bp 
ATGGAGAGCTACCACAAGCCTGACCAGCAGAAGCTGCAGGCCTTGAAGGACACGGCCAAC
CGCCTACGTATCAGCTCCATCCAGGCCACCACTGCGGCGGGCTCTGGCCACCCCACGTCA
TGCTGCAGCGCCGCAGAGATCATGGCTGTCCTCTTTTTCCACACCATGCGCTACAAGTCC
CAGGACCCCCGGAATCCGCACAATGACCGCTTTGTGCTCTCCAAGGGCCATGCAGCTCCC
ATCCTCTACGCGGTCTGGGCTGAAGCTGGTTTCCTGGCCGAGGCGGAGCTGCTGAACCTG
AGGAAGATCAGCTCCGACTTGGACGGGCACCCGGTCCCGAAACAAGCTTTCACCGACGTG
GCCACTGGCTCCCTGGGCCAGGGCCTCGGGGCCGCTTGTGGGATGGCCTACACCGGCAAA
TACTTCGACAAGGCCAGCTACCGAGTCTATTGCTTGCTGGGAGACGGGGAGCTGTCAGAG
GGCTCTGTATGGGAGGCCATGGCCTTCGCCAGCATCTATAAGCTGGACAACCTTGTGGCC
ATTCTAGACATCAATCGCCTGGGCCAGAGTGACCCGGCCCCACTGCAGCACCAGATGGAC
ATCTACCAGAAGCGGTGCGAGGCCTTCGGTTGGCATGCCATCATCGTGGATGGACACAGC
GTGGAGGAGCTGTGCAAGGCCTTTGGCCAGGCCAAGCACCAGCCAACAGCCATCATTGCC
AAGACCTTCAAGGGCCGAGGGATCACGGGGGTAGAAGATAAGGAGTCTTGGCATGGGAAG
CCCCTCCCCAAAAACATGGCTGAGCAGATCATCCAGGAGATCTACAGCCAGATCCAGAGC
AAAAAGAAGATCCTGGCAACCCCTCCACAGGAGGACGCACCCTCAGTGGACATTGCCAAC
ATCCGCATGCCCAGCCTGCCCAGCTACAAAGTTGGGGACAAGATAGCCACCCGCAAGGCC
TACGGGCAGGCATTGGCCAAGCTGGGCCATGCCAGTGACCGCATCATCGCCCTGGATGGG
GACACCAAAAATTCCACCTTCTCGGAGATCTTCAAAAAGGAGCACCCGGACCGCTTCATC
GAGTGCTACATTGCTGAGCAGAACATGGTGAGCATCGCGGTGGGCTGTGCCACCCGCAAC
AGGACGGTGCCCTTCTGCAGCACTTTTGCAGCCTTCTTCACGCGGGCCTTTGACCAGATT
CGCATGGCCGCCATCTCCGAGAGCAACATCAACCTCTGCGGCTCCCACTGCGGCGTTTCC
ATCGGGGAAGACGGGCCCTCCCAGATGGCCCTAGAAGATCTGGCTATGTTTCGGTCAGTC
CCCACATCAACTGTCTTTTACCCAAGTGATGGCGTTGCTACAGAGAAGGCAGTGGAACTA
GCCGCCAATACAAAGGGTATCTGCTTCATCCGGACCAGCCGCCCAGAAAATGCCATCATC
TATAACAACAATGAGGACTTCCAGGTCGGACAAGCCAAGGTGGTCCTGAAGAGCAAGGAT
GACCAGGTGACCGTTATCGGGGCTGGGGTGACCCTGCACGAGGCCTTGGCCGCTGCCGAA
CTGCTGAAGAAAGAAAAGATCAACATCCGCGTGCTGGACCCCTTCACCATCAAGCCCCTG
GACAGAAAACTCATTCTCGACAGCGCTCGTGCCACCAAGGGCAGGATCCTCACCGTGGAG
GACCATTATTATGAAGGTGGCATTGGTGAGGCTGTGTCCAGTGCAGTAGTGGGCGAGCCT
GGCATCACTGTCACCCACCTGGCAGTTAACCGGGTACCAAGAAGTGGGAAGCCGGCTGAG
CTGCTGAAGATGTTTGGTATCGACAGGGATGCCATTGCACAAGCTGTGAGGGGCCTCATC
ACCAAGGCCTAG
Enzyme 69 GenBank Gene ID AK289454 Link Image
Enzyme 69 GeneCard ID TKT Link Image
Enzyme 69 GenAtlas ID TKT Link Image
Enzyme 69 HGNC ID HGNC:11834 Link Image
Enzyme 69 Chromosome Location 3
Enzyme 69 Locus 3p14.3
Enzyme 69 SNPs SNPJam Report Link Image
Enzyme 69 General References
  1. McCool BA, Plonk SG, Martin PR, Singleton CK: Cloning of human transketolase cDNAs and comparison of the nucleotide sequence of the coding region in Wernicke-Korsakoff and non-Wernicke-Korsakoff individuals. J Biol Chem. 1993 Jan 15;268(2):1397-404. [PubMed Link Image]
  2. Schenk G, Layfield R, Candy JM, Duggleby RG, Nixon PF: Molecular evolutionary analysis of the thiamine-diphosphate-dependent enzyme, transketolase. J Mol Evol. 1997 May;44(5):552-72. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  6. Abedinia M, Layfield R, Jones SM, Nixon PF, Mattick JS: Nucleotide and predicted amino acid sequence of a cDNA clone encoding part of human transketolase. Biochem Biophys Res Commun. 1992 Mar 31;183(3):1159-66. [PubMed Link Image]
  7. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  8. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  9. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed Link Image]
  10. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  11. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  12. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  13. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  14. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  15. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 69 Metabolite References Not Available
Enzyme 70 [top]
Enzyme 70 ID 6150
Enzyme 70 Name Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
Enzyme 70 Synonyms
  1. Mannosidase alpha class 1A member 2
  2. Processing alpha-1,2-mannosidase IB
  3. Alpha-1,2-mannosidase IB
Enzyme 70 Gene Name MAN1A2
Enzyme 70 Protein Sequence >Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB 
MTTPALLPLSGRRIPPLNLGPPSFPHHRATLRLSEKFILLLILSAFITLCFGAFFFLPDS
SKHKRFDLGLEDVLIPHVDAGKGAKNPGVFLIHGPDEHRHREEEERLRNKIRADHEKALE
EAKEKLRKSREEIRAEIQTEKNKVVQEMKIKENKPLPPVPIPNLVGIRGGDPEDNDIREK
REKIKEMMKHAWDNYRTYGWGHNELRPIARKGHSPNIFGSSQMGATIVDALDTLYIMGLH
DEFLDGQRWIEDNLDFSVNSEVSVFEVNIRFIGGLLAAYYLSGEEIFKIKAVQLAEKLLP
AFNTPTGIPWAMVNLKSGVGRNWGWASAGSSILAEFGTLHMEFIHLSYLTGDLTYYKKVM
HIRKLLQKMDRPNGLYPNYLNPRTGRWGQYHTSVGGLGDSFYEYLLKAWLMSDKTDHEAR
KMYDDAIEAIEKHLIKKSRGGLTFIGEWKNGHLEKKMGHLACFAGGMFALGADGSRADKA
GHYLELGAEIARTCHESYDRTALKLGPESFKFDGAVEAVAVRQAEKYYILRPEVIETYWY
LWRFTHDPRYRQWGWEAALAIEKYCRVNGGFSGVKDVYSSTPTHDDVQQSFFLAETLKYL
YLLFSGDDLLPLDHWVFNTEAHPLPVLHLANTTLSGNPAVR
Enzyme 70 Number of Residues 641
Enzyme 70 Molecular Weight 73002.9
Enzyme 70 Theoretical pI 7.67
Enzyme 70 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • ion binding
  • mannosidase activity
  • mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
  • mannosyl-oligosaccharide mannosidase activity
  • metal ion binding
Process
—
Component
  • cell part
  • membrane
Enzyme 70 General Function Involved in mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
Enzyme 70 Specific Function Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2)
Enzyme 70 Pathways
Enzyme 70 Reactions
  • Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2 ALL_REAC (other) R05982(G) R06722(G)
Enzyme 70 Pfam Domain Function
Enzyme 70 Signals
  • None
Enzyme 70 Transmembrane Regions
  • 37-57
Enzyme 70 Essentiality Not Available
Enzyme 70 GenBank ID Protein Not Available
Enzyme 70 UniProtKB/Swiss-Prot ID O60476 Link Image
Enzyme 70 UniProtKB/Swiss-Prot Entry Name MA1A2_HUMAN Link Image
Enzyme 70 PDB ID Not Available
Enzyme 70 Cellular Location Not Available
Enzyme 70 Gene Sequence >1926 bp 
ATGACTACCCCAGCCCTGCTGCCCCTCTCTGGACGTAGGATACCACCTCTGAACCTGGGG
CCGCCTTCCTTCCCACATCACAGGGCTACCTTGAGACTTTCTGAGAAGTTTATTCTTCTC
CTTATTCTTAGTGCCTTCATCACTCTGTGTTTTGGGGCATTCTTTTTCCTTCCAGACTCT
TCAAAACACAAACGCTTTGATTTGGGTTTAGAAGATGTGTTAATTCCACATGTAGATGCC
GGTAAAGGGGCTAAAAACCCCGGAGTCTTCCTGATCCATGGACCCGATGAACATAGACAC
AGGGAAGAGGAAGAACGTCTGAGAAATAAAATTCGAGCTGATCATGAGAAGGCCTTGGAA
GAAGCAAAAGAAAAATTAAGAAAGTCAAGAGAGGAAATTCGAGCAGAAATTCAGACAGAG
AAAAATAAGGTAGTCCAAGAAATGAAGATAAAAGAGAACAAGCCACTGCCACCAGTCCCT
ATTCCCAACCTTGTAGGAATACGTGGTGGAGACCCAGAAGATAATGACATAAGAGAGAAA
AGGGAAAAAATTAAAGAGATGATGAAACATGCTTGGGATAACTATAGGACATATGGGTGG
GGACATAATGAACTCAGACCTATTGCAAGGAAAGGACACTCCCCTAACATATTTGGAAGT
TCACAAATGGGTGCTACCATAGTAGATGCTTTGGATACCCTTTATATCATGGGACTTCAT
GATGAATTCCTAGATGGGCAAAGATGGATTGAAGACAACCTTGATTTCAGTGTGAATTCA
GAGGTGTCTGTGTTTGAAGTCAACATTCGATTTATTGGAGGCCTACTTGCAGCATATTAC
CTATCAGGAGAGGAGATATTCAAGATTAAAGCAGTGCAATTGGCTGAGAAACTCCTTCCT
GCCTTTAACACACCTACTGGGATTCCTTGGGCAATGGTGAATTTGAAAAGTGGAGTAGGG
CGAAACTGGGGCTGGGCATCTGCAGGTAGCAGCATTCTGGCTGAATTTGGTACACTACAT
ATGGAGTTCATCCACCTCAGCTACTTGACAGGGGACCTGACTTACTACAAAAAGGTTATG
CACATTCGGAAACTACTTCAGAAAATGGATCGTCCAAATGGTCTTTATCCAAATTATTTG
AACCCCAGAACAGGGCGCTGGGGTCAGTATCATACATCTGTCGGTGGCCTGGGAGACAGT
TTTTATGAATACTTACTGAAAGCATGGTTGATGTCAGATAAAACAGACCATGAGGCAAGA
AAGATGTATGATGATGCTATTGAGGCTATAGAAAAACATCTTATTAAGAAGTCTCGTGGA
GGTCTTACCTTTATTGGAGAATGGAAGAATGGGCACTTGGAAAAAAAGATGGGGCATTTG
GCCTGCTTTGCTGGGGGAATGTTTGCACTAGGAGCAGATGGTTCCAGAGCAGATAAAGCT
GGTCATTATTTAGAGCTAGGGGCAGAAATTGCACGTACTTGTCATGAGTCATATGACAGA
ACTGCATTAAAGCTAGGTCCTGAATCATTCAAGTTTGATGGTGCAGTGGAGGCTGTGGCT
GTCCGGCAGGCTGAAAAGTATTATATCCTCCGTCCAGAAGTAATTGAAACCTATTGGTAC
CTATGGCGATTCACTCACGATCCAAGATACAGGCAGTGGGGCTGGGAAGCAGCACTGGCC
ATTGAAAAGTATTGCCGAGTTAATGGTGGGTTTTCTGGAGTCAAAGATGTATATTCCTCT
ACTCCTACACATGATGATGTACAGCAGAGCTTTTTTCTTGCTGAAACATTAAAATATTTG
TATCTGCTGTTCTCCGGTGATGACCTTTTACCTTTAGACCACTGGGTGTTTAATACAGAG
GCTCACCCTCTGCCTGTGTTACATTTAGCCAACACCACACTTTCAGGTAATCCTGCTGTT
CGATGA
Enzyme 70 GenBank Gene ID AF027156 Link Image
Enzyme 70 GeneCard ID MAN1A2 Link Image
Enzyme 70 GenAtlas ID MAN1A2 Link Image
Enzyme 70 HGNC ID HGNC:6822 Link Image
Enzyme 70 Chromosome Location 1
Enzyme 70 Locus 1p13
Enzyme 70 SNPs SNPJam Report Link Image
Enzyme 70 General References
  1. Tremblay LO, Campbell Dyke N, Herscovics A: Molecular cloning, chromosomal mapping and tissue-specific expression of a novel human alpha1,2-mannosidase gene involved in N-glycan maturation. Glycobiology. 1998 Jun;8(6):585-95. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 70 Metabolite References Not Available
Enzyme 71 [top]
Enzyme 71 ID 6151
Enzyme 71 Name Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
Enzyme 71 Synonyms
  1. ER alpha-1,2-mannosidase
  2. ER mannosidase 1
  3. ERMan1
  4. Man9GlcNAc2-specific-processing alpha-mannosidase
  5. Mannosidase alpha class 1B member 1
Enzyme 71 Gene Name MAN1B1
Enzyme 71 Protein Sequence >Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase 
MAACEGRRSGALGSSQSDFLTPPVGGAPWAVATTVVMYPPPPPPPHRDFISVTLSFGENY
DNSKSWRRRSCWRKWKQLSRLQRNMILFLLAFLLFCGLLFYINLADHWKALAFRLEEEQK
MRPEIAGLKPANPPVLPAPQKADTDPENLPEISSQKTQRHIQRGPPHLQIRPPSQDLKDG
TQEEATKRQEAPVDPRPEGDPQRTVISWRGAVIEPEQGTELPSRRAEVPTKPPLPPARTQ
GTPVHLNYRQKGVIDVFLHAWKGYRKFAWGHDELKPVSRSFSEWFGLGLTLIDALDTMWI
LGLRKEFEEARKWVSKKLHFEKDVDVNLFESTIRILGGLLSAYHLSGDSLFLRKAEDFGN
RLMPAFRTPSKIPYSDVNIGTGVAHPPRWTSDSTVAEVTSIQLEFRELSRLTGDKKFQEA
VEKVTQHIHGLSGKKDGLVPMFINTHSGLFTHLGVFTLGARADSYYEYLLKQWIQGGKQE
TQLLEDYVEAIEGVRTHLLRHSEPSKLTFVGELAHGRFSAKMDHLVCFLPGTLALGVYHG
LPASHMELAQELMETCYQMNRQMETGLSPEIVHFNLYPQPGRRDVEVKPADRHNLLRPET
VESLFYLYRVTGDRKYQDWGWEILQSFSRFTRVPSGGYSSINNVQDPQKPEPRDKMESFF
LGETLKYLFLLFSDDPNLLSLDAYVFNTEAHPLPIWTPA
Enzyme 71 Number of Residues 699
Enzyme 71 Molecular Weight 79579.2
Enzyme 71 Theoretical pI 7.80
Enzyme 71 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • ion binding
  • mannosidase activity
  • mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
  • mannosyl-oligosaccharide mannosidase activity
  • metal ion binding
Process
—
Component
  • cell part
  • membrane
Enzyme 71 General Function Involved in mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
Enzyme 71 Specific Function Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2)
Enzyme 71 Pathways
Enzyme 71 Reactions
  • Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2 ALL_REAC (other) R05982(G) R06722(G)
Enzyme 71 Pfam Domain Function
Enzyme 71 Signals
  • None
Enzyme 71 Transmembrane Regions
  • 85-105
Enzyme 71 Essentiality Not Available
Enzyme 71 GenBank ID Protein 218749883 Link Image
Enzyme 71 UniProtKB/Swiss-Prot ID Q9UKM7 Link Image
Enzyme 71 UniProtKB/Swiss-Prot Entry Name MA1B1_HUMAN Link Image
Enzyme 71 PDB ID 1X9D Link Image
Enzyme 71 PDB File Show
Enzyme 71 3D Structure
Enzyme 71 Cellular Location Not Available
Enzyme 71 Gene Sequence >2100 bp 
ATGGCTGCCTGCGAGGGCAGGAGAAGCGGAGCTCTCGGTTCCTCTCAGTCGGACTTCCTG
ACGCCGCCAGTGGGCGGGGCCCCTTGGGCCGTCGCCACCACTGTAGTCATGTACCCACCG
CCGCCGCCGCCGCCTCATCGGGACTTCATCTCGGTGACGCTGAGCTTTGGCGAGAACTAT
GACAACAGCAAGAGTTGGCGGCGGCGCTCGTGCTGGAGGAAATGGAAGCAACTGTCGAGA
TTGCAGCGGAATATGATTCTCTTCCTCCTTGCCTTTCTGCTTTTCTGTGGACTCCTCTTC
TACATCAACTTGGCTGACCATTGGAAAGCTCTGGCTTTCAGGCTAGAGGAAGAGCAGAAG
ATGAGGCCAGAAATTGCTGGGTTAAAACCAGCAAATCCACCCGTCTTACCAGCTCCTCAG
AAGGCGGACACCGACCCTGAGAACTTACCTGAGATTTCGTCACAGAAGACACAAAGACAC
ATCCAGCGGGGACCACCTCACCTGCAGATTAGACCCCCAAGCCAAGACCTGAAGGATGGG
ACCCAGGAGGAGGCCACAAAAAGGCAAGAAGCCCCTGTGGATCCCCGCCCGGAAGGAGAT
CCGCAGAGGACAGTCATCAGCTGGAGGGGAGCGGTGATCGAGCCTGAGCAGGGCACCGAG
CTCCCTTCAAGAAGAGCAGAAGTGCCCACCAAGCCTCCCCTGCCACCGGCCAGGACACAG
GGCACACCAGTGCATCTGAACTATCGCCAGAAGGGCGTGATTGACGTCTTCCTGCATGCA
TGGAAAGGATACCGCAAGTTTGCATGGGGCCATGACGAGCTGAAGCCTGTGTCCAGGTCC
TTCAGTGAGTGGTTTGGCCTCGGTCTCACACTGATCGACGCGCTGGACACCATGTGGATC
TTGGGTCTGAGGAAAGAATTTGAGGAAGCCAGGAAGTGGGTGTCGAAGAAGTTACACTTT
GAAAAGGACGTGGACGTCAACCTGTTTGAGAGCACGATCCGCATCCTGGGGGGGCTCCTG
AGTGCCTACCACCTGTCTGGGGACAGCCTCTTCCTGAGGAAAGCTGAGGATTTTGGAAAT
CGGCTAATGCCTGCCTTCAGAACACCATCCAAGATTCCTTACTCGGATGTGAACATCGGT
ACTGGAGTTGCCCACCCGCCACGGTGGACCTCCGACAGCACTGTGGCCGAGGTGACCAGC
ATTCAGCTGGAGTTCCGGGAGCTCTCCCGTCTCACAGGGGATAAGAAGTTTCAGGAGGCA
GTGGAGAAGGTGACACAGCACATCCACGGCCTGTCTGGGAAGAAGGATGGGCTGGTGCCC
ATGTTCATCAATACCCACAGTGGCCTCTTCACCCACCTGGGCGTATTCACGCTGGGCGCC
AGGGCCGACAGCTACTATGAGTACCTGCTGAAGCAGTGGATCCAGGGCGGGAAGCAGGAG
ACACAGCTGCTGGAAGACTACGTGGAAGCCATCGAGGGTGTCAGAACGCACCTGCTGCGG
CACTCCGAGCCCAGTAAGCTCACCTTTGTGGGGGAGCTTGCCCACGGCCGCTTCAGTGCC
AAGATGGACCACCTGGTGTGCTTCCTGCCAGGGACGCTGGCTCTGGGCGTCTACCACGGC
CTGCCCGCCAGCCACATGGAGCTGGCCCAGGAGCTCATGGAGACTTGTTACCAGATGAAC
CGGCAGATGGAGACGGGGCTGAGTCCCGAGATCGTGCACTTCAACCTTTACCCCCAGCCG
GGCCGTCGGGACGTGGAGGTCAAGCCAGCAGACAGGCACAACCTGCTGCGGCCAGAGACC
GTGGAGAGCCTGTTCTACCTGTACCGCGTCACAGGGGACCGCAAATACCAGGACTGGGGC
TGGGAGATTCTGCAGAGCTTCAGCCGATTCACACGGGTCCCCTCGGGTGGCTATTCTTCC
ATCAACAATGTCCAGGATCCTCAGAAGCCCGAGCCTAGGGACAAGATGGAGAGCTTCTTC
CTGGGGGAGACGCTCAAGTATCTGTTCTTGCTCTTCTCCGATGACCCAAACCTGCTCAGC
CTGGATGCCTACGTGTTCAACACCGAAGCCCACCCTCTGCCTATCTGGACCCCTGCCTAG
Enzyme 71 GenBank Gene ID NM_016219.3 Link Image
Enzyme 71 GeneCard ID MAN1B1 Link Image
Enzyme 71 GenAtlas ID MAN1B1 Link Image
Enzyme 71 HGNC ID HGNC:6823 Link Image
Enzyme 71 Chromosome Location 9
Enzyme 71 Locus 9q34
Enzyme 71 SNPs SNPJam Report Link Image
Enzyme 71 General References
  1. Tremblay LO, Herscovics A: Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis. Glycobiology. 1999 Oct;9(10):1073-8. [PubMed Link Image]
  2. Gonzalez DS, Karaveg K, Vandersall-Nairn AS, Lal A, Moremen KW: Identification, expression, and characterization of a cDNA encoding human endoplasmic reticulum mannosidase I, the enzyme that catalyzes the first mannose trimming step in mammalian Asn-linked oligosaccharide biosynthesis. J Biol Chem. 1999 Jul 23;274(30):21375-86. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Herscovics A, Romero PA, Tremblay LO: The specificity of the yeast and human class I ER alpha 1,2-mannosidases involved in ER quality control is not as strict previously reported. Glycobiology. 2002 Apr;12(4):14G-15G. [PubMed Link Image]
  7. Avezov E, Frenkel Z, Ehrlich M, Herscovics A, Lederkremer GZ: Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation. Mol Biol Cell. 2008 Jan;19(1):216-25. Epub 2007 Nov 14. [PubMed Link Image]
  8. Vallee F, Karaveg K, Herscovics A, Moremen KW, Howell PL: Structural basis for catalysis and inhibition of N-glycan processing class I alpha 1,2-mannosidases. J Biol Chem. 2000 Dec 29;275(52):41287-98. [PubMed Link Image]
  9. Karaveg K, Siriwardena A, Tempel W, Liu ZJ, Glushka J, Wang BC, Moremen KW: Mechanism of class 1 (glycosylhydrolase family 47) {alpha}-mannosidases involved in N-glycan processing and endoplasmic reticulum quality control. J Biol Chem. 2005 Apr 22;280(16):16197-207. Epub 2005 Feb 15. [PubMed Link Image]
Enzyme 71 Metabolite References Not Available
Enzyme 72 [top]
Enzyme 72 ID 6152
Enzyme 72 Name Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
Enzyme 72 Synonyms
  1. Man(9)-alpha-mannosidase
  2. Man9-mannosidase
  3. Mannosidase alpha class 1A member 1
  4. Processing alpha-1,2-mannosidase IA
  5. Alpha-1,2-mannosidase IA
Enzyme 72 Gene Name MAN1A1
Enzyme 72 Protein Sequence >Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA 
MPVGGLLPLFSSPAGGVLGGGLGGGGGRKGSGPAALRLTEKFVLLLVFSAFITLCFGAIF
FLPDSSKLLSGVLFHSSPALQPAADHKPGPGARAEDAAEGRARRREEGAPGDPEAALEDN
LARIRENHERALREAKETLQKLPEEIQRDILLEKKKVAQDQLRDKAPFRGLPPVDFVPPI
GVESREPADAAIREKRAKIKEMMKHAWNNYKGYAWGLNELKPISKGGHSSSLFGNIKGAT
IVDALDTLFIMEMKHEFEEAKSWVEENLDFNVNAEISVFEVNIRFVGGLLSAYYLSGEEI
FRKKAVELGVKLLPAFHTPSGIPWALLNMKSGIGRNWPWASGGSSILAEFGTLHLEFMHL
SHLSGNPIFAEKVMNIRTVLNKLEKPQGLYPNYLNPSSGQWGQHHVSVGGLGDSFYEYLL
KAWLMSDKTDLEAKKMYFDAVQAIETHLIRKSSSGLTYIAEWKGGLLEHKMGHLTCFAGG
MFALGADAAPEGMAQHYLELGAEIARTCHESYNRTFMKLGPEAFRFDGGVEAIATRQNEK
YYILRPEVMETYMYMWRLTHDPKYRKWAWEAVEALENHCRVNGGYSGLRDVYLLHESYDD
VQQSFFLAETLKYLYLIFSDDDLLPLEHWIFNSEAHLLPILPKDKKEVEIREE
Enzyme 72 Number of Residues 653
Enzyme 72 Molecular Weight 72967.9
Enzyme 72 Theoretical pI 6.44
Enzyme 72 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
  • ion binding
  • mannosidase activity
  • mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
  • mannosyl-oligosaccharide mannosidase activity
  • metal ion binding
Process
—
Component
  • cell part
  • membrane
Enzyme 72 General Function Involved in mannosyl-oligosaccharide 1,2-alpha-mannosidase activity
Enzyme 72 Specific Function Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2)
Enzyme 72 Pathways
Enzyme 72 Reactions
  • Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2 ALL_REAC (other) R05982(G) R06722(G)
Enzyme 72 Pfam Domain Function
Enzyme 72 Signals
  • None
Enzyme 72 Transmembrane Regions
  • 42-62
Enzyme 72 Essentiality Not Available
Enzyme 72 GenBank ID Protein 56202626 Link Image
Enzyme 72 UniProtKB/Swiss-Prot ID P33908 Link Image
Enzyme 72 UniProtKB/Swiss-Prot Entry Name MA1A1_HUMAN Link Image
Enzyme 72 PDB ID 1NXC Link Image
Enzyme 72 PDB File Show
Enzyme 72 3D Structure
Enzyme 72 Cellular Location Not Available
Enzyme 72 Gene Sequence >1962 bp 
ATGCCCGTGGGGGGCCTGTTGCCGCTCTTCAGCAGCCCCGCGGGCGGCGTCCTGGGCGGG
GGGCTCGGCGGCGGCGGTGGCAGGAAGGGGTCGGGCCCCGCCGCCCTCCGCCTGACGGAG
AAGTTCGTGCTGCTGCTGGTATTCAGCGCCTTCATCACGCTCTGCTTCGGGGCGATCTTC
TTCCTGCCAGACTCCTCCAAGCTGCTCAGCGGGGTCCTGTTCCACTCCAGCCCCGCCTTG
CAGCCGGCCGCCGACCACAAGCCCGGGCCCGGGGCGCGCGCCGAGGACGCGGCCGAGGGG
CGAGCCCGGCGCCGCGAGGAGGGGGCACCCGGGGACCCGGAGGCCGCCCTGGAGGACAAC
TTGGCCAGGATCCGCGAAAACCACGAGCGGGCTCTCAGGGAAGCCAAGGAGACCCTGCAG
AAGCTGCCCGAGGAGATCCAAAGAGACATCCTACTGGAGAAGAAGAAGGTGGCCCAGGAC
CAGCTGCGTGACAAGGCGCCGTTCAGAGGCCTGCCCCCGGTGGACTTCGTGCCCCCAATC
GGGGTGGAGAGCCGGGAGCCCGCCGACGCCGCCATCCGCGAGAAAAGGGCAAAGATCAAA
GAGATGATGAAACATGCTTGGAATAATTATAAAGGTTATGCCTGGGGATTAAATGAACTC
AAACCTATATCAAAAGGAGGCCATTCAAGCAGTTTGTTTGGTAACATCAAAGGAGCAACT
ATAGTAGATGCCCTGGATACACTTTTTATTATGGAAATGAAACATGAATTTGAAGAAGCA
AAATCATGGGTTGAAGAAAATTTAGATTTTAATGTGAATGCTGAAATTTCTGTCTTTGAA
GTAAATATACGCTTTGTTGGTGGACTACTCTCAGCCTACTATCTGTCTGGAGAAGAGATT
TTTCGAAAGAAAGCAGTGGAACTTGGGGTAAAATTGCTACCTGCATTTCATACTCCCTCT
GGAATACCTTGGGCATTGCTGAATATGAAAAGTGGTATTGGAAGGAACTGGCCCTGGGCC
TCTGGAGGCAGCAGTATTCTGGCAGAATTTGGAACCCTGCATTTGGAGTTTATGCACTTG
AGCCACTTATCAGGAAACCCCATCTTTGCTGAAAAGGTAATGAATATTCGAACAGTACTG
AACAAACTGGAAAAACCACAAGGCCTTTATCCTAACTATCTGAATCCCAGTAGTGGACAG
TGGGGTCAACATCATGTATCAGTTGGAGGACTTGGAGACAGCTTCTATGAGTATTTGCTG
AAGGCCTGGTTAATGTCTGACAAGACAGATCTGGAAGCTAAGAAGATGTATTTTGATGCT
GTTCAGGCTATCGAGACTCATTTGATCCGCAAGTCTAGCAGCGGACTAACTTATATCGCA
GAGTGGAAAGGGGGCCTCCTGGAGCACAAGATGGGCCACCTGACCTGCTTCGCGGGGGGC
ATGTTCGCACTCGGGGCTGATGCAGCTCCCGAAGGCATGGCCCAACACTACCTTGAACTC
GGGGCTGAAATTGCCCGTACTTGTCATGAATCATATAATCGAACATTTATGAAACTGGGA
CCAGAAGCTTTCAGATTTGATGGTGGTGTTGAAGCCATCGCTACAAGACAAAATGAAAAA
TACTACATCTTACGGCCAGAAGTTATGGAGACTTACATGTATATGTGGAGACTGACTCAT
GATCCAAAGTACAGGAAATGGGCCTGGGAAGCCGTAGAGGCCTTGGAAAACCATTGCAGA
GTGAATGGAGGCTATTCAGGCCTAAGGGATGTTTACCTTCTTCATGAGAGTTATGATGAT
GTGCAGCAGAGTTTCTTCCTGGCAGAGACATTGAAATATTTGTACCTAATATTTTCTGAC
GACGATCTTCTTCCACTGGAGCATTGGATCTTCAATAGCGAGGCACATCTTCTCCCTATC
CTCCCTAAAGATAAAAAGGAAGTTGAAATCAGAGAGGAATAA
Enzyme 72 GenBank Gene ID AL022722 Link Image
Enzyme 72 GeneCard ID MAN1A1 Link Image
Enzyme 72 GenAtlas ID MAN1A1 Link Image
Enzyme 72 HGNC ID HGNC:6821 Link Image
Enzyme 72 Chromosome Location 6
Enzyme 72 Locus 6q22
Enzyme 72 SNPs SNPJam Report Link Image
Enzyme 72 General References
  1. 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]
  2. Bause E, Bieberich E, Rolfs A, Volker C, Schmidt B: Molecular cloning and primary structure of Man9-mannosidase from human kidney. Eur J Biochem. 1993 Oct 15;217(2):535-40. [PubMed Link Image]
  3. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 72 Metabolite References Not Available
Enzyme 73 [top]
Enzyme 73 ID 6159
Enzyme 73 Name Ectonucleoside triphosphate diphosphohydrolase 4
Enzyme 73 Synonyms
  1. NTPDase 4
  2. Lysosomal apyrase-like protein of 70 kDa
  3. Uridine-diphosphatase
  4. UDPase
Enzyme 73 Gene Name ENTPD4
Enzyme 73 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 4 
MGRIGISCLFPASWHFSISPVGCPRILNTNLRQIMVISVLAAAVSLLYFSVVIIRNKYGR
LTRDKKFQRYLARVTDIEATDTNNPNVNYGIVVDCGSSGSRVFVYCWPRHNGNPHDLLDI
RQMRDKNRKPVVMKIKPGISEFATSPEKVSDYISPLLNFAAEHVPRAKHKETPLYILCTA
GMRILPESQQKAILEDLLTDIPVHFDFLFSDSHAEVISGKQEGVYAWIGINFVLGRFEHI
EDDDEAVVEVNIPGSESSEAIVRKRTAGILDMGGVSTQIAYEVPKTVSFASSQQEEVAKN
LLAEFNLGCDVHQTEHVYRVYVATFLGFGGNAARQRYEDRIFANTIQKNRLLGKQTGLTP
DMPYLDPCLPLDIKDEIQQNGQTIYLRGTGDFDLCRETIQPFMNKTNETQTSLNGVYQPP
IHFQNSEFYGFSEFYYCTEDVLRMGGDYNAAKFTKAAKDYCATKWSILRERFDRGLYASH
ADLHRLKYQCFKSAWMFEVFHRGFSFPVNYKSLKTALQVYDKEVQWTLGAILYRTRFLPL
RDIQQEAFRASHTHWRGVSFVYNHYLFSGCFLVVLLAILLYLLRLRRIHRRTPRSSSAAA
LWMEEGLPAQNAPGTL
Enzyme 73 Number of Residues 616
Enzyme 73 Molecular Weight 70254.8
Enzyme 73 Theoretical pI 8.39
Enzyme 73 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 73 General Function Involved in hydrolase activity
Enzyme 73 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 73 Pathways
Enzyme 73 Reactions
  • a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
Enzyme 73 Pfam Domain Function
Enzyme 73 Signals
  • None
Enzyme 73 Transmembrane Regions
  • 34-54 560-580
Enzyme 73 Essentiality Not Available
Enzyme 73 GenBank ID Protein 4758662 Link Image
Enzyme 73 UniProtKB/Swiss-Prot ID Q9Y227 Link Image
Enzyme 73 UniProtKB/Swiss-Prot Entry Name ENTP4_HUMAN Link Image
Enzyme 73 PDB ID Not Available
Enzyme 73 Cellular Location Not Available
Enzyme 73 Gene Sequence >1851 bp 
ATGGGGAGGATTGGCATCTCCTGTCTTTTTCCTGCTTCTTGGCATTTTAGCATATCTCCA
GTAGGGTGTCCTCGAATTCTGAATACCAATTTACGCCAAATTATGGTCATTAGTGTCCTG
GCTGCTGCTGTTTCACTTTTATATTTTTCTGTTGTCATAATCCGAAATAAGTATGGGCGA
CTAACCAGAGACAAGAAATTTCAAAGGTACCTGGCACGAGTTACCGACATTGAAGCTACA
GACACCAATAACCCCAATGTGAACTATGGGATCGTGGTGGACTGTGGTAGCAGTGGGTCT
CGAGTATTTGTTTACTGCTGGCCAAGGCATAATGGCAATCCACATGATCTGTTGGATATC
AGGCAAATGAGGGATAAAAACCGAAAGCCAGTGGTCATGAAGATAAAACCGGGCATTTCA
GAATTTGCTACCTCTCCAGAGAAAGTCAGTGATTACATTTCTCCACTTTTGAACTTTGCT
GCAGAGCATGTGCCACGGGCAAAACACAAAGAGACACCTCTCTACATTCTCTGCACGGCT
GGAATGAGAATCCTCCCCGAAAGCCAGCAGAAAGCTATTCTGGAAGACCTTCTGACCGAT
ATCCCCGTGCACTTTGACTTTCTGTTTTCTGACTCTCATGCAGAAGTAATTTCTGGGAAA
CAAGAAGGTGTGTATGCTTGGATTGGCATTAATTTTGTCCTTGGACGATTTGAGCATATT
GAAGATGATGATGAGGCCGTTGTGGAAGTTAACATTCCTGGAAGTGAAAGCAGCGAAGCC
ATTGTCCGTAAAAGGACAGCGGGCATTCTCGACATGGGCGGCGTGTCGACTCAGATAGCG
TACGAAGTCCCCAAAACTGTAAGCTTTGCGTCCTCACAGCAGGAAGAAGTAGCTAAAAAC
TTGTTAGCTGAATTTAACTTGGGATGTGATGTTCACCAAACTGAGCATGTGTATCGAGTC
TATGTGGCCACGTTTCTTGGGTTTGGTGGCAATGCTGCTCGACAGAGATACGAAGACAGA
ATATTTGCCAACACCATTCAAAAGAACAGGCTCCTGGGTAAACAGACTGGTCTGACTCCT
GATATGCCGTACTTGGACCCCTGCCTACCCCTAGACATTAAAGATGAAATCCAGCAAAAT
GGACAAACCATATACCTACGAGGGACTGGAGACTTTGACCTGTGTCGAGAGACTATCCAG
CCTTTCATGAATAAAACAAACGAGACCCAGACTTCCCTCAATGGGGTCTACCAGCCCCCA
ATTCACTTCCAGAACAGTGAATTCTATGGCTTCTCCGAATTCTACTACTGCACCGAGGAT
GTGTTACGAATGGGGGGAGACTACAATGCTGCTAAATTTACTAAAGCTGCAAAGGATTAT
TGTGCAACAAAGTGGTCCATTTTGCGGGAACGCTTTGACCGAGGACTGTACGCCTCTCAT
GCTGACCTCCACAGGCTTAAGTATCAGTGCTTCAAATCGGCCTGGATGTTTGAGGTGTTT
CATAGGGGCTTTTCGTTTCCTGTCAACTATAAAAGCTTAAAGACTGCCTTGCAAGTTTAC
GACAAGGAGGTTCAGTGGACCCTTGGAGCCATCCTCTACAGGACCCGCTTTCTACCATTA
AGAGACATCCAGCAGGAGGCCTTCCGAGCCAGTCACACCCACTGGCGGGGCGTTTCCTTT
GTCTACAACCACTACCTGTTCTCTGGCTGCTTCCTGGTGGTGCTGCTGGCCATCCTGCTG
TACCTGCTGCGGCTGCGGCGCATCCACAGGCGCACTCCCCGGAGCAGCTCGGCCGCCGCC
CTCTGGATGGAGGAGGGCCTTCCCGCCCAGAATGCCCCGGGGACCTTGTGA
Enzyme 73 GenBank Gene ID NM_004901.3 Link Image
Enzyme 73 GeneCard ID ENTPD4 Link Image
Enzyme 73 GenAtlas ID ENTPD4 Link Image
Enzyme 73 HGNC ID HGNC:14573 Link Image
Enzyme 73 Chromosome Location 8
Enzyme 73 Locus 8p21.3
Enzyme 73 SNPs SNPJam Report Link Image
Enzyme 73 General References
  1. Wang TF, Guidotti G: Golgi localization and functional expression of human uridine diphosphatase. J Biol Chem. 1998 May 1;273(18):11392-9. [PubMed Link Image]
  2. Biederbick A, Rose S, Elsasser HP: A human intracellular apyrase-like protein, LALP70, localizes to lysosomal/autophagic vacuoles. J Cell Sci. 1999 Aug;112 ( Pt 15):2473-84. [PubMed Link Image]
  3. Biederbick A, Kosan C, Kunz J, Elsasser HP: First apyrase splice variants have different enzymatic properties. J Biol Chem. 2000 Jun 23;275(25):19018-24. [PubMed Link Image]
  4. Nagase T, Ishikawa K, Nakajima D, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1997 Apr 28;4(2):141-50. [PubMed Link Image]
  5. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
Enzyme 73 Metabolite References Not Available
Enzyme 74 [top]
Enzyme 74 ID 6160
Enzyme 74 Name Ectonucleoside triphosphate diphosphohydrolase 6
Enzyme 74 Synonyms
  1. NTPDase 6
  2. CD39 antigen-like 2
Enzyme 74 Gene Name ENTPD6
Enzyme 74 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 6 
MKKGIRYETSRKTSYIFQQPQHGPWQTRMRKISNHGSLRVAKVAYPLGLCVGVFIYVAYI
KWHRATATQAFFSITRAAPGARWGQQAHSPLGTAADGHEVFYGIMFDAGSTGTRVHVFQF
TRPPRETPTLTHETFKALKPGLSAYADDVEKSAQGIRELLDVAKQDIPFDFWKATPLVLK
ATAGLRLLPGEKAQKLLQKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITINFLTGSLK
TPGGSSVGMLDLGGGSTQIAFLPRVEGTLQASPPGYLTALRMFNRTYKLYSYSYLGLGLM
SARLAILGGVEGQPAKDGKELVSPCLSPSFKGEWEHAEVTYRVSGQKAAASLHELCAARV
SEVLQNRVHRTEEVKHVDFYAFSYYYDLAAGVGLIDAEKGGSLVVGDFEIAAKYVCRTLE
TQPQSSPFSCMDLTYVSLLLQEFGFPRSKVLKLTRKIDNVETSWALGAIFHYIDSLNRQK
SPAS
Enzyme 74 Number of Residues 484
Enzyme 74 Molecular Weight 53246.7
Enzyme 74 Theoretical pI 9.52
Enzyme 74 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 74 General Function Involved in hydrolase activity
Enzyme 74 Specific Function Might support glycosylation reactions in the Golgi apparatus and, when released from cells, might catalyze the hydrolysis of extracellular nucleotides. Hydrolyzes preferentially nucleoside 5'-diphosphates, nucleoside 5'-triphosphates are hydrolyzed only to a minor extent, there is no hydrolysis of nucleoside 5'-monophosphates. The order of activity with different substrates is GDP > IDP >> UDP = CDP >> ADP
Enzyme 74 Pathways
Enzyme 74 Reactions
  • a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
Enzyme 74 Pfam Domain Function
Enzyme 74 Signals
  • None
Enzyme 74 Transmembrane Regions
  • 40-60
Enzyme 74 Essentiality Not Available
Enzyme 74 GenBank ID Protein 3335098 Link Image
Enzyme 74 UniProtKB/Swiss-Prot ID O75354 Link Image
Enzyme 74 UniProtKB/Swiss-Prot Entry Name ENTP6_HUMAN Link Image
Enzyme 74 PDB ID Not Available
Enzyme 74 Cellular Location Not Available
Enzyme 74 Gene Sequence >1455 bp 
ATGAAAAAAGGTATCCGTTATGAAACTTCCAGAAAAACGAGCTACATTTTTCAGCAGCCG
CAGCACGGTCCTTGGCAAACAAGGATGAGAAAAATATCCAACCACGGGAGCCTGCGGGTG
GCGAAGGTGGCATACCCCCTGGGGCTGTGTGTGGGCGTGTTCATCTATGTTGCCTACATC
AAGTGGCACCGGGCCACCGCCACCCAGGCCTTCTTCAGCATCACCAGGGCAGCCCCGGGG
GCCCGGTGGGGTCAGCAGGCCCACAGCCCCCTGGGGACAGCTGCAGACGGGCACGAGGTC
TTCTACGGGATCATGTTTGATGCAGGAAGCACTGGCACCCGAGTACACGTCTTCCAGTTC
ACCCGGCCCCCCAGAGAAACTCCCACGTTAACCCACGAAACCTTCAAAGCAGTGAAGCCA
GGTCTTTCTGCCTATGCTGATGATGTTGAAAAGAGCGCTCAGGGAATCCGGGAACTACTG
GATGTTGCTAAACAGGACATTCCGTTCGACTTCTGGAAGGCCACCCCTCTGGTCCTCAAG
GCCACAGCTGGCTTACGCCTGTTACCTGGAGAAAAGGCCCAGAAGTTACTGCAGAAGGTG
AAAGAAGTATTTAAAGCATCGCCTTTCCTTGTAGGGGATGACTGTGTTTCCATCATGAAC
GGAACAGATGAAGGCGTTTCGGCGTGGATCACCATCAACTTCCTGACAGGCAGCTTGAAA
ACTCCAGGAGGGAGCAGCGTGGGCATGCTGGACTTGGGCGGAGGATCCACTCAGATCGCC
TTCCTGCCACGCGTGGAGGGCACCCTGCAGGCCTCCCCACCCGGCTACCTGACGGCACTG
CGGATGTTTAACAGGACCTACAAGCTCTATTCCTACAGCTACCTCGGGCTCGGGCTGATG
TCGGCACGCCTGGCGATCCTGGGCGGCGTGGAGGGGCAGCCTGCTAAGGATGGAAAGGAG
TTGGTCAGCCCTTGCTTGTCTCCCAGTTTCAAAGGAGAGTGGGAACACGCAGAAGTCACG
TACAGGGTTTCAGGGCAGAAAGCAGCGGCAAGCCTGCACGAGCTGTGTGCTGCCAGAGTG
TCAGAGGTCCTTCAAAACAGAGTGCACAGGACGGAGGAAGTGAAGCATGTGGACTTCTAT
GCTTTCTCCTACTATTACGACCTTGCAGCTGGTGTGGGCCTCATAGATGCGGAGAAGGGA
GGCAGCCTGGTGGTGGGGGACTTCGAGATCGCAGCCAAGTACGTGTGTCGGACCCTGGAG
ACACAGCCGCAGAGCAGCCCCTTCTCATGCATGGACCTCACCTACGTCAGCCTGCTACTC
CAGGAGTTCGGCTTTCCCAGGAGCAAAGTGCTGAAGCTCACTCGGAAAATTGACAATGTT
GAGACCAGCTGGGCTCTGGGGGCCATTTTTCATTACATCGACTCCCTGAACAGACAGAAG
AGTCCAGCCTCATAG
Enzyme 74 GenBank Gene ID AF039916 Link Image
Enzyme 74 GeneCard ID ENTPD6 Link Image
Enzyme 74 GenAtlas ID ENTPD6 Link Image
Enzyme 74 HGNC ID HGNC:3368 Link Image
Enzyme 74 Chromosome Location 2
Enzyme 74 Locus 20p11.21
Enzyme 74 SNPs SNPJam Report Link Image
Enzyme 74 General References
  1. Chadwick BP, Frischauf AM: The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster. Genomics. 1998 Jun 15;50(3):357-67. [PubMed Link Image]
  2. Ivanenkov VV, Murphy-Piedmonte DM, Kirley TL: Bacterial expression, characterization, and disulfide bond determination of soluble human NTPDase6 (CD39L2) nucleotidase: implications for structure and function. Biochemistry. 2003 Oct 14;42(40):11726-35. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Yeung G, Mulero JJ, McGowan DW, Bajwa SS, Ford JE: CD39L2, a gene encoding a human nucleoside diphosphatase, predominantly expressed in the heart. Biochemistry. 2000 Oct 24;39(42):12916-23. [PubMed Link Image]
  7. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed Link Image]
Enzyme 74 Metabolite References Not Available
Enzyme 75 [top]
Enzyme 75 ID 6161
Enzyme 75 Name Ectonucleoside triphosphate diphosphohydrolase 5
Enzyme 75 Synonyms
  1. NTPDase 5
  2. CD39 antigen-like 4
  3. ER-UDPase
  4. Nucleoside diphosphatase
Enzyme 75 Gene Name ENTPD5
Enzyme 75 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 5 
MATSWGTVFFMLVVSCVCSAVSHRNQQTWFEGIFLSSMCPINVSASTLYGIMFDAGSTGT
RIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHW
KKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTV
NFLTGQLHGHRQETVGTLDLGGASTQITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTH
SYLGFGLKAARLATLGALETEGTDGHTFRSACLPRWLEAEWIFGGVKYQYGGNQEGEVGF
EPCYAEVLRVVRGKLHQPEEVQRGSFYAFSYYYDRAVDTDMIDYEKGGILKVEDFERKAR
EVCDNLENFTSGSPFLCMDLSYITALLKDGFGFADSTVLQLTKKVNNIETGWALGATFHL
LQSLGISH
Enzyme 75 Number of Residues 428
Enzyme 75 Molecular Weight 47517.0
Enzyme 75 Theoretical pI 6.29
Enzyme 75 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 75 General Function Involved in hydrolase activity
Enzyme 75 Specific Function Likely to promote reglycosylation reactions involved in glycoproteins folding and quality control in the endoplasmic reticulum. Hydrolyzes UDP, GDP and IDP but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate
Enzyme 75 Pathways
Enzyme 75 Reactions
  • a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
Enzyme 75 Pfam Domain Function
Enzyme 75 Signals
  • 1-20
Enzyme 75 Transmembrane Regions
  • None
Enzyme 75 Essentiality Not Available
Enzyme 75 GenBank ID Protein 3335102 Link Image
Enzyme 75 UniProtKB/Swiss-Prot ID O75356 Link Image
Enzyme 75 UniProtKB/Swiss-Prot Entry Name ENTP5_HUMAN Link Image
Enzyme 75 PDB ID Not Available
Enzyme 75 Cellular Location Not Available
Enzyme 75 Gene Sequence >1287 bp 
ATGGCCACTTCTTGGGGCACAGTCTTTTTCATGCTGGTGGTATCCTGTGTTTGCAGCGCT
GTCTCCCACAGGAACCAGCAGACTTGGTTTGAGGGTATCTTCCTGTCTTCCATGTGCCCC
ATCAATGTCAGCGCCAGCACCTTGTATGGAATTATGTTTGATGCAGGGAGCACTGGAACT
CGAATTCATGTTTACACCTTTGTGCAGAAAATGCCAGGACAGCTTCCAATTCTAGAAGGG
GAAGTTTTTGATTCTGTGAAGCCAGGACTTTCTGCTTTTGTAGATCAACCTAAGCAGGGT
GCTGAGACCGTTCAAGGGCTCTTAGAGGTGGCCAAAGACTCAATCCCCCGAAGTCACTGG
AAAAAGACCCCAGTGGTCCTAAAGGCAACAGCAGGACTACGCTTACTGCCAGAACACAAA
GCCAAGGCTCTGCTCTTTGAGGTAAAGGAGATCTTCAGGAAGTCACCTTTCCTGGTACCA
AAGGGCAGTGTTAGCATCATGGATGGATCCGACGAAGGCATATTAGCTTGGGTTACTGTG
AATTTTCTGACAGGTCAGCTGCATGGCCACAGACAGGAGACTGTGGGGACCTTGGACCTA
GGGGGAGCCTCCACCCAAATCACGTTCCTGCCCCAGTTTGAGAAAACTCTGGAACAAACT
CCTAGGGGCTACCTCACTTCCTTTGAGATGTTTAACAGCACTTATAAGCTCTATACACAT
AGTTACTTGGGATTTGGATTGAAAGCTGCAAGACTAGCAACCCTGGGAGCCCTGGAGACA
GAAGGGACTGATGGGCACACTTTCCGGAGTGCCTGTTTACCGAGATGGTTGGAAGCAGAG
TGGATCTTTGGGGGTGTGAAATACCAGTATGGTGGCAACCAAGAAGGGGAGGTGGGCTTT
GAGCCCTGCTATGCCGAAGTGCTGAGGGTGGTACGAGGAAAACTTCACCAGCCAGAGGAG
GTCCAGAGAGGTTCCTTCTATGCTTTCTCTTACTATTATGACCGAGCTGTTGACACAGAC
ATGATTGATTATGAAAAGGGGGGTATTTTAAAAGTTGAAGATTTTGAAAGAAAAGCCAGG
GAAGTGTGTGATAACTTGGAAAACTTCACCTCAGGCAGTCCTTTCCTGTGCATGGATCTC
AGCTACATCACAGCCCTGTTAAAGGATGGCTTTGGCTTTGCAGACAGCACAGTCTTACAG
CTCACAAAGAAAGTGAACAACATAGAGACGGGCTGGGCCTTGGGGGCCACCTTTCACCTG
TTGCAGTCTCTGGGCATCTCCCATTGA
Enzyme 75 GenBank Gene ID AF039918 Link Image
Enzyme 75 GeneCard ID ENTPD5 Link Image
Enzyme 75 GenAtlas ID ENTPD5 Link Image
Enzyme 75 HGNC ID HGNC:3367 Link Image
Enzyme 75 Chromosome Location 1
Enzyme 75 Locus 14q24
Enzyme 75 SNPs SNPJam Report Link Image
Enzyme 75 General References
  1. Chadwick BP, Frischauf AM: The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster. Genomics. 1998 Jun 15;50(3):357-67. [PubMed Link Image]
  2. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  3. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
Enzyme 75 Metabolite References Not Available
Enzyme 76 [top]
Enzyme 76 ID 6203
Enzyme 76 Name ADP-ribosyl cyclase 2
Enzyme 76 Synonyms
  1. Bone marrow stromal antigen 1
  2. BST-1
  3. Cyclic ADP-ribose hydrolase 2
  4. cADPr hydrolase 2
  5. CD157 antigen
Enzyme 76 Gene Name BST1
Enzyme 76 Protein Sequence >ADP-ribosyl cyclase 2 
MAAQGCAASRLLQLLLQLLLLLLLLAAGGARARWRGEGTSAHLRDIFLGRCAEYRALLSP
EQRNKNCTAIWEAFKVALDKDPCSVLPSDYDLFINLSRHSIPRDKSLFWENSHLLVNSFA
DNTRRFMPLSDVLYGRVADFLSWCRQKNDSGLDYQSCPTSEDCENNPVDSFWKRASIQYS
KDSSGVIHVMLNGSEPTGAYPIKGFFADYEIPNLQKEKITRIEIWVMHEIGGPNVESCGE
GSMKVLEKRLKDMGFQYSCINDYRPVKLLQCVDHSTHPDCALKSAAAATQRKAPSLYTEQ
RAGLIIPLFLVLASRTQL
Enzyme 76 Number of Residues 318
Enzyme 76 Molecular Weight 35723.5
Enzyme 76 Theoretical pI 7.86
Enzyme 76 GO Classification
Function
  • NAD+ nucleosidase activity
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing N-glycosyl compounds
Process
  • metabolic process
Component
—
Enzyme 76 General Function Involved in NAD+ nucleosidase activity
Enzyme 76 Specific Function Synthesizes cyclic ADP-ribose, a second messenger that elicits calcium release from intracellular stores. May be involved in pre-B-cell growth
Enzyme 76 Pathways
  • Nicotinate and Nicotinamide Metabolism (map00760 Link Image)
Enzyme 76 Reactions
  • NAD+ + H2O = ADP-ribose + nicotinamide [RN:R00102]
Enzyme 76 Pfam Domain Function
Enzyme 76 Signals
  • 1-28
Enzyme 76 Transmembrane Regions
  • None
Enzyme 76 Essentiality Not Available
Enzyme 76 GenBank ID Protein 63991381 Link Image
Enzyme 76 UniProtKB/Swiss-Prot ID Q10588 Link Image
Enzyme 76 UniProtKB/Swiss-Prot Entry Name BST1_HUMAN Link Image
Enzyme 76 PDB ID 1ISM Link Image
Enzyme 76 PDB File Show
Enzyme 76 3D Structure
Enzyme 76 Cellular Location Not Available
Enzyme 76 Gene Sequence >957 bp 
ATGGCGGCCCAGGGGTGCGCGGCATCGCGGCTGCTCCAGCTGCTGCTGCAGCTTCTGCTT
CTACTGTTGCTGCTGGCGGCGGGCGGGGCGCGCGCGCGGTGGCGCGGGGAGGGCACCAGC
GCACACTTGCGGGACATCTTCCTGGGCCGCTGCGCCGAGTACCGCGCACTGCTGAGTCCC
GAGCAGCGGAACAAGAACTGCACAGCCATCTGGGAAGCCTTTAAAGTGGCGCTGGACAAG
GATCCCTGCTCCGTGCTGCCCTCAGACTATGACCTTTTTATTAACTTGTCCAGGCACTCT
ATTCCCAGAGATAAGTCCCTGTTCTGGGAAAATAGCCACCTCCTTGTTAACAGCTTTGCA
GACAACACCCGTCGTTTTATGCCCCTGAGCGATGTTCTGTATGGCAGGGTTGCAGATTTC
TTGAGCTGGTGTCGACAGAAAAATGACTCTGGACTCGATTACCAATCCTGCCCTACATCA
GAAGACTGTGAAAATAATCCTGTGGATTCCTTTTGGAAAAGGGCATCCATCCAGTATTCC
AAGGATAGTTCTGGGGTGATCCACGTCATGCTGAATGGTTCAGAGCCAACAGGAGCCTAT
CCCATCAAAGGTTTTTTTGCAGATTATGAAATTCCAAACCTCCAGAAGGAAAAAATTACA
CGAATCGAGATCTGGGTTATGCATGAAATTGGGGGACCCAATGTGGAATCCTGCGGGGAA
GGCAGCATGAAAGTCCTGGAAAAGAGGCTGAAGGACATGGGGTTCCAGTACAGCTGTATT
AATGATTACCGACCAGTGAAGCTCTTACAGTGCGTGGACCACAGCACCCATCCTGACTGT
GCCTTAAAGTCGGCAGCAGCCGCTACTCAAAGAAAAGCCCCAAGTCTTTATACAGAACAA
AGGGCGGGTCTTATCATTCCCCTCTTTCTGGTGCTGGCTTCCAGGACTCAACTGTAA
Enzyme 76 GenBank Gene ID AC114744 Link Image
Enzyme 76 GeneCard ID BST1 Link Image
Enzyme 76 GenAtlas ID BST1 Link Image
Enzyme 76 HGNC ID HGNC:1118 Link Image
Enzyme 76 Chromosome Location 4
Enzyme 76 Locus 4p15
Enzyme 76 SNPs SNPJam Report Link Image
Enzyme 76 General References
  1. Kaisho T, Ishikawa J, Oritani K, Inazawa J, Tomizawa H, Muraoka O, Ochi T, Hirano T: BST-1, a surface molecule of bone marrow stromal cell lines that facilitates pre-B-cell growth. Proc Natl Acad Sci U S A. 1994 Jun 7;91(12):5325-9. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  6. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  7. Yamamoto-Katayama S, Ariyoshi M, Ishihara K, Hirano T, Jingami H, Morikawa K: Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities. J Mol Biol. 2002 Feb 22;316(3):711-23. [PubMed Link Image]
Enzyme 76 Metabolite References Not Available
Enzyme 77 [top]
Enzyme 77 ID 6209
Enzyme 77 Name Adenylate cyclase type 2
Enzyme 77 Synonyms
  1. ATP pyrophosphate-lyase 2
  2. Adenylate cyclase type II
  3. Adenylyl cyclase 2
Enzyme 77 Gene Name ADCY2
Enzyme 77 Protein Sequence >Adenylate cyclase type 2 
MWQEAMRRRRYLRDRSEEAAGGGDGLPRSRDWLYESYYCMSQQHPLIVFLLLIVMGSCLA
LLAVFFALGLEVEDHVAFLITVPTALAIFFAIFILVCIESVFKKLLRLFSLVIWICLVAM
GYLFMCFGGTVSPWDQVSFFLFIIFVVYTMLPFNMRDAIIASVLTSSSHTIVLSVCLSAT
PGGKEHLVWQILANVIIFICGNLAGAYHKHLMELALQQTYQDTCNCIKSRIKLEFEKRQQ
ERLLLSLLPAHIAMEMKAEIIQRLQGPKAGQMENTNNFHNLYVKRHTNVSILYADIVGFT
RLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVK
MGLDMCEAIKKVRDATGVDINMRVGVHSGNVLCGVIGLQKWQYDVWSHDVTLANHMEAGG
VPGRVHISSVTLEHLNGAYKVEEGDGDIRDPYLKQHLVKTYFVINPKGERRSPQHLFRPR
HTLDGAKMRASVRMTRYLESWGAAKPFAHLHHRDSMTTENGKISTTDVPMGQHNFQNRTL
RTKSQKKRFEEELNERMIQAIDGINAQKQWLKSEDIQRISLLFYNKVLEKEYRATALPAF
KYYVTCACLIFFCIFIVQILVLPKTSVLGISFGAAFLLLAFILFVCFAGQLLQCSKKASP
LLMWLLKSSGIIANRPWPRISLTIITTAIILMMAVFNMFFLSDSEETIPPTANTTNTSFS
ASNNQVAILRAQNLFFLPYFIYSCILGLISCSVFLRVNYELKMLIMMVALVGYNTILLHT
HAHVLGDYSQVLFERPGIWKDLKTMGSVSLSIFFITLLVLGRQNEYYCRLDFLWKNKFKK
EREEIETMENLNRVLLENVLPAHVAEHFLARSLKNEELYHQSYDCVCVMFASIPDFKEFY
TESDVNKEGLECLRLLNEIIADFDDLLSKPKFSGVEKIKTIGSTYMAATGLSAVPSQEHS
QEPERQYMHIGTMVEFAFALVGKLDAINKHSFNDFKLRVGINHGPVIAGVIGAQKPQYDI
WGNTVNVASRMDSTGVLDKIQVTEETSLVLQTLGYTCTCRGIINVKGKGDLKTYFVNTEM
SRSLSQSNVAS
Enzyme 77 Number of Residues 1091
Enzyme 77 Molecular Weight 123602.2
Enzyme 77 Theoretical pI 8.15
Enzyme 77 GO Classification
Function
  • adenylate cyclase activity
  • catalytic activity
  • cyclase activity
  • lyase activity
  • phosphorus-oxygen lyase activity
Process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • signaling
  • signaling pathway
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 77 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 77 Specific Function This is a membrane-bound, calmodulin-insensitive adenylyl cyclase
Enzyme 77 Pathways
Enzyme 77 Reactions
  • ATP = 3',5'-cyclic AMP + diphosphate [RN:R00089]
Enzyme 77 Pfam Domain Function
Enzyme 77 Signals
  • None
Enzyme 77 Transmembrane Regions
  • 46-66 76-96 108-128 133-153 159-179 187-207 602-622 628-652 680-701 734-755 763-780 801-821
Enzyme 77 Essentiality Not Available
Enzyme 77 GenBank ID Protein 115387102 Link Image
Enzyme 77 UniProtKB/Swiss-Prot ID Q08462 Link Image
Enzyme 77 UniProtKB/Swiss-Prot Entry Name ADCY2_HUMAN Link Image
Enzyme 77 PDB ID 1AB8 Link Image
Enzyme 77 PDB File Show
Enzyme 77 3D Structure
Enzyme 77 Cellular Location Not Available
Enzyme 77 Gene Sequence >3276 bp 
ATGTGGCAGGAGGCGATGCGGCGCCGCCGCTACCTGCGGGACCGCTCCGAGGAGGCGGCG
GGCGGCGGAGACGGGCTGCCGCGGTCCCGGGACTGGCTCTACGAGTCCTACTACTGCATG
AGCCAGCAGCACCCGCTCATCGTCTTCCTGCTGCTCATCGTCATGGGCTCCTGCCTCGCC
CTGCTCGCCGTCTTCTTCGCGCTCGGGCTGGAAGTTGAAGACCATGTGGCGTTTCTAATA
ACAGTTCCAACTGCCCTGGCGATTTTCTTTGCGATATTTATCCTGGTCTGCATCGAGTCT
GTGTTTAAGAAGCTGCTGCGCCTCTTCTCGTTGGTGATATGGATATGCCTTGTTGCCATG
GGATACCTGTTCATGTGTTTTGGAGGCACCGTCTCTCCCTGGGACCAGGTATCGTTCTTC
CTCTTCATCATCTTCGTGGTGTACACCATGCTGCCCTTCAACATGCGAGACGCCATCATT
GCCAGCGTCCTCACCTCCTCCTCCCACACCATCGTGCTTAGCGTCTGCCTGTCTGCAACA
CCGGGAGGCAAGGAGCACCTGGTCTGGCAGATCCTGGCCAATGTGATCATTTTCATCTGT
GGGAACCTGGCGGGAGCCTACCATAAGCACCTCATGGAACTCGCTCTTCAGCAAACATAT
CAGGACACCTGTAATTGCATCAAGTCGCGGATCAAGTTGGAATTTGAAAAACGTCAACAG
GAGCGGCTTCTGCTCTCCCTGCTGCCGGCCCACATCGCCATGGAGATGAAAGCGGAGATC
ATCCAGAGGCTGCAGGGCCCCAAGGCGGGCCAGATGGAGAACACAAATAACTTCCACAAC
CTGTATGTGAAGCGGCATACAAACGTGAGCATCTTATACGCTGACATCGTTGGCTTTACC
CGGCTGGCAAGTGACTGCTCCCCGGGAGAACTAGTCCACATGCTGAATGAGCTCTTTGGA
AAGTTTGATCAAATTGCAAAGGAGAATGAATGCATGAGAATTAAAATTTTAGGAGACTGC
TACTACTGTGTATCTGGACTCCCTATATCTCTCCCTAACCATGCCAAGAACTGTGTGAAA
ATGGGGCTGGACATGTGTGAAGCCATAAAGAAAGTGAGGGATGCTACTGGAGTTGATATC
AACATGCGCGTGGGCGTGCATTCTGGGAATGTCCTGTGTGGCGTGATTGGTCTGCAGAAG
TGGCAATATGATGTGTGGTCACATGATGTGACCTTGGCCAACCACATGGAAGCTGGAGGG
GTCCCTGGACGTGTTCACATTTCTTCTGTCACCCTGGAGCACTTGAATGGCGCTTATAAA
GTGGAGGAGGGAGATGGTGACATTAGGGACCCATATTTAAAACAGCACCTGGTGAAAACC
TACTTTGTGATCAACCCCAAGGGAGAACGACGGAGCCCCCAGCATCTCTTCAGACCTCGC
CACACCCTTGATGGAGCCAAAATGAGGGCCTCGGTCCGCATGACCCGGTACTTGGAGTCC
TGGGGGGCAGCCAAGCCCTTTGCACACCTACATCACAGGGACAGCATGACCACAGAGAAC
GGCAAGATCAGCACCACGGATGTACCCATGGGTCAGCATAATTTTCAAAATCGCACCTTA
AGAACCAAGTCACAAAAGAAGAGATTTGAAGAAGAATTGAATGAAAGGATGATTCAAGCA
ATTGATGGGATTAATGCACAGAAGCAATGGCTCAAGTCTGAAGACATTCAGAGAATCTCA
CTGCTTTTCTATAACAAAGTACTAGAAAAAGAGTACCGGGCCACGGCACTGCCAGCGTTC
AAGTATTATGTGACTTGTGCCTGTCTCATATTCTTCTGCATCTTCATTGTGCAGATTCTC
GTGCTGCCAAAAACGTCCGTCCTGGGCATCTCCTTTGGGGCTGCGTTTCTCTTGCTGGCC
TTCATCCTCTTCGTCTGCTTTGCTGGACAGCTTCTGCAATGCAGCAAAAAAGCCTCTCCC
CTGCTCATGTGGCTTTTGAAGTCCTCGGGCATCATTGCCAACCGCCCCTGGCCACGGATC
TCTCTCACGATCATCACCACAGCCATCATATTAATGATGGCCGTGTTCAACATGTTTTTC
CTGAGTGACTCAGAGGAAACAATCCCTCCAACTGCCAACACAACAAACACAAGCTTTTCA
GCCTCAAATAATCAGGTGGCGATTCTGCGTGCGCAGAATTTATTTTTCCTCCCGTACTTT
ATCTACAGCTGCATTCTGGGACTGATATCCTGTTCCGTGTTCCTGCGGGTAAACTATGAG
CTGAAGATGTTGATCATGATGGTGGCCTTGGTGGGCTACAACACCATCCTACTCCACACC
CACGCCCACGTCCTGGGCGACTACAGCCAGGTCTTATTTGAGAGACCAGGCATTTGGAAA
GACCTGAAGACCATGGGCTCTGTGTCTCTCTCTATATTCTTCATCACACTGCTTGTTCTG
GGTAGACAGAATGAATATTACTGTAGGTTAGACTTCTTATGGAAGAACAAATTCAAAAAA
GAGCGGGAGGAGATAGAGACCATGGAGAACCTGAACCGCGTGCTGCTGGAGAACGTGCTT
CCCGCGCACGTGGCTGAGCACTTCCTGGCCAGGAGCCTGAAGAATGAGGAGCTATACCAC
CAGTCCTATGACTGCGTCTGCGTCATGTTTGCCTCCATTCCGGATTTCAAAGAATTTTAT
ACAGAATCCGACGTGAACAAGGAGGGCTTGGAATGCCTTCGGCTCCTGAACGAGATCATC
GCTGACTTTGATGATCTTCTTTCCAAGCCAAAATTCAGTGGAGTTGAAAAGATTAAGACC
ATTGGCAGCACATACATGGCAGCAACAGGTCTGAGCGCTGTGCCCAGCCAGGAGCACTCC
CAGGAGCCCGAGCGGCAGTACATGCACATTGGCACCATGGTGGAGTTTGCTTTTGCCCTG
GTAGGGAAGCTGGATGCCATCAACAAGCACTCCTTCAACGACTTCAAATTGCGAGTGGGT
ATTAACCATGGACCTGTGATAGCTGGTGTGATTGGAGCTCAGAAGCCACAATATGATATC
TGGGGCAACACTGTCAATGTGGCCAGTAGGATGGACAGCACCGGAGTCCTGGACAAAATA
CAGGTTACCGAGGAGACGAGCCTCGTCCTGCAGACCCTCGGATACACGTGCACCTGTCGA
GGAATAATCAACGTGAAAGGAAAGGGGGACCTGAAGACGTACTTTGTAAACACAGAAATG
TCAAGGTCCCTTTCCCAGAGCAACGTGGCATCCTGA
Enzyme 77 GenBank Gene ID NM_020546.2 Link Image
Enzyme 77 GeneCard ID ADCY2 Link Image
Enzyme 77 GenAtlas ID ADCY2 Link Image
Enzyme 77 HGNC ID HGNC:233 Link Image
Enzyme 77 Chromosome Location 5
Enzyme 77 Locus 5p15.3
Enzyme 77 SNPs SNPJam Report Link Image
Enzyme 77 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  2. Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [PubMed Link Image]
  3. Stengel D, Parma J, Gannage MH, Roeckel N, Mattei MG, Barouki R, Hanoune J: Different chromosomal localization of two adenylyl cyclase genes expressed in human brain. Hum Genet. 1992 Sep-Oct;90(1-2):126-30. [PubMed Link Image]
  4. Hellevuo K, Yoshimura M, Kao M, Hoffman PL, Cooper DM, Tabakoff B: A novel adenylyl cyclase sequence cloned from the human erythroleukemia cell line. Biochem Biophys Res Commun. 1993 Apr 15;192(1):311-8. [PubMed Link Image]
Enzyme 77 Metabolite References Not Available
Enzyme 78 [top]
Enzyme 78 ID 6214
Enzyme 78 Name Nitric oxide synthase, inducible
Enzyme 78 Synonyms
  1. Hepatocyte NOS
  2. HEP-NOS
  3. Inducible NO synthase
  4. Inducible NOS
  5. iNOS
  6. NOS type II
Enzyme 78 Gene Name NOS2
Enzyme 78 Protein Sequence >Nitric oxide synthase, inducible 
MACPWKFLFKTKFHQYAMNGEKDINNNVEKAPCATSSPVTQDDLQYHNLSKQQNESPQPL
VETGKKSPESLVKLDATPLSSPRHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIM
TPKSLTRGPRDKPTPPDELLPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQ
LTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVRYSTNNGNI
RSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQLCIDLGWKPKYG
RFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWFRELELKWYALPAVANMLLEVG
GLEFPGCPFNGWYMGTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINI
AVLHSFQKQNVTIMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEM
LNYVLSPFYYYQVEAWKTHVWQDEKRRPKRREIPLKVLVKAVLFACMLMRKTMASRVRVT
ILFATETGKSEALAWDLGALFSCAFNPKVVCMDKYRLSCLEEERLLLVVTSTFGNGDCPG
NGEKLKKSLFMLKELNNKFRYAVFGLGSSMYPRFCAFAHDIDQKLSHLGASQLTPMGEGD
ELSGQEDAFRSWAVQTFKAACETFDVRGKQHIQIPKLYTSNVTWDPHHYRLVQDSQPLDL
SKALSSMHAKNVFTMRLKSRQNLQSPTSSRATILVELSCEDGQGLNYLPGEHLGVCPGNQ
PALVQGILERVVDGPTPHQTVRLEALDESGSYWVSDKRLPPCSLSQALTYFLDITTPPTQ
LLLQKLAQVATEEPERQRLEALCQPSEYSKWKFTNSPTFLEVLEEFPSLRVSAGFLLSQL
PILKPRFYSISSSRDHTPTEIHLTVAVVTYHTRDGQGPLHHGVCSTWLNSLKPQDPVPCF
VRNASGFHLPEDPSHPCILIGPGTGIAPFRSFWQQRLHDSQHKGVRGGRMTLVFGCRRPD
EDHIYQEEMLEMAQKGVLHAVHTAYSRLPGKPKVYVQDILRQQLASEVLRVLHKEPGHLY
VCGDVRMARDVAHTLKQLVAAKLKLNEEQVEDYFFQLKSQKRYHEDIFGAVFPYEAKKDR
VAVQPSSLEMSAL
Enzyme 78 Number of Residues 1153
Enzyme 78 Molecular Weight 131116.3
Enzyme 78 Theoretical pI 8.01
Enzyme 78 GO Classification
Function
  • FAD or FADH2 binding
  • FMN binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • binding
  • calmodulin binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • nitric-oxide synthase activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of one atom of oxygen
  • protein binding
  • purine nucleoside binding
  • transition metal ion binding
Process
