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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 2009-08-20 16:44:33
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
SDF File Show
PDB File Show
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 Blood
Value 2300.00 (2100.00-2650.00) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
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 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
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]
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. 1-O-acylceramide synthase precursor
  2. Calcium-dependent phospholipase A2 precursor
  3. Group IIF secretory phospholipase A2 precursor
  4. Cytosolic phospholipase A2
  5. Phospholipase A2 precursor
  6. Group XIIB secretory phospholipase A2-like protein precursor
  7. Group 10 secretory phospholipase A2 precursor
  8. Group IIE secretory phospholipase A2 precursor
  9. Group XIIA secretory phospholipase A2 precursor
  10. Phospholipase A2, membrane associated precursor
  11. Group IID secretory phospholipase A2 precursor
  12. Ectonucleoside triphosphate diphosphohydrolase 1
  13. Soluble calcium-activated nucleotidase 1
  14. Ectonucleoside triphosphate diphosphohydrolase 3
  15. Glycerol-3-phosphate dehydrogenase, mitochondrial precursor
  16. Glucosamine-6-phosphate isomerase
  17. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 1
  18. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 4
  19. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 2
  20. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 3
  21. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma 2
  22. Diacylglycerol kinase alpha
  23. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma 1
  24. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta 1
  25. Thyroid peroxidase precursor
  26. Lactoperoxidase precursor
  27. Myeloperoxidase precursor
  28. Eosinophil peroxidase precursor
  29. Arylsulfatase D precursor
  30. Arylsulfatase B precursor
  31. Arylsulfatase E precursor
  32. Annexin A3
  33. Type I inositol-1,4,5-trisphosphate 5-phosphatase
  34. Amiloride-sensitive amine oxidase [copper-containing] precursor
  35. Glyoxylate reductase/hydroxypyruvate reductase
  36. Membrane copper amine oxidase
  37. Retina-specific copper amine oxidase precursor
  38. Deoxyribonuclease-1 precursor
  39. Steryl-sulfatase precursor
  40. Cytosolic phospholipase A2 gamma precursor
  41. Group 3 secretory phospholipase A2 precursor
  42. Platelet-activating factor acetylhydrolase IB subunit alpha
  43. Bis(5'-adenosyl)-triphosphatase
  44. Protein-glutamine gamma-glutamyltransferase E precursor
  45. Protein-glutamine gamma-glutamyltransferase 2
  46. Protein-arginine deiminase type-6
  47. Coagulation factor XIII A chain precursor
  48. Protein-arginine deiminase type-4
  49. Protein-arginine deiminase type-3
  50. Protein-glutamine gamma-glutamyltransferase 5
  51. Protein-glutamine gamma-glutamyltransferase 4
  52. Protein-glutamine gamma-glutamyltransferase K
  53. Protein-arginine deiminase type-2
  54. Protein-arginine deiminase type-1
  55. Protein-glutamine gamma-glutamyltransferase 6
  56. Protein-glutamine gamma-glutamyltransferase Z
  57. Adenylate cyclase type 7
  58. Adenylate cyclase type 4
  59. Adenylate cyclase type 6
  60. Adenylate cyclase type 5
  61. Adenylate cyclase type 8
  62. Adenylate cyclase type 9
  63. Adenylate cyclase type 3
  64. Adenylate cyclase type 1
  65. Fumarylacetoacetase
  66. Serine--pyruvate aminotransferase
  67. Transketolase-like protein 1
  68. Transketolase
  69. Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
  70. Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
  71. Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
  72. Ectonucleoside triphosphate diphosphohydrolase 4
  73. Ectonucleoside triphosphate diphosphohydrolase 6
  74. Ectonucleoside triphosphate diphosphohydrolase 5 precursor
  75. ADP-ribosyl cyclase 2 precursor
  76. Adenylate cyclase type 2
  77. Nitric oxide synthase, inducible
  78. Nitric-oxide synthase, brain
  79. Nitric-oxide synthase, endothelial
  80. Protein O-mannosyl-transferase 1
  81. Protein O-mannosyl-transferase 2
  82. 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase
  83. Arachidonate 5-lipoxygenase
  84. Inositol-trisphosphate 3-kinase B
  85. Inositol-trisphosphate 3-kinase A
  86. Polypeptide N-acetylgalactosaminyltransferase 11
  87. Polypeptide N-acetylgalactosaminyltransferase 4
  88. Polypeptide N-acetylgalactosaminyltransferase 3
  89. Probable polypeptide N-acetylgalactosaminyltransferase 8
  90. Polypeptide N-acetylgalactosaminyltransferase-like protein 2
  91. Putative polypeptide N-acetylgalactosaminyltransferase-like protein 1
  92. Polypeptide N-acetylgalactosaminyltransferase 10
  93. Polypeptide N-acetylgalactosaminyltransferase 13
  94. Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3
  95. Putative polypeptide N-acetylgalactosaminyltransferase-like protein 4
  96. N-acetylgalactosaminyltransferase 7
  97. Polypeptide N-acetylgalactosaminyltransferase 6
  98. Polypeptide N-acetylgalactosaminyltransferase 14
  99. Polypeptide N-acetylgalactosaminyltransferase 2
  100. Polypeptide N-acetylgalactosaminyltransferase 12
  101. Polypeptide N-acetylgalactosaminyltransferase 1
  102. Polypeptide N-acetylgalactosaminyltransferase 5
  103. 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial precursor
  104. Retinal guanylyl cyclase 1 precursor
  105. Retinal guanylyl cyclase 2 precursor
  106. Gamma-enolase
  107. Cyclic nucleotide-gated cation channel alpha 3
  108. Cyclic nucleotide-gated cation channel beta 3
  109. Death-associated protein kinase 2
  110. Plasma membrane calcium-transporting ATPase 3
  111. Protein kinase C alpha type
  112. Serine/threonine-protein kinase 38
  113. MAP kinase-activated protein kinase 5
  114. Plasma membrane calcium-transporting ATPase 1
  115. Myosin light chain kinase 2, skeletal/cardiac muscle
  116. Calcium/calmodulin-dependent protein kinase type 1D
  117. Plasma membrane calcium-transporting ATPase 2
  118. Serine/threonine-protein kinase 38-like
  119. Calcium-transporting ATPase type 2C member 2
  120. Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing beta polypeptide
  121. Sarcoplasmic/endoplasmic reticulum calcium ATPase 3
  122. Death-associated protein kinase 1
  123. Vacuolar ATP synthase subunit B, kidney isoform
  124. Calcium/calmodulin-dependent protein kinase type 1G
  125. Vacuolar proton translocating ATPase 116 kDa subunit a isoform 4
  126. Calcium/calmodulin-dependent protein kinase kinase 1
  127. Calcium/calmodulin-dependent protein kinase type 1
  128. Proto-oncogene tyrosine-protein kinase Fyn
  129. Serine/threonine-protein kinase PLK3
  130. Calcium/calmodulin-dependent protein kinase kinase 2
  131. Plasma membrane calcium-transporting ATPase 4
  132. Serine/threonine-protein kinase DCAMKL1
  133. Protein kinase C beta type
  134. Protein kinase C zeta type
  135. Calcium/calmodulin-dependent protein kinase type IV
  136. Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
  137. Calcium-transporting ATPase type 2C member 1
  138. Ceramide kinase
  139. Myosin light chain kinase, smooth muscle
  140. Protein tyrosine kinase 2 beta
  141. Protein kinase C iota type
  142. Tyrosine-protein kinase SYK
  143. Ectonucleoside triphosphate diphosphohydrolase 2
  144. Calcium/calmodulin-dependent protein kinase type II delta chain
  145. Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
  146. Serine/threonine-protein kinase D1
  147. Protein kinase C gamma type
  148. Transient receptor potential cation channel subfamily M member 7
  149. N-sulphoglucosamine sulphohydrolase precursor
  150. Iduronate 2-sulfatase precursor
  151. N-acetylglucosamine-6-sulfatase precursor
  152. Glutamate [NMDA] receptor subunit zeta-1 precursor
  153. Lin-7 homolog A
  154. Glutamate [NMDA] receptor subunit 3B precursor
  155. Glutamate [NMDA] receptor subunit epsilon-1 precursor
  156. Glutamate [NMDA] receptor subunit epsilon-3 precursor
  157. Glutamate [NMDA] receptor subunit epsilon-2 precursor
  158. Glutamate [NMDA] receptor subunit epsilon-4 precursor
  159. AMBP protein precursor [Contains: Alpha-1-microglobulin
  160. Nuclear factor of activated T-cells, cytoplasmic 2
  161. Vitamin K-dependent gamma-carboxylase
  162. UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
  163. Basement membrane-specific heparan sulfate proteoglycan core protein precursor
  164. Vasopressin V1a receptor
  165. Coagulation factor VIII precursor
  166. Coagulation factor IX precursor
  167. Protein NDRG1
  168. Calcium-activated potassium channel subunit alpha 1
  169. Elastin precursor
  170. Collagen alpha-1(I) chain precursor
  171. Collagen alpha-2(I) chain precursor
  172. Beta-1-syntrophin
  173. Tropomyosin alpha-4 chain
  174. Calmodulin
  175. Vitamin D3 receptor
  176. Cytochrome P450 24A1, mitochondrial precursor
  177. Calbindin
  178. Glutamate receptor, ionotropic kainate 2 precursor
  179. Proprotein convertase subtilisin/kexin type 6 precursor
  180. Vasopressin V1b receptor
  181. Prothrombin precursor
  182. Leukotriene B4 receptor 1
  183. Protein kinase C delta type
  184. Serine/threonine-protein kinase D3
  185. Protein kinase C theta type
  186. Protein kinase C eta type
  187. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase eta 2
  188. Protein kinase C epsilon type
  189. Type II inositol-1,4,5-trisphosphate 5-phosphatase precursor
  190. Nuclear factor of activated T-cells, cytoplasmic 1
  191. Endothelial differentiation-related factor 1
  192. Calmodulin-like protein 3
  193. Protein S100-A8
  194. Laforin
  195. Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
  196. 5'-AMP-activated protein kinase catalytic subunit alpha-1
  197. 5'-AMP-activated protein kinase catalytic subunit alpha-2
  198. Histone H2A type 1-C
  199. Histone H2A type 1-J
  200. Histone H2A type 1-D
  201. Histone H2A type 2-C
  202. Prostaglandin F2-alpha receptor
  203. Oxytocin receptor
  204. Phospholipid scramblase 1
  205. Enhancer of filamentation 1
  206. P-selectin glycoprotein ligand 1 precursor
  207. Tenascin-R precursor
  208. Voltage-dependent L-type calcium channel subunit alpha-1D
  209. Transient receptor potential cation channel subfamily M member 2
  210. Vitamin K-dependent protein C precursor
  211. Osteocalcin
  212. Osteocalcin precursor
  213. Coagulation factor X precursor
  214. Growth-arrest-specific protein 6 precursor
  215. Coagulation factor VII precursor
  216. Thromboxane A2 receptor
  217. Free fatty acid receptor 3
  218. Free fatty acid receptor 2
  219. Free fatty acid receptor 1
  220. Protocadherin-8 precursor
  221. Parathyroid hormone precursor
  222. C-reactive protein precursor [Contains: C-reactive protein(1-205)]
  223. Salivary alpha-amylase precursor
  224. Pancreatic alpha-amylase precursor
  225. Annexin A5
  226. SPARC precursor
  227. Coagulation factor V precursor
  228. Parathyroid hormone-related protein precursor
  229. Matrix metalloproteinase-9 precursor
  230. Alpha-amylase 2B precursor
  231. fMet-Leu-Phe receptor
  232. FMLP-related receptor I
  233. Type-1 angiotensin II receptor
  234. N-acetylgalactosamine-6-sulfatase precursor
  235. Metabotropic glutamate receptor 5 precursor
  236. Collagenase 3 precursor
  237. Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform
  238. Alpha-S1-casein precursor [Contains: Casoxin-D]
  239. Nucleobindin-2 precursor
  240. Metabotropic glutamate receptor 1 precursor
  241. Tubulin beta-3 chain
  242. Voltage-dependent L-type calcium channel subunit alpha-1C
  243. Transient receptor potential cation channel subfamily M member 8
  244. Transient receptor potential cation channel subfamily V member 1
  245. Calcium-binding protein p22
  246. Small inducible cytokine B16 precursor
  247. Homer protein homolog 2
  248. Cysteinyl leukotriene receptor 1
  249. Endothelin-1 receptor precursor
  250. Annexin A2
  251. Protein S100-A9
  252. Extracellular sulfatase Sulf-1 precursor
  253. Perforin-1 precursor
  254. Gamma-aminobutyric acid type B receptor, subunit 1 precursor
  255. Neurogenic locus notch homolog protein 1 precursor
  256. Calcium-binding mitochondrial carrier protein Aralar2
  257. Transient receptor potential cation channel subfamily V member 6
  258. Cysteinyl leukotriene receptor 2
  259. 5-hydroxytryptamine 2B receptor
  260. Prostaglandin E2 receptor, EP1 subtype
  261. Pro-epidermal growth factor precursor
  262. Delta-type opioid receptor
  263. P2Y purinoceptor 2
  264. Interstitial collagenase precursor
  265. BCL2/adenovirus E1B 19 kDa protein-interacting protein 3
  266. Platelet-activating factor receptor
  267. Arylsulfatase H
  268. Endothelin B receptor precursor
  269. Gastrin/cholecystokinin type B receptor
  270. Recoverin
  271. Stromelysin-1 precursor
  272. Matrix metalloproteinase-20 precursor
  273. Short transient receptor potential channel 3
  274. Cardiac phospholamban
  275. Cubilin precursor
  276. Calretinin
  277. Mu-type opioid receptor