  • cellular nitrogen compound biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitric oxide biosynthetic process
  • nitrogen compound metabolic process
  • oxidation reduction
Component
—
Enzyme 78 General Function Involved in oxidoreductase activity
Enzyme 78 Specific Function Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions
Enzyme 78 Pathways
Enzyme 78 Reactions
  • L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+ [RN:R00557]
Enzyme 78 Pfam Domain Function
Enzyme 78 Signals
  • None
Enzyme 78 Transmembrane Regions
  • None
Enzyme 78 Essentiality Not Available
Enzyme 78 GenBank ID Protein Not Available
Enzyme 78 UniProtKB/Swiss-Prot ID P35228 Link Image
Enzyme 78 UniProtKB/Swiss-Prot Entry Name NOS2_HUMAN Link Image
Enzyme 78 PDB ID 2NSI Link Image
Enzyme 78 PDB File Show
Enzyme 78 3D Structure
Enzyme 78 Cellular Location Not Available
Enzyme 78 Gene Sequence >3462 bp 
ATGGCCTGTCCTTGGAAATTTCTGTTCAAGACCAAATTCCACCAGTATGCAATGAATGGG
GAAAAAGACATCAACAACAATGTGGAGAAAGCCCCCTGTGCCACCTCCAGTCCAGTGACA
CAGGATGACCTTCAGTATCACAACCTCAGCAAGCAGCAGAATGAGTCCCCGCAGCCCCTC
GTGGAGACGGGAAAGAAGTCTCCAGAATCTCTGGTCAAGCTGGATGCAACCCCATTGTCC
TCCCCACGGCATGTGAGGATCAAAAACTGGGGCAGCGGGATGACTTTCCAAGACACACTT
CACCATAAGGCCAAAGGGATTTTAACTTGCAGGTCCAAATCTTGCCTGGGGTCCATTATG
ACTCCCAAAAGTTTGACCAGAGGACCCAGGGACAAGCCTACCCCTCCAGATGAGCTTCTA
CCTCAAGCTATCGAATTTGTCAACCAATATTACGGCTCCTTCAAAGAGGCAAAAATAGAG
GAACATCTGGCCAGGGTGGAAGCGGTAACAAAGGAGATAGAAACAACAGGAACCTACCAA
CTGACGGGAGATGAGCTCATCTTCGCCACCAAGCAGGCCTGGCGCAATGCCCCACGCTGC
ATTGGGAGGATCCAGTGGTCCAACCTGCAGGTCTTCGATGCCCGCAGCTGTTCCACTGCC
CGGGAAATGTTTGAACACATCTGCAGACACGTGCGTTACTCCACCAACAATGGCAACATC
AGGTCGGCCATCACCGTGTTCCCCCAGCGGAGTGATGGCAAGCACGACTTCCGGGTGTGG
AATGCTCAGCTCATCCGCTATGCTGGCTACCAGATGCCAGATGGCAGCATCAGAGGGGAC
CCTGCCAACGTGGAATTCACTCAGCTGTGCATCGACCTGGGCTGGAAGCCCAAGTACGGC
CGCTTCGATGTGGTCCCCCTGGTCCTGCAGGCCAATGGCCGTGACCCTGAGCTCTTCGAA
ATCCCACCTGACCTTGTGCTTGAGGTGGCCATGGAACATCCCAAATACGAGTGGTTTCGG
GAACTGGAGCTAAAGTGGTACGCCCTGCCTGCAGTGGCCAACATGCTGCTTGAGGTGGGC
GGCCTGGAGTTCCCAGGGTGCCCCTTCAATGGCTGGTACATGGGCACAGAGATCGGAGTC
CGGGACTTCTGTGACGTCCAGCGCTACAACATCCTGGAGGAAGTGGGCAGGAGAATGGGC
CTGGAAACGCACAAGCTGGCCTCGCTCTGGAAAGACCAGGCTGTCGTTGAGATCAACATT
GCTGTGCTCCATAGTTTCCAGAAGCAGAATGTGACCATCATGGACCACCACTCGGCTGCA
GAATCCTTCATGAAGTACATGCAGAATGAATACCGGTCCCGTGGGGGCTGCCCGGCAGAC
TGGATTTGGCTGGTCCCTCCCATGTCTGGGAGCATCACCCCCGTGTTTCACCAGGAGATG
CTGAACTACGTCCTGTCCCCTTTCTACTACTATCAGGTAGAGGCCTGGAAAACCCATGTC
TGGCAGGACGAGAAGCGGAGACCCAAGAGAAGAGAGATTCCATTGAAAGTCTTGGTCAAA
GCTGTGCTCTTTGCCTGTATGCTGATGCGCAAGACAATGGCGTCCCGAGTCAGAGTCACC
ATCCTCTTTGCGACAGAGACAGGAAAATCAGAGGCGCTGGCCTGGGACCTGGGGGCCTTA
TTCAGCTGTGCCTTCAACCCCAAGGTTGTCTGCATGGATAAGTACAGGCTGAGCTGCCTG
GAGGAGGAACGGCTGCTGTTGGTGGTGACCAGTACGTTTGGCAATGGAGACTGCCCTGGC
AATGGAGAGAAACTGAAGAAATCGCTCTTCATGCTGAAAGAGCTCAACAACAAATTCAGG
TACGCTGTGTTTGGCCTCGGCTCCAGCATGTACCCTCGGTTCTGCGCCTTTGCTCATGAC
ATTGATCAGAAGCTGTCCCACCTGGGGGCCTCTCAGCTCACCCCGATGGGAGAAGGGGAT
GAGCTCAGTGGGCAGGAGGACGCCTTCCGCAGCTGGGCCGTGCAAACCTTCAAGGCAGCC
TGTGAGACGTTTGATGTCCGAGGCAAACAGCACATTCAGATCCCCAAGCTCTACACCTCC
AATGTGACCTGGGACCCGCACCACTACAGGCTCGTGCAGGACTCACAGCCTTTGGACCTC
AGCAAAGCCCTCAGCAGCATGCATGCCAAGAACGTGTTCACCATGAGGCTCAAATCTCGG
CAGAATCTACAAAGTCCGACATCCAGCCGTGCCACCATCCTGGTGGAACTCTCCTGTGAG
GATGGCCAAGGCCTGAACTACCTGCCGGGGGAGCACCTTGGGGTTTGCCCAGGCAACCAG
CCGGCCCTGGTCCAAGGCATCCTGGAGCGAGTGGTGGATGGCCCCACACCCCACCAGACA
GTGCGCCTGGAGGCCCTGGATGAGAGTGGCAGCTACTGGGTCAGTGACAAGAGGCTGCCC
CCCTGCTCACTCAGCCAGGCCCTCACCTACTTCCTGGACATCACCACACCCCCAACCCAG
CTGCTGCTCCAAAAGCTGGCCCAGGTGGCCACAGAAGAGCCTGAGAGACAGAGGCTGGAG
GCCCTGTGCCAGCCCTCAGAGTACAGCAAGTGGAAGTTCACCAACAGCCCCACATTCCTG
GAGGTGCTAGAGGAGTTCCCGTCCCTGCGGGTGTCTGCTGGCTTCCTGCTTTCCCAGCTC
CCCATTCTGAAGCCCAGGTTCTACTCCATCAGCTCCTCCCGGGATCACACGCCCACGGAG
ATCCACCTGACTGTGGCCGTGGTCACCTACCACACCCGAGATGGCCAGGGTCCCCTGCAC
CACGGCGTCTGCAGCACATGGCTCAACAGCCTGAAGCCCCAAGACCCAGTGCCCTGCTTT
GTGCGGAATGCCAGCGGCTTCCACCTCCCCGAGGATCCCTCCCATCCTTGCATCCTCATC
GGGCCTGGCACAGGCATCGCGCCCTTCCGCAGTTTCTGGCAGCAACGGCTCCATGACTCC
CAGCACAAGGGAGTGCGGGGAGGCCGCATGACCTTGGTGTTTGGGTGCCGCCGCCCAGAT
GAGGACCACATCTACCAGGAGGAGATGCTGGAGATGGCCCAGAAGGGGGTGCTGCATGCG
GTGCACACAGCCTATTCCCGCCTGCCTGGCAAGCCCAAGGTCTATGTTCAGGACATCCTG
CGGCAGCAGCTGGCCAGCGAGGTGCTCCGTGTGCTCCACAAGGAGCCAGGCCACCTCTAT
GTTTGCGGGGATGTGCGCATGGCCCGGGACGTGGCCCACACCCTGAAGCAGCTGGTGGCT
GCCAAGCTGAAATTGAATGAGGAGCAGGTCGAGGACTATTTCTTTCAGCTCAAGAGCCAG
AAGCGCTATCACGAAGATATCTTTGGTGCTGTATTTCCTTACGAGGCGAAGAAGGACAGG
GTGGCGGTGCAGCCCAGCAGCCTGGAGATGTCAGCGCTCTGA
Enzyme 78 GenBank Gene ID L24553 Link Image
Enzyme 78 GeneCard ID NOS2 Link Image
Enzyme 78 GenAtlas ID NOS2 Link Image
Enzyme 78 HGNC ID HGNC:7873 Link Image
Enzyme 78 Chromosome Location 1
Enzyme 78 Locus 17q11.2-q12
Enzyme 78 SNPs SNPJam Report Link Image
Enzyme 78 General References
  1. Sherman PA, Laubach VE, Reep BR, Wood ER: Purification and cDNA sequence of an inducible nitric oxide synthase from a human tumor cell line. Biochemistry. 1993 Nov 2;32(43):11600-5. [PubMed Link Image]
  2. Geller DA, Lowenstein CJ, Shapiro RA, Nussler AK, Di Silvio M, Wang SC, Nakayama DK, Simmons RL, Snyder SH, Billiar TR: Molecular cloning and expression of inducible nitric oxide synthase from human hepatocytes. Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3491-5. [PubMed Link Image]
  3. Charles IG, Palmer RM, Hickery MS, Bayliss MT, Chubb AP, Hall VS, Moss DW, Moncada S: Cloning, characterization, and expression of a cDNA encoding an inducible nitric oxide synthase from the human chondrocyte. Proc Natl Acad Sci U S A. 1993 Dec 1;90(23):11419-23. [PubMed Link Image]
  4. Maier R, Bilbe G, Rediske J, Lotz M: Inducible nitric oxide synthase from human articular chondrocytes: cDNA cloning and analysis of mRNA expression. Biochim Biophys Acta. 1994 Sep 21;1208(1):145-50. [PubMed Link Image]
  5. Park CS, Pardhasaradhi K, Gianotti C, Villegas E, Krishna G: Human retina expresses both constitutive and inducible isoforms of nitric oxide synthase mRNA. Biochem Biophys Res Commun. 1994 Nov 30;205(1):85-91. [PubMed Link Image]
  6. Hokari A, Zeniya M, Esumi H: Cloning and functional expression of human inducible nitric oxide synthase (NOS) cDNA from a glioblastoma cell line A-172. J Biochem (Tokyo). 1994 Sep;116(3):575-81. [PubMed Link Image]
  7. Guo FH, De Raeve HR, Rice TW, Stuehr DJ, Thunnissen FB, Erzurum SC: Continuous nitric oxide synthesis by inducible nitric oxide synthase in normal human airway epithelium in vivo. Proc Natl Acad Sci U S A. 1995 Aug 15;92(17):7809-13. [PubMed Link Image]
  8. Luss H, Li RK, Shapiro RA, Tzeng E, McGowan FX, Yoneyama T, Hatakeyama K, Geller DA, Mickle DA, Simmons RL, Billiar TR: Dedifferentiated human ventricular cardiac myocytes express inducible nitric oxide synthase mRNA but not protein in response to IL-1, TNF, IFNgamma, and LPS. J Mol Cell Cardiol. 1997 Apr;29(4):1153-65. [PubMed Link Image]
  9. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  10. McLay JS, Chatterjee P, Nicolson AG, Jardine AG, McKay NG, Ralston SH, Grabowski P, Haites NE, MacLeod AM, Hawksworth GM: Nitric oxide production by human proximal tubular cells: a novel immunomodulatory mechanism? Kidney Int. 1994 Oct;46(4):1043-9. [PubMed Link Image]
  11. Fujisawa H, Ogura T, Hokari A, Weisz A, Yamashita J, Esumi H: Inducible nitric oxide synthase in a human glioblastoma cell line. J Neurochem. 1995 Jan;64(1):85-91. [PubMed Link Image]
  12. Bloch KD, Wolfram JR, Brown DM, Roberts JD Jr, Zapol DG, Lepore JJ, Filippov G, Thomas JE, Jacob HJ, Bloch DB: Three members of the nitric oxide synthase II gene family (NOS2A, NOS2B, and NOS2C) colocalize to human chromosome 17. Genomics. 1995 Jun 10;27(3):526-30. [PubMed Link Image]
  13. Taylor BS, Alarcon LH, Billiar TR: Inducible nitric oxide synthase in the liver: regulation and function. Biochemistry (Mosc). 1998 Jul;63(7):766-81. [PubMed Link Image]
  14. Glynne PA, Darling KE, Picot J, Evans TJ: Epithelial inducible nitric-oxide synthase is an apical EBP50-binding protein that directs vectorial nitric oxide output. J Biol Chem. 2002 Sep 6;277(36):33132-8. Epub 2002 Jun 21. [PubMed Link Image]
  15. Li H, Raman CS, Glaser CB, Blasko E, Young TA, Parkinson JF, Whitlow M, Poulos TL: Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase. J Biol Chem. 1999 Jul 23;274(30):21276-84. [PubMed Link Image]
  16. Fischmann TO, Hruza A, Niu XD, Fossetta JD, Lunn CA, Dolphin E, Prongay AJ, Reichert P, Lundell DJ, Narula SK, Weber PC: Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation. Nat Struct Biol. 1999 Mar;6(3):233-42. [PubMed Link Image]
  17. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 78 Metabolite References Not Available
Enzyme 79 [top]
Enzyme 79 ID 6216
Enzyme 79 Name Nitric oxide synthase, brain
Enzyme 79 Synonyms
  1. Constitutive NOS
  2. NC-NOS
  3. NOS type I
  4. Neuronal NOS
  5. N-NOS
  6. nNOS
  7. bNOS
Enzyme 79 Gene Name NOS1
Enzyme 79 Protein Sequence >Nitric oxide synthase, brain 
MEDHMFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQA
GDIILAVNGRPLVDLSYDSALEVLRGIASETHVVLILRGPEGFTTHLETTFTGDGTPKTI
RVTQPLGPPTKAVDLSHQPPAGKEQPLAVDGASGPGNGPQHAYDDGQEAGSLPHANGLAP
RPPGQDPAKKATRVSLQGRGENNELLKEIEPVLSLLTSGSRGVKGGAPAKAEMKDMGIQV
DRDLDGKSHKPLPLGVENDRVFNDLWGKGNVPVVLNNPYSEKEQPPTSGKQSPTKNGSPS
KCPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVRTKGQLF
PLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRC
VGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVW
NSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQ
IPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGV
RDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSAT
ESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHV
WKGTNGTPTKRRAIGFKKLAEAVKFSAKLMGQAMAKRVKATILYATETGKSQAYAKTLCE
IFKHAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRHPNSVQ
EERKSYKVRFNSVSSYSDSQKSSGDGPDLRDNFESAGPLANVRFSVFGLGSRAYPHFCAF
GHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANN
SLISNDRSWKRNKFRLTFVAEAPELTQGLSNVHKKRVSAARLLSRQNLQSPKSSRSTIFV
RLHTNGSQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVELLEERNTALGV
ISNWTDELRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKGLQEY
EEWKWGKNPTIVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIV
SYRTRDGEGPIHHGVCSSWLNRIQADELVPCFVRGAPSFHLPRNPQVPCILVGPGTGIAP
FRSFWQQRQFDIQHKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSRE
PDKPKKYVQDILQEQLAESVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSAE
DAGVFISRMRDDNRYHEDIFGVTLRTYEVTNRLRSESIAFIEESKKDTDEVFSS
Enzyme 79 Number of Residues 1434
Enzyme 79 Molecular Weight 160969.1
Enzyme 79 Theoretical pI 7.44
Enzyme 79 GO Classification
Function
  • FAD or FADH2 binding
  • FMN binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • binding
  • calmodulin binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • nitric-oxide synthase activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of one atom of oxygen
  • protein binding
  • purine nucleoside binding
  • transition metal ion binding
Process
  • cellular nitrogen compound biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitric oxide biosynthetic process
  • nitrogen compound metabolic process
  • oxidation reduction
Component
—
Enzyme 79 General Function Involved in oxidoreductase activity
Enzyme 79 Specific Function Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter
Enzyme 79 Pathways
Enzyme 79 Reactions
  • L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+ [RN:R00557]
Enzyme 79 Pfam Domain Function
Enzyme 79 Signals
  • None
Enzyme 79 Transmembrane Regions
  • None
Enzyme 79 Essentiality Not Available
Enzyme 79 GenBank ID Protein 642526 Link Image
Enzyme 79 UniProtKB/Swiss-Prot ID P29475 Link Image
Enzyme 79 UniProtKB/Swiss-Prot Entry Name NOS1_HUMAN Link Image
Enzyme 79 PDB ID 1TLL Link Image
Enzyme 79 PDB File Show
Enzyme 79 3D Structure
Enzyme 79 Cellular Location Not Available
Enzyme 79 Gene Sequence >4305 bp 
ATGGAGGATCACATGTTCGGTGTTCAGCAAATCCAGCCCAATGTCATTTCTGTTCGTCTC
TTCAAGCGCAAAGTTGGGGGCCTGGGATTTCTGGTGAAGGAGCGGGTCAGTAAGCCGCCC
GTGATCATCTCTGACCTGATTCGTGGGGGCGCCGCAGAGCAGAGTGGCCTCATCCAGGCC
GGAGACATCATTCTTGCGGTCAACGGCCGGCCCTTGGTGGACCTGAGCTATGACAGCGCC
CTGGAGGTACTCAGAGGCATTGCCTCTGAGACCCACGTGGTCCTCATTCTGAGGGGCCCT
GAAGGTTTCACCACGCACCTGGAGACCACCTTTACAGGTGATGGGACCCCCAAGACCATC
CGGGTGACACAGCCCCTGGGTCCCCCCACCAAAGCCGTGGATCTGTCCCACCAGCCACCG
GCCGGCAAAGAACAGCCCCTGGCAGTGGATGGGGCCTCGGGTCCCGGGAATGGGCCTCAG
CATGCCTACGATGATGGGCAGGAGGCTGGCTCACTCCCCCATGCCAACGGCCTGGCCCCC
AGGCCCCCAGGCCAGGACCCCGCGAAGAAAGCAACCAGAGTCAGCCTCCAAGGCAGAGGG
GAGAACAATGAACTGCTCAAGGAGATAGAGCCTGTGCTGAGCCTTCTCACCAGTGGGAGC
AGAGGGGTCAAGGGAGGGGCACCTGCCAAGGCAGAGATGAAAGATATGGGAATCCAGGTG
GACAGAGATTTGGACGGCAAGTCACACAAACCTCTGCCCCTCGGCGTGGAGAACGACCGA
GTCTTCAATGACCTATGGGGGAAGGGCAATGTGCCTGTCGTCCTCAACAACCCATATTCA
GAGAAGGAGCAGCCCCCCACCTCAGGAAAACAGTCCCCCACAAAGAATGGCAGCCCCTCC
AAGTGTCCACGCTTCCTCAAGGTCAAGAACTGGGAGACTGAGGTGGTTCTCACTGACACC
CTCCACCTTAAGAGCACATTGGAAACGGGATGCACTGAGTACATCTGCATGGGCTCCATC
ATGCATCCTTCTCAGCATGCAAGGAGGCCTGAAGACGTCCGCACAAAAGGACAGCTCTTC
CCTCTCGCCAAAGAGTTTATTGATCAATACTATTCATCAATTAAAAGATTTGGCTCCAAA
GCCCACATGGAAAGGCTGGAAGAGGTGAACAAAGAGATCGACACCACTAGCACTTACCAG
CTCAAGGACACAGAGCTCATCTATGGGGCCAAGCACGCCTGGCGGAATGCCTCGCGCTGT
GTGGGCAGGATCCAGTGGTCCAAGCTGCAGGTATTCGATGCCCGTGACTGCACCACGGCC
CACGGGATGTTCAACTACATCTGTAACCATGTCAAGTATGCCACCAACAAAGGGAACCTC
AGGTCTGCCATCACCATATTCCCCCAGAGGACAGACGGCAAGCACGACTTCCGAGTCTGG
AACTCCCAGCTCATCCGCTACGCTGGCTACAAGCAGCCTGACGGCTCCACCCTGGGGGAC
CCAGCCAATGTGCAGTTCACAGAGATATGCATACAGCAGGGCTGGAAACCGCCTAGAGGC
CGCTTCGATGTCCTGCCGCTCCTGCTTCAGGCCAACGGCAATGACCCTGAGCTCTTCCAG
ATTCCTCCAGAGCTGGTGTTGGAAGTTCCCATCAGGCACCCCAAGTTTGAGTGGTTCAAG
GACCTGGGGCTGAAGTGGTACGGCCTCCCCGCCGTGTCCAACATGCTCCTAGAGATTGGC
GGCCTGGAGTTCAGCGCCTGTCCCTTCAGTGGCTGGTACATGGGCACAGAGATTGGTGTC
CGCGACTACTGTGACAACTCCCGCTACAATATCCTGGAGGAAGTGGCCAAGAAGATGAAC
TTAGACATGAGGAAGACGTCCTCCCTGTGGAAGGACCAGGCGCTGGTGGAGATCAATATC
GCGGTTCTCTATAGCTTCCAGAGTGACAAAGTGACCATTGTTGACCATCACTCCGCCACC
GAGTCCTTCATTAAGCACATGGAGAATGAGTACCGCTGCCGGGGGGGCTGCCCTGCCGAC
TGGGTGTGGATCGTGCCCCCCATGTCCGGAAGCATCACCCCTGTGTTCCACCAGGAGATG
CTCAACTACCGGCTCACCCCCTCCTTCGAATACCAGCCTGATCCCTGGAACACGCATGTC
TGGAAAGGCACCAACGGGACCCCCACAAAGCGGCGAGCCATCGGCTTCAAGAAGCTAGCA
GAAGCTGTCAAGTTCTCGGCCAAGCTGATGGGGCAGGCTATGGCCAAGAGGGTGAAAGCG
ACCATCCTCTATGCCACAGAGACAGGCAAATCGCAAGCTTATGCCAAGACCTTGTGTGAG
ATCTTCAAACACGCCTTTGATGCCAAGGTGATGTCCATGGAAGAATATGACATTGTGCAC
CTGGAACATGAAACTCTGGTCCTTGTGGTCACCAGCACCTTTGGCAATGGAGATCCCCCT
GAGAATGGGGAGAAATTCGGCTGTGCTTTGATGGAAATGAGGCACCCCAACTCTGTGCAG
GAAGAAAGGAAGAGCTACAAGGTCCGATTCAACAGCGTCTCCTCCTACTCTGACTCCCAA
AAATCATCAGGCGATGGGCCCGACCTCAGAGACAACTTTGAGAGTGCTGGACCCCTGGCC
AATGTGAGGTTCTCAGTTTTTGGCCTCGGCTCACGAGCATACCCTCACTTTTGCGCCTTC
GGACACGCTGTGGACACCCTCCTGGAAGAACTGGGAGGGGAGAGGATCCTGAAGATGAGG
GAAGGGGATGAGCTCTGTGGGCAGGAAGAGGCTTTCAGGACCTGGGCCAAGAAGGTCTTC
AAGGCAGCCTGTGATGTCTTCTGTGTGGGAGATGATGTCAACATTGAAAAGGCCAACAAT
TCCCTCATCAGCAATGATCGCAGCTGGAAGAGAAACAAGTTCCGCCTCACCTTTGTGGCC
GAAGCTCCAGAACTCACACAAGGTCTATCCAATGTCCACAAAAAGCGAGTCTCAGCTGCC
CGGCTCCTTAGCCGTCAAAACCTCCAGAGCCCTAAATCCAGTCGGTCAACTATCTTCGTG
CGTCTCCACACCAACGGGAGCCAGGAGCTGCAGTACCAGCCTGGGGACCACCTGGGTGTC
TTCCCTGGCAACCACGAGGACCTCGTGAATGCCCTGATCGAGCGGCTGGAGGACGCGCCG
CCTGTCAACCAGATGGTGAAAGTGGAACTGCTGGAGGAGCGGAACACGGCTTTAGGTGTC
ATCAGTAACTGGACAGACGAGCTCCGCCTCCCGCCCTGCACCATCTTCCAGGCCTTCAAG
TACTACCTGGACATCACCACGCCACCAACGCCTCTGCAGCTGCAGCAGTTTGCCTCCCTA
GCTACCAGCGAGAAGGAGAAGCAGCGTCTGCTGGTCCTCAGCAAGGGTTTGCAGGAGTAC
GAGGAATGGAAATGGGGCAAGAACCCCACCATCGTGGAGGTGCTGGAGGAGTTCCCATCT
ATCCAGATGCCGGCCACCCTGCTCCTGACCCAGCTGTCCCTGCTGCAGCCCCGCTACTAT
TCCATCAGCTCCTCCCCAGACATGTACCCTGATGAAGTGCACCTCACTGTGGCCATCGTT
TCCTACCGCACTCGAGATGGAGAAGGACCAATTCACCACGGCGTATGCTCCTCCTGGCTC
AACCGGATACAGGCTGACGAACTGGTCCCCTGTTTCGTGAGAGGAGCACCCAGCTTCCAC
CTGCCCCGGAACCCCCAAGTCCCCTGCATCCTCGTTGGACCAGGCACCGGCATTGCCCCT
TTCCGAAGCTTCTGGCAACAGCGGCAATTTGATATCCAACACAAAGGAATGAACCCCTGC
CCCATGGTCCTGGTCTTCGGGTGCCGGCAATCCAAGATAGATCATATCTACAGGGAAGAG
ACCCTGCAGGCCAAGAACAAGGGGGTCTTCAGAGAGCTGTACACGGCTTACTCCCGGGAG
CCAGACAAACCAAAGAAGTACGTGCAGGACATCCTGCAGGAGCAGCTGGCGGAGTCTGTG
TACCGAGCCCTGAAGGAGCAAGGGGGCCACATATACGTCTGTGGGGACGTCACCATGGCT
GCTGATGTCCTCAAAGCCATCCAGCGCATCATGACCCAGCAGGGGAAGCTCTCGGCAGAG
GACGCCGGCGTATTCATCAGCCGGATGAGGGATGACAACCGATACCATGAGGATATTTTT
GGAGTCACCCTGCGAACGTACGAAGTGACCAACCGCCTTAGATCTGAGTCCATTGCCTTC
ATTGAAGAGAGCAAAAAAGACACCGATGAGGTTTTCAGCTCCTAA
Enzyme 79 GenBank Gene ID U17327 Link Image
Enzyme 79 GeneCard ID NOS1 Link Image
Enzyme 79 GenAtlas ID NOS1 Link Image
Enzyme 79 HGNC ID HGNC:7872 Link Image
Enzyme 79 Chromosome Location 1
Enzyme 79 Locus 12q24.2-q24.31
Enzyme 79 SNPs SNPJam Report Link Image
Enzyme 79 General References
  1. Hall AV, Antoniou H, Wang Y, Cheung AH, Arbus AM, Olson SL, Lu WC, Kau CL, Marsden PA: Structural organization of the human neuronal nitric oxide synthase gene (NOS1). J Biol Chem. 1994 Dec 30;269(52):33082-90. [PubMed Link Image]
  2. Fujisawa H, Ogura T, Kurashima Y, Yokoyama T, Yamashita J, Esumi H: Expression of two types of nitric oxide synthase mRNA in human neuroblastoma cell lines. J Neurochem. 1994 Jul;63(1):140-5. [PubMed Link Image]
  3. Nakane M, Schmidt HH, Pollock JS, Forstermann U, Murad F: Cloned human brain nitric oxide synthase is highly expressed in skeletal muscle. FEBS Lett. 1993 Jan 25;316(2):175-80. [PubMed Link Image]
  4. Park CS, Gianotti C, Park R, Krishna G: Neuronal isoform of nitric oxide synthase is expressed at low levels in human retina. Cell Mol Neurobiol. 1996 Aug;16(4):499-515. [PubMed Link Image]
  5. Wang Y, Goligorsky MS, Lin M, Wilcox JN, Marsden PA: A novel, testis-specific mRNA transcript encoding an NH2-terminal truncated nitric-oxide synthase. J Biol Chem. 1997 Apr 25;272(17):11392-401. [PubMed Link Image]
Enzyme 79 Metabolite References Not Available
Enzyme 80 [top]
Enzyme 80 ID 6217
Enzyme 80 Name Nitric oxide synthase, endothelial
Enzyme 80 Synonyms
  1. Constitutive NOS
  2. cNOS
  3. EC-NOS
  4. Endothelial NOS
  5. eNOS
  6. NOS type III
  7. NOSIII
Enzyme 80 Gene Name NOS3
Enzyme 80 Protein Sequence >Nitric oxide synthase, endothelial 
MGNLKSVAQEPGPPCGLGLGLGLGLCGKQGPATPAPEPSRAPASLLPPAPEHSPPSSPLT
QPPEGPKFPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPRKLQGRPSPGPPAP
EQLLSQARDFINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRN
APRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGD
FRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQAPDEPP
ELFLLPPELVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMST
EIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDH
HAATASFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDPW
KGSAAKGTGITRKKTFKEVANAVKISASLMGTVMAKRVKATILYGSETGRAQSYAQQLGR
LFRKAFDPRVLCMDEYDVVSLEHETLVLVVTSTFGNGDPPENGESFAAALMEMSGPYNSS
PRPEQHKSYKIRFNSISCSDPLVSSWRRKRKESSNTDSAGALGTLRFCVFGLGSRAYPHF
CAFARAVDTRLEELGGERLLQLGQGDELCGQEEAFRGWAQAAFQAACETFCVGEDAKAAA
RDIFSPKRSWKRQRYRLSAQAEGLQLLPGLIHVHRRKMFQATIRSVENLQSSKSTRATIL
VRLDTGGQEGLQYQPGDHIGVCPPNRPGLVEALLSRVEDPPAPTEPVAVEQLEKGSPGGP
PPGWVRDPRLPPCTLRQALTFFLDITSPPSPQLLRLLSTLAEEPREQQELEALSQDPRRY
EEWKWFRCPTLLEVLEQFPSVALPAPLLLTQLPLLQPRYYSVSSAPSTHPGEIHLTVAVL
AYRTQDGLGPLHYGVCSTWLSQLKPGDPVPCFIRGAPSFRLPPDPSLPCILVGPGTGIAP
FRGFWQERLHDIESKGLQPTPMTLVFGCRCSQLDHLYRDEVQNAQQRGVFGRVLTAFSRE
PDNPKTYVQDILRTELAAEVHRVLCLERGHMFVCGDVTMATNVLQTVQRILATEGDMELD
EAGDVIGVLRDQQRYHEDIFGLTLRTQEVTSRIRTQSFSLQERQLRGAVPWAFDPPGSDT
NSP
Enzyme 80 Number of Residues 1203
Enzyme 80 Molecular Weight 133287.6
Enzyme 80 Theoretical pI 7.27
Enzyme 80 GO Classification
Function
  • FAD or FADH2 binding
  • FMN binding
  • NADP or NADPH binding
  • adenyl nucleotide binding
  • binding
  • calmodulin binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • nitric-oxide synthase activity
  • nucleoside binding
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of one atom of oxygen
  • protein binding
  • purine nucleoside binding
  • transition metal ion binding
Process
  • cellular nitrogen compound biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitric oxide biosynthetic process
  • nitrogen compound metabolic process
  • oxidation reduction
Component
—
Enzyme 80 General Function Involved in oxidoreductase activity
Enzyme 80 Specific Function Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets
Enzyme 80 Pathways
Enzyme 80 Reactions
  • L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+ [RN:R00557]
Enzyme 80 Pfam Domain Function
Enzyme 80 Signals
  • None
Enzyme 80 Transmembrane Regions
  • None
Enzyme 80 Essentiality Not Available
Enzyme 80 GenBank ID Protein Not Available
Enzyme 80 UniProtKB/Swiss-Prot ID P29474 Link Image
Enzyme 80 UniProtKB/Swiss-Prot Entry Name NOS3_HUMAN Link Image
Enzyme 80 PDB ID 3NOS Link Image
Enzyme 80 PDB File Show
Enzyme 80 3D Structure
Enzyme 80 Cellular Location Not Available
Enzyme 80 Gene Sequence >3612 bp 
ATGGGCAACTTGAAGAGCGTGGCCCAGGAGCCTGGGCCACCCTGCGGCCTGGGGCTGGGG
CTGGGCCTTGGGCTGTGCGGCAAGCAGGGCCCAGCCACCCCGGCCCCTGAGCCCAGCCGG
GCCCCAGCATCCCTACTCCCACCAGCGCCAGAACACAGCCCCCCGAGCTCCCCGCTAACC
CAGCCCCCAGAGGGGCCCAAGTTCCCTCGTGTGAAGAACTGGGAGGTGGGGAGCATCACC
TATGACACCCTCAGCGCCCAGGCGCAGCAGGATGGGCCCTGCACCCCAAGACGCTGCCTG
GGCTCCCTGGTATTTCCACGGAAACTACAGGGCCGGCCCTCCCCCGGCCCCCCGGCCCCT
GAGCAGCTGCTGAGTCAGGCCCGGGACTTCATCAACCAGTACTACAGCTCCATTAAGAGG
AGCGGCTCCCAGGCCCACGAACAGCGGCTTCAAGAGGTGGAAGCCGAGGTGGCAGCCACA
GGCACCTACCAGCTTAGGGAGAGCGAGCTGGTGTTCGGGGCTAAGCAGGCCTGGCGCAAC
GCTCCCCGCTGCGTGGGCCGGATCCAGTGGGGGAAGCTGCAGGTGTTCGATGCCCGGGAC
TGCAGGTCTGCACAGGAAATGTTCACCTACATCTGCAACCACATCAAGTATGCCACCAAC
CGGGGCAACCTTCGCTCGGCCATCACAGTGTTCCCGCAGCGCTGCCCTGGCCGAGGAGAC
TTCCGAATCTGGAACAGCCAGCTGGTGCGCTACGCGGGCTACCGGCAGCAGGACGGCTCT
GTGCGGGGGGACCCAGCCAACGTGGAGATCACCGAGCTCTGCATTCAGCACGGCTGGACC
CCAGGAAACGGTCGCTTCGACGTGCTGCCCCTGCTGCTGCAGGCCCCAGATGAGCCCCCA
GAACTCTTCCTTCTGCCCCCCGAGCTGGTCCTTGAGGTGCCCCTGGAGCACCCCACGCTG
GAGTGGTTTGCAGCCCTGGGCCTGCGCTGGTACGCCCTCCCGGCAGTGTCCAACATGCTG
CTGGAAATTGGGGGCCTGGAGTTCCCCGCAGCCCCCTTCAGTGGCTGGTACATGAGCACT
GAGATCGGCACGAGGAACCTGTGTGACCCTCACCGCTACAACATCCTGGAGGATGTGGCT
GTCTGCATGGACCTGGATACCCGGACCACCTCGTCCCTGTGGAAAGACAAGGCAGCAGTG
GAAATCAACGTGGCCGTGCTGCACAGTTACCAGCTAGCCAAAGTCACCATCGTGGACCAC
CACGCCGCCACGGCCTCTTTCATGAAGCACCTGGAGAATGAGCAGAAGGCCAGGGGGGGC
TGCCCTGCAGACTGGGCCTGGATCGTGCCCCCCATCTCGGGCAGCCTCACTCCTGTTTTC
CATCAGGAGATGGTCAACTATTTCCTGTCCCCGGCCTTCCGCTACCAGCCAGACCCCTGG
AAGGGGAGTGCCGCCAAGGGCACCGGCATCACCAGGAAGAAGACCTTTAAAGAAGTGGCC
AACGCCGTGAAGATCTCCGCCTCGCTCATGGGCACGGTGATGGCGAAGCGAGTGAAGGCG
ACAATCCTGTATGGCTCCGAGACCGGCCGGGCCCAGAGCTACGCACAGCAGCTGGGGAGA
CTCTTCCGGAAGGCTTTTGATCCCCGGGTCCTGTGTATGGATGAGTATGACGTGGTGTCC
CTCGAACACGAGACGCTGGTGCTGGTGGTAACCAGCACATTTGGGAATGGGGATCCCCCG
GAGAATGGAGAGAGCTTTGCAGCTGCCCTGATGGAGATGTCCGGCCCCTACAACAGCTCC
CCTCGGCCGGAACAGCACAAGAGTTATAAGATCCGCTTCAACAGCATCTCCTGCTCAGAC
CCACTGGTGTCCTCTTGGCGGCGGAAGAGGAAGGAGTCCAGTAACACAGACAGTGCAGGG
GCCCTGGGCACCCTCAGGTTCTGTGTGTTCGGGCTCGGCTCCCGGGCATACCCCCACTTC
TGCGCCTTTGCTCGTGCCGTGGACACACGGCTGGAGGAACTGGGCGGGGAGCGGCTGCTG
CAGCTGGGCCAGGGCGACGAGCTGTGCGGCCAGGAGGAGGCCTTCCGAGGCTGGGCCCAG
GCTGCCTTCCAGGCCGCCTGTGAGACCTTCTGTGTGGGAGAGGATGCCAAGGCCGCCGCC
CGAGACATCTTCAGCCCCAAACGGAGCTGGAAGCGCCAGAGGTACCGGCTGAGCGCCCAG
GCCGAGGGCCTGCAGTTGCTGCCAGGTCTGATCCACGTGCACAGGCGGAAGATGTTCCAG
GCTACAATCCGCTCAGTGGAAAACCTGCAAAGCAGCAAGTCCACGAGGGCCACCATCCTG
GTGCGCCTGGACACCGGAGGCCAGGAGGGGCTGCAGTACCAGCCGGGGGACCACATAGGT
GTCTGCCCGCCCAACCGGCCCGGCCTTGTGGAGGCGCTGCTGAGCCGCGTGGAGGACCCG
CCGGCGCCCACTGAGCCCGTGGCAGTAGAGCAGCTGGAGAAGGGCAGCCCTGGTGGCCCT
CCCCCCGGCTGGGTGCGGGACCCCCGGCTGCCCCCGTGCACGCTGCGCCAGGCTCTCACC
TTCTTCCTGGACATCACCTCCCCACCCAGCCCTCAGCTCTTGCGGCTGCTCAGCACCTTG
GCAGAAGAGCCCAGGGAACAGCAGGAGCTGGAGGCCCTCAGCCAGGATCCCCGACGCTAC
GAGGAGTGGAAGTGGTTCCGCTGCCCCACGCTGCTGGAGGTGCTGGAGCAGTTCCCGTCG
GTGGCGCTGCCTGCCCCACTGCTCCTCACCCAGCTGCCTCTGCTCCAGCCCCGGTACTAC
TCAGTCAGCTCGGCACCCAGCACCCACCCAGGAGAGATCCACCTCACTGTAGCTGTGCTG
GCATACAGGACTCAGGATGGGCTGGGCCCCCTGCACTATGGAGTCTGCTCCACGTGGCTA
AGCCAGCTCAAGCCCGGAGACCCTGTGCCCTGCTTCATCCGGGGGGCTCCCTCCTTCCGG
CTGCCACCCGATCCCAGCTTGCCCTGCATCCTGGTGGGTCCAGGCACTGGCATTGCCCCC
TTCCGGGGATTCTGGCAGGAGCGGCTGCATGACATTGAGAGCAAAGGGCTGCAGCCCACT
CCCATGACTTTGGTGTTCGGCTGCCGATGCTCCCAACTTGACCATCTCTACCGCGACGAG
GTGCAGAACGCCCAGCAGCGCGGGGTGTTTGGCCGAGTCCTCACCGCCTTCTCCCGGGAA
CCTGACAACCCCAAGACCTACGTGCAGGACATCCTGAGGACGGAGCTGGCTGCGGAGGTG
CACCGCGTGCTGTGCCTCGAGCGGGGCCACATGTTTGTCTGCGGCGATGTTACCATGGCA
ACCAACGTCCTGCAGACCGTGCAGCGCATCCTGGCGACGGAGGGCGACATGGAGCTGGAC
GAGGCCGGCGACGTCATCGGCGTGCTGCGGGATCAGCAACGCTACCACGAAGACATTTTC
GGGCTCACGCTGCGCACCCAGGAGGTGACAAGCCGCATACGCACCCAGAGCTTTTCCTTG
CAGGAGCGTCAGTTGCGGGGCGCAGTGCCCTGGGCGTTCGACCCTCCCGGCTCAGACACC
AACAGCCCCTGA
Enzyme 80 GenBank Gene ID M93718 Link Image
Enzyme 80 GeneCard ID NOS3 Link Image
Enzyme 80 GenAtlas ID NOS3 Link Image
Enzyme 80 HGNC ID HGNC:7876 Link Image
Enzyme 80 Chromosome Location 7
Enzyme 80 Locus 7q36
Enzyme 80 SNPs SNPJam Report Link Image
Enzyme 80 General References
  1. Janssens SP, Shimouchi A, Quertermous T, Bloch DB, Bloch KD: Cloning and expression of a cDNA encoding human endothelium-derived relaxing factor/nitric oxide synthase. J Biol Chem. 1992 Jul 25;267(21):14519-22. [PubMed Link Image]
  2. Marsden PA, Schappert KT, Chen HS, Flowers M, Sundell CL, Wilcox JN, Lamas S, Michel T: Molecular cloning and characterization of human endothelial nitric oxide synthase. FEBS Lett. 1992 Aug 3;307(3):287-93. [PubMed Link Image]
  3. Marsden PA, Heng HH, Scherer SW, Stewart RJ, Hall AV, Shi XM, Tsui LC, Schappert KT: Structure and chromosomal localization of the human constitutive endothelial nitric oxide synthase gene. J Biol Chem. 1993 Aug 15;268(23):17478-88. [PubMed Link Image]
  4. Nadaud S, Bonnardeaux A, Lathrop M, Soubrier F: Gene structure, polymorphism and mapping of the human endothelial nitric oxide synthase gene. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1027-33. [PubMed Link Image]
  5. Miyahara K, Kawamoto T, Sase K, Yui Y, Toda K, Yang LX, Hattori R, Aoyama T, Yamamoto Y, Doi Y, et al.: Cloning and structural characterization of the human endothelial nitric-oxide-synthase gene. Eur J Biochem. 1994 Aug 1;223(3):719-26. [PubMed Link Image]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  7. 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]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. Robinson LJ, Weremowicz S, Morton CC, Michel T: Isolation and chromosomal localization of the human endothelial nitric oxide synthase (NOS3) gene. Genomics. 1994 Jan 15;19(2):350-7. [PubMed Link Image]
  10. Sase K, Michel T: Expression of constitutive endothelial nitric oxide synthase in human blood platelets. Life Sci. 1995;57(22):2049-55. [PubMed Link Image]
  11. Garvey EP, Tuttle JV, Covington K, Merrill BM, Wood ER, Baylis SA, Charles IG: Purification and characterization of the constitutive nitric oxide synthase from human placenta. Arch Biochem Biophys. 1994 Jun;311(2):235-41. [PubMed Link Image]
  12. Dedio J, Konig P, Wohlfart P, Schroeder C, Kummer W, Muller-Esterl W: NOSIP, a novel modulator of endothelial nitric oxide synthase activity. FASEB J. 2001 Jan;15(1):79-89. [PubMed Link Image]
  13. Zimmermann K, Opitz N, Dedio J, Renne C, Muller-Esterl W, Oess S: NOSTRIN: a protein modulating nitric oxide release and subcellular distribution of endothelial nitric oxide synthase. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):17167-72. Epub 2002 Nov 21. [PubMed Link Image]
  14. Icking A, Matt S, Opitz N, Wiesenthal A, Muller-Esterl W, Schilling K: NOSTRIN functions as a homotrimeric adaptor protein facilitating internalization of eNOS. J Cell Sci. 2005 Nov 1;118(Pt 21):5059-69. Epub 2005 Oct 18. [PubMed Link Image]
  15. Schleicher M, Brundin F, Gross S, Muller-Esterl W, Oess S: Cell cycle-regulated inactivation of endothelial NO synthase through NOSIP-dependent targeting to the cytoskeleton. Mol Cell Biol. 2005 Sep;25(18):8251-8. [PubMed Link Image]
  16. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  17. Fischmann TO, Hruza A, Niu XD, Fossetta JD, Lunn CA, Dolphin E, Prongay AJ, Reichert P, Lundell DJ, Narula SK, Weber PC: Structural characterization of nitric oxide synthase isoforms reveals striking active-site conservation. Nat Struct Biol. 1999 Mar;6(3):233-42. [PubMed Link Image]
  18. Rosenfeld RJ, Garcin ED, Panda K, Andersson G, Aberg A, Wallace AV, Morris GM, Olson AJ, Stuehr DJ, Tainer JA, Getzoff ED: Conformational changes in nitric oxide synthases induced by chlorzoxazone and nitroindazoles: crystallographic and computational analyses of inhibitor potency. Biochemistry. 2002 Nov 26;41(47):13915-25. [PubMed Link Image]
  19. Yoshimura M, Yasue H, Nakayama M, Shimasaki Y, Sumida H, Sugiyama S, Kugiyama K, Ogawa H, Ogawa Y, Saito Y, Miyamoto Y, Nakao K: A missense Glu298Asp variant in the endothelial nitric oxide synthase gene is associated with coronary spasm in the Japanese. Hum Genet. 1998 Jul;103(1):65-9. [PubMed Link Image]
  20. Sofowora G, Dishy V, Xie HG, Imamura H, Nishimi Y, Morales CR, Morrow JD, Kim RB, Stein CM, Wood AJ: In-vivo effects of Glu298Asp endothelial nitric oxide synthase polymorphism. Pharmacogenetics. 2001 Dec;11(9):809-14. [PubMed Link Image]
  21. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 80 Metabolite References Not Available
Enzyme 81 [top]
Enzyme 81 ID 6234
Enzyme 81 Name Protein O-mannosyl-transferase 1
Enzyme 81 Synonyms
  1. Dolichyl-phosphate-mannose--protein mannosyltransferase 1
Enzyme 81 Gene Name POMT1
Enzyme 81 Protein Sequence >Protein O-mannosyl-transferase 1 
MWGFLKRPVVVTADINLSLVALTGMGLLSRLWRLTYPRAVVFDEVYYGQYISFYMKQIFF
LDDSGPPFGHMVLALGGYLGGFDGNFLWNRIGAEYSSNVPVWSLRLLPALAGALSVPMAY
QIVLELHFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFFNCQKHS
PFSLSWWFWLTLTGVACSCAVGIKYMGVFTYVLVLGVAAVHAWHLLGDQTLSNVGADVQC
CMRPACMGQMRMSQGVCVFCHLLARAVALLVIPVVLYLLFFYVHLILVFRSGPHDQIMSS
AFQASLEGGLARITQGQPLEVAFGSQVTLRNVFGKPVPCWLHSHQDTYPMIYENGRGSSH
QQQVTCYPFKDVNNWWIVKDPRRHQLVVSSPPRPVRHGDMVQLVHGMTTRSLNTHDVAAP
LSPHSQEVSCYIDYNISMPAQNLWRLEIVNRGSDTDVWKTILSEVRFVHVNTSAVLKLSG
AHLPDWGYRQLEIVGEKLSRGYHGSTVWNVEEHRYGASQEQRERERELHSPAQVDVSRNL
SFMARFSELQWRMLALRSDDSEHKYSSSPLEWVTLDTNIAYWLHPRTSAQIHLLGNIVIW
VSGSLALAIYALLSLWYLLRRRRNVHDLPQDAWLRWVLAGALCAGGWAVNYLPFFLMEKT
LFLYHYLPALTFQILLLPVVLQHISDHLCRSQLQRSIFSALVVAWYSSACHVSNTLRPLT
YGDKSLSPHELKALRWKDSWDILIRKH
Enzyme 81 Number of Residues 747
Enzyme 81 Molecular Weight 84908.0
Enzyme 81 Theoretical pI 8.55
Enzyme 81 GO Classification
Function
  • catalytic activity
  • mannosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid O-linked glycosylation
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • membrane
Enzyme 81 General Function Involved in mannosyltransferase activity
Enzyme 81 Specific Function Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient
Enzyme 81 Pathways Not Available
Enzyme 81 Reactions
  • dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein [RN:R04072 R07620]
Enzyme 81 Pfam Domain Function
Enzyme 81 Signals
  • None
Enzyme 81 Transmembrane Regions
  • 8-28 40-60 68-88 99-119 122-142 154-174 183-203 206-226 269-289 597-617 636-656 661-681
Enzyme 81 Essentiality Not Available
Enzyme 81 GenBank ID Protein 5257116 Link Image
Enzyme 81 UniProtKB/Swiss-Prot ID Q9Y6A1 Link Image
Enzyme 81 UniProtKB/Swiss-Prot Entry Name POMT1_HUMAN Link Image
Enzyme 81 PDB ID Not Available
Enzyme 81 Cellular Location Not Available
Enzyme 81 Gene Sequence >2244 bp 
ATGTGGGGATTTTTGAAGCGCCCTGTAGTGGTGACGGCTGACATCAACTTGAGCCTTGTG
GCCCTGACTGGGATGGGGTTACTGAGCCGGCTGTGGCGACTCACCTACCCGCGGGCTGTG
GTTTTTGACGAAGTATATTATGGGCAGTACATCTCTTTTTACATGAAACAAATCTTCTTC
TTGGATGACAGTGGGCCGCCATTTGGCCACATGGTGCTGGCCTTGGGAGGTTATTTAGGA
GGATTCGATGGCAATTTTTTGTGGAACAGAATTGGAGCAGAATACAGTAGCAACGTGCCT
GTGTGGTCCCTGCGCCTGCTGCCAGCACTCGCGGGGGCCTTGTCGGTCCCCATGGCCTAC
CAGATAGTGTTGGAGCTCCACTTTTCTCATTGTGCCGCCATGGGAGCTGCTCTGTTGATG
CTTATCAAGAATGCTCTCATCACTCAGTCAAGGCTAATGCTTTTGGAATCAGTGTTAATA
TTTTTCAATCTATTGGCCGTGTTGTCCTACCTGAAGTTCTTCAACTGCCAAAAGCACAGC
CCTTTTTCTCTGAGCTGGTGGTTCTGGCTAACACTGACAGGGGTCGCTTGTTCCTGTGCA
GTGGGCATCAAGTACATGGGTGTGTTCACGTACGTGCTCGTGCTGGGTGTTGCAGCTGTC
CATGCCTGGCACCTGCTTGGAGACCAGACTTTGTCCAATGTAGGTGCTGATGTCCAGTGC
TGCATGAGGCCGGCCTGTATGGGGCAGATGCGGATGTCACAGGGGGTCTGTGTGTTCTGT
CACTTGCTCGCCCGAGCAGTGGCTTTGCTGGTCATCCCGGTCGTCCTGTACTTACTGTTC
TTCTACGTCCACTTGATTCTAGTCTTCCGCTCTGGGCCCCACGACCAAATCATGTCCAGT
GCCTTCCAGGCCAGCTTAGAGGGAGGACTAGCTCGGATCACCCAGGGTCAGCCACTGGAG
GTGGCCTTTGGGTCCCAGGTCACTCTGAGGAACGTCTTTGGGAAACCTGTGCCCTGCTGG
CTTCATTCCCACCAGGACACCTACCCCATGATATATGAGAACGGCCGAGGCAGCTCCCAC
CAGCAACAGGTGACCTGTTACCCCTTCAAAGACGTCAATAACTGGTGGATTGTAAAGGAT
CCCAGGAGGCACCAGCTGGTGGTGAGCAGCCCTCCGAGACCTGTGAGGCACGGGGACATG
GTGCAGCTGGTCCACGGCATGACCACCCGCTCCCTGAACACGCATGATGTTGCAGCCCCC
CTGAGCCCCCATTCACAGGAGGTCTCCTGCTACATTGACTATAACATCTCCATGCCCGCC
CAGAACCTCTGGAGACTGGAAATTGTGAACAGAGGATCTGACACAGACGTCTGGAAGACC
ATCCTCTCAGAGGTCCGCTTTGTGCACGTGAACACTTCCGCTGTCTTAAAGCTGAGCGGG
GCTCACCTCCCTGACTGGGGGTATCGGCAACTGGAGATCGTCGGGGAGAAGCTGTCCCGG
GGCTACCACGGGAGCACGGTGTGGAACGTGGAGGAGCACCGATACGGCGCGAGCCAGGAG
CAGAGGGAGCGGGAACGGGAGCTGCACTCACCTGCGCAGGTGGACGTCAGCAGGAACCTC
AGCTTCATGGCGAGATTCTCGGAGCTGCAGTGGAGGATGCTGGCGCTGAGAAGTGATGAC
TCGGAACACAAGTACAGCTCCAGCCCACTGGAGTGGGTCACCCTGGACACCAATATTGCC
TACTGGCTGCACCCCAGGACCAGCGCTCAGATCCACCTACTTGGAAACATAGTGATCTGG
GTTTCGGGCAGCCTCGCTCTGGCCATCTACGCCCTGCTGTCCTTGTGGTACCTGCTCCGA
CGGCGAAGAAATGTCCATGACCTCCCTCAGGATGCCTGGCTGCGCTGGGTGCTGGCTGGG
GCGCTGTGTGCCGGTGGCTGGGCAGTGAACTACCTCCCGTTCTTCCTGATGGAGAAGACA
CTCTTCCTCTACCACTACCTGCCCGCACTCACCTTCCAAATCCTTCTGCTCCCTGTGGTC
CTGCAGCACATCAGCGACCACCTGTGCAGGTCCCAGCTCCAGAGGAATTCTTTCAGCGCC
CTGGTGGTGGCCTGGTACTCCTCCGCGTGCCACGTGTCCAACACGCTGCGCCCACTCACC
TACGGGGACAAGTCACTCTCGCCACATGAACTCAAGGCCCTTCGCTGGAAAGACAGCTGG
GACATCTTGATCCGAAAACACTAG
Enzyme 81 GenBank Gene ID AF095136 Link Image
Enzyme 81 GeneCard ID POMT1 Link Image
Enzyme 81 GenAtlas ID POMT1 Link Image
Enzyme 81 HGNC ID HGNC:9202 Link Image
Enzyme 81 Chromosome Location 9
Enzyme 81 Locus 9q34.1
Enzyme 81 SNPs SNPJam Report Link Image
Enzyme 81 General References
  1. Jurado LA, Coloma A, Cruces J: Identification of a human homolog of the Drosophila rotated abdomen gene (POMT1) encoding a putative protein O-mannosyl-transferase, and assignment to human chromosome 9q34.1. Genomics. 1999 Jun 1;58(2):171-80. [PubMed Link Image]
  2. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed Link Image]
  3. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Manya H, Chiba A, Yoshida A, Wang X, Chiba Y, Jigami Y, Margolis RU, Endo T: Demonstration of mammalian protein O-mannosyltransferase activity: coexpression of POMT1 and POMT2 required for enzymatic activity. Proc Natl Acad Sci U S A. 2004 Jan 13;101(2):500-5. Epub 2003 Dec 29. [PubMed Link Image]
  7. Beltran-Valero de Bernabe D, Currier S, Steinbrecher A, Celli J, van Beusekom E, van der Zwaag B, Kayserili H, Merlini L, Chitayat D, Dobyns WB, Cormand B, Lehesjoki AE, Cruces J, Voit T, Walsh CA, van Bokhoven H, Brunner HG: Mutations in the O-mannosyltransferase gene POMT1 give rise to the severe neuronal migration disorder Walker-Warburg syndrome. Am J Hum Genet. 2002 Nov;71(5):1033-43. Epub 2002 Oct 4. [PubMed Link Image]
  8. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  9. Kim DS, Hayashi YK, Matsumoto H, Ogawa M, Noguchi S, Murakami N, Sakuta R, Mochizuki M, Michele DE, Campbell KP, Nonaka I, Nishino I: POMT1 mutation results in defective glycosylation and loss of laminin-binding activity in alpha-DG. Neurology. 2004 Mar 23;62(6):1009-11. [PubMed Link Image]
  10. Currier SC, Lee CK, Chang BS, Bodell AL, Pai GS, Job L, Lagae LG, Al-Gazali LI, Eyaid WM, Enns G, Dobyns WB, Walsh CA: Mutations in POMT1 are found in a minority of patients with Walker-Warburg syndrome. Am J Med Genet A. 2005 Feb 15;133A(1):53-7. [PubMed Link Image]
  11. Balci B, Uyanik G, Dincer P, Gross C, Willer T, Talim B, Haliloglu G, Kale G, Hehr U, Winkler J, Topaloglu H: An autosomal recessive limb girdle muscular dystrophy (LGMD2) with mild mental retardation is allelic to Walker-Warburg syndrome (WWS) caused by a mutation in the POMT1 gene. Neuromuscul Disord. 2005 Apr;15(4):271-5. [PubMed Link Image]
Enzyme 81 Metabolite References Not Available
Enzyme 82 [top]
Enzyme 82 ID 6235
Enzyme 82 Name Protein O-mannosyl-transferase 2
Enzyme 82 Synonyms
  1. Dolichyl-phosphate-mannose--protein mannosyltransferase 2
Enzyme 82 Gene Name POMT2
Enzyme 82 Protein Sequence >Protein O-mannosyl-transferase 2 
MPPATGGGLAESELRPRRGRCGPQAARAAGRDVAAEAVARSPKRPAWGSRRFEAVGWWAL
LALVTLLSFATRFHRLDEPPHICWDETHFGKMGSYYINRTFFFDVHPPLGKMLIGLAGYL
SGYDGTFLFQKPGDKYEHHSYMGMRGFCAFLGSWLVPFAYLTVLDLSKSLSAALLTAALL
TFDTGCLTLSQYILLDPILMFFIMAAMLSMVKYNSCADRPFSAPWWFWLSLTGVSLAGAL
GVKFVGLFIILQVGLNTIADLWYLFGDLSLSLVTVGKHLTARVLCLIVLPLALYTATFAV
HFMVLSKSGPGDGFFSSAFQARLSGNNLHNASIPEHLAYGSVITVKNLRMAIGYLHSHRH
LYPEGIGARQQQVTTYLHKDYNNLWIIKKHNTNSDPLDPSFPVEFVRHGDIIRLEHKETS
RNLHSHYHEAPMTRKHYQVTGYGINGTGDSNDFWRIEVVNRKFGNRIKVLRSRIRFIHLV
TGCVLGSSGKVLPKWGWEQLEVTCTPYLKETLNSIWNVEDHINPKLPNISLDVLQPSFPE
ILLESHMVMIRGNSGLKPKDNEFTSKPWHWPINYQGLRFSGVNDTDFRVYLLGNPVVWWL
NLLSIALYLLSGSIIAVAMQRGARLPAEVAGLSQVLLRGGGQVLLGWTLHYFPFFLMGRV
LYFHHYFPAMLFSSMLTGILWDTLLRLCAWGLASWPLARGIHVAGILSLLLGTAYSFYLF
HPLAYGMVGPLAQDPQSPMAGLRWLDSWDF
Enzyme 82 Number of Residues 750
Enzyme 82 Molecular Weight 84213.2
Enzyme 82 Theoretical pI 9.43
Enzyme 82 GO Classification
Function
  • catalytic activity
  • mannosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid O-linked glycosylation
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • membrane
Enzyme 82 General Function Involved in mannosyltransferase activity
Enzyme 82 Specific Function Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient
Enzyme 82 Pathways Not Available
Enzyme 82 Reactions
  • dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein [RN:R04072 R07620]
Enzyme 82 Pfam Domain Function
Enzyme 82 Signals
  • None
Enzyme 82 Transmembrane Regions
  • 54-74 100-120 146-166 191-211 231-251 283-303 596-616 643-663 665-685 700-720
Enzyme 82 Essentiality Not Available
Enzyme 82 GenBank ID Protein 32455271 Link Image
Enzyme 82 UniProtKB/Swiss-Prot ID Q9UKY4 Link Image
Enzyme 82 UniProtKB/Swiss-Prot Entry Name POMT2_HUMAN Link Image
Enzyme 82 PDB ID Not Available
Enzyme 82 Cellular Location Not Available
Enzyme 82 Gene Sequence >2253 bp 
ATGCCGCCGGCCACGGGCGGAGGCCTGGCAGAGTCCGAGCTGCGTCCCCGGAGGGGCCGC
TGTGGCCCCCAGGCTGCTAGGGCCGCAGGCCGGGACGTGGCCGCTGAGGCTGTGGCGCGA
AGCCCCAAACGGCCTGCTTGGGGCTCACGGCGCTTCGAGGCGGTCGGCTGGTGGGCCCTG
CTGGCCTTGGTGACGCTGCTGTCCTTCGCCACCCGCTTCCACCGCTTGGACGAGCCGCCG
CACATCTGTTGGGATGAGACTCACTTTGGAAAAATGGGAAGTTACTATATCAACCGTACA
TTTTTCTTTGATGTGCACCCGCCCCTGGGAAAGATGCTGATAGGTCTTGCTGGCTACCTG
AGTGGATATGATGGTACCTTTTTGTTCCAGAAGCCTGGGGATAAATATGAGCATCACAGC
TACATGGGAATGAGAGGATTCTGTGCATTCCTTGGCTCCTGGCTGGTCCCCTTTGCCTAC
CTCACTGTACTGGATCTGTCCAAGTCCCTCTCGGCAGCACTGCTCACAGCTGCCCTCCTC
ACCTTTGACACGGGATGCCTCACTCTGTCCCAGTACATCCTCCTTGACCCCATCCTGATG
TTCTTCATCATGGCTGCCATGCTGAGCATGGTCAAGTACAACTCTTGCGCCGACAGGCCC
TTCTCTGCCCCCTGGTGGTTCTGGCTCAGCCTGACTGGCGTTAGTCTTGCTGGTGCTTTA
GGGGTCAAGTTTGTTGGCCTCTTTATCATCCTTCAAGTGGGGCTGAACACCATTGCAGAC
CTTTGGTACCTGTTCGGAGACCTCAGTCTTTCATTGGTGACTGTGGGAAAACACCTGACT
GCTCGTGTCCTGTGCCTCATAGTGCTGCCCCTGGCTCTCTATACAGCCACCTTTGCTGTT
CACTTCATGGTGCTGAGTAAAAGTGGCCCTGGTGACGGTTTCTTCAGTTCTGCCTTCCAG
GCCCGGCTTTCAGGGAACAACCTGCACAATGCTTCCATCCCTGAACACCTGGCCTACGGC
TCTGTGATCACTGTGAAGAACCTCCGGATGGCCATCGGCTATCTGCACTCCCACAGGCAC
CTCTACCCCGAGGGCATTGGTGCCCGTCAGCAGCAGGTCACCACCTATTTGCACAAGGAC
TACAACAACCTGTGGATTATCAAGAAACATAACACAAACTCAGATCCCCTAGACCCTTCC
TTCCCAGTGGAGTTTGTAAGACATGGAGACATTATTCGACTAGAACACAAAGAAACTTCC
CGGAACTTGCACAGTCACTATCATGAGGCCCCCATGACCCGGAAGCACTATCAGGTCACC
GGCTATGGCATAAATGGAACAGGGGACTCAAATGATTTCTGGCGGATTGAGGTCGTAAAC
AGAAAATTTGGAAACCGGATCAAAGTGCTGAGAAGTCGAATTCGCTTCATCCATTTGGTC
ACAGGTTGTGTCCTGGGCTCCTCGGGAAAGGTTCTGCCCAAGTGGGGCTGGGAGCAGTTG
GAAGTTACTTGCACCCCATACCTGAAAGAAACCCTCAACTCCATCTGGAATGTGGAGGAC
CATATCAATCCCAAGTTGCCAAACATCAGCCTGGATGTGCTACAGCCCAGTTTTCCTGAG
ATCTTGCTGGAATCCCACATGGTCATGATCCGGGGGAACAGTGGCCTCAAACCCAAGGAC
AATGAGTTCACGTCCAAACCCTGGCACTGGCCTATCAACTATCAGGGCCTACGCTTCTCA
GGGGTCAATGACACAGATTTCCGAGTCTATCTGCTTGGCAACCCGGTGGTTTGGTGGCTG
AATCTGTTGAGCATCGCCCTCTACCTCCTCTCAGGGAGCATCATTGCTGTAGCCATGCAG
AGAGGGGCACGGCTGCCAGCGGAGGTTGCAGGGTTGTCCCAGGTCCTGCTGCGAGGAGGC
GGCCAGGTCCTGCTCGGCTGGACACTCCATTACTTCCCGTTTTTCCTGATGGGCCGGGTC
CTCTACTTCCACCACTACTTCCCAGCCATGCTCTTCTCAAGCATGTTGACAGGCATTCTG
TGGGACACCCTCCTGCGGCTCTGTGCCTGGGGCTTGGCCTCATGGCCCCTGGCGAGGGGC
ATACATGTGGCGGGAATCCTGAGCCTGCTCCTGGGAACTGCCTACAGCTTCTACCTCTTC
CACCCTCTGGCTTACGGGATGGTTGGTCCCCTGGCCCAGGACCCCCAAAGTCCAATGGCA
GGACTAAGGTGGCTGGACTCATGGGACTTTTGA
Enzyme 82 GenBank Gene ID NM_013382.5 Link Image
Enzyme 82 GeneCard ID POMT2 Link Image
Enzyme 82 GenAtlas ID POMT2 Link Image
Enzyme 82 HGNC ID HGNC:19743 Link Image
Enzyme 82 Chromosome Location 1
Enzyme 82 Locus 14q24
Enzyme 82 SNPs SNPJam Report Link Image
Enzyme 82 General References
  1. Willer T, Amselgruber W, Deutzmann R, Strahl S: Characterization of POMT2, a novel member of the PMT protein O-mannosyltransferase family specifically localized to the acrosome of mammalian spermatids. Glycobiology. 2002 Nov;12(11):771-83. [PubMed Link Image]
  2. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Manya H, Chiba A, Yoshida A, Wang X, Chiba Y, Jigami Y, Margolis RU, Endo T: Demonstration of mammalian protein O-mannosyltransferase activity: coexpression of POMT1 and POMT2 required for enzymatic activity. Proc Natl Acad Sci U S A. 2004 Jan 13;101(2):500-5. Epub 2003 Dec 29. [PubMed Link Image]
  6. van Reeuwijk J, Janssen M, van den Elzen C, Beltran-Valero de Bernabe D, Sabatelli P, Merlini L, Boon M, Scheffer H, Brockington M, Muntoni F, Huynen MA, Verrips A, Walsh CA, Barth PG, Brunner HG, van Bokhoven H: POMT2 mutations cause alpha-dystroglycan hypoglycosylation and Walker-Warburg syndrome. J Med Genet. 2005 Dec;42(12):907-12. Epub 2005 May 13. [PubMed Link Image]
Enzyme 82 Metabolite References Not Available
Enzyme 83 [top]
Enzyme 83 ID 6237
Enzyme 83 Name 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase
Enzyme 83 Synonyms
  1. Cholestenol Delta-isomerase
  2. Delta(8)-Delta(7) sterol isomerase
  3. D8-D7 sterol isomerase
  4. Emopamil-binding protein
Enzyme 83 Gene Name EBP
Enzyme 83 Protein Sequence >3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase 
MTTNAGPLHPYWPQHLRLDNFVPNDRPTWHILAGLFSVTGVLVVTTWLLSGRAAVVPLGT
WRRLSLCWFAVCGFIHLVIEGWFVLYYEDLLGDQAFLSQLWKEYAKGDSRYILGDNFTVC
METITACLWGPLSLWVVIAFLRQHPLRFILQLVVSVGQIYGDVLYFLTEHRDGFQHGELG
HPLYFWFYFVFMNALWLVLPGVLVLDAVKHLTHAQSTLDAKATKAKSKKN
Enzyme 83 Number of Residues 230
Enzyme 83 Molecular Weight 26352.6
Enzyme 83 Theoretical pI 8.02
Enzyme 83 GO Classification
Function
  • catalytic activity
  • cholestenol delta-isomerase activity
  • intramolecular oxidoreductase activity
  • intramolecular oxidoreductase activity, transposing C=C bonds
  • isomerase activity
Process
  • alcohol metabolic process
  • metabolic process
  • small molecule metabolic process
  • sterol metabolic process
Component
  • cell part
  • endoplasmic reticulum
  • integral to membrane
  • intracellular membrane-bounded organelle
  • intrinsic to membrane
  • membrane part
  • membrane-bounded organelle
  • organelle
Enzyme 83 General Function Involved in cholestenol delta-isomerase activity
Enzyme 83 Specific Function Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers
Enzyme 83 Pathways
Enzyme 83 Reactions
  • 5alpha-cholest-7-en-3beta-ol = 5alpha-cholest-8-en-3beta-ol [RN:R03353]
Enzyme 83 Pfam Domain Function
Enzyme 83 Signals
  • None
Enzyme 83 Transmembrane Regions
  • 29-49 66-86 121-141 185-205
Enzyme 83 Essentiality Not Available
Enzyme 83 GenBank ID Protein 5729810 Link Image
Enzyme 83 UniProtKB/Swiss-Prot ID Q15125 Link Image
Enzyme 83 UniProtKB/Swiss-Prot Entry Name EBP_HUMAN Link Image
Enzyme 83 PDB ID Not Available
Enzyme 83 Cellular Location Not Available
Enzyme 83 Gene Sequence >693 bp 
ATGACTACCAACGCGGGCCCCTTGCACCCATACTGGCCTCAGCACCTAAGACTGGACAAC
TTTGTACCTAATGACCGCCCCACCTGGCATATACTGGCTGGCCTCTTCTCTGTCACAGGG
GTCTTAGTCGTGACCACATGGCTGTTGTCAGGTCGTGCTGCGGTTGTCCCATTGGGGACT
TGGCGGCGACTGTCCCTGTGCTGGTTTGCAGTGTGTGGGTTCATTCACCTGGTGATCGAG
GGCTGGTTCGTTCTCTACTACGAAGACCTGCTTGGAGACCAAGCCTTCTTATCTCAACTC
TGGAAAGAGTATGCCAAGGGAGACAGCCGATACATCCTGGGTGACAACTTCACAGTGTGC
ATGGAAACCATCACAGCTTGCCTGTGGGGACCACTCAGCCTGTGGGTGGTGATCGCCTTT
CTCCGCCAGCATCCCCTCCGCTTCATTCTACAGCTTGTGGTCTCTGTGGGCCAGATCTAT
GGGGATGTGCTCTACTTCCTGACAGAGCACCGCGACGGATTCCAGCACGGAGAGCTGGGC
CACCCTCTCTACTTCTGGTTTTACTTTGTCTTCATGAATGCCCTGTGGCTGGTGCTGCCT
GGAGTCCTTGTGCTTGATGCTGTGAAGCACCTCACTCATGCCCAGAGCACGCTGGATGCC
AAGGCCACAAAAGCCAAGAGCAAGAAGAACTGA
Enzyme 83 GenBank Gene ID NM_006579.2 Link Image
Enzyme 83 GeneCard ID EBP Link Image
Enzyme 83 GenAtlas ID EBP Link Image
Enzyme 83 HGNC ID HGNC:3133 Link Image
Enzyme 83 Chromosome Location Not Available
Enzyme 83 Locus Not Available
Enzyme 83 SNPs SNPJam Report Link Image
Enzyme 83 General References
  1. Hanner M, Moebius FF, Weber F, Grabner M, Striessnig J, Glossmann H: Phenylalkylamine Ca2+ antagonist binding protein. Molecular cloning, tissue distribution, and heterologous expression. J Biol Chem. 1995 Mar 31;270(13):7551-7. [PubMed Link Image]
  2. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Moebius FF, Soellner KE, Fiechtner B, Huck CW, Bonn G, Glossmann H: Histidine77, glutamic acid81, glutamic acid123, threonine126, asparagine194, and tryptophan197 of the human emopamil binding protein are required for in vivo sterol delta 8-delta 7 isomerization. Biochemistry. 1999 Jan 19;38(3):1119-27. [PubMed Link Image]
  5. Moebius FF, Fitzky BU, Wietzorrek G, Haidekker A, Eder A, Glossmann H: Cloning of an emopamil-binding protein (EBP)-like protein that lacks sterol delta8-delta7 isomerase activity. Biochem J. 2003 Aug 15;374(Pt 1):229-37. [PubMed Link Image]
  6. Derry JM, Gormally E, Means GD, Zhao W, Meindl A, Kelley RI, Boyd Y, Herman GE: Mutations in a delta 8-delta 7 sterol isomerase in the tattered mouse and X-linked dominant chondrodysplasia punctata. jderry@immunex.com. Nat Genet. 1999 Jul;22(3):286-90. [PubMed Link Image]
  7. Braverman N, Lin P, Moebius FF, Obie C, Moser A, Glossmann H, Wilcox WR, Rimoin DL, Smith M, Kratz L, Kelley RI, Valle D: Mutations in the gene encoding 3 beta-hydroxysteroid-delta 8, delta 7-isomerase cause X-linked dominant Conradi-Hunermann syndrome. Nat Genet. 1999 Jul;22(3):291-4. [PubMed Link Image]
  8. Has C, Bruckner-Tuderman L, Muller D, Floeth M, Folkers E, Donnai D, Traupe H: The Conradi-Hunermann-Happle syndrome (CDPX2) and emopamil binding protein: novel mutations, and somatic and gonadal mosaicism. Hum Mol Genet. 2000 Aug 12;9(13):1951-5. [PubMed Link Image]
  9. Becker K, Csikos M, Horvath A, Karpati S: Identification of a novel mutation in 3beta-hydroxysteroid-Delta8-Delta7-isomerase in a case of Conradi-Hunermann-Happle syndrome. Exp Dermatol. 2001 Aug;10(4):286-9. [PubMed Link Image]
Enzyme 83 Metabolite References Not Available
Enzyme 84 [top]
Enzyme 84 ID 6260
Enzyme 84 Name Arachidonate 5-lipoxygenase
Enzyme 84 Synonyms
  1. 5-LO
  2. 5-lipoxygenase
Enzyme 84 Gene Name ALOX5
Enzyme 84 Protein Sequence >Arachidonate 5-lipoxygenase 
MPSYTVTVATGSQWFAGTDDYIYLSLVGSAGCSEKHLLDKPFYNDFERGAVDSYDVTVDE
ELGEIQLVRIEKRKYWLNDDWYLKYITLKTPHGDYIEFPCYRWITGDVEVVLRDGRAKLA
RDDQIHILKQHRRKELETRQKQYRWMEWNPGFPLSIDAKCHKDLPRDIQFDSEKGVDFVL
NYSKAMENLFINRFMHMFQSSWNDFADFEKIFVKISNTISERVMNHWQEDLMFGYQFLNG
CNPVLIRRCTELPEKLPVTTEMVECSLERQLSLEQEVQQGNIFIVDFELLDGIDANKTDP
CTLQFLAAPICLLYKNLANKIVPIAIQLNQIPGDENPIFLPSDAKYDWLLAKIWVRSSDF
HVHQTITHLLRTHLVSEVFGIAMYRQLPAVHPIFKLLVAHVRFTIAINTKAREQLICECG
LFDKANATGGGGHVQMVQRAMKDLTYASLCFPEAIKARGMESKEDIPYYFYRDDGLLVWE
AIRTFTAEVVDIYYEGDQVVEEDPELQDFVNDVYVYGMRGRKSSGFPKSVKSREQLSEYL
TVVIFTASAQHAAVNFGQYDWCSWIPNAPPTMRAPPPTAKGVVTIEQIVDTLPDRGRSCW
HLGAVWALSQFQENELFLGMYPEEHFIEKPVKEAMARFRKNLEAIVSVIAERNKKKQLPY
YYLSPDRIPNSVAI
Enzyme 84 Number of Residues 674
Enzyme 84 Molecular Weight 77982.6
Enzyme 84 Theoretical pI 5.54
Enzyme 84 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • iron ion binding
  • lipoxygenase activity
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
  • oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
  • transition metal ion binding
Process
  • carboxylic acid metabolic process
  • cellular metabolic process
  • fatty acid metabolic process
  • icosanoid metabolic process
  • leukotriene metabolic process
  • metabolic process
  • monocarboxylic acid metabolic process
  • organic acid metabolic process
  • oxidation reduction
  • oxoacid metabolic process
  • unsaturated fatty acid metabolic process
Component
—
Enzyme 84 General Function Involved in metal ion binding
Enzyme 84 Specific Function Catalyzes the first step in leukotriene biosynthesis, and thereby plays a role in inflammatory processes
Enzyme 84 Pathways
Enzyme 84 Reactions
  • (1) arachidonate + O2 = (5S,6S,7E,9E,11Z,14Z)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O (overall reaction) [RN:R08527]
  • (2) (1a) arachidonate + O2 = (5S,6E,8Z,11Z,14Z)-5-hydroperoxyicosa-6,8,11,14-tetraenoate [RN:R01595]
  • (3) (1b) (5S,6E,8Z,11Z,14Z)-5-hydroperoxyicosa-6,8,11,14-tetraenoate = (5S,6S,7E,9E,11Z,14Z)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O [RN:R03058]
Enzyme 84 Pfam Domain Function
Enzyme 84 Signals
  • None
Enzyme 84 Transmembrane Regions
  • None
Enzyme 84 Essentiality Not Available
Enzyme 84 GenBank ID Protein Not Available
Enzyme 84 UniProtKB/Swiss-Prot ID P09917 Link Image
Enzyme 84 UniProtKB/Swiss-Prot Entry Name LOX5_HUMAN Link Image
Enzyme 84 PDB ID Not Available
Enzyme 84 Cellular Location Not Available
Enzyme 84 Gene Sequence >2025 bp 
ATGCCCTCCTACACGGTCACCGTGGCCACTGGCAGCCAGTGGTTCGCCGGCACTGACGAC
TACATCTACCTCAGCCTCGTGGGCTCGGCGGGCTGCAGCGAGAAGCACCTGCTGGACAAG
CCCTTCTACAACGACTTCGAGCGTGGCGCGGTGGATTCATACGACGTGACTGTGGACGAG
GAACTGGGCGAGATCCAGCTGGTCAGAATCGAGAAGCGCAAGTACTGGCTGAATGACGAC
TGGTACCTGAAGTACATCACGCTGAAGACGCCCCACGGGGACTACATCGAGTTCCCCTGC
TACCGCTGGATCACCGGCGATGTCGAGGTTGTCCTGAGGGATGGACGCGCAAAGTTGGCC
CGAGATGACCAAATTCACATTCTCAAGCAACACCGACGTAAAGAACTGGAAACACGGCAA
AAACAATATCGATGGATGGAGTGGAACCCTGGCTTCCCCTTGAGCATCGATGCCAAATGC
CACAAGGATTTACCCCGTGATATCCAGTTTGATAGTGAAAAAGGAGTGGACTTTGTTCTG
AATTACTCCAAAGCGATGGAGAACCTGTTCATCAACCGCTTCATGCACATGTTCCAGTCT
TCTTGGAATGACTTCGCCGACTTTGAGAAAATCTTTGTCAAGATCAGCAACACTATTTCT
GAGCGGGTCATGAATCACTGGCAGGAAGACCTGATGTTTGGCTACCAGTTCCTGAATGGC
TGCAACCCTGTGTTGATCCGGCGCTGCACAGAGCTGCCCGAGAAGCTCCCGGTGACCACG
GAGATGGTAGAGTGCAGCCTGGAGCGGCAGCTCAGCTTGGAGCAGGAGGTCCAGCAAGGG
AACATTTTCATCGTGGACTTTGAGCTGCTGGATGGCATCGATGCCAACAAAACAGACCCC
TGCACACTCCAGTTCCTGGCCGCTCCCATCTGCTTGCTGTATAAGAACCTGGCCAACAAG
ATTGTCCCCATTGCCATCCAGCTCAACCAAATCCCGGGAGATGAGAACCCTATTTTCCTC
CCTTCGGATGCAAAATACGACTGGCTTTTGGCCAAAATCTGGGTGCGTTCCAGTGACTTC
CACGTCCACCAGACCATCACCCACCTTCTGCGAACACATCTGGTGTCTGAGGTTTTTGGC
ATTGCAATGTACCGCCAGCTGCCTGCTGTGCACCCCATTTTCAAGCTGCTGGTGGCACAC
GTGAGATTCACCATTGCAATCAACACCAAGGCCCGTGAGCAGCTCATCTGCGAGTGTGGC
CTCTTTGACAAGGCCAACGCCACAGGGGGCGGTGGGCACGTGCAGATGGTGCAGAGGGCC
ATGAAGGACCTGACCTATGCCTCCCTGTGCTTTCCCGAGGCCATCAAGGCCCGGGGCATG
GAGAGCAAAGAAGACATCCCCTACTACTTCTACCGGGACGACGGGCTCCTGGTGTGGGAA
GCCATCAGGACGTTCACGGCCGAGGTGGTAGACATCTACTACGAGGGCGACCAGGTGGTG
GAGGAGGACCCGGAGCTGCAGGACTTCGTGAACGATGTCTACGTGTACGGCATGCGGGGC
CGCAAGTCCTCAGGCTTCCCCAAGTCGGTCAAGAGCCGGGAGCAGCTGTCGGAGTACCTG
ACCGTGGTGATCTTCACCGCCTCCGCCCAGCACGCCGCGGTCAACTTCGGCCAGTACGAC
TGGTGCTCCTGGATCCCCAATGCGCCCCCAACCATGCGAGCCCCGCCACCGACTGCCAAG
GGCGTGGTGACCATTGAGCAGATCGTGGACACGCTGCCCGACCGCGGCCGCTCCTGCTGG
CATCTGGGTGCAGTGTGGGCGCTGAGCCAGTTCCAGGAAAACGAGCTGTTCCTGGGCATG
TACCCAGAAGAGCATTTTATCGAGAAGCCTGTGAAGGAAGCCATGGCCCGATTCCGCAAG
AACCTCGAGGCCATTGTCAGCGTGATTGCTGAGCGCAACAAGAAGAAGCAGCTGCCATAT
TACTACTTGTCCCCAGACCGGATTCCGAACAGTGTGGCCATCTGA
Enzyme 84 GenBank Gene ID J03600 Link Image
Enzyme 84 GeneCard ID ALOX5 Link Image
Enzyme 84 GenAtlas ID ALOX5 Link Image
Enzyme 84 HGNC ID HGNC:435 Link Image
Enzyme 84 Chromosome Location 1
Enzyme 84 Locus 10q11.2
Enzyme 84 SNPs SNPJam Report Link Image
Enzyme 84 General References
  1. Dixon RA, Jones RE, Diehl RE, Bennett CD, Kargman S, Rouzer CA: Cloning of the cDNA for human 5-lipoxygenase. Proc Natl Acad Sci U S A. 1988 Jan;85(2):416-20. [PubMed Link Image]
  2. Matsumoto T, Funk CD, Radmark O, Hoog JO, Jornvall H, Samuelsson B: Molecular cloning and amino acid sequence of human 5-lipoxygenase. Proc Natl Acad Sci U S A. 1988 Jan;85(1):26-30. [PubMed Link Image]
  3. Matsumoto T, Funk CD, Radmark O, Hoog JO, Jornvall H, Samuelsson B: Molecular cloning and amino acid sequence of human 5-lipoxygenase. Adv Prostaglandin Thromboxane Leukot Res. 1989;19:466-9. [PubMed Link Image]
  4. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Funk CD, Hoshiko S, Matsumoto T, Rdmark O, Samuelsson B: Characterization of the human 5-lipoxygenase gene. Proc Natl Acad Sci U S A. 1989 Apr;86(8):2587-91. [PubMed Link Image]
  7. Hoshiko S, Radmark O, Samuelsson B: Characterization of the human 5-lipoxygenase gene promoter. Proc Natl Acad Sci U S A. 1990 Dec;87(23):9073-7. [PubMed Link Image]
  8. Rouzer CA, Samuelsson B: Reversible, calcium-dependent membrane association of human leukocyte 5-lipoxygenase. Proc Natl Acad Sci U S A. 1987 Nov;84(21):7393-7. [PubMed Link Image]
  9. Nguyen T, Falgueyret JP, Abramovitz M, Riendeau D: Evaluation of the role of conserved His and Met residues among lipoxygenases by site-directed mutagenesis of recombinant human 5-lipoxygenase. J Biol Chem. 1991 Nov 15;266(32):22057-62. [PubMed Link Image]
  10. Ishii S, Noguchi M, Miyano M, Matsumoto T, Noma M: Mutagenesis studies on the amino acid residues involved in the iron-binding and the activity of human 5-lipoxygenase. Biochem Biophys Res Commun. 1992 Feb 14;182(3):1482-90. [PubMed Link Image]
  11. Woods JW, Evans JF, Ethier D, Scott S, Vickers PJ, Hearn L, Heibein JA, Charleson S, Singer II: 5-lipoxygenase and 5-lipoxygenase-activating protein are localized in the nuclear envelope of activated human leukocytes. J Exp Med. 1993 Dec 1;178(6):1935-46. [PubMed Link Image]
  12. Werz O, Szellas D, Steinhilber D, Radmark O: Arachidonic acid promotes phosphorylation of 5-lipoxygenase at Ser-271 by MAPK-activated protein kinase 2 (MK2). J Biol Chem. 2002 Apr 26;277(17):14793-800. Epub 2002 Feb 13. [PubMed Link Image]
  13. Luo M, Jones SM, Phare SM, Coffey MJ, Peters-Golden M, Brock TG: Protein kinase A inhibits leukotriene synthesis by phosphorylation of 5-lipoxygenase on serine 523. J Biol Chem. 2004 Oct 1;279(40):41512-20. Epub 2004 Jul 26. [PubMed Link Image]
  14. Flamand N, Lefebvre J, Surette ME, Picard S, Borgeat P: Arachidonic acid regulates the translocation of 5-lipoxygenase to the nuclear membranes in human neutrophils. J Biol Chem. 2006 Jan 6;281(1):129-36. Epub 2005 Nov 7. [PubMed Link Image]
  15. Strid T, Svartz J, Franck N, Hallin E, Ingelsson B, Soderstrom M, Hammarstrom S: Distinct parts of leukotriene C(4) synthase interact with 5-lipoxygenase and 5-lipoxygenase activating protein. Biochem Biophys Res Commun. 2009 Apr 17;381(4):518-22. Epub 2009 Feb 20. [PubMed Link Image]
  16. Flamand N, Luo M, Peters-Golden M, Brock TG: Phosphorylation of serine 271 on 5-lipoxygenase and its role in nuclear export. J Biol Chem. 2009 Jan 2;284(1):306-13. Epub 2008 Nov 1. [PubMed Link Image]
  17. Goodman JE, Bowman ED, Chanock SJ, Alberg AJ, Harris CC: Arachidonate lipoxygenase (ALOX) and cyclooxygenase (COX) polymorphisms and colon cancer risk. Carcinogenesis. 2004 Dec;25(12):2467-72. Epub 2004 Aug 12. [PubMed Link Image]
Enzyme 84 Metabolite References Not Available
Enzyme 85 [top]
Enzyme 85 ID 6271
Enzyme 85 Name Inositol-trisphosphate 3-kinase B
Enzyme 85 Synonyms
  1. Inositol 1,4,5-trisphosphate 3-kinase B
  2. IP3 3-kinase B
  3. IP3K B
  4. InsP 3-kinase B
Enzyme 85 Gene Name ITPKB
Enzyme 85 Protein Sequence >Inositol-trisphosphate 3-kinase B 
MAVYCYALNSLVIMNSANEMKSGGGPGPSGSETPPPPRRAVLSPGSVFSPGRGASFLFPP
AESLSPEEPRSPGGWRSGRRRLNSSSGSGSGSSGSSVSSPSWAGRLRGDRQQVVAAGTLS
PPGPEEAKRKLRILQRELQNVQVNQKVGMFEAHIQAQSSAIQAPRSPRLGRARSPSPCPF
RSSSQPPGRVLVQGARSEERRTKSWGEQCPETSGTDSGRKGGPSLCSSQVKKGMPPLPGR
AAPTGSEAQGPSAFVRMEKGIPASPRCGSPTAMEIDKRGSPTPGTRSCLAPSLGLFGASL
TMATEVAARVTSTGPHRPQDLALTEPSGRARELEDLQPPEALVERQGQFLGSETSPAPER
GGPRDGEPPGKMGKGYLPCGMPGSGEPEVGKRPEETTVSVQSAESSDSLSWSRLPRALAS
VGPEEARSGAPVGGGRWQLSDRVEGGSPTLGLLGGSPSAQPGTGNVEAGIPSGRMLEPLP
CWDAAKDLKEPQCPPGDRVGVQPGNSRVWQGTMEKAGLAWTRGTGVQSEGTWESQRQDSD
ALPSPELLPQDPDKPFLRKACSPSNIPAVIITDMGTQEDGALEETQGSPRGNLPLRKLSS
SSASSTGFSSSYEDSEEDISSDPERTLDPNSAFLHTLDQQKPRVSKSWRKIKNMVHWSPF
VMSFKKKYPWIQLAGHAGSFKAAANGRILKKHCESEQRCLDRLMVDVLRPFVPAYHGDVV
KDGERYNQMDDLLADFDSPCVMDCKMGIRTYLEEELTKARKKPSLRKDMYQKMIEVDPEA
PTEEEKAQRAVTKPRYMQWRETISSTATLGFRIEGIKKEDGTVNRDFKKTKTREQVTEAF
REFTKGNHNILIAYRDRLKAIRTTLEVSPFFKCHEVIGSSLLFIHDKKEQAKVWMIDFGK
TTPLPEGQTLQHDVPWQEGNREDGYLSGLNNLVDILTEMSQDAPLA
Enzyme 85 Number of Residues 946
Enzyme 85 Molecular Weight 102375.3
Enzyme 85 Theoretical pI 8.56
Enzyme 85 GO Classification
Function
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • inositol trisphosphate 3-kinase activity
  • inositol trisphosphate kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
—
Component
—
Enzyme 85 General Function Involved in inositol trisphosphate 3-kinase activity
Enzyme 85 Specific Function ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
Enzyme 85 Pathways
Enzyme 85 Reactions
  • ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate [RN:R03433]
Enzyme 85 Pfam Domain Function
Enzyme 85 Signals
  • None
Enzyme 85 Transmembrane Regions
  • None
Enzyme 85 Essentiality Not Available
Enzyme 85 GenBank ID Protein 14329672 Link Image
Enzyme 85 UniProtKB/Swiss-Prot ID P27987 Link Image
Enzyme 85 UniProtKB/Swiss-Prot Entry Name IP3KB_HUMAN Link Image
Enzyme 85 PDB ID Not Available
Enzyme 85 Cellular Location Not Available
Enzyme 85 Gene Sequence >2841 bp 
ATGGCTGTGTACTGCTATGCGCTCAATAGCCTGGTGATCATGAATAGCGCCAACGAGATG
AAGAGCGGCGGCGGCCCGGGGCCCAGTGGCAGCGAGACGCCCCCGCCCCCGAGGAGGGCA
GTGCTGAGCCCCGGCAGCGTTTTCAGCCCCGGGAGAGGCGCCTCTTTCCTCTTCCCCCCA
GCCGAGTCGCTGTCCCCCGAGGAGCCCCGGAGCCCCGGGGGCTGGCGGAGCGGCCGGCGC
AGGCTGAATAGTAGCAGCGGCAGTGGCAGCGGCAGCAGCGGCAGTAGCGTGAGCAGCCCA
AGTTGGGCTGGTCGCCTGCGAGGGGACCGGCAGCAGGTGGTGGCAGCCGGTACCCTCTCC
CCGCCAGGGCCGGAGGAGGCCAAGAGGAAGCTGCGGATCTTGCAGCGCGAGTTGCAGAAC
GTGCAGGTGAACCAGAAAGTGGGCATGTTTGAGGCGCACATCCAGGCACAGAGCTCCGCC
ATTCAAGCGCCCCGCAGCCCGCGTTTGGGCAGGGCTCACTCGCCCTCCCCGTGCCCCTTC
CGCAGCAGCAGTCAGCCCCCTGGAAGGGTCCTGGTTCAGGGCGCCCGGAGCGAGGAACGG
AGGACAAAGTCCTGGGGGGAGCAATGTTCAGAGACTTCAGGAACCGACTCCGGGAGGAAA
GGAGGGCCCAGCCTATGCTCCTCGCAGGTGAAGAAAGGAATGCCACCTCTTCCCGGCCGG
GCTGCCCCTACAGGATCAGAGGCTCAGGGTCCATCCGCTTTTGTAAGGATGGAGAAGGGT
ATCCCTGCCAGTCCCCGCTGTGGCTCACCCACAGCTATGGAAATTGACAAAAGGGGCTCT
CCTACCCCGGGAACTCGGAGCTGCCTAGCTCCCTCATTGGGGCTGTTCGCCCCTAGCTTC
CCGATGGCCACGGAAGTGGCAGCGAGAGTTACATCCACTGGGCCACACCGTCCACAGGAT
CTTGCCCTCACTGAGCCGTCTGGGAGAGCCCGTGAGCTTGAGGACCTGCAGCCCCCAGAG
GCCCTGGTGGAGAGGCAGGGGCAGTTTCTGGGCAGTGAGACAAGCCCAGCCCCAGAAAGG
GGCGGGCCCCGCGATGGAGAACCCCCTGGGAAGATGGGGAAAGGATATCTGCCCTGTGGC
ATGCCGGGCTCTGGGGAGCCTGAAGTGGGCAAAAGGCCAGAGGAGACGACTGTGAGCGTG
CAAAGCGCAGAGTCCTCTGATTCCCTGAGCTGGTCCAGGCTGCCCAGGGCCCTGGCCTCC
GTAGGCCCTGAGGAGGCCCGAAGTGGGGCCCCCGTGGGCGGGGGGCGTTGGCAGCTCTCC
GACAGAGTGGAGGGAGGGTCCCCAACGCTGGGCTTGCTTGGGGGCAGCCCCTCAGCACAG
CCGGGGACCGGGAATGTGGAGGCGGGAATTCCTTCTGGCAGAATGCTGGAGCCTTTGCCC
TGTTGGGACGCTGCGAAAGATCTGAAAGAACCTCAGTGCCCTCCTGGGGACAGGGTGGGT
GTGCAGCCTGGGAACTCCAGGGTTTGGCAGGGCACCATGGAGAAAGCCGGTTTGGCTTGG
ACGCGTGGCACAGGGGTGCAATCAGAGGGGACTTGGGAAAGCCAGCGGCAGGACAGTGAT
GCCCTCCCAAGTCCGGAGCTGCTACCCCAAGATCAGGACAAGCCTTTCCTGAGGAAGGCC
TGCAGCCCCAGCAACATACCTGCTGTCATCATTACAGACATGGGCACCCAGGAGGATGGG
GCCTTGGAGGAGACGCAGGGAAGCCCTCGGGGCAACCTGCCCCTGAGGAAACTGTCCTCT
TCCTCGGCCTCCTCCACGGGCTTCTCCTCATCCTACGAAGACTCAGAGGAGGACATCTCC
AGTGACCCTGAGCGCACCCTGGACCCCAACTCAGCTTTCCTGCATACCCTGGACCAGCAG
AAACCTAGAGTGAGCAAATCATGGAGGAAGATAAAAAACATGGTGCACTGGTCTCCCTTC
GTCATGTCCTTCAAGAAGAAGTACCCCTGGATCCAGCTGGCAGGACACGCAGGGAGTTTC
AAGGCAGCTGCCAATGGCAGGATCCTGAAGAAGCACTGTGAGTCAGAGCAGCGCTGCCTG
GACCGGCTGATGGTGGATGTGCTGAGGCCCTTCGTACCTGCCTACCATGGGGATGTGGTG
AAGGACGGGGAGCGCTACAACCAGATGGACGACCTGCTGGCCGACTTCGACTCGCCCTGT
GTGATGGACTGCAAGATGGGAATCAGGACCTACCTGGAGGAGGAGCTCACGAAGGCCCGG
AAGAAGCCCAGCCTGCGGAAGGACATGTACCAGAAGATGATCGAGGTGGACCCCGAGGCC
CCCACCGAGGAGGAAAAAGCACAGCGGGCTGTGACCAAGCCACGGTACATGCAGTGGCGG
GAGACCATCAGCTCCACGGCCACCCTGGGGTTCAGGATCGAGGGAATCAAGAAAGAAGAC
GGCACCGTGAACCGGGACTTCAAGAAGACCAAAACGAGGGAGCAGGTCACCGAGGCCTTC
AGAGAGTTCACTAAAGGAAACCATAACATCCTGATCGCCTATCGGGACCGGCTGAAGGCC
ATTCGAACCACTCTAGAAGTTTCTCCCTTCTTCAAGTGCCACGAGGTCATTGGCAGCTCC
CTCCTCTTCATCCACGACAAGAAGGAACAGGCCAAAGTGTGGATGATCGACTTTGGGAAA
ACCACGCCCCTGCCTGAGGGCCAGACCCTGCAGCATGACGTCCCCTGGCAGGAGGGGAAC
CGGGAGGATGGCTACCTCTCGGGGCTCAATAACCTCGTCGACATCCTGACCGAGATGTCC
CAGGATGCCCCACTCGCCTGA
Enzyme 85 GenBank Gene ID AJ242780 Link Image
Enzyme 85 GeneCard ID ITPKB Link Image
Enzyme 85 GenAtlas ID ITPKB Link Image
Enzyme 85 HGNC ID HGNC:6179 Link Image
Enzyme 85 Chromosome Location 1
Enzyme 85 Locus 1q42.13
Enzyme 85 SNPs SNPJam Report Link Image
Enzyme 85 General References
  1. Dewaste V, Roymans D, Moreau C, Erneux C: Cloning and expression of a full-length cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase B. Biochem Biophys Res Commun. 2002 Feb 22;291(2):400-5. [PubMed Link Image]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Takazawa K, Perret J, Dumont JE, Erneux C: Molecular cloning and expression of a new putative inositol 1,4,5-trisphosphate 3-kinase isoenzyme. Biochem J. 1991 Sep 15;278 ( Pt 3):883-6. [PubMed Link Image]
  5. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  7. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 85 Metabolite References Not Available
Enzyme 86 [top]
Enzyme 86 ID 6272
Enzyme 86 Name Inositol-trisphosphate 3-kinase A
Enzyme 86 Synonyms
  1. Inositol 1,4,5-trisphosphate 3-kinase A
  2. IP3 3-kinase A
  3. IP3K A
  4. InsP 3-kinase A
Enzyme 86 Gene Name ITPKA
Enzyme 86 Protein Sequence >Inositol-trisphosphate 3-kinase A 
MTLPGGPTGMARPGGARPCSPGLERAPRRSVGELRLLFEARCAAVAAAAAAGEPRARGAK
RRGGQVPNGLPRAPPAPVIPQLTVTAEEPDVPPTSPGPPERERDCLPAAGSSHLQQPRRL
STSSVSSTGSSSLLEDSEDDLLSDSESRSRGNVQLEAGEDVGQKNHWQKIRTMVNLPVIS
PFKKRYAWVQLAGHTGSFKAAGTSGLILKRCSEPERYCLARLMADALRGCVPAFHGVVER
DGESYLQLQDLLDGFDGPCVLDCKMGVRTYLEEELTKARERPKLRKDMYKKMLAVDPEAP
TEEEHAQRAVTKPRYMQWREGISSSTTLGFRIEGIKKADGSCSTDFKTTRSREQVLRVFE
EFVQGDEEVLRRYLNRLQQIRDTLEVSEFFRRHEVIGSSLLFVHDHCHRAGVWLIDFGKT
TPLPDGQILDHRRPWEEGNREDGYLLGLDNLIGILASLAER
Enzyme 86 Number of Residues 461
Enzyme 86 Molecular Weight 51008.3
Enzyme 86 Theoretical pI 7.72
Enzyme 86 GO Classification
Function
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • inositol trisphosphate 3-kinase activity
  • inositol trisphosphate kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
—
Component
—
Enzyme 86 General Function Involved in inositol trisphosphate 3-kinase activity
Enzyme 86 Specific Function ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
Enzyme 86 Pathways
Enzyme 86 Reactions
  • ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate [RN:R03433]
Enzyme 86 Pfam Domain Function
Enzyme 86 Signals
  • None
Enzyme 86 Transmembrane Regions
  • None
Enzyme 86 Essentiality Not Available
Enzyme 86 GenBank ID Protein 32105 Link Image
Enzyme 86 UniProtKB/Swiss-Prot ID P23677 Link Image
Enzyme 86 UniProtKB/Swiss-Prot Entry Name IP3KA_HUMAN Link Image
Enzyme 86 PDB ID 1W2F Link Image
Enzyme 86 PDB File Show
Enzyme 86 3D Structure
Enzyme 86 Cellular Location Not Available
Enzyme 86 Gene Sequence >1386 bp 
ATGACCCTGCCCGGGGGCCCAACGGGCATGGCGCGGCCGGGGGGCGCGAGGCCCTGCAGC
CCGGGGCTGGAGCGGGCCCCGCGCCGGAGTGTCGGGGAGCTGCGCCTGCTCTTCGAGGCG
CGCTGTGCGGCGGTCGCTGCGGCCGCCGCCGCGGGGGAGCCCCGGGCCCGCGGGGCCAAG
CGGCGTGGGGGACAGGTCCCCAACGGGCTTCCGCGGGCTCCCCCGGCCCCGGTGATCCCT
CAGCTGACCGTGACAGCCGAGGAGCCCGACGTGCCCCCGACCAGCCCTGGGCCGCCGGAG
CGGGAGAGGGACTGCCTCCCGGCAGCGGGCTCTTCGCACCTGCAGCAGCCGCGCCGCCTT
TCCACCTCGTCGGTCTCCTCCACTGGCTCCTCGTCGCTGCTCGAGGACTCGGAGGACGAC
CTGCTGAGCGACAGTGAGAGCCGGAGCCGCGGCAACGTGCAGCTGGAAGCGGGCGAGGAC
GTGGGTCAGAAAAACCACTGGCAGAAGATCCGGACCATGGTCAATCTGCCGGTCATAAGC
CCTTTCAAGAAGCGCTACGCCTGGGTGCAGCTGGCAGGGCACACTGGGAGTTTTAAGGCG
GCGGGCACCAGCGGGCTGATCCTGAAGCGCTGCTCGGAGCCGGAGCGCTACTGCCTGGCG
CGGCTGATGGCTGACGCGCTGCGCGGCTGCGTGCCTGCCTTCCACGGCGTGGTGGAGCGC
GACGGCGAAAGCTACCTGCAGCTGCAGGACCTGCTCGATGGCTTCGACGGACCTTGTGTG
CTCGACTGCAAAATGGGCGTCAGGACTTACCTAGAGGAGGAGCTGACCAAGGCCCGTGAG
CGGCCCAAGCTGCGGAAGGACATGTACAAGAAAATGCTGGCGGTGGATCCTGAAGCTCCC
ACGGAGGAGGAGCACGCGCAGCGCGCCGTCACCAAGCCGCGCTACATGCAGTGGCGGGAA
GGCATCAGCTCCAGCACCACCCTCGGCTTCCGCATCGAGGGCATCAAGAAAGCGGACGGC
TCCTGCAGCACCGACTTCAAGACTACGCGAAGCCGAGAGCAGGTGCTTCGCGTCTTTGAA
GAGTTTGTGCAAGGAGATGAGGAAGTGCTGAGGCGGTATCTGAACCGCCTGCAGCAGATC
CGGGACACCCTGGAGGTATCCGAGTTCTTCAGGAGGCACGAGGTGATCGGCAGCTCGCTC
CTCTTTGTGCACGATCACTGCCATCGCGCCGGCGTGTGGCTCATCGACTTCGGCAAGACC
ACGCCCCTCCCCGATGGCCAGATCCTGGACCACCGGCGGCCCTGGGAGGAGGGCAACCGC
GAGGACGGCTATTTGCTGGGGCTGGACAATCTCATTGGCATCCTGGCCAGCCTGGCTGAG
AGATGA
Enzyme 86 GenBank Gene ID X54938 Link Image
Enzyme 86 GeneCard ID ITPKA Link Image
Enzyme 86 GenAtlas ID ITPKA Link Image
Enzyme 86 HGNC ID HGNC:6178 Link Image
Enzyme 86 Chromosome Location 1
Enzyme 86 Locus 15q15.1
Enzyme 86 SNPs SNPJam Report Link Image
Enzyme 86 General References
  1. Takazawa K, Perret J, Dumont JE, Erneux C: Molecular cloning and expression of a human brain inositol 1,4,5-trisphosphate 3-kinase. Biochem Biophys Res Commun. 1991 Jan 31;174(2):529-35. [PubMed Link Image]
  2. Takazawa K, Perret J, Dumont JE, Erneux C: Human brain inositol 1,4,5-trisphosphate 3-kinase cDNA sequence. Nucleic Acids Res. 1990 Dec 11;18(23):7141. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Gonzalez B, Schell MJ, Letcher AJ, Veprintsev DB, Irvine RF, Williams RL: Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase. Mol Cell. 2004 Sep 10;15(5):689-701. [PubMed Link Image]
Enzyme 86 Metabolite References Not Available
Enzyme 87 [top]
Enzyme 87 ID 6281
Enzyme 87 Name Polypeptide N-acetylgalactosaminyltransferase 11
Enzyme 87 Synonyms
  1. Polypeptide GalNAc transferase 11
  2. GalNAc-T11
  3. pp-GaNTase 11
  4. Protein-UDP acetylgalactosaminyltransferase 11
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11
Enzyme 87 Gene Name GALNT11
Enzyme 87 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 11 
MGSVTVRYFCYGCLFTSATWTVLLFVYFNFSEVTQPLKNVPVKGSGPHGPSPKKFYPRFT
RGPSRVLEPQFKANKIDDVIDSRVEDPEEGHLKFSSELGMIFNERDQELRDLGYQKHAFN
MLISDRLGYHRDVPDTRNAACKEKFYPPDLPAASVVICFYNEAFSALLRTVHSVIDRTPA
HLLHEIILVDDDSDFDDLKGELDEYVQKYLPGKIKVIRNTKREGLIRGRMIGAAHATGEV
LVFLDSHCEVNVMWLQPLLAAIREDRHTVVCPVIDIISADTLAYSSSPVVRGGFNWGLHF
KWDLVPLSELGRAEGATAPIKSPTMAGGLFAMNRQYFHELGQYDSGMDIWGGENLEISFR
IWMCGGKLFIIPCSRVGHIFRKRRPYGSPEGQDTMTHNSLRLAHVWLDEYKEQYFSLRPD
LKTKSYGNISERVELRKKLGCKSFKWYLDNVYPEMQISGSHAKPQQPIFVNRGPKRPKVL
QRGRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSLLCLDMS
ETRSSDPPRLMKCHGSGGSQQWTFGKNNRLYQVSVGQCLRAVDPLGQKGSVAMAICDGSS
SQQWHLEG
Enzyme 87 Number of Residues 608
Enzyme 87 Molecular Weight 68918.4
Enzyme 87 Theoretical pI 8.27
Enzyme 87 GO Classification Not Available
Enzyme 87 General Function Involved in polypeptide N-acetylgalactosaminyltransfera
Enzyme 87 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Displays the same enzyme activity toward Muc1, Muc4.1, and EA2 than GALNT1. Does not appear to be involved in glycosylation of erythropoietin
Enzyme 87 Pathways
Enzyme 87 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 87 Pfam Domain Function
Enzyme 87 Signals
  • None
Enzyme 87 Transmembrane Regions
  • 7-29
Enzyme 87 Essentiality Not Available
Enzyme 87 GenBank ID Protein 5630076 Link Image
Enzyme 87 UniProtKB/Swiss-Prot ID Q8NCW6 Link Image
Enzyme 87 UniProtKB/Swiss-Prot Entry Name GLT11_HUMAN Link Image
Enzyme 87 PDB ID Not Available
Enzyme 87 Cellular Location Not Available
Enzyme 87 Gene Sequence >1827 bp 
ATGGGAAGTGTCACAGTTCGGTATTTCTGTTATGGGTGCCTTTTTACATCTGCGACCTGG
ACAGTTTTGCTTTTTGTTTATTTCAACTTCAGTGAAGTGACTCAGCCACTTAAGAATGTG
CCCGTCAAGGGGTCTGGGCCCCACGGACCATCTCCAAAAAAATTCTATCCCCGTTTCACT
CGAGGCCCAAGTCGAGTGCTCGAGCCACAGTTCAAAGCAAACAAAATTGACGATGTGATA
GACAGTCGTGTTGAAGATCCAGAAGAAGGCCACTTGAAATTCTCTTCTGAATTAGGTATG
ATTTTTAATGAACGCGATCAAGAGTTGAGAGACTTGGGCTATCAGAAACATGCTTTTAAT
ATGCTTATCAGTGACCGCTTGGGCTACCACAGAGATGTGCCAGACACAAGGAATGCAGCA
TGTAAAGAAAAGTTCTACCCACCTGACCTGCCAGCTGCTAGTGTTGTTATCTGTTTCTAT
AATGAAGCGTTTTCTGCCTTGCTTCGGACAGTGCACAGTGTCATAGACCGCACGCCAGCA
CACCTGCTTCATGAGATCATCCTTGTGGATGATGATAGTGACTTTGATGATTTGAAAGGA
GAACTAGATGAATATGTCCAAAAATACCTCCCTGGAAAAATTAAAGTCATAAGAAATACA
AAGCGTGAGGGGTTGATTCGAGGGAGAATGATTGGCGCGGCCCACGCGACAGGAGAAGTC
CTTGTGTTCCTGGACAGCCACTGTGAAGTGAATGTGATGTGGCTGCAGCCCTTGCTGGCC
GCCATCCGTGAGGACCGGCACACCGTGGTGTGCCCAGTGATTGACATCATCAGCGCCGAC
ACGCTGGCCTACAGCTCGTCCCCTGTCGTCCGCGGAGGGTTCAACTGGGGACTGCACTTC
AAATGGGATCTTGTCCCCCTTTCTGAGCTAGGACGAGCGGAGGGAGCCACTGCACCAATA
AAGTCACCAACAATGGCTGGAGGTTTGTTTGCCATGAACAGACAGTATTTCCATGAACTT
GGACAGTATGATAGTGGCATGGATATCTGGGGAGGAGAAAATTTGGAAATATCATTTCGG
ATCTGGATGTGTGGCGGTAAGCTCTTCATCATCCCTTGCTCTAGAGTAGGACACATTTTC
CGAAAAAGGCGACCATATGGATCTCCCGAAGGCCAGGACACCATGACACACAACTCTTTG
CGGCTGGCACATGTCTGGTTGGATGAATACAAGGAGCAGTATTTTTCCTTAAGACCTGAC
CTGAAGACGAAAAGCTATGGCAATATCAGTGAGCGTGTGGAACTGAGAAAGAAGTTGGGC
TGTAAATCATTTAAATGGTATTTGGATAATGTATACCCAGAGATGCAGATATCTGGGTCC
CACGCCAAACCCCAACAACCCATTTTTGTCAATAGAGGGCCAAAACGACCCAAAGTCCTT
CAACGTGGAAGGCTCTATCACCTCCAGACCAACAAATGCCTGGTGGCCCAGGGCCGCCCA
AGTCAGAAGGGAGGTCTCGTGGTGCTTAAGGCCTGTGACTACAGTGACCCAAATCAGATC
TGGATCTATAATGAAGAGCATGAATTGGTTTTAAATAGTCTCCTTTGTCTAGATATGTCA
GAGACTCGCTCATCAGACCCGCCACGGCTCATGAAATGCCACGGGTCAGGAGGATCCCAG
CAGTGGACCTTTGGGAAAAACAATCGGCTATACCAGGTGTCGGTTGGACAGTGCCTGAGA
GCAGTGGATCCCCTGGGTCAGAAGGGCTCTGTCGCCATGGCGATCTGCGATGGCTCCTCT
TCACAGCAGTGGCATTTGGAAGGTTAA
Enzyme 87 GenBank Gene ID AC006017 Link Image
Enzyme 87 GeneCard ID GALNT11 Link Image
Enzyme 87 GenAtlas ID GALNT11 Link Image
Enzyme 87 HGNC ID HGNC:19875 Link Image
Enzyme 87 Chromosome Location 7
Enzyme 87 Locus 7q36.1
Enzyme 87 SNPs SNPJam Report Link Image
Enzyme 87 General References
  1. Schwientek T, Bennett EP, Flores C, Thacker J, Hollmann M, Reis CA, Behrens J, Mandel U, Keck B, Schafer MA, Haselmann K, Zubarev R, Roepstorff P, Burchell JM, Taylor-Papadimitriou J, Hollingsworth MA, Clausen H: Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila. J Biol Chem. 2002 Jun 21;277(25):22623-38. Epub 2002 Mar 29. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 87 Metabolite References Not Available
Enzyme 88 [top]
Enzyme 88 ID 6282
Enzyme 88 Name Polypeptide N-acetylgalactosaminyltransferase 4
Enzyme 88 Synonyms
  1. Polypeptide GalNAc transferase 4
  2. GalNAc-T4
  3. pp-GaNTase 4
  4. Protein-UDP acetylgalactosaminyltransferase 4
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4
Enzyme 88 Gene Name GALNT4
Enzyme 88 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 4 
MAVRWTWAGKSCLLLAFLTVAYIFVELLVSTFHASAGAGRARELGSRRLSGLQKNTEDLS
RPLYKKPPADSRALGEWGKASKLQLNEDELKQQEELIERYAINIYLSDRISLHRHIEDKR
MYECKSQKFNYRTLPTTSVIIAFYNEAWSTLLRTIHSVLETSPAVLLKEIILVDDLSDRV
YLKTQLETYISNLDRVRLIRTNKREGLVRARLIGATFATGDVLTFLDCHCECNSGWLEPL
LERIGRDETAVVCPVIDTIDWNTFEFYMQIGEPMIGGFDWRLTFQWHSVPKQERDRRISR
IDPIRSPTMAGGLFAVSKKYFQYLGTYDTGMEVWGGENLELSFRVWQCGGKLEIHPCSHV
GHVFPKRAPYARPNFLQNTARAAEVWMDEYKEHFYNRNPPARKEAYGDISERKLLRERLR
CKSFDWYLKNVFPNLHVPEDRPGWHGAIRSRGISSECLDYNSPDNNPTGANLSLFGCHGQ
GGNQFFEYTSNKEIRFNSVTELCAEVPEQKNYVGMQNCPKDGFPVPANIIWHFKEDGTIF
HPHSGLCLSAYRTPEGRPDVQMRTCDALDKNQIWSFEK
Enzyme 88 Number of Residues 578
Enzyme 88 Molecular Weight 66607.2
Enzyme 88 Theoretical pI 7.80
Enzyme 88 GO Classification Not Available
Enzyme 88 General Function Involved in polypeptide N-acetylgalactosaminyltransfera
Enzyme 88 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has a highest activity toward Muc7, EA2 and Muc2, with a lowest activity than GALNT2. Glycosylates 'Thr-57' of SELPLG
Enzyme 88 Pathways
Enzyme 88 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 88 Pfam Domain Function
Enzyme 88 Signals
  • None
Enzyme 88 Transmembrane Regions
  • 13-35
Enzyme 88 Essentiality Not Available
Enzyme 88 GenBank ID Protein 22137798 Link Image
Enzyme 88 UniProtKB/Swiss-Prot ID Q8N4A0 Link Image
Enzyme 88 UniProtKB/Swiss-Prot Entry Name GALT4_HUMAN Link Image
Enzyme 88 PDB ID Not Available
Enzyme 88 Cellular Location Not Available
Enzyme 88 Gene Sequence >1737 bp 
ATGGCGGTGAGGTGGACTTGGGCAGGCAAGAGCTGCCTGCTGCTGGCGTTTTTAACAGTG
GCCTATATCTTCGTGGAGCTCTTGGTCTCTACTTTTCATGCCTCCGCAGGAGCCGGCCGT
GCCAGGGAGCTGGGGTCAAGAAGGCTCTCAGGCCTCCAGAAAAATACGGAGGATTTGTCT
CGACCGCTTTATAAGAAGCCCCCTGCAGATTCCCGTGCACTTGGGGAGTGGGGGAAAGCC
AGCAAACTCCAGCTCAACGAGGATGAACTGAAGCAGCAAGAAGAACTCATTGAGAGATAC
GCCATCAATATTTACCTCAGTGACAGGATTTCCCTGCATCGACACATAGAGGATAAAAGA
ATGTATGAGTGTAAGTCCCAGAAGTTCAACTATAGGACACTTCCTACCACCTCTGTTATC
ATTGCTTTCTATAACGAAGCCTGGTCGACTTTGCTCCGTACCATTCACAGTGTTTTAGAA
ACTTCTCCTGCAGTTCTTTTGAAAGAGATCATCTTGGTGGATGACTTGAGTGACAGAGTT
TATTTGAAGACACAACTTGAAACTTACATCAGCAATCTTGATAGAGTACGCTTGATTAGG
ACCAATAAGCGAGAGGGGCTGGTTAGGGCCCGTCTGATTGGGGCCACTTTCGCCACTGGG
GACGTCCTCACTTTCCTGGATTGTCACTGTGAGTGTAATTCCGGTTGGCTGGAACCGCTT
TTGGAAAGGATTGGGAGAGATGAAACAGCAGTTGTGTGTCCTGTTATAGACACAATTGAT
TGGAATACTTTTGAATTCTATATGCAGATAGGGGAGCCCATGATTGGTGGGTTTGACTGG
CGTTTAACATTTCAGTGGCATTCTGTCCCCAAACAGGAAAGGGACAGGCGGATATCAAGA
ATTGACCCCATCAGATCACCTACCATGGCTGGAGGACTGTTTGCTGTCAGCAAGAAATAT
TTTCAGTACCTTGGAACGTATGACACAGGAATGGAAGTGTGGGGAGGTGAAAACCTTGAG
CTGTCTTTTAGGGTGTGGCAGTGTGGTGGCAAATTGGAGATCCACCCGTGTTCCCACGTG
GGCCATGTGTTCCCCAAGCGGGCACCATATGCTCGCCCCAATTTCCTACAGAATACTGCT
CGGGCAGCAGAAGTTTGGATGGATGAATACAAAGAGCACTTCTACAATAGAAACCCTCCA
GCAAGAAAAGAAGCTTATGGTGATATTTCTGAAAGAAAATTACTACGAGAGCGGTTGAGA
TGCAAGAGCTTTGACTGGTATTTGAAAAACGTTTTTCCTAATTTACATGTTCCAGAGGAT
AGACCAGGCTGGCATGGGGCTATTCGCAGTAGAGGGATCTCGTCTGAATGTTTAGATTAT
AATTCTCCTGACAACAACCCCACAGGTGCTAACCTTTCACTGTTTGGATGCCATGGTCAA
GGAGGCAATCAATTCTTTGAATATACTTCAAACAAAGAAATAAGGTTTAATTCTGTGACA
GAGTTATGTGCAGAGGTACCTGAGCAAAAAAATTATGTGGGAATGCAAAATTGTCCCAAA
GATGGGTTCCCTGTACCAGCAAACATTATTTGGCATTTTAAAGAAGATGGAACTATTTTT
CACCCACACTCAGGACTGTGTCTTAGTGCTTATCGGACACCGGAGGGCCGACCTGATGTA
CAAATGAGAACTTGTGATGCTCTAGATAAAAATCAAATTTGGAGTTTTGAGAAATAG
Enzyme 88 GenBank Gene ID BC036390 Link Image
Enzyme 88 GeneCard ID GALNT4 Link Image
Enzyme 88 GenAtlas ID GALNT4 Link Image
Enzyme 88 HGNC ID HGNC:4126 Link Image
Enzyme 88 Chromosome Location 1
Enzyme 88 Locus 12q21.33
Enzyme 88 SNPs SNPJam Report Link Image
Enzyme 88 General References
  1. Bennett EP, Hassan H, Mandel U, Mirgorodskaya E, Roepstorff P, Burchell J, Taylor-Papadimitriou J, Hollingsworth MA, Merkx G, van Kessel AG, Eiberg H, Steffensen R, Clausen H: Cloning of a human UDP-N-acetyl-alpha-D-Galactosamine:polypeptide N-acetylgalactosaminyltransferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat. J Biol Chem. 1998 Nov 13;273(46):30472-81. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Hassan H, Reis CA, Bennett EP, Mirgorodskaya E, Roepstorff P, Hollingsworth MA, Burchell J, Taylor-Papadimitriou J, Clausen H: The lectin domain of UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-T4 directs its glycopeptide specificities. J Biol Chem. 2000 Dec 8;275(49):38197-205. [PubMed Link Image]
Enzyme 88 Metabolite References Not Available
Enzyme 89 [top]
Enzyme 89 ID 6283
Enzyme 89 Name Polypeptide N-acetylgalactosaminyltransferase 3
Enzyme 89 Synonyms
  1. Polypeptide GalNAc transferase 3
  2. GalNAc-T3
  3. pp-GaNTase 3
  4. Protein-UDP acetylgalactosaminyltransferase 3
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
Enzyme 89 Gene Name GALNT3
Enzyme 89 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 3 
MAHLKRLVKLHIKRHYHKKFWKLGAVIFFFIIVLVLMQREVSVQYSKEESRMERNMKNKN
KMLDLMLEAVNNIKDAMPKMQIGAPVRQNIDAGERPCLQGYYTAAELKPVLDRPPQDSNA
PGASGKAFKTTNLSVEEQKEKERGEAKHCFNAFASDRISLHRDLGPDTRPPECIEQKFKR
CPPLPTTSVIIVFHNEAWSTLLRTVHSVLYSSPAILLKEIILVDDASVDEYLHDKLDEYV
KQFSIVKIVRQRERKGLITARLLGATVATAETLTFLDAHCECFYGWLEPLLARIAENYTA
VVSPDIASIDLNTFEFNKPSPYGSNHNRGNFDWSLSFGWESLPDHEKQRRKDETYPIKTP
TFAGGLFSISKEYFEYIGSYDEEMEIWGGENIEMSFRVWQCGGQLEIMPCSVVGHVFRSK
SPHSFPKGTQVIARNQVRLAEVWMDEYKEIFYRRNTDAAKIVKQKAFGDLSKRFEIKHRL
QCKNFTWYLNNIYPEVYVPDLNPVISGYIKSVGQPLCLDVGENNQGGKPLIMYTCHGLGG
NQYFEYSAQHEIRHNIQKELCLHAAQGLVQLKACTYKGHKTVVTGEQIWEIQKDQLLYNP
FLKMCLSANGEHPSLVSCNPSDPLQKWILSQND
Enzyme 89 Number of Residues 633
Enzyme 89 Molecular Weight 72609.8
Enzyme 89 Theoretical pI 8.06
Enzyme 89 GO Classification Not Available
Enzyme 89 General Function Cell wall/membrane/envelope biogenesis
Enzyme 89 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. Probably glycosylates fibronectin in vivo. Glycosylates FGF23. Plays a central role in phosphate homeostasis
Enzyme 89 Pathways
Enzyme 89 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 89 Pfam Domain Function
Enzyme 89 Signals
  • None
Enzyme 89 Transmembrane Regions
  • 20-37
Enzyme 89 Essentiality Not Available
Enzyme 89 GenBank ID Protein 62822129 Link Image
Enzyme 89 UniProtKB/Swiss-Prot ID Q14435 Link Image
Enzyme 89 UniProtKB/Swiss-Prot Entry Name GALT3_HUMAN Link Image
Enzyme 89 PDB ID Not Available
Enzyme 89 Cellular Location Not Available
Enzyme 89 Gene Sequence >1902 bp 
ATGGCTCACCTAAAGCGACTAGTAAAATTACACATTAAAAGACATTACCATAAAAAGTTC
TGGAAGCTTGGTGCAGTAATTTTTTTCTTTATAATAGTTTTGGTTTTAATGCAAAGAGAA
GTAAGTGTTCAATATTCCAAAGAGGAATCAAGGATGGAAAGGAACATGAAAAACAAAAAC
AAGATGTTGGATTTAATGCTAGAAGCTGTAAACAATATTAAGGATGCCATGCCAAAAATG
CAAATAGGAGCACCTGTCAGGCAAAACATTGATGCTGGTGAGAGACCTTGTTTGCAAGGA
TATTATACAGCAGCAGAATTGAAGCCTGTCCTTGACCGTCCACCTCAGGATTCAAATGCA
CCTGGTGCTTCTGGTAAAGCATTCAAGACAACCAATTTAAGTGTTGAAGAGCAAAAGGAA
AAGGAACGTGGGGAAGCTAAACACTGCTTTAATGCTTTCGCAAGTGACAGGATTTCTTTG
CACCGAGATCTTGGACCAGACACTCGACCTCCTGAATGTATTGAACAAAAATTTAAGCGC
TGCCCTCCCCTGCCCACCACCAGTGTCATAATAGTTTTTCATAATGAAGCGTGGTCCACG
TTGCTTAGAACTGTCCACAGTGTGCTCTATTCTTCACCTGCAATACTGCTGAAGGAAATC
ATTTTGGTGGATGATGCTAGTGTAGATGAGTACTTACATGATAAACTAGATGAATATGTA
AAACAATTTTCTATAGTAAAAATAGTCAGACAAAGAGAAAGAAAAGGTCTGATCACTGCT
CGGTTGCTAGGAGCAACAGTCGCAACAGCTGAAACGCTCACATTTTTAGATGCTCACTGT
GAGTGTTTCTATGGTTGGCTAGAACCTCTGTTGGCCAGAATAGCTGAGAACTACACGGCT
GTCGTAAGTCCAGATATTGCATCCATAGATCTGAACACGTTTGAATTCAACAAACCTTCT
CCTTATGGAAGTAACCATAACCGTGGAAATTTTGACTGGAGTCTTTCATTTGGCTGGGAG
TCGCTTCCTGATCATGAGAAGCAAAGAAGGAAAGATGAAACCTACCCAATTAAAACACCC
ACTTTTGCAGGAGGACTTTTTTCCATATCAAAAGAATATTTTGAGTATATTGGAAGCTAT
GATGAAGAAATGGAAATCTGGGGAGGTGAAAATATAGAAATGTCTTTCAGAGTATGGCAA
TGTGGTGGGCAGTTGGAGATTATGCCTTGCTCTGTTGTTGGACATGTTTTTCGCAGCAAA
AGCCCTCATAGCTTTCCAAAAGGCACTCAGGTGATTGCTAGAAACCAAGTTCGCCTTGCA
GAAGTCTGGATGGATGAATACAAGGAAATATTTTATAGGAGAAATACAGATGCAGCAAAA
ATTGTTAAACAAAAAGCATTTGGTGATCTTTCAAAAAGATTTGAAATAAAACACCGCCTT
CAGTGTAAAAATTTTACATGGTATCTGAACAACATTTATCCAGAGGTGTATGTGCCAGAC
CTTAATCCTGTTATATCTGGATACATTAAAAGCGTTGGTCAGCCTCTATGTCTGGATGTT
GGAGAAAACAATCAAGGAGGCAAACCATTAATTATGTATACATGTCATGGACTTGGGGGA
AACCAGTACTTTGAATACTCTGCTCAACATGAAATTCGGCACAACATCCAGAAGGAATTA
TGTCTTCATGCTGCTCAAGGTCTCGTTCAGCTGAAGGCATGTACCTACAAAGGTCACAAG
ACAGTTGTCACTGGAGAGCAGATATGGGAGATCCAGAAGGATCAACTTCTATACAATCCA
TTCTTAAAAATGTGCCTTTCAGCAAATGGAGAGCATCCAAGTTTAGTGTCATGCAACCCA
TCAGATCCACTCCAAAAATGGATACTTAGCCAAAATGATTAA
Enzyme 89 GenBank Gene ID AC009495 Link Image
Enzyme 89 GeneCard ID GALNT3 Link Image
Enzyme 89 GenAtlas ID GALNT3 Link Image
Enzyme 89 HGNC ID HGNC:4125 Link Image
Enzyme 89 Chromosome Location 2
Enzyme 89 Locus 2q24-q31
Enzyme 89 SNPs SNPJam Report Link Image
Enzyme 89 General References
  1. Bennett EP, Hassan H, Clausen H: cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3. J Biol Chem. 1996 Jul 19;271(29):17006-12. [PubMed Link Image]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Wandall HH, Hassan H, Mirgorodskaya E, Kristensen AK, Roepstorff P, Bennett EP, Nielsen PA, Hollingsworth MA, Burchell J, Taylor-Papadimitriou J, Clausen H: Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3. J Biol Chem. 1997 Sep 19;272(38):23503-14. [PubMed Link Image]
  5. Rottger S, White J, Wandall HH, Olivo JC, Stark A, Bennett EP, Whitehouse C, Berger EG, Clausen H, Nilsson T: Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus. J Cell Sci. 1998 Jan;111 ( Pt 1):45-60. [PubMed Link Image]
  6. Onitsuka K, Shibao K, Nakayama Y, Minagawa N, Hirata K, Izumi H, Matsuo K, Nagata N, Kitazato K, Kohno K, Itoh H: Prognostic significance of UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-3 (GalNAc-T3) expression in patients with gastric carcinoma. Cancer Sci. 2003 Jan;94(1):32-6. [PubMed Link Image]
  7. Topaz O, Shurman DL, Bergman R, Indelman M, Ratajczak P, Mizrachi M, Khamaysi Z, Behar D, Petronius D, Friedman V, Zelikovic I, Raimer S, Metzker A, Richard G, Sprecher E: Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis. Nat Genet. 2004 Jun;36(6):579-81. Epub 2004 May 9. [PubMed Link Image]
  8. Frishberg Y, Topaz O, Bergman R, Behar D, Fisher D, Gordon D, Richard G, Sprecher E: Identification of a recurrent mutation in GALNT3 demonstrates that hyperostosis-hyperphosphatemia syndrome and familial tumoral calcinosis are allelic disorders. J Mol Med. 2005 Jan;83(1):33-8. Epub 2004 Dec 15. [PubMed Link Image]
  9. Kato K, Jeanneau C, Tarp MA, Benet-Pages A, Lorenz-Depiereux B, Bennett EP, Mandel U, Strom TM, Clausen H: Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation. J Biol Chem. 2006 Jul 7;281(27):18370-7. Epub 2006 Apr 25. [PubMed Link Image]
Enzyme 89 Metabolite References Not Available
Enzyme 90 [top]
Enzyme 90 ID 6284
Enzyme 90 Name Probable polypeptide N-acetylgalactosaminyltransferase 8
Enzyme 90 Synonyms
  1. Polypeptide GalNAc transferase 8
  2. GalNAc-T8
  3. pp-GaNTase 8
  4. Protein-UDP acetylgalactosaminyltransferase 8
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8
Enzyme 90 Gene Name GALNT8
Enzyme 90 Protein Sequence >Probable polypeptide N-acetylgalactosaminyltransferase 8 
MMFWRKLPKALFIGLTLAIAVNLLLVFSSKGTLQNLFTGGLHRELPLHLNKRYGAVIKRL
SHLEVELQDLKESMKLALRQQENVNSTLKRAKDEVRPLLKAMETKVNETKKHKTQMKLFP
HSQLFRQWGEDLSEAQQKAAQDLFRKFGYNAYLSNQLPLNRTIPDTRDYRCLRKTYPSQL
PSLSVILIFVNEALSIIQRAITSIINRTPSRLLKEIILVDDFSSNGELKVHLDEKIKLYN
QKYPGLLKIIRHPERKGLAQARNTGWEAATADVVAILDAHIEVNVGWAEPILARIQEDRT
VIVSPVFDNIRFDTFKLDKYELAVDGFNWELWCRYDALPQAWIDLHDVTAPVKSPSIMGI
LAANRHFLGEIGSLDGGMLIYGGENVELSLRVWQCGGKVEILPCSRIAHLERHHKPYALD
LTAALKRNALRVAEIWMDEHKHMVYLAWNIPLQNSGIDFGDVSSRMALREKLKCKTFDWY
LKNVYPLLKPLHTIVGYGRMKNLLDENVCLDQGPVPGNTPIMYYCHEFSSQNVYYHLTGE
LYVGQLIAEASASDRCLTDPGKAEKPTLEPCSKAAKNRLHIYWDFKPGGAVINRDTKRCL
EMKKDLLGSHVLVLQTCSTQVWEIQHTVRDWGQTNSQ
Enzyme 90 Number of Residues 637
Enzyme 90 Molecular Weight 72850.8
Enzyme 90 Theoretical pI 9.16
Enzyme 90 GO Classification Not Available
Enzyme 90 General Function Cell wall/membrane/envelope biogenesis
Enzyme 90 Specific Function Probably catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor
Enzyme 90 Pathways
Enzyme 90 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 90 Pfam Domain Function
Enzyme 90 Signals
  • None
Enzyme 90 Transmembrane Regions
  • 7-29
Enzyme 90 Essentiality Not Available
Enzyme 90 GenBank ID Protein 7657926 Link Image
Enzyme 90 UniProtKB/Swiss-Prot ID Q9NY28 Link Image
Enzyme 90 UniProtKB/Swiss-Prot Entry Name GALT8_HUMAN Link Image
Enzyme 90 PDB ID Not Available
Enzyme 90 Cellular Location Not Available
Enzyme 90 Gene Sequence >1914 bp 
ATGATGTTTTGGAGGAAACTCCCCAAAGCCCTCTTCATTGGGCTGACTCTGGCCATTGCT
GTCAATCTCCTTCTGGTATTTTCTAGCAAGGGGACTTTACAAAACCTGTTTACGGGTGGT
CTCCACAGGGAGCTTCCTTTACATCTGAATAAACGCTACGGGGCAGTGATAAAGAGACTC
TCCCACTTGGAGGTGGAATTGCAGGATCTGAAAGAAAGTATGAAATTAGCTCTGAGGCAA
CAAGAAAATGTGAACAGCACACTGAAGAGGGCGAAAGATGAAGTACGCCCTCTTCTAAAG
GCAATGGAAACCAAGGTGAATGAGACAAAGAAGCACAAAACCCAAATGAAACTCTTCCCA
CACTCACAGCTTTTCAGGCAATGGGGCGAGGATCTTTCTGAGGCCCAGCAGAAGGCGGCC
CAGGACCTCTTCCGGAAGTTTGGTTACAACGCGTACCTCAGCAACCAGCTGCCTCTCAAT
CGCACCATCCCCGACACGCGAGACTACAGATGTCTTCGGAAGACATATCCTTCCCAACTC
CCATCCCTCAGTGTCATTCTCATATTCGTGAATGAAGCTCTGTCCATTATACAACGGGCC
ATCACCAGTATCATCAACCGGACGCCCTCTCGATTGTTGAAGGAAATCATCTTGGTGGAT
GATTTCAGCTCAAATGGAGAACTAAAGGTACACTTGGATGAGAAGATTAAGCTTTACAAC
CAGAAGTATCCAGGACTACTGAAAATAATACGGCATCCTGAAAGGAAAGGTCTTGCTCAA
GCCCGCAACACTGGCTGGGAAGCTGCCACAGCAGACGTGGTCGCCATCTTGGATGCTCAC
ATTGAAGTCAATGTTGGGTGGGCAGAGCCAATCTTGGCTCGGATTCAGGAGGACCGCACT
GTGATTGTGTCTCCTGTGTTTGACAACATTCGTTTTGACACCTTCAAACTGGATAAGTAT
GAACTGGCAGTTGATGGGTTTAACTGGGAACTCTGGTGCCGCTACGATGCACTGCCACAA
GCCTGGATTGATCTGCATGATGTCACTGCCCCAGTGAAGAGTCCTTCAATCATGGGCATC
CTGGCTGCTAACAGGCACTTCCTGGGAGAGATCGGGTCTCTGGATGGTGGAATGCTCATC
TATGGAGGAGAGAACGTGGAGCTTAGCCTGAGGGTGTGGCAGTGTGGAGGGAAGGTCGAG
ATTTTGCCCTGTTCCCGGATTGCCCACCTAGAGAGACACCACAAGCCCTACGCCTTGGAT
CTCACCGCTGCCTTGAAGCGCAATGCTCTGCGAGTGGCCGAAATCTGGATGGATGAGCAC
AAACACATGGTCTACTTGGCCTGGAACATACCTCTCCAGAACTCTGGAATAGATTTTGGA
GACGTTTCTTCCAGAATGGCACTCCGGGAAAAACTGAAATGTAAAACTTTTGACTGGTAC
CTGAAAAATGTTTATCCACTCTTGAAGCCACTCCACACCATCGTGGGCTATGGAAGAATG
AAAAACCTATTGGATGAAAATGTCTGCTTGGATCAGGGACCCGTTCCAGGCAACACCCCC
ATCATGTATTACTGCCATGAATTCAGCTCACAGAATGTCTACTATCACCTAACTGGGGAG
CTCTATGTGGGACAACTGATTGCAGAGGCCAGTGCTAGTGATCGCTGCCTGACAGACCCT
GGCAAGGCGGAGAAGCCCACCTTAGAACCATGCTCCAAGGCAGCTAAGAATAGACTGCAT
ATATATTGGGATTTTAAACCGGGAGGAGCTGTCATAAACAGAGATACCAAGCGGTGTCTG
GAGATGAAGAAGGATCTTTTGGGTAGCCACGTGCTTGTGCTCCAGACCTGTAGCACGCAA
GTGTGGGAAATCCAGCACACTGTCAGAGACTGGGGTCAGACCAACAGCCAGTGA
Enzyme 90 GenBank Gene ID AJ271385 Link Image
Enzyme 90 GeneCard ID GALNT8 Link Image
Enzyme 90 GenAtlas ID GALNT8 Link Image
Enzyme 90 HGNC ID HGNC:4130 Link Image
Enzyme 90 Chromosome Location 1
Enzyme 90 Locus 12p13.3
Enzyme 90 SNPs SNPJam Report Link Image
Enzyme 90 General References
  1. White KE, Lorenz B, Evans WE, Meitinger T, Strom TM, Econs MJ: Molecular cloning of a novel human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T8, and analysis as a candidate autosomal dominant hypophosphatemic rickets (ADHR) gene. Gene. 2000 Apr 4;246(1-2):347-56. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 90 Metabolite References Not Available
Enzyme 91 [top]
Enzyme 91 ID 6285
Enzyme 91 Name Polypeptide N-acetylgalactosaminyltransferase-like protein 2
Enzyme 91 Synonyms
  1. Polypeptide GalNAc transferase-like protein 2
  2. GalNAc-T-like protein 2
  3. pp-GaNTase-like protein 2
  4. Protein-UDP acetylgalactosaminyltransferase-like protein 2
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2
Enzyme 91 Gene Name GALNTL2
Enzyme 91 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase-like protein 2 
MLLRKRYRHRPCRLQFLLLLLMLGCVLMMVAMLHPPHHTLHQTVTAQASKHSPEARYRLD
FGESQDWVLEAEDEGEEYSPLEGLPPFISLREDQLLVAVALPQARRNQSQGRRGGSYRLI
KQPRRQDKEAPKRDWGADEDGEVSEEEELTPFSLDPRGLQEALSARIPLQRALPEVRHPL
CLQQHPQDSLPTASVILCFHDEAWSTLLRTVHSILDTVPRAFLKEIILVDDLSQQGQLKS
ALSEYVARLEGVKLLRSNKRLGAIRARMLGATRATGDVLVFMDAHCECHPGWLEPLLSRI
AGDRSRVVSPVIDVIDWKTFQYYPSKDLQRGVLDWKLDFHWEPLPEHVRKALQSPISPIR
SPVVPGEVVAMDRHYFQNTGAYDSLMSLRGGENLELSFKAWLCGGSVEILPCSRVGHIYQ
NQDSHSPLDQEATLRNRVRIAETWLGSFKETFYKHSPEAFSLSKAEKPDCMERLQLQRRL
GCRTFHWFLANVYPELYPSEPRPSFSGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSR
QQQYLQHTSRKEIHFGSPQHLCFAVRQEQVILQNCTEEGLAIHQQHWDFQENGMIVHILS
GKCMEAVVQENNKDLYLRPCDGKARQQWRFDQINAVDER
Enzyme 91 Number of Residues 639
Enzyme 91 Molecular Weight 73062.8
Enzyme 91 Theoretical pI 6.90
Enzyme 91 GO Classification Not Available
Enzyme 91 General Function Involved in polypeptide N-acetylgalactosaminyltransfera
Enzyme 91 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, it is able to transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. Prefers Muc1a as substrate
Enzyme 91 Pathways
Enzyme 91 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 91 Pfam Domain Function
Enzyme 91 Signals
  • None
Enzyme 91 Transmembrane Regions
  • 12-34
Enzyme 91 Essentiality Not Available
Enzyme 91 GenBank ID Protein 190014583 Link Image
Enzyme 91 UniProtKB/Swiss-Prot ID Q8N3T1 Link Image
Enzyme 91 UniProtKB/Swiss-Prot Entry Name GLTL2_HUMAN Link Image
Enzyme 91 PDB ID Not Available
Enzyme 91 Cellular Location Not Available
Enzyme 91 Gene Sequence >1920 bp 
ATGCTCCTAAGGAAGCGATACAGGCACAGACCATGCAGACTCCAGTTCCTCCTGCTGCTC
CTGATGCTGGGATGCGTCCTGATGATGGTGGCGATGTTGCACCCTCCCCACCACACCCTG
CACCAGACTGTCACAGCCCAAGCCAGCAAGCACAGCCCTGAAGCCAGGTACCGCCTGGAC
TTTGGGGAATCCCAGGATTGGGTACTGGAAGCTGAGGATGAGGGTGAAGAGTACAGCCCT
CTGGAGGGCCTGCCACCCTTTATCTCACTGCGGGAGGATCAGCTGCTGGTGGCCGTGGCC
TTACCCCAGGCCAGAAGGAACCAGAGCCAGGGCAGGAGAGGTGGGAGCTACCGCCTCATC
AAGCAGCCAAGGAGGCAGGATAAGGAAGCCCCAAAGAGGGACTGGGGGGCTGATGAGGAC
GGGGAGGTGTCTGAAGAAGAGGAGTTGACCCCGTTCAGCCTGGACCCACGTGGCCTCCAG
GAGGCACTCAGTGCCCGCATCCCCCTCCAGAGGGCTCTGCCCGAGGTGCGGCACCCACTG
TGTCTGCAGCAGCACCCTCAGGACAGCCTGCCCACAGCCAGCGTCATCCTCTGTTTCCAT
GATGAGGCCTGGTCCACTCTCCTGCGGACTGTACACAGCATCCTCGACACAGTGCCCAGG
GCCTTCCTGAAGGAGATCATCCTCGTGGACGACCTCAGCCAGCAAGGACAACTCAAGTCT
GCTCTCAGCGAATATGTGGCCAGGCTGGAGGGGGTGAAGTTACTCAGGAGCAACAAGAGG
CTGGGTGCCATCAGGGCCCGGATGCTGGGGGCCACCAGAGCCACCGGGGATGTGCTCGTC
TTCATGGATGCCCACTGCGAGTGCCACCCAGGCTGGCTGGAGCCCCTCCTCAGCAGAATA
GCTGGTGACAGGAGCCGAGTGGTATCTCCGGTGATAGATGTGATTGACTGGAAGACTTTC
CAGTATTACCCCTCAAAGGACCTGCAGCGTGGGGTGTTGGACTGGAAGCTGGATTTCCAC
TGGGAACCTTTGCCAGAGCATGTGAGGAAGGCCCTCCAGTCCCCCATAAGCCCCATCAGG
AGCCCTGTGGTGCCCGGAGAGGTGGTGGCCATGGACAGACATTACTTCCAAAACACTGGA
GCGTATGACTCTCTTATGTCGCTGCGAGGTGGTGAAAACCTCGAACTGTCTTTCAAGGCC
TGGCTCTGTGGTGGCTCTGTTGAAATCCTTCCCTGCTCTCGGGTAGGACACATCTACCAA
AATCAGGATTCCCATTCCCCCCTCGACCAGGAGGCCACCCTGAGGAACAGGGTTCGCATT
GCTGAGACCTGGCTGGGGTCATTCAAAGAAACCTTCTACAAGCATAGCCCAGAGGCCTTC
TCCTTGAGCAAGGCTGAGAAGCCAGACTGCATGGAACGCTTGCAGCTGCAAAGGAGACTG
GGTTGTCGGACATTCCACTGGTTTCTGGCTAATGTCTACCCTGAGCTGTACCCATCTGAA
CCCAGGCCCAGTTTCTCTGGAAAGCTCCACAACACTGGACTTGGGCTCTGTGCAGACTGC
CAGGCAGAAGGGGACATCCTGGGCTGTCCCATGGTGTTGGCTCCTTGCAGTGACAGCCGG
CAGCAACAGTACCTGCAGCACACCAGCAGGAAGGAGATTCACTTTGGCAGCCCACAGCAC
CTGTGCTTTGCTGTCAGGCAGGAGCAGGTGATTCTTCAGAACTGCACGGAGGAAGGCCTG
GCCATCCACCAGCAGCACTGGGACTTCCAGGAGAATGGGATGATTGTCCACATTCTTTCT
GGGAAATGCATGGAAGCTGTGGTGCAAGAAAACAATAAAGATTTGTACCTGCGTCCGTGT
GATGGAAAAGCCCGCCAGCAGTGGCGTTTTGACCAGATCAATGCTGTGGATGAACGATGA
Enzyme 91 GenBank Gene ID NM_054110.4 Link Image
Enzyme 91 GeneCard ID GALNTL2 Link Image
Enzyme 91 GenAtlas ID GALNTL2 Link Image
Enzyme 91 HGNC ID HGNC:21531 Link Image
Enzyme 91 Chromosome Location 3
Enzyme 91 Locus 3p25.1
Enzyme 91 SNPs SNPJam Report Link Image