  278. Anthrax toxin receptor 1 precursor
  279. Mannose-binding protein C precursor
  280. 5-hydroxytryptamine 2A receptor
  281. Pulmonary surfactant-associated protein A2 precursor
  282. S-arrestin
  283. Cytochrome P450 2R1
  284. Bone morphogenetic protein 7 precursor
  285. 5-hydroxytryptamine 2C receptor
  286. Histamine H3 receptor
  287. Extracellular calcium-sensing receptor precursor
  288. Low-density lipoprotein receptor-related protein 2 precursor
  289. Fibroblast growth factor 23 precursor
  290. Prostaglandin D2 receptor
  291. Tumor necrosis factor receptor superfamily member 11B precursor
  292. Caldesmon
  293. Progressive ankylosis protein homolog
  294. CD209 antigen
  295. Membrane-bound transcription factor site-1 protease precursor
  296. Calsenilin
  297. 72 kDa type IV collagenase precursor
  298. Gonadotropin-releasing hormone receptor
  299. Heparanase precursor
  300. Dual specificity protein phosphatase 2
  301. Asialoglycoprotein receptor 2
  302. Myosin regulatory light chain 2, nonsarcomeric
  303. Parvalbumin alpha
  304. Inositol 1,4,5-trisphosphate receptor type 1
  305. Epithelial-cadherin precursor
  306. Transient receptor potential cation channel subfamily V member 4
  307. Matrix metalloproteinase-14 precursor
  308. Cadherin-15 precursor
  309. C-type lectin domain family 4 member M
  310. Matrilysin precursor
  311. P2Y purinoceptor 1
  312. Polypeptide N-acetylgalactosaminyltransferase 14
  313. Peroxiredoxin-2
  314. Sodium/calcium exchanger 1 precursor
  315. Sodium/potassium/calcium exchanger 4 precursor
  316. Sodium-dependent phosphate transport protein 2C
  317. 4F2 cell-surface antigen heavy chain
  318. Dual oxidase 2 precursor
  319. Sodium/potassium/calcium exchanger 2 precursor
  320. Solute carrier family 12 member 3
  321. Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing alpha polypeptide
  322. Sodium/potassium/calcium exchanger 1
  323. Sodium/potassium/calcium exchanger 3 precursor
  324. Calcium-binding mitochondrial carrier protein Aralar1
  325. Large neutral amino acids transporter small subunit 1
  326. Sodium/calcium exchanger 3 precursor
  327. Sodium/calcium exchanger 2 precursor
  328. Inositol-trisphosphate 3-kinase C
  329. CDNA PSEC0079 fis, clone NT2RP2004049, highly similar to Group XII secretory phospholipase A2
  330. Sodium-dependent phosphate transport protein 2B
  331. Phosphatidylglycerophosphate synthase 1
  332. Hematopoietic cell signal transducer
  333. Testicular soluble adenylyl cyclase
  334. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4
  335. Phospholipase C eta 1
  336. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase epsilon-1
  337. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
  338. Polypeptide N-acetylgalactosaminyltransferase 9
  339. Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC
  340. Dual oxidase 1 precursor
  341. Transketolase-like protein 2
  342. Beta-1,4-galactosyltransferase 6
  343. Sn1-specific diacylglycerol lipase alpha
  344. Sn1-specific diacylglycerol lipase beta
  345. Serine/threonine-protein kinase D2
  346. Phospholipase A2, group IIC
  347. 1-acylglycerophosphocholine O-acyltransferase 1
  348. Phospholipid scramblase 2
  349. Phospholipid scramblase 3
  350. Phospholipid scramblase 4
  351. Phospholipase B1
  352. Serum deprivation-response protein
  353. Lysophosphatidic acid receptor 4
  354. Membrane-associated phosphatidylinositol transfer protein 1
  355. Membrane-associated phosphatidylinositol transfer protein 2
  356. Membrane-associated phosphatidylinositol transfer protein 3
  357. Phospholipase C zeta 1
  358. N-acylneuraminate-9-phosphatase
  359. UDP-glucose:glycoprotein glucosyltransferase 2 precursor
  360. Bestrophin-1
  361. Bestrophin-2
  362. Bestrophin-3
  363. Bestrophin-4
  364. Neuronal acetylcholine receptor subunit alpha-10 precursor
  365. Neuronal acetylcholine receptor subunit alpha-9 precursor
  366. Alpha-1A adrenergic receptor
  367. Alpha-1B adrenergic receptor
  368. Alpha-1D adrenergic receptor
  369. A-kinase anchor protein 7 isoforms alpha and beta
  370. A-kinase anchor protein 13
  371. Transmembrane protein 16K
  372. Transmembrane protein 16A
  373. Transmembrane protein 16B
  374. Transmembrane protein 16C
  375. Transmembrane protein 16D
  376. Transmembrane protein 16E
  377. Transmembrane protein 16F
  378. Transmembrane protein 16G
  379. Transmembrane protein 16H
  380. Transmembrane protein 16J
  381. Ankyrin repeat and sterile alpha motif domain-containing protein 1B
  382. Anthrax toxin receptor 2 precursor
  383. Annexin A11
  384. Annexin A13
  385. Annexin A1
  386. Annexin A4
  387. Annexin A6
  388. Annexin A7
  389. Annexin A8
  390. Arylsulfatase F precursor
  391. Arylsulfatase G precursor
  392. Arylsulfatase I precursor
  393. Arylsulfatase J precursor
  394. Arylsulfatase K precursor
  395. Asialoglycoprotein receptor 1
  396. Sodium/potassium-transporting ATPase gamma chain
  397. Transcriptional regulator ATRX
  398. ADAMTS-13 precursor
  399. Uncharacterized protein ENSP00000329640
  400. Annexin A8-like protein 1
  401. Annexin A8-like 2
  402. Transforming growth factor-beta-induced protein ig-h3 precursor
  403. Class B basic helix-loop-helix protein 8
  404. B2 bradykinin receptor
  405. Bone morphogenetic protein 8A precursor
  406. Bone morphogenetic protein 8B precursor
  407. Bombesin receptor subtype-3
  408. B box and SPRY domain-containing protein
  409. Scavenger receptor cysteine-rich type 1 protein M130 precursor
  410. Complement C1q subcomponent subunit A precursor
  411. Complement C1q subcomponent subunit B precursor
  412. Complement C1q subcomponent subunit C precursor
  413. Complement C1r subcomponent precursor
  414. Complement C1s subcomponent precursor
  415. Coiled-coil and C2 domain-containing protein 1A
  416. C5a anaphylatoxin chemotactic receptor
  417. Voltage-dependent calcium channel subunit alpha-2/delta-1 precursor
  418. Voltage-dependent calcium channel subunit alpha-2/delta-2 precursor
  419. Voltage-dependent calcium channel subunit alpha-2/delta-3 precursor
  420. Voltage-dependent calcium channel subunit alpha-2/delta-4 precursor
  421. 45 kDa calcium-binding protein precursor
  422. Calcineurin-binding protein Cabin 1
  423. Calcium-binding tyrosine phosphorylation-regulated protein
  424. Voltage-dependent P/Q-type calcium channel subunit alpha-1A
  425. Voltage-dependent N-type calcium channel subunit alpha-1B
  426. Voltage-dependent R-type calcium channel subunit alpha-1E
  427. Voltage-dependent L-type calcium channel subunit alpha-1F
  428. Voltage-dependent T-type calcium channel subunit alpha-1G
  429. Voltage-dependent T-type calcium channel subunit alpha-1H
  430. Voltage-dependent T-type calcium channel subunit alpha-1I
  431. Voltage-dependent L-type calcium channel subunit alpha-1S
  432. Voltage-dependent L-type calcium channel subunit beta-1
  433. Voltage-dependent L-type calcium channel subunit beta-2
  434. Voltage-dependent L-type calcium channel subunit beta-3
  435. Voltage-dependent L-type calcium channel subunit beta-4
  436. Calcium-binding and coiled-coil domain-containing protein 1
  437. Cadherin-10 precursor
  438. Cadherin-11 precursor
  439. Cadherin-12 precursor
  440. Cadherin-13 precursor
  441. Cadherin-16 precursor
  442. Cadherin-17 precursor
  443. Cadherin-18 precursor
  444. Cadherin-19 precursor
  445. Cadherin-20 precursor
  446. Cadherin-22 precursor
  447. Cadherin-23 precursor
  448. Cadherin-24 precursor
  449. Cadherin-like protein 26 precursor
  450. Cadherin-like protein 28 precursor
  451. Cadherin-2 precursor
  452. Cadherin-3 precursor
  453. Cadherin-4 precursor
  454. Cadherin-5 precursor
  455. Cadherin-6 precursor
  456. Cadherin-7 precursor
  457. Cadherin-8 precursor
  458. Cadherin-9 precursor
  459. LOC389118 protein
  460. Cell adhesion molecule 3 precursor
  461. Cell adhesion molecule 4 precursor
  462. VWFA and cache domain-containing protein 1 precursor
  463. Calcitonin precursor [Contains: Calcitonin; Katacalcin
  464. Calmodulin-like protein 5
  465. Calreticulin-3 precursor
  466. Calreticulin precursor
  467. Calumenin precursor
  468. Calnexin precursor
  469. D1 dopamine receptor-interacting protein calcyon
  470. CaM kinase-like vesicle-associated protein
  471. Calcium signal-modulating cyclophilin ligand
  472. Calpain-10
  473. Calpain-11
  474. Calpain-12
  475. Calpain-13
  476. Uncharacterized protein ENSP00000381805
  477. Calpain-1 catalytic subunit
  478. Calpain-2 catalytic subunit precursor
  479. Calpain-3
  480. Calpain-7
  481. Uncharacterized protein CAPN8
  482. Calpain-9
  483. Calcineurin subunit B isoform 1
  484. Calcineurin subunit B isoform 2
  485. Macrophage-capping protein
  486. Calcium-dependent secretion activator 1
  487. Calcium-dependent secretion activator 2
  488. Calsequestrin-1 precursor
  489. Calsequestrin-2 precursor
  490. Calcyphosin
  491. E3 ubiquitin-protein ligase CBL
  492. E3 ubiquitin-protein ligase CBL-B
  493. Signal transduction protein CBL-C
  494. Voltage-dependent calcium channel gamma-1 subunit
  495. Voltage-dependent calcium channel gamma-2 subunit
  496. Voltage-dependent calcium channel gamma-3 subunit
  497. Voltage-dependent calcium channel gamma-4 subunit
  498. Voltage-dependent calcium channel gamma-5 subunit
  499. Voltage-dependent calcium channel gamma-6 subunit
  500. Voltage-dependent calcium channel gamma-7 subunit
  501. Voltage-dependent calcium channel gamma-8 subunit
  502. Voltage-dependent calcium channel gamma-like subunit
  503. Cholecystokinin receptor type A
  504. C-C motif chemokine 16 precursor
  505. C-C motif chemokine 28 precursor
  506. C-C chemokine receptor type 10
  507. C-C chemokine receptor type 1
  508. C-C chemokine receptor type 2
  509. C-C chemokine receptor type 3
  510. C-C chemokine receptor type 4
  511. C-C chemokine receptor type 5
  512. C-C chemokine receptor type 6
  513. C-C chemokine receptor type 9
  514. Carcinoembryonic antigen-related cell adhesion molecule 3 precursor
  515. Centrin-1
  516. Centrin-2
  517. Calcium homeostasis endoplasmic reticulum protein
  518. Cartilage intermediate layer protein 1 precursor
  519. CDGSH iron sulfur domain 2
  520. C-type lectin domain family 10 member A
  521. C-type lectin domain family 4 member A
  522. C-type lectin domain family 4 member C
  523. C-type lectin domain family 4 member K
  524. C-type lectin domain family 5 member A
  525. cDNA FLJ78073, highly similar to Homo sapiens calcium-dependent chloride channel-1
  526. Calcium activated chloride channel family member 2
  527. Chloride channel, calcium activated, family member 4
  528. Claudin-10
  529. Claudin-11
  530. Claudin-12
  531. Claudin-14
  532. Claudin-15
  533. Claudin-16
  534. Claudin-17
  535. Claudin-18
  536. Claudin-19
  537. Claudin-1
  538. Claudin-20
  539. Claudin-22
  540. Claudin-23
  541. Uncharacterized protein ENSP00000333484
  542. Claudin-2
  543. Claudin-3
  544. Claudin-9
  545. Calmegin precursor
  546. Clathrin heavy chain 1
  547. Clathrin heavy chain 2
  548. CMRF35-like molecule 9 precursor
  549. Chromogranin-A precursor
  550. CNGA4 protein
  551. Uncharacterized protein C2orf32
  552. Collectin sub-family member 12
  553. Coactosin-like protein
  554. Copine-1
  555. Copine-3
  556. Copine-4
  557. Copine-5
  558. Copine-6
  559. Copine-7
  560. Copine-8
  561. Copine-9
  562. Calpain small subunit 1
  563. Calpain small subunit 2
  564. Cysteine-rich secretory protein 2 precursor
  565. Cornulin
  566. CREB-regulated transcription coactivator 1
  567. CREB-regulated transcription coactivator 2
  568. Calsyntenin-1 precursor
  569. Calsyntenin-2 precursor
  570. Calsyntenin-3 precursor
  571. Cation channel sperm-associated protein 1
  572. Cation channel sperm-associated protein 2
  573. Cation channel sperm-associated protein 3
  574. Cation channel sperm-associated protein 4
  575. High affinity interleukin-8 receptor A
  576. High affinity interleukin-8 receptor B
  577. C-X-C chemokine receptor type 4
  578. C-X-C motif chemokine 11 precursor
  579. C-X-C motif chemokine 13 precursor
  580. Calcyclin-binding protein
  581. Neuronal migration protein doublecortin
  582. Deleted in malignant brain tumors 1 protein precursor
  583. Dentin matrix acidic phosphoprotein 1 precursor
  584. Dentin matrix protein 4 precursor
  585. DnaJ homolog subfamily C member 5
  586. Deoxyribonuclease gamma precursor
  587. Double C2-like domain-containing protein alpha
  588. Double C2-like domain-containing protein beta
  589. Desmocollin-1 precursor
  590. Desmocollin-2 precursor
  591. Desmocollin-3 precursor
  592. Desmoglein-1 precursor
  593. Desmoglein-2 precursor
  594. Desmoglein-3 precursor
  595. Desmoglein-4 precursor
  596. Dentin sialophosphoprotein precursor [Contains: Dentin phosphoprotein
  597. Elongation factor 2 kinase
  598. EF-hand domain-containing family member A1
  599. EF-hand domain-containing family member A2
  600. EF-hand domain-containing protein 1
  601. Elastase-1 precursor
  602. Enkurin
  603. Ectonucleoside triphosphate diphosphohydrolase 7