Enzyme 91 General References
  1. Cheng L, Tachibana K, Iwasaki H, Kameyama A, Zhang Y, Kubota T, Hiruma T, Tachibana K, Kudo T, Guo JM, Narimatsu H: Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15. FEBS Lett. 2004 May 21;566(1-3):17-24. [PubMed Link Image]
  2. Kumar S, Connor JR, Dodds RA, Halsey W, Van Horn M, Mao J, Sathe G, Mui P, Agarwal P, Badger AM, Lee JC, Gowen M, Lark MW: Identification and initial characterization of 5000 expressed sequenced tags (ESTs) each from adult human normal and osteoarthritic cartilage cDNA libraries. Osteoarthritis Cartilage. 2001 Oct;9(7):641-53. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  6. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 91 Metabolite References Not Available
Enzyme 92 [top]
Enzyme 92 ID 6286
Enzyme 92 Name Putative polypeptide N-acetylgalactosaminyltransferase-like protein 1
Enzyme 92 Synonyms
  1. Polypeptide GalNAc transferase-like protein 1
  2. GalNAc-T-like protein 1
  3. pp-GaNTase-like protein 1
  4. Protein-UDP acetylgalactosaminyltransferase-like protein 1
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 1
Enzyme 92 Gene Name GALNTL1
Enzyme 92 Protein Sequence >Putative polypeptide N-acetylgalactosaminyltransferase-like protein 1 
MRKIRANAIAILTVAWILGTFYYLWQDNRAHAASSGGRGAQRAGRRSEQLREDRTIPLIV
TGTPSKGFDEKAYLSAKQLKAGEDPYRQHAFNQLESDKLSPDRPIRDTRHYSCPSVSYSS
DLPATSVIITFHNEARSTLLRTVKSVLNRTPANLIQEIILVDDFSSDPEDCLLLTRIPKV
KCLRNDRREGLIRSRVRGADVAAATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVVSPII
DVISLDNFAYLAASADLRGGFDWSLHFKWEQIPLEQKMTRTDPTRPIRTPVIAGGIFVID
KSWFNHLGKYDAQMDIWGGENFELSFRVWMCGGSLEIVPCSRVGHVFRKRHPYNFPEGNA
LTYIRNTKRTAEVWMDEYKQYYYEARPSAIGKAFGSVATRIEQRKKMNCKSFRWYLENVY
PELTVPVKEALPGIIKQGVNCLESQGQNTAGDFLLGMGICRGSAKNPQPAQAWLFSDHLI
QQQGKCLAATSTLMSSPGSPVILQMCNPREGKQKWRRKGSFIQHSVSGLCLETKPAQLVT
SKCQADAQAQQWQLLPHT
Enzyme 92 Number of Residues 558
Enzyme 92 Molecular Weight 63073.6
Enzyme 92 Theoretical pI 9.47
Enzyme 92 GO Classification Not Available
Enzyme 92 General Function Involved in polypeptide N-acetylgalactosaminyltransfera
Enzyme 92 Specific Function May catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor
Enzyme 92 Pathways
Enzyme 92 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 92 Pfam Domain Function
Enzyme 92 Signals
  • None
Enzyme 92 Transmembrane Regions
  • 7-26
Enzyme 92 Essentiality Not Available
Enzyme 92 GenBank ID Protein 270265827 Link Image
Enzyme 92 UniProtKB/Swiss-Prot ID Q8N428 Link Image
Enzyme 92 UniProtKB/Swiss-Prot Entry Name GLTL1_HUMAN Link Image
Enzyme 92 PDB ID Not Available
Enzyme 92 Cellular Location Not Available
Enzyme 92 Gene Sequence >1677 bp 
ATGAGGAAGATCCGCGCCAATGCCATCGCCATCCTGACCGTAGCCTGGATCCTGGGCACT
TTCTACTACTTATGGCAGGACAACCGAGCCCACGCAGCATCCTCCGGCGGCCGGGGCGCG
CAGAGGGCAGGCAGGAGGTCGGAGCAGCTCCGCGAGGACCGCACCATCCCGCTCATTGTG
ACAGGAACTCCCTCGAAAGGCTTTGATGAGAAGGCCTACCTGTCGGCCAAGCAGCTGAAG
GCTGGAGAGGACCCCTACAGACAGCACGCCTTCAACCAGCTGGAGAGTGACAAGCTGAGC
CCAGACCGGCCCATCCGGGACACCCGCCATTACAGCTGCCCATCTGTGTCCTACTCCTCG
GACCTGCCAGCCACCAGCGTCATCATCACCTTCCACAATGAGGCCCGTTCCACCCTGCTG
CGCACAGTGAAGAGTGTCCTGAACCGAACTCCTGCCAACTTGATCCAGGAGATCATTTTA
GTGGATGACTTCAGCTCAGATCCGGAAGACTGTCTACTCCTGACCAGGATCCCCAAGGTC
AAGTGCCTGCGCAATGATCGGCGGGAAGGGCTGATCCGGTCCCGAGTGCGTGGGGCGGAC
GTGGCTGCAGCTACCGTTCTCACCTTTCTGGATAGCCACTGCGAAGTGAACACCGAGTGG
CTGCCGCCCATGCTGCAGCGGGTGAAGGAGGACCACACCCGCGTGGTGAGTCCCATCATT
GATGTCATCAGTCTGGATAATTTTGCCTACCTTGCAGCATCTGCTGACCTTCGTGGAGGG
TTCGACTGGAGCCTGCATTTCAAGTGGGAGCAGATCCCTCTTGAGCAGAAGATGACCCGG
ACAGACCCCACCAGGCCCATAAGGACGCCTGTCATAGCTGGAGGAATCTTCGTGATCGAC
AAGTCCTGGTTTAACCACTTGGGAAAGTATGATGCCCAGATGGACATCTGGGGGGGAGAG
AATTTTGAGCTCTCCTTCAGGGTGTGGATGTGTGGTGGCAGTCTGGAGATCGTCCCCTGC
AGCCGGGTGGGCCATGTCTTCAGGAAACGGCACCCCTACAACTTCCCTGAGGGTAATGCC
CTCACCTACATCAGGAATACTAAGCGCACTGCAGAAGTGTGGATGGATGAATACAAGCAA
TACTACTATGAGGCCCGGCCCTCGGCCATCGGGAAGGCCTTCGGCAGTGTGGCTACGCGG
ATAGAGCAGAGGAAGAAGATGAACTGCAAGTCCTTCCGCTGGTACCTGGAGAACGTCTAC
CCAGAGCTCACGGTCCCCGTGAAGGAAGCACTCCCCGGCATCATTAAGCAGGGGGTGAAC
TGCTTAGAATCTCAGGGCCAGAACACAGCTGGTGACTTCCTGCTTGGAATGGGGATCTGC
AGAGGGTCTGCCAAGAACCCGCAGCCCGCCCAGGCATGGCTGTTCAGTGACCACCTCATC
CAGCAGCAGGGGAAGTGCCTGGCTGCCACCTCCACCTTAATGTCCTCCCCTGGATCCCCA
GTCATACTGCAGATGTGCAACCCTAGAGAAGGCAAGCAGAAATGGAGGAGAAAAGGATCT
TTCATCCAGCATTCAGTCAGTGGCCTCTGCCTGGAGACAAAGCCTGCCCAGCTGGTGACC
AGCAAGTGTCAGGCTGACGCCCAGGCCCAGCAGTGGCAGCTGTTGCCACACACATGA
Enzyme 92 GenBank Gene ID NM_001168368.1 Link Image
Enzyme 92 GeneCard ID GALNTL1 Link Image
Enzyme 92 GenAtlas ID GALNTL1 Link Image
Enzyme 92 HGNC ID HGNC:23233 Link Image
Enzyme 92 Chromosome Location 1
Enzyme 92 Locus 14q24.1
Enzyme 92 SNPs SNPJam Report Link Image
Enzyme 92 General References
  1. Hirosawa M, Nagase T, Ishikawa K, Kikuno R, Nomura N, Ohara O: Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain. DNA Res. 1999 Oct 29;6(5):329-36. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 92 Metabolite References Not Available
Enzyme 93 [top]
Enzyme 93 ID 6287
Enzyme 93 Name Polypeptide N-acetylgalactosaminyltransferase 10
Enzyme 93 Synonyms
  1. Polypeptide GalNAc transferase 10
  2. GalNAc-T10
  3. pp-GaNTase 10
  4. Protein-UDP acetylgalactosaminyltransferase 10
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10
Enzyme 93 Gene Name GALNT10
Enzyme 93 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 10 
MRRKEKRLLQAVALVLAALVLLPNVGLWALYRERQPDGTPGGSGAAVAPAAGQGSHSRQK
KTFFLGDGQKLKDWHDKEAIRRDAQRVGNGEQGRPYPMTDAERVDQAYRENGFNIYVSDK
ISLNRSLPDIRHPNCNSKRYLETLPNTSIIIPFHNEGWSSLLRTVHSVLNRSPPELVAEI
VLVDDFSDREHLKKPLEDYMALFPSVRILRTKKREGLIRTRMLGASVATGDVITFLDSHC
EANVNWLPPLLDRIARNRKTIVCPMIDVIDHDDFRYETQAGDAMRGAFDWEMYYKRIPIP
PELQKADPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQYEISFKVWMCGGRM
EDIPCSRVGHIYRKYVPYKVPAGVSLARNLKRVAEVWMDEYAEYIYQRRPEYRHLSAGDV
AVQKKLRSSLNCKSFKWFMTKIAWDLPKFYPPVEPPAAAWGEIRNVGTGLCADTKHGALG
SPLRLEGCVRGRGEAAWNNMQVFTFTWREDIRPGDPQHTKKFCFDAISHTSPVTLYDCHS
MKGNQLWKYRKDKTLYHPVSGSCMDCSESDHRIFMNTCNPSSLTQQWLFEHTNSTVLEKF
NRN
Enzyme 93 Number of Residues 603
Enzyme 93 Molecular Weight 68991.2
Enzyme 93 Theoretical pI 8.74
Enzyme 93 GO Classification Not Available
Enzyme 93 General Function Involved in metal ion binding
Enzyme 93 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward Muc5Ac and EA2 peptide substrates
Enzyme 93 Pathways
Enzyme 93 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 93 Pfam Domain Function
Enzyme 93 Signals
  • None
Enzyme 93 Transmembrane Regions
  • 12-31
Enzyme 93 Essentiality Not Available
Enzyme 93 GenBank ID Protein 28268676 Link Image
Enzyme 93 UniProtKB/Swiss-Prot ID Q86SR1 Link Image
Enzyme 93 UniProtKB/Swiss-Prot Entry Name GLT10_HUMAN Link Image
Enzyme 93 PDB ID Not Available
Enzyme 93 Cellular Location Not Available
Enzyme 93 Gene Sequence >1812 bp 
ATGAGGCGGAAGGAGAAGCGGCTCCTGCAGGCGGTGGCGCTGGTGCTGGCGGCCCTGGTC
CTCCTGCCCAACGTGGGGCTTTGGGCGCTGTACCGCGAGCGGCAGCCCGACGGCACCCCT
GGGGGATCGGGGGCGGCGGTGGCGCCGGCGGCGGGACAGGGCTCACACAGTCGACAAAAG
AAAACGTTTTTCTTGGGAGATGGGCAGAAGCTGAAGGACTGGCATGACAAGGAGGCCATC
CGGAGGGACGCTCAGCGCGTAGGAAATGGAGAACAAGGAAGACCTTACCCCATGACCGAT
GCTGAGAGAGTGGATCAGGCATACCGAGAAAATGGATTTAACATCTACGTCAGTGATAAA
ATCTCCTTGAATCGCTCTCTCCCAGATATCCGGCACCCAAACTGCAACAGCAAGCGCTAC
CTGGAGACACTTCCCAACACAAGCATCATCATCCCCTTCCACAACGAGGGCTGGTCCTCC
CTCCTCCGCACCGTCCACAGTGTGCTCAATCGCTCGCCTCCAGAGCTGGTCGCCGAGATT
GTACTGGTCGACGACTTCAGTGATCGAGAGCACCTGAAGAAGCCTCTTGAAGACTACATG
GCCCTTTTCCCCAGTGTGAGGATTCTTCGAACCAAGAAACGGGAAGGGCTGATAAGGACC
CGAATGCTGGGGGCCTCAGTGGCAACTGGGGATGTCATCACATTCTTGGATTCACACTGT
GAAGCCAATGTCAACTGGCTTCCCCCCTTGCTTGACCGCATTGCTCGGAACCGCAAGACC
ATTGTGTGCCCGATGATTGATGTAATTGACCATGACGACTTTCGGTACGAGACACAGGCA
GGGGATGCCATGCGGGGAGCCTTTGACTGGGAGATGTACTACAAGCGGATCCCGATCCCT
CCAGAACTGCAGAAAGCTGACCCCAGCGACCCATTTGAGTCTCCCGTGATGGCCGGTGGA
CTGTTCGCCGTGGATCGGAAGTGGTTCTGGGAACTCGGCGGGTATGACCCAGGCTTGGAG
ATCTGGGGAGGGGAGCAGTATGAAATCTCCTTCAAGGTGTGGATGTGTGGGGGCCGCATG
GAGGACATCCCCTGCTCCAGGGTGGGCCATATCTACAGGAAGTATGTGCCCTACAAGGTC
CCGGCCGGAGTCAGCCTGGCCCGGAACCTTAAGCGGGTGGCCGAAGTGTGGATGGATGAG
TACGCAGAGTACATTTACCAGCGCCGGCCTGAATACCGCCACCTCTCCGCTGGGGATGTC
GCAGTCCAGAAAAAGCTCCGCAGCTCCCTTAACTGCAAGAGTTTCAAGTGGTTTATGACG
AAGATAGCCTGGGACCTGCCCAAATTCTACCCACCCGTGGAGCCCCCGGCTGCAGCTTGG
GGGGAGATCCGAAATGTGGGCACAGGGCTGTGTGCAGACACAAAGCACGGGGCCTTGGGC
TCCCCACTAAGGCTAGAGGGCTGCGTCCGAGGCCGTGGGGAGGCTGCCTGGAACAACATG
CAGGTATTCACCTTCACCTGGAGAGAGGACATCCGGCCTGGAGACCCCCAGTACACCAAG
AAGTTCTGCTTTGATGCCATTTCCCACACCAGCCCTGTCACGCTGTACGACTGCCACAGC
ATGAAGGGCAACCAGCTGTGGAAATACCGCAAAGACAAGACCCTGTACCACCCTGTCAGT
GGCAGCTGCATGGACTGCAGTGAAAGTGACCATAGGATCTTCATGAACACCTGCAACCCA
TCCTCTCTCACCCAGCAATGGCTGTTTGAACACACCAACTCAACAGTCTTGGAAAAATTC
AATAGGAACTGA
Enzyme 93 GenBank Gene ID AB078145 Link Image
Enzyme 93 GeneCard ID GALNT10 Link Image
Enzyme 93 GenAtlas ID GALNT10 Link Image
Enzyme 93 HGNC ID HGNC:19873 Link Image
Enzyme 93 Chromosome Location 5
Enzyme 93 Locus 5q33.2
Enzyme 93 SNPs SNPJam Report Link Image
Enzyme 93 General References
  1. Cheng L, Tachibana K, Zhang Y, Guo J, Kahori Tachibana K, Kameyama A, Wang H, Hiruma T, Iwasaki H, Togayachi A, Kudo T, Narimatsu H: Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T10. FEBS Lett. 2002 Nov 6;531(2):115-21. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Jikuya H, Takano J, Kikuno R, Hirosawa M, Nagase T, Nomura N, Ohara O: Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones. DNA Res. 2003 Feb 28;10(1):49-57. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Kubota T, Shiba T, Sugioka S, Furukawa S, Sawaki H, Kato R, Wakatsuki S, Narimatsu H: Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10). J Mol Biol. 2006 Jun 9;359(3):708-27. Epub 2006 Apr 19. [PubMed Link Image]
Enzyme 93 Metabolite References Not Available
Enzyme 94 [top]
Enzyme 94 ID 6288
Enzyme 94 Name Polypeptide N-acetylgalactosaminyltransferase 13
Enzyme 94 Synonyms
  1. Polypeptide GalNAc transferase 13
  2. GalNAc-T13
  3. pp-GaNTase 13
  4. Protein-UDP acetylgalactosaminyltransferase 13
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13
Enzyme 94 Gene Name GALNT13
Enzyme 94 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 13 
MRRFVYCKVVLATSLMWVLVDVFLLLYFSECNKCDDKKERSLLPALRAVISRNQEGPGEM
GKAVLIPKDDQEKMKELFKINQFNLMASDLIALNRSLPDVRLEGCKTKVYPDELPNTSVV
IVFHNEAWSTLLRTVYSVINRSPHYLLSEVILVDDASERDFLKLTLENYVKNLEVPVKII
RMEERSGLIRARLRGAAASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVI
SDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREMDRRKGDRTLPVRTPTMAGGLFSIDRN
YFEEIGTYDAGMDIWGGENLEMSFRIWQCGGSLEIVTCSHVGHVFRKATPYTFPGGTGHV
INKNNRRLAEVWMDEFKDFFYIISPGVVKVDYGDVSVRKTLRENLKCKPFSWYLENIYPD
SQIPRRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDL
CLDVSRLNGPVIMLKCHHMRGNQLWEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMQDCS
GSRSQQWLLRNMTLGT
Enzyme 94 Number of Residues 556
Enzyme 94 Molecular Weight 64050.1
Enzyme 94 Theoretical pI 6.82
Enzyme 94 GO Classification Not Available
Enzyme 94 General Function Involved in polypeptide N-acetylgalactosaminyltransfera
Enzyme 94 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. Able to glycosylate SDC3. May be responsible for the synthesis of Tn antigen in neuronal cells
Enzyme 94 Pathways
Enzyme 94 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 94 Pfam Domain Function
Enzyme 94 Signals
  • None
Enzyme 94 Transmembrane Regions
  • 5-27
Enzyme 94 Essentiality Not Available
Enzyme 94 GenBank ID Protein 145309313 Link Image
Enzyme 94 UniProtKB/Swiss-Prot ID Q8IUC8 Link Image
Enzyme 94 UniProtKB/Swiss-Prot Entry Name GLT13_HUMAN Link Image
Enzyme 94 PDB ID Not Available
Enzyme 94 Cellular Location Not Available
Enzyme 94 Gene Sequence >1671 bp 
ATGAGGAGATTTGTCTACTGCAAGGTGGTTCTAGCCACTTCGCTGATGTGGGTTCTTGTT
GATGTCTTCTTACTGCTGTACTTCAGTGAATGTAACAAATGTGATGACAAGAAGGAGAGA
TCTCTGCTGCCTGCATTGAGGGCTGTTATTTCAAGAAACCAAGAAGGGCCAGGAGAAATG
GGAAAAGCTGTGTTGATTCCTAAAGATGACCAGGAGAAAATGAAAGAGCTGTTTAAAATC
AATCAGTTTAACCTTATGGCCAGTGATTTGATTGCCCTTAATAGAAGTCTGCCAGATGTA
AGATTAGAAGGATGTAAGACAAAAGTCTACCCTGATGAACTTCCAAACACAAGTGTAGTC
ATTGTGTTTCATAATGAAGCTTGGAGCACTCTCCTTAGAACTGTTTACAGTGTGATAAAT
CGTTCCCCACACTATCTACTCTCAGAGGTCATCTTGGTAGATGATGCCAGTGAAAGAGAT
TTTCTCAAGTTGACATTAGAGAATTACGTGAAAAATTTAGAAGTGCCAGTAAAAATTATT
AGGATGGAAGAACGCTCTGGGTTAATACGTGCCCGTCTTCGAGGAGCAGCTGCTTCAAAA
GGGCAGGTCATAACTTTTCTTGATGCACACTGTGAATGCACGTTAGGATGGCTGGAGCCT
TTGCTGGCAAGAATAAAGGAAGACAGGAAAACGGTTGTCTGCCCTATCATTGATGTGATT
AGTGATGATACTTTTGAATATATGGCTGGGTCAGACATGACTTATGGGGGTTTTAACTGG
AAACTGAATTTCCGCTGGTATCCTGTTCCCCAAAGAGAAATGGACAGGAGGAAAGGAGAC
AGAACATTACCTGTCAGGACCCCTACTATGGCTGGTGGCCTATTTTCTATTGACAGAAAC
TACTTTGAAGAGATAGGAACTTACGATGCAGGAATGGATATCTGGGGTGGAGAGAATCTT
GAAATGTCTTTTAGGATTTGGCAATGTGGAGGCTCCTTGGAGATTGTTACTTGCTCCCAT
GTTGGTCATGTTTTTCGGAAGGCAACTCCATACACTTTTCCTGGTGGCACTGGTCATGTC
ATCAACAAGAACAACAGGAGACTGGCAGAAGTTTGGATGGATGAATTTAAAGATTTCTTC
TACATCATATCCCCAGGTGTTGTCAAAGTGGATTATGGAGATGTGTCAGTCAGAAAAACA
CTAAGAGAAAATCTGAAGTGTAAGCCCTTTTCTTGGTACCTAGAAAACATCTATCCGGAC
TCCCAGATCCCAAGACGTTATTACTCACTTGGTGAGATAAGAAATGTTGAAACCAATCAG
TGTTTAGACAACATGGGCCGCAAGGAAAATGAAAAAGTGGGTATATTCAACTGTCATGGT
ATGGGAGGAAATCAGGTATTTTCTTACACTGCTGACAAAGAAATCCGAACCGATGACTTG
TGCTTGGATGTTTCTAGACTCAATGGACCTGTAATCATGTTAAAATGCCACCATATGAGA
GGAAATCAGTTATGGGAATATGATGCTGAGAGACTCACGTTGCGACATGTTAACAGTAAC
CAATGTCTCGATGAACCTTCTGAAGAAGACAAAATGGTGCCTACAATGCAGGACTGTAGT
GGAAGCAGATCCCAACAGTGGCTGCTAAGGAACATGACCTTGGGCACATGA
Enzyme 94 GenBank Gene ID NM_052917.2 Link Image
Enzyme 94 GeneCard ID GALNT13 Link Image
Enzyme 94 GenAtlas ID GALNT13 Link Image
Enzyme 94 HGNC ID HGNC:23242 Link Image
Enzyme 94 Chromosome Location 2
Enzyme 94 Locus 2q24.1
Enzyme 94 SNPs SNPJam Report Link Image
Enzyme 94 General References
  1. Zhang Y, Iwasaki H, Wang H, Kudo T, Kalka TB, Hennet T, Kubota T, Cheng L, Inaba N, Gotoh M, Togayachi A, Guo J, Hisatomi H, Nakajima K, Nishihara S, Nakamura M, Marth JD, Narimatsu H: Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen. J Biol Chem. 2003 Jan 3;278(1):573-84. Epub 2002 Oct 28. [PubMed Link Image]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  3. Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins. DNA Res. 2001 Aug 31;8(4):179-87. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
Enzyme 94 Metabolite References Not Available
Enzyme 95 [top]
Enzyme 95 ID 6289
Enzyme 95 Name Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3
Enzyme 95 Synonyms
  1. Polypeptide GalNAc transferase-like protein 3
  2. GalNAc-T-like protein 3
  3. pp-GaNTase-like protein 3
  4. Protein-UDP acetylgalactosaminyltransferase-like protein 3
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 3
  6. Williams-Beuren syndrome chromosomal region 17 protein
Enzyme 95 Gene Name WBSCR17
Enzyme 95 Protein Sequence >Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3 
MASLRRVKVLLVLNLIAVAGFVLFLAKCRPIAVRSGDAFHEIRPRAEVANLSAHSASPIQ
DAVLKRLSLLEDIVYRQLNGLSKSLGLIEGYGGRGKGGLPATLSPAEEEKAKGPHEKYGY
NSYLSEKISLDRSIPDYRPTKCKELKYSKDLPQISIIFIFVNEALSVILRSVHSAVNHTP
THLLKEIILVDDNSDEEELKVPLEEYVHKRYPGLVKVVRNQKREGLIRARIEGWKVATGQ
VTGFFDAHVEFTAGWAEPVLSRIQENRKRVILPSIDNIKQDNFEVQRYENSAHGYSWELW
CMYISPPKDWWDAGDPSLPIRTPAMIGCSFVVNRKFFGEIGLLDPGMDVYGGENIELGIK
VWLCGGSMEVLPCSRVAHIERKKKPYNSNIGFYTKRNALRVAEVWMDDYKSHVYIAWNLP
LENPGIDIGDVSERRALRKSLKCKNFQWYLDHVYPEMRRYNNTVAYGELRNNKAKDVCLD
QGPLENHTAILYPCHGWGPQLARYTKEGFLHLGALGTTTLLPDTRCLVDNSKSRLPQLLD
CDKVKSSLYKRWNFIQNGAIMNKGTGRCLEVENRGLAGIDLILRSCTGQRWTIKNSIK
Enzyme 95 Number of Residues 598
Enzyme 95 Molecular Weight 67750.5
Enzyme 95 Theoretical pI 9.17
Enzyme 95 GO Classification Not Available
Enzyme 95 General Function Involved in polypeptide N-acetylgalactosaminyltransfera
Enzyme 95 Specific Function May catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor
Enzyme 95 Pathways
Enzyme 95 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 95 Pfam Domain Function
Enzyme 95 Signals
  • None
Enzyme 95 Transmembrane Regions
  • 7-27
Enzyme 95 Essentiality Not Available
Enzyme 95 GenBank ID Protein 21552746 Link Image
Enzyme 95 UniProtKB/Swiss-Prot ID Q6IS24 Link Image
Enzyme 95 UniProtKB/Swiss-Prot Entry Name GLTL3_HUMAN Link Image
Enzyme 95 PDB ID Not Available
Enzyme 95 Cellular Location Not Available
Enzyme 95 Gene Sequence >1797 bp 
ATGGCTTCACTGAGAAGAGTCAAAGTGCTGTTGGTGTTGAACTTGATCGCGGTAGCCGGC
TTCGTGCTCTTCCTGGCCAAGTGCCGGCCCATCGCGGTGCGCAGCGGAGACGCCTTCCAC
GAGATCCGGCCGCGCGCCGAGGTGGCCAACCTCAGCGCGCACAGCGCCAGCCCCATCCAG
GATGCGGTCCTGAAGCGCCTGTCGCTGCTGGAGGACATCGTGTACCGGCAGCTGAATGGC
TTATCCAAATCCCTTGGGCTCATTGAAGGTTATGGTGGGCGGGGTAAAGGGGGCCTTCCG
GCTACTCTTTCCCCGGCTGAAGAAGAAAAGGCTAAGGGACCCCATGAGAAGTATGGCTAC
AATTCATACCTCAGTGAAAAAATTTCACTGGACCGTTCCATTCCGGATTATCGTCCCACC
AAGTGTAAGGAGCTCAAGTACTCCAAGGACCTGCCCCAGATATCCATCATATTCATCTTC
GTGAACGAGGCCCTGTCGGTGATCCTGCGGTCCGTGCACAGTGCCGTCAATCACACGCCC
ACACACCTGCTGAAGGAAATCATTCTGGTGGATGACAACAGCGACGAAGAGGAGCTGAAG
GTCCCCCTAGAGGAGTATGTCCACAAACGCTACCCCGGGCTGGTGAAGGTGGTAAGAAAT
CAGAAGAGGGAAGGCCTGATCCGCGCTCGCATTGAGGGCTGGAAGGTGGCTACCGGGCAG
GTCACTGGCTTCTTTGATGCCCACGTGGAATTCACCGCTGGCTGGGCTGAGCCGGTTCTA
TCCCGCATCCAGGAAAACCGGAAGCGTGTGATCCTCCCCTCCATTGACAACATCAAACAG
GACAACTTTGAGGTGCAGCGGTACGAGAACTCGGCCCACGGGTACAGCTGGGAGCTGTGG
TGCATGTACATCAGCCCCCCAAAAGACTGGTGGGACGCCGGAGACCCTTCTCTCCCCATC
AGGACCCCAGCCATGATAGGCTGCTCGTTCGTGGTCAACAGGAAGTTCTTCGGTGAAATT
GGTCTTCTGGATCCTGGCATGGATGTATACGGAGGAGAAAATATTGAACTGGGAATCAAG
GTATGGCTCTGTGGGGGCAGCATGGAGGTCCTTCCTTGCTCACGGGTGGCCCACATTGAG
CGGAAGAAGAAGCCATATAATAGCAACATTGGCTTCTACACCAAGAGGAATGCTCTTCGC
GTTGCTGAGGTCTGGATGGACGATTACAAGTCTCATGTGTACATAGCGTGGAACCTGCCG
CTGGAGAATCCGGGAATTGACATCGGTGATGTCTCCGAAAGAAGAGCATTAAGGAAAAGT
TTAAAGTGTAAGAATTTCCAGTGGTACCTGGACCATGTTTACCCAGAAATGAGAAGATAC
AATAATACCGTTGCTTACGGGGAGCTTCGCAACAACAAGGCAAAAGACGTCTGCTTGGAC
CAGGGGCCGCTGGAGAACCACACAGCAATATTGTATCCGTGCCATGGCTGGGGACCACAG
CTTGCCCGCTACACCAAGGAAGGCTTCCTGCACTTGGGTGCCCTGGGGACCACCACACTC
CTCCCTGACACCCGCTGCCTGGTGGACAACTCCAAGAGTCGGCTGCCCCAGCTCCTGGAC
TGCGACAAGGTCAAGAGCAGCCTGTACAAGCGCTGGAACTTCATCCAGAATGGAGCCATC
ATGAACAAGGGCACGGGACGCTGCCTGGAGGTGGAGAACCGGGGCCTGGCTGGCATCGAC
CTCATCCTCCGCAGCTGCACAGGTCAGAGGTGGACCATTAAGAACTCCATCAAGTAG
Enzyme 95 GenBank Gene ID AF410457 Link Image
Enzyme 95 GeneCard ID WBSCR17 Link Image
Enzyme 95 GenAtlas ID WBSCR17 Link Image
Enzyme 95 HGNC ID HGNC:16347 Link Image
Enzyme 95 Chromosome Location 7
Enzyme 95 Locus 7q11.23
Enzyme 95 SNPs SNPJam Report Link Image
Enzyme 95 General References
  1. Merla G, Ucla C, Guipponi M, Reymond A: Identification of additional transcripts in the Williams-Beuren syndrome critical region. Hum Genet. 2002 May;110(5):429-38. Epub 2002 Mar 28. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
Enzyme 95 Metabolite References Not Available
Enzyme 96 [top]
Enzyme 96 ID 6290
Enzyme 96 Name Putative polypeptide N-acetylgalactosaminyltransferase-like protein 4
Enzyme 96 Synonyms
  1. Polypeptide GalNAc transferase-like protein 4
  2. GalNAc-T-like protein 4
  3. pp-GaNTase-like protein 4
  4. Protein-UDP acetylgalactosaminyltransferase-like protein 4
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 4
Enzyme 96 Gene Name GALNTL4
Enzyme 96 Protein Sequence >Putative polypeptide N-acetylgalactosaminyltransferase-like protein 4 
MVCTRKTKTLVSTCVILSGMTNIICLLYVGWVTNYIASVYVRGQEPAPDKKLEEDKGDTL
KIIERLDHLENVIKQHIQEAPAKPEEAEAEPFTDSSLFAHWGQELSPEGRRVALKQFQYY
GYNAYLSDRLPLDRPLPDLRPSGCRNLSFPDSLPEVSIVFIFVNEALSVLLRSIHSAMER
TPPHLLKEIILVDDNSSNEELKEKLTEYVDKVNSQKPGFIKVVRHSKQEGLIRSRVSGWR
AATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFDNIKYDNFEIEEYPLAAQGF
DWELWCRYLNPPKAWWKLENSTAPIRSPALIGCFIVDRQYFQEIGLLDEGMEVYGGENVE
LGIRVWQCGGSVEVLPCSRIAHIERAHKPYTEDLTAHVRRNALRVAEVWMDEFKSHVYMA
WNIPQEDSGIDIGDITARKALRKQLQCKTFRWYLVSVYPEMRMYSDIIAYGVLQNSLKTD
LCLDQGPDTENVPIMYICHGMTPQNVYYTSSQQIHVGILSPTVDDDDNRCLVDVNSRPRL
IECSYAKAKRMKLHWQFSQGGPIQNRKSKRCLELQENSDLEFGFQLVLQKCSGQHWSITN
VLRSLAS
Enzyme 96 Number of Residues 607
Enzyme 96 Molecular Weight 69560.0
Enzyme 96 Theoretical pI 6.46
Enzyme 96 GO Classification Not Available
Enzyme 96 General Function Involved in polypeptide N-acetylgalactosaminyltransfera
Enzyme 96 Specific Function May catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor
Enzyme 96 Pathways
Enzyme 96 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 96 Pfam Domain Function
Enzyme 96 Signals
  • None
Enzyme 96 Transmembrane Regions
  • 13-35
Enzyme 96 Essentiality Not Available
Enzyme 96 GenBank ID Protein 222446618 Link Image
Enzyme 96 UniProtKB/Swiss-Prot ID Q6P9A2 Link Image
Enzyme 96 UniProtKB/Swiss-Prot Entry Name GLTL4_HUMAN Link Image
Enzyme 96 PDB ID Not Available
Enzyme 96 Cellular Location Not Available
Enzyme 96 Gene Sequence >1824 bp 
ATGGTGTGCACCAGGAAGACCAAAACTTTGGTGTCCACTTGCGTGATCCTGAGCGGCATG
ACTAACATCATCTGCCTGCTCTACGTGGGCTGGGTCACCAACTACATCGCCAGCGTGTAT
GTGCGGGGGCAGGAGCCGGCGCCCGACAAGAAGCTGGAGGAAGACAAAGGGGACACTCTG
AAGATTATTGAGCGGCTGGACCACCTGGAGAATGTCATCAAGCAGCACATTCAAGAGGCT
CCTGCCAAGCCTGAGGAGGCAGAGGCCGAGCCCTTCACAGACTCCTCTCTGTTTGCACAC
TGGGGCCAGGAGCTCAGCCCCGAAGGCCGGCGCGTGGCCCTGAAGCAATTCCAGTACTAC
GGCTACAACGCCTACCTCAGCGACCGCCTGCCCCTGGACCGGCCCCTGCCTGACCTCAGA
CCCAGTGGGTGCCGTAACCTCTCATTTCCTGACAGCCTGCCAGAGGTGAGCATCGTGTTC
ATCTTCGTCAATGAAGCGCTTTCAGTGCTGCTGCGCTCCATCCACTCGGCCATGGAACGC
ACGCCCCCACATCTGCTCAAGGAGATCATTCTGGTGGATGACAACAGCAGTAACGAGGAA
CTGAAGGAGAAGCTGACCGAATATGTGGACAAGGTGAACAGCCAGAAGCCAGGCTTCATC
AAAGTCGTGCGTCACAGCAAGCAGGAAGGCCTCATCCGCTCCAGGGTCAGTGGCTGGAGG
GCGGCCACTGCCCCTGTGGTGGCACTCTTTGATGCCCACGTGGAGTTCAATGTGGGCTGG
GCTGAACCTGTACTCACCCGCATCAAGGAGAACCGGAAGCGGATCATCTCGCCATCCTTT
GATAACATCAAATATGACAACTTTGAGATAGAAGAGTACCCGCTGGCTGCCCAGGGCTTT
GACTGGGAGCTGTGGTGCCGCTACCTAAATCCCCCCAAGGCCTGGTGGAAGCTGGAGAAC
TCCACAGCGCCAATCAGGAGCCCTGCCCTCATTGGCTGCTTCATTGTGGACCGGCAGTAC
TTCCAGGAGATCGGCCTGCTGGACGAAGGCATGGAAGTCTACGGGGGCGAGAATGTGGAG
CTTGGGATCAGGGTGTGGCAGTGTGGCGGGAGTGTGGAGGTCCTGCCCTGCTCACGGATT
GCCCACATTGAGCGAGCCCACAAGCCCTACACAGAGGACCTCACCGCCCATGTCCGCAGG
AACGCTCTCAGGGTGGCTGAAGTCTGGATGGATGAATTTAAAAGCCACGTCTACATGGCA
TGGAACATACCGCAGGAGGACTCAGGAATTGACATTGGGGACATCACTGCAAGGAAGGCT
CTCAGGAAACAGCTGCAGTGCAAGACCTTCCGGTGGTACCTGGTCAGCGTGTACCCAGAG
ATGAGGATGTACTCCGACATCATTGCCTATGGAGTGCTGCAGAATTCTCTGAAGACTGAT
TTGTGTCTTGACCAGGGGCCAGATACAGAGAATGTCCCCATCATGTACATCTGCCATGGG
ATGACGCCTCAGAACGTGTACTACACGAGCAGTCAGCAGATCCATGTGGGCATTCTGAGC
CCCACCGTGGATGATGATGACAACCGATGCCTGGTGGACGTCAACAGCCGGCCCCGGCTC
ATCGAATGCAGCTACGCCAAAGCCAAGAGGATGAAGCTTCACTGGCAGTTCTCTCAGGGA
GGACCCATCCAGAACCGCAAGTCTAAGCGCTGTCTGGAGCTGCAGGAGAATAGCGACCTG
GAGTTCGGCTTCCAGCTGGTGTTGCAGAAGTGCTCGGGCCAGCACTGGAGCATCACCAAC
GTCCTGAGGAGCCTCGCGTCCTGA
Enzyme 96 GenBank Gene ID NM_198516.2 Link Image
Enzyme 96 GeneCard ID GALNTL4 Link Image
Enzyme 96 GenAtlas ID GALNTL4 Link Image
Enzyme 96 HGNC ID HGNC:30488 Link Image
Enzyme 96 Chromosome Location 1
Enzyme 96 Locus 11p15.3
Enzyme 96 SNPs SNPJam Report Link Image
Enzyme 96 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 96 Metabolite References Not Available
Enzyme 97 [top]
Enzyme 97 ID 6291
Enzyme 97 Name N-acetylgalactosaminyltransferase 7
Enzyme 97 Synonyms
  1. Polypeptide GalNAc transferase 7
  2. GalNAc-T7
  3. pp-GaNTase 7
  4. Protein-UDP acetylgalactosaminyltransferase 7
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7
Enzyme 97 Gene Name GALNT7
Enzyme 97 Protein Sequence >N-acetylgalactosaminyltransferase 7 
MRLKIGFILRSLLVVGSFLGLVVLWSSLTPRPDDPSPLSRMREDRDVNDPMPNRGGNGLA
PGEDRFKPVVPWPHVEGVEVDLESIRRINKAKNEQEHHAGGDSQKDIMQRQYLTFKPQTF
TYHDPVLRPGILGNFEPKEPEPPGVVGGPGEKAKPLVLGPEFKQAIQASIKEFGFNMVAS
DMISLDRSVNDLRQEECKYWHYDENLLTSSVVIVFHNEGWSTLMRTVHSVIKRTPRKYLA
EIVLIDDFSNKEHLKEKLDEYIKLWNGLVKVFRNERREGLIQARSIGAQKAKLGQVLIYL
DAHCEVAVNWYAPLVAPISKDRTICTVPLIDVINGNTYEIIPQGGGDEDGYARGAWDWSM
LWKRVPLTPQEKRLRKTKTEPYRSPAMAGGLFAIEREFFFELGLYDPGLQIWGGENFEIS
YKIWQCGGKLLFVPCSRVGHIYRLEGWQGNPPPIYVGSSPTLKNYVRVVEVWWDEYKDYF
YASRPESQALPYGDISELKKFREDHNCKSFKWFMEEIAYDITSHYPLPPKNVDWGEIRGF
ETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGADGSKVMITHC
NLNEFKEWQYFKNLHRFTHIPSGKCLDRSEVLHQVFISNCDSSKTTQKWEMNNIHSV
Enzyme 97 Number of Residues 657
Enzyme 97 Molecular Weight 75388.6
Enzyme 97 Theoretical pI 7.12
Enzyme 97 GO Classification Not Available
Enzyme 97 General Function Involved in polypeptide N-acetylgalactosaminyltransfera
Enzyme 97 Specific Function Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified
Enzyme 97 Pathways Not Available
Enzyme 97 Reactions Not Available
Enzyme 97 Pfam Domain Function
Enzyme 97 Signals
  • None
Enzyme 97 Transmembrane Regions
  • 7-29
Enzyme 97 Essentiality Not Available
Enzyme 97 GenBank ID Protein 6318186 Link Image
Enzyme 97 UniProtKB/Swiss-Prot ID Q86SF2 Link Image
Enzyme 97 UniProtKB/Swiss-Prot Entry Name GALT7_HUMAN Link Image
Enzyme 97 PDB ID Not Available
Enzyme 97 Cellular Location Not Available
Enzyme 97 Gene Sequence >1974 bp 
ATGAGGCTGAAGATTGGGTTCATCTTACGCAGTTTGCTGGTGGTGGGAAGCTTCCTGGGG
CTAGTGGTCCTCTGGTCTTCCCTGACCCCGCGGCCGGACGACCCAAGCCCGCTGAGCAGG
ATGAGGGAAGACAGAGATGTCAATGACCCCATGCCCAACCGAGGCGGCAATGGACTAGCT
CCTGGGGAGGACAGATTCAAACCTGTGGTACCATGGCCTCATGTTGAAGGAGTAGAAGTG
GACTTAGAGTCTATTAGAAGAATAAACAAGGCCAAAAATGAACAAGAGCACCATGCTGGA
GGAGATTCCCAGAAAGATATCATGCAGAGGCAGTATCTCACATTTAAGCCTCAGACATTC
ACCTACCATGATCCTGTGCTTCGCCCAGGGATCCTCGGTAACTTTGAACCCAAAGAACCT
GAGCCTCCTGGAGTGGTTGGTGGCCCTGGAGAGAAAGCCAAGCCATTGGTTTTGGGACCA
GAATTCAAACAAGCAATTCAAGCCAGCATTAAAGAGTTTGGATTTAACATGGTGGCAAGT
GACATGATCTCACTGGACCGCAACGTCAATGACTTACGCCAAGAAGAATGCAAGTATTGG
CATTATGATGAAAACTTGCTCACTTCGAGCGTTGTCATTGTCTTCCATAATGAAGGATGG
TCAACCCTCATGAGAACAGTCCACAGTGTAATTAAAAGGACTCCAAGGAAATATTTAGCA
GAAATTGTGTTAATTGACGATTTCAGTAATAAAGAACACTTAAAAGAAAAACTGGATGAA
TATATTAAGCTGTGGAATGGCCTAGTGAAGGTATTTCGAAATGAAAGAAGGGAAGGTTTA
ATTCAAGCACGAAGTATTGGTGCTCAGAAGGCTAAACTTGGACAGGTTTTGATATACCTT
GATGCCCACTGTGAAGTGGCAGTTAACTGGTATGCACCACTTGTAGCTCCCATATCTAAG
GACAGAACCATTTGCACTGTGCCGCTTATAGATGTCATAAATGGCAACACATATGAAATT
ATACCCCAAGGGGGTGGTGATGAAGATGGGTATGCCCGAGGAGCATGGGATTGGAGTATG
CTCTGGAAACGGGTGCCTCTGACCCCTCAAGAGAAGAGACTGAGAAAAACAAAAACTGAA
CCGTATCGGTCCCCAGCCATGGCTGGGGGATTATGTGCCATTGAACGAGAGTTCTTCTTT
GAATTGGGTCTCTATGATCCAAGTCTCCAGATTTGGGGTGGTGAAAACTTTGAGATCTCA
TACAAGATATGGCAGTGTGGTGGCAAATTATTATTTGTTCCTTGTTCTCGTGTTGGACAT
ATCTACCGTCTTGAGGGCTGGCAAGGAAATCCTCCGCCCATTTATGTTGGGTCTTCTCCA
ACTCTGAAGAATTATGTTAGAGTTGTGGAGGTTTGGTGGGATGAATATAAAGACTACTTC
TATGCTAGTCGTCCTGAATCGCAGGCATTACCATATGGGGATATATCGGAGCTGAAAAAA
TTTCGAGAAGATCACAACTGCCAAAGTTTTAAGTGGTTCATGGAAGAAATAGCTTATGAT
ATCACCTCACACTACCCTTTGCCACCCAAAAATGTTGACTGGGGAGAAATCAGAGGCTTC
GAAACTGCTTACTGCATTGATAGCATGGGAAAAACAAATGGAGGCTTTGTTGAACTAGGA
CCCTGCCACAGGATGGGAGGGAATCAGCTTTTCAGAATCAATGAAGCAAATCAACTCATG
CAGTATGACCAGTGTTTGACAAAGGGAGCTGATGGATCAAAAGTTATGATTACACACTGT
AATCTAAATGAATTTAAGGAATGGCAGTACTTCAAGAACCTGCACAGATTTACTCATATT
CCTTCAGGAAAGTGTTTAGATCGCTCAGAGGTCCTGCATCAAGTATTCATCTCCAATTGT
GACTCCAGTAAAACGACTCAAAAATGGGAAATGAATAACATCCATAGTGTTTAG
Enzyme 97 GenBank Gene ID AJ002744 Link Image
Enzyme 97 GeneCard ID GALNT7 Link Image
Enzyme 97 GenAtlas ID GALNT7 Link Image
Enzyme 97 HGNC ID HGNC:4129 Link Image
Enzyme 97 Chromosome Location 4
Enzyme 97 Locus 4q31.1
Enzyme 97 SNPs SNPJam Report Link Image
Enzyme 97 General References
  1. Bennett EP, Hassan H, Hollingsworth MA, Clausen H: A novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates. FEBS Lett. 1999 Oct 29;460(2):226-30. [PubMed Link Image]
  2. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 97 Metabolite References Not Available
Enzyme 98 [top]
Enzyme 98 ID 6292
Enzyme 98 Name Polypeptide N-acetylgalactosaminyltransferase 6
Enzyme 98 Synonyms
  1. Polypeptide GalNAc transferase 6
  2. GalNAc-T6
  3. pp-GaNTase 6
  4. Protein-UDP acetylgalactosaminyltransferase 6
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6
Enzyme 98 Gene Name GALNT6
Enzyme 98 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 6 
MRLLRRRHMPLRLAMVGCAFVLFLFLLHRDVSSREEATEKPWLKSLVSRKDHVLDLMLEA
MNNLRDSMPKLQIRAPEAQQTLFSINQSCLPGFYTPAELKPFWERPPQDPNAPGADGKAF
QKSKWTPLETQEKEEGYKKHCFNAFASDRISLQRSLGPDTRPPECVDQKFRRCPPLATTS
VIIVFHNEAWSTLLRTVYSVLHTTPAILLKEIILVDDASTEEHLKEKLEQYVKQLQVVRV
VRQEERKGLITARLLGASVAQAEVLTFLDAHCECFHGWLEPLLARIAEDKTVVVSPDIVT
IDLNTFEFAKPVQRGRVHSRGNFDWSLTFGWETLPPHEKQRRKDETYPIKSPTFAGGLFS
ISKSYFEHIGTYDNQMEIWGGENVEMSFRVWQCGGQLEIIPCSVVGHVFRTKSPHTFPKG
TSVIARNQVRLAEVWMDSYKKIFYRRNLQAAKMAQEKSFGDISERLQLREQLHCHNFSWY
LHNVYPEMFVPDLTPTFYGAIKNLGTNQCLDVGENNRGGKPLIMYSCHGLGGNQYFEYTT
QRDLRHNIAKQLCLHVSKGALGLGSCHFTGKNSQVPKDEEWELAQDQLIRNSGSGTCLTS
QDKKPAMAPCNPSDPHQLWLFV
Enzyme 98 Number of Residues 622
Enzyme 98 Molecular Weight 71158.1
Enzyme 98 Theoretical pI 8.25
Enzyme 98 GO Classification Not Available
Enzyme 98 General Function Cell wall/membrane/envelope biogenesis
Enzyme 98 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. May participate in synthesis of oncofetal fibronectin. Has activity toward Muc1a, Muc2, EA2 and fibronectin peptides
Enzyme 98 Pathways
Enzyme 98 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 98 Pfam Domain Function
Enzyme 98 Signals
  • None
Enzyme 98 Transmembrane Regions
  • 9-28
Enzyme 98 Essentiality Not Available
Enzyme 98 GenBank ID Protein 115298684 Link Image
Enzyme 98 UniProtKB/Swiss-Prot ID Q8NCL4 Link Image
Enzyme 98 UniProtKB/Swiss-Prot Entry Name GALT6_HUMAN Link Image
Enzyme 98 PDB ID Not Available
Enzyme 98 Cellular Location Not Available
Enzyme 98 Gene Sequence >1869 bp 
ATGAGGCTCCTCCGCAGACGCCACATGCCCCTGCGCCTGGCCATGGTGGGCTGCGCCTTT
GTGCTCTTCCTCTTCCTCCTGCATAGGGATGTGAGCAGCAGAGAGGAGGCCACAGAGAAG
CCGTGGCTGAAGTCCCTGGTGAGCCGGAAGGATCACGTCCTGGACCTCATGCTGGAGGCC
ATGAACAACCTTAGAGATTCAATGCCCAAGCTCCAAATCAGGGCTCCAGAAGCCCAGCAG
ACTCTGTTCTCCATAAACCAGTCCTGCCTCCCTGGGTTCTATACCCCAGCTGAACTGAAG
CCCTTCTGGGAACGGCCACCACAGGACCCCAATGCCCCTGGGGCAGATGGAAAAGCATTT
CAGAAGAGCAAGTGGACCCCCCTGGAGACCCAGGAAAAGGAAGAAGGCTATAAGAAGCAC
TGTTTCAATGCCTTTGCCAGCGACCGGATCTCCCTGCAGAGGTCCCTGGGGCCAGACACC
CGACCACCTGAGTGTGTGGACCAGAAGTTCCGGCGCTGCCCCCCACTGGCCACCACCAGC
GTGATCATTGTGTTCCACAACGAAGCCTGGTCCACACTGCTGCGAACAGTGTACAGCGTC
CTACACACCACCCCTGCCATCTTGCTCAAGGAGATCATACTGGTGGATGATGCCAGCACA
GAGGAGCACCTAAAGGAGAAGCTGGAGCAGTACGTGAAGCAGCTGCAGGTGGTGAGGGTG
GTGCGGCAGGAGGAGCGGAAGGGGCTGATCACCGCCCGGCTGCTGGGGGCCAGCGTGGCA
CAGGCGGAGGTGCTCACGTTCCTGGATGCCCACTGTGAGTGCTTCCACGGCTGGCTGGAG
CCCCTCCTGGCTCGAATCGCTGAGGACAAGACAGTGGTGGTGAGCCCAGACATCGTCACC
ATCGACCTTAATACTTTTGAGTTCGCCAAGCCCGTCCAGAGGGGCAGAGTCCATAGCCGA
GGCAACTTTGACTGGAGCCTGACCTTCGGCTGGGAAACACTTCCTCCACATGAGAAGCAG
AGGCGCAAGGATGAAACCTACCCCATCAAATCCCCGACGTTTGCTGGTGGCCTCTTCTCC
ATCTCCAAGTCCTACTTTGAGCACATCGGTACCTATGATAATCAGATGGAGATCTGGGGA
GGGGAGAACGTGGAAATGTCCTTCCGGGTGTGGCAGTGTGGGGGCCAGCTGGAGATCATC
CCCTGCTCTGTCGTAGGCCATGTGTTCCGGACCAAGAGCCCCCACACCTTCCCCAAGGGC
ACTAGTGTCATTGCTCGCAATCAAGTGCGCCTGGCAGAGGTCTGGATGGACAGCTACAAG
AAGATTTTCTATAGGAGAAATCTGCAGGCAGCAAAGATGGCCCAAGAGAAATCCTTCGGT
GACATTTCGGAACGACTGCAGCTGAGGGAACAACTGCACTGTCACAACTTTTCCTGGTAC
CTGCACAATGTCTACCCAGAGATGTTTGTTCCTGACCTGACGCCCACCTTCTATGGTGCC
ATCAAGAACCTCGGCACCAACCAATGCCTGGATGTGGGTGAGAACAACCGCGGGGGGAAG
CCCCTCATCATGTACTCCTGCCACGGCCTTGGCGGCAACCAGTACTTTGAGTACACAACT
CAGAGGGACCTTCGCCACAACATCGCAAAGCAGCTGTGTCTACATGTCAGCAAGGGTGCT
CTGGGCCTTGGGAGCTGTCACTTCACTGGCAAGAATAGCCAGGTCCCCAAGGACGAGGAA
TGGGAATTGGCCCAGGATCAGCTCATCAGGAACTCAGGATCTGGTACCTGCCTGACATCC
CAGGACAAAAAGCCAGCCATGGCCCCCTGCAATCCCAGTGACCCCCATCAGTTGTGGCTC
TTTGTCTAG
Enzyme 98 GenBank Gene ID NM_007210.3 Link Image
Enzyme 98 GeneCard ID GALNT6 Link Image
Enzyme 98 GenAtlas ID GALNT6 Link Image
Enzyme 98 HGNC ID HGNC:4128 Link Image
Enzyme 98 Chromosome Location 1
Enzyme 98 Locus 12q13
Enzyme 98 SNPs SNPJam Report Link Image
Enzyme 98 General References
  1. Bennett EP, Hassan H, Mandel U, Hollingsworth MA, Akisawa N, Ikematsu Y, Merkx G, van Kessel AG, Olofsson S, Clausen H: Cloning and characterization of a close homologue of human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy. J Biol Chem. 1999 Sep 3;274(36):25362-70. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 98 Metabolite References Not Available
Enzyme 99 [top]
Enzyme 99 ID 6293
Enzyme 99 Name Polypeptide N-acetylgalactosaminyltransferase 14
Enzyme 99 Synonyms
  1. Polypeptide GalNAc transferase 14
  2. GalNAc-T14
  3. pp-GaNTase 14
  4. Protein-UDP acetylgalactosaminyltransferase 14
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14
Enzyme 99 Gene Name GALNT14
Enzyme 99 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 14 
MRRLTRRLVLPVFGVLWITVLLFFWVTKRKLEVPTGPEVQTPKPSDADWDDLWDQFDERR
YLNAKKWRVGDDPYKLYAFNQRESERISSNRAIPDTRHLRCTLLVYCTDLPPTSIIITFH
NEARSTLLRTIRSVLNRTPTHLIREIILVDDFSNDPDDCKQLIKLPKVKCLRNNERQGLV
RSRIRGADIAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVCPVIDIINLDTFTYIE
SASELRGGFDWSLHFQWEQLSPEQKARRLDPTEPIRTPIIAGGLFVIDKAWFDYLGKYDM
DMDIWGGENFEISFRVWMCGGSLEIVPCSRVGHVFRKKHPYVFPDGNANTYIKNTKRTAE
VWMDEYKQYYYAARPFALERPFGNVESRLDLRKNLRCQSFKWYLENIYPELSIPKESSIQ
KGNIRQRQKCLESQRQNNQETPNLKLSPCAKVKGEDAKSQVWAFTYTQQILQEELCLSVI
TLFPGAPVVLVLCKNGDDRQQWTKTGSHIEHIASHLCLDTDMFGDGTENGKEIVVNPCES
SLMSQHWDMVSS
Enzyme 99 Number of Residues 552
Enzyme 99 Molecular Weight 64320.0
Enzyme 99 Theoretical pI 7.78
Enzyme 99 GO Classification Not Available
Enzyme 99 General Function Involved in polypeptide N-acetylgalactosaminyltransfera
Enzyme 99 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). May be involved in O-glycosylation in kidney
Enzyme 99 Pathways
Enzyme 99 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 99 Pfam Domain Function
Enzyme 99 Signals
  • None
Enzyme 99 Transmembrane Regions
  • 7-26
Enzyme 99 Essentiality Not Available
Enzyme 99 GenBank ID Protein 28268674 Link Image
Enzyme 99 UniProtKB/Swiss-Prot ID Q96FL9 Link Image
Enzyme 99 UniProtKB/Swiss-Prot Entry Name GLT14_HUMAN Link Image
Enzyme 99 PDB ID Not Available
Enzyme 99 Cellular Location Not Available
Enzyme 99 Gene Sequence >1659 bp 
ATGCGGCGCCTGACTCGTCGGCTGGTTCTGCCAGTCTTCGGGGTGCTCTGGATCACGGTG
CTGCTGTTCTTCTGGGTAACCAAGAGGAAGTTGGAGGTGCCGACGGGACCTGAAGTGCAG
ACCCCTAAGCCTTCGGACGCTGACTGGGACGACCTGTGGGACCAGTTTGATGAGCGGCGG
TATCTGAATGCCAAAAAGTGGCGCGTTGGTGACGACCCCTATAAGCTGTATGCTTTCAAC
CAGCGGGAGAGTGAGCGGATCTCCAGCAATCGGGCCATCCCGGACACTCGCCATCTGAGA
TGCACACTGCTGGTGTATTGCACGGACCTTCCACCCACTAGCATCATCATCACCTTCCAC
AACGAGGCCCGCTCCACGCTGCTCAGGACCATCCGCAGTGTATTAAACCGCACCCCTACG
CATCTGATCCGGGAAATCATATTAGTGGATGACTTCAGCAATGATCCTGATGACTGTAAA
CAGCTCATCAAGTTGCCCAAGGTGAAATGCTTGCGCAATAATGAACGGCAAGGTCTGGTC
CGGTCCCGGATTCGGGGCGCTGACATCGCCCAGGGCACCACTCTGACTTTCCTCGACAGC
CACTGTGAGGTGAACAGGGACTGGCTCCAGCCTCTGTTGCACAGGGTCAAAGAGGACTAC
ACGCGGGTGGTGTGCCCTGTGATCGATATCATTAACCTGGACACCTTCACCTACATCGAG
TCTGCCTCGGAGCTCAGAGGGGGGTTTGACTGGAGCCTCCACTTCCAGTGGGAGCAGCTC
TCCCCAGAGCAGAAGGCTCGGCGCCTGGACCCCACGGAGCCCATCAGGACTCCTATCATA
GCTGGAGGGCTCTTCGTGATCGACAAAGCTTGGTTTGATTACCTGGGGAAATATGATATG
GACATGGACATCTGGGGTGGGGAGAACTTTGAAATCTCCTTCCGAGTGTGGATGTGCGGG
GGCAGCCTAGAGATCGTCCCCTGCAGCCGAGTGGGGCACGTCTTCCGGAAGAAGCACCCC
TACGTTTTCCCTGATGGAAATGCCAACACGTATATAAAGAACACCAAGCGGACAGCTGAA
GTGTGGATGGATGAATACAAGCAATACTATTACGCTGCCCGGCCATTCGCCCTGGAGAGG
CCCTTCGGGAATGTTGAGAGCAGATTGGACCTGAGGAAGAATCTGCGCTGCCAGAGCTTC
AAGTGGTACCTGGAGAATATCTACCCTGAACTCAGCATCCCCAAGGAGTCCTCCATCCAG
AAGGGCAATATCCGACAGAGACAGAAGTGCCTGGAATCTCAAAGGCAGAACAACCAAGAA
ACCCCAAACCTAAAGTTGAGCCCCTGTGCCAAGGTCAAAGGCGAAGATGCAAAGTCCCAG
GTATGGGCCTTCACATACACCCAGCAGATCCTCCAGGAGGAGCTGTGCCTGTCAGTCATC
ACCTTGTTCCCTGGCGCCCCAGTGGTTCTTGTCCTTTGCAAGAATGGAGATGACCGACAG
CAATGGACCAAAACTGGTTCCCACATCGAGCACATAGCATCCCACCTCTGCCTCGATACA
GATATGTTCGGTGATGGCACCGAGAACGGCAAGGAAATCGTCGTCAACCCATGTGAGTCC
TCACTCATGAGCCAGCACTGGGACATGGTGAGCTCTTGA
Enzyme 99 GenBank Gene ID AB078144 Link Image
Enzyme 99 GeneCard ID GALNT14 Link Image
Enzyme 99 GenAtlas ID GALNT14 Link Image
Enzyme 99 HGNC ID HGNC:22946 Link Image
Enzyme 99 Chromosome Location 2
Enzyme 99 Locus 2p23.1
Enzyme 99 SNPs SNPJam Report Link Image
Enzyme 99 General References
  1. Wang H, Tachibana K, Zhang Y, Iwasaki H, Kameyama A, Cheng L, Guo J, Hiruma T, Togayachi A, Kudo T, Kikuchi N, Narimatsu H: Cloning and characterization of a novel UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, pp-GalNAc-T14. Biochem Biophys Res Commun. 2003 Jan 17;300(3):738-44. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 99 Metabolite References Not Available
Enzyme 100 [top]
Enzyme 100 ID 6294
Enzyme 100 Name Polypeptide N-acetylgalactosaminyltransferase 2
Enzyme 100 Synonyms
  1. Polypeptide GalNAc transferase 2
  2. GalNAc-T2
  3. pp-GaNTase 2
  4. Protein-UDP acetylgalactosaminyltransferase 2
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2
  6. Polypeptide N-acetylgalactosaminyltransferase 2 soluble form
Enzyme 100 Gene Name GALNT2
Enzyme 100 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 2 
MRRRSRMLLCFAFLWVLGIAYYMYSGGGSALAGGAGGGAGRKEDWNEIDPIKKKDLHHSN
GEEKAQSMETLPPGKVRWPDFNQEAYVGGTMVRSGQDPYARNKFNQVESDKLRMDRAIPD
TRHDQCQRKQWRVDLPATSVVITFHNEARSALLRTVVSVLKKSPPHLIKEIILVDDYSND
PEDGALLGKIEKVRVLRNDRREGLMRSRVRGADAAQAKVLTFLDSHCECNEHWLEPLLER
VAEDRTRVVSPIIDVINMDNFQYVGASADLKGGFDWNLVFKWDYMTPEQRRSRQGNPVAP
IKTPMIAGGLFVMDKFYFEELGKYDMMMDVWGGENLEISFRVWQCGGSLEIIPCSRVGHV
FRKQHPYTFPGGSGTVFARNTRRAAEVWMDEYKNFYYAAVPSARNVPYGNIQSRLELRKK
LSCKPFKWYLENVYPELRVPDHQDIAFGALQQGTNCLDTLGHFADGVVGVYECHNAGGNQ
EWALTKEKSVKHMDLCLTVVDRAPGSLIKLQGCRENDSRQKWEQIEGNSKLRHVGSNLCL
DSRTAKSGGLSVEVCGPALSQQWKFTLNLQQ
Enzyme 100 Number of Residues 571
Enzyme 100 Molecular Weight 64732.3
Enzyme 100 Theoretical pI 8.46
Enzyme 100 GO Classification Not Available
Enzyme 100 General Function Involved in manganese ion binding
Enzyme 100 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region
Enzyme 100 Pathways
Enzyme 100 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 100 Pfam Domain Function
Enzyme 100 Signals
  • None
Enzyme 100 Transmembrane Regions
  • 7-24
Enzyme 100 Essentiality Not Available
Enzyme 100 GenBank ID Protein 158261119 Link Image
Enzyme 100 UniProtKB/Swiss-Prot ID Q10471 Link Image
Enzyme 100 UniProtKB/Swiss-Prot Entry Name GALT2_HUMAN Link Image
Enzyme 100 PDB ID Not Available
Enzyme 100 Cellular Location Not Available
Enzyme 100 Gene Sequence >1716 bp 
ATGCGGCGGCGCTCGCGGATGCTGCTCTGCTTCGCCTTCCTGTGGGTGCTGGGCATCGCC
TACTACATGTACTCGGGGGGCGGCTCTGCGCTGGCCGGGGGCGCGGGCGGCGGCGCCGGC
AGGAAGGAGGACTGGAATGAAATTGACCCCATTAAAAAGAAAGACCTTCATCACAGCAAT
GGAGAAGAGAAAGCACAAAGCATGGAGACCCTCCCTCCAGGGAAAGTACGGTGGCCAGAC
TTTAACCAGGAAGCTTATGTTGGAGGGACGATGGTCCGCTCCGGGCAGGACCCTTACGCC
CGCAACAAGTTCAACCAGGTGGAGAGTGATAAGCTTCGAATGGACAGAGCCATCCCTGAC
ACCCGGCATGACCAGTGTCAGCGGAAGCAGTGGCGGGTGGATCTGCCGGCCACCAGCGTG
GTGATCACGTTTCACAATGAAGCCAGGTCGGCCCTACTCAGGACCGTGGTCAGCGTGCTT
AAGAAAAGCCCGCCCCATCTCATAAAAGAAATCATCTTGGTGGATGACTACAGCAATGAT
CCTGAGGACGGGGCTCTCTTGGGGAAAATTGAGAAAGTGCGAGTTCTTAGAAATGATCGA
CGAGAAGGCCTCATGCGCTCACGGGTTCGGGGGGCCGATGCTGCCCAAGCCAAGGTCCTG
ACCTTCCTGGACAGTCACTGCGAGTGTAATGAGCACTGGCTGGAGCCCCTCCTGGAAAGG
GTGGCGGAGGACAGGACTCGGGTTGTGTCACCCATCATCGATGTCATTAATATGGACAAC
TTTCAGTATGTGGGGGCATCTGCTGACTTGAAGGGCGGTTTTGACTGGAACTTGGTATTC
AAGTGGGATTACATGACGCCTGAGCAGAGAAGGTCCCGGCAGGGGAACCCAGTCGCCCCT
ATAAAAACCCCCATGATTGCTGGTGGGCTGTTTGTGATGGATAAGTTCTATTTTGAAGAA
CTGGGGAAGTACGACATGATGATGGATGTGTGGGGAGGAGAGAACCTAGAGATCTCGTTC
CGCGTGTGGCAGTGTGGTGGCAGCCTGGAGATCATCCCGTGCAGCCGTGTGGGACACGTG
TTCCGGAAGCAGCACCCCTACACGTTCCCGGGTGGCAGTGGCACTGTCTTTGCCCGAAAC
ACCCGCCGGGCAGCAGAGGTCTGGATGGATGAATACAAAAATTTCTATTATGCAGCAGTG
CCTTCTGCTAGAAACGTTCCTTATGGAAATATTCAGAGCAGATTGGAGCTTAGGAAGAAA
CTCAGCTGCAAGCCTTTCAAATGGTACCTTGAAAATGTCTATCCAGAGTTAAGGGTTCCA
GACCATCAGGATATAGCTTTTGGGGCCTTGCAGCAGGGAACTAACTGCCTCGACACTTTG
GGACACTTTGCTGATGGTGTGGTTGGAGTTTATGAATGTCACAATGCTGGGGGAAACCAG
GAATGGGCCTTGACGAAGGAGAAGTCGGTGAAGCACATGGATTTGTGCCTTACTGTGGTG
GACCGGGCACCGGGCTCTCTTATAAAGCTGCAGGGCTGCCGAGAAAATGACAGCAGACAG
AAATGGGAACAGATCGAGGGCAACTCCAAGCTGAGGCACGTGGGCAGCAACCTGTGCCTG
GACAGTCGCACGGCCAAGAGCGGGGGCCTAAGCGTGGAGATGTGTGGCCCGGCCCTTTCG
CAGCAGTGGAAGTTCACGCTCAACCTGCAGCAGTAG
Enzyme 100 GenBank Gene ID AK290048 Link Image
Enzyme 100 GeneCard ID GALNT2 Link Image
Enzyme 100 GenAtlas ID GALNT2 Link Image
Enzyme 100 HGNC ID HGNC:4124 Link Image
Enzyme 100 Chromosome Location 1
Enzyme 100 Locus 1q41-q42
Enzyme 100 SNPs SNPJam Report Link Image
Enzyme 100 General References
  1. White T, Bennett EP, Takio K, Sorensen T, Bonding N, Clausen H: Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. J Biol Chem. 1995 Oct 13;270(41):24156-65. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Wandall HH, Hassan H, Mirgorodskaya E, Kristensen AK, Roepstorff P, Bennett EP, Nielsen PA, Hollingsworth MA, Burchell J, Taylor-Papadimitriou J, Clausen H: Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3. J Biol Chem. 1997 Sep 19;272(38):23503-14. [PubMed Link Image]
  6. Rottger S, White J, Wandall HH, Olivo JC, Stark A, Bennett EP, Whitehouse C, Berger EG, Clausen H, Nilsson T: Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus. J Cell Sci. 1998 Jan;111 ( Pt 1):45-60. [PubMed Link Image]
  7. Iwasaki H, Zhang Y, Tachibana K, Gotoh M, Kikuchi N, Kwon YD, Togayachi A, Kudo T, Kubota T, Narimatsu H: Initiation of O-glycan synthesis in IgA1 hinge region is determined by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2. J Biol Chem. 2003 Feb 21;278(8):5613-21. Epub 2002 Nov 15. [PubMed Link Image]
Enzyme 100 Metabolite References Not Available
Enzyme 101 [top]
Enzyme 101 ID 6295
Enzyme 101 Name Polypeptide N-acetylgalactosaminyltransferase 12
Enzyme 101 Synonyms
  1. Polypeptide GalNAc transferase 12
  2. GalNAc-T12
  3. pp-GaNTase 12
  4. Protein-UDP acetylgalactosaminyltransferase 12
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12
Enzyme 101 Gene Name GALNT12
Enzyme 101 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 12 
MWGRTARRRCPRELRRGREALLVLLALLALAGLGSVLRAQRGAGAGAAEPGPPRTPRPGR
REPVMPRPPVPANALGARGEAVRLQLQGEELRLQEESVRLHQINIYLSDRISLHRRLPER
WNPLCKEKKYDYDNLPRTSVIIAFYNEAWSTLLRTVYSVLETSPDILLEEVILVDDYSDR
EHLKERLANELSGLPKVRLIRANKREGLVRARLLGASAARGDVLTFLDCHCECHEGWLEP
LLQRIHEEESAVVCPVIDVIDWNTFEYLGNSGEPQIGGFDWRLVFTWHTVPERERIRMQS
PVDVIRSPTMAGGLFAVSKKYFEYLGSYDTGMEVWGGENLEFSFRIWQCGGVLETHPCSH
VGHVFPKQAPYSRNKALANSVRAAEVWMDEFKELYYHRNPRARLEPFGDVTERKQLRDKL
QCKDFKWFLETVYPELHVPEDRPGFFGMLQNKGLTDYCFDYNPPDENQIVGHQVILYLCH
GMGQNQFFEYTSQKEIRYNTHQPEGCIAVEAGMDTLIMHLCEETAPENQKFILQEDGSLF
HEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKWFFKERML
Enzyme 101 Number of Residues 581
Enzyme 101 Molecular Weight 66937.8
Enzyme 101 Theoretical pI 6.78
Enzyme 101 GO Classification Not Available
Enzyme 101 General Function Involved in polypeptide N-acetylgalactosaminyltransfera
Enzyme 101 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with Muc2 and Muc7. Displays enzymatic activity toward the Gal-NAc- Muc5AC glycopeptide, but no detectable activity to mono-GalNAc- glycosylated Muc1a, Muc2, Muc7 and EA2. May play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs
Enzyme 101 Pathways
Enzyme 101 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 101 Pfam Domain Function
Enzyme 101 Signals
  • None
Enzyme 101 Transmembrane Regions
  • 20-37
Enzyme 101 Essentiality Not Available
Enzyme 101 GenBank ID Protein 22122074 Link Image
Enzyme 101 UniProtKB/Swiss-Prot ID Q8IXK2 Link Image
Enzyme 101 UniProtKB/Swiss-Prot Entry Name GLT12_HUMAN Link Image
Enzyme 101 PDB ID Not Available
Enzyme 101 Cellular Location Not Available
Enzyme 101 Gene Sequence >1746 bp 
ATGTGGGGGCGCACGGCGCGGCGGCGCTGCCCGCGGGAACTGCGGCGCGGCCGGGAGGCG
CTGTTGGTGCTCCTGGCGCTACTGGCGTTGGCCGGGCTGGGCTCGGTGCTGCGGGCGCAG
CGTGGGGCCGGGGCCGGGGCTGCCGAGCCGGGACCCCCGCGCACCCCGCGCCCCGGGCGG
CGCGAGCCGGTCATGCCGCGGCCGCCGGTGCCGGCGAACGCGCTGGGCGCGCGGGGCGAG
GCGGTGCGGCTGCAGCTGCAGGGCGAGGAGCTGCGGCTGCAGGAGGAGAGCGTGCGGCTG
CACCAGATTAACATCTACCTCAGCGACCGCATCTCACTGCACCGCCGCCTGCCCGTGCGC
TGGAACCCGCTGTGCAAAGAGAAGAAATATGATTATGATAATTTGCCCAGGACATCTGTT
ATCATAGCATTTTATAATGAAGCCTGGTCAACTCTCCTTCGGACAGTTTACAGTGTCCTT
GAGACATCCCCGGATATCCTGCTAGAAGAAGTGATCCTTGTAGATGACTACAGTGATAGA
GAGCACCTGAAGGAGCGCTTGGCCAATGAGCTTTCGGGACTGCCCAAGGTGCGCCTGATC
CGCGCCAACAAGAGAGAGGGCCTGGTGCGAGCCCGGCTGCTGGGGGCGTCTGCGGCGAGG
GGCGATGTTCTGACCTTCCTGGACTGTCACTGTGAGTGCCACGAAGGGTGGCTGGAGCCG
CTGCTGCAGAGGATCCATGAAGAGGAGTCGGCAGTGGTGTGCCCGGTGATTGATGTGATC
GACTGGAACACCTTCGAATACCTGGGGAACTCCGGGGAGCCCCAGATCGGCGGTTTCGAC
TGGAGGCTGGTGTTCACGTGGCACACAGTTCCTGAGAGGGAGAGGATACGGATGCAATCC
CCCGTCGATGTCATCAGGTCTCCAACAATGGCTGGTGGGCTGTTTGCTGTGAGTAAGAAA
TATTTTGAATATCTGGGGTCTTATGATACAGGAATGGAAGTTTGGGGAGGAGAAAACCTC
GAATTTTCCTTTAGGATCTGGCAGTGTGGTGGGGTTCTGGAAACACACCCATGTTCCCAT
GTTGGCCATGTTTTCCCCAAGCAAGCTCCCTACTCCCGCAACAAGGCTCTGGCCAACAGT
GTTCGTGCAGCTGAAGTATGGATGGATGAATTTAAAGAGCTCTACTACCATCGCAACCCC
CGTGCCCGCTTGGAACCTTTTGGGGATGTGACAGAGAGGAAGCAGCTCCGGGACAAGCTC
CAGTGTAAAGACTTCAAGTGGTTCTTGGAGACTGTGTATCCAGAACTGCATGTGCCTGAG
GACAGGCCTGGCTTCTTCGGGATGCTCCAGAACAAAGGACTAACAGACTACTGCTTTGAC
TATAACCCTCCCGATGAAAACCAGATTGTGGGACACCAGGTCATTCTGTACCTCTGTCAT
GGGATGGGCCAGAATCAGTTTTTCGAGTACACGTCCCAGAAAGAAATACGCTATAACACC
CACCAGCCTGAGGGCTGCATTGCTGTGGAAGCAGGAATGGATACCCTTATCATGCATCTC
TGCGAAGAAACTGCCCCAGAGAATCAGAAGTTCATCTTGCAGGAGGATGGATCTTTATTT
CACGAACAGTCCAAGAAATGTGTCCAGGCTGCGAGGAAGGAGTCGAGTGACAGTTTCGTT
CCACTCTTACGAGACTGCACCAACTCGGATCATCAGAAATGGTTCTTCAAAGAGCGCATG
TTATGA
Enzyme 101 GenBank Gene ID AB078146 Link Image
Enzyme 101 GeneCard ID GALNT12 Link Image
Enzyme 101 GenAtlas ID GALNT12 Link Image
Enzyme 101 HGNC ID HGNC:19877 Link Image
Enzyme 101 Chromosome Location 9
Enzyme 101 Locus 9q22.33
Enzyme 101 SNPs SNPJam Report Link Image
Enzyme 101 General References
  1. Guo JM, Zhang Y, Cheng L, Iwasaki H, Wang H, Kubota T, Tachibana K, Narimatsu H: Molecular cloning and characterization of a novel member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, pp-GalNAc-T12. FEBS Lett. 2002 Jul 31;524(1-3):211-8. [PubMed Link Image]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
Enzyme 101 Metabolite References Not Available
Enzyme 102 [top]
Enzyme 102 ID 6296
Enzyme 102 Name Polypeptide N-acetylgalactosaminyltransferase 1
Enzyme 102 Synonyms
  1. Polypeptide GalNAc transferase 1
  2. GalNAc-T1
  3. pp-GaNTase 1
  4. Protein-UDP acetylgalactosaminyltransferase 1
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1
  6. Polypeptide N-acetylgalactosaminyltransferase 1 soluble form
Enzyme 102 Gene Name GALNT1
Enzyme 102 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 1 
MRKFAYCKVVLATSLIWVLLDMFLLLYFSECNKCDEKKERGLPAGDVLEPVQKPHEGPGE
MGKPVVIPKEDQEKMKEMFKINQFNLMASEMIALNRSLPDVRLEGCKTKVYPDNLPTTSV
VIVFHNEAWSTLLRTVHSVINRSPRHMIEEIVLVDDASERDFLKRPLESYVKKLKVPVHV
IRMEQRSGLIRARLKGAAVSKGQVITFLDAHCECTVGWLEPLLARIKHDRRTVVCPIIDV
ISDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREMDRRKGDRTLPVRTPTMAGGLFSIDR
DYFQEIGTYDAGMDIWGGENLEISFRIWQCGGTLEIVTCSHVGHVFRKATPYTFPGGTGQ
IINKNNRRLAEVWMDEFKNFFYIISPGVTKVDYGDISSRVGLRHKLQCKPFSWYLENIYP
DSQIPRHYFSLGEIRNVETNQCLDNMARKENEKVGIFNCHGMGGNQVFSYTANKEIRTDD
LCLDVSKLNGPVTMLKCHHLKGNQLWEYDPVKLTLQHVNSNQCLDKATEEDSQVPSIRDC
NGSRSQQWLLRNVTLPEIF
Enzyme 102 Number of Residues 559
Enzyme 102 Molecular Weight 64218.5
Enzyme 102 Theoretical pI 7.77
Enzyme 102 GO Classification Not Available
Enzyme 102 General Function Involved in manganese ion binding
Enzyme 102 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7
Enzyme 102 Pathways
Enzyme 102 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 102 Pfam Domain Function
Enzyme 102 Signals
  • None
Enzyme 102 Transmembrane Regions
  • 9-28
Enzyme 102 Essentiality Not Available
Enzyme 102 GenBank ID Protein 13124891 Link Image
Enzyme 102 UniProtKB/Swiss-Prot ID Q10472 Link Image
Enzyme 102 UniProtKB/Swiss-Prot Entry Name GALT1_HUMAN Link Image
Enzyme 102 PDB ID 1XHB Link Image
Enzyme 102 PDB File Show
Enzyme 102 3D Structure
Enzyme 102 Cellular Location Not Available
Enzyme 102 Gene Sequence >1680 bp 
ATGAGAAAATTTGCATACTGCAAGGTGGTCCTAGCCACCTCCTTGATTTGGGTACTCTTG
GATATGTTCCTGCTGCTTTACTTCAGTGAATGCAACAAATGTGATGAAAAAAAGGAGAGA
GGACTTCCTGCTGGAGATGTTCTAGAGCCAGTACAAAAGCCTCATGAAGGTCCTGGAGAA
ATGGGGAAACCAGTCGTCATTCCTAAAGAGGATCAAGAAAAGATGAAAGAGATGTTTAAA
ATCAATCAGTTCAATTTAATGGCAAGTGAGATGATTGCACTCAACAGATCTTTACCAGAT
GTTAGGTTAGAAGGGTGTAAAACAAAGGTGTATCCAGATAATCTTCCTACAACAAGTGTG
GTGATTGTTTTCCACAATGAGGCTTGGAGCACACTTCTGCGAACTGTCCATAGTGTCATT
AATCGCTCACCAAGACACATGATAGAAGAAATTGTTCTAGTAGATGATGCCAGTGAAAGA
GACTTTTTGAAAAGGCCTTTAGAGAGTTATGTGAAAAAACTAAAAGTACCAGTTCATGTA
ATTCGAATGGAACAACGTTCTGGATTGATCAGAGCTAGATTAAAAGGAGCTGCTGTGTCT
AAAGGCCAAGTGATCACCTTCCTGGATGCCCATTGTGAGTGTACAGTGGGATGGCTGGAG
CCTCTCTTGGCCAGGATCAAACATGACAGGAGAACAGTGGTGTGTCCCATCATCGATGTG
ATCAGTGATGATACTTTTGAGTACATGGCAGGCTCTGATATGACCTATGGTGGGTTCAAC
TGGAAGCTCAATTTTCGCTGGTATCCTGTTCCCCAAAGAGAAATGGACAGAAGGAAAGGT
GATCGGACTCTTCCTGTCAGGACACCTACCATGGCAGGAGGCCTTTTTTCAATAGACAGA
GATTACTTTCAGGAAATTGGAACATATGATGCTGGAATGGATATTTGGGGAGGAGAAAAC
CTAGAAATTTCCTTTAGGATTTGGCAGTGTGGAGGAACTTTGGAAATTGTTACATGCTCA
CATGTTGGACATGTGTTTCGGAAAGCTACACCTTACACGTTTCCAGGAGGCACAGGGCAG
ATTATCAATAAAAATAACAGACGACTTGCAGAAGTGTGGATGGATGAATTCAAGAATTTC
TTCTATATAATTTCTCCAGGTGTTACAAAGGTAGATTATGGAGATATATCGTCAAGAGTT
GGTCTAAGACACAAACTACAATGCAAACCTTTTTCCTGGTACCTAGAGAATATATATCCT
GATTCTCAAATTCCACGTCACTATTTCTCATTGGGAGAGATACGAAATGTGGAAACGAAT
CAGTGTCTAGATAACATGGCTAGAAAAGAGAATGAAAAAGTTGGAATTTTTAATTGCCAT
GGTATGGGGGGTAATCAGGTTTTCTCTTATACTGCCAACAAAGAAATTAGAACAGATGAC
CTTTGCTTGGATGTTTCCAAACTTAATGGCCCAGTTACAATGCTCAAATGCCACCACCTA
AAAGGCAACCAACTCTGGGAGTATGACCCAGTGAAATTAACCCTGCAGCATGTGAACAGT
AATCAGTGCCTGGATAAAGCCACAGAAGAGGATAGCCAGGTGCCCAGCATTAGAGACTGC
AATGGAAGTCGGTCCCAGCAGTGGCTTCTTCGAAACGTCACCCTGCCAGAAATATTCTGA
Enzyme 102 GenBank Gene ID NM_020474.3 Link Image
Enzyme 102 GeneCard ID GALNT1 Link Image
Enzyme 102 GenAtlas ID GALNT1 Link Image
Enzyme 102 HGNC ID HGNC:4123 Link Image
Enzyme 102 Chromosome Location 1
Enzyme 102 Locus 18q12.1
Enzyme 102 SNPs SNPJam Report Link Image
Enzyme 102 General References
  1. Meurer JA, Naylor JM, Baker CA, Thomsen DR, Homa FL, Elhammer AP: cDNA cloning, expression, and chromosomal localization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase. J Biochem (Tokyo). 1995 Sep;118(3):568-74. [PubMed Link Image]
  2. White T, Bennett EP, Takio K, Sorensen T, Bonding N, Clausen H: Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. J Biol Chem. 1995 Oct 13;270(41):24156-65. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Meurer JA, Drong RF, Homa FL, Slightom JL, Elhammer AP: Organization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase gene and a related processed pseudogene. Glycobiology. 1996 Mar;6(2):231-41. [PubMed Link Image]
  5. Wandall HH, Hassan H, Mirgorodskaya E, Kristensen AK, Roepstorff P, Bennett EP, Nielsen PA, Hollingsworth MA, Burchell J, Taylor-Papadimitriou J, Clausen H: Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3. J Biol Chem. 1997 Sep 19;272(38):23503-14. [PubMed Link Image]
  6. Rottger S, White J, Wandall HH, Olivo JC, Stark A, Bennett EP, Whitehouse C, Berger EG, Clausen H, Nilsson T: Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus. J Cell Sci. 1998 Jan;111 ( Pt 1):45-60. [PubMed Link Image]
Enzyme 102 Metabolite References Not Available
Enzyme 103 [top]
Enzyme 103 ID 6297
Enzyme 103 Name Polypeptide N-acetylgalactosaminyltransferase 5
Enzyme 103 Synonyms
  1. Polypeptide GalNAc transferase 5
  2. GalNAc-T5
  3. pp-GaNTase 5
  4. Protein-UDP acetylgalactosaminyltransferase 5
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5
Enzyme 103 Gene Name GALNT5
Enzyme 103 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 5 
MNRIRKFFRGSGRVLAFIFVASVIWLLFDMAALRLSFSEINTRVIKEDIVRRERIGFRVQ
PDQGKIFYSSIKEMKPPLRGHGKGAWGKENVRKTEESVLKVEVDLDQTQRERKMQNALGR
GKVVPLWHPAHLQTLPVTPNKQKTDGRGTKPEASSHQGTPKQTTAQGAPKTSFIAAKGTQ
VVKISVHMGRVSLKQEPRKSHSPSSDTSKLAAERDLNVTISLSTDRPKQRSQAVANERAH
PASTAVPKSGEAMALNKTKTQSKEVNANKHKANTSLPFPKFTVNSNRLRKQSINETPLGS
LSKDDGARGAHGKKLNFSESHLVIITKEEEQKADPKEVSNSKTKTIFPKVLGKSQSKHIS
RNRSEMSSSSLAPHRVPLSQTNHALTGGLEPAKINITAKAPSTEYNQSHIKALLPEDSGT
HQVLRIDVTLSPRDPKAPGQFGRPVVVPHGKEKEAERRWKEGNFNVYLSDLIPVDRAIED
TRPAGCAEQLVHNNLPTTSVIMCFVDEVWSTLLRSVHSVINRSPPHLIKEILLVDDFSTK
DYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLDSHVECNVGWLEP
LLERVYLSRKKVACPVIEVINDKDMSYMTVDNFQRGIFVWPMNFGWRTIPPDVIAKNRIK
ETDTIRCPVMAGGLFSIDKSYFFELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSR
VGHIFRNDNPYSFPKDRMKTVERNLVRVAEVWLDEYKELFYGHGDHLIDQGLDVGNLTQQ
RELRKKLKCKSFKWYLENVFPDLRAPIVRASGVLINVALGKCISIENTTVILEDCDGSKE
LQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGLKWLHKSTSVFHPELVNHIVF
ENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKFEKYYEA
Enzyme 103 Number of Residues 940
Enzyme 103 Molecular Weight 106265.3
Enzyme 103 Theoretical pI 10.07
Enzyme 103 GO Classification Not Available
Enzyme 103 General Function Involved in polypeptide N-acetylgalactosaminyltransfera
Enzyme 103 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward EA2 peptide substrate, but has a weak activity toward Muc2 or Muc1b substrates
Enzyme 103 Pathways
Enzyme 103 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 103 Pfam Domain Function
Enzyme 103 Signals
  • None
Enzyme 103 Transmembrane Regions
  • 13-35
Enzyme 103 Essentiality Not Available
Enzyme 103 GenBank ID Protein 32698686 Link Image
Enzyme 103 UniProtKB/Swiss-Prot ID Q7Z7M9 Link Image
Enzyme 103 UniProtKB/Swiss-Prot Entry Name GALT5_HUMAN Link Image
Enzyme 103 PDB ID Not Available
Enzyme 103 Cellular Location Not Available
Enzyme 103 Gene Sequence >2823 bp 
ATGAACAGGATCCGAAAGTTTTTCCGAGGAAGTGGGCGAGTCTTGGCATTTATCTTTGTA
GCTTCTGTCATCTGGCTCCTCTTTGACATGGCAGCTCTCCGCCTCTCATTCAGTGAGATC
AACACTCGGGTCATCAAGGAAGACATTGTGAGGAGGGAGCGGATAGGATTCAGAGTTCAG
CCAGACCAAGGAAAAATTTTTTACAGCAGCATAAAAGAGATGAAACCTCCCCTAAGGGGA
CATGGGAAAGGGGCATGGGGCAAAGAGAATGTTAGAAAAACTGAGGAGAGTGTGCTCAAG
GTTGAGGTGGACTTGGACCAAACCCAGAGGGAAAGAAAAATGCAGAATGCCCTGGGAAGG
GGCAAGGTTGTGCCGTTGTGGCATCCTGCACATCTGCAGACCCTCCCTGTGACTCCTAAC
AAGCAGAAGACAGACGGGAGAGGCACCAAACCTGAAGCCTCCTCTCACCAGGGGACACCA
AAGCAAACGACAGCTCAGGGGGCTCCAAAGACCTCATTCATAGCAGCAAAAGGAACTCAG
GTAGTCAAAATATCAGTACACATGGGACGTGTCAGTTTAAAACAGGAGCCCCGGAAGAGT
CATAGTCCCAGCAGTGACACATCAAAACTAGCAGCTGAAAGGGACTTGAATGTGACCATC
AGTCTTAGTACTGATAGACCAAAGCAGCGATCACAGGCAGTAGCAAACGAGAGGGCACAC
CCTGCCAGCACAGCAGTGCCGAAGTCTGGGGAAGCCATGGCCTTAAACAAAACTAAGACT
CAGAGCAAAGAAGTCAATGCAAATAAACACAAAGCCAATACGAGTCTTCCTTTTCCTAAG
TTCACTGTCAATTCAAATCGCTTAAGGAAGCAATCTATTAATGAGACACCTTTGGGAAGT
TTGTCAAAGGATGATGGAGCTAGAGGGGCTCATGGGAAGAAACTCAATTTCTCTGAAAGC
CATCTTGTGATTATAACCAAAGAGGAAGAGCAAAAGGCAGACCCCAAAGAGGTCTCTAAT
TCTAAAACCAAAACAATATTTCCTAAAGTATTGGGTAAAAGCCAAAGTAAACACATTTCC
AGGAATAGAAGTGAGATGTCTTCCTCTTCACTTGCTCCACATAGAGTGCCACTGTCCCAA
ACTAACCATGCTTTAACTGGAGGGCTAGAGCCAGCAAAAATCAACATAACTGCCAAAGCC
CCCTCTACAGAATACAACCAGAGTCATATAAAAGCCCTTTTACCTGAAGACAGTGGAACG
CACCAGGTGTTAAGAATTGATGTGACACTTTCTCCAAGGGACCCCAAAGCTCCAGGGCAG
TTTGGGCGTCCTGTAGTTGTCCCCCATGGAAAGGAGAAGGAGGCAGAAAGAAGATGGAAA
GAAGGAAACTTCAATGTCTACCTTAGCGATTTGATCCCAGTGGATAGAGCCATTGAAGAC
ACCAGACCTGCTGGATGTGCAGAGCAGCTAGTTCACAATAACCTCCCAACCACCAGTGTC
ATCATGTGCTTTGTGGATGAAGTGTGGTCCACTCTCCTGAGATCTGTTCACAGTGTCATC
AATCGCTCTCCTCCACACCTCATCAAGGAGATTCTGCTGGTAGATGACTTCAGCACCAAA
GACTATCTAAAAGATAATTTGGATAAATACATGTCCCAGTTTCCAAAAGTTCGGATTCTT
CGCCTCAAAGAGAGACATGGCTTAATAAGGGCCAGGCTGGCAGGAGCACAGAATGCAACA
GGTGATGTGTTGACATTTTTAGATTCTCATGTGGAATGTAACGTTGGTTGGTTGGAACCT
CTTCTGGAAAGAGTTTATTTAAGTAGAAAGAAAGTGGCCTGTCCAGTAATCGAAGTCATC
AATGATAAGGATATGAGTTACATGACAGTGGATAACTTTCAAAGAGGCATCTTTGTGTGG
CCCATGAACTTTGGTTGGAGAACAATTCCTCCAGATGTCATTGCAAAAAACAGAATTAAA
GAAACTGATACAATAAGGTGCCCTGTCATGGCTGGTGGATTGTTTTCTATTGACAAAAGT
TACTTTTTTGAACTTGGAACATACGACCCTGGCCTTGATGTTTGGGGTGGGGAAAATATG
GAGCTCTCATTCAAGGTGTGGATGTGTGGTGGTGAAATTGAGATCATTCCCTGCTCCCGA
GTGGGCCATATATTCAGAAATGACAATCCATATTCCTTCCCCAAAGACCGGATGAAGACA
GTGGAGCGGAACTTGGTGCGGGTTGCCGAGGTCTGGCTGGATGAGTATAAGGAGCTGTTC
TATGGCCACGGAGACCACCTCATCGACCAAGGGCTAGATGTTGGCAACCTCACCCAGCAA
AGGGAGCTGCGAAAGAAACTGAAGTGCAAAAGTTTCAAATGGTACTTGGAGAATGTCTTT
CCTGACTTAAGGGCTCCCATTGTGAGAGCTAGTGGTGTGCTTATTAATGTGGCTTTGGGT
AAATGCATTTCCATTGAAAACACTACAGTCATTCTGGAAGACTGCGATGGGAGCAAAGAG
CTTCAACAATTTAATTACACCTGGTTAAGACTTATTAAATGTGGAGAATGGTGTATAGCC
CCCATCCCTGATAAAGGAGCCGTAAGGCTGCACCCTTGTGATAACAGAAACAAAGGGCTA
AAATGGCTGCATAAATCAACATCAGTCTTTCATCCAGAACTGGTGAATCACATTGTTTTT
GAAAACAATCAGCAATTATTATGCTTGGAAGGAAATTTTTCTCAAAAGATCCTGAAAGTA
GCTGCCTGTGACCCAGTGAAGCCATATCAAAAGTGGAAATTTGAAAAATATTATGAAGCC
TGA
Enzyme 103 GenBank Gene ID NM_014568.1 Link Image
Enzyme 103 GeneCard ID GALNT5 Link Image
Enzyme 103 GenAtlas ID GALNT5 Link Image
Enzyme 103 HGNC ID HGNC:4127 Link Image
Enzyme 103 Chromosome Location 2
Enzyme 103 Locus 2q24.1
Enzyme 103 SNPs SNPJam Report Link Image
Enzyme 103 General References
  1. Simmons AD, Musy MM, Lopes CS, Hwang LY, Yang YP, Lovett M: A direct interaction between EXT proteins and glycosyltransferases is defective in hereditary multiple exostoses. Hum Mol Genet. 1999 Nov;8(12):2155-64. [PubMed Link Image]
  2. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 103 Metabolite References Not Available
Enzyme 104 [top]
Enzyme 104 ID 6331
Enzyme 104 Name 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
Enzyme 104 Synonyms
  1. 25-OHD-1 alpha-hydroxylase
  2. 25-hydroxyvitamin D(3) 1-alpha-hydroxylase
  3. VD3 1A hydroxylase
  4. Calcidiol 1-monooxygenase
  5. Cytochrome P450 subfamily XXVIIB polypeptide 1
  6. Cytochrome P450C1 alpha
  7. Cytochrome P450VD1-alpha
  8. Cytochrome p450 27B1
Enzyme 104 Gene Name CYP27B1
Enzyme 104 Protein Sequence >25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial 
MTQTLKYASRVFHRVRWAPELGASLGYREYHSARRSLADIPGPSTPSFLAELFCKGGLSR
LHELQVQGAAHFGPVWLASFGTVRTVYVAAPALVEELLRQEGPRPERCSFSPWTEHRRCR
QRACGLLTAEGEEWQRLRSLLAPLLLRPQAAARYAGTLNNVVCDLVRRLRRQRGRGTGPP
ALVRDVAGEFYKFGLEGIAAVLLGSRLGCLEAQVPPDTETFIRAVGSVFVSTLLTMAMPH
WLRHLVPGPWGRLCRDWDQMFAFAQRHVERREAEAAMRNGGQPEKDLESGAHLTHFLFRE
ELPAQSILGNVTELLLAGVDTVSNTLSWALYELSRHPEVQTALHSEITAALSPGSSAYPS
ATVLSQLPLLKAVVKEVLRLYPVVPGNSRVPDKDIHVGDYIIPKNTLVTLCHYATSRDPA
QFPEPNSFRPARWLGEGPTPHPFASLPFGFGKRSCMGRRLAELELQMALAQILTHFEVQP
EPGAAPVRPKTRTVLVPERSINLQFLDR
Enzyme 104 Number of Residues 508
Enzyme 104 Molecular Weight 56503.5
Enzyme 104 Theoretical pI 9.39
Enzyme 104 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
—
Enzyme 104 General Function Involved in monooxygenase activity
Enzyme 104 Specific Function Catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D) plays an important role in normal bone growth, calcium metabolism, and tissue differentiation
Enzyme 104 Pathways
Enzyme 104 Reactions
  • calcidiol + NADPH + H+ + O2 = calcitriol + NADP+ + H2O [RN:R03610]
Enzyme 104 Pfam Domain Function
Enzyme 104 Signals
  • None
Enzyme 104 Transmembrane Regions
  • None
Enzyme 104 Essentiality Not Available
Enzyme 104 GenBank ID Protein Not Available
Enzyme 104 UniProtKB/Swiss-Prot ID O15528 Link Image
Enzyme 104 UniProtKB/Swiss-Prot Entry Name CP27B_HUMAN Link Image
Enzyme 104 PDB ID Not Available
Enzyme 104 Cellular Location Not Available
Enzyme 104 Gene Sequence >1527 bp 
ATGACCCAGACCCTCAAGTACGCCTCCAGAGTGTTCCATCGCGTCCGCTGGGCGCCCGAG
TTGGGCGCCTCCCTAGGCTACCGAGAGTACCACTCAGCACGCCGGAGCTTGGCAGACATC
CCAGGCCCCTCTACGCCCAGCTTTCTGGCCGAACTTTTCTGCAAGGGGGGGCTGTCGAGG
CTACACGAGCTGCAGGTGCAGGGCGCCGCGCACTTCGGGCCGGTGTGGCTAGCCAGCTTT
GGGACAGTGCGCACCGTGTACGTGGCTGCCCCTGCACTCGTCGAGGAGCTGCTGCGACAG
GAGGGACCCCGGCCCGAGCGCTGCAGCTTCTCGCCCTGGACGGAGCACCGCCGCTGCCGC
CAGCGGGCTTGCGGACTGCTCACTGCGGAAGGCGAAGAATGGCAAAGGCTCCGCAGTCTC
CTGGCCCCGCTCCTCCTCCGGCCTCAAGCGGCCGCCCGCTACGCCGGAACCCTGAACAAC
GTAGTCTGCGACCTTGTGCGGCGTCTGAGGCGCCAGCGGGGACGTGGCACGGGGCCGCCC
GCCCTGGTTCGGGACGTGGCGGGGGAATTTTACAAGTTCGGACTGGAAGGCATCGCCGCG
GTTCTGCTCGGCTCGCGCTTGGGCTGCCTGGAGGCTCAAGTGCCACCCGACACGGAGACC
TTCATCCGCGCTGTGGGCTCGGTGTTTGTGTCCACGCTGTTGACCATGGCGATGCCCCAC
TGGCTGCGCCACCTTGTGCCTGGGCCCTGGGGCCGCCTCTGCCGAGACTGGGACCAGATG
TTTGCATTTGCTCAGAGGCACGTGGAGCGGCGAGAGGCAGAGGCAGCCATGAGGAACGGA
GGACAGCCCGAGAAGGACCTGGAGTCTGGGGCGCACCTGACCCACTTCCTGTTCCGGGAA
GAGTTGCCTGCCCAGTCCATCCTGGGAAATGTGACAGAGTTGCTATTGGCGGGAGTGGAC
ACGGTGTCCAACACGCTCTCTTGGGCTCTGTATGAGCTCTCCCGGCACCCCGAAGTCCAG
ACAGCACTCCACTCAGAGATCACAGCTGCCCTGAGCCCTGGCTCCAGTGCCTACCCCTCA
GCCACTGTTCTGTCCCAGCTGCCCCTGCTGAAGGCGGTGGTCAAGGAAGTGCTAAGACTG
TACCCTGTGGTACCTGGAAATTCTCGTGTCCCAGACAAAGACATTCATGTGGGTGACTAT
ATTATCCCCAAAAATACGCTGGTCACTCTGTGTCACTATGCCACTTCAAGGGACCCTGCC
CAGTTCCCAGAGCCAAATTCTTTTCGTCCAGCTCGCTGGCTGGGGGAGGGTCCCACCCCC
CACCCATTTGCATCTCTTCCCTTTGGCTTTGGCAAGCGCAGCTGTATGGGGAGACGCCTG
GCAGAGCTTGAATTGCAAATGGCTTTGGCCCAGATCCTAACACATTTTGAGGTGCAGCCT
GAGCCAGGTGCGGCCCCAGTTAGACCCAAGACCCGGACTGTCCTGGTACCTGAAAGGAGC
ATCAACCTACAGTTTTTGGACAGATAG
Enzyme 104 GenBank Gene ID AB005038 Link Image
Enzyme 104 GeneCard ID CYP27B1 Link Image
Enzyme 104 GenAtlas ID CYP27B1 Link Image
Enzyme 104 HGNC ID HGNC:2606 Link Image
Enzyme 104 Chromosome Location 1
Enzyme 104 Locus 12q13.1-q13.3
Enzyme 104 SNPs SNPJam Report Link Image
Enzyme 104 General References
  1. Fu GK, Portale AA, Miller WL: Complete structure of the human gene for the vitamin D 1alpha-hydroxylase, P450c1alpha. DNA Cell Biol. 1997 Dec;16(12):1499-507. [PubMed Link Image]
  2. Monkawa T, Yoshida T, Wakino S, Shinki T, Anazawa H, Deluca HF, Suda T, Hayashi M, Saruta T: Molecular cloning of cDNA and genomic DNA for human 25-hydroxyvitamin D3 1 alpha-hydroxylase. Biochem Biophys Res Commun. 1997 Oct 20;239(2):527-33. [PubMed Link Image]
  3. Fu GK, Lin D, Zhang MY, Bikle DD, Shackleton CH, Miller WL, Portale AA: Cloning of human 25-hydroxyvitamin D-1 alpha-hydroxylase and mutations causing vitamin D-dependent rickets type 1. Mol Endocrinol. 1997 Dec;11(13):1961-70. [PubMed Link Image]
  4. Kitanaka S, Takeyama K, Murayama A, Sato T, Okumura K, Nogami M, Hasegawa Y, Niimi H, Yanagisawa J, Tanaka T, Kato S: Inactivating mutations in the 25-hydroxyvitamin D3 1alpha-hydroxylase gene in patients with pseudovitamin D-deficiency rickets. N Engl J Med. 1998 Mar 5;338(10):653-61. [PubMed Link Image]
  5. Wang JT, Lin CJ, Burridge SM, Fu GK, Labuda M, Portale AA, Miller WL: Genetics of vitamin D 1alpha-hydroxylase deficiency in 17 families. Am J Hum Genet. 1998 Dec;63(6):1694-702. [PubMed Link Image]
  6. Smith SJ, Rucka AK, Berry JL, Davies M, Mylchreest S, Paterson CR, Heath DA, Tassabehji M, Read AP, Mee AP, Mawer EB: Novel mutations in the 1alpha-hydroxylase (P450c1) gene in three families with pseudovitamin D-deficiency rickets resulting in loss of functional enzyme activity in blood-derived macrophages. J Bone Miner Res. 1999 May;14(5):730-9. [PubMed Link Image]
  7. Kitanaka S, Murayama A, Sakaki T, Inouye K, Seino Y, Fukumoto S, Shima M, Yukizane S, Takayanagi M, Niimi H, Takeyama K, Kato S: No enzyme activity of 25-hydroxyvitamin D3 1alpha-hydroxylase gene product in pseudovitamin D deficiency rickets, including that with mild clinical manifestation. J Clin Endocrinol Metab. 1999 Nov;84(11):4111-7. [PubMed Link Image]
  8. Wang X, Zhang MY, Miller WL, Portale AA: Novel gene mutations in patients with 1alpha-hydroxylase deficiency that confer partial enzyme activity in vitro. J Clin Endocrinol Metab. 2002 Jun;87(6):2424-30. [PubMed Link Image]
Enzyme 104 Metabolite References Not Available
Enzyme 105 [top]
Enzyme 105 ID 6356
Enzyme 105 Name Retinal guanylyl cyclase 1
Enzyme 105 Synonyms
  1. RETGC-1
  2. Guanylate cyclase 2D, retinal
  3. Rod outer segment membrane guanylate cyclase
  4. ROS-GC
Enzyme 105 Gene Name GUCY2D
Enzyme 105 Protein Sequence >Retinal guanylyl cyclase 1 
MTACARRAGGLPDPGLCGPAWWAPSLPRLPRALPRLPLLLLLLLLQPPALSAVFTVGVLG
PWACDPIFSRARPDLAARLAAARLNRDPGLAGGPRFEVALLPEPCRTPGSLGAVSSALAR
VSGLVGPVNPAACRPAELLAEEAGIALVPWGCPWTQAEGTTAPAVTPAADALYALLRAFG
WARVALVTAPQDLWVEAGRSLSTALRARGLPVASVTSMEPLDLSGAREALRKVRDGPRVT
AVIMVMHSVLLGGEEQRYLLEAAEELGLTDGSLVFLPFDTIHYALSPGPEALAALANSSQ
LRRAHDAVLTLTRHCPSEGSVLDSLRRAQERRELPSDLNLQQVSPLFGTIYDAVFLLARG
VAEARAAAGGRWVSGAAVARHIRDAQVPGFCGDLGGDEEPPFVLLDTDAAGDRLFATYML
DPARGSFLSAGTRMHFPRGGSAPGPDPSCWFDPNNICGGGLEPGLVFLGFLLVVGMGLAG
AFLAHYVRHRLLHMQMVSGPNKIILTVDDITFLHPHGGTSRKVAQGSRSSLGARSMSDIR
SGPSQHLDSPNIGVYEGDRVWLKKFPGDQHIAIRPATKTAFSKLQELRHENVALYLGLFL
ARGAEGPAALWEGNLAVVSEHCTRGSLQDLLAQREIKLDWMFKSSLLLDLIKGIRYLHHR
GVAHGRLKSRNCIVDGRFVLKITDHGHGRLLEAQKVLPEPPRAEDQLWTAPELLRDPALE
RRGTLAGDVFSLAIIMQEVVCRSAPYAMLELTPEEVVQRVRSPPPLCRPLVSMDQAPVEC
ILLMKQCWAEQPELRPSMDHTFDLFKNINKGRKTNIIDSMLRMLEQYSSNLEDLIRERTE
ELELEKQKTDRLLTQMLPPSVAEALKTGTPVEPEYFEQVTLYFSDIVGFTTISAMSEPIE
VVDLLNDLYTLFDAIIGSHDVYKVETIGDAYMVASGLPQRNGQRHAAEIANMSLDILSAV
GTFRMRHMPEVPVRIRIGLHSGPCVAGVVGLTMPRYCLFGDTVNTASRMESTGLPYRIHV
NLSTVGILRALDSGYQVELRGRTELKGKGAEDTFWLVGRRGFNKPIPKPPDLQPGSSNHG
ISLQEIPPERRRKLEKARPGQFS
Enzyme 105 Number of Residues 1103
Enzyme 105 Molecular Weight 120057.2
Enzyme 105 Theoretical pI 7.47
Enzyme 105 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cyclase activity
  • guanylate cyclase activity
  • kinase activity
  • lyase activity
  • nucleoside binding
  • phosphorus-oxygen lyase activity
  • protein kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cGMP biosynthetic process
  • cellular metabolic process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • signaling
  • signaling pathway
Component
—
Enzyme 105 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 105 Specific Function Probably plays a specific functional role in the rods and/or cones of photoreceptors. It may be the enzyme involved in the resynthesis of cGMP required for recovery of the dark state after phototransduction
Enzyme 105 Pathways
Enzyme 105 Reactions
  • GTP = 3',5'-cyclic GMP + diphosphate [RN:R00434]
Enzyme 105 Pfam Domain Function
Enzyme 105 Signals
  • 1-51
Enzyme 105 Transmembrane Regions
  • 463-487
Enzyme 105 Essentiality Not Available
Enzyme 105 GenBank ID Protein 2695890 Link Image
Enzyme 105 UniProtKB/Swiss-Prot ID Q02846 Link Image
Enzyme 105 UniProtKB/Swiss-Prot Entry Name GUC2D_HUMAN Link Image
Enzyme 105 PDB ID Not Available
Enzyme 105 Cellular Location Not Available
Enzyme 105 Gene Sequence >3312 bp 
ATGACCGCCTGCGCCCGCCGAGCGGGTGGGCTTCCGGACCCCGGGCTCTGCGGTCCCGCG
TGGTGGGCTCCGTCCCTGCCCCGCCTCCCCCGGGCCCTGCCCCGGCTCCCGCTCCTGCTG
CTCCTGCTTCTGCTGCAGCCCCCCGCCCTCTCCGCCGTGTTCACGGTGGGGGTCCTGGGC
CCCTGGGCTTGCGACCCCATCTTCTCTCGGGCTCGCCCGGACCTGGCCGCCCGCCTGGCC
GCCGCCCGCCTGAACCGCGACCCCGGCCTGGCAGGCGGTCCCCGCTTCGAGGTAGCGCTG
CTGCCCGAGCCTTGCCGGACGCCGGGCTCGCTGGGGGCCGTGTCCTCCGCGCTGGCCCGC
GTGTCGGGCCTCGTGGGTCCGGTGAACCCTGCGGCCTGCCGGCCAGCCGAGCTGCTCGCC
GAAGAAGCCGGGATCGCGCTGGTGCCCTGGGGCTGCCCCTGGACGCAGGCGGAGGGCACC
ACGGCCCCTGCCGTGACCCCCGCCGCGGATGCCCTCTACGCCCTGCTTCGCGCATTCGGC
TGGGCGCGCGTGGCCCTGGTCACCGCCCCCCAGGACCTGTGGGTGGAGGCGGGACGCTCA
CTGTCCACGGCACTCAGGGCCCGGGGCCTGCCTGTCGCCTCCGTGACTTCCATGGAGCCC
TTGGACCTGTCTGGAGCCCGGGAGGCCCTGAGGAAGGTTCGGGACGGGCCCAGGGTCACA
GCAGTGATCATGGTGATGCACTCGGTGCTGCTGGGTGGCGAGGAGCAGCGCTACCTCCTG
GAGGCCGCAGAGGAGCTGGGCCTGACCGATGGCTCCCTGGTCTTCCTGCCCTTCGACACG
ATCCACTACGCCTTGTCCCCAGGCCCGGAGGCCTTGGCCGCACTCGCCAACAGCTCCCAG
CTTCGCAGGGCCCACGATGCCGTGCTCACCCTCACGCGCCACTGTCCCTCTGAAGGCAGC
GTGCTGGACAGCCTGCGCAGGGCTCAAGAGCGCCGCGAGCTGCCCTCTGACCTCAATCTG
CAGCAGGTCTCCCCACTCTTTGGCACCATCTATGACGCGGTCTTCTTGCTGGCAAGGGGC
GTGGCAGAAGCGCGGGCTGCCGCAGGTGGCAGATGGGTGTCCGGAGCAGCTGTGGCCCGC
CACATCCGGGATGCGCAGGTCCCTGGCTTCTGCGGGGACCTAGGAGGAGACGAGGAGCCC
CCATTCGTGCTGCTAGACACGGACGCGGCGGGAGACCGGCTTTTTGCCACATACATGCTG
GATCCTGCCCGGGGCTCCTTCCTCTCCGCCGGTACCCGGATGCACTTCCCGCGTGGGGGA
TCAGCACCCGGACCTGACCCCTCGTGCTGGTTCGATCCAAACAACATCTGCGGTGGAGGA
CTGGAGCCGGGCCTCGTCTTTCTTGGCTTCCTCCTGGTGGTTGGGATGGGGCTGGCTGGG
GCCTTCCTGGCCCATTATGTGAGGCACCGGCTACTTCACATGCAAATGGTCTCCGGCCCC
AACAAGATCATCCTGACCGTGGACGACATCACCTTTCTCCACCCACATGGGGGCACCTCT
CGAAAGGTGGCCCAGGGGAGTCGATCAAGTCTGGGTGCCCGCAGCATGTCAGACATTCGC
AGCGGCCCCAGCCAACACTTGGACAGCCCCAACATTGGTGTCTATGAGGGAGACAGGGTT
TGGCTGAAGAAATTCCCAGGGGATCAGCACATAGCTATCCGCCCAGCAACCAAGACGGCC
TTCTCCAAGCTCCAGGAGCTCCGGCATGAGAACGTGGCCCTCTACCTGGGGCTTTTCCTG
GCTCGGGGAGCAGAAGGCCCTGCGGCCCTCTGGGAGGGCAACCTGGCTGTGGTCTCAGAG
CACTGCACGCGGGGCTCTCTTCAGGACCTCCTCGCTCAGAGAGAAATAAAGCTGGACTGG
ATGTTCAAGTCCTCCCTCCTGCTGGACCTTATCAAGGGAATAAGGTATCTGCACCATCGA
GGCGTGGCTCATGGGCGGCTGAAGTCACGGAACTGCATAGTGGATGGCAGATTCGTACTC
AAGATCACTGACCACGGCCACGGGAGACTGCTGGAAGCACAGAAGGTGCTACCGGAGCCT
CCCAGAGCGGAGGACCAGCTGTGGACAGCCCCGGAGCTGCTTAGGGACCCAGCCCTGGAG
CGCCGGGGAACGCTGGCCGGCGACGTCTTTAGCTTGGCCATCATCATGCAAGAAGTAGTG
TGCCGCAGTGCCCCTTATGCCATGCTGGAGCTCACTCCCGAGGAAGTGGTGCAGAGGGTG
CGGAGCCCCCCTCCACTGTGTCGGCCCTTGGTGTCCATGGACCAGGCACCTGTCGAGTGT
ATCCTCCTGATGAAGCAGTGCTGGGCAGAGCAGCCGGAACTTCGGCCCTCCATGGACCAC
ACCTTCGACCTGTTCAAGAACATCAACAAGGGCCGGAAGACGAACATCATTGACTCGATG
CTTCGGATGCTGGAGCAGTACTCTAGTAACCTGGAGGATCTGATCCGGGAGCGCACGGAG
GAGCTGGAGCTGGAAAAGCAGAAGACAGACCGGCTGCTTACACAGATGCTGCCTCCGTCT
GTGGCTGAGGCCTTGAAGACGGGGACACCAGTGGAGCCCGAGTACTTTGAGCAAGTGACA
CTGTACTTTAGTGACATTGTGGGCTTCACCACCATCTCTGCCATGAGTGAGCCCATTGAG
GTTGTGGACCTGCTCAACGATCTCTACACACTCTTTGATGCCATCATTGGTTCCCACGAT
GTCTACAAGGTGGAGACAATAGGGGACGCCTATATGGTGGCCTCGGGGCTGCCCCAGCGG
AATGGGCAGCGACACGCGGCAGAGATCGCCAACATGTCACTGGACATCCTCAGTGCCGTG
GGCACTTTCCGCATGCGCCATATGCCTGAGGTTCCCGTGCGCATCCGCATAGGCCTGCAC
TCGGGTCCATGCGTGGCAGGCGTGGTGGGCCTCACCATGCCGCGGTACTGCCTGTTTGGG
GACACGGTCAACACCGCCTCGCGCATGGAGTCCACCGGGCTGCCTTACCGCATCCACGTG
AACTTGAGCACTGTGGGGATTCTCCGTGCTCTGGACTCGGGCTACCAGGTGGAGCTGCGA
GGCCGCACGGAGCTGAAGGGCAAGGGCGCCGAGGACACTTTCTGGCTAGTGGGCAGACGC
GGCTTCAACAAGCCCATCCCCAAACCGCCTGACCTGCAACCGGGGTCCAGCAACCACGGC
ATCAGCCTGCAGGAGATCCCACCCGAGCGGCGACGGAAGCTGGAGAAGGCGCGGCCGGGC
CAGTTCTCTTGA
Enzyme 105 GenBank Gene ID AJ222657 Link Image
Enzyme 105 GeneCard ID GUCY2D Link Image
Enzyme 105 GenAtlas ID GUCY2D Link Image
Enzyme 105 HGNC ID HGNC:4689 Link Image
Enzyme 105 Chromosome Location 1
Enzyme 105 Locus 17p13.1
Enzyme 105 SNPs SNPJam Report Link Image
Enzyme 105 General References
  1. Shyjan AW, de Sauvage FJ, Gillett NA, Goeddel DV, Lowe DG: Molecular cloning of a retina-specific membrane guanylyl cyclase. Neuron. 1992 Oct;9(4):727-37. [PubMed Link Image]
  2. Oliveira L, Miniou P, Viegas-Pequignot E, Rozet JM, Dollfus H, Pittler SJ: Human retinal guanylate cyclase (GUC2D) maps to chromosome 17p13.1. Genomics. 1994 Jul 15;22(2):478-81. [PubMed Link Image]
  3. Liu Y, Ruoho AE, Rao VD, Hurley JH: Catalytic mechanism of the adenylyl and guanylyl cyclases: modeling and mutational analysis. Proc Natl Acad Sci U S A. 1997 Dec 9;94(25):13414-9. [PubMed Link Image]
  4. Perrault I, Rozet JM, Calvas P, Gerber S, Camuzat A, Dollfus H, Chatelin S, Souied E, Ghazi I, Leowski C, Bonnemaison M, Le Paslier D, Frezal J, Dufier JL, Pittler S, Munnich A, Kaplan J: Retinal-specific guanylate cyclase gene mutations in Leber's congenital amaurosis. Nat Genet. 1996 Dec;14(4):461-4. [PubMed Link Image]
  5. Perrault I, Rozet JM, Gerber S, Kelsell RE, Souied E, Cabot A, Hunt DM, Munnich A, Kaplan J: A retGC-1 mutation in autosomal dominant cone-rod dystrophy. Am J Hum Genet. 1998 Aug;63(2):651-4. [PubMed Link Image]
  6. Kelsell RE, Gregory-Evans K, Payne AM, Perrault I, Kaplan J, Yang RB, Garbers DL, Bird AC, Moore AT, Hunt DM: Mutations in the retinal guanylate cyclase (RETGC-1) gene in dominant cone-rod dystrophy. Hum Mol Genet. 1998 Jul;7(7):1179-84. [PubMed Link Image]
  7. Duda T, Venkataraman V, Goraczniak R, Lange C, Koch KW, Sharma RK: Functional consequences of a rod outer segment membrane guanylate cyclase (ROS-GC1) gene mutation linked with Leber's congenital amaurosis. Biochemistry. 1999 Jan 12;38(2):509-15. [PubMed Link Image]
  8. Dharmaraj SR, Silva ER, Pina AL, Li YY, Yang JM, Carter CR, Loyer MK, El-Hilali HK, Traboulsi EK, Sundin OK, Zhu DK, Koenekoop RK, Maumenee IH: Mutational analysis and clinical correlation in Leber congenital amaurosis. Ophthalmic Genet. 2000 Sep;21(3):135-50. [PubMed Link Image]
  9. Koenekoop RK, Fishman GA, Iannaccone A, Ezzeldin H, Ciccarelli ML, Baldi A, Sunness JS, Lotery AJ, Jablonski MM, Pittler SJ, Maumenee I: Electroretinographic abnormalities in parents of patients with Leber congenital amaurosis who have heterozygous GUCY2D mutations. Arch Ophthalmol. 2002 Oct;120(10):1325-30. [PubMed Link Image]
  10. Udar N, Yelchits S, Chalukya M, Yellore V, Nusinowitz S, Silva-Garcia R, Vrabec T, Hussles Maumenee I, Donoso L, Small KW: Identification of GUCY2D gene mutations in CORD5 families and evidence of incomplete penetrance. Hum Mutat. 2003 Feb;21(2):170-1. [PubMed Link Image]
  11. Tucker CL, Ramamurthy V, Pina AL, Loyer M, Dharmaraj S, Li Y, Maumenee IH, Hurley JB, Koenekoop RK: Functional analyses of mutant recessive GUCY2D alleles identified in Leber congenital amaurosis patients: protein domain comparisons and dominant negative effects. Mol Vis. 2004 Apr 20;10:297-303. [PubMed Link Image]
  12. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 105 Metabolite References Not Available
Enzyme 106 [top]
Enzyme 106 ID 6365
Enzyme 106 Name Retinal guanylyl cyclase 2
Enzyme 106 Synonyms
  1. RETGC-2
  2. Guanylate cyclase 2F, retinal
  3. Guanylate cyclase F
  4. GC-F
  5. Rod outer segment membrane guanylate cyclase 2
  6. ROS-GC2
Enzyme 106 Gene Name GUCY2F
Enzyme 106 Protein Sequence >Retinal guanylyl cyclase 2 
MFLGLGRFSRLVLWFAAFRKLLGHHGLASAKFLWCLCLLSVMSLPQQVWTLPYKIGVVGP
WACDSLFSKALPEVAARLAIERINRDPSFDLSYSFEYVILNEDCQTSRALSSFISHHQMA
SGFIGPTNPGYCEAASLLGNSWDKGIFSWACVNYELDNKISYPTFSRTLPSPIRVLVTVM
KYFQWAHAGVISSDEDIWVHTANRVASALRSHGLPVGVVLTTGQDSQSMRKALQRIHQAD
RIRIIIMCMHSALIGGETQMHLLECAHDLKMTDGTYVFVPYDALLYSLPYKHTPYQVLRN
NPKLREAYDAVLTITVESQEKTFYQAFTEAAARGEIPEKLEFDQVSPLFGTIYNSIYFIA
QAMNNAMKENGQAGAASLVQHSRNMQFHGFNQLMRTDSNGNGISEYVILDTNLKEWELHS
TYTVDMEMELLRFGGTPIHFPGGRPPRADAKCWFAEGKICHGGIDPAFAMMVCLTLLIAL
LSINGFAYFIRRRINKIQLIKGPNRILLTLEDVTFINPHFGSKRGSRASVSFQITSEVQS
GRSPRLSFSSGSLTPATYENSNIAIYEGDWVWLKKFSLGDFGDLKSIKSRASDVFEMMKD
LRHENINPLLGFFYDSGMFAIVTEFCSRGSLEDILTNQDVKLDWMFKSSLLLDLIKGMKY
LHHREFVHGRLKSRNCVVDGRFVLKVTDYGFNDILEMLRLSEEESSMEELLWTAPELLRA
PRGSRLGSFAGDVYSFAIIMQEVMVRGTPFCMMDLPAQEIINRLKKPPPVYRPVVPPEHA
PPECLQLMKQCWAEAAEQRPTFDEIFNQFKTFNKGKKTNIIDSMLRMLEQYSSNLEDLIR
ERTEELEIEKQKTEKLLTQMLPPSVAESLKKGCTVEPEGFDLVTLYFSDIVGFTTISAMS
EPIEVVDLLNDLYTLFDAIIGSHDVYKVETIGDAYMVASGLPKRNGSRHAAEIANMSLDI
LSSVGTFKMRHMPEVPVRIRIGLHSGPVVAGVVGLTMPRYCLFGDTVNTASRMESTGLPY
RIHVSLSTVTILQNLSEGYEVELRGRTELKGKGTEETFWLIGKKGFMKPLPVPPPVDKDG
QVGHGLQPVEIAAFQRRKAERQLVRNKP
Enzyme 106 Number of Residues 1108
Enzyme 106 Molecular Weight 124820.9
Enzyme 106 Theoretical pI 7.20
Enzyme 106 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cyclase activity
  • guanylate cyclase activity
  • kinase activity
  • lyase activity
  • nucleoside binding
  • phosphorus-oxygen lyase activity
  • protein kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cGMP biosynthetic process
  • cellular metabolic process
  • cellular nitrogen compound metabolic process
  • cyclic nucleotide biosynthetic process
  • intracellular signaling pathway
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside monophosphate biosynthetic process
  • nucleoside monophosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • signaling
  • signaling pathway
Component
—
Enzyme 106 General Function Involved in phosphorus-oxygen lyase activity
Enzyme 106 Specific Function Probably plays a specific functional role in the rods and/or cones of photoreceptors. It may be the enzyme involved in the resynthesis of cGMP required for recovery of the dark state after phototransduction
Enzyme 106 Pathways
Enzyme 106 Reactions
  • GTP = 3',5'-cyclic GMP + diphosphate [RN:R00434]
Enzyme 106 Pfam Domain Function
Enzyme 106 Signals
  • 1-50
Enzyme 106 Transmembrane Regions
  • 468-490
Enzyme 106 Essentiality Not Available
Enzyme 106 GenBank ID Protein 4680397 Link Image
Enzyme 106 UniProtKB/Swiss-Prot ID P51841 Link Image
Enzyme 106 UniProtKB/Swiss-Prot Entry Name GUC2F_HUMAN Link Image
Enzyme 106 PDB ID Not Available
Enzyme 106 Cellular Location Not Available
Enzyme 106 Gene Sequence >3327 bp 
ATGTTCCTGGGACTCGGGCGCTTTTCTCGCCTTGTTCTCTGGTTTGCGGCTTTCAGGAAA
CTGCTGGGACACCATGGCCTTGCATCTGCCAAGTTCCTGTGGTGCTTGTGCCTTCTGTCT
GTCATGTCCCTTCCGCAGCAGGTGTGGACACTCCCCTACAAGATAGGGGTGGTGGGCCCT
TGGGCTTGTGATTCGCTGTTTTCAAAGGCCCTGCCTGAGGTTGCTGCGCGATTAGCCATT
GAGCGAATCAACCGGGACCCATCTTTTGACCTGAGTTATTCTTTTGAATACGTGATTCTC
AATGAAGACTGCCAGACTTCGAGGGCTCTCTCCAGTTTCATTTCCCACCACCAGATGGCC
TCAGGATTTATTGGACCTACCAACCCTGGCTACTGCGAGGCAGCCTCGCTCCTGGGAAAC
AGCTGGGACAAAGGAATTTTCTCTTGGGCTTGTGTGAATTATGAATTAGACAATAAAATT
AGCTACCCGACCTTTTCTCGGACACTCCCTTCTCCCATCCGGGTGCTTGTAACTGTCATG
AAATATTTCCAGTGGGCTCATGCTGGAGTCATTTCCTCAGATGAAGACATTTGGGTGCAT
ACAGCCAATCGAGTCGCAAGTGCTCTTCGGAGCCACGGCTTACCTGTAGGGGTCGTCCTG
ACCACAGGACAAGACAGCCAAAGCATGCGGAAAGCCCTCCAGAGGATTCACCAGGCAGAC
AGAATTCGCATAATCATCATGTGTATGCATTCAGCTTTGATTGGGGGAGAGACTCAGATG
CATCTCTTGGAATGTGCTCATGATCTGAAAATGACTGATGGAACCTACGTCTTTGTTCCT
TATGATGCCCTGCTCTACAGTTTACCTTATAAGCACACCCCCTACCGGGTCCTAAGGAAC
AACCCAAAGCTCCGGGAAGCCTATGATGCAGTGTTGACCATTACAGTGGAGTCCCAAGAA
AAGACCTTCTATCAAGCCTTCACAGAGGCAGCAGCAAGAGGTGAAATTCCTGAGAAGCTG
GAGTTCGATCAAGTTTCACCGTTGTTTGGAACCATCTACAATTCAATTTACTTTATCGCA
CAAGCCATGAATAATGCTATGAAAGAAAATGGACAGGCTGGTGCTGCCAGCCTGGTTCAG
CATTCCAGAAACATGCAGTTCCATGGATTCAACCAGTTGATGAGGACAGATTCAAATGGA
AATGGAATTTCAGAATATGTAATCCTGGACACCAACTTGAAAGAATGGGAACTCCATAGC
ACCTACACTGTGGACATGGAAATGGAGCTGCTACGTTTCGGAGGGACCCCTATTCACTTC
CCTGGTGGCAGGCCCCCTAGAGCAGATGCAAAATGCTGGTTTGCAGAAGGGAAGATCTGC
CATGGAGGCATCGACCCTGCCTTTGCCATGATGGTCTGCCTTACTTTGCTTATAGCCCTG
CTGTCTATTAATGGATTTGCTTACTTTATAAGGCGTCGTATAAATAAAATCCAGTTGATC
AAAGGACCCAATAGAATTCTACTGACTTTGGAGGATGTAACGTTTATCAATCCCCACTTT
GGCAGTAAGAGAGGAAGTCGTGCCAGTGTAAGCTTCCAGATTACCTCAGAGGTCCAAAGT
GGGAGGTCCCCAAGACTCTCCTTTTCTTCAGGGAGTCTAACTCCAGCTACCTATGAAAAC
TCCAACATAGCGATTTATGAGGGTGATTGGGTGTGGCTGAAAAAGTTCTCCCTTGGAGAT
TTTGGAGACCTTAAGTCCATCAAATCAAGAGCAAGTGATGTGTTCGAAATGATGAAGGAC
TTGCGTCATGAGAATATTAACCCTTTATTGGGTTTCTTCTATGATTCGGGGATGTTTGCC
ATTGTGACAGAATTCTGTTCCCGAGGGAGCCTAGAAGACATACTGACAAATCAAGATGTG
AAACTTGACTGGATGTTTAAATCATCACTCTTGCTGGATCTCATAAAGGGCATGAAGTAC
TTACACCACAGAGAGTTTGTTCATGGGAGGCTAAAGTCTCGAAACTGTGTGGTAGATGGG
CGTTTTGTACTAAAAGTGACAGATTATGGCTTTAACGACATCTTAGAAATGCTGAGACTC
TCTGAAGAGGAATCTTCTATGGAAGAGCTGCTGTGGACGGCCCCTGAACTGTTGAGAGCT
CCAAGAGGCAGCAGGTTAGGTTCTTTTGCAGGAGATGTCTATAGCTTTGCCATCATCATG
CAAGAAGTGATGGTCCGGGGTACCCCATTCTGCATGATGGATCTGCCAGCTCAAGAAATC
ATAAACAGACTTAAGAAGCCTCCTCCTGTGTACAGACCAGTAGTTCCTCCTGAGCATGCC
CCTCCAGAATGTCTCCAGCTGATGAAGCAGTGCTGGGCTGAGGCTGCAGAACAACGACCA
ACTTTTGATGAAATATTTAACCAGTTTAAAACTTTTAATAAAGGGAAGAAGACCAATATT
ATTGATTCTATGCTTCGGATGTTGGAGCAATATTCTAGCAACTTGGAAGATTTGATTCGG
GAGCGGACTGAAGAGCTGGAAATTGAAAAACAGAAAACGGAAAAGCTTCTAACACAGATG
CTACCACCATCAGTTGCTGAATCTCTCAAAAAGGGCTGCACAGTTGAACCTGAGGGCTTT
GACTTGGTCACCTTGTACTTCAGCGACATTGTGGGCTTCACAACCATTTCAGCCATGAGT
GAGCCCATTGAGGTCGTGGATCTTCTGAATGACCTGTACACACTCTTTGATGCAATAATT
GGCAGTCATGATGTCTACAAGGTAGAGACCATTGGAGATGCCTACATGGTGGCTTCAGGC
CTCCCAAAGAGGAATGGCAGTAGGCATGCAGCTGAGATTGCAAACATGTCCTTAGATATC
CTGAGCTCTGTGGGCACTTTCAAGATGCGGCACATGCCAGAAGTGCCGGTCCGAATTCGA
ATTGGCCTTCACTCAGGGCCGGTTGTTGCTGGAGTGGTGGGCCTCACCATGCCCAGATAC
TGCTTGTTTGGAGACACTGTGAACACAGCTTCTCGGATGGAATCTACAGGCTTACCTTAT
CGCATTCATGTCAGTCTCAGCACTGTTACAATTCTTCAAAATCTGAGTGAGGGCTATGAA
GTGGAGCTTCGAGGAAGAACAGAGCTCAAGGGCAAAGGCACAGAGGAAACCTTCTGGCTG
ATTGGGAAAAAAGGCTTCATGAAGCCCCTTCCTGTGCCCCCACCAGTGGACAAAGATGGG
CAAGTGGGCCATGGCCTGCAACCAGTGGAGATTGCAGCCTTCCAAAGAAGAAAAGCAGAA
AGGCAGTTGGTGAGAAACAAGCCATAA
Enzyme 106 GenBank Gene ID AL031387 Link Image
Enzyme 106 GeneCard ID GUCY2F Link Image
Enzyme 106 GenAtlas ID GUCY2F Link Image
Enzyme 106 HGNC ID HGNC:4691 Link Image
Enzyme 106 Chromosome Location Not Available
Enzyme 106 Locus Not Available
Enzyme 106 SNPs SNPJam Report Link Image
Enzyme 106 General References
  1. Lowe DG, Dizhoor AM, Liu K, Gu Q, Spencer M, Laura R, Lu L, Hurley JB: Cloning and expression of a second photoreceptor-specific membrane retina guanylyl cyclase (RetGC), RetGC-2. Proc Natl Acad Sci U S A. 1995 Jun 6;92(12):5535-9. [PubMed Link Image]
  2. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  3. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
  4. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 106 Metabolite References Not Available
Enzyme 107 [top]
Enzyme 107 ID 6375
Enzyme 107 Name Gamma-enolase
Enzyme 107 Synonyms
  1. 2-phospho-D-glycerate hydro-lyase
  2. Enolase 2
  3. Neural enolase
  4. Neuron-specific enolase
  5. NSE
Enzyme 107 Gene Name ENO2
Enzyme 107 Protein Sequence >Gamma-enolase 
MSIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRDGDKQRYLGK
GVLKAVDHINSTIAPALISSGLSVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCK
AGAAERELPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGAESFRD
AMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKI
VIGMDVAASEFYRDGKYDLDFKSPTDPSRYITGDQLGALYQDFVRDYPVVSIEDPFDQDD
WAAWSKFTANVGIQIVGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLA
QENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEELGDE
ARFAGHNFRNPSVL
Enzyme 107 Number of Residues 434
Enzyme 107 Molecular Weight 47268.1
Enzyme 107 Theoretical pI 4.65
Enzyme 107 GO Classification
Function
  • binding
  • carbon-oxygen lyase activity
  • catalytic activity
  • cation binding
  • hydro-lyase activity
  • ion binding
  • lyase activity
  • magnesium ion binding
  • metal ion binding
  • phosphopyruvate hydratase activity
Process
  • alcohol metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
  • macromolecular complex
  • phosphopyruvate hydratase complex
  • protein complex
Enzyme 107 General Function Involved in magnesium ion binding
Enzyme 107 Specific Function Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival
Enzyme 107 Pathways
Enzyme 107 Reactions
  • 2-phospho-D-glycerate = phosphoenolpyruvate + H2O [RN:R00658]
Enzyme 107 Pfam Domain Function
Enzyme 107 Signals
  • None
Enzyme 107 Transmembrane Regions
  • None
Enzyme 107 Essentiality Not Available
Enzyme 107 GenBank ID Protein 930063 Link Image
Enzyme 107 UniProtKB/Swiss-Prot ID P09104 Link Image
Enzyme 107 UniProtKB/Swiss-Prot Entry Name ENOG_HUMAN Link Image
Enzyme 107 PDB ID 1TE6 Link Image
Enzyme 107 PDB File Show
Enzyme 107 3D Structure
Enzyme 107 Cellular Location Not Available
Enzyme 107 Gene Sequence >1299 bp 
TCCATACAGAAGATCTGGGCCCGGGAGATCCTGGACTCCCGTGGGAACCCCACAGTGGAG
GTGGATCTCTATACTGCCAAAGGTCTTTTCCGGGCTGCAGTGCCCAGTGGAGCCTCTACG
GGCATCTATGAGGCCCTGGAGCTGAGGGATGGAGACAAACAGCGTTACTTAGGCAAAGGT
GTCCTGAAGGCAGTGGACCACATCAACTCCACCATCGCGCCAGCCCTCATCAGCTCAGGT
CTCTCTGTGGTGGAGCAAGAGAAGCTGGACAACCTGATGCTGGAGTTGGATGGGACTGAG
AACAAATCCAAGTTTGGGGCCAATGCCATCCTGGGTGTGTCTCTGGCCGTGTGTAAGGCA
GGGGCAGCTGAGCGGGAACTGCCCCTGTATCGCCACATTGCTCAGCTGGCCGGGAACTCA
GACCTCATCCTGCCTGTGCCGGCCTTCAACGTGATCAATGGTGGCTCTCATGCTGGCAAC
AAGCTGGCCATGCAGGAGTTCATGATCCTCCCAGTGGGAGCTGAGAGCTTTCGGGATGCC
ATGCGACTAGGTGCAGAGGTCTACCATACTCTCAAGGGAGTCATCAAGGACAAATACGGC
AAGGATGCCACCAATGTGGGGGATGAAGGTGGCTTTGCCCCCAATATCCTGGAGAACAGT
GAAGCCTTGGAGCTGGTTAAGGAAGCCATCGACAAGGCTGGCTACACGGAAAAAATGGTT
ATTGGCATGGATGTTGCTGCCTCAGAGTTTTATCGTGATGGCAAATATGACTTGGACTTC
AAGTCTCCCACTGATCCTTCCCGATACATCACTGGGGACCAGCTGGGGGCACTCTACCAG
GACTTTGTCAGGGACTATCCTGTGGTCTCCATTGAGGACCCATTTGACCAGGATGATTGG
GCTGCCTGGTCCAAGTTCACAGCCAATGTAGGGATCCAGATTGTGGGTGATGACCTGACA
GTGACCAACCCAAAACGTATTGAGCGGGCAGTGGAAGAAAAGGCCTGCAACTGTCTGCTG
CTCAAGGTCAACCAGATCGGCTCGGTCACTGAAGCCATCCAAGCGTGCAAGCTGGCCCAG
GAGAATGGCTGGGGGGTCATGGTGAGTCATCGCTCAGGAGAGACTGAGGACACATTCATT
GCTGACCTGGTGGTGGGGCTGTGCACAGGCCAGATCAAGACTGGTGCCCCGTGCCGTTCT
GAACGTCTGGCTAAATACAATCAGCTCATGAGAATTGAGGAAGAGCTGGGGGATGAAGCT
CGCTTTGCCGGACATAACTTCCGTAATCCCAGTGTGCTG
Enzyme 107 GenBank Gene ID X13120 Link Image
Enzyme 107 GeneCard ID ENO2 Link Image
Enzyme 107 GenAtlas ID ENO2 Link Image
Enzyme 107 HGNC ID HGNC:3353 Link Image
Enzyme 107 Chromosome Location 1
Enzyme 107 Locus 12p13
Enzyme 107 SNPs SNPJam Report Link Image
Enzyme 107 General References
  1. McAleese SM, Dunbar B, Fothergill JE, Hinks LJ, Day IN: Complete amino acid sequence of the neurone-specific gamma isozyme of enolase (NSE) from human brain and comparison with the non-neuronal alpha form (NNE). Eur J Biochem. 1988 Dec 15;178(2):413-7. [PubMed Link Image]
  2. Van Obberghen E, Kamholz J, Bishop JG 3rd, Zomzely-Neurath C, Lazzarini RA, Lazzarini RA: Human gamma enolase: isolation of a cDNA clone and expression in normal and tumor tissues of human origin. J Neurosci Res. 1988 Apr;19(4):450-6. [PubMed Link Image]
  3. Oliva D, Barba G, Barbieri G, Giallongo A, Feo S: Cloning, expression and sequence homologies of cDNA for human gamma enolase. Gene. 1989 Jul 15;79(2):355-60. [PubMed Link Image]
  4. Oliva D, Cali L, Feo S, Giallongo A: Complete structure of the human gene encoding neuron-specific enolase. Genomics. 1991 May;10(1):157-65. [PubMed Link Image]
  5. Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA: Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. Genome Res. 1997 Mar;7(3):268-80. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Day IN, Allsopp MT, Moore DC, Thompson RJ: Sequence conservation in the 3'-untranslated regions of neurone-specific enolase, lymphokine and protooncogene mRNAs. FEBS Lett. 1987 Sep 28;222(1):139-43. [PubMed Link Image]
  8. Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM: Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics. 2005 Sep;4(9):1240-50. Epub 2005 Jun 11. [PubMed Link Image]
  9. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  10. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  11. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  12. Chai G, Brewer JM, Lovelace LL, Aoki T, Minor W, Lebioda L: Expression, purification and the 1.8 angstroms resolution crystal structure of human neuron specific enolase. J Mol Biol. 2004 Aug 20;341(4):1015-21. [PubMed Link Image]
Enzyme 107 Metabolite References Not Available
Enzyme 108 [top]
Enzyme 108 ID 6413
Enzyme 108 Name Cyclic nucleotide-gated cation channel alpha-3
Enzyme 108 Synonyms
  1. Cone photoreceptor cGMP-gated channel subunit alpha
  2. Cyclic nucleotide-gated channel alpha-3
  3. CNG channel alpha-3
  4. CNG-3
  5. CNG3
Enzyme 108 Gene Name CNGA3
Enzyme 108 Protein Sequence >Cyclic nucleotide-gated cation channel alpha-3 
MAKINTQYSHPSRTHLKVKTSDRDLNRAENGLSRAHSSSEETSSVLQPGIAMETRGLADS
GQGSFTGQGIARLSRLIFLLRRWAARHVHHQDQGPDSFPDRFRGAELKEVSSQESNAQAN
VGSQEPADRGRSAWPLAKCNTNTSNNTEEEKKTKKKDAIVVDPSSNLYYRWLTAIALPVF
YNWYLLICRACFDELQSEYLMLWLVLDYSADVLYVLDVLVRARTGFLEQGLMVSDTNRLW
QHYKTTTQFKLDVLSLVPTDLAYLKVGTNYPEVRFNRLLKFSRLFEFFDRTETRTNYPNM
FRIGNLVLYILIIIHWNACIYFAISKFIGFGTDSWVYPNISIPEHGRLSRKYIYSLYWST
LTLTTIGETPPPVKDEEYLFVVVDFLVGVLIFATIVGNVGSMISNMNASRAEFQAKIDSI
KQYMQFRKVTKDLETRVIRWFDYLWANKKTVDEKEVLKSLPDKLKAEIAINVHLDTLKKV
RIFQDCEAGLLVELVLKLRPTVFSPGDYICKKGDIGKEMYIINEGKLAVVADDGVTQFVV
LSDGSYFGEISILNIKGSKSGNRRTANIRSIGYSDLFCLSKDDLMEALTEYPEAKKALEE
KGRQILMKDNLIDEELARAGADPKDLEEKVEQLGSSLDTLQTRFARLLAEYNATQMKMKQ
RLSQLESQVKGGGDKPLADGEVPGDATKTEDKQQ
Enzyme 108 Number of Residues 694
Enzyme 108 Molecular Weight 78837.4
Enzyme 108 Theoretical pI 7.80
Enzyme 108 GO Classification
Function
  • ion channel activity
  • ion transmembrane transporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • membrane
Enzyme 108 General Function Involved in ion channel activity
Enzyme 108 Specific Function Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cyclic GMP which leads to an opening of the cation channel and thereby causing a depolarization of cone photoreceptors. Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficacy of the channel when coexpressed with CNGB3. Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones
Enzyme 108 Pathways Not Available
Enzyme 108 Reactions Not Available
Enzyme 108 Pfam Domain Function
Enzyme 108 Signals
  • None
Enzyme 108 Transmembrane Regions
  • 171-192 305-325 378-397
Enzyme 108 Essentiality Not Available
Enzyme 108 GenBank ID Protein 62988794 Link Image
Enzyme 108 UniProtKB/Swiss-Prot ID Q16281 Link Image
Enzyme 108 UniProtKB/Swiss-Prot Entry Name CNGA3_HUMAN Link Image
Enzyme 108 PDB ID Not Available
Enzyme 108 Cellular Location Not Available
Enzyme 108 Gene Sequence >2085 bp 
ATGGCCAAGATCAACACCCAATACTCCCACCCCTCCAGGACCCACCTCAAGGTAAAGACC
TCAGACCGAGATCTCAATCGCGCTGAAAATGGCCTCAGCAGAGCCCACTCGTCAAGTGAG
GAGACATCGTCAGTGCTGCAGCCGGGGATCGCCATGGAGACCAGAGGACTGGCTGACTCC
GGGCAGGGCTCCTTCACCGGCCAGGGGATCGCCAGGCTGTCGCGCCTCATCTTCTTGCTG
CGCAGGTGGGCTGCCAGGCATGTGCACCACCAGGACCAGGGACCGGACTCTTTTCCTGAT
CGTTTCCGTGGAGCCGAGCTTAAGGAGGTGTCCAGCCAAGAAAGCAATGCCCAGGCAAAT
GTGGGCAGCCAGGAGCCAGCAGACAGAGGGAGAAGCGCCTGGCCCCTGGCCAAATGCAAC
ACTAACACCAGCAACAACACGGAGGAGGAGAAGAAGACGAAAAAGAAGGATGCGATCGTG
GTGGACCCGTCCAGCAACCTGTACTACCGCTGGCTGACCGCCATCGCCCTGCCTGTCTTC
TATAACTGGTATCTGCTTATTTGCAGGGCCTGTTTCGATGAGCTGCAGTCCGAGTACCTG
ATGCTGTGGCTGGTCCTGGACTACTCGGCAGATGTCCTGTATGTCTTGGATGTGCTTGTA
CGAGCTCGGACAGGTTTTCTCGAGCAAGGCTTAATGGTCAGTGATACCAACAGGCTGTGG
CAGCATTACAAGACGACCACGCAGTTCAAGCTGGATGTGTTGTCCCTGGTCCCCACCGAC
CTGGCTTACTTAAAGGTGGGCACAAACTACCCAGAAGTGAGGTTCAACCGCCTACTGAAG
TTTTCCCGGCTCTTTGAATTCTTTGACCGCACAGAGACAAGGACCAACTACCCCAATATG
TTCAGGATTGGGAACTTGGTCTTGTACATTCTCATCATCATCCACTGGAATGCCTGCATC
TACTTTGCCATTTCCAAGTTCATTGGTTTTGGGACAGACTCCTGGGTCTACCCAAACATC
TCAATCCCAGAGCATGGGCGCCTCTCCAGGAAGTACATTTACAGTCTCTACTGGTCCACC
TTGACCCTTACCACCATTGGTGAGACCCCACCCCCCGTGAAAGATGAGGAGTATCTCTTT
GTGGTCGTAGACTTCTTGGTGGGTGTTCTGATTTTTGCCACCATTGTGGGCAATGTGGGC
TCCATGATCTCGAATATGAATGCCTCACGGGCAGAGTTCCAGGCCAAGATTGATTCCATC
AAGCAGTACATGCAGTTCCGCAAGGTCACCAAGGACTTGGAGACGCGGGTTATCCGGTGG
TTTGACTACCTGTGGGCCAACAAGAAGACGGTGGATGAGAAGGAGGTGCTCAAGAGCCTC
CCAGACAAGCTGAAGGCTGAGATCGCCATCAACGTGCACCTGGACACGCTGAAGAAGGTT
CGCATCTTCCAGGACTGTGAGGCAGGGCTGCTGGTGGAGCTGGTGCTGAAGCTGCGACCC
ACTGTGTTCAGCCCTGGGGATTATATCTGCAAGAAGGGAGATATTGGGAAGGAGATGTAC
ATCATCAACGAGGGCAAGCTGGCCGTGGTGGCTGATGATGGGGTCACCCAGTTCGTGGTC
CTCAGCGATGGCAGCTACTTCGGGGAGATCAGCATTCTGAACATCAAGGGGAGCAAGTCG
GGGAACCGCAGGACGGCCAACATCCGCAGCATTGGCTACTCAGACCTGTTCTGCCTCTCA
AAGGACGATCTCATGGAGGCCCTCACCGAGTACCCCGAAGCCAAGAAGGCCCTGGAGGAG
AAAGGACGGCAGATCCTGATGAAAGACAACCTGATCGATGAGGAGCTGGCCAGGGCGGGC
GCGGACCCCAAGGACCTTGAGGAGAAAGTGGAGCAGCTGGGGTCCTCCCTGGACACCCTG
CAGACCAGGTTTGCACGCCTCCTGGCTGAGTACAACGCCACCCAGATGAAGATGAAGCAG
CGTCTCAGCCAACTGGAAAGCCAGGTGAAGGGTGGTGGGGACAAGCCCCTGGCTGATGGG
GAAGTTCCCGGGGATGCTACAAAAACAGAGGACAAACAACAGTGA
Enzyme 108 GenBank Gene ID AC092675 Link Image
Enzyme 108 GeneCard ID CNGA3 Link Image
Enzyme 108 GenAtlas ID CNGA3 Link Image
Enzyme 108 HGNC ID HGNC:2150 Link Image
Enzyme 108 Chromosome Location 2
Enzyme 108 Locus 2q11.2
Enzyme 108 SNPs SNPJam Report Link Image
Enzyme 108 General References