  604. Ectonucleoside triphosphate diphosphohydrolase 8
  605. Protein FAM62A
  606. Protein FAM62B
  607. Extended-synaptotagmin 3
  608. RNA-binding protein EWS
  609. Fumarylacetoacetate hydrolase domain-containing protein 2A
  610. Fumarylacetoacetate hydrolase domain-containing protein 2B
  611. Fumarylacetoacetate hydrolase domain-containing protein 1
  612. Fibulin-2 precursor
  613. Fibrillin-1 precursor
  614. Fibrillin-2 precursor
  615. Fibrillin-3 precursor
  616. F-box only protein 43
  617. Ficolin-2 precursor
  618. Alpha-2-HS-glycoprotein precursor
  619. FK506-binding protein 1A
  620. FK506-binding protein 7 precursor
  621. FK506-binding protein 8
  622. Feline leukemia virus subgroup C receptor-related protein 2
  623. FMLP-related receptor II
  624. Extracellular matrix protein FRAS1 precursor
  625. FRAS1-related extracellular matrix protein 1 precursor
  626. FRAS1-related extracellular matrix protein 2 precursor
  627. FRAS1-related extracellular matrix protein 3 precursor
  628. Uncharacterized protein C14orf155
  629. Furin precursor
  630. Frizzled-10 precursor
  631. Frizzled-1 precursor
  632. Frizzled-2 precursor
  633. Frizzled-3 precursor
  634. Frizzled-4 precursor
  635. Frizzled-5 precursor
  636. Frizzled-6 precursor
  637. Frizzled-7 precursor
  638. Frizzled-8 precursor
  639. Frizzled-9 precursor
  640. Protein G6b precursor
  641. Gamma-aminobutyric acid type B receptor subunit 2 precursor
  642. GC-rich sequence DNA-binding factor
  643. Gelsolin precursor
  644. Glucagon receptor precursor
  645. Polypeptide N-acetylgalactosaminyltransferase 17
  646. Putative polypeptide N-acetylgalactosaminyltransferase-like protein 5
  647. Uncharacterized protein GNAT3
  648. Putative gonadotropin-releasing hormone II receptor
  649. G-protein coupled receptor family C group 6 member A precursor
  650. Sphingosine 1-phosphate receptor GPR6
  651. Grancalcin
  652. Glutamate receptor 2 precursor
  653. RAS guanyl-releasing protein 1
  654. Calcium and DAG-regulated guanine nucleotide exchange factor I
  655. Gastrin-releasing peptide receptor
  656. Guanylyl cyclase-activating protein 1
  657. Guanylyl cyclase-activating protein 2
  658. Guanylyl cyclase-activating protein 3
  659. Histone H2A type 1
  660. Histone H2A type 1-A
  661. Histone H2A type 1-B
  662. Histone H2A type 1-H
  663. Histone H2A type 2-A
  664. Histone H2A type 2-B
  665. Histone H2A type 3
  666. Homer protein homolog 1
  667. Homer protein homolog 3
  668. Neuron-specific calcium-binding protein hippocalcin
  669. Hippocalcin-like protein 1
  670. Hippocalcin-like protein 4
  671. Inhibitor of Bruton tyrosine kinase
  672. Calpastatin
  673. Immunoglobulin superfamily member 2 precursor
  674. IGSF5 protein
  675. Inversin
  676. Integrin beta-7 precursor
  677. Integrin beta-1-binding protein 2
  678. Intelectin-1 precursor
  679. Inositol 1,4,5-trisphosphate receptor type 2
  680. Inositol 1,4,5-trisphosphate receptor type 3
  681. C-jun-amino-terminal kinase-interacting protein 1
  682. Junctional sarcoplasmic reticulum protein 1
  683. Calcium/calmodulin-dependent protein kinase type 1B
  684. Kv channel-interacting protein 1
  685. Kv channel-interacting protein 2
  686. Kv channel-interacting protein 4
  687. Calcium-activated potassium channel subunit beta-1
  688. Calcium-activated potassium channel subunit beta-2
  689. Calcium-activated potassium channel subunit beta-3
  690. Calcium-activated potassium channel subunit beta-4
  691. Small conductance calcium-activated potassium channel protein 1
  692. Small conductance calcium-activated potassium channel protein 2
  693. Small conductance calcium-activated potassium channel protein 3
  694. Intermediate conductance calcium-activated potassium channel protein 4
  695. Potassium channel subfamily T member 1
  696. Potassium channel subfamily T member 2
  697. Uncharacterized protein ENSP00000382770
  698. KiSS-1 receptor
  699. Klotho precursor
  700. Phosphorylase b kinase regulatory subunit alpha, liver isoform
  701. Keratinocyte proline-rich protein
  702. Lethal(2) giant larvae protein homolog 2
  703. Leukocyte-associated immunoglobulin-like receptor 1 precursor
  704. Linker for activation of T-cells family member 1
  705. Late cornified envelope protein 2A
  706. Late cornified envelope protein 2B
  707. Late cornified envelope protein 2C
  708. Late cornified envelope protein 2D
  709. Lck-interacting transmembrane adapter 1
  710. Lin-7 homolog B
  711. Lin-7 homolog C
  712. Liprin-beta-1
  713. Leukocyte immunoglobulin-like receptor subfamily B member 1 precursor
  714. Leukocyte immunoglobulin-like receptor subfamily B member 2 precursor
  715. Leukocyte immunoglobulin-like receptor subfamily B member 4 precursor
  716. Vesicular integral-membrane protein VIP36 precursor
  717. Latrophilin-1 precursor
  718. Latrophilin-2 precursor
  719. Prolow-density lipoprotein receptor-related protein 1 precursor
  720. Low-density lipoprotein receptor-related protein 5 precursor
  721. Leukotriene B4 receptor 2
  722. Mannan-binding lectin serine protease 2 precursor
  723. Multiple coagulation factor deficiency protein 2 precursor
  724. Multiple C2 and transmembrane domain-containing protein 1
  725. Multiple C2 and transmembrane domain-containing protein 2
  726. Microfibril-associated glycoprotein 4 precursor
  727. Magnesium-dependent phosphatase 1
  728. Mitochondrial intermediate peptidase, mitochondrial precursor
  729. MIST
  730. Myosin light chain 1, skeletal muscle isoform
  731. Myosin light chain 3, skeletal muscle isoform
  732. Myosin regulatory light chain 2, atrial isoform
  733. Myosin regulatory light chain 2, skeletal muscle isoform
  734. Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
  735. Stromelysin-2 precursor
  736. Stromelysin-3 precursor
  737. Macrophage metalloelastase precursor
  738. Matrix metalloproteinase-15 precursor
  739. Matrix metalloproteinase-16 precursor
  740. Matrix metalloproteinase-17 precursor
  741. Matrix metalloproteinase-19 precursor
  742. Matrix metalloproteinase-21 precursor
  743. Matrix metalloproteinase-24 precursor
  744. Matrix metalloproteinase-25 precursor
  745. Matrix metalloproteinase-26 precursor
  746. Matrix metalloproteinase-27 precursor
  747. Matrix metalloproteinase-28 precursor
  748. Neutrophil collagenase precursor
  749. Macrophage mannose receptor 2 precursor
  750. Mas-related G-protein coupled receptor member X1
  751. Myosin regulatory light chain
  752. Protein MRVI1
  753. Cell surface glycoprotein MUC18 precursor
  754. Mucin and cadherin-like protein precursor
  755. Myosin light polypeptide 3
  756. Myosin light polypeptide 4
  757. Superfast myosin regulatory light chain 2
  758. Myosin light polypeptide 6
  759. Myosin light polypeptide 6B
  760. Myosin regulatory light chain 2, smooth muscle isoform
  761. Myosin light chain 2, lymphocyte-specific
  762. Myosin-VI
  763. Myosin-IXb
  764. NKG2D ligand 1 precursor
  765. NKG2D ligand 2 precursor
  766. NKG2D ligand 3 precursor
  767. Voltage gated channel-like protein 1
  768. Neurocalcin-delta
  769. Sodium/potassium/calcium exchanger 5 precursor
  770. Sodium/potassium/calcium exchanger 6 precursor
  771. Neuronal calcium sensor 1
  772. Neuroendocrine convertase 1 precursor
  773. Neurogranin
  774. Nuclear factor of activated T-cells, cytoplasmic 3
  775. Nuclear factor of activated T-cells, cytoplasmic 4
  776. Substance-P receptor
  777. Substance-K receptor
  778. Neuromedin-K receptor
  779. Glutamate [NMDA] receptor subunit 3A precursor
  780. NADPH oxidase 5
  781. Neuropeptide FF receptor 1
  782. Neuropeptide FF receptor 2
  783. Neuronal pentraxin-1 precursor
  784. Neuronal pentraxin-2 precursor
  785. Similar to portion of neuronal pentraxin i NPX1 or NP1
  786. Neuronal pentraxin receptor
  787. Neurotensin receptor type 1
  788. Neurotensin receptor type 2
  789. Nucleobindin-1 precursor
  790. Oncomodulin
  791. Kappa-type opioid receptor
  792. Sigma 1-type opioid receptor
  793. Otopetrin-1
  794. P2X purinoceptor 1
  795. P2Y purinoceptor 4
  796. P2Y purinoceptor 6
  797. P2Y purinoceptor 11
  798. Cytosolic phospholipase A2 delta
  799. Cytosolic phospholipase A2 epsilon
  800. Cytosolic phospholipase A2 zeta
  801. Protocadherin-11 X-linked precursor
  802. Protocadherin-11 Y-linked precursor
  803. Protocadherin-10 precursor
  804. Protocadherin-12 precursor
  805. Protocadherin-15 precursor
  806. Protocadherin-16 precursor
  807. Protocadherin-17 precursor
  808. Protocadherin-18 precursor
  809. Protocadherin-19 precursor
  810. Protocadherin-20 precursor
  811. Protocadherin-21
  812. Dachsous-2
  813. Protocadherin alpha 1 precursor
  814. Protocadherin alpha 2 precursor
  815. Protocadherin alpha 3 precursor
  816. Protocadherin alpha 4 precursor
  817. Protocadherin alpha 5 precursor
  818. Protocadherin alpha 6 precursor
  819. Protocadherin alpha 7 precursor
  820. Protocadherin alpha 8 precursor
  821. Protocadherin alpha 9 precursor
  822. Protocadherin alpha 10 precursor
  823. Protocadherin alpha 11 precursor
  824. Protocadherin alpha 12 precursor
  825. Protocadherin alpha 13 precursor
  826. Protocadherin beta 1 precursor
  827. Protocadherin beta 2 precursor
  828. Protocadherin beta 3 precursor
  829. Protocadherin beta 4 precursor
  830. Protocadherin beta 5 precursor
  831. Protocadherin beta 6 precursor
  832. Protocadherin beta 7 precursor
  833. Protocadherin beta 8 precursor
  834. Protocadherin beta 9 precursor
  835. Protocadherin beta 10 precursor
  836. Protocadherin beta 11 precursor
  837. Protocadherin beta 12 precursor
  838. Protocadherin beta 13 precursor
  839. Protocadherin beta 14 precursor
  840. Protocadherin beta 15 precursor
  841. Protocadherin beta 16 precursor
  842. Protocadherin-psi2
  843. Protocadherin alpha C1 precursor
  844. Protocadherin alpha C2 precursor
  845. Protocadherin gamma A1 precursor
  846. Protocadherin gamma A2 precursor
  847. Protocadherin gamma A3 precursor
  848. Protocadherin gamma A4 precursor
  849. Protocadherin gamma A5 precursor
  850. Protocadherin gamma A6 precursor
  851. Protocadherin gamma A7 precursor
  852. Protocadherin gamma A8 precursor
  853. Protocadherin gamma A9 precursor
  854. Protocadherin gamma A10 precursor
  855. Protocadherin gamma A11 precursor
  856. Protocadherin gamma A12 precursor
  857. Protocadherin gamma B1 precursor
  858. Protocadherin gamma B2 precursor
  859. Protocadherin gamma B3 precursor
  860. Protocadherin gamma B4 precursor
  861. Protocadherin gamma B5 precursor
  862. Protocadherin gamma B6 precursor
  863. Protocadherin gamma B7 precursor
  864. Protocadherin gamma C3 precursor
  865. Protocadherin gamma C4 precursor
  866. Protocadherin gamma C5 precursor
  867. Protocadherin-9 precursor
  868. Protein piccolo
  869. Proprotein convertase subtilisin/kexin type 7 precursor
  870. Proprotein convertase subtilisin/kexin type 9 precursor
  871. Programmed cell death 6-interacting protein
  872. Programmed cell death protein 6
  873. Prostaglandin E2 receptor EP3 subtype
  874. Astrocytic phosphoprotein PEA-15
  875. Polycystic kidney disease 2-like 1 protein
  876. Polycystin-1 precursor
  877. Polycystin-2
  878. Prokineticin receptor 1
  879. Prokineticin receptor 2
  880. Calcium-independent phospholipase A2-gamma
  881. Plastin-1
  882. Periostin precursor
  883. Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
  884. Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
  885. Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform
  886. Serine/threonine-protein phosphatase with EF-hands 1
  887. Serine/threonine-protein phosphatase with EF-hands 2
  888. Protein phosphatase 1 regulatory subunit 1A
  889. Bone marrow proteoglycan precursor
  890. E3 ubiquitin-protein ligase parkin
  891. Salivary acidic proline-rich phosphoprotein 1/2 precursor
  892. Presenilin-1
  893. Parathyroid hormone/parathyroid hormone-related peptide receptor precursor
  894. Peroxidasin homolog
  895. Cardiac peroxidase
  896. Orexigenic neuropeptide QRFP receptor
  897. Ras GTPase-activating protein 4
  898. Calcipressin-1
  899. Reticulocalbin-1 precursor
  900. Reticulocalbin-2 precursor
  901. Lithostathine 1 alpha precursor
  902. Lithostathine 1 beta precursor
  903. GTP-binding protein REM 1
  904. Regucalcin
  905. Ras-specific guanine nucleotide-releasing factor 2
  906. Rho GTPase-activating protein
  907. Regulating synaptic membrane exocytosis protein 1
  908. Repetin
  909. Ryanodine receptor 1
  910. Ryanodine receptor 2
  911. Ryanodine receptor 3
  912. Protein S100-B
  913. Protein S100-P
  914. Protein S100-Z
  915. Protein S100-A1
  916. Protein S100-A2
  917. Protein S100-A3
  918. Protein S100-A4
  919. Protein S100-A10
  920. Protein S100-A11
  921. Solute carrier family 22 member 6
  922. Sodium- and chloride-dependent transporter XTRP3
  923. Serum amyloid P-component precursor
  924. Sarcolipin
  925. Protein transport protein Sec31A
  926. Secretogranin-2 precursor
  927. Solute carrier family 25 member 24
  928. Small calcium-binding mitochondrial carrier 2
  929. Solute carrier family 25 member 23
  930. Secernin-1
  931. Protein SET
  932. Pulmonary surfactant-associated protein A1 precursor
  933. Sodium/hydrogen exchanger 6
  934. SNARE-associated protein Snapin
  935. p130Cas-associated protein
  936. Alpha-1-syntrophin
  937. Beta-2-syntrophin
  938. Sorcin
  939. Spectrin alpha chain, brain
  940. Spectrin beta chain, brain 1
  941. Sarcalumenin precursor
  942. Sarcoplasmic reticulum histidine-rich calcium-binding protein precursor
  943. Somatostatin receptor type 2
  944. Translocon-associated protein subunit alpha precursor
  945. Translocon-associated protein subunit beta precursor
  946. Translocon-associated protein subunit delta precursor
  947. Translocon-associated protein subunit gamma
  948. Statherin precursor
  949. Stanniocalcin-2 precursor
  950. Stromal interaction molecule 1 precursor
  951. Striatin-3
  952. Striatin-4
  953. Syntaxin-binding protein 5
  954. Extracellular sulfatase Sulf-2 precursor
  955. Synaptic vesicle glycoprotein 2A
  956. Synaptic vesicle glycoprotein 2B
  957. Synaptic vesicle glycoprotein 2C
  958. Synapsin-3
  959. Synaptophysin
  960. Synaptotagmin-10
  961. Synaptotagmin-11
  962. Synaptotagmin-13
  963. Synaptotagmin-1
  964. Synaptotagmin-2
  965. Synaptotagmin-3
  966. Synaptotagmin-4
  967. Synaptotagmin-5
  968. Synaptotagmin-6
  969. Synaptotagmin-7
  970. Synaptotagmin-9
  971. Synaptotagmin-like protein 3
  972. Gamma-synuclein
  973. Taste receptor type 2 member 10
  974. Taste receptor type 2 member 16
  975. Taste receptor type 2 member 40
  976. Taste receptor type 2 member 3
  977. Taste receptor type 2 member 4
  978. Taste receptor type 2 member 7
  979. Taste receptor type 2 member 9
  980. Transgelin
  981. Tubulin beta-2C chain
  982. Tubulin beta-4 chain
  983. Tubulin beta chain
  984. Tubulin beta-6 chain
  985. Translationally-controlled tumor protein
  986. Tescalcin
  987. Trefoil factor 1 precursor
  988. Testican-2 precursor
  989. Tuberoinfundibular peptide of 39 residues precursor
  990. Trimeric intracellular cation channel type A
  991. Trimeric intracellular cation channel type B
  992. Troponin C, slow skeletal and cardiac muscles
  993. Troponin C, skeletal muscle
  994. Troponin I, slow skeletal muscle
  995. Troponin I, fast skeletal muscle
  996. Troponin I, cardiac muscle
  997. Troponin T, slow skeletal muscle
  998. Troponin T, cardiac muscle
  999. Troponin T, fast skeletal muscle
  1000. DNA topoisomerase I, mitochondrial precursor
  1001. Prosalusin precursor
  1002. Protein tyrosine phosphatase type IVA protein 3
  1003. Two pore calcium channel protein 1
  1004. Two pore calcium channel protein 2
  1005. Tropomyosin alpha-1 chain
  1006. Tropomyosin beta chain
  1007. Tropomyosin alpha-3 chain
  1008. Thyrotropin-releasing hormone receptor
  1009. Trichohyalin
  1010. Short transient receptor potential channel 1
  1011. Short transient receptor potential channel 4
  1012. Short transient receptor potential channel 5
  1013. Short transient receptor potential channel 6
  1014. Short transient receptor potential channel 7
  1015. Melastatin 1
  1016. Transient receptor potential cation channel subfamily M member 3
  1017. Transient receptor potential cation channel subfamily M member 4
  1018. Transient receptor potential cation channel subfamily V member 2
  1019. Transient receptor potential cation channel subfamily V member 3
  1020. Transient receptor potential cation channel subfamily V member 5
  1021. Trypsin-1 precursor
  1022. Trypsin-2 precursor
  1023. Trypsin-3 precursor
  1024. Tau-tubulin kinase 1
  1025. Alpha-taxilin
  1026. Thioredoxin domain-containing protein 4 precursor
  1027. UBX domain-containing protein 2
  1028. UDP-glucose:glycoprotein glucosyltransferase 1 precursor
  1029. Protein unc-13 homolog A
  1030. Protein unc-13 homolog B
  1031. Protein unc-13 homolog C
  1032. Urotensin II receptor
  1033. Vesicle-associated membrane protein 4
  1034. Synaptobrevin-like protein 1
  1035. Villin-1
  1036. Visinin-like protein 1
  1037. Chemokine XC receptor 1
  1038. Protein Z-dependent protease inhibitor precursor
  1039. Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
  1040. Serine/threonine-protein phosphatase 4 catalytic subunit
  1041. Serine/threonine-protein phosphatase 5
  1042. Serine/threonine-protein phosphatase 6
  1043. Putative myosin light chain kinase 3
  1044. Protein phosphatase 1D
  1045. Protein phosphatase 1E
  1046. Protein phosphatase 1F
  1047. Protein phosphatase 1G
  1048. Protein phosphatase 1M
  1049. Ubiquitin-like domain-containing CTD phosphatase 1
  1050. PH domain leucine-rich repeat protein phosphatase-like
  1051. PH domain leucine-rich repeat-containing protein phosphatase
  1052. RNA polymerase II subunit A C-terminal domain phosphatase
  1053. Dual specificity protein phosphatase 10
  1054. Dual specificity protein phosphatase 12
  1055. Dual specificity protein phosphatase 16
  1056. Dual specificity protein phosphatase 19
  1057. Dual specificity protein phosphatase 1
  1058. Dual specificity protein phosphatase 3
  1059. Dual specificity protein phosphatase 5
  1060. Dual specificity protein phosphatase 6
  1061. Dual specificity protein phosphatase 7
  1062. Dual specificity protein phosphatase 8
  1063. Cytosolic phospholipase A2 beta
  1064. Nitric oxide synthase 2A (Inducible, hepatocytes)
  1065. UDP-N-acetyl-alpha-D-galactosamine:polypeptide N- acetylgalactosaminyltransferase 5 (GalNAc-T5) (cDNA FLJ75131, highly similar to Homo sapiens UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 5 (GalNAc-T5) (GALNT5), mRNA)
  1066. 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)
  1067. Pp-GalNAc-transferase 20 (Williams-Beuren syndrome chromosome region 17, isoform CRA_d) (Williams-Beuren syndrome chromosome region 17) (cDNA FLJ76765, highly similar to Homo sapiens Williams-Beuren syndrome chromosome region 17 (WBSCR17), mRNA)
  1068. Calcium/calmodulin-dependent protein kinase ID (Calcium/calmodulin- dependent protein kinase ID, isoform CRA_b) (cDNA FLJ76987, highly similar to Homo sapiens calcium/calmodulin-dependent protein kinase ID (CAMK1D), transcript variant 1, mRNA)
  1069. cDNA FLJ75193, highly similar to Homo sapiens calcium/calmodulin- dependent protein kinase II alpha-B subunit mRNA (Calcium/calmodulin- dependent protein kinase (CaM kinase) II alpha, isoform CRA_b)
  1070. Calcium/calmodulin-dependent protein kinase (CaM kinase) II beta
  1071. Calcium/calmodulin-dependent protein kinase isoform A (Fragment)
  1072. 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)
  1073. CDKN3 protein (Cyclin-dependent kinase inhibitor 3 (CDK2-associated dual specificity phosphatase), isoform CRA_c)
  1074. Dual specificity protein phosphatase 14
  1075. Uncharacterized protein DUSP15
  1076. Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta
  1077. PPM1B beta isoform variant 4
  1078. Serine/threonine protein phosphatase (EC 3.1.3.16)
  1079. 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)
  1080. Serine/threonine protein phosphatase (EC 3.1.3.16)
  1081. Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1
  1082. Dual specificity protein phosphatase 21
  1083. Uncharacterized protein CDC14C
  1084. Glutamyl aminopeptidase
  1085. Bone morphogenetic protein 1
  1086. cDNA FLJ75328, highly similar to Homo sapiens ATPase, Ca++ transporting, cardiac muscle, fast twitch1 (ATP2A1), transcript variant b, mRNA
  1087. Putative uncharacterized protein DKFZp686I0955
  1088. cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
  1089. NOS1 mutant (Nitric oxide synthase 1 (Neuronal), isoform CRA_c)
  1090. UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 8 (GalNAc-T8)
  1091. cDNA PSEC0182 fis, clone OVARC1001636, highly similar to N-acetylgalactosaminyltransferase 7 (EC 2.4.1.-)
  1092. cDNA FLJ42944 fis, clone BRSTN2004863, highly similar to PolypeptideN-acetylgalactosaminyltransferase 11 (EC 2.4.1.41)
  1093. Calcium/calmodulin-dependent protein kinase type 1 (Calcium/calmodulin-dependent protein kinase I, isoform CRA_a) (cDNA, FLJ95825, Homo sapiens calcium/calmodulin-dependent protein kinase I (CAMK1),mRNA)
  1094. Phospholipase A2, group VI (Cytosolic, calcium-independent) (Phospholipase A2, group VI (Cytosolic, calcium-independent), isoform CRA_a)
  1095. cDNA FLJ31512 fis, clone NT2RI1000048, highly similar to Dual specificity protein phosphatase 18 (EC 3.1.3.48)
  1096. cDNA, FLJ95698, Homo sapiens dual specificity phosphatase 4 (DUSP4), transcript variant 1, mRNA (Dual specificity phosphatase 4, isoform CRA_a)
  1097. cDNA, FLJ94996, highly similar to Homo sapiens dual specificity phosphatase 9 (DUSP9), mRNA
  1098. cDNA FLJ45992 fis, clone SKMUS2008585, highly similar to Homo sapiens dual specificity phosphatase 13 (DUSP13), transcript variant 3, mRNA
  1099. Protein phosphatase 1A isoform 1 (Protein phosphatase 1A (Formerly 2C), magnesium-dependent, alpha isoform, isoform CRA_a)
  1100. cDNA, FLJ92643, Homo sapiens protein phosphatase 1, catalytic subunit, beta isoform(PPP1CB), mRNA (Protein phosphatase 1, catalytic subunit, beta isoform, isoform CRA_a)
  1101. Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
  1102. Serine/threonine protein phosphatase
  1103. cDNA FLJ41117 fis, clone BRACE2006821, highly similar to Dopamine- and cAMP-regulated neuronalphospho protein
  1104. CDC14 cell division cycle 14 homolog A (S. cerevisiae)
  1105. ATPase, Ca++ transporting, plasma membrane 4 (ATPase, Ca++ transporting, plasma membrane 4, isoform CRA_a)
Enzyme 1 [top]
Enzyme 1 ID 5286
Enzyme 1 Name 1-O-acylceramide synthase precursor
Enzyme 1 Synonyms
  1. ACS
  2. Lysosomal phospholipase A2
  3. Lysophospholipase 3
  4. LPLA2
  5. LCAT-like lysophospholipase
  6. LLPL
Enzyme 1 Gene Name LYPLA3
Enzyme 1 Protein Sequence >1-O-acylceramide synthase precursor 
MGLHLRPYRVGLLPDGLLFLLLLLMLLADPALPAGRHPPVVLVPGDLGNQLEAKLDKPTV
VHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNIRLVYNKTSRATQFPDGVDVRVPGFGK
TFSLEFLDPSKSSVGSYFHTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREM
IEEMYQLYGGPVVLVAHSMGNMYTLYFLQRQPQAWKDKYIRAFVSLGAPWGGVAKTLRVL
ASGDNNRIPVIGPLKIREQQRSAVSTSWLLPYNYTWSPEKVFVQTPTINYTLRDYRKFFQ
DIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDPKICFGDGD
GTVNLKSALQCQAWQSRQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP
Enzyme 1 Number of Residues 412
Enzyme 1 Molecular Weight 46658
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 groups other than amino-acyl groups
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 1 General Function Not Available
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 Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 4589720 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q8NCC3 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name LYPA3_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 LYPLA3 Link Image
Enzyme 1 GenAtlas ID LYPLA3 Link Image
Enzyme 1 HGNC ID HGNC:17163 Link Image
Enzyme 1 Chromosome Location 16
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. 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 precursor
Enzyme 2 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase
  2. PLA2-10
  3. Group V phospholipase A2
Enzyme 2 Gene Name PLA2G5
Enzyme 2 Protein Sequence >Calcium-dependent phospholipase A2 precursor 
MKGLLPLAWFLACSVPAVQGGLLDLKSMIEKVTGKNALTNYGFYGCYCGWGGRGTPKDGT
DWCCWAHDHCYGRLEEKGCNIRTQSYKYRFAWGVVTCEPGPFCHVNLCACDRKLVYCLKR
NLRSYNPQYQYFPNILCS
Enzyme 2 Number of Residues 138
Enzyme 2 Molecular Weight 15674
Enzyme 2 Theoretical pI 8.48
Enzyme 2 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 2 General Function Not Available
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
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-20
Enzyme 2 Transmembrane Regions Not Available
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 460915 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 U03090 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]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5288
Enzyme 3 Name Group IIF secretory phospholipase A2 precursor
Enzyme 3 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase GIIF
  2. GIIF sPLA2
  3. sPLA(2-IIF
Enzyme 3 Gene Name PLA2G2F
Enzyme 3 Protein Sequence >Group IIF secretory phospholipase A2 precursor 
MKKFFTVAILAGSVLSTAHGSLLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEV
DWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTEIVCSDLNKTECDKQTCMCDKNMVLC
LMNQTYREEYRGFLNVYCQGPTPNCSIYEPPPEEVTCSHQSPAPPAPP
Enzyme 3 Number of Residues 168
Enzyme 3 Molecular Weight 18658
Enzyme 3 Theoretical pI 4.94
Enzyme 3 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 3 General Function Not Available
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
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-20
Enzyme 3 Transmembrane Regions Not Available
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]
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[Includes: Phospholipase A2
  3. Phosphatidylcholine 2- acylhydrolase
  4. 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 85212
Enzyme 4 Theoretical pI 5.03