  1. Wissinger B, Muller F, Weyand I, Schuffenhauer S, Thanos S, Kaupp UB, Zrenner E: Cloning, chromosomal localization and functional expression of the gene encoding the alpha-subunit of the cGMP-gated channel in human cone photoreceptors. Eur J Neurosci. 1997 Dec;9(12):2512-21. [PubMed Link Image]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Distler M, Biel M, Flockerzi V, Hofmann F: Expression of cyclic nucleotide-gated cation channels in non-sensory tissues and cells. Neuropharmacology. 1994 Nov;33(11):1275-82. [PubMed Link Image]
  5. Sundin OH, Yang JM, Li Y, Zhu D, Hurd JN, Mitchell TN, Silva ED, Maumenee IH: Genetic basis of total colourblindness among the Pingelapese islanders. Nat Genet. 2000 Jul;25(3):289-93. [PubMed Link Image]
  6. Peng C, Rich ED, Varnum MD: Subunit configuration of heteromeric cone cyclic nucleotide-gated channels. Neuron. 2004 May 13;42(3):401-10. [PubMed Link Image]
  7. Kohl S, Marx T, Giddings I, Jagle H, Jacobson SG, Apfelstedt-Sylla E, Zrenner E, Sharpe LT, Wissinger B: Total colourblindness is caused by mutations in the gene encoding the alpha-subunit of the cone photoreceptor cGMP-gated cation channel. Nat Genet. 1998 Jul;19(3):257-9. [PubMed Link Image]
  8. Wissinger B, Gamer D, Jagle H, Giorda R, Marx T, Mayer S, Tippmann S, Broghammer M, Jurklies B, Rosenberg T, Jacobson SG, Sener EC, Tatlipinar S, Hoyng CB, Castellan C, Bitoun P, Andreasson S, Rudolph G, Kellner U, Lorenz B, Wolff G, Verellen-Dumoulin C, Schwartz M, Cremers FP, Apfelstedt-Sylla E, Zrenner E, Salati R, Sharpe LT, Kohl S: CNGA3 mutations in hereditary cone photoreceptor disorders. Am J Hum Genet. 2001 Oct;69(4):722-37. Epub 2001 Aug 30. [PubMed Link Image]
  9. Johnson S, Michaelides M, Aligianis IA, Ainsworth JR, Mollon JD, Maher ER, Moore AT, Hunt DM: Achromatopsia caused by novel mutations in both CNGA3 and CNGB3. J Med Genet. 2004 Feb;41(2):e20. [PubMed Link Image]
  10. Liu C, Varnum MD: Functional consequences of progressive cone dystrophy-associated mutations in the human cone photoreceptor cyclic nucleotide-gated channel CNGA3 subunit. Am J Physiol Cell Physiol. 2005 Jul;289(1):C187-98. Epub 2005 Mar 2. [PubMed Link Image]
  11. Nishiguchi KM, Sandberg MA, Gorji N, Berson EL, Dryja TP: Cone cGMP-gated channel mutations and clinical findings in patients with achromatopsia, macular degeneration, and other hereditary cone diseases. Hum Mutat. 2005 Mar;25(3):248-58. [PubMed Link Image]
  12. Reuter P, Koeppen K, Ladewig T, Kohl S, Baumann B, Wissinger B: Mutations in CNGA3 impair trafficking or function of cone cyclic nucleotide-gated channels, resulting in achromatopsia. Hum Mutat. 2008 Oct;29(10):1228-36. [PubMed Link Image]
Enzyme 108 Metabolite References Not Available
Enzyme 109 [top]
Enzyme 109 ID 6416
Enzyme 109 Name Cyclic nucleotide-gated cation channel beta-3
Enzyme 109 Synonyms
  1. Cone photoreceptor cGMP-gated channel subunit beta
  2. Cyclic nucleotide-gated cation channel modulatory subunit
  3. Cyclic nucleotide-gated channel beta-3
  4. CNG channel beta-3
Enzyme 109 Gene Name CNGB3
Enzyme 109 Protein Sequence >Cyclic nucleotide-gated cation channel beta-3 
MFKSLTKVNKVKPIGENNENEQSSRRNEEGSHPSNQSQQTTAQEENKGEEKSLKTKSTPV
TSEEPHTNIQDKLSKKNSSGDLTTNPDPQNAAEPTGTVPEQKEMDPGKEGPNSPQNKPPA
APVINEYADAQLHNLVKRMRQRTALYKKKLVEGDLSSPEASPQTAKPTAVPPVKESDDKP
TEHYYRLLWFKVKKMPLTEYLKRIKLPNSIDSYTDRLYLLWLLLVTLAYNWNCWFIPLRL
VFPYQTADNIHYWLIADIICDIIYLYDMLFIQPRLQFVRGGDIIVDSNELRKHYRTSTKF
QLDVASIIPFDICYLFFGFNPMFRANRMLKYTSFFEFNHHLESIMDKAYIYRVIRTTGYL
LFILHINACVYYWASNYEGIGTTRWVYDGEGNEYLRCYYWAVRTLITIGGLPEPQTLFEI
VFQLLNFFSGVFVFSSLIGQMRDVIGAATANQNYFRACMDDTIAYMNNYSIPKLVQKRVR
TWYEYTWDSQRMLDESDLLKTLPTTVQLALAIDVNFSIISKVDLFKGCDTQMIYDMLLRL
KSVLYLPGDFVCKKGEIGKEMYIIKHGEVQVLGGPDGTKVLVTLKAGSVFGEISLLAAGG
GNRRTANVVAHGFANLLTLDKKTLQEILVHYPDSERILMKKARVLLKQKAKTAEATPPRK
DLALLFPPKEETPKLFKTLLGGTGKASLARLLKLKREQAAQKKENSEGGEEEGKENEDKQ
KENEDKQKENEDKGKENEDKDKGREPEEKPLDRPECTASPIAVEEEPHSVRRTVLPRGTS
RQSLIISMAPSAEGGEEVLTIEVKEKAKQ
Enzyme 109 Number of Residues 809
Enzyme 109 Molecular Weight 92248.8
Enzyme 109 Theoretical pI 8.11
Enzyme 109 GO Classification
Function
  • ion channel activity
  • ion transmembrane transporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • membrane
Enzyme 109 General Function Involved in ion channel activity
Enzyme 109 Specific Function Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cGMP which leads to an opening of the cation channel and thereby causing a depolarization of rod photoreceptors. Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficiency of the channel when coexpressed with CNGA3. Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones
Enzyme 109 Pathways Not Available
Enzyme 109 Reactions Not Available
Enzyme 109 Pfam Domain Function
Enzyme 109 Signals
  • None
Enzyme 109 Transmembrane Regions
  • 217-237 251-271 303-323 360-380 418-438 505-525
Enzyme 109 Essentiality Not Available
Enzyme 109 GenBank ID Protein 116642889 Link Image
Enzyme 109 UniProtKB/Swiss-Prot ID Q9NQW8 Link Image
Enzyme 109 UniProtKB/Swiss-Prot Entry Name CNGB3_HUMAN Link Image
Enzyme 109 PDB ID Not Available
Enzyme 109 Cellular Location Not Available
Enzyme 109 Gene Sequence >2430 bp 
ATGTTTAAATCGCTGACAAAAGTCAACAAGGTGAAGCCTATAGGAGAGAACAATGAGAAT
GAACAAAGTTCTCGTCGGAATGAAGAAGGCTCTCACCCAAGTAATCAGTCTCAGCAAACC
ACAGCACAGGAAGAAAACAAAGGTGAAGAGAAATCTCTCAAAACCAAGTCAACTCCAGTC
ACGTCTGAAGAGCCACACACCAACATACAAGACAAACTCTCCAAGAAAAATTCCTCTGGA
GATCTGACCACAAACCCTGACCCTCAAAATGCAGCAGAACCAACTGGAACAGTGCCAGAG
CAGAAGGAAATGGACCCCGGGAAAGAAGGTCCAAACAGCCCACAAAACAAACCGCCTGCA
GCTCCTGTTATAAATGAGTATGCCGATGCCCAGCTACACAACCTGGTGAAAAGAATGCGT
CAAAGAACAGCCCTCTACAAGAAAAAGTTGGTAGAGGGAGATCTCTCCTCACCCGAAGCC
AGCCCACAAACTGCAAAGCCCACGGCTGTACCACCAGTAAAAGAAAGCGATGATAAGCCA
ACAGAACATTACTACAGGCTGTTGTGGTTCAAAGTCAAAAAGATGCCTTTAACAGAGTAC
TTAAAGCGAATTAAACTTCCAAACAGCATAGATTCATACACAGATCGACTCTATCTCCTG
TGGCTCTTGCTTGTCACTCTTGCCTATAACTGGAACTGCTGTTTTATACCACTGCGCCTC
GTCTTCCCATATCAAACCGCAGACAACATACACTACTGGCTTATTGCGGACATCATATGT
GATATCATCTACCTTTATGATATGCTATTTATCCAGCCCAGACTCCAGTTTGTAAGAGGA
GGAGACATAATAGTGGATTCAAATGAGCTAAGGAAACACTACAGGACTTCTACAAAATTT
CAGTTGGATGTCGCATCAATAATACCATTTGATATTTGCTACCTCTTCTTTGGGTTTAAT
CCAATGTTTAGAGCAAATAGGATGTTAAAGTACACTTCATTTTTTGAATTTAATCATCAC
CTAGAGTCTATAATGGACAAAGCATATATCTACAGAGTTATTCGAACAACTGGATACTTG
CTGTTTATTCTGCACATTAATGCCTGTGTTTATTACTGGGCTTCAAACTATGAAGGAATT
GGCACTACTAGATGGGTGTATGATGGGGAAGGAAACGAGTATCTGAGATGTTATTATTGG
GCAGTTCGAACTTTAATTACCATTGGTGGCCTTCCAGAACCACAAACTTTATTTGAAATT
GTTTTTCAACTCTTGAATTTTTTTTCTGGAGTTTTTGTGTTCTCCAGTTTAATTGGTCAG
ATGAGAGATGTGATTGGAGCAGCTACAGCCAATCAGAACTACTTCCGCGCCTGCATGGAT
GACACCATTGCCTACATGAACAATTACTCCATTCCTAAACTTGTGCAAAAGCGAGTTCGG
ACTTGGTATGAATATACATGGGACTCTCAAAGAATGCTAGATGAGTCTGATTTGCTTAAG
ACCCTACCAACTACGGTCCAGTTAGCCCTCGCCATTGATGTGAACTTCAGCATCATCAGC
AAAGTCGACTTGTTCAAGGGTTGTGATACACAGATGATTTATGACATGTTGCTAAGATTG
AAATCCGTTCTCTATTTGCCTGGTGACTTTGTCTGCAAAAAGGGAGAAATTGGCAAGGAA
ATGTATATCATCAAGCATGGAGAAGTCCAAGTTCTTGGAGGCCCTGATGGTACTAAAGTT
CTGGTTACTCTGAAAGCTGGGTCGGTGTTTGGAGAAATCAGCCTTCTAGCAGCAGGAGGA
GGAAACCGTCGAACTGCCAATGTGGTGGCCCACGGGTTTGCCAATCTTTTAACTCTAGAC
AAAAAGACCCTCCAAGAAATTCTAGTGCATTATCCAGATTCTGAAAGGATCCTCATGAAG
AAAGCCAGAGTGCTTTTAAAGCAGAAGGCTAAGACCGCAGAAGCAACCCCTCCAAGAAAA
GATCTTGCCCTCCTCTTCCCACCGAAAGAAGAGACACCCAAACTGTTTAAAACTCTCCTA
GGAGGCACAGGAAAAGCAAGTCTTGCAAGACTACTCAAATTGAAGCGAGAGCAAGCAGCT
CAGAAGAAAGAAAATTCTGAAGGAGGAGAGGAAGAAGGAAAAGAAAATGAAGATAAACAA
AAAGAAAATGAAGATAAACAAAAAGAAAATGAAGATAAAGGAAAAGAAAATGAAGATAAA
GATAAAGGAAGAGAGCCAGAAGAGAAGCCACTGGACAGACCTGAATGTACAGCAAGTCCT
ATTGCAGTGGAGGAAGAACCCCACTCAGTTAGAAGGACAGTTTTACCCAGAGGGACTTCT
CGTCAATCACTCATTATCAGCATGGCTCCTTCTGCTGAGGGCGGAGAAGAGGTTCTTACT
ATTGAAGTCAAAGAAAAGGCTAAGCAATAA
Enzyme 109 GenBank Gene ID NM_019098.4 Link Image
Enzyme 109 GeneCard ID CNGB3 Link Image
Enzyme 109 GenAtlas ID CNGB3 Link Image
Enzyme 109 HGNC ID HGNC:2153 Link Image
Enzyme 109 Chromosome Location 8
Enzyme 109 Locus 8q21.3
Enzyme 109 SNPs SNPJam Report Link Image
Enzyme 109 General References
  1. Kohl S, Baumann B, Broghammer M, Jagle H, Sieving P, Kellner U, Spegal R, Anastasi M, Zrenner E, Sharpe LT, Wissinger B: Mutations in the CNGB3 gene encoding the beta-subunit of the cone photoreceptor cGMP-gated channel are responsible for achromatopsia (ACHM3) linked to chromosome 8q21. Hum Mol Genet. 2000 Sep 1;9(14):2107-16. [PubMed Link Image]
  2. Sundin OH, Yang JM, Li Y, Zhu D, Hurd JN, Mitchell TN, Silva ED, Maumenee IH: Genetic basis of total colourblindness among the Pingelapese islanders. Nat Genet. 2000 Jul;25(3):289-93. [PubMed Link Image]
  3. Rojas CV, Maria LS, Santos JL, Cortes F, Alliende MA: A frameshift insertion in the cone cyclic nucleotide gated cation channel causes complete achromatopsia in a consanguineous family from a rural isolate. Eur J Hum Genet. 2002 Oct;10(10):638-42. [PubMed Link Image]
  4. Johnson S, Michaelides M, Aligianis IA, Ainsworth JR, Mollon JD, Maher ER, Moore AT, Hunt DM: Achromatopsia caused by novel mutations in both CNGA3 and CNGB3. J Med Genet. 2004 Feb;41(2):e20. [PubMed Link Image]
  5. Kohl S, Varsanyi B, Antunes GA, Baumann B, Hoyng CB, Jagle H, Rosenberg T, Kellner U, Lorenz B, Salati R, Jurklies B, Farkas A, Andreasson S, Weleber RG, Jacobson SG, Rudolph G, Castellan C, Dollfus H, Legius E, Anastasi M, Bitoun P, Lev D, Sieving PA, Munier FL, Zrenner E, Sharpe LT, Cremers FP, Wissinger B: CNGB3 mutations account for 50% of all cases with autosomal recessive achromatopsia. Eur J Hum Genet. 2005 Mar;13(3):302-8. [PubMed Link Image]
  6. Nishiguchi KM, Sandberg MA, Gorji N, Berson EL, Dryja TP: Cone cGMP-gated channel mutations and clinical findings in patients with achromatopsia, macular degeneration, and other hereditary cone diseases. Hum Mutat. 2005 Mar;25(3):248-58. [PubMed Link Image]
Enzyme 109 Metabolite References Not Available
Enzyme 110 [top]
Enzyme 110 ID 6447
Enzyme 110 Name Death-associated protein kinase 2
Enzyme 110 Synonyms
  1. DAP kinase 2
  2. DAP-kinase-related protein 1
  3. DRP-1
Enzyme 110 Gene Name DAPK2
Enzyme 110 Protein Sequence >Death-associated protein kinase 2 
MFQASMRSPNMEPFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSR
ASRRGVSREEIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKES
LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIED
GVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANIT
AVSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMVRRESV
VNLENFRKQYVRRRWKLSFSIVSLCNHLTRSLMKKVHLRPDEDLRNCESDTEEDIARRKA
LHPRRRSSTS
Enzyme 110 Number of Residues 370
Enzyme 110 Molecular Weight 42897.7
Enzyme 110 Theoretical pI 6.92
Enzyme 110 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
—
Enzyme 110 General Function Involved in protein kinase activity
Enzyme 110 Specific Function Calcium/calmodulin-dependent serine/threonine kinase which acts as a positive regulator of apoptosis
Enzyme 110 Pathways Not Available
Enzyme 110 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 110 Pfam Domain Function
Enzyme 110 Signals
  • None
Enzyme 110 Transmembrane Regions
  • None
Enzyme 110 Essentiality Not Available
Enzyme 110 GenBank ID Protein 6521210 Link Image
Enzyme 110 UniProtKB/Swiss-Prot ID Q9UIK4 Link Image
Enzyme 110 UniProtKB/Swiss-Prot Entry Name DAPK2_HUMAN Link Image
Enzyme 110 PDB ID Not Available
Enzyme 110 Cellular Location Not Available
Enzyme 110 Gene Sequence >1113 bp 
ATGTTCCAGGCCTCAATGAGGAGTCCAAACATGGAGCCATTCAAGCAGCAGAAGGTGGAG
GACTTTTATGACATCGGAGAGGAGCTGGGGAGTGGCCAGTTTGCCATCGTGAAGAAGTGC
CGGGAGAAGAGCACGGGGCTTGAGTATGCAGCCAAGTTCATCAAGAAGCGGCAGAGCCGG
GCGAGCCGGCGCGGTGTGAGCCGGGAGGAGATCGAGCGGGAGGTGAGCATCCTGCGGCAG
GTGCTGCACCACAATGTCATCACGCTGCACGACGTCTATGAGAACCGCACCGACGTGGTG
CTCATCCTTGAGCTAGTGTCTGGAGGAGAGCTCTTCGATTTCCTGGCCCAGAAGGAGTCA
CTGAGTGAGGAGGAGGCCACCAGCTTCATTAAGCAGATCCTGGATGGGGTGAACTACCTT
CACACAAAGAAAATTGCTCACTTTGATCTCAAGCCAGAAAACATTATGTTGTTAGACAAG
AATATTCCCATTCCACACATCAAGCTGATTGACTTTGGTCTGGCTCACGAAATAGAAGAT
GGAGTTGAATTTAAGAATATTTTTGGGACGCCGGAATTTGTTGCTCCAGAAATTGTGAAC
TACGAGCCCCTGGGTCTGGAGGCTGACATGTGGAGCATAGGCGTCATCACCTACATCCTC
TTAAGTGGAGCATCCCCTTTCCTGGGAGACACGAAGCAGGAAACACTGGCAAATATCACA
GCAGTGAGTTACGACTTTGATGAGGAATTCTTCAGCCAGACGAGCGAGCTGGCCAAGGAC
TTTATTCGGAAGCTTCTGGTTAAAGAGACCCGGAAACGGCTCACAATCCAAGAGGCTCTC
AGACACCCCTGGATCACGCCGGTGGACAACCAGCAAGCCATGGTGCGCAGGGAGTCTGTG
GTCAATCTGGAGAACTTCAGGAAGCAGTATGTCCGCAGGCGGTGGAAGCTTTCCTTCAGC
ATCGTGTCCCTGTGCAACCACCTCACCCGCTCGCTGATGAAGAAGGTGCACCTGAGGCCG
GATGAGGACCTGAGGAACTGTGAGAGTGACACTGAGGAGGACATCGCCAGGAGGAAAGCC
CTCCACCCACGGAGGAGGAGCAGCACCTCCTAA
Enzyme 110 GenBank Gene ID AB018001 Link Image
Enzyme 110 GeneCard ID DAPK2 Link Image
Enzyme 110 GenAtlas ID DAPK2 Link Image
Enzyme 110 HGNC ID HGNC:2675 Link Image
Enzyme 110 Chromosome Location 1
Enzyme 110 Locus 15q22.31
Enzyme 110 SNPs SNPJam Report Link Image
Enzyme 110 General References
  1. Kawai T, Nomura F, Hoshino K, Copeland NG, Gilbert DJ, Jenkins NA, Akira S: Death-associated protein kinase 2 is a new calcium/calmodulin-dependent protein kinase that signals apoptosis through its catalytic activity. Oncogene. 1999 Jun 10;18(23):3471-80. [PubMed Link Image]
  2. Inbal B, Shani G, Cohen O, Kissil JL, Kimchi A: Death-associated protein kinase-related protein 1, a novel serine/threonine kinase involved in apoptosis. Mol Cell Biol. 2000 Feb;20(3):1044-54. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Shani G, Henis-Korenblit S, Jona G, Gileadi O, Eisenstein M, Ziv T, Admon A, Kimchi A: Autophosphorylation restrains the apoptotic activity of DRP-1 kinase by controlling dimerization and calmodulin binding. EMBO J. 2001 Mar 1;20(5):1099-113. [PubMed Link Image]
  5. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  7. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 110 Metabolite References Not Available
Enzyme 111 [top]
Enzyme 111 ID 6448
Enzyme 111 Name Plasma membrane calcium-transporting ATPase 3
Enzyme 111 Synonyms
  1. PMCA3
  2. Plasma membrane calcium ATPase isoform 3
  3. Plasma membrane calcium pump isoform 3
Enzyme 111 Gene Name ATP2B3
Enzyme 111 Protein Sequence >Plasma membrane calcium-transporting ATPase 3 
MGDMANSSIEFHPKPQQQRDVPQAGGFGCTLAELRTLMELRGAEALQKIEEAYGDVSGLC
RRLKTSPTEGLADNTNDLEKRRQIYGQNFIPPKQPKTFLQLVWEALQDVTLIILEVAAIV
SLGLSFYAPPGEESEACGNVSGGAEDEGEAEAGWIEGAAILLSVICVVLVTAFNDWSKEK
QFRGLQSRIEQEQKFTVIRNGQLLQVPVAALVVGDIAQVKYGDLLPADGVLIQANDLKID
ESSLTGESDHVRKSADKDPMLLSGTHVMEGSGRMVVTAVGVNSQTGIIFTLLGAGGEEEE
KKDKKGKQQDGAMESSQTKAKKQDGAVAMEMQPLKSAEGGEMEEREKKKANAPKKEKSVL
QGKLTKLAVQIGKAGLVMSAITVIILVLYFVIETFVVEGRTWLAECTPVYVQYFVKFFII
GVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTT
NRMTVVQSYLGDTHYKEIPAPSALTPKILDLLVHAISINSAYTTKILPPEKEGALPRQVG
NKTECALLGFVLDLKRDFQPVREQIPEDKLYKVYTFNSVRKSMSTVIRMPDGGFRLFSKG
ASEILLKKCTNILNSNGELRGFRPRDRDDMVRKIIEPMACDGLRTICIAYRDFSAGQEPD
WDNENEVVGDLTCIAVVGIEDPVRPEVPEAIRKCQRAGITVRMVTGDNINTARAIAAKCG
IIQPGEDFLCLEGKEFNRRIRNEKGEIEQERLDKVWPKLRVLARSSPTDKHTLVKGIIDS
TTGEQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVM
WGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTFASLALA
TEPPTESLLLRKPYGRDKPLISRTMMKNILGHAVYQLAIIFTLLFVGELFFDIDSGRNAP
LHSPPSEHYTIIFNTFVMMQLFNEINARKIHGERNVFDGIFSNPIFCTIVLGTFGIQIVI
VQFGGKPFSCSPLSTEQWLWCLFVGVGELVWGQVIATIPTSQLKCLKEAGHGPGKDEMTD
EELAEGEEEIDHAERELRRGQILWFRGLNRIQTQIRVVKAFRSSLYEGLEKPESKTSIHN
FMATPEFLINDYTHNIPLIDDTDVDENEERLRAPPPPSPNQNNNAIDSGIYLTTHVTKSA
TSSVFSSSPGSPLHSVETSL
Enzyme 111 Number of Residues 1220
Enzyme 111 Molecular Weight 134196.0
Enzyme 111 Theoretical pI 5.29
Enzyme 111 GO Classification
Function
  • ATP binding
  • ATPase activity, coupled to transmembrane movement of ions
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • calcium ion transmembrane transporter activity
  • calcium-transporting ATPase activity
  • catalytic activity
  • cation transmembrane transporter activity
  • di-, tri-valent inorganic cation transmembrane transporter activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • inorganic cation transmembrane transporter activity
  • ion transmembrane transporter activity
  • nucleoside binding
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • calcium ion transport
  • cation transport
  • cellular nitrogen compound metabolic process
  • di-, tri-valent inorganic cation transport
  • divalent metal ion transport
  • establishment of localization
  • ion transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • transport
Component
  • cell part
  • membrane
Enzyme 111 General Function Involved in ATP binding
Enzyme 111 Specific Function This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell
Enzyme 111 Pathways Not Available
Enzyme 111 Reactions
  • ATP + H2O + Ca2+cis = ADP + phosphate + Ca2+trans [RN:R00086]
Enzyme 111 Pfam Domain Function
Enzyme 111 Signals
  • None
Enzyme 111 Transmembrane Regions
  • 98-118 156-176 365-384 418-435 850-869 880-900 921-943 962-983 1003-1024 1035-1056
Enzyme 111 Essentiality Not Available
Enzyme 111 GenBank ID Protein 48255955 Link Image
Enzyme 111 UniProtKB/Swiss-Prot ID Q16720 Link Image
Enzyme 111 UniProtKB/Swiss-Prot Entry Name AT2B3_HUMAN Link Image
Enzyme 111 PDB ID Not Available
Enzyme 111 Cellular Location Not Available
Enzyme 111 Gene Sequence >3663 bp 
ATGGGCGACATGGCCAATAGTTCCATCGAGTTCCACCCCAAGCCCCAGCAGCAGCGGGAT
GTCCCCCAGGCTGGAGGCTTTGGGTGCACGCTGGCGGAGCTGCGCACCCTCATGGAGCTG
CGAGGGGCCGAGGCGCTGCAGAAGATCGAGGAGGCCTACGGGGATGTCAGCGGGCTCTGC
CGGAGGCTGAAGACCTCACCCACAGAGGGCCTGGCGGACAACACCAATGACCTGGAGAAG
CGCAGGCAGATCTACGGGCAGAACTTCATCCCCCCAAAGCAACCCAAGACCTTCCTGCAG
CTGGTGTGGGAGGCCCTGCAGGACGTGACCCTCATCATCCTGGAGGTGGCTGCCATCGTC
TCTCTGGGCCTCTCGTTCTATGCGCCGCCAGGAGAGGAGAGTGAAGCCTGTGGGAATGTG
TCGGGAGGCGCAGAAGATGAGGGCGAGGCCGAAGCTGGCTGGATCGAGGGGGCTGCCATC
CTGCTGTCCGTCATCTGTGTGGTGCTGGTCACGGCCTTCAATGACTGGAGCAAGGAGAAG
CAGTTCCGAGGCCTGCAGAGCCGAATTGAGCAGGAGCAGAAGTTCACGGTCATCCGGAAC
GGGCAGCTCCTCCAGGTCCCCGTGGCTGCGCTGGTGGTGGGGGACATTGCCCAGGTCAAG
TACGGCGACCTGCTGCCAGCCGACGGCGTGCTCATCCAGGCCAATGACCTCAAGATCGAC
GAGAGCTCCCTGACGGGCGAGTCTGACCACGTGCGCAAGTCAGCTGACAAAGATCCCATG
CTGCTCTCAGGCACTCATGTCATGGAAGGTTCTGGAAGAATGGTGGTGACCGCCGTTGGC
GTGAATTCCCAGACAGGCATCATCTTCACGCTGCTTGGAGCTGGCGGAGAGGAGGAAGAG
AAGAAAGATAAGAAAGGCAAGCAGCAGGATGGGGCCATGGAGAGTAGCCAGACCAAAGCT
AAGAAGCAGGATGGTGCAGTGGCCATGGAGATGCAGCCCCTGAAGAGCGCGGAGGGTGGG
GAGATGGAGGAGCGGGAGAAGAAGAAAGCCAACGCACCCAAAAAGGAGAAGTCTGTCCTT
CAGGGGAAGCTCACAAAGCTAGCCGTGCAGATCGGGAAAGCAGGGCTGGTGATGTCTGCC
ATCACCGTCATCATCCTGGTCCTCTACTTTGTGATTGAGACGTTTGTCGTGGAAGGCCGG
ACATGGCTGGCAGAGTGCACGCCGGTCTATGTACAATACTTCGTGAAGTTCTTCATCATT
GGTGTCACTGTGCTGGTCGTGGCTGTCCCAGAGGGCCTGCCTCTTGCTGTCACCATCTCC
TTAGCTTACTCTGTCAAGAAAATGATGAAAGACAACAACCTGGTGCGCCACCTGGATGCC
TGCGAGACCATGGGCAACGCCACAGCCATCTGCTCCGACAAGACGGGCACGCTCACCACC
AACCGTATGACCGTGGTCCAGTCCTACCTAGGAGACACCCACTACAAAGAGATTCCGGCC
CCCAGCGCCCTGACCCCTAAGATCCTCGACCTCCTGGTCCATGCCATCTCCATCAACAGT
GCCTATACCACCAAAATACTACCTCCTGAGAAGGAAGGCGCCCTCCCACGCCAGGTGGGC
AATAAGACGGAGTGCGCCCTGCTGGGCTTCGTCTTGGACCTGAAGCGGGACTTCCAGCCC
GTGCGCGAGCAGATCCCGGAAGACAAGCTTTACAAAGTGTACACCTTCAACTCGGTCCGC
AAGTCCATGAGCACAGTCATCCGCATGCCCGACGGTGGCTTCCGCCTCTTCAGCAAGGGG
GCCTCAGAGATCCTCTTGAAAAAGTGCACCAACATCTTGAACAGCAATGGCGAACTCCGG
GGCTTTCGGCCTCGGGACCGGGACGACATGGTGAGGAAGATCATCGAGCCGATGGCTTGC
GATGGCCTCCGCACCATCTGCATCGCCTACCGGGACTTCTCTGCAGGCCAGGAGCCCGAC
TGGGACAACGAGAATGAGGTCGTGGGTGACCTCACCTGCATAGCTGTCGTGGGCATTGAG
GACCCTGTGCGGCCCGAGGTCCCTGAAGCTATCCGAAAATGCCAGCGTGCTGGCATCACA
GTCCGCATGGTGACTGGGGACAACATCAACACGGCCCGGGCCATCGCAGCCAAATGCGGC
ATCATCCAGCCCGGGGAGGACTTCCTGTGCCTAGAAGGGAAGGAGTTCAACCGGCGGATC
CGCAATGAGAAAGGCGAGATAGAACAGGAGCGGCTGGACAAGGTGTGGCCCAAGCTGAGG
GTGCTGGCCCGGTCGTCTCCCACCGACAAGCACACACTGGTCAAAGGGATTATCGACAGC
ACCACTGGTGAGCAGCGGCAGGTGGTGGCTGTGACAGGGGATGGCACCAACGATGGGCCG
GCCCTCAAGAAGGCGGACGTGGGCTTCGCCATGGGCATCGCAGGGACCGACGTGGCCAAG
GAGGCCTCCGACATCATCCTGACCGATGACAACTTCACCAGCATCGTCAAGGCAGTCATG
TGGGGCCGTAACGTCTATGACAGCATCTCCAAGTTCCTGCAGTTTCAACTGACGGTCAAT
GTGGTGGCTGTGATCGTGGCCTTCACAGGTGCCTGCATTACTCAGGACTCTCCTCTCAAA
GCCGTGCAGATGTTGTGGGTGAACTTGATCATGGACACATTTGCCTCTCTGGCCCTGGCG
ACGGAGCCACCCACAGAGTCGCTGCTGCTGCGGAAGCCGTACGGCCGCGACAAGCCCCTC
ATCTCCCGCACCATGATGAAGAACATTCTGGGCCACGCCGTGTACCAGCTCGCCATCATC
TTCACCCTGCTGTTTGTCGGGGAGCTCTTCTTCGACATCGACAGCGGGAGGAATGCGCCC
CTGCACTCGCCACCCTCAGAGCACTACACCATCATCTTCAACACGTTCGTCATGATGCAG
CTCTTTAACGAGATCAACGCCCGCAAGATCCACGGCGAGAGGAACGTGTTCGACGGCATC
TTCAGCAACCCCATCTTCTGCACCATCGTTTTGGGCACTTTCGGGATTCAGATTGTCATC
GTCCAGTTTGGCGGGAAGCCCTTCAGCTGCTCCCCACTATCCACAGAACAGTGGCTCTGG
TGCCTGTTTGTTGGTGTTGGGGAGCTGGTCTGGGGACAGGTCATTGCCACCATCCCCACC
AGCCAGCTCAAGTGCCTGAAGGAAGCCGGGCACGGGCCCGGGAAGGACGAGATGACCGAC
GAGGAGCTGGCCGAAGGCGAGGAAGAGATCGACCATGCCGAGCGGGAGCTCCGCAGGGGC
CAGATCCTCTGGTTCCGGGGCCTGAACCGGATTCAGACGCAGATCCGGGTGGTGAAAGCG
TTCCGTAGCTCGCTCTATGAAGGCCTGGAGAAACCAGAATCCAAGACCTCCATTCACAAC
TTCATGGCCACGCCCGAGTTTCTGATCAATGACTACACCCACAACATCCCGCTCATTGAC
GACACGGACGTGGACGAGAACGAGGAGCGCCTCCGGGCCCCCCCGCCCCCGTCCCCCAAC
CAGAACAACAACGCCATAGACAGCGGCATCTACCTGACCACGCATGTCACCAAGTCAGCT
ACCTCTTCAGTGTTTTCCTCCAGTCCCGGGAGCCCGCTCCACAGCGTGGAGACGTCCCTC
TAA
Enzyme 111 GenBank Gene ID NM_001001344.2 Link Image
Enzyme 111 GeneCard ID ATP2B3 Link Image
Enzyme 111 GenAtlas ID ATP2B3 Link Image
Enzyme 111 HGNC ID HGNC:816 Link Image
Enzyme 111 Chromosome Location Not Available
Enzyme 111 Locus Not Available
Enzyme 111 SNPs SNPJam Report Link Image
Enzyme 111 General References
  1. Brown BJ, Hilfiker H, DeMarco SJ, Zacharias DA, Greenwood TM, Guerini D, Strehler EE: Primary structure of human plasma membrane Ca(2+)-ATPase isoform 3. Biochim Biophys Acta. 1996 Aug 14;1283(1):10-3. [PubMed Link Image]
  2. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  3. Wang MG, Yi H, Hilfiker H, Carafoli E, Strehler EE, McBride OW: Localization of two genes encoding plasma membrane Ca2+ ATPases isoforms 2 (ATP2B2) and 3 (ATP2B3) to human chromosomes 3p26-->p25 and Xq28, respectively. Cytogenet Cell Genet. 1994;67(1):41-5. [PubMed Link Image]
  4. Mallon AM, Platzer M, Bate R, Gloeckner G, Botcherby MR, Nordsiek G, Strivens MA, Kioschis P, Dangel A, Cunningham D, Straw RN, Weston P, Gilbert M, Fernando S, Goodall K, Hunter G, Greystrong JS, Clarke D, Kimberley C, Goerdes M, Blechschmidt K, Rump A, Hinzmann B, Mundy CR, Miller W, Poustka A, Herman GE, Rhodes M, Denny P, Rosenthal A, Brown SD: Comparative genome sequence analysis of the Bpa/Str region in mouse and Man. Genome Res. 2000 Jun;10(6):758-75. [PubMed Link Image]
  5. Stauffer TP, Hilfiker H, Carafoli E, Strehler EE: Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes. J Biol Chem. 1993 Dec 5;268(34):25993-6003. [PubMed Link Image]
  6. Stauffer TP, Hilfiker H, Carafoli E, Strehler EE: Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes. J Biol Chem. 1994 Dec 16;269(50):32022. [PubMed Link Image]
Enzyme 111 Metabolite References Not Available
Enzyme 112 [top]
Enzyme 112 ID 6476
Enzyme 112 Name Protein kinase C alpha type
Enzyme 112 Synonyms
  1. PKC-A
  2. PKC-alpha
Enzyme 112 Gene Name PRKCA
Enzyme 112 Protein Sequence >Protein kinase C alpha type 
MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGF
GKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGS
LLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDA
KNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRL
SVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNME
LRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKG
TEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYV
NGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIA
DFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDG
EDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMTKHPAKRLGCGPEGERDVREHAFFRRI
DWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVN
PQFVHPILQSAV
Enzyme 112 Number of Residues 672
Enzyme 112 Molecular Weight 76763.5
Enzyme 112 Theoretical pI 7.05
Enzyme 112 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • kinase activity
  • metal ion binding
  • nucleoside binding
  • protein kinase C activity
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
  • transition metal ion binding
  • zinc ion binding
Process
  • cellular metabolic process
  • intracellular signaling pathway
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • signaling
  • signaling pathway
Component
—
Enzyme 112 General Function Involved in protein serine/threonine kinase activity
Enzyme 112 Specific Function PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters
Enzyme 112 Pathways Not Available
Enzyme 112 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 112 Pfam Domain Function
Enzyme 112 Signals
  • None
Enzyme 112 Transmembrane Regions
  • None
Enzyme 112 Essentiality Not Available
Enzyme 112 GenBank ID Protein 35483 Link Image
Enzyme 112 UniProtKB/Swiss-Prot ID P17252 Link Image
Enzyme 112 UniProtKB/Swiss-Prot Entry Name KPCA_HUMAN Link Image
Enzyme 112 PDB ID Not Available
Enzyme 112 Cellular Location Not Available
Enzyme 112 Gene Sequence >2019 bp 
ATGGCTGACGTTTTCCCGGGCAACGACTCCACGGCGTCTCAGGACGTGGCCAACCGCTTC
GCCCGCAAAGGGGCGCTGAGGCAGAAGAACGTGCACGAGGTGAAGGACCACAAATTCATC
GCGCGCTTCTTCAAGCAGCCCACCTTCTGCAGCCACTGCACCGACTTCATCTGGGGGTTT
GGGAAACAAGGCTTCCAGTGCCAAGTTTGCTGTTTTGTGGTCCACAAGAGGTGCCATGAA
TTTGTTACTTTTTCTTGTCCGGGTGCGGATAAGGGACCCGACACTGATGACCCCAGGAGC
AAGCACAAGTTCAAAATCCACACTTACGGAAGCCCCACCTTCTGCGATCACTGTGGGTCA
CTGCTCTATGGACTTATCCATCAAGGGATGAAATGTGACACCTGCGATATGAACGTTCAC
AAGCAATGCGTCATCAATGTCCCCAGCCTCTGCGGAATGGATCACACTGAGAAGAGGGGG
CGGATTTACCTAAAGGCTGAGGTTGCTGATGAAAAGCTCCATGTCACAGTACGAGATGCA
AAAAATCTAATCCCTATGGATCCAAACGGGCTTTCAGATCCTTATGTGAAGCTGAAACTT
ATTCCTGATCCCAAGAATGAAAGCAAGCAAAAAACCAAAACCATCCGCTCCACACTAAAT
CCGCAGTGGAATGAGTCCTTTACATTCAAATTGAAACCTTCAGACAAAGACCGACGACTG
TCTGTAGAAATCTGGGACTGGGATCGAACAACAAGGAATGACTTCATGGGATCCCTTTCC
TTTGGAGTTTCGGAGCTGATGAAGATGCCGGCCAGTGGATGGTACAAGTTGCTTAACCAA
GAAGAAGGTGAGTACTACAACGTACCCATTCCGGAAGGGGACGAGGAAGGAAACATGGAA
CTCAGGCAGAAATTCGAGAAAGCCAAACTTGGCCCTGCTGGCAACAAAGTCATCAGTCCC
TCTGAAGACAGGAAACAACCTTCCAACAACCTTGACCGAGTGAAACTCACGGACTTCAAT
TTCCTCATGGTGTTGGGAAAGGGGAGTTTTGGAAAGGTGATGCTTGCCGACAGGAAGGGC
ACAGAAGAACTGTATGCAATCAAAATCCTGAAGAAGGATGTGGTGATTCAGGATGATGAC
GTGGAGTGCACCATGGTAGAAAAGCGAGTCTTGGCCCTGCTTGACAAACCCCCGTTCTTG
ACGCAGCTGCACTCCTGCTTCCAGACAGTGGATCGGCTGTACTTCGTCATGGAATATGTC
AACGGTGGGGACCTCATGTACCACATTCAGCAAGTAGGAAAATTTAAGGAACCACAAGCA
GTATTCTATGCGGCAGAGATTTCCATCGGATTGTTCTTTCTTCATAAAAGAGGAATCATT
TATAGGGATCTGAAGTTAGATAACGTCATGTTGGATTCAGAAGGACATATCAAAATTGCT
GACTTTGGGATGTGCAAGGAACACATGATGGATGGAGTCACGACCAGGACCTTCTGTGGG
ACTCCAGATTATATCGCCCCAGAGATAATCGCTTATCAGCCGTATGGAAAATCTGTGGAC
TGGTGGGCCTATGGCGTCCTGTTGTATGAAATGCTTGCCGGGCAGCCTCCATTTGATGGT
GAAGATGAAGACGAGCTATTTCAGTCTATCATGGAGCACAACGTTTCCTATCCAAAATCC
TTGTCCAAGGAGGCTGTTTCTATCTGCAAAGGACTGATGACCAAACACCCAGCCAAGCGG
CTGGGCTGTGGGCCTGAGGGGGAGAGGGACGTGAGAGAGCATGCCTTCTTCCGGAGGATC
GACTGGGAAAAACTGGAGAACAGGGAGATCCAGCCACCATTCAAGCCCAAAGTGTGTGGC
AAAGGAGCAGAGAACTTTGACAAGTTCTTCACACGAGGACAGCCCGTCTTAACACCACCT
GATCAGCTGGTTATTGCTAACATAGACCAGTCTGATTTTGAAGGGTTCTCGTATGTCAAC
CCCCAGTTTGTGCACCCCATCTTACAGAGTGCAGTATGA
Enzyme 112 GenBank Gene ID X52479 Link Image
Enzyme 112 GeneCard ID PRKCA Link Image
Enzyme 112 GenAtlas ID PRKCA Link Image
Enzyme 112 HGNC ID HGNC:9393 Link Image
Enzyme 112 Chromosome Location 1
Enzyme 112 Locus 17q22-q23.2
Enzyme 112 SNPs SNPJam Report Link Image
Enzyme 112 General References
  1. Finkenzeller G, Marme D, Hug H: Sequence of human protein kinase C alpha. Nucleic Acids Res. 1990 Apr 25;18(8):2183. [PubMed Link Image]
  2. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. McSwine-Kennick RL, McKeegan EM, Johnson MD, Morin MJ: Phorbol diester-induced alterations in the expression of protein kinase C isozymes and their mRNAs. Analysis in wild-type and phorbol diester-resistant HL-60 cell clones. J Biol Chem. 1991 Aug 15;266(23):15135-43. [PubMed Link Image]
  5. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  6. Zemlickova E, Dubois T, Kerai P, Clokie S, Cronshaw AD, Wakefield RI, Johannes FJ, Aitken A: Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C. Biochem Biophys Res Commun. 2003 Aug 1;307(3):459-65. [PubMed Link Image]
  7. Dev KK, Nakanishi S, Henley JM: The PDZ domain of PICK1 differentially accepts protein kinase C-alpha and GluR2 as interacting ligands. J Biol Chem. 2004 Oct 1;279(40):41393-7. Epub 2004 Jul 9. [PubMed Link Image]
  8. Makagiansar IT, Williams S, Dahlin-Huppe K, Fukushi J, Mustelin T, Stallcup WB: Phosphorylation of NG2 proteoglycan by protein kinase C-alpha regulates polarized membrane distribution and cell motility. J Biol Chem. 2004 Dec 31;279(53):55262-70. Epub 2004 Oct 25. [PubMed Link Image]
  9. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  10. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  11. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  12. Chen D, Gould C, Garza R, Gao T, Hampton RY, Newton AC: Amplitude control of protein kinase C by RINCK, a novel E3 ubiquitin ligase. J Biol Chem. 2007 Nov 16;282(46):33776-87. Epub 2007 Sep 24. [PubMed Link Image]
  13. Wissing J, Jansch L, Nimtz M, Dieterich G, Hornberger R, Keri G, Wehland J, Daub H: Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics. 2007 Mar;6(3):537-47. Epub 2006 Dec 27. [PubMed Link Image]
  14. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  15. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  16. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  17. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  18. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  19. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  20. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 112 Metabolite References Not Available
Enzyme 113 [top]
Enzyme 113 ID 6479
Enzyme 113 Name Serine/threonine-protein kinase 38
Enzyme 113 Synonyms
  1. NDR1 protein kinase
  2. Nuclear Dbf2-related kinase 1
Enzyme 113 Gene Name STK38
Enzyme 113 Protein Sequence >Serine/threonine-protein kinase 38 
MAMTGSTPCSSMSNHTKERVTMTKVTLENFYSNLIAQHEEREMRQKKLEKVMEEEGLKDE
EKRLRRSAHARKETEFLRLKRTRLGLEDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKIL
RKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEFLPGGDMMTLLMK
KDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKA
HRTEFYRNLNHSLPSDFTFQNMNSKRKAETWKRNRRQLAFSTVGTPDYIAPEVFMQTGYN
KLCDWWSLGVIMYEMLIGYPPFCSETPQETYKKVMNWKETLTFPPEVPISEKAKDLILRF
CCEWEHRIGAPGVEEIKSNSFFEGVDWEHIRERPAAISIEIKSIDDTSNFDEFPESDILK
PTVATSNHPETDYKNKDWVFINYTYKRFEGLTARGAIPSYMKAAK
Enzyme 113 Number of Residues 465
Enzyme 113 Molecular Weight 54189.8
Enzyme 113 Theoretical pI 7.17
Enzyme 113 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
—
Enzyme 113 General Function Involved in protein serine/threonine kinase activity
Enzyme 113 Specific Function Negative regulator of MAP3K1/2 signaling. Converts MAP3K2 from its phosphorylated form to its nonphosphorylated form and inhibits autophosphorylation of MAP3K2
Enzyme 113 Pathways Not Available
Enzyme 113 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 113 Pfam Domain Function
Enzyme 113 Signals
  • None
Enzyme 113 Transmembrane Regions
  • None
Enzyme 113 Essentiality Not Available
Enzyme 113 GenBank ID Protein 15082350 Link Image
Enzyme 113 UniProtKB/Swiss-Prot ID Q15208 Link Image
Enzyme 113 UniProtKB/Swiss-Prot Entry Name STK38_HUMAN Link Image
Enzyme 113 PDB ID Not Available
Enzyme 113 Cellular Location Not Available
Enzyme 113 Gene Sequence >1398 bp 
ATGGCAATGACAGGCTCAACACCTTGCTCATCCATGAGTAACCACACAAAGGAAAGGGTG
ACAATGACCAAAGTGACACTGGAGAATTTTTATAGCAACCTTATCGCTCAACATGAAGAA
CGAGAAATGAGACAAAAGAAGTTAGAAAAGGTGATGGAAGAAGAAGGCCTAAAAGATGAG
GAGAAACGACTCCGGAGATCAGCACATGCTCGGAAGGAAACAGAGTTTCTTCGTTTGAAG
AGAACAAGACTTGGATTGGAAGATTTTGAGTCCTTAAAAGTAATAGGCAGAGGAGCATTT
GGTGAGGTACGGCTTGTTCAGAAGAAAGATACGGGACATGTGTATGCAATGAAAATACTC
CGTAAAGCAGATATGCTTGAAAAAGAGCAGGTTGGCCACATTCGTGCGGAGCGTGACATT
CTAGTGGAGGCAGACAGTTTGTGGGTTGTGAAAATGTTCTATAGTTTTCAGGATAAGCTA
AACCTCTACCTAATCATGGAGTTCCTGCCTGGAGGGGACATGATGACCTTGTTGATGAAA
AAAGACACTCTGACAGAAGAGGAGACTCAGTTTTATATAGCAGAAACAGTATTAGCCATA
GACTCTATTCACCAACTTGGATTCATCCACAGAGACATCAAACCAGACAACCTTCTTTTG
GACAGCAAGGGCCATGTGAAACTTTCTGACTTTGGTCTTTGCACAGGACTGAAAAAAGCA
CATAGGACAGAATTTTATAGGAATCTGAACCACAGCCTCCCCAGTGATTTCACTTTCCAG
AACATGAATTCCAAAAGGAAAGCAGAAACCTGGAAAAGAAATAGACGTCAGCTAGCCTTC
TCCACAGTAGGCACTCCTGACTACATTGCTCCTGAGGTGTTCATGCAGACCGGGTACAAC
AAGCTCTGTGATTGGTGGTCGCTTGGGGTGATCATGTATGAGATGCTCATCGGCTACCCA
CCTTTCTGTTCTGAGACCCCTCAAGAGACATATAAGAAGGTGATGAACTGGAAAGAAACT
TTGACTTTTCCTCCAGAAGTTCCCATCTCTGAGAAAGCCAAGGATCTAATTTTGAGGTTC
TGCTGTGAATGGGAACATAGAATTGGAGCTCCTGGAGTTGAGGAAATAAAAAGTAACTCT
TTTTTTGAAGGCGTTGACTGGGAACATATCAGAGAGAGACCTGCTGCAATATCTATTGAA
ATCAAAAGCATTGATGATACCTCAAACTTCGATGAGTTTCCAGAATCTGATATTCTTAAG
CCAACAGTGGCCACAAGTAATCATCCTGAGACTGACTACAAGAACAAAGACTGGGTCTTC
ATCAATTACACGTACAAGCGCTTTGAGGGCCTGACTGCAAGGGGGGCAATACCTTCCTAC
ATGAAAGCAGCAAAATAG
Enzyme 113 GenBank Gene ID BC012085 Link Image
Enzyme 113 GeneCard ID STK38 Link Image
Enzyme 113 GenAtlas ID STK38 Link Image
Enzyme 113 HGNC ID HGNC:17847 Link Image
Enzyme 113 Chromosome Location 6
Enzyme 113 Locus 6p21
Enzyme 113 SNPs SNPJam Report Link Image
Enzyme 113 General References
  1. Millward T, Cron P, Hemmings BA: Molecular cloning and characterization of a conserved nuclear serine(threonine) protein kinase. Proc Natl Acad Sci U S A. 1995 May 23;92(11):5022-6. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Tamaskovic R, Bichsel SJ, Rogniaux H, Stegert MR, Hemmings BA: Mechanism of Ca2+-mediated regulation of NDR protein kinase through autophosphorylation and phosphorylation by an upstream kinase. J Biol Chem. 2003 Feb 28;278(9):6710-8. Epub 2002 Dec 17. [PubMed Link Image]
  5. Devroe E, Erdjument-Bromage H, Tempst P, Silver PA: Human Mob proteins regulate the NDR1 and NDR2 serine-threonine kinases. J Biol Chem. 2004 Jun 4;279(23):24444-51. Epub 2004 Apr 2. [PubMed Link Image]
  6. Bichsel SJ, Tamaskovic R, Stegert MR, Hemmings BA: Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase by the hMOB1 protein. J Biol Chem. 2004 Aug 20;279(34):35228-35. Epub 2004 Jun 14. [PubMed Link Image]
  7. Takeuchi T, Inoue S, Yokosawa H: Identification and Herc5-mediated ISGylation of novel target proteins. Biochem Biophys Res Commun. 2006 Sep 22;348(2):473-7. Epub 2006 Jul 28. [PubMed Link Image]
  8. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  9. Fujiki R, Chikanishi T, Hashiba W, Ito H, Takada I, Roeder RG, Kitagawa H, Kato S: GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis. Nature. 2009 May 21;459(7245):455-9. Epub 2009 Apr 19. [PubMed Link Image]
  10. Enomoto A, Kido N, Ito M, Morita A, Matsumoto Y, Takamatsu N, Hosoi Y, Miyagawa K: Negative regulation of MEKK1/2 signaling by serine-threonine kinase 38 (STK38). Oncogene. 2008 Mar 20;27(13):1930-8. Epub 2007 Oct 1. [PubMed Link Image]
  11. Bhattacharya S, Large E, Heizmann CW, Hemmings B, Chazin WJ: Structure of the Ca2+/S100B/NDR kinase peptide complex: insights into S100 target specificity and activation of the kinase. Biochemistry. 2003 Dec 16;42(49):14416-26. [PubMed Link Image]
  12. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 113 Metabolite References Not Available
Enzyme 114 [top]
Enzyme 114 ID 6492
Enzyme 114 Name MAP kinase-activated protein kinase 5
Enzyme 114 Synonyms
  1. MAPK-activated protein kinase 5
  2. MAPKAP kinase 5
  3. MAPKAPK-5
  4. p38-regulated/activated protein kinase
Enzyme 114 Gene Name MAPKAPK5
Enzyme 114 Protein Sequence >MAP kinase-activated protein kinase 5 
MSEESDMDKAIKETSILEEYSINWTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKAR
NEVRLHMMCATHPNIVQIIEVFANSVQFPHESSPRARLLIVMEMMEGGELFHRISQHRHF
TEKQASQVTKQIALALRHCHLLNIAHRDLKPENLLFKDNSLDAPVKLCDFGFAKIDQGDL
MTPQFTPYYVAPQVLEAQRRHQKEKSGIIPTSPTPYTYNKSCDLWSLGVIIYVMLCGYPP
FYSKHHSRTIPKDMRRKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLD
HPWLNSTEALDNVLPSAQLMMDKAVVAGIQQAHAEQLANMRIQDLKVSLKPLHSVNNPIL
RKRKLLGTKPKDSVYIHDHENGAEDSNVALEKLRDVIAQCILPQAGKGENEDEKLNEVMQ
EAWKYNRECKLLRDTLQSFSWNGRGFTDKVDRLKLAEIVKQVIEEQTTSHESQ
Enzyme 114 Number of Residues 473
Enzyme 114 Molecular Weight 54220.0
Enzyme 114 Theoretical pI 7.86
Enzyme 114 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
—
Enzyme 114 General Function Involved in protein kinase activity
Enzyme 114 Specific Function Mediates stress-induced small heat shock protein 27 phosphorylation
Enzyme 114 Pathways Not Available
Enzyme 114 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 114 Pfam Domain Function
Enzyme 114 Signals
  • None
Enzyme 114 Transmembrane Regions
  • None
Enzyme 114 Essentiality Not Available
Enzyme 114 GenBank ID Protein 21237768 Link Image
Enzyme 114 UniProtKB/Swiss-Prot ID Q8IW41 Link Image
Enzyme 114 UniProtKB/Swiss-Prot Entry Name MAPK5_HUMAN Link Image
Enzyme 114 PDB ID Not Available
Enzyme 114 Cellular Location Not Available
Enzyme 114 Gene Sequence >1422 bp 
ATGTCGGAGGAGAGCGACATGGACAAAGCCATCAAGGAAACTTCCATTTTAGAAGAATAC
AGTATCAATTGGACTCAGAAGCTGGGAGCTGGAATTAGTGGTCCAGTTAGAGTCTGTGTA
AAGAAATCTACTCAAGAACGGTTTGCGCTGAAAATTCTTCTTGATCGTCCAAAAGCTAGA
AATGAGGTACGTCTGCACATGATGTGTGCCACACACCCAAACATAGTTCAGATTATTGAA
GTGTTTGCTAACAGTGTCCAGTTTCCCCATGAGTCCAGCCCTAGGGCCCGACTCTTAATT
GTAATGGAGATGATGGAAGGGGGAGAGCTATTTCACAGAATCAGCCAGCACCGGCACTTT
ACAGAGAAGCAAGCCAGCCAAGTAACAAAGCAGATAGCTTTGGCTCTGCGGCACTGTCAC
TTGTTAAACATTGCGCACAGAGACCTCAAGCCTGAAAATCTGCTTTTTAAGGATAACTCT
TTGGATGCCCCAGTGAAGTTGTGTGACTTTGGATTTGCCAAGATTGACCAAGGTGACTTG
ATGACACCCCAGTTCACCCCTTATTATGTAGCACCCCAGGTACTGGAGGCGCAAAGAAGG
CATCAGAAGGAGAAATCTGGCATCATACCTACCTCACCGACGCCCTACACTTACAACAAG
AGCTGTGACTTGTGGTCCCTAGGGGTGATTATCTATGTGATGCTGTGCGGATACCCTCCT
TTTTACTCCAAACACCACAGCCGGACTATCCCAAAGGATATGCGAAGAAAGATCATGACA
GGCAGTTTTGAGTTCCCAGAGGAAGAGTGGAGTCAGATCTCAGAGATGGCCAAAGATGTT
GTGAGGAAGCTCCTGAAGGTCAAACCGGAGGAGAGACTCACCATCGAGGGAGTGCTGGAC
CACCCCTGGCTCAATTCCACCGAGGCCCTGGATAATGTGCTGCCTTCTGCTCAGCTGATG
ATGGACAAGGCAGTGGTTGCAGGAATCCAGCAGGCTCACGCGGAACAGTTGGCCAACATG
AGAATCCAGGATCTGAAAGTCAGCCTCAAACCCCTGCACTCAGTGAACAACCCCATTCTG
CGGAAGAGGAAGTTACTTGGCACCAAGCCAAAGGACAGTGTCTATATCCACGACCATGAG
AATGGAGCCGAGGATTCCAATGTTGCCTTGGAAAAACTCCGAGATGTGATTGCTCAGTGT
ATTCTCCCCCAGGCTGGTAAAGGAGAGAATGAAGATGAGAAACTGAATGAAGTAATGCAG
GAGGCTTGGAAGTATAACCGGGAATGCAAACTCCTAAGAGATACTCTGCAGAGCTTCAGC
TGGAATGGTCGTGGATTCACAGATAAAGTAGATCGACTAAAACTGGCAGAAATTGTGAAG
CAGGTGATAGAAGAGCAAACCACGTCCCACGAATCCCAATAA
Enzyme 114 GenBank Gene ID NM_139078.1 Link Image
Enzyme 114 GeneCard ID MAPKAPK5 Link Image
Enzyme 114 GenAtlas ID MAPKAPK5 Link Image
Enzyme 114 HGNC ID HGNC:6889 Link Image
Enzyme 114 Chromosome Location 1
Enzyme 114 Locus 12q24.13
Enzyme 114 SNPs SNPJam Report Link Image
Enzyme 114 General References
  1. New L, Jiang Y, Zhao M, Liu K, Zhu W, Flood LJ, Kato Y, Parry GC, Han J: PRAK, a novel protein kinase regulated by the p38 MAP kinase. EMBO J. 1998 Jun 15;17(12):3372-84. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Sudo T, Maruyama M, Osada H: p62 functions as a p38 MAP kinase regulator. Biochem Biophys Res Commun. 2000 Mar 16;269(2):521-5. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  8. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  9. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 114 Metabolite References Not Available
Enzyme 115 [top]
Enzyme 115 ID 6496
Enzyme 115 Name Plasma membrane calcium-transporting ATPase 1
Enzyme 115 Synonyms
  1. PMCA1
  2. Plasma membrane calcium ATPase isoform 1
  3. Plasma membrane calcium pump isoform 1
Enzyme 115 Gene Name ATP2B1
Enzyme 115 Protein Sequence >Plasma membrane calcium-transporting ATPase 1 
MGDMANNSVAYSGVKNSLKEANHDGDFGITLAELRALMELRSTDALRKIQESYGDVYGIC
TKLKTSPNEGLSGNPADLERREAVFGKNFIPPKKPKTFLQLVWEALQDVTLIILEIAAIV
SLGLSFYQPPEGDNALCGEVSVGEEEGEGETGWIEGAAILLSVVCVVLVTAFNDWSKEKQ
FRGLQSRIEQEQKFTVIRGGQVIQIPVADITVGDIAQVKYGDLLPADGILIQGNDLKIDE
SSLTGESDHVKKSLDKDPLLLSGTHVMEGSGRMVVTAVGVNSQTGIIFTLLGAGGEEEEK
KDEKKKEKKNKKQDGAIENRNKAKAQDGAAMEMQPLKSEEGGDGDEKDKKKANLPKKEKS
VLQGKLTKLAVQIGKAGLLMSAITVIILVLYFVIDTFWVQKRPWLAECTPIYIQYFVKFF
IIGVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTL
TMNRMTVVQAYINEKHYKKVPEPEAIPPNILSYLVTGISVNCAYTSKILPPEKEGGLPRH
VGNKTECALLGLLLDLKRDYQDVRNEIPEEALYKVYTFNSVRKSMSTVLKNSDGSYRIFS
KGASEIILKKCFKILSANGEAKVFRPRDRDDIVKTVIEPMASEGLRTICLAFRDFPAGEP
EPEWDNENDIVTGLTCIAVVGIEDPVRPEVPDAIKKCQRAGITVRMVTGDNINTARAIAT
KCGILHPGEDFLCLEGKDFNRRIRNEKGEIEQERIDKIWPKLRVLARSSPTDKHTLVKGI
IDSTVSDQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVK
AVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTLASL
ALATEPPTESLLLRKPYGRNKPLISRTMMKNILGHAFYQLVVVFTLLFAGEKFFDIDSGR
NAPLHAPPSEHYTIVFNTFVLMQLFNEINARKIHGERNVFEGIFNNAIFCTIVLGTFVVQ
IIIVQFGGKPFSCSELSIEQWLWSIFLGMGTLLWGQLISTIPTSRLKFLKEAGHGTQKEE
IPEEELAEDVEEIDHAERELRRGQILWFRGLNRIQTQMDVVNAFQSGSSIQGALRRQPSI
ASQHHDVTNISTPTHIRVVNAFRSSLYEGLEKPESRSSIHNFMTHPEFRIEDSEPHIPLI
DDTDAEDDAPTKRNSSPPPSPNKNNNAVDSGIHLTIEMNKSATSSSPGSPLHSLETSL
Enzyme 115 Number of Residues 1258
Enzyme 115 Molecular Weight 138754.0
Enzyme 115 Theoretical pI 5.88
Enzyme 115 GO Classification
Function
  • ATP binding
  • ATPase activity, coupled to transmembrane movement of ions
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • calcium ion transmembrane transporter activity
  • calcium-transporting ATPase activity
  • catalytic activity
  • cation transmembrane transporter activity
  • di-, tri-valent inorganic cation transmembrane transporter activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • inorganic cation transmembrane transporter activity
  • ion transmembrane transporter activity
  • nucleoside binding
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • calcium ion transport
  • cation transport
  • cellular nitrogen compound metabolic process
  • di-, tri-valent inorganic cation transport
  • divalent metal ion transport
  • establishment of localization
  • ion transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • transport
Component
  • cell part
  • membrane
Enzyme 115 General Function Involved in ATP binding
Enzyme 115 Specific Function This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell
Enzyme 115 Pathways Not Available
Enzyme 115 Reactions
  • ATP + H2O + Ca2+cis = ADP + phosphate + Ca2+trans [RN:R00086]
Enzyme 115 Pfam Domain Function
Enzyme 115 Signals
  • None
Enzyme 115 Transmembrane Regions
  • 98-118 155-175 367-386 420-437 853-872 883-903 924-946 965-986 1006-1027 1038-1059
Enzyme 115 Essentiality Not Available
Enzyme 115 GenBank ID Protein 48255945 Link Image
Enzyme 115 UniProtKB/Swiss-Prot ID P20020 Link Image
Enzyme 115 UniProtKB/Swiss-Prot Entry Name AT2B1_HUMAN Link Image
Enzyme 115 PDB ID Not Available
Enzyme 115 Cellular Location Not Available
Enzyme 115 Gene Sequence >3663 bp 
ATGGGCGACATGGCAAACAACTCAGTTGCTTACAGTGGTGTGAAAAACTCTTTGAAGGAA
GCTAATCATGATGGAGACTTTGGAATTACGCTCGCAGAGCTGCGGGCTCTCATGGAGCTC
AGGTCCACAGATGCATTACGAAAAATACAGGAAAGCTATGGAGATGTCTATGGAATTTGC
ACCAAATTGAAAACATCTCCCAATGAAGGTTTAAGTGGAAACCCTGCAGATTTAGAAAGA
AGAGAAGCAGTGTTTGGAAAGAATTTTATACCTCCTAAAAAGCCAAAAACCTTTCTTCAA
TTAGTATGGGAAGCATTACAAGATGTCACTTTAATTATATTAGAAATTGCAGCCATAGTA
TCATTGGGCCTTTCTTTTTATCAGCCTCCAGAAGGGGATAATGCACTTTGTGGAGAAGTT
TCTGTTGGGGAGGAAGAAGGTGAAGGTGAAACTGGTTGGATTGAAGGAGCTGCAATCCTC
TTGTCTGTAGTGTGTGTGGTGTTAGTAACAGCTTTCAATGACTGGAGTAAGGAAAAACAG
TTTAGAGGTTTGCAGAGCCGAATTGAACAAGAACAGAAGTTCACTGTCATCAGGGGTGGT
CAGGTCATTCAGATACCTGTAGCTGACATTACTGTTGGAGATATTGCTCAAGTGAAATAT
GGTGATCTTCTTCCAGCTGACGGCATACTTATTCAAGGCAACGATCTTAAAATTGATGAA
AGCTCATTGACTGGTGAATCAGATCATGTTAAAAAGTCTTTAGATAAGGATCCCTTACTT
CTATCAGGTACTCATGTAATGGAAGGCTCTGGAAGAATGGTAGTTACAGCTGTAGGTGTA
AATTCTCAAACTGGAATTATCTTTACCTTACTTGGAGCTGGAGGTGAAGAGGAAGAGAAG
AAAGATGAGAAGAAAAAGGAAAAGAAAAATAAGAAACAAGATGGAGCTATTGAGAATCGC
AACAAAGCAAAAGCCCAGGATGGTGCAGCCATGGAAATGCAGCCATTGAAGAGTGAAGAA
GGTGGAGATGGTGATGAAAAAGATAAAAAGAAAGCAAATTTGCCAAAAAAGGAAAAATCT
GTTTTACAAGGGAAACTTACAAAACTGGCTGTTCAGATTGGCAAAGCAGGTCTGTTGATG
TCTGCCATCACAGTTATCATTCTAGTATTATATTTTGTCATTGACACCTTCTGGGTTCAG
AAAAGACCATGGCTTGCTGAGTGCACACCAATTTATATACAATACTTTGTGAAGTTCTTC
ATTATTGGAGTTACAGTTTTAGTGGTCGCAGTGCCAGAAGGTCTTCCACTTGCAGTCACG
ATCTCACTGGCTTATTCAGTCAAAAAAATGATGAAAGATAATAACTTAGTAAGGCATCTG
GATGCTTGTGAAACCATGGGAAATGCTACAGCTATTTGTTCAGATAAAACAGGAACTTTG
ACAATGAACAGAATGACAGTCGTTCAAGCTTACATAAATGAAAAACATTATAAAAAGGTT
CCTGAACCAGAAGCTATTCCACCAAATATTTTGTCCTATCTTGTAACAGGAATTTCTGTG
AATTGTGCTTATACATCAAAAATATTGCCACCAGAGAAAGAGGGTGGATTACCTCGTCAC
GTTGGTAATAAAACTGAATGTGCCTTGTTGGGACTTCTTTTGGATTTAAAACGGGATTAT
CAGGATGTTAGAAATGAAATACCAGAAGAAGCACTGTACAAAGTCTACACCTTCAATTCT
GTTAGGAAGTCCATGAGTACTGTCCTGAAAAATTCAGATGGAAGTTATCGAATATTCAGC
AAGGGTGCATCTGAGATAATTCTGAAAAAGTGTTTCAAAATCTTGAGTGCTAATGGTGAG
GCAAAAGTATTCAGACCAAGGGACCGTGATGATATTGTAAAAACTGTGATTGAACCGATG
GCATCAGAAGGCTTGAGAACCATATGTCTTGCATTCAGAGATTTTCCAGCAGGAGAACCA
GAACCAGAGTGGGATAATGAAAATGATATTGTCACCGGCCTTACATGCATTGCTGTTGTG
GGGATTGAAGATCCTGTGAGACCTGAGGTGCCAGATGCAATTAAAAAGTGTCAGAGGGCT
GGAATTACTGTGCGGATGGTCACTGGTGATAATATTAATACTGCTCGGGCCATTGCTACC
AAATGTGGTATTTTACATCCTGGGGAAGATTTTCTGTGCCTAGAAGGTAAAGATTTTAAC
AGAAGAATACGAAATGAAAAAGGAGAGATTGAGCAAGAGAGGATAGACAAGATTTGGCCA
AAACTTCGAGTACTTGCAAGATCATCTCCTACTGATAAGCATACACTGGTTAAAGGTATA
ATTGACAGCACTGTCTCAGACCAACGCCAGGTTGTAGCTGTAACTGGTGATGGTACAAAT
GATGGCCCAGCACTAAAGAAAGCAGATGTTGGATTTGCAATGGGTATTGCTGGAACTGAT
GTAGCTAAAGAAGCATCCGATATTATTCTCACAGATGACAACTTTACAAGCATTGTTAAA