Enzyme 4 GO Classification
Function
  • carboxylic ester hydrolase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • lipase activity
  • phospholipase activity
Process
  • cellular lipid metabolism
  • lipid metabolism
  • membrane lipid metabolism
  • metabolism
  • phospholipid catabolism
  • phospholipid metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 4 General Function Not Available
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
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 190007 Link Image
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. 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]
  4. 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]
  5. 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]
  6. 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]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5290
Enzyme 5 Name Phospholipase A2 precursor
Enzyme 5 Synonyms
  1. Phosphatidylcholine 2- acylhydrolase
  2. Group IB phospholipase A2
Enzyme 5 Gene Name PLA2G1B
Enzyme 5 Protein Sequence >Phospholipase A2 precursor 
MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPV
DELDKCCQTHDNCYDQAKKLDSCKFLLDNPYTHTYSYSCSGSAITCSSKNKECEAFICNC
DRNAAICFSKAPYNKAHKNLDTKKYCQS
Enzyme 5 Number of Residues 148
Enzyme 5 Molecular Weight 16360
Enzyme 5 Theoretical pI 7.91
Enzyme 5 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 5 General Function Not Available
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
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-15
Enzyme 5 Transmembrane Regions Not Available
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 387025 Link Image
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
GATGAACTGGACAAGTGCTGCCAGACACATGACAACTGCTACGACCAGGCCAAGAAGCTG
GACAGCTGTAAATTTCTGCTGGACAACCCGTACACCCACACCTATTCATACTCGTGCTCT
GGCTCGGCAATCACCTGTAGCAGCAAAAACAAAGAGTGTGAGGCCTTCATTTGCAACTGC
GACCGCAACGCTGCCATCTGCTTTTCAAAAGCTCCATATAACAAGGCACACAAGAACCTG
GACACCAAGAAGTATTGTCAGAGTTGA
Enzyme 5 GenBank Gene ID M21056 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 12
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. 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]
  3. 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 precursor
Enzyme 6 Synonyms
  1. Group XIII secretory phospholipase A2-like protein
  2. GXIII sPLA2-like
  3. GXIIB
Enzyme 6 Gene Name PLA2G12B
Enzyme 6 Protein Sequence >Group XIIB secretory phospholipase A2-like protein precursor 
MKLASGFLVLWLSLGGGLAQSDTSPDTEESYSDWGLRHLRGSFESVNSYFDSFLELLGGK
NGVCQYRCRYGKAPMPRPGYKPQEPNGCGSYFLGLKVPESMDLGIPAMTKCCNQLDVCYD
TCGANKYRCDAKFRWCLHSICSDLKRSLGFVSKVEAACDSLVDTVFNTVWTLGCRPFMNS
QRAACICAEEEKEEL
Enzyme 6 Number of Residues 195
Enzyme 6 Molecular Weight 21659
Enzyme 6 Theoretical pI 5.81
Enzyme 6 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
  • extracellular region
Enzyme 6 General Function Not Available
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 Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 13560707 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 >585 bp 
ATGAAGCTGGCCAGTGGCTTCTTGGTTTTGTGGCTCAGCCTTGGGGGTGGCCTGGCTCAG
AGCGACACGAGCCCTGACACGGAGGAGTCCTATTCAGACTGGGGCCTTCGGCACCTCCGG
GGAAGCTTTGAATCCGTCAATAGCTACTTCGATTCTTTTCTGGAGCTGCTGGGAGGGAAG
AATGGAGTCTGTCAGTACAGGTGCCGATATGGAAAGGCACCAATGCCCAGACCTGGCTAC
AAGCCCCAAGAGCCCAATGGCTGCGGCTCCTATTTCCTGGGTCTCAAGGTACCAGAAAGT
ATGGACTTGGGCATTCCAGCAATGACAAAGTGCTGCAACCAGCTGGATGTCTGTTATGAC
ACTTGCGGTGCCAACAAATATCGCTGTGATGCAAAATTCCGATGGTGTCTCCACTCGATC
TGCTCTGACCTTAAGCGGAGTCTGGGCTTTGTCTCCAAAGTGGAAGCCTGTGATTCCCTG
GTTGACACTGTGTTCAACACCGTGTGGACCTTGGGCTGCCGCCCCTTTATGAATAGTCAG
CGGGCAGCTTGCATCTGTGCAGAGGAGGAGAAGGAAGAGTTATGA
Enzyme 6 GenBank Gene ID AF349540 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 10
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]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5292
Enzyme 7 Name Group 10 secretory phospholipase A2 precursor
Enzyme 7 Synonyms
  1. Group X secretory phospholipase A2
  2. Phosphatidylcholine 2-acylhydrolase GX
  3. GX sPLA2
  4. sPLA2-X
Enzyme 7 Gene Name PLA2G10
Enzyme 7 Protein Sequence >Group 10 secretory phospholipase A2 precursor 
MLLLLLPSLLLLLLLPGPGSGEASRILRVHRRGILELAGTVGCVGPRTPIAYMKYGCFCG
LGGHGQPRDAIDWCCHGHDCCYTRAEEAGCSPKTERYSWQCVNQSVLCGPAENKCQELLC
KCDQEIANCLAQTEYNLKYLFYPQFLCEPDSPKCD
Enzyme 7 Number of Residues 155
Enzyme 7 Molecular Weight 17132
Enzyme 7 Theoretical pI 6.46
Enzyme 7 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 7 General Function Not Available
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
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-21
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 2289237 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID O15496 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name PA2GX_HUMAN Link Image
Enzyme 7 PDB ID Not Available
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 16
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]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5294
Enzyme 8 Name Group IIE secretory phospholipase A2 precursor
Enzyme 8 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase GIIE
  2. GIIE sPLA2
  3. sPLA(2-IIE
Enzyme 8 Gene Name PLA2G2E
Enzyme 8 Protein Sequence >Group IIE secretory phospholipase A2 precursor 
MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDW
CCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNL
GTYNRKYAHYPNKLCTGPTPPC
Enzyme 8 Number of Residues 142
Enzyme 8 Molecular Weight 15989
Enzyme 8 Theoretical pI 8.28
Enzyme 8 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 8 General Function Not Available
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
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-19
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 7108923 Link Image
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]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5296
Enzyme 9 Name Group XIIA secretory phospholipase A2 precursor
Enzyme 9 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase GXII
  2. GXII sPLA2
Enzyme 9 Gene Name PLA2G12A
Enzyme 9 Protein Sequence >Group XIIA secretory phospholipase A2 precursor 
MALLSRPALTLLLLLMAAVVRCQEQAQTTDWRATLKTIRNGVHKIDTYLNAALDLLGGED
GLCQYKCSDGSKPFPRYGYKPSPPNGCGSPLFGVHLNIGIPSLTKCCNQHDRCYETCGKS
KNDCDEEFQYCLSKICRDVQKTLGLTQHVQACETTVELLFDSVIHLGCKPYLDSQRAACR
CHYEEKTDL
Enzyme 9 Number of Residues 189
Enzyme 9 Molecular Weight 21067
Enzyme 9 Theoretical pI 7.27
Enzyme 9 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
  • extracellular region
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides
Enzyme 9 Pathways
Enzyme 9 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-22
Enzyme 9 Transmembrane Regions Not Available
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]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5301
Enzyme 10 Name Phospholipase A2, membrane associated precursor
Enzyme 10 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase
  2. Group IIA phospholipase A2
  3. GIIC sPLA2
  4. Non-pancreatic secretory phospholipase A2
  5. NPS-PLA2
Enzyme 10 Gene Name PLA2G2A
Enzyme 10 Protein Sequence >Phospholipase A2, membrane associated precursor 
MKTLLLLAVIMIFGLLQAHGNLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDAT
DRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFAR
NKTTYNKKYQYYSNKHCRGSTPRC
Enzyme 10 Number of Residues 144
Enzyme 10 Molecular Weight 16083
Enzyme 10 Theoretical pI 9.51
Enzyme 10 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 10 General Function Not Available
Enzyme 10 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 10 Pathways
Enzyme 10 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-20
Enzyme 10 Transmembrane Regions Not Available
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 190889 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P14555 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PA2GA_HUMAN Link Image
Enzyme 10 PDB ID 1DB4 Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >435 bp 
ATGAAGACCCTCCTACTGTTGGCAGTGATCATGATCTTTGGCCTACTGCAGGCCCATGGG
AATTTGGTGAATTTCCACAGAATGATCAAGTTGACGACAGGAAAGGAAGCCGCACTCAGT
TATGGCTTCTACGGCTGCCACTGTGGCGTGGGTGGCAGAGGATCCCCCAAGGATGCAACG
GATCGCTGCTGTGTCACTCATGACTGTTGCTACAAACGTCTGGAGAAACGTGGATGTGGC
ACCAAATTTCTGAGCTACAAGTTTAGCAACTCGGGGAGCAGAATCACCTGTGCAAAACAG
GACTCCTGCAGAAGTCAACTGTGTGAGTGTGATAAGGCTGCTGCCACCTGTTTTGCTAGA
AACAAGACGACCTACAATAAAAAGTACCAGTACTATTCCAATAAACACTGCAGAGGGAGC
ACCCCTCGTTGCTGA
Enzyme 10 GenBank Gene ID M22430 Link Image
Enzyme 10 GeneCard ID PLA2G2A Link Image
Enzyme 10 GenAtlas ID PLA2G2A Link Image
Enzyme 10 HGNC ID HGNC:9031 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 1p35
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 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. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5302
Enzyme 11 Name Group IID secretory phospholipase A2 precursor
Enzyme 11 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase GIID
  2. GIID sPLA2
  3. PLA2IID
  4. sPLA(2-IID
  5. Secretory-type PLA, stroma-associated homolog
Enzyme 11 Gene Name PLA2G2D
Enzyme 11 Protein Sequence >Group IID secretory phospholipase A2 precursor 
MELALLCGLVVMAGVIPIQGGILNLNKMVKQVTGKMPILSYWPYGCHCGLGGRGQPKDAT
DWCCQTHDCCYDHLKTQGCSIYKDYYRYNFSQGNIHCSDKGSWCEQQLCACDKEVAFCLK
RNLDTYQKRLRFYWRPHCRGQTPGC
Enzyme 11 Number of Residues 145
Enzyme 11 Molecular Weight 16546
Enzyme 11 Theoretical pI 8.28
Enzyme 11 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 11 General Function Not Available
Enzyme 11 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 11 Pathways
Enzyme 11 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-20
Enzyme 11 Transmembrane Regions Not Available
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 5771420 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID Q9UNK4 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name PA2GD_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >438 bp 
ATGGAACTTGCACTGCTGTGTGGGCTGGTGGTGATGGCTGGTGTGATTCCAATCCAGGGC
GGGATCCTGAACCTGAACAAGATGGTCAAGCAAGTGACTGGGAAAATGCCCATCCTCTCC
TACTGGCCCTACGGCTGTCACTGCGGACTAGGTGGCAGAGGCCAACCCAAAGATGCCACG
GACTGGTGCTGCCAGACCCATGACTGCTGCTATGACCACCTGAAGACCCAGGGGTGCGGC
ATCTACAAGGACTATTACAGATACAACTTTTCCCAGGGGAACATCCACTGCTCTGACAAG
GGAAGCTGGTGTGAGCAGCAGCTGTGTGCCTGTGACAAGGAGGTGGCCTTCTGCCTGAAG
CGCAACCTGGACACCTACCAGAAGCGACTGCGTTTCTACTGGCGGCCCCACTGCCGGGGG
CAGACCCCTGGGTGCTAG
Enzyme 11 GenBank Gene ID AF112982 Link Image
Enzyme 11 GeneCard ID PLA2G2D Link Image
Enzyme 11 GenAtlas ID PLA2G2D Link Image
Enzyme 11 HGNC ID HGNC:9033 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 1p36.12
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 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]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5313
Enzyme 12 Name Ectonucleoside triphosphate diphosphohydrolase 1
Enzyme 12 Synonyms
  1. NTPDase 1
  2. Ecto-ATP diphosphohydrolase
  3. ATPDase
  4. Lymphoid cell activation antigen
  5. Ecto-apyrase
  6. CD39 antigen
Enzyme 12 Gene Name ENTPD1
Enzyme 12 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 1 
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
Enzyme 12 Number of Residues 510
Enzyme 12 Molecular Weight 57965
Enzyme 12 Theoretical pI 6.29
Enzyme 12 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 12 General Function Not Available
Enzyme 12 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 12 Pathways
Enzyme 12 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • 17-37 479-499
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 765256 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P49961 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name ENTP1_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 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 12 GenBank Gene ID S73813 Link Image
Enzyme 12 GeneCard ID ENTPD1 Link Image
Enzyme 12 GenAtlas ID ENTPD1 Link Image
Enzyme 12 HGNC ID HGNC:3363 Link Image
Enzyme 12 Chromosome Location 10
Enzyme 12 Locus 10q24
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Maliszewski CR, Delespesse GJ, Schoenborn MA, Armitage RJ, Fanslow WC, Nakajima T, Baker E, Sutherland GR, Poindexter K, Birks C, et al.: The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. J Immunol. 1994 Oct 15;153(8):3574-83. [PubMed Link Image]
  2. Robson SC, Kaczmarek E, Siegel JB, Candinas D, Koziak K, Millan M, Hancock WW, Bach FH: Loss of ATP diphosphohydrolase activity with endothelial cell activation. J Exp Med. 1997 Jan 6;185(1):153-63. [PubMed Link Image]
  3. Matsumoto M, Sakurai Y, Kokubo T, Yagi H, Makita K, Matsui T, Titani K, Fujimura Y, Narita N: The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II. FEBS Lett. 1999 Jun 25;453(3):335-40. [PubMed Link Image]
  4. Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O: Purification and properties of human placental ATP diphosphohydrolase. Eur J Biochem. 1995 Nov 15;234(1):66-74. [PubMed Link Image]
  5. Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y: Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. Int J Hematol. 1998 Oct;68(3):297-310. [PubMed Link Image]