GCAGTTATGTGGGGACGAAATGTCTATGACAGCATCTCAAAATTCCTTCAGTTCCAACTT
ACTGTTAATGTAGTAGCAGTGATTGTTGCTTTTACGGGCGCCTGCATTACTCAAGACTCA
CCGCTTAAGGCTGTGCAGATGCTGTGGGTAAACCTCATAATGGATACACTCGCTTCCCTG
GCTCTGGCAACGGAACCACCCACTGAGTCTCTCTTGCTTCGGAAACCTTATGGTAGAAAT
AAGCCTCTCATCTCACGTACAATGATGAAGAATATTTTGGGTCATGCATTCTATCAACTT
GTAGTAGTCTTTACACTCTTATTTGCTGGAGAAAAGTTTTTTGACATTGATAGTGGAAGA
AATGCTCCTTTGCATGCTCCTCCTTCAGAACATTATACTATTGTTTTTAATACCTTTGTG
CTGATGCAACTTTTCAACGAAATAAATGCCCGGAAAATTCATGGTGAAAGAAATGTATTC
GAAGGAATCTTTAACAATGCCATCTTCTGCACAATTGTTTTAGGCACTTTTGTGGTACAG
ATAATAATTGTGCAGTTTGGTGGAAAACCTTTCAGTTGTTCAGAACTTTCAATAGAACAG
TGGCTATGGTCAATATTCCTAGGAATGGGAACATTACTCTGGGGCCAGCTTATTTCAACA
ATTCCAACTAGCCGTTTAAAATTCCTCAAAGAAGCTGGTCATGGAACACAAAAGGAAGAA
ATACCTGAGGAGGAATTAGCAGAGGATGTTGAAGAGATTGATCACGCTGAAAGGGAGTTG
CGGCGTGGCCAAATCTTGTGGTTTAGAGGTCTGAACAGAATCCAAACACAGATTCGAGTG
GTGAATGCATTTCGTAGTTCTTTATATGAAGGGTTAGAAAAACCGGAATCAAGAAGTTCG
ATTCACAACTTTATGACACATCCTGAGTTTAGGATAGAAGATTCAGAGCCTCATATCCCC
CTTATTGATGACACTGATGCCGAAGATGATGCTCCTACAAAACGTAACTCCAGTCCTCCA
CCCTCTCCCAACAAAAATAACAATGCTGTTGACAGTGGAATTCACCTTACAATAGAAATG
AACAAGTCTGCTACCTCTTCATCCCCAGGAAGCCCACTACATAGTTTGGAAACATCACTC
TGA
Enzyme 115 GenBank Gene ID Not Available
Enzyme 115 GeneCard ID ATP2B1 Link Image
Enzyme 115 GenAtlas ID ATP2B1 Link Image
Enzyme 115 HGNC ID HGNC:814 Link Image
Enzyme 115 Chromosome Location 1
Enzyme 115 Locus 12q21.3
Enzyme 115 SNPs SNPJam Report Link Image
Enzyme 115 General References
  1. Verma AK, Filoteo AG, Stanford DR, Wieben ED, Penniston JT, Strehler EE, Fischer R, Heim R, Vogel G, Mathews S, et al.: Complete primary structure of a human plasma membrane Ca2+ pump. J Biol Chem. 1988 Oct 5;263(28):14152-9. [PubMed Link Image]
  2. Kumar R, Haugen JD, Penniston JT: Molecular cloning of a plasma membrane calcium pump from human osteoblasts. J Bone Miner Res. 1993 Apr;8(4):505-13. [PubMed Link Image]
  3. Hilfiker H, Strehler-Page MA, Stauffer TP, Carafoli E, Strehler EE: Structure of the gene encoding the human plasma membrane calcium pump isoform 1. J Biol Chem. 1993 Sep 15;268(26):19717-25. [PubMed Link Image]
  4. Strehler EE, Strehler-Page MA, Vogel G, Carafoli E: mRNAs for plasma membrane calcium pump isoforms differing in their regulatory domain are generated by alternative splicing that involves two internal donor sites in a single exon. Proc Natl Acad Sci U S A. 1989 Sep;86(18):6908-12. [PubMed Link Image]
  5. Kessler F, Falchetto R, Heim R, Meili R, Vorherr T, Strehler EE, Carafoli E: Study of calmodulin binding to the alternatively spliced C-terminal domain of the plasma membrane Ca2+ pump. Biochemistry. 1992 Dec 1;31(47):11785-92. [PubMed Link Image]
  6. Stauffer TP, Hilfiker H, Carafoli E, Strehler EE: Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes. J Biol Chem. 1993 Dec 5;268(34):25993-6003. [PubMed Link Image]
  7. Stauffer TP, Hilfiker H, Carafoli E, Strehler EE: Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes. J Biol Chem. 1994 Dec 16;269(50):32022. [PubMed Link Image]
  8. Howard A, Legon S, Walters JR: Human and rat intestinal plasma membrane calcium pump isoforms. Am J Physiol. 1993 Nov;265(5 Pt 1):G917-25. [PubMed Link Image]
  9. James PH, Pruschy M, Vorherr TE, Penniston JT, Carafoli E: Primary structure of the cAMP-dependent phosphorylation site of the plasma membrane calcium pump. Biochemistry. 1989 May 16;28(10):4253-8. [PubMed Link Image]
  10. Wang KK, Wright LC, Machan CL, Allen BG, Conigrave AD, Roufogalis BD: Protein kinase C phosphorylates the carboxyl terminus of the plasma membrane Ca(2+)-ATPase from human erythrocytes. J Biol Chem. 1991 May 15;266(14):9078-85. [PubMed Link Image]
  11. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  12. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  13. Benkwitz C, Kubisch C, Kraft K, Neyses L: Investigation of the Met-267 Arg exchange in isoform 1 of the human plasma membrane calcium pump in patients with essential hypertension by the amplification-created restriction site technique. J Mol Med. 1997 Jan;75(1):62-6. [PubMed Link Image]
Enzyme 115 Metabolite References Not Available
Enzyme 116 [top]
Enzyme 116 ID 6509
Enzyme 116 Name Myosin light chain kinase 2, skeletal/cardiac muscle
Enzyme 116 Synonyms
  1. MLCK2
Enzyme 116 Gene Name MYLK2
Enzyme 116 Protein Sequence >Myosin light chain kinase 2, skeletal/cardiac muscle 
MATENGAVELGIQNPSTDKAPKGPTGERPLAAGKDPGPPDPKKAPDPPTLKKDAKAPASE
KGDGTLAQPSTSSQGPKGEGDRGGGPAEGSAGPPAALPQQTATPETSVKKPKAEQGASGS
QDPGKPRVGKKAAEGQAAARRGSPAFLHSPSCPAIISSSEKLLAKKPPSEASELTFEGVP
MTHSPTDPRPAKAEEGKNILAESQKEVGEKTPGQAGQAKMQGDTSRGIEFQAVPSEKSEV
GQALCLTAREEDCFQILDDCPPPPAPFPHRMVELRTGNVSSEFSMNSKEALGGGKFGAVC
TCMEKATGLKLAAKVIKKQTPKDKEMVLLEIEVMNQLNHRNLIQLYAAIETPHEIVLFME
YIEGGELFERIVDEDYHLTEVDTMVFVRQICDGILFMHKMRVLHLDLKPENILCVNTTGH
LVKIIDFGLARRYNPNEKLKVNFGTPEFLSPEVVNYDQISDKTDMWSMGVITYMLLSGLS
PFLGDDDTETLNNVLSGNWYFDEETFEAVSDEAKDFVSNLIVKDQRARMNAAQCLAHPWL
NNLAEKAKRCNRRLKSQILLKKYLMKRRWKKNFIAVSAANRFKKISSSGALMALGV
Enzyme 116 Number of Residues 596
Enzyme 116 Molecular Weight 64684.3
Enzyme 116 Theoretical pI 7.03
Enzyme 116 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
—
Enzyme 116 General Function Involved in protein serine/threonine kinase activity
Enzyme 116 Specific Function Implicated in the level of global muscle contraction and cardiac function. Phosphorylates a specific serine in the N- terminus of a myosin light chain
Enzyme 116 Pathways Not Available
Enzyme 116 Reactions
  • ATP + [myosin light chain] = ADP + [myosin light chain] phosphate [RN:R03150]
Enzyme 116 Pfam Domain Function
Enzyme 116 Signals
  • None
Enzyme 116 Transmembrane Regions
  • None
Enzyme 116 Essentiality Not Available
Enzyme 116 GenBank ID Protein 13194657 Link Image
Enzyme 116 UniProtKB/Swiss-Prot ID Q9H1R3 Link Image
Enzyme 116 UniProtKB/Swiss-Prot Entry Name MYLK2_HUMAN Link Image
Enzyme 116 PDB ID Not Available
Enzyme 116 Cellular Location Not Available
Enzyme 116 Gene Sequence >1791 bp 
ATGGCGACAGAAAATGGAGCAGTTGAGCTGGGAATTCAGAACCCATCAACAGACAAGGCA
CCTAAAGGTCCCACAGGTGAAAGACCCCTGGCTGCAGGGAAAGACCCTGGCCCCCCAGAC
CCAAAGAAAGCTCCGGATCCACCCACCCTGAAGAAAGATGCCAAAGCCCCTGCCTCAGAG
AAAGGGGATGGTACCCTGGCCCAACCCTCAACTAGCAGCCAAGGCCCCAAAGGAGAGGGT
GACAGGGGCGGGGGGCCCGCGGAGGGCAGTGCTGGGCCCCCGGCAGCCCTGCCCCAGCAG
ACTGCGACACCTGAGACCAGCGTCAAGAAGCCCAAGGCTGAGCAGGGAGCCTCAGGCAGC
CAGGATCCTGGAAAGCCCAGGGTGGGCAAGAAGGCAGCAGAGGGCCAAGCAGCAGCCAGG
AGGGGCTCACCTGCCTTTCTGCATAGCCCCAGCTGTCCTGCCATCATCTCCAGTTCTGAG
AAGCTGCTGGCCAAGAAGCCCCCAAGCGAGGCATCAGAGCTCACCTTTGAAGGGGTGCCC
ATGACCCACAGCCCCACGGATCCCAGGCCAGCCAAGGCAGAAGAAGGAAAGAACATCCTG
GCAGAGAGCCAGAAGGAAGTGGGAGAGAAAACCCCAGGCCAGGCTGGCCAGGCTAAGATG
CAAGGGGACACCTCGAGGGGGATTGAGTTCCAGGCTGTTCCCTCAGAGAAATCCGAGGTG
GGGCAGGCCCTCTGTCTCACAGCCAGGGAGGAGGACTGCTTCCAGATTTTGGATGATTGC
CCGCCACCTCCGGCCCCCTTCCCTCACCGCATGGTGGAGCTGAGGACCGGGAATGTCAGC
AGTGAATTCAGTATGAACTCCAAGGAGGCGCTCGGAGGTGGCAAGTTTGGGGCAGTCTGT
ACCTGCATGGAGAAAGCCACAGGCCTCAAGCTGGCAGCCAAGGTCATCAAGAAACAGACT
CCCAAAGACAAGGAAATGGTGTTGCTGGAGATTGAGGTCATGAACCAGCTGAACCACCGC
AATCTGATCCAGCTGTATGCAGCCATCGAGACTCCGCATGAGATCGTCCTGTTCATGGAG
TACATCGAGGGCGGAGAGCTCTTCGAGAGGATTGTGGATGAGGACTACCATCTGACCGAG
GTGGACACCATGGTGTTTGTCAGGCAGATCTGTGACGGGATCCTCTTCATGCACAAGATG
AGGGTTTTGCACCTGGACCTCAAGCCAGAGAACATCCTGTGTGTCAACACCACCGGGCAT
TTGGTGAAGATCATTGACTTTGGCCTGGCACGGAGGTATAACCCCAACGAGAAGCTGAAG
GTGAACTTTGGGACCCCAGAGTTCCTGTCACCTGAGGTGGTGAATTATGACCAAATCTCC
GATAAGACAGACATGTGGAGTATGGGGGTGATCACCTACATGCTGCTGAGCGGCCTCTCC
CCCTTCCTGGGAGATGATGACACAGAGACCCTAAACAACGTTCTATCTGGCAACTGGTAC
TTTGATGAAGAGACCTTTGAGGCCGTATCAGACGAGGCCAAAGACTTTGTCTCCAACCTC
ATCGTCAAGGACCAGAGGGCCCGGATGAACGCTGCCCAGTGTCTCGCCCATCCCTGGCTC
AACAACCTGGCGGAGAAAGCCAAACGCTGTAACCGACGCCTTAAGTCCCAGATCTTGCTT
AAGAAATACCTCATGAAGAGGCGCTGGAAGAAAAACTTCATTGCTGTCAGCGCTGCCAAC
CGCTTCAAGAAGATCAGCAGCTCGGGGGCACTGATGGCTCTGGGGGTCTGA
Enzyme 116 GenBank Gene ID AF325549 Link Image
Enzyme 116 GeneCard ID MYLK2 Link Image
Enzyme 116 GenAtlas ID MYLK2 Link Image
Enzyme 116 HGNC ID HGNC:16243 Link Image
Enzyme 116 Chromosome Location 2
Enzyme 116 Locus 20q13.31
Enzyme 116 SNPs SNPJam Report Link Image
Enzyme 116 General References
  1. Davis JS, Hassanzadeh S, Winitsky S, Lin H, Satorius C, Vemuri R, Aletras AH, Wen H, Epstein ND: The overall pattern of cardiac contraction depends on a spatial gradient of myosin regulatory light chain phosphorylation. Cell. 2001 Nov 30;107(5):631-41. [PubMed Link Image]
  2. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 116 Metabolite References Not Available
Enzyme 117 [top]
Enzyme 117 ID 6517
Enzyme 117 Name Calcium/calmodulin-dependent protein kinase type 1D
Enzyme 117 Synonyms
  1. CaM kinase I delta
  2. CaM kinase ID
  3. CaM-KI delta
  4. CaMKI delta
  5. CaMKI-like protein kinase
  6. CKLiK
Enzyme 117 Gene Name CAMK1D
Enzyme 117 Protein Sequence >Calcium/calmodulin-dependent protein kinase type 1D 
MARENGESSSSWKKQAEDIKKIFEFKETLGTGAFSEVVLAEEKATGKLFAVKCIPKKALK
GKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSGGELFDRIVEKGFYTEKD
ASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYYSQDEESKIMISDFGLSKMEGKGDVMST
ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAEYEF
DSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQAARHPWIAGDTALNKNIHESVSAQIRKN
FAKSKWRQAFNATAVVRHMRKLHLGSSLDSSNASVSSSLSLASQKDCLAPSTLCSFISSS
SGVSGVGAERRPRPTTVTAVHSGSK
Enzyme 117 Number of Residues 385
Enzyme 117 Molecular Weight 42913.4
Enzyme 117 Theoretical pI 7.23
Enzyme 117 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
—
Enzyme 117 General Function Involved in protein kinase activity
Enzyme 117 Specific Function Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade. May regulate calcium-mediated granulocyte function. May play a role in apoptosis of erythroleukemia cells. Activates MAP kinase MAPK3. In vitro, phosphorylates transcription factor CREM isoform Beta and probably CREB1
Enzyme 117 Pathways Not Available
Enzyme 117 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 117 Pfam Domain Function
Enzyme 117 Signals
  • None
Enzyme 117 Transmembrane Regions
  • None
Enzyme 117 Essentiality Not Available
Enzyme 117 GenBank ID Protein Not Available
Enzyme 117 UniProtKB/Swiss-Prot ID Q8IU85 Link Image
Enzyme 117 UniProtKB/Swiss-Prot Entry Name KCC1D_HUMAN Link Image
Enzyme 117 PDB ID Not Available
Enzyme 117 Cellular Location Not Available
Enzyme 117 Gene Sequence >1158 bp 
ATGGCCCGGGAGAACGGCGAGAGCAGCTCCTCCTGGAAAAAGCAAGCTGAAGACATCAAG
AAGATCTTCGAGTTCAAAGAGACCCTCGGAACCGGGGCCTTTTCCGAAGTGGTTTTAGCT
GAAGAGAAGGCAACTGGCAAGCTCTTTGCTGTGAAGTGTATCCCTAAGAAGGCGCTGAAG
GGCAAGGAAAGCAGCATAGAGAATGAGATAGCCGTCCTGAGAAAGATTAAGCATGAAAAT
ATTGTTGCCCTGGAAGACATTTATGAAAGCCCAAATCACCTGTACTTGGTCATGCAGCTG
GTGTCCGGTGGAGAGCTGTTTGACCGGATAGTGGAGAAGGGGTTTTATACAGAGAAGGAT
GCCAGCACTCTGATCCGCCAAGTCTTGGACGCCGTGTACTATCTCCACAGAATGGGCATC
GTCCACAGAGACCTCAAGCCCGAAAATCTCTTGTACTACAGTCAAGATGAGGAGTCCAAA
ATAATGATCAGTGACTTTGGATTGTCAAAAATGGAGGGCAAAGGAGATGTGATGTCCACT
GCCTGTGGAACTCCAGGCTATGTCGCTCCTGAAGTCCTCGCCCAGAAACCTTACAGCAAA
GCCGTTGACTGCTGGTCCATCGGAGTGATTGCCTACATCTTGCTCTGCGGCTACCCTCCT
TTTTATGATGAAAATGACTCCAAGCTCTTTGAGCAGATCCTCAAGGCGGAATATGAGTTT
GACTCTCCCTACTGGGATGACATCTCCGACTCTGCAAAAGACTTCATTCGGAACCTGATG
GAGAAGGACCCGAATAAAAGATACACGTGTGAGCAGGCAGCTCGGCACCCATGGATCGCT
GGTGACACAGCCCTCAACAAAAACATCCACGAGTCCGTCAGCGCCCAGATCCGGAAAAAC
TTTGCCAAGAGCAAATGGAGACAAGCATTTAATGCCACGGCCGTCGTGAGACATATGAGA
AAACTACACCTCGGCAGCAGCCTGGACAGTTCAAATGCAAGTGTTTCGAGCAGCCTCAGT
TTGGCCAGCCAAAAAGACTGTCTGGCACCTTCCACGCTCTGTAGTTTCATTTCTTCTTCG
TCGGGGGTCTCAGGAGTTGGAGCCGAGCGGAGACCCAGGCCCACCACTGTGACGGCAGTG
CACTCTGGAAGCAAGTGA
Enzyme 117 GenBank Gene ID AB081726 Link Image
Enzyme 117 GeneCard ID CAMK1D Link Image
Enzyme 117 GenAtlas ID CAMK1D Link Image
Enzyme 117 HGNC ID HGNC:19341 Link Image
Enzyme 117 Chromosome Location 1
Enzyme 117 Locus 10p13
Enzyme 117 SNPs SNPJam Report Link Image
Enzyme 117 General References
  1. Ishikawa Y, Tokumitsu H, Inuzuka H, Murata-Hori M, Hosoya H, Kobayashi R: Identification and characterization of novel components of a Ca2+/calmodulin-dependent protein kinase cascade in HeLa cells. FEBS Lett. 2003 Aug 28;550(1-3):57-63. [PubMed Link Image]
  2. Verploegen S, Lammers JW, Koenderman L, Coffer PJ: Identification and characterization of CKLiK, a novel granulocyte Ca(++)/calmodulin-dependent kinase. Blood. 2000 Nov 1;96(9):3215-23. [PubMed Link Image]
  3. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  6. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 117 Metabolite References Not Available
Enzyme 118 [top]
Enzyme 118 ID 6522
Enzyme 118 Name Plasma membrane calcium-transporting ATPase 2
Enzyme 118 Synonyms
  1. PMCA2
  2. Plasma membrane calcium ATPase isoform 2
  3. Plasma membrane calcium pump isoform 2
Enzyme 118 Gene Name ATP2B2
Enzyme 118 Protein Sequence >Plasma membrane calcium-transporting ATPase 2 
MGDMTNSDFYSKNQRNESSHGGEFGCTMEELRSLMELRGTEAVVKIKETYGDTEAICRRL
KTSPVEGLPGTAPDLEKRKQIFGQNFIPPKKPKTFLQLVWEALQDVTLIILEIAAIISLG
LSFYHPPGEGNEGCATAQGGAEDEGEAEAGWIEGAAILLSVICVVLVTAFNDWSKEKQFR
GLQSRIEQEQKFTVVRAGQVVQIPVAEIVVGDIAQVKYGDLLPADGLFIQGNDLKIDESS
LTGESDQVRKSVDKDPMLLSGTHVMEGSGRMLVTAVGVNSQTGIIFTLLGAGGEEEEKKD
KKGVKKGDGLQLPAADGAAASNAADSANASLVNGKMQDGNVDASQSKAKQQDGAAAMEMQ
PLKSAEGGDADDRKKASMHKKEKSVLQGKLTKLAVQIGKAGLVMSAITVIILVLYFTVDT
FVVNKKPWLPECTPVYVQYFVKFFIIGVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNL
VRHLDACETMGNATAICSDKTGTLTTNRMTVVQAYVGDVHYKEIPDPSSINTKTMELLIN
AIAINSAYTTKILPPEKEGALPRQVGNKTECGLLGFVLDLKQDYEPVRSQMPEEKLYKVY
TFNSVRKSMSTVIKLPDESFRMYSKGASEIVLKKCCKILNGAGEPRVFRPRDRDEMVKKV
IEPMACDGLRTICVAYRDFPSSPEPDWDNENDILNELTCICVVGIEDPVRPEVPEAIRKC
QRAGITVRMVTGDNINTARAIAIKCGIIHPGEDFLCLEGKEFNRRIRNEKGEIEQERIDK
IWPKLRVLARSSPTDKHTLVKGIIDSTHTEQRQVVAVTGDGTNDGPALKKADVGFAMGIA
GTDVAKEASDIILTDDNFSSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACIT
QDSPLKAVQMLWVNLIMDTFASLALATEPPTETLLLRKPYGRNKPLISRTMMKNILGHAV
YQLALIFTLLFVGEKMFQIDSGRNAPLHSPPSEHYTIIFNTFVMMQLFNEINARKIHGER
NVFDGIFRNPIFCTIVLGTFAIQIVIVQFGGKPFSCSPLQLDQWMWCIFIGLGELVWGQV
IATIPTSRLKFLKEAGRLTQKEEIPEEELNEDVEEIDHAERELRRGQILWFRGLNRIQTQ
IRVVKAFRSSLYEGLEKPESRTSIHNFMAHPEFRIEDSQPHIPLIDDTDLEEDAALKQNS
SPPSSLNKNNSAIDSGINLTTDTSKSATSSSPGSPIHSLETSL
Enzyme 118 Number of Residues 1243
Enzyme 118 Molecular Weight 136875.2
Enzyme 118 Theoretical pI 5.68
Enzyme 118 GO Classification
Function
  • ATP binding
  • ATPase activity, coupled to transmembrane movement of ions
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • calcium ion transmembrane transporter activity
  • calcium-transporting ATPase activity
  • catalytic activity
  • cation transmembrane transporter activity
  • di-, tri-valent inorganic cation transmembrane transporter activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • inorganic cation transmembrane transporter activity
  • ion transmembrane transporter activity
  • nucleoside binding
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • calcium ion transport
  • cation transport
  • cellular nitrogen compound metabolic process
  • di-, tri-valent inorganic cation transport
  • divalent metal ion transport
  • establishment of localization
  • ion transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • transport
Component
  • cell part
  • membrane
Enzyme 118 General Function Involved in ATP binding
Enzyme 118 Specific Function This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell
Enzyme 118 Pathways Not Available
Enzyme 118 Reactions
  • ATP + H2O + Ca2+cis = ADP + phosphate + Ca2+trans [RN:R00086]
Enzyme 118 Pfam Domain Function
Enzyme 118 Signals
  • None
Enzyme 118 Transmembrane Regions
  • 95-115 153-173 391-410 444-461 876-895 906-926 947-969 988-1009 1029-1050 1061-1082
Enzyme 118 Essentiality Not Available
Enzyme 118 GenBank ID Protein 48255951 Link Image
Enzyme 118 UniProtKB/Swiss-Prot ID Q01814 Link Image
Enzyme 118 UniProtKB/Swiss-Prot Entry Name AT2B2_HUMAN Link Image
Enzyme 118 PDB ID Not Available
Enzyme 118 Cellular Location Not Available
Enzyme 118 Gene Sequence >3732 bp 
ATGGGTGACATGACCAACAGCGACTTTTACTCCAAAAACCAAAGAAATGAGTCGAGCCAT
GGGGGCGAGTTCGGGTGCACAATGGAGGAGCTCCGCTCCCTCATGGAGCTGCGGGGCACT
GAGGCTGTGGTCAAGATCAAGGAGACTTATGGGGACACCGAAGCCATCTGCCGGCGCCTC
AAAACCTCACCTGTTGAAGGTTTGCCGGGCACCGCTCCAGACCTGGAAAAGAGAAAGCAA
ATTTTTGGGCAAAACTTTATACCTCCAAAGAAGCCAAAAACCTTCCTGCAGCTCGTGTGG
GAGGCGCTGCAGGACGTGACGCTCATCATCCTGGAGATTGCCGCCATCATCTCCCTGGGG
CTGTCCTTCTACCACCCGCCCGGCGAGGGCAACGAAGGATGTGCGACGGCCCAGGGTGGG
GCAGAGGATGAAGGAGAGGCAGAGGCAGGTTGGATCGAGGGGGCCGCCATTCTCCTCTCA
GTTATCTGTGTGGTCCTGGTCACGGCCTTCAATGACTGGAGCAAAGAGAAACAGTTCCGG
GGCCTGCAGAGCCGCATCGAGCAGGAACAGAAATTTACCGTGGTCCGGGCTGGCCAGGTG
GTCCAGATCCCTGTGGCTGAGATCGTGGTTGGGGACATAGCCCAGGTCAAATATGGTGAC
CTCCTCCCTGCCGACGGCCTCTTCATCCAGGGCAATGACCTCAAGATTGATGAAAGCTCC
CTAACTGGAGAGTCTGACCAGGTGCGCAAGTCCGTGGACAAGGACCCCATGCTGCTGTCA
GGAACCCACGTGATGGAGGGCTCAGGACGGATGTTGGTGACTGCTGTGGGTGTGAACTCT
CAGACTGGCATCATCTTTACCCTCCTGGGGGCTGGTGGTGAAGAGGAAGAGAAGAAAGAC
AAAAAAGGTGTGAAGAAGGGGGATGGCCTTCAGCTACCAGCAGCAGACGGTGCGGCAGCT
TCAAATGCTGCAGATAGTGCGAATGCCAGCCTAGTCAATGGTAAAATGCAGGATGGCAAT
GTGGACGCCAGCCAGAGCAAAGCCAAACAACAGGACGGGGCAGCCGCCATGGAGATGCAG
CCCCTCAAGAGTGCCGAGGGCGGCGACGCTGACGACAGGAAGAAGGCCAGCATGCACAAG
AAGGAGAAGTCCGTGCTGCAGGGCAAGCTCACCAAGCTGGCTGTGCAGATCGGGAAGGCG
GGCTTGGTGATGTCAGCCATCACGGTGATCATCCTGGTGCTCTACTTCACTGTGGACACC
TTCGTGGTCAACAAGAAGCCGTGGCTGCCTGAGTGCACGCCCGTCTACGTGCAGTACTTT
GTCAAGTTCTTCATCATTGGCGTGACGGTGCTGGTGGTCGCCGTGCCCGAGGGGCTCCCT
CTGGCCGTCACCATCTCGTTGGCCTATTCGGTGAAGAAAATGATGAAGGACAACAACCTG
GTACGCCACCTGGATGCCTGTGAGACCATGGGCAATGCCACAGCCATCTGCTCAGACAAG
ACAGGCACGCTGACCACCAATCGCATGACAGTGGTACAGGCCTATGTCGGCGACGTCCAC
TATAAAGAGATCCCCGACCCCAGCTCCATCAACACCAAGACCATGGAGCTGCTGATCAAT
GCCATCGCCATCAACAGCGCCTACACCACCAAGATTCTGCCCCCAGAGAAGGAGGGCGCC
CTGCCTCGGCAGGTGGGCAACAAGACGGAGTGCGGCCTGCTGGGCTTCGTGCTGGACCTG
AAGCAGGACTACGAGCCCGTGCGCAGCCAGATGCCAGAGGAGAAGTTGTACAAAGTGTAC
ACCTTCAACTCCGTGCGCAAGTCCATGAGCACTGTCATCAAGCTGCCCGACGAGAGCTTC
CGCATGTACAGCAAGGGGGCTTCTGAGATCGTGCTCAAGAAGTGCTGCAAAATCCTCAAT
GGGGCGGGAGAGCCTCGTGTCTTCCGGCCCCGCGACCGGGACGAGATGGTAAAGAAGGTG
ATTGAGCCCATGGCTTGCGATGGGCTCCGCACTATCTGCGTGGCCTACCGCGACTTCCCC
AGCAGCCCGGAGCCGGACTGGGACAATGAGAATGACATCCTCAACGAACTCACCTGCATC
TGCGTGGTGGGCATCGAGGACCCGGTGCGGCCAGAGGTCCCAGAAGCCATCCGCAAGTGC
CAGCGGGCAGGCATCACGGTCCGCATGGTCACTGGCGACAATATCAACACGGCTCGGGCC
ATCGCCATCAAGTGTGGCATCATCCATCCTGGGGAGGACTTTCTGTGCCTCGAGGGCAAG
GAGTTCAACAGGAGGATCCGCAACGAGAAGGGGGAGATTGAGCAGGAGCGAATTGACAAG
ATCTGGCCAAAGCTGCGGGTGCTGGCTCGCTCCTCCCCAACGGACAAGCATACCCTGGTT
AAAGGCATCATCGACAGCACACACACTGAGCAGCGGCAGGTGGTGGCCGTGACGGGGGAC
GGGACCAACGACGGGCCTGCACTCAAGAAGGCCGACGTGGGCTTCGCCATGGGCATCGCA
GGCACTGACGTGGCCAAGGAGGCCTCAGACATCATCCTGACAGACGACAATTTCAGCAGC
ATCGTCAAGGCAGTGATGTGGGGCCGCAACGTCTATGACAGCATCTCCAAATTCTTGCAG
TTCCAGCTCACCGTCAACGTGGTGGCCGTGATTGTGGCCTTCACAGGCGCCTGCATCACG
CAGGACTCCCCTCTGAAGGCCGTGCAGATGCTCTGGGTGAACCTCATCATGGACACGTTT
GCCTCGCTGGCACTGGCCACTGAGCCGCCCACGGAGACCCTGCTGCTGAGGAAGCCGTAC
GGCCGCAACAAGCCGCTCATCTCCAGGACCATGATGAAGAACATCCTGGGCCATGCTGTC
TACCAGCTTGCCCTCATCTTCACCCTGCTCTTTGTTGGCGAGAAGATGTTCCAGATCGAC
AGCGGGAGGAACGCGCCCCTGCATTCGCCACCCTCAGAACATTACACCATCATCTTCAAC
ACCTTCGTCATGATGCAGCTCTTCAACGAGATCAACGCCCGCAAGATCCACGGCGAGCGC
AATGTCTTTGACGGCATCTTCCGGAACCCCATCTTCTGCACCATCGTGCTGGGCACCTTT
GCCATCCAGATAGTGATCGTGCAGTTTGGAGGGAAGCCATTCAGCTGCTCTCCACTGCAG
CTGGACCAGTGGATGTGGTGCATATTCATTGGGTTAGGAGAGCTCGTTTGGGGCCAGGTC
ATCGCCACCATCCCGACCAGCAGACTCAAGTTCCTCAAGGAGGCAGGCAGGCTCACACAG
AAGGAGGAGATCCCGGAGGAGGAGCTCAACGAGGACGTGGAGGAGATCGACCACGCGGAG
CGGGAGCTGCGGCGGGGCCAGATCCTGTGGTTCCGAGGCCTGAATCGGATCCAGACACAG
ATCCGCGTCGTGAAGGCGTTCCGTAGCTCTCTCTATGAAGGTTTAGAAAAGCCTGAATCT
CGAACCTCCATCCATAACTTCATGGCTCATCCTGAATTCCGGATCGAAGATTCCCAGCCC
CACATCCCCCTCATTGATGACACCGACCTGGAAGAAGATGCCGCGCTCAAGCAGAACTCG
AGCCCGCCGTCATCCCTCAACAAGAACAACAGCGCCATCGACAGTGGGATCAACCTGACG
ACCGACACAAGCAAATCAGCTACCTCTTCAAGTCCAGGGAGCCCCATCCACAGCCTGGAG
ACGTCGCTTTAG
Enzyme 118 GenBank Gene ID NM_001001331.2 Link Image
Enzyme 118 GeneCard ID ATP2B2 Link Image
Enzyme 118 GenAtlas ID ATP2B2 Link Image
Enzyme 118 HGNC ID HGNC:815 Link Image
Enzyme 118 Chromosome Location 3
Enzyme 118 Locus 3p25.3
Enzyme 118 SNPs SNPJam Report Link Image
Enzyme 118 General References
  1. Brandt P, Ibrahim E, Bruns GA, Neve RL: Determination of the nucleotide sequence and chromosomal localization of the ATP2B2 gene encoding human Ca(2+)-pumping ATPase isoform PMCA2. Genomics. 1992 Oct;14(2):484-7. [PubMed Link Image]
  2. Latif F, Duh FM, Gnarra J, Tory K, Kuzmin I, Yao M, Stackhouse T, Modi W, Geil L, Schmidt L, et al.: von Hippel-Lindau syndrome: cloning and identification of the plasma membrane Ca(++)-transporting ATPase isoform 2 gene that resides in the von Hippel-Lindau gene region. Cancer Res. 1993 Feb 15;53(4):861-7. [PubMed Link Image]
  3. Heim R, Hug M, Iwata T, Strehler EE, Carafoli E: Microdiversity of human-plasma-membrane calcium-pump isoform 2 generated by alternative RNA splicing in the N-terminal coding region. Eur J Biochem. 1992 Apr 1;205(1):333-40. [PubMed Link Image]
  4. Stauffer TP, Hilfiker H, Carafoli E, Strehler EE: Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes. J Biol Chem. 1993 Dec 5;268(34):25993-6003. [PubMed Link Image]
  5. Stauffer TP, Hilfiker H, Carafoli E, Strehler EE: Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes. J Biol Chem. 1994 Dec 16;269(50):32022. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
Enzyme 118 Metabolite References Not Available
Enzyme 119 [top]
Enzyme 119 ID 6538
Enzyme 119 Name Serine/threonine-protein kinase 38-like
Enzyme 119 Synonyms
  1. NDR2 protein kinase
  2. Nuclear Dbf2-related kinase 2
Enzyme 119 Gene Name STK38L
Enzyme 119 Protein Sequence >Serine/threonine-protein kinase 38-like 
MAMTAGTTTTFPMSNHTRERVTVAKLTLENFYSNLILQHEERETRQKKLEVAMEEEGLAD
EEKKLRRSQHARKETEFLRLKRTRLGLDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKI
LRKSDMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLIMEFLPGGDMMTLLM
KKDTLTEEETQFYISETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKK
AHRTEFYRNLTHNPPSDFSFQNMNSKRKAETWKKNRRQLAYSTVGTPDYIAPEVFMQTGY
NKLCDWWSLGVIMYEMLIGYPPFCSETPQETYRKVMNWKETLVFPPEVPISEKAKDLILR
FCIDSENRIGNSGVEEIKGHPFFEGVDWEHIRERPAAIPIEIKSIDDTSNFDDFPESDIL
QPVPNTTEPDYKSKDWVFLNYTYKRFEGLTQRGSIPTYMKAGKL
Enzyme 119 Number of Residues 464
Enzyme 119 Molecular Weight 54002.4
Enzyme 119 Theoretical pI 6.80
Enzyme 119 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
—
Enzyme 119 General Function Involved in protein serine/threonine kinase activity
Enzyme 119 Specific Function Involved in the regulation of structural processes in differentiating and mature neuronal cells
Enzyme 119 Pathways Not Available
Enzyme 119 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 119 Pfam Domain Function
Enzyme 119 Signals
  • None
Enzyme 119 Transmembrane Regions
  • None
Enzyme 119 Essentiality Not Available
Enzyme 119 GenBank ID Protein 24307971 Link Image
Enzyme 119 UniProtKB/Swiss-Prot ID Q9Y2H1 Link Image
Enzyme 119 UniProtKB/Swiss-Prot Entry Name ST38L_HUMAN Link Image
Enzyme 119 PDB ID Not Available
Enzyme 119 Cellular Location Not Available
Enzyme 119 Gene Sequence >1395 bp 
ATGGCAATGACGGCAGGGACTACAACAACCTTTCCTATGAGCAACCATACCCGGGAAAGA
GTGACTGTAGCCAAGCTCACATTGGAGAATTTTTATAGCAACCTAATTTTACAGCATGAA
GAGAGAGAAACCAGGCAGAAGAAATTAGAAGTGGCCATGGAAGAAGAAGGATTAGCAGAT
GAAGAGAAAAAGTTACGTCGATCACAACACGCTCGCAAAGAAACAGAGTTCTTACGGCTC
AAAAGGACCAGACTTGGCTTGGATGACTTTGAGTCTCTGAAAGTTATAGGAAGAGGAGCT
TTTGGAGAGGTGCGGTTGGTCCAGAAGAAAGATACAGGCCATATCTATGCAATGAAGATA
TTGAGAAAGTCTGATATGCTTGAAAAAGAGCAGGTGGCCCATATCCGAGCAGAAAGAGAT
ATTTTGGTAGAAGCAGATGGTGCCTGGGTGGTGAAGATGTTTTACAGTTTTCAGGATAAG
AGGAATCTTTATCTAATCATGGAATTTCTCCCTGGAGGTGACATGATGACATTGCTAATG
AAGAAAGACACCTTGACAGAAGAGGAAACACAGTTCTACATTTCAGAGACTGTTCTGGCA
ATAGATGCGATCCACCAGTTGGGTTTCATCCATCGGGATATTAAGCCAGACAACCTTTTA
TTGGATGCCAAGGGTCATGTAAAATTATCTGATTTTGGTTTATGTACGGGATTAAAGAAA
GCTCACAGGACTGAATTTTATAGAAATCTCACACACAACCCACCAAGTGACTTCTCATTT
CAGAACATGAACTCAAAGAGGAAAGCAGAAACTTGGAAGAAGAACAGGAGACAACTGGCA
TATTCCACAGTTGGGACACCAGATTACATTGCTCCAGAAGTATTCATGCAGACTGGTTAC
AACAAATTGTGTGACTGGTGGTCTTTGGGAGTGATTATGTATGAAATGCTAATAGGATAT
CCACCTTTCTGCTCTGAAACACCTCAAGAAACGTACAGAAAAGTGATGAACTGGAAAGAA
ACTCTGGTATTTCCTCCAGAGGTACCTATATCTGAGAAAGCCAAGGACTTAATTCTCAGA
TTTTGTATTGATTCTGAAAACAGAATTGGAAATAGTGGAGTAGAAGAAATAAAAGGTCAT
CCCTTTTTTGAAGGTGTCGACTGGGAGCACATAAGGGAAAGGCCAGCAGCAATCCCTATA
GAAATCAAAAGCATTGATGATACTTCAAATTTTGATGACTTCCCTGAATCTGATATTTTA
CAACCAGTGCCAAATACCACAGAACCGGACTACAAATCCAAAGACTGGGTTTTTCTCAAT
TATACCTATAAAAGGTTTGAAGGGTTGACTCAACGTGGCTCTATCCCCACCTACATGAAA
GCTGGGAAGTTATGA
Enzyme 119 GenBank Gene ID NM_015000.3 Link Image
Enzyme 119 GeneCard ID STK38L Link Image
Enzyme 119 GenAtlas ID STK38L Link Image
Enzyme 119 HGNC ID HGNC:17848 Link Image
Enzyme 119 Chromosome Location 1
Enzyme 119 Locus 12p11.23
Enzyme 119 SNPs SNPJam Report Link Image
Enzyme 119 General References
  1. Stegert MR, Tamaskovic R, Bichsel SJ, Hergovich A, Hemmings BA: Regulation of NDR2 protein kinase by multi-site phosphorylation and the S100B calcium-binding protein. J Biol Chem. 2004 May 28;279(22):23806-12. Epub 2004 Mar 22. [PubMed Link Image]
  2. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Feb 26;6(1):63-70. [PubMed Link Image]
  3. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Devroe E, Erdjument-Bromage H, Tempst P, Silver PA: Human Mob proteins regulate the NDR1 and NDR2 serine-threonine kinases. J Biol Chem. 2004 Jun 4;279(23):24444-51. Epub 2004 Apr 2. [PubMed Link Image]
  7. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 119 Metabolite References Not Available
Enzyme 120 [top]
Enzyme 120 ID 6547
Enzyme 120 Name Calcium-transporting ATPase type 2C member 2
Enzyme 120 Synonyms
  1. ATPase 2C2
  2. Secretory pathway Ca(2+)-ATPase 2
Enzyme 120 Gene Name ATP2C2
Enzyme 120 Protein Sequence >Calcium-transporting ATPase type 2C member 2 
MVEGRVSEFLKKLGFSGGGRQYQALEKDEEEALIDEQSELKAIEKEKKVTALPPKEACKC
QKEDLARAFCVDLHTGLSEFSVTQRRLAHGWNEFVADNSEPVWKKYLDQFKNPLILLLLG
SALVSVLTKEYEDAVSIATAVLVVVTVAFIQEYRSEKSLEELTKMVPPECNCLREGKLQH
LLARELVPGDVVSLSIGDRIPADIRLTEVTDLLVDESSFTGEAEPCSKTDSPLTGGGDLT
TLSNIVFMGTLVQYGRGQGVVIGTGESSQFGEVFKMMQAEETPKTPLQKSMDRLGKQLTL
FSFGIIGLIMLIGWSQGKQLLSMFTIGVSLAVAAIPEGLPIVVMVTLVLGVLRMAKKRVI
VKKLPIVETLGCCSVLCSDKTGTLTANEMTVTQLVTSDGLRAEVSGVGYDGQGTVCLLPS
KEVIKEFSNVSVGKLVEAGCVANNAVIRKNAVMGQPTEGALMALAMKMDLSDIKNSYIRK
KEIPFSSEQKWMAVKCSLKTEDQEDIYFMKGALEEVIRYCTMYNNGGIPLPLTPQQRSFC
LQEEKRMGSLGLRVLALASGPELGRLTFLGLVGIIDPPRVGVKEAVQVLSESGVSVKMIT
GDALETALAIGRNIGLCNGKLQAMSGEEVDSVEKGELADRVGKVSVFFRTSPKHKLKIIK
ALQESGAIVAMTGDGVNDAVALKSADIGIAMGQTGTDVSKEAANMILVDDDFSAIMNAVE
EGKGIFYNIKNFVRFQLSTSISALSLITLSTVFNLPSPLNAMQILWINIIMDGPPAQSLG
VEPVDKDAFRQPPRSVRDTILSRALILKILMSAAIIISGTLFIFWKEMPEDRASTPRTTT
MTFTCFVFFDLFNALTCRSQTKLIFEIGFLRNHMFLYSVLGSILGQLAVIYIPPLQRVFQ
TENLGALDLLFLTGLASSVFILSELLKLCEKYCCSPKRVQMHPEDV
Enzyme 120 Number of Residues 946
Enzyme 120 Molecular Weight 103186.5
Enzyme 120 Theoretical pI 5.32
Enzyme 120 GO Classification
Function
  • ATP binding
  • ATPase activity, coupled to transmembrane movement of ions
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • calcium ion transmembrane transporter activity
  • calcium-transporting ATPase activity
  • catalytic activity
  • cation transmembrane transporter activity
  • di-, tri-valent inorganic cation transmembrane transporter activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • inorganic cation transmembrane transporter activity
  • ion transmembrane transporter activity
  • nucleoside binding
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • calcium ion transport
  • cation transport
  • cellular nitrogen compound metabolic process
  • di-, tri-valent inorganic cation transport
  • divalent metal ion transport
  • establishment of localization
  • ion transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 120 General Function Involved in ATP binding
Enzyme 120 Specific Function This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium
Enzyme 120 Pathways Not Available
Enzyme 120 Reactions
  • ATP + H2O + Ca2+cis = ADP + phosphate + Ca2+trans [RN:R00086]
Enzyme 120 Pfam Domain Function
Enzyme 120 Signals
  • None
Enzyme 120 Transmembrane Regions
  • 107-127 130-150 232-252 294-314 332-352 751-771 805-825 838-855 875-895 906-926
Enzyme 120 Essentiality Not Available
Enzyme 120 GenBank ID Protein 55668314 Link Image
Enzyme 120 UniProtKB/Swiss-Prot ID O75185 Link Image
Enzyme 120 UniProtKB/Swiss-Prot Entry Name AT2C2_HUMAN Link Image
Enzyme 120 PDB ID Not Available
Enzyme 120 Cellular Location Not Available
Enzyme 120 Gene Sequence >2841 bp 
ATGGTCGAGGGACGCGTCTCCGAGTTCCTGAAGAAACTCGGCTTCTCGGGCGGGGGCCGC
CAGTACCAGGCGCTGGAGAAGGACGAAGAGGAAGCCTTGATTGATGAACAGAGTGAGCTG
AAAGCCATCGAGAAAGAGAAGAAGGTGACAGCCCTGCCCCCCAAGGAAGCGTGCAAATGC
CAGAAAGAGGATTTGGCCAGAGCGTTTTGTGTGGACTTACACACTGGGCTGTCGGAGTTC
TCGGTGACGCAGCGCCGGCTGGCCCATGGCTGGAATGAGTTTGTTGCTGACAACAGCGAA
CCTGTGTGGAAGAAATACCTGGATCAGTTTAAGAACCCCCTGATCCTGCTGCTGCTGGGC
TCTGCCCTGGTGAGTGTCCTCACCAAGGAGTATGAGGACGCCGTCAGCATCGCCACGGCA
GTGCTTGTCGTGGTCACTGTCGCCTTCATCCAGGAGTACAGGTCGGAGAAATCTCTGGAA
GAGCTGACCAAGATGGTTCCTCCAGAATGTAACTGCCTAAGAGAAGGAAAACTCCAGCAC
CTGCTTGCTCGAGAACTGGTTCCTGGTGATGTCGTATCTCTCTCGATCGGAGACCGGATC
CCTGCAGACATCCGACTCACTGAGGTCACGGACCTCTTGGTGGATGAATCCAGTTTCACC
GGGGAAGCCGAGCCATGTAGTAAAACAGACAGCCCCTTGACAGGCGGTGGGGACCTCACC
ACCCTCAGCAACATCGTCTTCATGGGGACCCTGGTGCAGTATGGGAGGGGCCAGGGGGTC
GTGATTGGAACAGGGGAAAGCTCTCAGTTCGGAGAAGTGTTTAAGATGATGCAGGCTGAA
GAGACACCTAAAACTCCTTTGCAGAAAAGCATGGACAGGCTAGGAAAGCAACTGACACTC
TTCTCCTTTGGCATAATCGGTCTCATCATGCTCATTGGCTGGTCGCAAGGGAAACAACTC
CTGAGTATGTTCACGATCGGGGTCAGCCTGGCTGTGGCGGCCATTCCAGAGGGTCTGCCC
ATCGTCGTCATGGTGACGCTGGTCCTGGGAGTGCTGCGGATGGCCAAGAAGCGGGTCATC
GTGAAGAAGTTACCCATCGTGGAGACTTTAGGTTGCTGCAGCGTTCTCTGTTCTGACAAG
ACGGGGACTCTGACTGCCAATGAAATGACAGTGACCCAGCTTGTAACGTCAGATGGGCTT
CGTGCCGAGGTCAGCGGAGTTGGGTATGACGGTCAAGGGACTGTGTGTCTTCTACCATCC
AAGGAAGTCATTAAGGAATTTTCCAATGTCTCAGTGGGAAAGTTAGTGGAGGCGGGCTGT
GTTGCCAACAATGCGGTCATCAGAAAGAACGCCGTGATGGGGCAGCCCACCGAGGGTGCA
TTGATGGCCCTGGCGATGAAGATGGACTTAAGTGATATTAAAAATTCATATATAAGAAAA
AAAGAGATTCCATTCAGTTCAGAGCAGAAGTGGATGGCGGTGAAATGCAGTCTGAAGACT
GAGGATCAGGAAGACATTTACTTCATGAAAGGGGCCTTGGAAGAGGTGATCCGCTACTGC
ACCATGTACAACAACGGGGGCATCCCCCTGCCGCTGACGCCCCAGCAGAGGTCATTCTGC
CTGCAGGAAGAGAAGAGGATGGGGTCGCTCGGTTTGCGGGTGCTGGCCCTGGCTTCTGGG
CCCGAGCTGGGGCGGCTGACGTTTCTCGGTCTTGTGGGCATCATTGACCCCCCGAGAGTT
GGCGTGAAGGAAGCAGTCCAGGTTCTCTCCGAGTCTGGTGTGTCTGTGAAGATGATAACG
GGGGATGCCCTGGAGACGGCCTTGGCCATAGGAAGAAACATCGGCCTGTGCAACGGGAAG
CTGCAAGCCATGTCCGGGGAGGAGGTGGACAGCGTGGAGAAGGGCGAGCTGGCCGACCGC
GTGGGGAAGGTGTCCGTGTTCTTCAGGACCAGCCCAAAGCACAAGCTCAAAATCATCAAG
GCTCTGCAGGAGTCAGGGGCGATCGTGGCCATGACTGGGGATGGGGTGAACGACGCAGTG
GCCCTGAAGTCTGCAGACATTGGGATCGCCATGGGGCAGACAGGGACGGACGTCAGCAAA
GAGGCCGCCAACATGATCCTGGTGGATGATGACTTCTCAGCCATCATGAATGCAGTGGAG
GAAGGCAAGGGTATTTTTTACAACATCAAAAACTTTGTCCGATTCCAGCTGAGCACGAGC
ATCTCCGCCCTGAGTCTCATCACTCTGTCCACCGTGTTCAACCTGCCCAGCCCCCTCAAC
GCCATGCAGATCCTATGGATCAACATCATCATGGATGGGCCACCGGCGCAGAGCTTGGGG
GTAGAGCCCGTTGACAAAGACGCCTTCAGGCAGCCACCACGGAGTGTGCGGGACACCATC
CTCAGCAGAGCCCTCATCCTGAAGATCCTCATGTCCGCGGCCATCATCATCAGCGGGACC
CTCTTTATCTTCTGGAAGGAGATGCCTGAAGACAGAGCAAGCACTCCCCGCACCACGACG
ATGACGTTCACTTGTTTTGTGTTTTTCGATCTCTTCAACGCCTTGACCTGCCGCTCTCAG
ACCAAGCTGATATTTGAGATCGGCTTTCTCAGGAACCACATGTTCCTCTACTCCGTCCTG
GGGTCCATCCTGGGGCAGCTGGCGGTCATTTACATCCCCCCGCTGCAGAGGGTCTTCCAG
ACGGAGAACCTGGGAGCGCTTGATTTGCTGTTTTTAACTGGATTGGCCTCATCCGTCTTC
ATTTTGTCAGAGCTCCTCAAACTATGTGAAAAATACTGTTGCAGCCCCAAGAGAGTCCAG
ATGCACCCTGAAGATGTGTAG
Enzyme 120 GenBank Gene ID AY791884 Link Image
Enzyme 120 GeneCard ID ATP2C2 Link Image
Enzyme 120 GenAtlas ID ATP2C2 Link Image
Enzyme 120 HGNC ID HGNC:29103 Link Image
Enzyme 120 Chromosome Location 1
Enzyme 120 Locus 16q24.1
Enzyme 120 SNPs SNPJam Report Link Image
Enzyme 120 General References
  1. Vanoevelen J, Dode L, Van Baelen K, Fairclough RJ, Missiaen L, Raeymaekers L, Wuytack F: The secretory pathway Ca2+/Mn2+-ATPase 2 is a Golgi-localized pump with high affinity for Ca2+ ions. J Biol Chem. 2005 Jun 17;280(24):22800-8. Epub 2005 Apr 14. [PubMed Link Image]
  2. Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Jun 30;5(3):169-76. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 120 Metabolite References Not Available
Enzyme 121 [top]
Enzyme 121 ID 6548
Enzyme 121 Name Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit beta
Enzyme 121 Synonyms
  1. PI3K-C2-beta
  2. PtdIns-3-kinase C2 subunit beta
  3. C2-PI3K
  4. Phosphoinositide 3-kinase-C2-beta
Enzyme 121 Gene Name PIK3C2B
Enzyme 121 Protein Sequence >Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit beta 
MSSTQGNGEHWKSLESVGISRKELAMAEALQMEYDALSRLRHDKEENRAKQNADPSLISW
DEPGVDFYSKPAGRRTDLKLLRGLSGSDPTLNYNSLSPQEGPPNHSTSQGPQPGSDPWPK
GSLSGDYLYIFDGSDGGVSSSPGPGDIEGSCKKLSPPPLPPRASIWDTPPLPPRKGSPSS
SKISQPSDINTFSLVEQLPGKLLEHRILEEEEVLGGGGQGRLLGSVDYDGINDAITRLNL
KSTYDAEMLRDATRGWKEGRGPLDFSKDTSGKPVARSKTMPPQVPPRTYASRYGNRKNAT
PGKNRRISAAPVGSRPHTVANGHELFEVSEERDEEVAAFCHMLDILRSGSDIQDYFLTGY
VWSAVTPSPEHLGDEVNLKVTVLCDRLQEALTFTCNCSSTVDLLIYQTLCYTHDDLRNVD
VGDFVLKPCGLEEFLQNKHALGSHEYIQYCRKFDIDIRLQLMEQKVVRSDLARTVNDDQS
PSTLNYLVHLQERPVKQTISRQALSLLFDTYHNEVDAFLLADGDFPLKADRVVQSVKAIC
NALAAVETPEITSALNQLPPCPSRMQPKIQKDPSVLAVRENREKVVEALTAAILDLVELY
CNTFNADFQTAVPGSRKHDLVQEACHFARSLAFTVYATHRIPIIWATSYEDFYLSCSLSH
GGKELCSPLQTRRAHFSKYLFHLIVWDQQICFPVQVNRLPRETLLCATLYALPIPPPGSS
SEANKQRRVPEALGWVTTPLFNFRQVLTCGRKLLGLWPATQENPSARWSAPNFHQPDSVI
LQIDFPTSAFDIKFTSPPGDKFSPRYEFGSLREEDQRKLKDIMQKESLYWLTDADKKRLW
EKRYYCHSEVSSLPLVLASAPSWEWACLPDIYVLLKQWTHMNHQDALGLLHATFPDQEVR
RMAVQWIGSLSDAELLDYLPQLVQALKYECYLDSPLVRFLLKRAVSDLRVTHYFFWLLKD
GLKDSQFSIRYQYLLAALLCCCGKGLREEFNRQCWLVNALAKLAQQVREAAPSARQGILR
TGLEEVKQFFALNGSCRLPLSPSLLVKGIVPRDCSYFNSNAVPLKLSFQNVDPLGENIRV
IFKCGDDLRQDMLTLQMIRIMSKIWVQEGLDMRMVIFRCFSTGRGRGMVEMIPNAETLRK
IQVEHGVTGSFKDRPLADWLQKHNPGEDEYEKAVENFIYSCAGCCVATYVLGICDRHNDN
IMLKTTGHMFHIDFGRFLGHAQMFGNIKRDRAPFVFTSDMAYVINGGDKPSSRFHDFVDL
CCQAYNLIRKHTHLFLNLLGLMLSCGIPELSDLEDLKYVYDALRPQDTEANATTYFTRLI
ESSLGSVATKLNFFIHNLAQMKFTGSDDRLTLSFASRTHTLKSSGRISDVFLCRHEKIFH
PNKGYIYVVKVMRENTHEATYIQRTFEEFQELHNKLRLLFPSSHLPSFPSRFVIGRSRGE
AVAERRREELNGYIWHLIHAPPEVAECDLVYTFFHPLPRDEKAMGTSPAPKSSDGTWARP
VGKVGGEVKLSISYKNNKLFIMVMHIRGLQLLQDGNDPDPYVKIYLLPDPQKTTKRKTKV
ARKTCNPTYNEMLVYDGIPKGDLQQRELQLSVLSEQGFWENVLLGEVNIRLRELDLAQEK
TGWFALGSRSHGTL
Enzyme 121 Number of Residues 1634
Enzyme 121 Molecular Weight 184766.1
Enzyme 121 Theoretical pI 7.30
Enzyme 121 GO Classification
Function
  • 1-phosphatidylinositol-3-kinase activity
  • binding
  • catalytic activity
  • inositol or phosphatidylinositol kinase activity
  • kinase activity
  • lipid binding
  • lipid kinase activity
  • phosphoinositide 3-kinase activity
  • phosphoinositide binding
  • phospholipid binding
  • phosphotransferase activity, alcohol group as acceptor
  • protein binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biological regulation
  • cell communication
  • cellular process
  • glycerophospholipid metabolic process
  • intracellular signal transduction
  • metabolic process
  • organophosphate metabolic process
  • phosphoinositide metabolic process
  • phosphoinositide phosphorylation
  • phosphoinositide-mediated signaling
  • phospholipid metabolic process
  • regulation of biological process
  • regulation of cellular process
  • second-messenger-mediated signaling
  • signal transduction
Component
  • macromolecular complex
  • phosphoinositide 3-kinase complex
  • protein complex
Enzyme 121 General Function Involved in binding
Enzyme 121 Specific Function Phosphorylates PtdIns and PtdIns4P with a preference for PtdIns. Does not phosphorylate PtdIns(4,5)P2. May be involved in EGF and PDGF signaling cascades
Enzyme 121 Pathways
  • Phosphatidylinositol signaling system (map04070 Link Image)
Enzyme 121 Reactions
  • ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate [RN:R05795]
Enzyme 121 Pfam Domain Function
Enzyme 121 Signals
  • None
Enzyme 121 Transmembrane Regions
  • None
Enzyme 121 Essentiality Not Available
Enzyme 121 GenBank ID Protein 2076604 Link Image
Enzyme 121 UniProtKB/Swiss-Prot ID O00750 Link Image
Enzyme 121 UniProtKB/Swiss-Prot Entry Name P3C2B_HUMAN Link Image
Enzyme 121 PDB ID Not Available
Enzyme 121 Cellular Location Not Available
Enzyme 121 Gene Sequence >4905 bp 
ATGTCTTCGACTCAGGACAATGGGGAACACTGGAAGTCCCTGGAGTCTGTGGGCATCAGC
CGCAAAGAACTAGCGATGGCCGAAGCCCTGCAGATGGAGTATGATGCCCTGTCCCGGCTC
CGGCATGACAAGGAGGAGAACAGAGCCAAGCAGAACGCAGACCCCTCTCTCATCAGCTGG
GATGAGCCTGGGGTAGACTTTTACAGCAAGCCAGCAGGAAGGCGGACCGACCTCAAGCTG
TTACGCGGTCTCTCTGGCTCTGATCCTACCCTTAACTACAACTCACTATCCCCACAGGAA
GGGCCGCCCAACCACTCTACCTCCCAAGGGCCACAGCCTGGCTCAGATCCCTGGCCCAAA
GGCTCCCTGTCTGGAGACTATCTCTACATTTTTGATGGTTCAGATGGGGGAGTCTCTTCG
TCCCCAGGACCAGGGGACATAGAGGGCTCTTGCAAGAAACTATCCCCACCTCCTCTGCCT
CCCCGAGCTTCTATCTGGGATACCCCTCCCCTGCCTCCCAGAAAGGGGTCCCCCTCATCC
TCCAAGATCTCCCAGCCCAGTGACATCAACACTTTCTCTTTGGTCGAACAATTGCCAGGC
AAACTGCTAGAGCATCGGATCCTAGAAGAGGAAGAGGTGCTGGGAGGTGGGGGTCAGGGG
CGCCTACTGGGGTCTGTGGACTATGATGGTATCAATGATGCAATTACTAGGCTCAACTTG
AAATCGACCTATGATGTGGAGATGTTGCGGGATGCCACCAGGGGCTGGAAGGAGGGCCGA
GGGCCGCTGGACTTCAGCAAAGACACCTCTGGAAAACCCGTGGCCAGGAGCAAGACTATG
CCCCCTCAGGTGCCCCCCCGCACCTATGCCTCCCGCTATGGCAACCGAAAGAATGCGACG
CCTGGCAAGAACCGCCGGATTTCTGCAGCCCCGGTGGGCTCCCGGCCCCACACTGTTGCC
AATGGCCATGAGTTGTTTGAGGTCTCAGAAGAGAGAGATGAGGAGGTTGCTGCATTTTGC
CACATGCTGGATATCCTTCGATCTGGCTCTGACATCCAAGACTACTTCCTCACTGGCTAT
GTCTGGAGTGCTGTCACCCCTAGCCCAGAGCACCTCGGGGATGAGGTCAACCTGAAGGTG
ACTGTGTTGTGTGACAGGCTTCAAGAGGCACTCACTTTCACCTGCAACTGTTCCTCCACT
GTAGACTTGCTTATCTACCAGACCCTGTGCTACACCCATGATGACCTGAGGAATGTGGAC
GTGGGTGACTTTGTGCTAAAGCCCTGCGGGCTGGAGGAGTTCCTGCAGAACAAGCATGCC
TTGGGCAGTCATGAGTACATCCAATACTGCCGCAAGTTTGACATTGACATTCGGCTACAG
CTGATGGAGCAGAAGGTTGTGCGCAGTGACCTGGCCCGGACGGTGAATGATGACCAGAGC
CCCTCCACCTTGAACTACCTCGTCCATCTCCAAGAGAGGCCTGTCAAGCAGACCATCAGC
AGGCAGGCCCTGAGTCTTCTGTTCGACACTTACCACAATGAGGTGGATGCCTTCCTGCTG
GCTGATGGAGACTTCCCACTGAAGGCTGACAGGGTGGTCCAGTCCGTCAAGGCCATCTGC
AACGCCCTGGCCGCCGTGGAAACCCCTGAGATCACCAGTGCTCTCAACCAGCTGCCCCCC
TGCCCCTCCCGCATGCAGCCTAAAATTCAGAAGGATCCCAGTGTCTTGGCTGTGAGGGAA
AACCGAGAGAAGGTCGTGGAAGCCCTGACCGCTGCCATCTTGGACCTGGTGGAGCTGTAC
TGCAACACATTCAACGCAGACTTCCAGACGGCAGTGCCCGGGAGCCGCAAGCATGACCTG
GTCCAGGAGGCCTGCCATTTCGCCAGGTCCCTGGCCTTCACTGTCTATGCCACCCACCGC
ATCCCCATCATCTGGGCTACCAGCTATGAAGATTTCTACCTCTCCTGCTCCCTCAGCCAT
GGCGGCAAGGACATGTGCAGCCCCCTGCAGACCCGAAGAGCTCACTTCTCCAAGTACCTC
TTCCACCTCATCGTCTGGGACCAGCAGATCTGCTTCCCAGTGCAGGTGAACCGGCTGCCT
CGGGAGACACTGCTGTGTGCCACTCTCTATGCTCTGCCCATCCCCCCACCGGGGAGCTCC
TCAGAGGCCAATAAGCAGCGGCGGGTGCCTGAAGCCCTGGGCTGGGTCACTACCCCACTC
TTCAACTTCAGGCAGGTCCTGACCTGTGGCCGGAAGCTTCTGGGTTTGTGGCCAGCAACA
CAGGAAAATCCCAGCGCCCGTTGGAGTGCACCTAATTTCCACCAGCCAGACAGTGTCATC
CTGCAGATTGACTTCCCCACCTCGGCCTTTGACATCAAGTTCACCAGCCCCCCTGGAGAC
AAGTTCAGCCCCCGCTATGAGTTTGGCAGCCTCCGGGAAGAAGACCAGCGCAAGCTTAAA
GACATCATGCAGAAAGAGTCCTTGTACTGGCTCACTGATGCTGACAAGAAGCGCCTGTGG
GAGAAGCGATATTACTGCCACTCGGAGGTGAGCTCGCTCCCCCTGGTGCTCGCCAGCGCC
CCCAGCTGGGAGTGGGCTTGCCTGCCTGACATCTATGTTCTCCTGAAGCAGTGGACCCAC
ATGAACCACCAGGATGCCCTGGGGCTCCTGCATGCCACCTTCCCGGACCAGGAGGTGCGT
CGTATGGCTGTGCAGTGGATTGGCTCACTCTCAGATGCTGAGCTGCTAGACTACCTGCCC
CAGCTGGTACAGGCCCTGAAGTATGAATGCTACCTGGACAGCCCGTTGGTGCGCTTCCTC
CTGAAACGAGCTGTGTCTGACTTGAGAGTGACTCACTACTTCTTCTGGTTACTGAAGGAC
GGCCTCAAGGACTCTCAGTTCAGCATCCGCTACCAGTATCTGCTGGCAGCCTTACTGTGC
TGCTGTGGCAAGGGGCTGAGAGAAGAGTTTAACCGCCAGTGCTGGCTTGTCAATGCCCTG
GCCAAACTGGCCCAGCAGGTCCGGGAGGCAGCCCCATCTGCAAGGCAGGGAATCCTCCGC
ACGGGCCTGGAGGAGGTGAAGCAGTTCTTTGCCCTCAATGGCTCGTGCCGCTTGCCACTC
AGCCCCAGTCTGCTGGTTAAGGGAATTGTGCCCAGGGACTGTTCCTACTTCAACTCCAAT
GCTGTCCCCCTCAAACTCTCCTTCCAAAATGTGGATCCCCTGGGTGAGAACATCCGTGTC
ATCTTCAAGTGTGGGGACGACCTTCGCCAGGACATGCTAACGCTGCAGATGATTCGCATC
ATGAGCAAGATCTGGGTCCAGGAGGGGCTGGACATGCGCATGGTCATCTTCCGCTGCTTC
TCCACCGGCCGGGGCAGAGGGATGGTGGAGATGATCCCTAATGCTGAGACCCTGCGTAAG
ATCCAGGTGGAGCATGGGGTGACCGGCTCGTTCAAGGACCGGCCCCTGGCAGACTGGCTG
CAGAAACACAACCCTGGGGAGGACGAGTATGAGAAGGCTGTGGAGAACTTTATCTACTCC
TGCGCTGGCTGCTGCGTGGCCACGTACGTCTTGGGCATCTGTGACCGACATAATGACAAC
ATCATGCTGAAGACCACTGGTCACATGTTCCACATTGATTTTGGCCGCTTCCTGGGCCAT
GCCCAGATGTTTGGCAACATCAAGCGGGACCGTGCCCCCTTTGTCTTCACCTCGGACATG
GCGTATGTCATCAACGGGGGTGACAAGCCTTCCAGCCGCTTCCATGATTTTGTTGACCTT
TGCTGCCAAGCCTACAACCTCATTCGCAAGCACACCCACCTCTTCCTCAACCTTCTGGGC
CTGATGTTGTCCTGTGGGATCCCTGAACTCTCAGACCTGGAGGACCTCAAGTATGTGTAC
GATGCCCTGAGGCCTCAGGATACAGAGGCCAATGCCACTACCTACTTCACTAGGTTGATT
GAGTCCAGCCTGGGCAGTGTAGCCACAAAGCTCAATTTTTTCATCCATAATCTGGCTCAG
ATGAAGTTCACGGGCTCAGATGACCGGCTGACCCTCTCCTTTGCCTCCCGAACACACACT
CTCAAGAGCTCTGGCCGAATCAGTGATGTTTTCCTCTGCCGCCATGAGAAGATCTTCCAC
CCCAACAAAGGCTATATATATGTGGTAAAGGTGATGCGAGAGAACACTCACGAGGCCACC
TACATCCAGCGGACCTTTGAGGAGTTCCAGGAATTACACAATAAGTTGCGGCTGCTCTTC
CCTTCTTCCCACTTGCCCAGCTTCCCTAGTCGCTTCGTGATCGGCCGCTCCCGGGGAGAG
GCGGTGGCCGAGCGGCGGAGGGAGGAGCTAAACGGTTACATCTGGCACTTGATCCACGCA
CCCCCTGAGGTGGCCGAGTGTGATTTGGTGTACACCTTCTTCCACCCACTGCCCCGGGAT
GAGAAGGCTATGGGCACCAGCCCAGCTCCTAAGTCCTCAGATGGCACATGGGCCCGGCCC
GTCGGAAAGGTGGGAGGGGAGGTGAAGCTGTCCATCTCCTACAAAAACAATAAACTCTTC
ATCATGGTGATGCATATTCGGGGCTTGCAACTGCTCCAGGATGGAAATGACCCTGACCCC
TATGTGAAAATTTACCTCCTTCCTGACCCTCAGAAAACCACTAAGAGGAAAACCAAAGTG
GCCCGGAAAACCTGCAATCCTACCTACAATGAGATGTTGGTATATGATGGGATCCCCAAG
GGTGACCTGCAGCAGCGGGAGCTCCAGCTGAGCGTGCTGAGTGAGCAGGGATTCTGGGAG
AACGTCCTCCTCGGTGAGGTGAACATCCGCCTGCGAGAGCTGGACCTGGCTCAGGAGAAG
ACCGGCTGGTTCGCCCTGGGATCTCGAAGTCATGGCACCTTGTGA
Enzyme 121 GenBank Gene ID Y11312 Link Image
Enzyme 121 GeneCard ID PIK3C2B Link Image
Enzyme 121 GenAtlas ID PIK3C2B Link Image
Enzyme 121 HGNC ID HGNC:8972 Link Image
Enzyme 121 Chromosome Location 1
Enzyme 121 Locus 1q32
Enzyme 121 SNPs SNPJam Report Link Image
Enzyme 121 General References
  1. Brown RA, Ho LK, Weber-Hall SJ, Shipley JM, Fry MJ: Identification and cDNA cloning of a novel mammalian C2 domain-containing phosphoinositide 3-kinase, HsC2-PI3K. Biochem Biophys Res Commun. 1997 Apr 17;233(2):537-44. [PubMed Link Image]
  2. Arcaro A, Volinia S, Zvelebil MJ, Stein R, Watton SJ, Layton MJ, Gout I, Ahmadi K, Downward J, Waterfield MD: Human phosphoinositide 3-kinase C2beta, the role of calcium and the C2 domain in enzyme activity. J Biol Chem. 1998 Dec 4;273(49):33082-90. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Arcaro A, Zvelebil MJ, Wallasch C, Ullrich A, Waterfield MD, Domin J: Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors. Mol Cell Biol. 2000 Jun;20(11):3817-30. [PubMed Link Image]
  5. Wheeler M, Domin J: Recruitment of the class II phosphoinositide 3-kinase C2beta to the epidermal growth factor receptor: role of Grb2. Mol Cell Biol. 2001 Oct;21(19):6660-7. [PubMed Link Image]
  6. El Sheikh SS, Domin J, Tomtitchong P, Abel P, Stamp G, Lalani EN: Topographical expression of class IA and class II phosphoinositide 3-kinase enzymes in normal human tissues is consistent with a role in differentiation. BMC Clin Pathol. 2003 Oct 16;3(1):4. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 121 Metabolite References Not Available
Enzyme 122 [top]
Enzyme 122 ID 6551
Enzyme 122 Name Sarcoplasmic/endoplasmic reticulum calcium ATPase 3
Enzyme 122 Synonyms
  1. SERCA3
  2. SR Ca(2+)-ATPase 3
  3. Calcium pump 3
Enzyme 122 Gene Name ATP2A3
Enzyme 122 Protein Sequence >Sarcoplasmic/endoplasmic reticulum calcium ATPase 3 
MEAAHLLPAADVLRHFSVTAEGGLSPAQVTGARERYGPNELPSEEGKSLWELVLEQFEDL
LVRILLLAALVSFVLAWFEEGEETTTAFVEPLVIMLILVANAIVGVWQERNAESAIEALK
EYEPEMGKVIRSDRKGVQRIRARDIVPGDIVEVAVGDKVPADLRLIEIKSTTLRVDQSIL
TGESVSVTKHTEAIPDPRAVNQDKKNMLFSGTNITSGKAVGVAVATGLHTELGKIRSQMA
AVEPERTPLQRKLDEFGRQLSHAISVICVAVWVINIGHFADPAHGGSWLRGAVYYFKIAV
ALAVAAIPEGLPAVITTCLALGTRRMARKNAIVRSLPSVETLGCTSVICSDKTGTLTTNQ
MSVCRMFVVAEADAGSCLLHEFTISGTTYTPEGEVRQGDQPVRCGQFDGLVELATICALC
NDSALDYNEAKGVYEKVGEATETALTCLVEKMNVFDTDLQALSRVERAGACNTVIKQLMR
KEFTLEFSRDRKSMSVYCTPTRPHPTGQGSKMFVKGAPESVIERCSSVRVGSRTAPLTPT
SREQILAKIRDWGSGSDTLRCLALATRDAPPRKEDMELDDCSKFVQYETDLTFVGCVGML
DPPRPEVAACITRCYQAGIRVVMITGDNKGTAVAICRRLGIFGDTEDVAGKAYTGREFDD
LSPEQQRQACRTARCFARVEPAHKSRIVENLQSFNEITAMTGDGVNDAPALKKAEIGIAM
GSGTAVAKSAAEMVLSDDNFASIVAAVEEGRAIYSNMKQFIRYLISSNVGEVVCIFLTAI
LGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMEKLPRSPREALISGWLFFRYLAI
GVYVGLATVAAATWWFVYDAEGPHINFYQLRNFLKCSEDNPLFAGIDCEVFESRFPTTMA
LSVLVTIEMCNALNSVSENQSLLRMPPWMNPWLLVAVAMSMALHFLILLVPPLPLIFQVT
PLSGRQWVVVLQISLPVILLDEALKYLSRNHMHACLYPGLLRTVSQAWSRQPLTTSWTPD
HTGRNEPEVSAGNRVESPVCTSD
Enzyme 122 Number of Residues 1043
Enzyme 122 Molecular Weight 113976.2
Enzyme 122 Theoretical pI 5.26
Enzyme 122 GO Classification
Function
  • ATP binding
  • ATPase activity, coupled to transmembrane movement of ions
  • ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • calcium ion transmembrane transporter activity
  • calcium-transporting ATPase activity
  • catalytic activity
  • cation transmembrane transporter activity
  • di-, tri-valent inorganic cation transmembrane transporter activity
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • inorganic cation transmembrane transporter activity
  • ion transmembrane transporter activity
  • nucleoside binding
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • calcium ion transport
  • cation transport
  • cellular nitrogen compound metabolic process
  • di-, tri-valent inorganic cation transport
  • divalent metal ion transport
  • establishment of localization
  • ion transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • membrane part
Enzyme 122 General Function Involved in ATP binding
Enzyme 122 Specific Function This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Transports calcium ions from the cytosol into the sarcoplasmic/endoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction
Enzyme 122 Pathways Not Available
Enzyme 122 Reactions
  • ATP + H2O + Ca2+cis = ADP + phosphate + Ca2+trans [RN:R00086]
Enzyme 122 Pfam Domain Function
Enzyme 122 Signals
  • None
Enzyme 122 Transmembrane Regions
  • 49-69 90-110 254-273 296-313 758-777 788-808 829-851 898-917 931-949 965-985
Enzyme 122 Essentiality Not Available
Enzyme 122 GenBank ID Protein 28373109 Link Image
Enzyme 122 UniProtKB/Swiss-Prot ID Q93084 Link Image
Enzyme 122 UniProtKB/Swiss-Prot Entry Name AT2A3_HUMAN Link Image
Enzyme 122 PDB ID Not Available
Enzyme 122 Cellular Location Not Available
Enzyme 122 Gene Sequence >3132 bp 
ATGGAGGCGGCGCATCTGCTCCCGGCCGCCGACGTGCTGCGCCACTTCTCGGTGACAGCC
GAGGGCGGCCTGAGCCCGGCGCAGGTGACCGGCGCGCGGGAGCGCTACGGCCCCAACGAG
CTCCCGAGTGAGGAAGGGAAGTCCCTGTGGGAGCTGGTGCTGGAACAGTTTGAGGACCTC
CTGGTGCGCATCCTGCTGCTGGCTGCCCTTGTCTCCTTTGTCCTGGCCTGGTTCGAGGAG
GGCGAGGAGACCACGACCGCCTTCGTGGAGCCCCTGGTCATCATGCTGATCCTCGTGGCC
AACGCCATTGTGGGCGTGTGGCAGGAACGCAACGCCGAGAGTGCCATCGAGGCCCTGAAG
GAGTATGAGCCTGAGATGGGCAAGGTGATCCGCTCGGACCGCAAGGGCGTGCAGAGGATC
CGTGCCCGGGACATCGTCCCAGGGGACATTGTAGAAGTGGCAGTGGGGGACAAAGTGCCT
GCTGACCTCCGCCTCATCGAGATCAAGTCCACCACGCTGCGAGTGGACCAGTCCATCCTG
ACGGGTGAATCTGTGTCCGTGACCAAGCACACAGAGGCCATCCCAGACCCCAGAGCTGTG
AACCAGGACAAGAAGAACATGCTGTTTTCTGGCACCAATATCACATCGGGCAAAGCGGTG
GGTGTGGCCGTGGCCACCGGCCTGCACACGGAGCTGGGCAAGATCCGGAGCCAGATGGCG
GCAGTCGAGCCCGAGCGGACGCCGCTGCAGCGCAAGCTGGACGAGTTTGGACGGCAGCTG
TCCCACGCCATCTCTGTGATCTGCGTGGCCGTGTGGGTCATCAACATCGGCCACTTCGCC
GACCCGGCCCACGGTGGCTCCTGGCTGCGTGGCGCTGTCTACTACTTCAAGATCGCCGTG
GCCCTGGCGGTGGCGGCCATCCCCGAGGGCCTCCCGGCTGTCATCACTACATGCCTGGCA
CTGGGCACGCGGCGCATGGCACGCAAGAACGCCATCGTGCGAAGCCTGCCGTCCGTGGAG
ACCCTGGGCTGCACCTCAGTCATCTGCTCCGACAAGACGGGCACGCTCACCACCAATCAG
ATGTCTGTCTGCCGGATGTTCGTGGTAGCCGAGGCCGATGCGGGCTCCTGCCTTTTGCAC
GAGTTCACCATCTCGGGTACCACGTATACCCCCGAGGGCGAAGTGCGGCAGGGGGATCAG
CCTGTGCGCTGCGGCCAGTTCGACGGGCTGGTGGAGCTGGCGACCATCTGCGCCCTGTGC
AACGACTCGGCTCTGGACTACAACGAGGCCAAGGGTGTGTATGAGAAGGTGGGAGAGGCC
ACGGAGACAGCTCTGACTTGCCTGGTGGAGAAGATGAACGTGTTCGACACCGACCTGCAG
GCTCTGTCCCGGGTGGAGCGAGCTGGCGCCTGTAACACGGTCATCAAGCAGCTGATGCGG
AAGGAGTTCACCCTGGAGTTCTCCCGAGACCGGAAATCCATGTCCGTGTACTGCACGCCC
ACCCGCCCTCACCCTACTGGCCAGGGCAGCAAGATGTTTGTGAAGGGGGCTCCTGAGAGT
GTGATCGAGCGCTGTAGCTCAGTCCGCGTGGGGAGCCGCACAGCACCCCTGACCCCCACC
TCCAGGGAGCAGATCCTGGCAAAGATCCGGGATTGGGGCTCAGGCTCAGACACGCTGCGC
TGCCTGGCACTGGCCACCCGGGACGCGCCCCCAAGGAAGGAGGACATGGAGCTGGACGAC
TGCAGCAAGTTTGTGCAGTACGAGACGGACCTGACCTTCGTGGGCTGCGTAGGCATGCTG
GACCCGCCGCGACCTGAGGTGGCTGCCTGCATCACACGCTGCTACCAGGCGGGCATCCGC
GTGGTCATGATCACGGGGGATAACAAAGGCACTGCCGTGGCCATCTGCCGCAGGCTTGGC
ATCTTTGGGGACACGGAAGACGTGGCGGGCAAGGCCTACACGGGCCGCGAGTTTGATGAC
CTCAGCCCCGAGCAGCAGCGCCAGGCCTGCCGCACCGCCCGCTGCTTCGCCCGCGTGGAG
CCCGCACACAAGTCCCGCATCGTGGAGAACCTGCAGTCCTTTAACGAGATCACTGCTATG
ACTGGCGATGGAGTGAACGACGCACCAGCCCTGAAGAAAGCAGAGATCGGCATCGCCATG
GGCTCAGGCACGGCCGTGGCCAAGTCGGCGGCAGAGATGGTGCTGTCAGATGACAACTTT
GCCTCCATCGTGGCTGCGGTGGAGGAGGGCCGGGCCATCTACAGCAACATGAAGCAATTC
ATCCGCTACCTCATCTCCTCCAATGTTGGCGAGGTCGTCTGCATCTTCCTCACGGCAATT
CTGGGCCTGCCCGAAGCCCTGATCCCTGTGCAGCTGCTCTGGGTGAACCTGGTGACAGAC
GGCCTACCTGCCACGGCTCTGGGCTTCAACCCGCCAGACCTGGACATCATGGAGAAGCTG
CCCCGGAGCCCCCGAGAAGCCCTCATCAGTGGCTGGCTCTTCTTCCGATACCTGGCTATC
GGAGTGTACGTAGGCCTGGCCACAGTGGCTGCCGCCACCTGGTGGTTTGTGTATGACGCC
GAGGGACCTCACATCAACTTCTACCAGCTGAGGAACTTCCTGAAGTGCTCCGAAGACAAC
CCGCTCTTTGCCGGCATCGACTGTGAGGTGTTCGAGTCACGCTTCCCCACCACCATGGCC
TTGTCCGTGCTCGTGACCATTGAAATGTGCAATGCCCTCAACAGCGTCTCGGAGAACCAG
TCGCTGCTGCGGATGCCGCCCTGGATGAACCCCTGGCTGCTGGTGGCTGTGGCCATGTCC
ATGGCCCTGCACTTCCTCATCCTGCTCGTGCCGCCCCTGCCTCTCATTTTCCAGGTGACC
CCACTGAGCGGGCGCCAGTGGGTGGTGGTGCTCCAGATATCTCTGCCTGTCATCCTGCTG
GATGAGGCCCTCAAGTACCTGTCCCGGAACCACATGCACGCCTGTCTTTATCCAGGCCTT
CTCAGGACAGTCTCGCAGGCCTGGAGTAGGCAGCCGCTGACCACCTCTTGGACCCCAGAC
CACACCGGAAGAAATGAGCCAGAAGTGAGCGCTGGGAACAGAGTGGAGTCTCCGGTGTGT
ACCTCAGACTGA
Enzyme 122 GenBank Gene ID NM_174955.1 Link Image
Enzyme 122 GeneCard ID ATP2A3 Link Image
Enzyme 122 GenAtlas ID ATP2A3 Link Image
Enzyme 122 HGNC ID HGNC:813 Link Image
Enzyme 122 Chromosome Location 1
Enzyme 122 Locus 17p13.3
Enzyme 122 SNPs SNPJam Report Link Image
Enzyme 122 General References
  1. Dode L, Wuytack F, Kools PF, Baba-Aissa F, Raeymaekers L, Brike F, van de Ven WJ, Casteels R: cDNA cloning, expression and chromosomal localization of the human sarco/endoplasmic reticulum Ca(2+)-ATPase 3 gene. Biochem J. 1996 Sep 1;318 ( Pt 2):689-99. [PubMed Link Image]
  2. Dode L, De Greef C, Mountian I, Attard M, Town MM, Casteels R, Wuytack F: Structure of the human sarco/endoplasmic reticulum Ca2+-ATPase 3 gene. Promoter analysis and alternative splicing of the SERCA3 pre-mRNA. J Biol Chem. 1998 May 29;273(22):13982-94. [PubMed Link Image]
  3. Poch E, Leach S, Snape S, Cacic T, MacLennan DH, Lytton J: Functional characterization of alternatively spliced human SERCA3 transcripts. Am J Physiol. 1998 Dec;275(6 Pt 1):C1449-58. [PubMed Link Image]
  4. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  7. Wuytack F, Papp B, Verboomen H, Raeymaekers L, Dode L, Bobe R, Enouf J, Bokkala S, Authi KS, Casteels R: A sarco/endoplasmic reticulum Ca(2+)-ATPase 3-type Ca2+ pump is expressed in platelets, in lymphoid cells, and in mast cells. J Biol Chem. 1994 Jan 14;269(2):1410-6. [PubMed Link Image]
  8. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 122 Metabolite References Not Available
Enzyme 123 [top]
Enzyme 123 ID 6555
Enzyme 123 Name Death-associated protein kinase 1
Enzyme 123 Synonyms
  1. DAP kinase 1
Enzyme 123 Gene Name DAPK1
Enzyme 123 Protein Sequence >Death-associated protein kinase 1 
MTVFRQENVDDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGVSRED
IEREVSILKEIQHPNVITLHEVYENKTDVILILELVAGGELFDFLAEKESLTEEEATEFL
KQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAHKIDFGNEFKNIFGT
PEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEY
FSNTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWIKPKDTQQALSRKASAVNMEKFKKFA
ARKKWKQSVRLISLCQRLSRSFLSRSNMSVARSDDTLDEEDSFVMKAIIHAINDDNVPGL
QHLLGSLSNYDVNQPNKHGTPPLLIAAGCGNIQILQLLIKRGSRIDVQDKGGSNAVYWAA
RHGHVDTLKFLSENKCPLDVKDKSGEMALHVAARYGHADVAQLLCSFGSNPNIQDKEEET
PLHCAAWHGYYSVAKALCEAGCNVNIKNREGETPLLTASARGYHDIVECLAEHGADLNAC
DKDGHIALHLAVRRCQMEVIKTLLSQGCFVDYQDRHGNTPLHVACKDGNMPIVVALCEAN
CNLDISNKYGRTPLHLAANNGILDVVRYLCLMGASVEALTTDGKTAEDLARSEQHEHVAG
LLARLRKDTHRGLFIQQLRPTQNLQPRIKLKLFGHSGSGKTTLVESLKCGLLRSFFRRRR
PRLSSTNSSRFPPSPLASKPTVSVSINNLYPGCENVSVRSRSMMFEPGLTKGMLEVFVAP
THHPHCSADDQSTKAIDIQNAYLNGVGDFSVWEFSGNPVYFCCYDYFAANDPTSIHVVVF
SLEEPYEIQLNQVIFWLSFLKSLVPVEEPIAFGGKLKNPLQVVLVATHADIMNVPRPAGG
EFGYDKDTSLLKEIRNRFGNDLHISNKLFVLDAGASGSKDMKVLRNHLQEIRSQIVSVCP
PMTHLCEKIISTLPSWRKLNGPNQLMSLQQFVYDVQDQLNPLASEEDLRRIAQQLHSTGE
INIMQSETVQDVLLLDPRWLCTNVLGKLLSVETPRALHHYRGRYTVEDIQRLVPDSDVEE
LLQILDAMDICARDLSSGTMVDVPALIKTDNLHRSWADEEDEVMVYGGVRIVPVEHLTPF
PCGIFHKVQVNLCRWIHQQSTEGDADIRLWVNGCKLANRGAELLVLLVNHGQGIEVQVRG
LETEKIKCCLLLDSVCSTIENVMATTLPGLLTVKHYLSPQQLREHHEPVMIYQPRDFFRA
QTLKETSLTNTMGGYKESFSSIMCFGCHDVYSQASLGMDIHASDLNLLTRRKLSRLLDPP
DPLGKDWCLLAMNLGLPDLVAKYNTNNGAPKDFLPSPLHALLREWTTYPESTVGTLMSKL
RELGRRDAADFLLKASSVFKINLDGNGQEAYASSCNSGTSYNSISSVVSR
Enzyme 123 Number of Residues 1430
Enzyme 123 Molecular Weight 160071.6
Enzyme 123 Theoretical pI 6.82
Enzyme 123 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • biological regulation
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
  • regulation of biological process
  • regulation of cellular process
  • signal transduction
Component
—
Enzyme 123 General Function Involved in protein binding
Enzyme 123 Specific Function Calcium/calmodulin-dependent serine/threonine kinase which acts as a positive regulator of apoptosis
Enzyme 123 Pathways Not Available
Enzyme 123 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 123 Pfam Domain Function
Enzyme 123 Signals
  • None
Enzyme 123 Transmembrane Regions
  • None
Enzyme 123 Essentiality Not Available
Enzyme 123 GenBank ID Protein 89363047 Link Image
Enzyme 123 UniProtKB/Swiss-Prot ID P53355 Link Image
Enzyme 123 UniProtKB/Swiss-Prot Entry Name DAPK1_HUMAN Link Image
Enzyme 123 PDB ID 1JKT Link Image
Enzyme 123 PDB File Show
Enzyme 123 3D Structure
Enzyme 123 Cellular Location Not Available
Enzyme 123 Gene Sequence >4293 bp 
ATGACCGTGTTCAGGCAGGAAAACGTGGATGATTACTACGACACCGGCGAGGAACTTGGC
AGTGGACAGTTTGCGGTTGTGAAGAAATGCCGTGAGAAAAGCACCGGCCTCCAGTATGCC
GCCAAATTCATCAAGAAAAGGAGGACTAAGTCCAGCCGGCGGGGTGTGAGCCGCGAGGAC
ATCGAGCGGGAGGTCAGCATCCTGAAGGAGATCCAGCACCCCAATGTCATCACCCTGCAC
GAGGTCTATGAGAACAAGACGGACGTCATCCTGATCTTGGAACTCGTTGCAGGTGGCGAG
CTGTTTGACTTCTTAGCTGAAAAGGAATCTTTAACTGAAGAGGAAGCAACTGAATTTCTC
AAACAAATTCTTAATGGTGTTTACTACCTGCACTCCCTTCAAATCGCCCACTTTGATCTT
AAGCCTGAGAACATAATGCTTTTGGATAGAAATGTCCCCAAACCTCGGATCAAGATCATT
GACTTTGGGTTGGCCCATAAAATTGACTTTGGAAATGAATTTAAAAACATATTTGGGACT
CCAGAGTTTGTCGCTCCTGAGATAGTCAACTATGAACCTCTTGGTCTTGAGGCAGATATG
TGGAGTATCGGGGTAATAACCTATATCCTCCTAAGTGGGGCCTCCCCATTTCTTGGAGAC
ACTAAGCAAGAAACGTTAGCAAATGTATCCGCTGTCAACTACGAATTTGAGGATGAATAC
TTCAGTAATACCAGTGCCCTAGCCAAAGATTTCATAAGAAGACTTCTGGTCAAGGATCCA
AAGAAGAGAATGACAATTCAAGATAGTTTGCAGCATCCCTGGATCAAGCCTAAAGATACA
CAACAGGCACTTAGTAGAAAAGCATCAGCAGTAAACATGGAGAAATTCAAGAAGTTTGCA
GCCCGGAAAAAATGGAAACAATCCGTTCGCTTGATATCACTGTGCCAAAGATTATCCAGG
TCATTCCTGTCCAGAAGTAACATGAGTGTTGCCAGAAGCGATGATACTCTGGATGAGGAA
GACTCCTTTGTGATGAAAGCCATCATCCATGCCATCAACGATGACAATGTCCCAGGCCTG
CAGCACCTTCTGGGCTCATTATCCAACTATGATGTTAACCAACCCAACAAGCACGGGACA
CCTCCATTACTCATTGCTGCTGGCTGTGGGAATATTCAAATACTACAGTTGCTCATTAAA
AGAGGCTCGAGAATCGATGTCCAGGATAAGGGCGGGTCCAATGCCGTCTACTGGGCTGCT
CGGCATGGCCACGTCGATACCTTGAAATTTCTCAGTGAGAACAAATGCCCTTTGGATGTG
AAAGACAAGTCTGGAGAGATGGCCCTCCACGTGGCAGCTCGCTATGGCCATGCTGACGTG
GCTCAGTTACTGTGCAGCTTCGGCTCAAATCCCAATATCCAGGACAAGGAAGAAGAAACC
CCCCTGCACTGTGCTGCTTGGCACGGCTATTACTCTGTGGCCAAAGCCCTTTGTGAAGCC
GGCTGTAACGTGAACATCAAGAACCGAGAAGGAGAGACGCCCCTCCTGACAGCCTCTGCC
AGGGGCTACCACGACATCGTGGAGTGTCTGGCCGAACATGGAGCCGACCTTAATGCTTGC
GACAAGGACGGACACATTGCCCTTCATCTGGCTGTAAGACGGTGTCAGATGGAGGTAATC
AAGACTCTCCTCAGCCAAGGGTGTTTCGTCGATTATCAAGACAGGCACGGCAATACTCCC
CTCCATGTGGCATGTAAAGATGGCAACATGCCTATCGTGGTGGCCCTCTGTGAAGCAAAC
TGCAATTTGGACATCTCCAACAAGTATGGGCGAACGCCTCTGCACCTTGCGGCCAACAAC
GGAATCCTAGACGTGGTCCGGTATCTCTGTCTGATGGGAGCCAGCGTTGAGGCGCTGACC
ACGGACGGAAAGACGGCAGAAGATCTTGCTAGATCGGAACAGCACGAGCACGTAGCAGGT
CTCCTTGCAAGACTTCGAAAGGATACGCACCGAGGACTCTTCATCCAGCAGCTCCGACCC
ACACAGAACCTGCAGCCAAGAATTAAGCTCAAGCTGTTTGGCCACTCGGGATCCGGGAAA
ACCACCCTTGTAGAATCTCTCAAGTGTGGGCTGCTGAGGAGCTTTTTCAGAAGGCGTCGG
CCCAGACTGTCTTCCACCAACTCCAGCAGGTTCCCACCTTCACCCCTGGCTTCTAAGCCC
ACAGTCTCAGTGAGCATCAACAACCTGTACCCAGGCTGCGAGAACGTGAGTGTGAGGAGC
CGCAGCATGATGTTCGAGCCGGGTCTTACCAAAGGGATGCTGGAGGTGTTTGTGGCCCCG
ACCCACCACCCGCACTGCTCGGCCGATGACCAGTCCACCAAGGCCATCGACATCCAGAAC
GCTTATTTGAATGGAGTTGGCGATTTCAGCGTGTGGGAGTTCTCTGGAAATCCTGTGTAT
TTCTGCTGTTATGACTATTTTGCTGCAAATGATCCCACGTCAATCCATGTTGTTGTCTTT
AGTCTAGAAGAGCCCTATGAGATCCAGCTGAACCAAGTGATTTTCTGGCTCAGTTTCCTG
AAGTCCCTTGTCCCAGTTGAAGAACCCATAGCCTTCGGTGGCAAGCTGAAGAACCCACTC
CAAGTTGTCCTGGTGGCCACCCACGCTGACATCATGAATGTTCCTCGACCGGCTGGAGGC
GAGTTTGGATATGACAAAGACACATCGTTGCTGAAAGAGATTAGGAACAGGTTTGGAAAT
GATCTTCACATTTCAAATAAGCTGTTTGTTCTGGATGCTGGGGCTTCTGGGTCAAAGGAC
ATGAAGGTACTTCGAAATCATCTGCAAGAAATACGAAGCCAGATTGTTTCGGTCTGTCCT
CCCATGACTCACCTGTGTGAGAAAATCATCTCCACGCTGCCTTCCTGGAGGAAGCTCAAT
GGACCCAACCAGCTGATGTCGCTGCAGCAGTTTGTGTACGACGTGCAGGACCAGCTGAAC
CCCCTGGCCAGCGAGGAGGACCTCAGGCGCATTGCTCAGCAGCTCCACAGCACAGGCGAG
ATCAACATCATGCAAAGTGAAACAGTTCAGGACGTGCTGCTCCTGGACCCCCGCTGGCTC
TGCACAAACGTCCTGGGGAAGTTGCTGTCCGTGGAGACCCCACGGGCGCTGCACCACTAC
CGGGGCCGCTACACCGTGGAGGACATCCAGCGCCTGGTGCCCGACAGCGACGTGGAGGAG
CTGCTGCAGATCCTCGATGCCATGGACATCTGCGCCCGGGACCTGAGCAGCGGGACCATG
GTGGACGTCCCAGCCCTGATCAAGACAGACAACCTGCACCGCTCCTGGGCTGATGAGGAG
GACGAGGTGATGGTGTATGGTGGCGTGCGCATCGTGCCCGTGGAACACCTCACCCCCTTC
CCATGTGGCATCTTTCACAAGGTCCAGGTGAACCTGTGCCGGTGGATCCACCAGCAAAGC
ACAGAGGGCGACGCGGACATCCGCCTGTGGGTGAATGGCTGCAAGCTGGCCAACCGTGGG
GCCGAGCTGCTGGTGCTGCTGGTCAACCACGGCCAGGGCATTGAGGTCCAGGTCCGCGGC
CTGGAGACGGAGAAGATCAAGTGCTGCCTGCTGCTGGACTCGGTGTGCAGCACCATTGAG
AACGTCATGGCCACCACGCTGCCAGGGCTCCTGACCGTGAAGCATTACCTGAGCCCCCAG
CAGCTGCGGGAGCACCATGAGCCCGTCATGATCTACCAGCCACGGGACTTCTTCCGGGCA
CAGACTCTGAAGGAAACCTCACTGACCAACACCATGGGGGGGTACAAGGAAAGCTTCAGC
AGCATCATGTGCTTCGGGTGTCACGACGTCTACTCACAGGCCAGCCTCGGCATGGACATC
CATGCATCAGACCTGAACCTCCTCACTCGGAGGAAACTGAGTCGCCTGCTGGACCCGCCC
GACCCCCTGGGGAAGGACTGGTGCCTTCTCGCCATGAACTTAGGCCTCCCTGACCTCGTG
GCAAAGTACAACACCAGTAACGGGGCTCCCAAGGATTTCCTCCCCAGCCCCCTCCACGCC
CTGCTGCGGGAATGGACCACCTACCCTGAGAGCACAGTGGGCACCCTCATGTCCAAACTG
AGGGAGCTGGGTCGCCGGGATGCCGCAGACTTTTTGCTGAAGGCATCCTCTGTGTTCAAA
ATCAACCTGGATGGCAATGGCCAGGAGGCCTATGCCTCGAGCTGCAACAGCGGCACCTCT
TACAATTCCATTAGCTCTGTTGTATCCCGGTGA
Enzyme 123 GenBank Gene ID NM_004938.2 Link Image
Enzyme 123 GeneCard ID DAPK1 Link Image
Enzyme 123 GenAtlas ID DAPK1 Link Image
Enzyme 123 HGNC ID HGNC:2674 Link Image
Enzyme 123 Chromosome Location 9
Enzyme 123 Locus 9q34.1
Enzyme 123 SNPs SNPJam Report Link Image
Enzyme 123 General References
  1. Deiss LP, Feinstein E, Berissi H, Cohen O, Kimchi A: Identification of a novel serine/threonine kinase and a novel 15-kD protein as potential mediators of the gamma interferon-induced cell death. Genes Dev. 1995 Jan 1;9(1):15-30. [PubMed Link Image]
  2. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  3. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Inbal B, Shani G, Cohen O, Kissil JL, Kimchi A: Death-associated protein kinase-related protein 1, a novel serine/threonine kinase involved in apoptosis. Mol Cell Biol. 2000 Feb;20(3):1044-54. [PubMed Link Image]
  6. Shohat G, Spivak-Kroizman T, Cohen O, Bialik S, Shani G, Berrisi H, Eisenstein M, Kimchi A: The pro-apoptotic function of death-associated protein kinase is controlled by a unique inhibitory autophosphorylation-based mechanism. J Biol Chem. 2001 Dec 14;276(50):47460-7. Epub 2001 Sep 28. [PubMed Link Image]
  7. Lee YR, Yuan WC, Ho HC, Chen CH, Shih HM, Chen RH: The Cullin 3 substrate adaptor KLHL20 mediates DAPK ubiquitination to control interferon responses. EMBO J. 2010 May 19;29(10):1748-61. Epub 2010 Apr 13. [PubMed Link Image]
  8. Tereshko V, Teplova M, Brunzelle J, Watterson DM, Egli M: Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression. Nat Struct Biol. 2001 Oct;8(10):899-907. [PubMed Link Image]
  9. Velentza AV, Wainwright MS, Zasadzki M, Mirzoeva S, Schumacher AM, Haiech J, Focia PJ, Egli M, Watterson DM: An aminopyridazine-based inhibitor of a pro-apoptotic protein kinase attenuates hypoxia-ischemia induced acute brain injury. Bioorg Med Chem Lett. 2003 Oct 20;13(20):3465-70. [PubMed Link Image]
  10. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 123 Metabolite References Not Available
Enzyme 124 [top]
Enzyme 124 ID 6590
Enzyme 124 Name V-type proton ATPase subunit B, kidney isoform
Enzyme 124 Synonyms
  1. V-ATPase subunit B 1
  2. Endomembrane proton pump 58 kDa subunit
  3. Vacuolar proton pump subunit B 1
Enzyme 124 Gene Name ATP6V1B1
Enzyme 124 Protein Sequence >V-type proton ATPase subunit B, kidney isoform 
MAMEIDSRPGGLPGSSCNLGAAREHMQAVTRNYITHPRVTYRTVCSVNGPLVVLDRVKFA
QYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPVSED
MLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARG
QKIPIFSAAGLPHNEIAAQICRQAGLVKKSKAVLDYHDDNFAIVFAAMGVNMETARFFKS
DFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEA
LREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRGGSITQIPILTMPNDDITHPIP
DLTGFITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHGDVSNQLYACY
AIGKDVQAMKAVVGEEALTSEDLLYLEFLQKFEKNFINQGPYENRSVFESLDLGWKLLRI
FPKEMLKRIPQAVIDEFYSREGALQDLAPDTAL
Enzyme 124 Number of Residues 513
Enzyme 124 Molecular Weight 56832.5
Enzyme 124 Theoretical pI 5.37
Enzyme 124 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • cation transmembrane transporter activity
  • hydrogen ion transmembrane transporter activity
  • hydrogen ion transporting ATP synthase activity, rotational mechanism
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
  • inorganic cation transmembrane transporter activity
  • ion transmembrane transporter activity
  • monovalent inorganic cation transmembrane transporter activity
  • nucleoside binding
  • proton-transporting ATPase activity, rotational mechanism
  • purine nucleoside binding
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • ATP metabolic process
  • ATP synthesis coupled proton transport
  • cellular nitrogen compound metabolic process
  • establishment of localization
  • hydrogen transport
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • proton transport
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleoside triphosphate metabolic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • purine ribonucleoside triphosphate metabolic process
  • transport
Component
  • macromolecular complex
  • protein complex
  • proton-transporting V-type ATPase, V1 domain
  • proton-transporting two-sector ATPase complex
  • proton-transporting two-sector ATPase complex, catalytic domain
Enzyme 124 General Function Involved in ATP binding
Enzyme 124 Specific Function Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells
Enzyme 124 Pathways
Enzyme 124 Reactions Not Available
Enzyme 124 Pfam Domain Function
Enzyme 124 Signals
  • None
Enzyme 124 Transmembrane Regions
  • None
Enzyme 124 Essentiality Not Available
Enzyme 124 GenBank ID Protein 62897863 Link Image
Enzyme 124 UniProtKB/Swiss-Prot ID P15313 Link Image
Enzyme 124 UniProtKB/Swiss-Prot Entry Name VATB1_HUMAN Link Image
Enzyme 124 PDB ID Not Available
Enzyme 124 Cellular Location Not Available
Enzyme 124 Gene Sequence >1542 bp 
ATGGCCATGGAGATAGACAGCAGGCCTGGGGGGCTCCCCGGCAGTAGCTGCAACCTAGGT
GCAGCCCGAGAACACATGCAGGCGGTCATCCGAAACTACATCACCCACCCCCGTGTCACC
TACAGGACTGTGTGCAGCGTGAACGGGCCCCTGGTGGTGCTGGACCGGGTCAAGTTTGCC
CAGTATGCGGAGATCGTCCACTTCACCCTCCCAGATGGGACTCAGAGGAGCGGGCAGGTG
CTTGAGGTGGCTGGCACCAAGGCGATTGTTCAGGTGTTTGAAGGGACATCAGGGATCGAT
GCCAGGAAGACCACTTGCGAATTTACAGGGGACATCCTACGAACTCCGGTGTCAGAGGAC
ATGCTGGGTCGGGTTTTCAATGGCTCCGGCAAGCCCATTGACAAGGGGCCAGTGGTCATG
GCGGAGGACTTTCTGGATATCAATGGCCAGCCCATCAACCCGCACTCCCGCATCTACCCC
GAGGAGATGATTCAGACGGGCATTTCTCCTATTGACGTCATGAACAGCATTGCCCGCGGC
CAGAAGATCCCCATCTTCTCAGCAGCCGGGCTCCCCCACAATGAGATTGCCGCTCAGATC
TGCCGCCAGGCGGGGCTGGTGAAGAAGTCCAAGGCTGTGCTGGATTACCATGACGACAAC
TTCGCCATCGTCTTTGCAGCCATGGGGGTGAACATGGAGACAGCCAGATTCTTCAAGTCT
GACTTTGAGCAGAATGGAACCATGGGGAACGTCTGCCTCTTCCTGAACTTGGCCAATGAC
CCCACGATCGAGCGGATCATCACCCCGCGCCTGGCGCTGACCACTGCTGAATTCCTTGCC
TACCAGTGTGAGAAGCATGTGCTGGTCATACTGACGGACATGAGTTCCTATGCAGAGGCC
TTGCGGGAGGTCTCTGCTGCTAGAGAGGAGGTGCCTGGGCGCCGAGGGTTTCCTGGATAT
ATGTACACAGACCTGGCCACCATCTACGAGCGGGCGGGCCGCGTGGAGGGTCGGGGAGGA
TCCATCACACAGATCCCCATCCTCACCATGCCCAACGACGATATCACCCACCCTATCCCA
GACTTGACGGGCTTCATCACAGAGGGACAGATCTACGTGGACAGACAGCTTCACAACAGA
CAGATCTACCCCCCCATCAACGTGCTCCCTTCCCTGTCGCGGCTGATGAAGTCAGCCATT
GGGGAAGGCATGACAAGAAAGGACCATGGAGATGTCTCCAACCAGCTGTACGCCTGCTAT
GCCATCGGGAAGGACGTGCAGGCCATGAAGGCAGTAGTTGGGGAGGAGGCGCTCACCTCT
GAGGACCTGCTCTACCTGGAATTCCTGCAGAAGTTTGAGAAGAACTTCATCAATCAGGGC
CCCTACGAGAACCGCTCGGTGTTCGAGTCGCTGGACCTGGGCTGGAAGCTGCTGCGCATC
TTCCCCAAGGAGATGCTGAAGCGCATTCCGCAGGCCGTGATCGACGAGTTCTATTCCCGC
GAGGGGGCGCTGCAGGACCTCGCGCCTGACACTGCGCTCTAG
Enzyme 124 GenBank Gene ID AK223151 Link Image
Enzyme 124 GeneCard ID ATP6V1B1 Link Image
Enzyme 124 GenAtlas ID ATP6V1B1 Link Image
Enzyme 124 HGNC ID HGNC:853 Link Image
Enzyme 124 Chromosome Location 2
Enzyme 124 Locus 2p13.1
Enzyme 124 SNPs SNPJam Report Link Image
Enzyme 124 General References
  1. Sudhof TC, Fried VA, Stone DK, Johnston PA, Xie XS: Human endomembrane H+ pump strongly resembles the ATP-synthetase of Archaebacteria. Proc Natl Acad Sci U S A. 1989 Aug;86(16):6067-71. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Pushkin A, Abuladze N, Newman D, Muronets V, Sassani P, Tatishchev S, Kurtz I: The COOH termini of NBC3 and the 56-kDa H+-ATPase subunit are PDZ motifs involved in their interaction. Am J Physiol Cell Physiol. 2003 Mar;284(3):C667-73. Epub 2002 Nov 20. [PubMed Link Image]
  5. Karet FE, Finberg KE, Nelson RD, Nayir A, Mocan H, Sanjad SA, Rodriguez-Soriano J, Santos F, Cremers CW, Di Pietro A, Hoffbrand BI, Winiarski J, Bakkaloglu A, Ozen S, Dusunsel R, Goodyer P, Hulton SA, Wu DK, Skvorak AB, Morton CC, Cunningham MJ, Jha V, Lifton RP: Mutations in the gene encoding B1 subunit of H+-ATPase cause renal tubular acidosis with sensorineural deafness. Nat Genet. 1999 Jan;21(1):84-90. [PubMed Link Image]
  6. Stover EH, Borthwick KJ, Bavalia C, Eady N, Fritz DM, Rungroj N, Giersch AB, Morton CC, Axon PR, Akil I, Al-Sabban EA, Baguley DM, Bianca S, Bakkaloglu A, Bircan Z, Chauveau D, Clermont MJ, Guala A, Hulton SA, Kroes H, Li Volti G, Mir S, Mocan H, Nayir A, Ozen S, Rodriguez Soriano J, Sanjad SA, Tasic V, Taylor CM, Topaloglu R, Smith AN, Karet FE: Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive distal renal tubular acidosis with new evidence for hearing loss. J Med Genet. 2002 Nov;39(11):796-803. [PubMed Link Image]
  7. Ruf R, Rensing C, Topaloglu R, Guay-Woodford L, Klein C, Vollmer M, Otto E, Beekmann F, Haller M, Wiedensohler A, Leumann E, Antignac C, Rizzoni G, Filler G, Brandis M, Weber JL, Hildebrandt F: Confirmation of the ATP6B1 gene as responsible for distal renal tubular acidosis. Pediatr Nephrol. 2003 Feb;18(2):105-9. Epub 2002 Dec 18. [PubMed Link Image]
Enzyme 124 Metabolite References Not Available
Enzyme 125 [top]
Enzyme 125 ID 6591
Enzyme 125 Name Calcium/calmodulin-dependent protein kinase type 1G
Enzyme 125 Synonyms
  1. CaM kinase I gamma
  2. CaM kinase IG
  3. CaM-KI gamma
  4. CaMKI gamma
  5. CaMKIG
  6. CaMK-like CREB kinase III
  7. CLICK III
Enzyme 125 Gene Name CAMK1G
Enzyme 125 Protein Sequence >Calcium/calmodulin-dependent protein kinase type 1G 
MGRKEEDDCSSWKKQTTNIRKTFIFMEVLGSGAFSEVFLVKQRLTGKLFALKCIKKSPAF
RDSSLENEIAVLKKIKHENIVTLEDIYESTTHYYLVMQLVSGGELFDRILERGVYTEKDA
SLVIQQVLSAVKYLHENGIVHRDLKPENLLYLTPEENSKIMITDFGLSKMEQNGIMSTAC
GTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESKLFEKIKEGYYEFES
PFWDDISESAKDFICHLLEKDPNERYTCEKALSHPWIDGNTALHRDIYPSVSLQIQKNFA
KSKWRQAFNAAAVVHHMRKLHMNLHSPGVRPEVENRPPETQASETSRPSSPEITITEAPV
LDHSVALPALTQLPCQHGRRPTAPGGRSLNCLVNGSLHISSSLVPMHQGSLAAGPCGCCS
SCLNIGSKGKSSYCSEPTLLKKANKKQNFKSEVMVPVKASGSSHCRAGQTGVCLIM
Enzyme 125 Number of Residues 476
Enzyme 125 Molecular Weight 53086.5
Enzyme 125 Theoretical pI 7.78
Enzyme 125 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
—
Enzyme 125 General Function Involved in protein kinase activity
Enzyme 125 Specific Function Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade. In vitro phosphorylates transcription factor CREB1
Enzyme 125 Pathways Not Available
Enzyme 125 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 125 Pfam Domain Function
Enzyme 125 Signals
  • None
Enzyme 125 Transmembrane Regions
  • None
Enzyme 125 Essentiality Not Available
Enzyme 125 GenBank ID Protein 16755792 Link Image
Enzyme 125 UniProtKB/Swiss-Prot ID Q96NX5 Link Image
Enzyme 125 UniProtKB/Swiss-Prot Entry Name KCC1G_HUMAN Link Image
Enzyme 125 PDB ID Not Available
Enzyme 125 Cellular Location Not Available
Enzyme 125 Gene Sequence >1431 bp 
ATGGGTCGAAAGGAAGAAGATGACTGCAGTTCCTGGAAGAAACAGACCACCAACATCCGG
AAAACCTTCATTTTTATGGAAGTGCTGGGATCAGGAGCTTTCTCAGAAGTTTTCCTGGTG
AAGCAAAGACTGACTGGGAAGCTCTTTGCTCTGAAGTGCATCAAGAAGTCACCTGCCTTC
CGGGACAGCAGCCTGGAGAATGAGATTGCTGTGTTGAAAAAGATCAAGCATGAAAACATT
GTGACCCTGGAGGACATCTATGAGAGCACCACCCACTACTACCTGGTCATGCAGCTTGTT
TCTGGTGGGGAGCTCTTTGACCGGATCCTGGAGCGGGGTGTCTACACAGAGAAGGATGCC
AGTCTGGTGATCCAGCAGGTCTTGTCGGCAGTGAAATACCTACATGAGAATGGCATCGTC
CACAGAGACTTAAAGCCCGAAAACCTGCTTTACCTTACCCCTGAAGAGAACTCTAAGATC
ATGATCACTGACTTTGGTCTGTCCAAGATGGAACAGAATGGCATCATGTCCACTGCCTGT
GGGACCCCAGGCTACGTGGCTCCAGAAGTGCTGGCCCAGAAACCCTACAGCAAGGCTGTG
GATTGCTGGTCCATCGGCGTCATCACCTACATATTGCTCTGTGGATACCCCCCGTTCTAT
GAAGAAACGGAGTCTAAGCTTTTCGAGAAGATCAAGGAGGGCTACTATGAGTTTGAGTCT
CCATTCTGGGATGACATTTCTGAGTCAGCCAAGGACTTTATTTGCCACTTGCTTGAGAAG
GATCCGAACGAGCGGTACACCTGTGAGAAGGCCTTGAGTCATCCCTGGATTGACGGAAAC
ACAGCCCTCCACCGGGACATCTACCCATCAGTCAGCCTCCAGATCCAGAAGAACTTTGCT
AAGAGCAAGTGGAGGCAAGCCTTCAACGCAGCAGCCGTGGTGCACCACATGAGGAAGCTA
CACATGAACCTGCACAGCCCGGGCATCCGCCCAGAGGTGGAGAACAGGCCGCCTGAAACT
CAAGCCTCAGAAACCTCTAGACCCAGCTCCCCTGAGATCACCATCACCGAGGCACCTGTC
CTGGACCACAGTGTAGCACTCCCTGCCCTGACCCAATTACCCTGCCAGCATGGCCGCCGG
CCCACTGCCCCTGGTGGCAGGTCCCTCAACTGCCTGGTCAATGGCTCCCTCCACATCAGC
AGCAGCCTGGTGCCCATGCATCAGGGGTCCCTGGCCGCCGGGCCCTGTGGCTGCTGCTCC
AGCTGCCTGAACATTGGGAACAAAGGAAAGTCCTCCTACTGCTCTGAGCCCACACTCCTC
AAAAAGGCCAACAAAAAACAGAACTTCAAGTCGGAGGTCATGGTACCAGTTAAAGCCAGT
GGCAGCTCCCACTGCCGGGCAGGGCAGACTGGAGTCTGTCTCATTATGTGA
Enzyme 125 GenBank Gene ID AF428261 Link Image
Enzyme 125 GeneCard ID CAMK1G Link Image
Enzyme 125 GenAtlas ID CAMK1G Link Image
Enzyme 125 HGNC ID HGNC:14585 Link Image
Enzyme 125 Chromosome Location 1
Enzyme 125 Locus 1q32-q41
Enzyme 125 SNPs SNPJam Report Link Image
Enzyme 125 General References
  1. Schutte BC, Bjork BC, Coppage KB, Malik MI, Gregory SG, Scott DJ, Brentzell LM, Watanabe Y, Dixon MJ, Murray JC: A preliminary gene map for the Van der Woude syndrome critical region derived from 900 kb of genomic sequence at 1q32-q41. Genome Res. 2000 Jan;10(1):81-94. [PubMed Link Image]
  2. Takemoto-Kimura S, Terai H, Takamoto M, Ohmae S, Kikumura S, Segi E, Arakawa Y, Furuyashiki T, Narumiya S, Bito H: Molecular cloning and characterization of CLICK-III/CaMKIgamma, a novel membrane-anchored neuronal Ca2+/calmodulin-dependent protein kinase (CaMK). J Biol Chem. 2003 May 16;278(20):18597-605. Epub 2003 Mar 11. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 125 Metabolite References Not Available
Enzyme 126 [top]
Enzyme 126 ID 6603
Enzyme 126 Name V-type proton ATPase 116 kDa subunit a isoform 4
Enzyme 126 Synonyms
  1. V-ATPase 116 kDa isoform a4
  2. Vacuolar proton translocating ATPase 116 kDa subunit a isoform 4
  3. Vacuolar proton translocating ATPase 116 kDa subunit a kidney isoform
Enzyme 126 Gene Name ATP6V0A4
Enzyme 126 Protein Sequence >V-type proton ATPase 116 kDa subunit a isoform 4 
MVSVFRSEEMCLSQLFLQVEAAYCCVAELGELGLVQFKDLNMNVNSFQRKFVNEVRRCES
LERILRFLEDEMQNEIVVQLLEKSPLTPLPREMITLETVLEKLEGELQEANQNQQALKQS
FLELTELKYLLKKTQDFFETETNLADDFFTEDTSGLLELKAVPAYMTGKLGFIAGVINRE
RMASFERLLWRICRGNVYLKFSEMDAPLEDPVTKEEIQKNIFIIFYQGEQLRQKIKKICD
GFRATVYPCPEPAVERREMLESVNVRLEDLITVITQTESHRQRLLQEAAANWHSWLIKVQ
KMKAVYHILNMCNIDVTQQCVIAEIWFPVADATRIKRALEQGMELSGSSMAPIMTTVQSK
TAPPTFNRTNKFTAGFQNIVDAYGVGSYREINPAPYTIITFPFLFAVMFGDCGHGTVMLL
AALWMILNERRLLSQKTDNEIWNTFFHGRYLILLMGIFSIYTGLIYNDCFSKSLNIFGSS
WSVQPMFRNGTWNTHVMEESLYLQLDPAIPGVYFGNPYPFGIDPIWNLASNKLTFLNSYK
MKMSVILGIVQMVFGVILSLFNHIYFRRTLNIILQFIPEMIFILCLFGYLVFMIIFKWCC
FDVHVSQHAPSILIHFINMFLFNYSDSSNAPLYKHQQEVQSFFVVMALISVPWMLLIKPF
ILRASHRKSQLQASRIQEDATENIEGDSSSPSSRSGQRTSADTHGALDDHGEEFNFGDVF
VHQAIHTIEYCLGCISNTASYLRLWALSLAHAQLSEVLWTMVMNSGLQTRGWGGIVGVFI
IFAVFAVLTVAILLIMEGLSAFLHALRLHWVEFQNKFYVGDGYKFSPFSFKHILDGTAEE
Enzyme 126 Number of Residues 840
Enzyme 126 Molecular Weight 96385.0
Enzyme 126 Theoretical pI 6.01
Enzyme 126 GO Classification
Function
  • cation transmembrane transporter activity
  • hydrogen ion transmembrane transporter activity
  • inorganic cation transmembrane transporter activity
  • ion transmembrane transporter activity
  • monovalent inorganic cation transmembrane transporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • ATP biosynthetic process
  • ATP synthesis coupled proton transport
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
Component
  • macromolecular complex
  • protein complex
  • proton-transporting two-sector ATPase complex, proton-transporting domain
Enzyme 126 General Function Involved in hydrogen ion transmembrane transporter activity
Enzyme 126 Specific Function Part of the proton channel of the V-ATPase that is involved in normal vectorial acid transport into the urine by the kidney
Enzyme 126 Pathways Not Available
Enzyme 126 Reactions Not Available
Enzyme 126 Pfam Domain Function
Enzyme 126 Signals
  • None
Enzyme 126 Transmembrane Regions
  • 403-423 450-470 546-566 576-596 603-623 642-662 744-764 775-795
Enzyme 126 Essentiality Not Available
Enzyme 126 GenBank ID Protein 85386053 Link Image
Enzyme 126 UniProtKB/Swiss-Prot ID Q9HBG4 Link Image
Enzyme 126 UniProtKB/Swiss-Prot Entry Name VPP4_HUMAN Link Image
Enzyme 126 PDB ID Not Available
Enzyme 126 Cellular Location Not Available
Enzyme 126 Gene Sequence >2523 bp 
ATGGTGTCTGTGTTTCGAAGCGAGGAGATGTGTTTGTCACAACTGTTTCTCCAGGTGGAA
GCTGCATATTGCTGTGTGGCTGAGCTCGGAGAGCTCGGATTGGTTCAGTTCAAAGATTTA
AATATGAATGTGAACAGCTTTCAAAGGAAATTTGTGAATGAAGTCAGAAGGTGTGAATCA
CTGGAGAGAATCCTCCGTTTTCTGGAAGACGAGATGCAAAATGAGATTGTAGTTCAGTTG
CTCGAGAAAAGCCCACTGACCCCGCTCCCACGGGAAATGATTACCCTGGAGACTGTTCTA
GAAAAACTGGAAGGAGAGTTACAGGAAGCCAACCAGAACCAGCAGGCCTTGAAACAAAGC
TTCCTAGAACTGACAGAACTGAAATACCTCCTGAAGAAAACCCAAGACTTCTTTGAGACG
GAAACCAATTTAGCTGATGATTTCTTTACTGAGGACACTTCTGGCCTCCTGGAGTTGAAA
GCAGTGCCTGCATATATGACCGGAAAGTTGGGGTTCATAGCCGGTGTGATCAACAGGGAG
AGGATGGCTTCCTTTGAGCGGTTACTGTGGCGAATCTGCCGAGGAAACGTGTACTTGAAG
TTCAGTGAGATGGACGCCCCTCTGGAGGATCCTGTGACGAAAGAAGAAATTCAGAAGAAC
ATATTCATCATATTTTACCAAGGAGAGCAGCTCAGGCAGAAAATCAAGAAGATCTGTGAT
GGGTTTCGAGCCACTGTCTACCCTTGCCCAGAGCCTGCGGTGGAGCGCAGAGAGATGTTG
GAGAGCGTCAATGTGAGGCTGGAAGATTTAATCACCGTCATAACACAAACAGAGTCTCAC
CGCCAGCGCCTGCTGCAGGAAGCCGCTGCCAACTGGCACTCCTGGCTCATCAAGGTGCAG
AAGATGAAAGCTGTCTACCACATCCTGAACATGTGCAACATCGACGTCACCCAGCAGTGT
GTCATCGCCGAGATCTGGTTCCCGGTGGCAGATGCCACACGTATCAAGAGGGCACTGGAG
CAAGGCATGGAACTAAGTGGCTCCTCCATGGCCCCCATCATGACCACAGTGCAATCTAAA
ACAGCCCCTCCCACATTTAACAGGACCAATAAATTCACAGCTGGCTTCCAGAATATTGTT
GATGCCTATGGTGTCGGCAGCTACCGGGAGATAAACCCAGCCCCCTACACCATCATCACT
TTCCCCTTCCTGTTCGCTGTGATGTTTGGAGACTGTGGTCATGGAACCGTGATGCTCCTG
GCTGCACTTTGGATGATTCTGAATGAGAGACGCTTGCTCTCCCAGAAGACAGACAATGAG
ATTTGGAACACCTTCTTCCACGGGCGCTATCTGATCCTACTTATGGGCATCTTCTCCATC
TACACGGGTTTGATCTACAATGACTGCTTCTCCAAGTCCTTGAACATCTTTGGCTCTTCT
TGGAGTGTCCAACCCATGTTCAGAAACGGCACATGGAATACTCATGTAATGGAGGAAAGT
CTATATCTGCAGCTGGACCCAGCCATACCAGGAGTGTATTTTGGAAATCCATACCCGTTT
GGGATTGATCCGATTTGGAACTTGGCTTCAAACAAACTCACATTTCTGAACTCGTATAAA
ATGAAGATGTCGGTGATCCTGGGAATTGTCCAGATGGTTTTCGGTGTCATCCTCAGCCTT
TTCAATCACATATACTTCAGAAGAACTCTCAACATCATTCTGCAATTTATCCCTGAGATG
ATTTTTATCCTGTGTCTGTTTGGATACCTGGTTTTCATGATCATTTTCAAATGGTGCTGC
TTTGACGTCCATGTATCTCAGCACGCCCCCAGCATCCTCATCCACTTCATCAACATGTTT
CTGTTTAACTACAGTGACTCTTCCAACGCACCCCTCTACAAACATCAGCAAGAAGTCCAA
AGTTTCTTTGTGGTTATGGCTTTGATTTCTGTGCCGTGGATGCTTCTGATTAAGCCGTTT
ATTCTTAGAGCCAGTCATCGGAAATCCCAGCTGCAGGCATCCAGGATCCAAGAAGATGCC
ACTGAGAACATTGAAGGTGATAGCTCCAGCCCTTCTAGCCGTTCTGGCCAGAGGACTTCT
GCAGATACCCACGGGGCTCTGGACGACCATGGAGAAGAGTTCAACTTTGGAGACGTCTTT
GTCCACCAAGCCATCCACACCATCGAGTACTGCCTGGGCTGCATTTCAAACACAGCCTCC
TACCTGCGGCTCTGGGCCCTCAGCCTGGCTCATGCACAACTGTCTGAAGTGCTCTGGACT
ATGGTGATGAACAGCGGCCTTCAGACGCGAGGCTGGGGAGGAATCGTCGGGGTTTTTATT
ATTTTTGCCGTATTTGCTGTCCTGACAGTAGCCATCCTTCTGATCATGGAGGGCCTCTCT
GCTTTCCTGCACGCCCTGCGACTGCACTGGGTTGAGTTCCAGAACAAGTTCTATGTCGGG
GATGGTTACAAGTTTTCTCCATTCTCCTTTAAACACATCCTGGATGGCACAGCCGAGGAG
TAG
Enzyme 126 GenBank Gene ID NM_020632.2 Link Image
Enzyme 126 GeneCard ID ATP6V0A4 Link Image
Enzyme 126 GenAtlas ID ATP6V0A4 Link Image
Enzyme 126 HGNC ID HGNC:866 Link Image
Enzyme 126 Chromosome Location 7
Enzyme 126 Locus 7q34
Enzyme 126 SNPs SNPJam Report Link Image
Enzyme 126 General References
  1. Smith AN, Skaug J, Choate KA, Nayir A, Bakkaloglu A, Ozen S, Hulton SA, Sanjad SA, Al-Sabban EA, Lifton RP, Scherer SW, Karet FE: Mutations in ATP6N1B, encoding a new kidney vacuolar proton pump 116-kD subunit, cause recessive distal renal tubular acidosis with preserved hearing. Nat Genet. 2000 Sep;26(1):71-5. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  4. Stover EH, Borthwick KJ, Bavalia C, Eady N, Fritz DM, Rungroj N, Giersch AB, Morton CC, Axon PR, Akil I, Al-Sabban EA, Baguley DM, Bianca S, Bakkaloglu A, Bircan Z, Chauveau D, Clermont MJ, Guala A, Hulton SA, Kroes H, Li Volti G, Mir S, Mocan H, Nayir A, Ozen S, Rodriguez Soriano J, Sanjad SA, Tasic V, Taylor CM, Topaloglu R, Smith AN, Karet FE: Novel ATP6V1B1 and ATP6V0A4 mutations in autosomal recessive distal renal tubular acidosis with new evidence for hearing loss. J Med Genet. 2002 Nov;39(11):796-803. [PubMed Link Image]
Enzyme 126 Metabolite References Not Available
Enzyme 127 [top]
Enzyme 127 ID 6612
Enzyme 127 Name Calcium/calmodulin-dependent protein kinase kinase 1
Enzyme 127 Synonyms
  1. CaM-KK 1
  2. CaM-kinase kinase 1
  3. CaMKK 1
  4. CaM-kinase IV kinase
  5. Calcium/calmodulin-dependent protein kinase kinase alpha
  6. CaM-KK alpha
  7. CaM-kinase kinase alpha
  8. CaMKK alpha
Enzyme 127 Gene Name CAMKK1
Enzyme 127 Protein Sequence >Calcium/calmodulin-dependent protein kinase kinase 1 
MEGGPAVCCQDPRAELVERVAAIDVTHLEEADGGPEPTRNGVDPPPRARAASVIPGSTSR
LLPARPSLSARKLSLQERPAGSYLEAQAGPYATGPASHISPRAWRRPTIESHHVAISDAE
DCVQLNQYKLQSEIGKGAYGVVRLAYNESEDRHYAMKVLSKKKLLKQYGFPRRPPPRGSQ
AAQGGPAKQLLPLERVYQEIAILKKLDHVNVVKLIEVLDDPAEDNLYLVFDLLRKGPVME
VPCDKPFSEEQARLYLRDVILGLEYLHCQKIVHRDIKPSNLLLGDDGHVKIADFGVSNQF
EGNDAQLSSTAGTPAFMAPEAISDSGQSFSGKALDVWATGVTLYCFVYGKCPFIDDFILA
LHRKIKNEPVVFPEEPEISEELKDLILKMLDKNPETRIGVPDIKLHPWVTKNGEEPLPSE
EEHCSVVEVTEEEVKNSVRLIPSWTTVILVKSMLRKRSFGNPFEPQARREERSMSAPGNL
LVKEGFGEGGKSPELPGVQEDEAAS
Enzyme 127 Number of Residues 505
Enzyme 127 Molecular Weight 55735.0
Enzyme 127 Theoretical pI 5.55
Enzyme 127 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
—
Enzyme 127 General Function Involved in protein kinase activity
Enzyme 127 Specific Function Calcium/calmodulin-dependent protein kinase that belongs to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1, CAMK1D, CAMK1G and CAMK4. Involved in regulating cell apoptosis. Promotes cell survival by phosphorylating AKT1/PKB that inhibits pro-apoptotic BAD/Bcl2-antagonist of cell death
Enzyme 127 Pathways Not Available
Enzyme 127 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 127 Pfam Domain Function
Enzyme 127 Signals
  • None
Enzyme 127 Transmembrane Regions
  • None
Enzyme 127 Essentiality Not Available
Enzyme 127 GenBank ID Protein 23499314 Link Image
Enzyme 127 UniProtKB/Swiss-Prot ID Q8N5S9 Link Image
Enzyme 127 UniProtKB/Swiss-Prot Entry Name KKCC1_HUMAN Link Image
Enzyme 127 PDB ID Not Available
Enzyme 127 Cellular Location Not Available
Enzyme 127 Gene Sequence >1518 bp 
ATGGAGGGGGGTCCAGCTGTCTGCTGCCAGGATCCTCGGGCAGAGCTGGTAGAACGGGTG
GCAGCCATCGATGTGACTCACTTGGAGGAGGCAGATGGTGGCCCAGAGCCTACTAGAAAC
GGTGTGGACCCCCCACCACGGGCCAGAGCTGCCTCTGTGATCCCTGGCAGTACTTCAAGA
CTGCTCCCAGCCCGGCCTAGCCTCTCAGCCAGGAAGCTTTCCCTACAGGAGCGGCCAGCA
GGAAGCTATCTGGAGGCGCAGGCTGGGCCTTATGCCACGGGGCCTGCCAGCCACATCTCC
CCCCGGGCCTGGCGGAGGCCCACCATCGAGTCCCACCACGTGGCCATCTCAGATGCAGAG
GACTGCGTGCAGCTGAACCAGTACAAGCTGCAGAGTGAGATTGGCAAGGGTGCCTACGGT
GTGGTGAGGCTGGCCTACAACGAAAGTGAAGACAGACACTATGCAATGAAAGTCCTTTCC
AAAAAGAAGTTACTGAAGCAGTATGGCTTTCCACGTCGCCCTCCCCCGAGAGGGTCCCAG
GCTGCCCAGGGAGGACCAGCCAAGCAGCTGCTGCCCCTGGAGCGGGTGTACCAGGAGATT
GCCATCCTGAAGAAGCTGGACCACGTGAATGTGGTCAAACTGATCGAGGTCCTGGATGAC
CCAGCTGAGGACAACCTCTATTTGGTGTTTGACCTCCTGAGAAAGGGGCCCGTCATGGAA
GTGCCCTGTGACAAGCCCTTCTCGGAGGAGCAAGCTCGCCTCTACCTGCGGGACGTCATC
CTGGGCCTCGAGTACTTGCACTGCCAGAAGATCGTCCACAGGGACATCAAGCCATCCAAC
CTGCTCCTGGGGGATGATGGGCACGTGAAGATCGCCGACTTTGGCGTCAGCAACCAGTTT
GAGGGGAACGACGCTCAGCTGTCCAGCACGGCGGGAACCCCAGCATTCATGGCCCCCGAG
GCCATTTCTGATTCCGGCCAGAGCTTCAGTGGGAAGGCCTTGGATGTATGGGCCACTGGC
GTCACGTTGTACTGCTTTGTCTATGGGAAGTGCCCATTCATCGACGATTTCATCCTGGCC
CTCCACAGGAAGATCAAGAATGAGCCCGTGGTGTTTCCTGAGGAGCCAGAAATCAGCGAG
GAGCTCAAGGACCTGATCCTGAAGATGTTAGACAAGAATCCCGAGACGAGAATTGGGGTG
CCAGACATCAAGTTGCACCCTTGGGTGACCAAGAACGGGGAGGAGCCCCTTCCTTCGGAG
GAGGAGCACTGCAGCGTGGTGGAGGTGACAGAGGAGGAGGTTAAGAACTCAGTCAGGCTC
ATCCCCAGCTGGACCACGGTGATCCTGGTGAAGTCCATGCTGAGGAAGCGTTCCTTTGGG
AACCCGTTTGAGCCCCAAGCACGGAGGGAAGAGCGATCCATGTCTGCTCCAGGAAACCTA
CTGGTGAAAGAAGGGTTTGGTGAAGGGGGCAAGAGCCCAGAGCTCCCCGGCGTCCAGGAA
GACGAGGCTGCATCCTGA
Enzyme 127 GenBank Gene ID AF425232 Link Image
Enzyme 127 GeneCard ID CAMKK1 Link Image
Enzyme 127 GenAtlas ID CAMKK1 Link Image
Enzyme 127 HGNC ID HGNC:1469 Link Image
Enzyme 127 Chromosome Location 1
Enzyme 127 Locus 17p13.2
Enzyme 127 SNPs SNPJam Report Link Image
Enzyme 127 General References
  1. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Ishikawa Y, Tokumitsu H, Inuzuka H, Murata-Hori M, Hosoya H, Kobayashi R: Identification and characterization of novel components of a Ca2+/calmodulin-dependent protein kinase cascade in HeLa cells. FEBS Lett. 2003 Aug 28;550(1-3):57-63. [PubMed Link Image]
  4. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  5. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  6. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
  7. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 127 Metabolite References Not Available
Enzyme 128 [top]
Enzyme 128 ID 6617
Enzyme 128 Name Calcium/calmodulin-dependent protein kinase type 1
Enzyme 128 Synonyms
  1. CaM kinase I
  2. CaM-KI
  3. CaM kinase I alpha
  4. CaMKI-alpha
Enzyme 128 Gene Name CAMK1
Enzyme 128 Protein Sequence >Calcium/calmodulin-dependent protein kinase type 1 
MLGAVEGPRWKQAEDIRDIYDFRDVLGTGAFSEVILAEDKRTQKLVAIKCIAKEALEGKE
GSMENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGELFDRIVEKGFYTERDASR
LIFQVLDAVKYLHDLGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKMEDPGSVLSTACG
TPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSP
YWDDISDSAKDFIRHLMEKDPEKRFTCEQALQHPWIAGDTALDKNIHQSVSEQIKKNFAK
SKWKQAFNATAVVRHMRKLQLGTSQEGQGQTASHGELLTPVAGGPAAGCCCRDCCVEPGT
ELSPTLPHQL
Enzyme 128 Number of Residues 370
Enzyme 128 Molecular Weight 41336.7
Enzyme 128 Theoretical pI 4.92
Enzyme 128 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • protein kinase activity
  • protein serine/threonine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
—
Enzyme 128 General Function Involved in protein kinase activity
Enzyme 128 Specific Function Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes like transcriptional regulation, hormone production, translational regulation, regulation of actin filament organization and neurite outgrowth. Involved in calcium- dependent activation of the ERK pathway. Recognizes the substrate consensus sequence [MVLIF]-x-R-x(2)-[ST]- x(3)-[MVLIF]. Phosphorylates EIF4G3/eIF4GII. In vitro phosphorylates CREB1, ATF1, CTFR, MYL9, SYN1/synapsin I and SYNII/synapsin II
Enzyme 128 Pathways Not Available
Enzyme 128 Reactions
  • ATP + a protein = ADP + a phosphoprotein [RN:R00162]
Enzyme 128 Pfam Domain Function
Enzyme 128 Signals
  • None
Enzyme 128 Transmembrane Regions
  • None
Enzyme 128 Essentiality Not Available
Enzyme 128 GenBank ID Protein 76827734 Link Image
Enzyme 128 UniProtKB/Swiss-Prot ID Q14012 Link Image
Enzyme 128 UniProtKB/Swiss-Prot Entry Name KCC1A_HUMAN Link Image
Enzyme 128 PDB ID 1A06 Link Image
Enzyme 128 PDB File Show
Enzyme 128 3D Structure
Enzyme 128 Cellular Location Not Available
Enzyme 128 Gene Sequence >1113 bp 
ATGCTGGGGGCAGTGGAAGGCCCCAGGTGGAAGCAGGCGGAGGACATTAGAGACATCTAC
GACTTCCGAGATGTTCTGGGCACGGGGGCCTTCTCGGAGGTGATCCTGGCAGAAGATAAG
AGGACGCAGAAGCTGGTGGCCATCAAATGCATTGCCAAGGAGGCCCTGGAGGGCAAGGAA
GGCAGCATGGAGAATGAGATTGCTGTCCTGCACAAGATCAAGCACCCCAACATTGTAGCC
CTGGATGACATCTATGAGAGTGGGGGCCACCTCTACCTCATCATGCAGCTGGTGTCGGGT
GGGGAGCTCTTTGACCGTATTGTGGAAAAAGGCTTCTACACGGAGCGGGACGCCAGCCGC
CTCATCTTCCAGGTGCTGGATGCTGTGAAATACCTGCATGACCTGGGCATTGTACACCGG
GATCTCAAGCCAGAGAATCTGCTGTACTACAGCCTGGATGAAGACTCCAAAATCATGATC
TCCGACTTTGGCCTCTCCAAGATGGAGGACCCGGGCAGTGTGCTCTCCACCGCCTGTGGA
ACTCCGGGATACGTGGCCCCTGAAGTCCTGGCCCAGAAGCCCTACAGCAAGGCTGTGGAT
TGCTGGTCCATAGGTGTCATCGCCTACATCTTGCTCTGCGGTTACCCTCCCTTCTATGAC
GAGAATGATGCCAAACTCTTTGAACAGATTTTGAAGGCCGAGTACGAGTTTGACTCTCCT
TACTGGGACGACATCTCTGACTCTGCCAAAGATTTCATCCGGCACTTGATGGAGAAGGAC
CCAGAGAAAAGATTCACCTGTGAGCAGGCCTTGCAGCACCCATGGATTGCAGGAGATACA
GCTCTAGATAAGAATATCCACCAGTCGGTGAGTGAGCAGATCAAGAAGAACTTTGCCAAG
AGCAAGTGGAAGCAAGCCTTCAATGCCACGGCTGTGGTGCGGCACATGAGGAAACTGCAG
CTGGGCACCAGCCAGGAGGGGCAGGGGCAGACGGCGAGCCATGGGGAGCTGCTGACACCA
GTGGCTGGGGGGCCGGCAGCTGGCTGTTGCTGTCGAGACTGCTGCGTGGAGCCGGGCACA
GAACTGTCCCCCACACTGCCCCACCAGCTCTAG
Enzyme 128 GenBank Gene ID BC106754 Link Image
Enzyme 128 GeneCard ID CAMK1 Link Image
Enzyme 128 GenAtlas ID CAMK1 Link Image
Enzyme 128 HGNC ID HGNC:1459 Link Image
Enzyme 128 Chromosome Location 3
Enzyme 128 Locus 3p25.3
Enzyme 128 SNPs SNPJam Report Link Image
Enzyme 128 General References
  1. Haribabu B, Hook SS, Selbert MA, Goldstein EG, Tomhave ED, Edelman AM, Snyderman R, Means AR: Human calcium-calmodulin dependent protein kinase I: cDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase I kinase. EMBO J. 1995 Aug 1;14(15):3679-86. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  4. Hsu LS, Tsou AP, Chi CW, Lee CH, Chen JY: Cloning, expression and chromosomal localization of human Ca2+/calmodulin-dependent protein kinase kinase. J Biomed Sci. 1998;5(2):141-9. [PubMed Link Image]
  5. Hsu LS, Chen GD, Lee LS, Chi CW, Cheng JF, Chen JY: Human Ca2+/calmodulin-dependent protein kinase kinase beta gene encodes multiple isoforms that display distinct kinase activity. J Biol Chem. 2001 Aug 17;276(33):31113-23. Epub 2001 Jun 6. [PubMed Link Image]
  6. Qin H, Raught B, Sonenberg N, Goldstein EG, Edelman AM: Phosphorylation screening identifies translational initiation factor 4GII as an intracellular target of Ca(2+)/calmodulin-dependent protein kinase I. J Biol Chem. 2003 Dec 5;278(49):48570-9. Epub 2003 Sep 24. [PubMed Link Image]
  7. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed Link Image]
Enzyme 128 Metabolite References Not Available
Enzyme 129 [top]
Enzyme 129 ID 6618
Enzyme 129 Name Tyrosine-protein kinase Fyn
Enzyme 129 Synonyms
  1. Proto-oncogene Syn
  2. Proto-oncogene c-Fyn
  3. Src-like kinase
  4. SLK
  5. p59-Fyn
Enzyme 129 Gene Name FYN
Enzyme 129 Protein Sequence >Tyrosine-protein kinase Fyn 
MGCVQCKDKEATKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQG
LTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWW
EARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESET
TKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCC
RLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKT
LKPGTMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKDGEGR
ALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEY
TARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVE
RGYRMPCPQDCPISLHELMIHCWKKDPEERPTFEYLQSFLEDYFTATEPQYQPGENL
Enzyme 129 Number of Residues 537
Enzyme 129 Molecular Weight 60761.5
Enzyme 129 Theoretical pI 6.65
Enzyme 129 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • non-membrane spanning protein tyrosine kinase activity
  • nucleoside binding
  • protein binding
  • protein kinase activity
  • protein tyrosine kinase activity
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolic process
  • metabolic process
  • peptidyl-tyrosine phosphorylation
  • phosphate metabolic process
  • phosphorus metabolic process
  • phosphorylation
  • protein amino acid phosphorylation
Component
—
Enzyme 129 General Function Involved in protein kinase activity
Enzyme 129 Specific Function Implicated in the control of cell growth. Plays a role in the regulation of intracellular calcium levels, with isoform 2 showing the greater ability to mobilize cytoplasmic calcium in comparison to isoform 1. Required in brain development and mature brain function with important roles in the regulation of axon growth, axon guidance, and neurite extension. Blocks axon outgrowth and attraction induced by NTN1 by phosphorylating its receptor DDC
Enzyme 129 Pathways Not Available
Enzyme 129 Reactions
  • ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate [RN:R02584]
Enzyme 129 Pfam Domain Function
Enzyme 129 Signals
  • None
Enzyme 129 Transmembrane Regions
  • None
Enzyme 129 Essentiality Not Available
Enzyme 129 GenBank ID Protein 197692287 Link Image
Enzyme 129 UniProtKB/Swiss-Prot ID P06241 Link Image
Enzyme 129 UniProtKB/Swiss-Prot Entry Name FYN_HUMAN Link Image
Enzyme 129 PDB ID Not Available
Enzyme 129 Cellular Location Not Available
Enzyme 129 Gene Sequence >1614 bp 
ATGGGCTGTGTGCAATGTAAGGATAAAGAAGCAACAAAACTGACGGAGGAGAGGGACGGC
AGCCTGAACCAGAGCTCTGGGTACCGCTATGGCACAGACCCCACCCCTCAGCACTACCCC
AGCTTCGGTGTGACCTCCATCCCCAACTACAACAACTTCCACGCAGCCGGGGGCCAAGGA
CTCACCGTCTTTGGAGGTGTGAACTCTTCGTCTCATACGGGGACCTTGCGTACGAGAGGA
GGAACAGGAGTGACACTCTTTGTGGCCCTTTATGACTATGAAGCACGGACAGAAGATGAC
CTGAGTTTTCACAAAGGAGAAAAATTTC