  6. Kaczmarek E, Koziak K, Sevigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC: Identification and characterization of CD39/vascular ATP diphosphohydrolase. J Biol Chem. 1996 Dec 20;271(51):33116-22. [PubMed Link Image]
  7. Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed Link Image]
  8. Koziak K, Kaczmarek E, Kittel A, Sevigny J, Blusztajn JK, Schulte Am Esch J 2nd, Imai M, Guckelberger O, Goepfert C, Qawi I, Robson SC: Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae. J Biol Chem. 2000 Jan 21;275(3):2057-62. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5314
Enzyme 13 Name Soluble calcium-activated nucleotidase 1
Enzyme 13 Synonyms
  1. SCAN-1
  2. Apyrase homolog
  3. Putative NF-kappa-B-activating protein 107
  4. Putative MAPK-activating protein PM09
Enzyme 13 Gene Name CANT1
Enzyme 13 Protein Sequence >Soluble calcium-activated nucleotidase 1 
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
Enzyme 13 Number of Residues 401
Enzyme 13 Molecular Weight 44840
Enzyme 13 Theoretical pI 5.98
Enzyme 13 GO Classification Not Available
Enzyme 13 General Function Not Available
Enzyme 13 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 13 Pathways
Enzyme 13 Reactions
  • A nucleoside diphosphate + H2O = a nucleotide + phosphate
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • 45-62
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 22218108 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q8WVQ1 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name CANT1_HUMAN Link Image
Enzyme 13 PDB ID 1S1D Link Image
Enzyme 13 PDB File Show
Enzyme 13 3D Structure
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1116 bp 
ATGACCAAGGCCGCGGACCCCCGCTTCCGCCCCCGCTGGAAGGTGATCCTGACGTTCTTT
GTGGGTGCTGCCATCCTCTGGCTGCTCTGCTCCCACCGCCCGGCCCCCGGCAGGCCCCCC
ACCCACAATGCACACAACTGGAGGCTCGGCCAGGCGCCCGCCAACTGGTACAATGACACC
TACCCCCTGTCTCCCCCACAAAGGACACCGGCTGGGATTCGGTATCGAATCGCAGTTATC
GCAGACCTGGACACAGAGTCAAGGGCCCAAGAGGAAAACACCTGGTTCAGTTACCTGAAA
AAGGGCTACCTGACCCTGTCAGACAGTGGGGACAAGGTGGCCGTGGAATGGGACAAAGAC
CATGGGGTCCTGGAGTCCCACCTGGCGGAGAAGGGGAGAGGCATGGAGCTATCCGACCTG
ATTGTTTTCAATGGGAAACTCTACTCCGTGGATGACCGGACGGGGGTCGTCTACCAGATC
GAAGGCAGCAAAGCCGTGCCCTGGGTGATTCTGTCCGACGGCGACGGCACCGTGGAGAAA
GGCTTCAAGGCCGAATGGCTGGCAGTGAAGGACGAGCGTCTGTACGTGGGCGGCCTGGGC
AAGGAGTGGACGACCACTACGGGTGATGTGGTGAACGAGAACCCGGAGTGGGTGAAGGTG
GTGGGCTACAAGGGCAGCGTGGACCACGAGAACTGGGTGTCCAACTACAACGCCCTGCGG
GCTGCTGCCGGCATCCAGCCGCCAGGCTACCTCATCCATGAGTCTGCCTGCTGGAGTGAC
ACGCTGCAGCGCTGGTTCTTCCTGCCGCGCCGCGCCAGCCAGGAGCGCTACAGCGAGAAG
GACGACGAGCGCAAGGGCGCCAACCTGCTGCTGAGCGCCTCCCCTGACTTCGGCGACATC
GCTGTGAGCCACGTCGGGGCGGTGGTCCCCACTCACGGCTTCTCGTCCTTCAAGTTCATC
CCCAACACCGACGACCAGATCATTGTGGCCCTCAAATCCGAGGAGGACAGCGGCAGAGTC
GCCTCCTACATCATGGCCTTCACGCTGGACGGGCGCTTCCTGTTGCCGGAGACCAAGATC
GGAAGCGTGAAATACGAAGGCATCGAGTTCATTTAA
Enzyme 13 GenBank Gene ID AF328554 Link Image
Enzyme 13 GeneCard ID CANT1 Link Image
Enzyme 13 GenAtlas ID CANT1 Link Image
Enzyme 13 HGNC ID HGNC:19721 Link Image
Enzyme 13 Chromosome Location 17
Enzyme 13 Locus 17q25.3
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Smith TM, Hicks-Berger CA, Kim S, Kirley TL: Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases. Arch Biochem Biophys. 2002 Oct 1;406(1):105-15. [PubMed Link Image]
  2. Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S: Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003 May 22;22(21):3307-18. [PubMed Link Image]
  3. Failer BU, Braun N, Zimmermann H: Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J Biol Chem. 2002 Oct 4;277(40):36978-86. Epub 2002 Aug 6. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5318
Enzyme 14 Name Ectonucleoside triphosphate diphosphohydrolase 3
Enzyme 14 Synonyms
  1. NTPDase 3
  2. Ecto-ATP diphosphohydrolase
  3. ATPDase
  4. Ecto-apyrase
  5. CD39 antigen-like 3
  6. HB6
Enzyme 14 Gene Name ENTPD3
Enzyme 14 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 3 
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
Enzyme 14 Number of Residues 529
Enzyme 14 Molecular Weight 59106
Enzyme 14 Theoretical pI 6.40
Enzyme 14 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Has a threefold preference for the hydrolysis of ATP over ADP
Enzyme 14 Pathways
Enzyme 14 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-37
Enzyme 14 Transmembrane Regions Not Available
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 3335100 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID O75355 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name ENTP3_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 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
CCCATAGAACCACCTGTCTTTGTGGGCACCCTCGCTTTCTTCACAGTGGCAGCCTTGCTG
TGTCTGGCATTTCTTGCATACCTGTGTTCAGCAACCAGAAGAAAGAGGCACTCCGAGCAT
GCCTTTGACCATGCAGTGGATTCTGACTGA
Enzyme 14 GenBank Gene ID AF039917 Link Image
Enzyme 14 GeneCard ID ENTPD3 Link Image
Enzyme 14 GenAtlas ID ENTPD3 Link Image
Enzyme 14 HGNC ID HGNC:3365 Link Image
Enzyme 14 Chromosome Location 3
Enzyme 14 Locus 3p21.3
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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. 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]
  4. 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 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5429
Enzyme 15 Name Glycerol-3-phosphate dehydrogenase, mitochondrial precursor
Enzyme 15 Synonyms
  1. GPD-M
  2. GPDH-M
  3. mtGPD
Enzyme 15 Gene Name GPD2
Enzyme 15 Protein Sequence >Glycerol-3-phosphate dehydrogenase, mitochondrial precursor 
MAFQKAVKGTILVGGGALATVLGLSQFAHYRRKQMNLAYVKAADCISEPVNREPPSREAQ
LLTLQNTSEFDILVIGGGATGSGCALDAVTRGLKTALVERDDFSSGTSSRSTKLIHGGVR
YLQKAIMKLDIEQYRMVKEALHERANLLEIAPHLSAPLPIMLPVYKWWQLPYYWVGIKLY
DLVAGSNCLKSSYVLSKSRALEHFPMLQKDKLVGAIVYYDGQHNDARMNLAIALTAARYG
AATANYMEVVSLLKKTDPQTGKVHVSGARCKDVLTGQEFDVRAKCVINATGPFTDSVRKM
DDKDAAAICQPSAGVHIVMPGYYSPESMGLLDPATSDGRVIFFLPWQKMTIAGTTDTPTD
VTHHPIPSEEDINFILNEVRNYLSCDVEVRRGDVLAAWSGIRPLVTDPKSADTQSISRNH
VVDISESGLITIAGGKWTTYRSMAEDTINAAVKTHNLKAGPSRTVGLFLQGGKDWSPTLY
IRLVQDYGLESEVAQHLAATYGDKAFEVAKMASVTGKRWPIVGVRLVSEFPYIEAEVKYG
IKEYACTAVDMISRRTRLAFLNVQAAEEALPRIVELMGRELNWDDYKKQEQLETARKFLY
YEMGYKSRSEQLTDRSEISLLPSDIDRYKKRFHKFDADQKGFITIVDVQRVLESINVQMD
ENTLHEILNEVDLNKNGQVELNEFLQLMSAIQKGRVSGSRLAILMKTAEENLDRRVPIPV
DRSCGGL
Enzyme 15 Number of Residues 727
Enzyme 15 Molecular Weight 80835
Enzyme 15 Theoretical pI 7.58
Enzyme 15 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • glycerol-3-phosphate dehydrogenase activity
  • ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
Process
  • alcohol metabolism
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • glycerol metabolism
  • glycerol-3-phosphate metabolism
  • metabolism
  • physiological process
  • polyol metabolism
Component
  • glycerol-3-phosphate dehydrogenase complex
  • protein complex
  • unlocalized protein complex
Enzyme 15 General Function Energy production and conversion
Enzyme 15 Specific Function sn-glycerol 3-phosphate + acceptor = glycerone phosphate + reduced acceptor
Enzyme 15 Pathways
Enzyme 15 Reactions
  • sn-glycerol 3-phosphate + acceptor = glycerone phosphate + reduced acceptor
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-23
Enzyme 15 Transmembrane Regions Not Available
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 533693 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P43304 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name GPDM_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >2184 bp 
ATGGCATTTCAAAAGGCAGTGAAAGGGACGATTCTTGTTGGAGGAGGTGCTCTTGCAACT
GTTTTAGGACTTTCTCAGTTTGCTCATTACAGAAGGAAACAAATGAACCTGGCCTATGTT
AAAGCAGCAGACTGCATTTCAGAACCAGTTAACAGGGAGCCTCCTTCCAGAGAAGCTCAG
CTACTGACTTTGCAAAACACATCTGAATTTGATATCCTTGTTATTGGAGGAGGAGCAACA
GGAAGTGGCTGTGCGCTAGATGCTGTCACCAGAGGACTAAAAACAGCCCTTGTAGAAAGA
GATGATTTCTCATCAGGGACCAGCAGCAGAAGCACTAAATTGATCCATGGTGGTGTGAGA
TATCTGCAGAAGGCCATCATGAAGTTGGATATTGAGCAGTATAGGATGGTAAAAGAAGCC
CTTCATGAGCGTGCCAACCTGCTAGAAATTGCTCCCCATTTATCAGCTCCATTGCCTATA
ATGCTTCCAGTTTACAAGTGGTGGCAGTTACCTTACTACTGGGTAGGAATCAAGCTGTAT
GATTTGGTTGCAGGAAGCAATTGCCTAAAAAGCAGTTATGTCCTCAGCAAATCAAGAGCC
CTTGAACATTTCCCAATGCTCCAGAAGGACAAACTGGTAGGAGCAATTGTCTACTATGAC
GGACAACATAACGATGCACGGATGAACCTTGCCATTGCTCTGACTGCTGCCAGGTATGGG
GCTGCCACAGCCAATTACATGGAGGTAGTGAGCTTGCTCAAGAAGACAGACCCCCAGACA
GGGAAAGTGCATGTGAGCGGCGCACGGTGCAAGGATGTCCTCACAGGGCAGGAATTTGAC
GTGAGAGCCAAATGTGTTATCAATGCCACGGGACCTTTCACGGACTCTGTGCGCAAAATG
GATGATAAAGACGCAGCAGCTATCTGCCAGCCAAGTGCTGGTGTCCATATTGTGATGCCT
GGTTATTACAGCCCAGAGAGCATGGGACTTCTTGACCCAGCGACCAGTGATGGGCGAGTT
ATTTTCTTCTTACCCTGGCAAAAGATGACGATCGCTGGCACTACTGATACTCCAACTGAT
GTTACACACCATCCAATTCCTTCAGAAGAAGATATCAACTTCATTTTGAATGAAGTGCGT
AATTACCTGAGTTGTGATGTTGAAGTGAGAAGAGGGGATGTCCTGGCAGCATGGAGTGGA
ATCCGTCCTCTTGTTACAGACCCCAAATCTGCAGATACTCAGTCTATCTCCCGAAATCAT
GTTGTTGATATCAGTGAGAGTGGCCTTATTACTATAGCAGGTGGAAAGTGGACAACTTAT
CGGTCTATGGCAGAAGATACCATAAATGCTGCTGTCAAAACTCATAATTTAAAAGCAGGA
CCAAGTAGAACAGTTGGGCTTTTCCTTCAAGGGGGTAAAGATTGGAGCCCCACACTCTAC
ATTAGGCTTGTGCAGGATTATGGACTTGAAAGCGAGGTGGCACAGCATCTTGCCGCCACC
TATGGTGATAAGGCCTTTGAGGTGGCCAAAATGGCAAGTGTGACTGGCAAAAGGTGGCCT
ATTGTTGGAGTACATCTTGTGTCAGAATTTCCATATATTGAAGCAGAGGTGAAATATGGG
ATTAAGGAGTATGCCTGCACTGCTGTGGATATGATTTCACGTCGTACTCGCCTGGCCTTT
CTAAATGTCCAGGCAGCAGAGGAAGCCCTACCCAGGATTGTTGAACTGATGGGCAGGGAA
CTGAATTGGGATGATTATAAGAAGCAGGAACAACTTGAAACAGCCAGGAAGTTTCTATAT
TATGAAATGGGCTATAAATCTCGATCAGAACAGTTAACAGATCGCTCTGAAATTAGCCTA
CTGCCTTCAGACATTGACAGGTATAAGAAGAGATTTCATAAGTTTGATGCAGACCAGAAA
GGCTTTATTACCATTGTTGATGTTCAGCGTGTATTAGAGAGTATCAATGTCCAAATGGAT
GAAAATACACTCCATGAAATTCTAAATGAAGTTGATTTGAATAAAAATGGACAGGTTGAA
CTCAATGAATTTTTGCAGCTGATGAGTGCTATTCAAAAAGGAAGGGTATCTGGAAGCCGG
CTTGCTATACTAATGAAAACTGCAGAAGAGAACCTCGACAGAAGAGTTCCAATTCCAGTG
GACCGTAGTTGTGGAGGATTGTGA
Enzyme 15 GenBank Gene ID U12424 Link Image
Enzyme 15 GeneCard ID GPD2 Link Image
Enzyme 15 GenAtlas ID GPD2 Link Image
Enzyme 15 HGNC ID HGNC:4456 Link Image
Enzyme 15 Chromosome Location 2
Enzyme 15 Locus 2q24.1
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 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. Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5443
Enzyme 16 Name Glucosamine-6-phosphate isomerase
Enzyme 16 Synonyms
  1. Glucosamine-6- phosphate deaminase
  2. GNPDA
  3. GlcN6P deaminase
  4. Oscillin
Enzyme 16 Gene Name GNPDA1
Enzyme 16 Protein Sequence >Glucosamine-6-phosphate isomerase 
MKLIILEHYSQASEWAAKYIRNRIIQFNPGPEKYFTLGLPTGSTPLGCYKKLIEYYKNGD
LSFKYVKTFNMDEYVGLPRDHPESYHSFMWNNFFKHIDIHPENTHILDGNAVDLQAECDA
FEEKIKAAGGIELFVGGIGPDGHIAFNEPGSSLVSRTRVKTLAMDTILANARFFDGELTK
VPTMALTVGVGTVMDAREVMILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTVFVCD
EDATLELKVKTVKYFKGLMLVHNKLVDPLYSIKEKETEKSQSSKKPYSD
Enzyme 16 Number of Residues 289
Enzyme 16 Molecular Weight 32669
Enzyme 16 Theoretical pI 6.91
Enzyme 16 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 metabolism
  • amine metabolism
  • amino sugar metabolism
  • carbohydrate metabolism
  • glucosamine metabolism
  • macromolecule metabolism
  • metabolism
  • nitrogen compound metabolism
  • physiological process
Component
—
Enzyme 16 General Function Carbohydrate transport and metabolism
Enzyme 16 Specific Function D-glucosamine 6-phosphate + H(2)O = D-fructose 6-phosphate + NH(3)
Enzyme 16 Pathways
Enzyme 16 Reactions
  • D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + ammonia
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 2935438 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID P46926 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name GNPI_HUMAN Link Image
Enzyme 16 PDB ID 1NE7 Link Image
Enzyme 16 PDB File Show
Enzyme 16 3D Structure
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >870 bp 
ATGAAGCTCATCATCCTGGAGCACTATTCTCAGGCGAGCGAGTGGGCGGCTAAATACATC
AGGAACCGTATCATCCAGTTTAACCCAGGGCCAGAGAAGTACTTCACCCTGGGGCTCCCC
ACTGGGAGTACCCCACTTGGCTGCTACAAGAAGCTGATTGAATACTATAAGAATGGGGAC
CTGTCCTTTAAATATGTGAAGACCTTCAACATGGATGAGTACGTGGGCCTTCCTCGAGAC
CACCCGGAGAGTTACCACTCCTTCATGTGGAACAACTTCTTCAAGCACATTGACATCCAC
CCAGAAAACACCCACATTCTGGATGGGAATGCAGTCGACCTACAGGCAGAATGTGATGCC
TTTGAAGAGAAGATCAAGGCTGCAGGTGGGATCGAGCTATTTGTTGGAGGCATCGGCCCT
GATGGACACATTGCCTTCAACGAGCCAGGCTCCAGTCTGGTGTCCAGGACCCGTGTGAAG
ACGCTGGCCATGGATACCATCCTGGCCAATGCTAGGTTCTTCGATGGAGAACTCACCAAG
GTGCCCACCATGGCCTTGACGGTGGGGGTGGGCACTGTCATGGATGCTAGAGAGGTGATG
ATCCTTATCACAGGTGCTCACAAGGCATTTGCTCTGTACAAGGCCATCGAGGAGGGAGTG
AACCACATGTGGACCGTGTCTGCCTTCCAGCAGCATCCCCGCACCGTGTTTGTGTGTGAC
GAGGATGCCACCTTGGAGCTGAAAGTGAAGACTGTCAAGTATTTCAAAGGTTTAATGCTT
GTTCATAACAAGTTGGTGGACCCCTTGTACAGTATCAAAGAGAAAGAAACTGAGAAAAGC
CAATCTTCGAAGAAACCATACAGCGATTAG
Enzyme 16 GenBank Gene ID AF048826 Link Image
Enzyme 16 GeneCard ID GNPDA1 Link Image
Enzyme 16 GenAtlas ID GNPDA1 Link Image
Enzyme 16 HGNC ID HGNC:4417 Link Image
Enzyme 16 Chromosome Location 5
Enzyme 16 Locus 5q21
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 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. 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]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5454
Enzyme 17 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 1
Enzyme 17 Synonyms
  1. Phosphoinositide phospholipase C
  2. Phospholipase C- beta-1
  3. PLC-beta-1
  4. PLC-I
  5. PLC-154
Enzyme 17 Gene Name PLCB1
Enzyme 17 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 17 Number of Residues 1216
Enzyme 17 Molecular Weight 138568
Enzyme 17 Theoretical pI 6.12
Enzyme 17 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphodiesterase activity
  • ion binding
  • lipase activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • signal transduction
Component
—
Enzyme 17 General Function Cell cycle control, cell division, chromosome partitioning
Enzyme 17 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 17 Pathways
Enzyme 17 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 9368448 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q9NQ66 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name PLCB1_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >3651 bp 
ATGGCCGGGGCTCAACCCGGAGTGCACGCCTTGCAACTCAAGCCCGTGTGCGTGTCCGAC
AGCCTCAAGAAGGGCACCAAATTCGTCAAGTGGGATGATGATTCAACTATTGTTACTCCA
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 17 GenBank Gene ID AJ278313 Link Image
Enzyme 17 GeneCard ID PLCB1 Link Image
Enzyme 17 GenAtlas ID PLCB1 Link Image
Enzyme 17 HGNC ID HGNC:15917 Link Image
Enzyme 17 Chromosome Location 20
Enzyme 17 Locus 20p12
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. 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]
  2. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
  3. 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. 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 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5455
Enzyme 18 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 4
Enzyme 18 Synonyms
  1. Phosphoinositide phospholipase C
  2. Phospholipase C- beta-4
  3. PLC-beta-4
Enzyme 18 Gene Name PLCB4
Enzyme 18 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 18 Number of Residues 1175
Enzyme 18 Molecular Weight 134465
Enzyme 18 Theoretical pI 6.90
Enzyme 18 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphodiesterase activity
  • ion binding
  • lipase activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • signal transduction
Component
—
Enzyme 18 General Function Replication, recombination and repair
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. This form has a role in retina signal transduction
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 762826 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q15147 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name PLCB4_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >3069 bp 
ATGAACAATAACTGGAATGTGTGTTTCTTTCTTTTCTGCCCTAGTATTACTAGAACATTT
GCATCGGGAAAAACAGAAAAGGTGATCTTTCAAGCACTCAAGGAGTTAGGTCTTCCCAGT
GGAAAGAATGATGAAATTGAGCCCACAGCATTTTCTTATGAAAAGTTCTATGAACTGACA
CAAAAGATTTGTCCTCGGACAGATATAGAAGATCTTTTCAAAAAAATCAATGGAGACAAA
ACTGATTATTTAACGGTAGACCAATTAGTGAGCTTTCTAAATGAACATCAACGAGATCCT
CGATTGAATGAAATTTTATTTCCATTTTATGATGCCAAAAGGGCAATGCAGATCATTGAG
ATGTATGAACCTGATGAAGATTTGAAGAAAAAAGGCCTTATATCAAGTGATGGGTTTTGC
AGATATCTGATGTCAGATGAAAACGCCCCAGTCTTCCTAGATCGTTTAGAACTTTACCAA
GAAATGGACCATCCTCTGGCTCACTACTTCATCAGTTCTTCCCATAACACTTATCTCACT
GGCAGACAGTTCGGCGGGAAGTCTTCGGTAGAAATGTACAGACAGGTTCTCCTGGCTGGT
TGCAGATGTGTTGAACTTGACTGCTGGGATGGAAAAGGTGAGGACCAAGAACCAATAATA
ACTCATGGAAAAGCAATGTGTACAGATATCCTTTTTAAGGATGTAATTCAAGCCATCAAG
GAAACTGCATTTGTCACATCAGAATATCCTGTAATTCTCTCCTTTGAAAATCACTGCAGC
AAATATCAACAGTACAAGATGTCCAAATATTGCGAAGATCTATTTGGGGATCTCCTGTTG
AAACAAGCACTTGAATCACATCCACTGGAACCAGGCAGACCTTTGCCATCCCCCAATGAC
CTCAAAAGAAAAATACTCATAAAAAACAAGCGGCTGAAACCTGAAGTTGAAAAAAAACAG
CTGGAAGCTTTGAGAAGCATGATGGAAGCTGGAGAATCTGCCTCCCCAGCAAACATCTTA
GAGGACGATAATGAAGAGGAGATCGAAAGTGCTGACCAAGAGGAGGAAGCTCACCCCGAA
TTCAAATTTGGAAATGAACTTTCTGCTGATGACTTGGGTCACAAGGAAGCTGTTGCAAAT
AGCGTCAAGAAGGGCCTGGTCACTGTAGAAGATGAGCAGGCGTGGATGGCATCTTATAAA
TATGTAGGTGCTACCACTAATATCCATCCATATTTGTCCACAATGATCAACTATGCCCAG
CCTGTAAAGTTTCAAGGTTTCCATGTGGCAGAAGAACGCAATATTCATTATAACATGTCT
TCTTTTAATGAATCAGTCGGTCTTGGCTACTTGAAGACACATGCAATTGAATTTGTCAAT
TATAACAAACGGCAAATGAGTCGCATTTACCCCAAGGGAGGCCGAGTCGATTCCAGTAAT
TACATGCCTCAGATTTTCTGGAACGCTGGCTGCCAGATGGTTTCACTGAACTATCAAACC
CCAGATTTAGCGATGCAATTGAATCAGGGAAAATTTGAGTATAATGGATCGTGCGGGTAC
CTTCTCAAACCAGATTTCATGAGGCGGCCTGATCGAACATTTGACCCCTTCTCTGAAACG
CCTGTTGATGGGGTTATTGCAGCCACTTGCTCAGTGCAGGTTATATCAGGTCAATTCTTA
TCAGATAAGAAAATTGGCACCTACGTAGAGGTGGATATGTATGGGTTGCCCACTGACACC
ATACGTAAGGAATTCCGAACTCGCATGGTTATGAATAATGGACTCAATCCAGTTTACAAT
GAAGAGTCACTTGTATTTCGGAAGGTGATCCTGCCGGACCTGGCTGTCTTGAGAATAGCT
GTGTATGATGATAACAACAAGCTGATTGGCCAGAGGATTCCTCCGCTTGATGGCCTCCAA
GCCGGATATCGACACATTTCCCTTCGAAATGAGGGAAATAAACCATTATCACTACCAACA
ATTTTCTGCAATATTGTTCTTAAAACATATGTGCCTGATGGATTTGGAGATATCGTGGAT
GCTTTATCAGATCCAAAGACATTTCTCTCAATTACAGAAAAGAGAGCAGACCAAATGAGA
GCTATGGGCATTGAGACTAGTGACATAGCCGACGTGCCCAGTGACACTTCCAAAAATGAC
AAGAAAGGAAAGGCCAACACCGCCAAAGCAAATGTGACCCCTCAGAGTAGCTCTGAGCTC
AGACCAACCACCACGGCTGCCCTGCCGTCTGGTGTGGAAGCCAAGAAAGGTATTGAACTT
ATCCCTCAAGTAAGGATAGAAGACTTAAAGCAGATGAAGGCTTACTTGAAGCATTTAAAG
AAACAGCAGAAGGAGCTAAATTCTTTAAAGAAGAAACATGCAAAGGAACACAGTACCATG
CAGAAGTTACACTGCACGCAAGTTGACAAAATTGTGGCACAGTATGACAAAGAGAAGTCG
ACTCATGAGAAAATCCTAGAGAAGGCAATGAAGAAGAAAGGGGGAAGTAATTGTCTTGAA
ATGAAGAAAGAAACAGAAATTAAAATTCAGACGCTGACATCAGATCACAAATCTAAGGTC
AAGGAGATTGTAGCACAGCACACAAAGGAATGGTCAGAAATGATCAATACTCACAGTGCT
GAGGAGCAAGAAATCCGAGACCTGCACCTCAGCCAGCAGTGTGAGCTGCTGAAAAAGCTA
CTCATCAATGCCCACGAGCAGCAAACCCAGCAGCTGAAACTGTCCCATGACAGGGAAAGC
AAGGAAATGCGAGCACACCAGGCTAAGATTTCTATGGAAAATAGCAAAGCCATCAGCCAA
GATAAATCTATCAAGAATAAAGCAGAACGGGAAAGGCGAGTCAGGGAGTTAAACAGCAGC
AACACTAAAAAGTTTCTGGAAGAAAGAAAGAGACTTGCCATGAAGCAGTCCAAAGAAATG
GATCAGTTGAAAAAAGTCCAGCTTGAACATCTAGAATTCCTAGAGAAACAGAATGAGCAG
GCGAAGGAGATGCAGCAGATGGTGAAATTGGAAGCCGAGATGGACCGCAGACCAGCAACA
GTAGTATGA
Enzyme 18 GenBank Gene ID L41349 Link Image
Enzyme 18 GeneCard ID PLCB4 Link Image
Enzyme 18 GenAtlas ID PLCB4 Link Image
Enzyme 18 HGNC ID HGNC:9059 Link Image
Enzyme 18 Chromosome Location 20
Enzyme 18 Locus 20p12
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 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]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5456
Enzyme 19 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 2
Enzyme 19 Synonyms
  1. Phosphoinositide phospholipase C
  2. Phospholipase C- beta-2
  3. PLC-beta-2
Enzyme 19 Gene Name PLCB2
Enzyme 19 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 2 
MSLLNPVLLPPKVKAYLSQGERFIKWDDETTVASPVILRVDPKGYYLYWTYQSKEMEFLD
ITSIRDTRFGKFAKMPKSQKLRDVFNMDFPDNSFLLKTLTVVSGPDMVDLTFHNFVSYKE
NVGKAWAEDVLALVKHPLTANASRSTFLDKILVKLKMQLNSEGKIPVKNFFQMFPADRKR
VEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSYHAKAKPYMTKEH
LTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPEN
SVLAQDKLLLHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDC
WKGKPPDEEPIITHGFTMTTDIFFKEAIEAIAESAFKTSPYPIILSFENHVDSPRQQAKM
AEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKNQFSGPTSSSKDTGGE
AEGSSPPSAPAVWAGEEGTELEEEEVEEEEEEESGNLDEEEIKKMQSDEGTAGLEVTAYE
EMSSLVNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQMSRIY
PKGTRMDSSNYMPQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEFMRRP
DKQFNPFSVDRIDVVVATTLSITVISGQFLSERSVRTYVEVELFGLPGDPKRRYRTKLSP
STNSINPVWKEEPFVFEKILMPELASLRVAVMEEGNKFLGHRIIPINALNSGYHHLCLHS
ESNMPLTMPALFIFLEMKDYIPGAWADLTVALANPIKFFSAHDTKSVKLKEAMGGLPEKP
FPLASPVASQVNGALAPTSNGSPAARAGAREEAMKEAAEPRTASLEELRELKGVVKLQRR
HEKELRELERRGARRWEELLQRGAAQLAELGPPGVGGVGACKLGPGKGSRKKRSLPREES
AGAAPGEGPEGVDGRVRELKDRLELELLRQGEEQYECVLKRKEQHVAEQISKMMELAREK
QAAELKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREINNSHIQEVV
QVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEARMKGLEAEVKESVRA
CLRTCFPSEAKDKPERACECPPELCEQDPLIAKADAQESRL
Enzyme 19 Number of Residues 1181
Enzyme 19 Molecular Weight 133681
Enzyme 19 Theoretical pI 6.28
Enzyme 19 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphodiesterase activity
  • ion binding
  • lipase activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • signal transduction
Component
—
Enzyme 19 General Function Replication, recombination and repair
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
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 190040 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q00722 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name PLCB2_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >3546 bp 
ATGTCTCTGCTCAACCCTGTCCTGCTGCCCCCCAAGGTGAAGGCCTATCTGAGCCAAGGG
GAGCGCTTCATCAAATGGGATGATGAAACTACAGTTGCCTCTCCAGTTATCCTCCGTGTG
GATCCTAAGGGCTACTACTTATACTGGACGTATCAAAGTAAGGAGATGGAGTTTCTGGAT
ATCACCAGCATCCGGGATACTCGCTTTGGGAAGTTTGCCAAGATGCCCAAGAGCCAGAAG
CTCCGGGACGTCTTCAACATGGACTTTCCTGATAACAGTTTCCTGCTGAAGACACTCACG
GTGGTGTCCGGCCCGGACATGGTGGACCTCACCTTCCACAACTTCGTCTCCTACAAGGAG
AACGTGGGCAAGGCCTGGGCTGAGGACGTACTGGCCCTAGTCAAACATCCGCTGACGGCC
AACGCCTCCCGCAGCACCTTCCTGGACAAGATCCTTGTGAAGCTCAAGATGCAGCTCAAC
TCTGAAGGGAAGATTCCGGTGAAGAACTTTTTCCAGATGTTTCCTGCTGACCGCAAGCGG
GTGGAAGCTGCTCTCAGTGCCTGCCACCTCCCCAAAGGCAAAAATGACGCCATCAATCCT
GAGGACTTCCCAGAACCTGTCTACAAGAGTTTCCTCATGAGCCTCTGTCCTCGGCCAGAA
ATAGATGAGATCTTCACTTCTTACCATGCTAAGGCCAAACCCTACATGACGAAGGAGCAC
CTGACCAAATTCATCAACCAGAAACAGCGGGACTCCCGGCTTAACTCCCTGCTGTTCCCG
CCAGCACGGCCTGACCAGGTGCAGGGCCTCATCGACAAGTATGAGCCCAGTGGCATCAAT
GCACAGAGGGGCCAGCTGTCACCTGAAGGCATGGTCTGGTTTCTCTGTGGGCCAGAGAAC
AGCGTGCTGGCCCAGGACAAGCTGCTGCTCCACCACGACATGACGCAGCCACTCAATCAT
TACTTCATCAACTCGTCCCACAACACCTACCTGACAGCCGGCCAGTTCTCAGGCCTCTCC
TCGGCTGAGATGTACCGCCAGGTGCTGCTCTCTGGCTGCCGTTGCGTGGAGCTAGACTGC
TGGAAGGGGAAACCCCCTGACGAGGAGCCCATTATCACCCATGGCTTCACCATGACCACA
GACATCTTCTTCAAAGAAGCAATTGAGGCTATTGCAGAAAGTGCCTTTAAGACCTCCCCC
TATCCCATCATCCTGTCGTTTGAGAACCATGTGGACTCACCCCGCCAGCAGGCTAAGATG
GCTGAGTATTGCCGGACGATCTTTGGGGATATGCTGCTCACAGAGCCCCTGGAAAAGTTC
CCACTAAAACCAGGTGTCCCCCTGCCCAGCCCTGAGGATCTCAGGGGCAAGATCCTCATC
AAGAACAAGAAGAACCAGTTTTCTGGCCCCACCTCCTCCAGTAAGGATACCGGTGGGGAG
GCTGAGGGCAGCAGCCCACCCAGTGCCCCTGCAGTGTGGGCTGGCGAGGAAGGGACTGAG
CTGGAGGAGGAGGAGGTGGAAGAGGAAGAGGAGGAGGAGTCAGGAAACCTGGATGAAGAA
GAGATTAAGAAGATGCAGTCGGATGAGGGCACAGCGGGCCTGGAAGTGACGGCTTATGAG
GAGATGTCCAGCCTAGTCAATTACATCCAGCCCACCAAGTTCGTCTCCTTTGAGTTCTCT
GCCCAAAAGAACCGAAGTTATGTCATCTCGTCCTTCACAGAGCTCAAGGCATATGACCTG
CTCTCCAAGGCCTCGGTGCAGTTTGTGGACTACAACAAGCGCCAGATGAGCCGCATTTAC
CCCAAGGGAACCCGCATGGACTCCTCCAACTACATGCCCCAGATGTTCTGGAATGCTGGA
TGCCAGATGGTTGCCCTCAACTTCCAGACGATGGACTTGCCCATGCAGCAGAACATGGCA
GTATTTGAGTTCAACGGGCAGAGCGGCTACCTCCTCAAGCATGAGTTCATGCGCCGGCCG
GACAAGCAGTTCAACCCCTTCTCAGTGGACCGCATCGACGTGGTGGTGGCCACCACCCTT
TCCATTACGGTGATCTCTGGGCAGTTCCTGTCAGAACGCAGCGTGCGCACCTATGTAGAA
GTGGAGCTGTTTGGCCTTCCTGGGGACCCCAAGAGGCGCTATCGAACTAAGCTGTCACCC
AGTACTAACTCCATCAATCCTGTCTGGAAGGAGGAGCCCTTTGTCTTTGAGAAGATCTTG
ATGCCTGAGCTGGCCTCCCTCAGAGTGGCTGTGATGGAGGAAGGCAACAAGTTTCTTGGA
CACCGCATCATCCCCATCAATGCCCTAAATTCTGGGTACCACCACCTGTGCCTGCACAGT
GAGAGCAACATGCCCCTCACCATGCCTGCGCTCTTCATCTTCCTGGAGATGAAGGACTAC
ATACCTGGTGCTTGGGCAGATCTCACTGTGGCCCTCGCCAACCCCATTAAGTTCTTCAGT
GCCCATGACACGAAGTCTGTGAAGCTCAAGGAGGCCATGGGAGGTCTGCCTGAGAAGCCC
TTCCCACTGGCGAGTCCAGTTGCCAGCCAGGTCAATGGGGCGTTGGCCCCAACGAGCAAT
GGGTCACCAGCAGCCAGGGCCGGGGCCAGGGAAGAGGCTATGAAAGAAGCTGCGGAGCCG
CGGACCGCCAGCCTGGAGGAGCTCCGGGAGCTAAAGGGCGTGGTGAAGCTGCAGCGGCGG
CACGAGAAGGAGCTGCGAGAGTTGGAGCGGCGCGGAGCGCGGCGCTGGGAGGAGCTGCTG
CAGCGGGGCGCGGCGCAGCTGGCGGAGCTCGGGCCACCGGGCGTGGGGGGCGTCGGGGCC
TGCAAGCTCGGTCCCGGCAAGGGCTCTCGCAAGAAGAGGAGCCTGCCCCGCGAGGAGAGC
GCCGGAGCCGCGCCGGGCGAGGGCCCTGAGGGCGTGGACGGGCGCGTGCGGGAGCTGAAA
GACAGGCTGGAGCTGGAGCTGCTGCGGCAGGGCGAGGAGCAGTACGAGTGCGTTCTGAAG
CGCAAGGAGCAGCACGTGGCCGAGCAAATCTCCAAAATGATGGAGCTGGCCAGAGAGAAA
CAGGCGGCAGAGCTGAAGGCCCTGAAGGAGACGTCGGAGAACGACACCAAAGAGATGAAG
AAAAAGCTGGAGACAAAGAGACTGGAGCGGATCCAGGGCATGACCAAAGTCACCACAGAC
AAGATGGCCCAGGAGAGGTTGAAGAGAGAGATTAACAACTCCCACATCCAGGAAGTAGTG
CAGGTGATCAAGCAGATGACGGAGAACTTGGAGAGGCACCAGGAGAAGCTGGAGGAGAAG
CAGGCGGCTTGCCTGGAACAGATACGGGAGATGGAAAAGCAGTTCCAGAAGGAGGCGCTG
GCAGAGTACGAGGCCAGGATGAAGGGTCTGGAGGCAGAGGTGAAGGAGTCGGTGAGGGCC
TGCCTCAGGACCTGCTTTCCCTCCGAGGCCAAGGACAAGCCTGAGAGGGCCTGCGAGTGC
CCCCCAGAGCTGTGTGAGCAGGACCCACTCATAGCAAAGGCAGATGCCCAGGAGAGCCGC
CTCTGA
Enzyme 19 GenBank Gene ID M95678 Link Image
Enzyme 19 GeneCard ID PLCB2 Link Image
Enzyme 19 GenAtlas ID PLCB2 Link Image
Enzyme 19 HGNC ID HGNC:9055 Link Image
Enzyme 19 Chromosome Location 15
Enzyme 19 Locus 15q15
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 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]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5460
Enzyme 20 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 3
Enzyme 20 Synonyms
  1. Phosphoinositide phospholipase C
  2. Phospholipase C- beta-3
  3. PLC-beta-3
Enzyme 20 Gene Name PLCB3
Enzyme 20 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 20 Number of Residues 1234
Enzyme 20 Molecular Weight 138801
Enzyme 20 Theoretical pI 5.66
Enzyme 20 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphodiesterase activity
  • ion binding
  • lipase activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • signal transduction
Component
—
Enzyme 20 General Function Not Available
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 836665 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q01970 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name PLCB3_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 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
GCGAGGCTCCCCCAGGAGATCCGCCGGAGCCTGCTGGGCGAGATGCCGGAGGGGCTGGGG
GACGGGCCTCTGGTGGCCTGTGCCAGCAACGGTCACGCACCCGGGAGCAGCGGGCACCTG
TCGGGCGCTGACTCGGAGAGCCAGGAGGAGAACACGCAGCTCTGA
Enzyme 20 GenBank Gene ID U26425 Link Image
Enzyme 20 GeneCard ID PLCB3 Link Image
Enzyme 20 GenAtlas ID PLCB3 Link Image
Enzyme 20 HGNC ID HGNC:9056 Link Image
Enzyme 20 Chromosome Location 11
Enzyme 20 Locus 11q13
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 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. 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]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5462
Enzyme 21 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma 2
Enzyme 21 Synonyms
  1. Phosphoinositide phospholipase C
  2. PLC-gamma-2
  3. Phospholipase C-gamma-2
  4. PLC-IV
Enzyme 21 Gene Name PLCG2
Enzyme 21 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma 2 
MSTTVNVDSLAEYEKSQIKRALELGTVMTVFSFRKSTPERRTVQVIMETRQVAWSKTADK
IEGFLDIMEIKEIRPGKNSKDFERAKAVRQKEDCCFTILYGTQFVLSTLSLAADSKEDAV
NWLSGLKILHQEAMNASTPTIIESWLRKQIYSVDQTRRNSISLRELKTILPLINFKVSSA
KFLKDKFVEIGAHKDELSFEQFHLFYKKLMFEQQKSILDEFKKDSSVFILGNTDRPDASA
VYLHDFQRFLIHEQQEHWAQDLNKVRERMTKFIDDTMRETAEPFLFVDEFLTYLFSRENS
IWDEKYDAVDMQDMNNPLSHYWISSSHNTYLTGDQLRSESSPEAYIRCLRMGCRCIELDC
WDGPDGKPVIYHGWTRTTKIKFDDVVQAIKDHAFVTSSFPVILSIEEHCSVEQQRHMAKA
FKEVFGDLLLTKPTEASADQLPSPSQLREKIIIKHKKLGPRGDVDVNMEDKKDEHKQQGE
LYMWDSIDQKWTRHYCAIADAKLSFSDDIEQTMEEEVPQDIPPTELHFGEKWFHKKVEKR
TSAEKLLQEYCMETGGKDGTFLVRESETFPNDYTLSFWRSGRVQHCRIRSTMEGGTLKYY
LTDNLTFSSIYALIQHYRETHLRCAEFELRLTDPVPNPNPHESKPWYYDSLSRGEAEDML
MRIPRDGAFLIRKREGSDSYAITFRARGKVKHCRINRDGRHFVLGTSAYFESLVELVSYY
EKHSLYRKMRLRYPVTPELLERYNMERDINSLYDVSRMYVDPSEINPSMPQRTVKALYDY
KAKRSDELSFCRGALIHNVSKEPGGWWKGDYGTRIQQYFPSNYVEDISTADFEELEKQII
EDNPLGSLCRGILDLNTYNVVKAPQGKNQKSFVFILEPKQQGYPPVEFATDRVEELFEWF
QSIREITWKIDTKENNMKYWEKNQSIAIELSDLVVYCKPTSKTKDNLENPDFREIRSFVE
TKADSIIRQKPVDLLKYNQKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALNFQTADKY
MQMNHALFSLNGRTGYVLQPESMRTEKYDPMPPESQRKILMTLTVKVLGARHLPKLGRSI
ACPFVEVEICGAEYDNNKFKTTVVNDNGLSPIWAPTQEKVTFEIYDPNLAFLRFVVYEED
MFSDPNFLAHATYPIKAVKSGFRSVPLKNGYSEDIELASLLVFCEMRPVLESEEELYSSC
RQLRRRQEELNNQLFLYDTHQNLRNANRDALVKEFSVNENQLQLYQEKCNKRLREKRVSN
SKFYS
Enzyme 21 Number of Residues 1265
Enzyme 21 Molecular Weight 147919
Enzyme 21 Theoretical pI 6.66
Enzyme 21 GO Classification Not Available
Enzyme 21 General Function Not Available
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. It is a crucial enzyme in transmembrane signaling
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 Not Available
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 35514 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID P16885 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name PLCG2_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >3759 bp 
ATGTCCACCACGGTCAATGTAGATTCCCTTGCGGAATATGAGAAGAGCCAGATCAAGAGA
GCCCTGGAGCTGGGGACGGTGATGACTGTGTTCAGCTTCCGCAAGTCCACCCCCGAGCGG
AGAACCGTCCAGGTGATCATGGAGACGCGGCAGGTGGCCTGGAGCAAGACCGCCGACAAG
ATCGAGGGCTTCTTGGATATCATGGAAATAAAAGAAATCCGCCCAGGGAAGAACTCCAAA
GATTTCGAGCGAGCAAAAGCAGTTCGCCAGAAAGAAGACTGCTGCTTCACCATCCTATAT
GGCACTCAGTTCGTCCTCAGCACGCTCAGCTTGGCAGCTGACTCTAAAGAGGATGCAGTT
AACTGGCTCTCTGGCTTGAAAATCTTACACCAGGAAGCGATGAATGCGTCCACGCCCACC
ATTATCGAGAGTTGGCTGAGAAAGCAGATATATTCTGTGGATCAAACCAGAAGAAACAGC
ATCAGTCTCCGAGAGTTGAAGACCATCTTGCCCCTGATCAACTTTAAAGTGAGCAGTGCC
AAGTTCCTTAAAGATAAGTTTGTGGAAATAGGAGCACACAAAGATGAGCTCAGCTTTGAA
CAGTTCCATCTCTTCTATAAAAAACTTATGTTTGAACAGCAAAAATCGATTCTCGATGAA
TTCAAAAAGGATTCGTCCGTGTTCATCCTGGGGAACACTGACAGGCCGGATGCCTCTGCT
GTTTACCTGCATGACTTCCAGAGGTTTCTCATACATGAACAGCAGGAGCATTGGGCTCAG
GATCTGAACAAAGTCCGTGAGCGGATGACAAAGTTCATTGATGACACCATGCGTGAAACT
GCTGAGCCTTTCTTGTTTGTGGATGAGTTCCTCACGTACCTGTTTTCACGAGAAAACAGC
ATCTGGGATGAGAAGTATGACGCGGTGGACATGCAGGACATGAACAACCCCCTGTCTCAT
TACTGGATCTCCTCGTCACATAACACGTACCTTACAGGTGACCAGCTGCGGAGCGAGTCG
TCCCCAGAAGCTTACATCCGCTGCCTGCGCATGGGCTGTCGCTGCATTGAACTGGACTGC
TGGGACGGGCCCGATGGGAAGCCGGTCATCTACCATGGCTGGACGCGGACTACCAAGATC
AAGTTTGATGACGTCGTGCAGGCCATCAAAGACCACGCCTTTGTTACCTCGAGCTTCCCA
GTGATCCTGTCCATCGAGGAGCACTGCAGCGTGGAGCAACAGCGTCACATGGCCAAGGCC
TTCAAGGAAGTATTTGGCGACCTGCTGTTGACGAAGCCCACGGAGGCCAGTGCTGACCAG
CTGCCCTCGCCCAGCCAGCTGCGGGAGAAGATCATCATCAAGCATAAGAAGCTGGGCCCC
CGAGGCGATGTGGATGTCAACATGGAGGACAAGAAGGACGAACACAAGCAACAGGGGGAG
CTGTACATGTGGGATTCCATTGACCAGAAATGGACTCGGCACTACTGCGCCATTGCTGAT
GCCAAGCTGTCCTTCAGTGATGACATTGAACAGACTATGGAGGAGGAAGTGCCCCAGGAT
ATACCCCCTACAGAACTACATTTTGGGGAGAAATGGTTCCACAAGAAGGTGGAGAAGAGG
ACGAGTGCCGAGAAGTTGCTGCAGGAATACTGCATGGAGACGGGGGGCAAGGATGGCACC
TTCCTGGTTCGGGAGAGCGAGACCTTCCCCAATGACTACACCCTGTCCTTCTGGCGGTCA
GGCCGGGTCCAGCACTGCCGGATCCGCTCCACCATGGAGGGCGGGACCCTGAAATACTAC
TTGACTGACAACCTGAGGTTCAGGAGGATGTATGCCCTCATCCAGCACTACCGCGAGACG
CACCTGCCGTGCGCCGAGTTCGAGCTGCGGCTCACGGACCCTGTGCCCAACCCCAACCCC
CACGAGTCCAAGCCGTGGTACTATGACAGCCTGAGCCGCGGAGAGGCAGAGGACATGCTG
ATGAGGATTCCCCGGGACGGGGCCTTCCTGATCCGGAAGCGAGAGGGGAGCGACTCCTAT
GCCATCACCTTCAGGGCTAGGGGCAAGGTAAAGCATTGTCGCATCAACCGGGACGGCCGG
CACTTTGTGCTGGGGACCTCCGCCTATTTTGAGAGTCTGGTGGAGCTCGTCAGTTACTAC
GAGAAGCATTCACTCTACCGAAAGATGAGACTGCGCTACCCCGTGACCCCCGAGCTCCTG
GAGCGCTACAATACGGAAAGAGATATAAACTCCCTCTACGACGTCAGCAGAATGTATGTG
GATCCCAGTGAAATCAATCCGTCCATGCCTCAGAGAACCGTGAAAGCTCTGTATGACTAC
AAAGCCAAGCGAAGCGATGAGCTGAGCTTCTGCCGTGGTGCCCTCATCCACAATGTCTCC
AAGGAGCCCGGGGGCTGGTGGAAAGGAGACTATGGAACCAGGATCCAGCAGTACTTCCCA
TCCAACTACGTCGAGGACATCTCAACTGCAGACTTCGAGGAGCTAGAAAAGCAGATTATT
GAAGACAATCCCTTAGGGTCTCTTTGCAGAGGAATATTGGACCTCAATACCTATAACGTC
GTGAAAGCCCCTCAGGGAAAAAACCAGAAGTCCTTTGTCTTCATCCTGGAGCCCAAGGAG
CAGGGCGATCCTCCGGTGGAGTTTGCCACAGACAGGGTGGAGGAGCTCTTTGAGTGGTTT
CAGAGCATCCGAGAGATCACGTGGAAGATTGACAGCAAGGAGAACAACATGAAGTACTGG
GAGAAGAACCAGTCCATCGCCATCGAGCTCTCTGACCTGGTTGTCTACTGCAAACCAACC
AGCAAAACCAAGGACAACTTAGAAAATCCTGACTTCCGAGAAATCCGCTCCTTTGTGGAG
ACGAAGGCTGACAGCATCATCAGACAGAAGCCCGTCGACCTCCTGAAGTACAATCAAAAG
GGCCTGACCCGCGTCTACCCAAAGGGACAAAGAGTTGACTCTTCAAACTACGACCCCTTC
CGCCTCTGGCTGTGCGGTTCTCAGATGGTGGCACTCAATTTCCAGACGGCAGATAAGTAC
ATGCAGATGAATCACGCATTGTTTTCTCTCAACGGGCGCACGGGCTACGTTCTGCAGCCT
GAGAGCATGAGGACAGAGAAATATGACCCGATGCCACCCGAGTCCCAGAGGAAGATCCTG
ATGACGCTGACAGTCAAGGTTCTCGGTGCTCGCCATCTCCCCAAACTTGGACGAAGTATT
GCCTGTCCCTTTGTAGAAGTGGAGATCTGTGGAGCCGAGTATGGCAACAACAAGTTCAAG
ACGACGGTTGTGAATGATAATGGCCTCAGCCCTATCTGGGCTCCAACACAGGAGAAGGTG
ACATTTGAAATTTATGACCCAAACCTGGCATTTCTGCGCTTTGTGGTTTATGAAGAAGAT
ATGTTCAGCGATCCCAACTTTCTTGCTCATGCCACTTACCCCATTAAAGCAGTCAAATCA
GGATTCAGGTCCGTTCCTCTGAAGAATGGGTACAGCGAGGACATAGAGCTGGCTTCCCTC
CTGGTTTTCTGTGAGATGCGGCCAGTCCTGGAGAGCGAAGAGGAACTTTACTCCTCCTGT
CGCCAGCTGAGGAGGCGGCAAGAAGAACTGAACAACCAGCTCTTTCTGTATGACACACAC
CAGAACTTGCGCAATGCCAACCGGGATGCCCTGGTTAAAGAGTTCAGTGTTAATGAGAAC
CACTCCAGCTGTACCAGGAGAAATGCAACAAGAGGTTAA
Enzyme 21 GenBank Gene ID X14034 Link Image
Enzyme 21 GeneCard ID PLCG2 Link Image
Enzyme 21 GenAtlas ID PLCG2 Link Image
Enzyme 21 HGNC ID HGNC:9066 Link Image
Enzyme 21 Chromosome Location 16
Enzyme 21 Locus 16q24.1
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 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. 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]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5465
Enzyme 22 Name Diacylglycerol kinase alpha
Enzyme 22 Synonyms
  1. Diglyceride kinase alpha
  2. DGK-alpha
  3. DAG kinase alpha
  4. 80 kDa diacylglycerol kinase
Enzyme 22 Gene Name DGKA
Enzyme 22 Protein Sequence >Diacylglycerol kinase alpha 
MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAKYVQGDAIGYEGFQQFLKIY
LEVDNVPRHLSLALFQSFETGHCLNETNVTKDVVCLNDVSCYFSLLEGGRPEDKLEFTFK
LYDTDRNGILDSSEVDKIILQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSQAEW
VRAGATTVPLLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKY
TVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLTGLHC
VWCHLEIHDDCLQAVGHECDCGLLRDHILPPSSIYPSVLASGPDRKNSKTSQKTMDDLNL
STSEALRIDPVPNTHPLLVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRL
FKDVPDSRILVCGGDGTVGWILETIDKANLPVLPPVAVLPLGTGNDLARCLRWGGGYEGQ
NLAKILKDLEMSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIM
REKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVL
NIPSMHGGSNLWGDTRRPHGDIYGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLE
GAIEMGQIYTKLKNAGRRLAKCSEITFHTTKTLPMQIDVEPWMQTPCTIKITHKNQMPML
MGPPPRSTNFFGFLS
Enzyme 22 Number of Residues 735
Enzyme 22 Molecular Weight 82673
Enzyme 22 Theoretical pI 6.71
Enzyme 22 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • diacylglycerol kinase activity
  • ion binding
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • intracellular signaling cascade
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 22 General Function Not Available
Enzyme 22 Specific Function Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity
Enzyme 22 Pathways
Enzyme 22 Reactions
  • ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 30823 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID P23743 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name DGKA_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 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 22 GenBank Gene ID X62535 Link Image
Enzyme 22 GeneCard ID DGKA Link Image
Enzyme 22 GenAtlas ID DGKA Link Image
Enzyme 22 HGNC ID HGNC:2849 Link Image
Enzyme 22 Chromosome Location 12
Enzyme 22 Locus 12q13.3
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 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. 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]
  3. 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]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5476
Enzyme 23 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma 1
Enzyme 23 Synonyms
  1. Phosphoinositide phospholipase C
  2. PLC-gamma-1
  3. Phospholipase C-gamma-1
  4. PLC-II
  5. PLC-148
Enzyme 23 Gene Name PLCG1
Enzyme 23 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 23 Number of Residues 1290
Enzyme 23 Molecular Weight 148534
Enzyme 23 Theoretical pI 5.91
Enzyme 23 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphodiesterase activity
  • ion binding
  • lipase activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • signal transduction
Component
—
Enzyme 23 General Function Not Available
Enzyme 23 Specific Function PLC-gamma is a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase
Enzyme 23 Pathways
Enzyme 23 Reactions
  • 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 190038 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID P19174 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name PLCG1_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 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 23 GenBank Gene ID M34667 Link Image
Enzyme 23 GeneCard ID PLCG1 Link Image
Enzyme 23 GenAtlas ID PLCG1 Link Image
Enzyme 23 HGNC ID HGNC:9065 Link Image
Enzyme 23 Chromosome Location Not Available
Enzyme 23 Locus Not Available
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 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. 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]
  4. 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]
  5. 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 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 5479
Enzyme 24 Name 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta 1
Enzyme 24 Synonyms
  1. Phosphoinositide phospholipase C
  2. PLC-delta-1
  3. Phospholipase C-delta-1
  4. PLC-III
Enzyme 24 Gene Name PLCD1
Enzyme 24 Protein Sequence >1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta 1 
MDSGRDFLTLHGLQDDEDLQALLKGSQLLKVKSSSWRRERFYKLQEDCKTIWQESRKVMR
TPESQLFSIEDIQEVRMGHRTEGLEKFARDVPEDRCFSIVFKDQRNTLDLIAPSPADAQH
WVLGLHKIIHHSGSMDQRQKLQHWIHSCLRKADKNKDNKMSFKELQNFLKELNIQVDDSY
ARKIFRECDHSQTDSLEDEEIEAFYKMLTQRVEIDRTFAEAAGPGETLSVDQLVTFLQHQ
QREEAAGPALALSLIERYEPSETTKAQRQMTKDGFLMYLLSADGSAFSLAHRRVYQDMGQ
PLSHYLVSSSHNTYLLEDQLAGPSSTEAYIRALCKGCRCLELDCWDGPNQEPIIYHGYTF
TSKILFCDVLRAIRDYAFKASPYPVILSLENHCTLEQQRVMARHLHAILGPMLLNRPLDG
VTNSLPSPEQLKGKILLKGKKLGGLLPPGGEGGPEATVVSDEDEAAEMEDEAVRSRVQHK
PKEDKLRLAQELSDMVIYCKSVHFGGFSSPGTPGQAFYEMASFSENRALRLLQESGNGFV
RHNVGHLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYQDRFQDNGACG
YVLKPAFLRDPNGTFNPRALAQGPWWARKRLNIRVISGQQLPKVNKNKNSIVDPKVTVEI
HGVSRDVASRQTAVITNNGFNPWWDTEFAFEVVVPDLALIRFLVEDYDASSKNDFIGQST
IPLNSLKQGYRHVHLMSKNGDQHPSATLFVKISLQD
Enzyme 24 Number of Residues 756
Enzyme 24 Molecular Weight 85764
Enzyme 24 Theoretical pI 6.61
Enzyme 24 GO Classification
Function
  • binding
  • calcium ion binding
  • carboxylic ester hydrolase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphodiesterase activity
  • ion binding
  • lipase activity
  • phosphoinositide phospholipase C activity
  • phospholipase C activity
  • phospholipase activity
  • phosphoric diester hydrolase activity
  • phosphoric ester hydrolase activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • signal transduction
Component
—
Enzyme 24 General Function Not Available
Enzyme 24 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 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 483920 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID P51178 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name PLCD1_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >2271 bp 
ATGGACTCGGGCCGGGACTTCCTGACCCTGCACGGCCTACAGGATGATGAGGATCTACAG
GCGCTGCTGAAGGGCAGCCAGCTCCTGAAGGTGAAGTCCAGCTCATGGAGGAGAGAGCGG
TTCTACAAGTTGCAGGAGGACTGCAAGACCATCTGGCAGGAGTCCCGCAAGGTCATGCGG
ACCCCGGAGTCCCAGCTGTTCTCCATCGAGGACATTCAGGAGGTGCGAATGGGGCACCGC
ACGGAGGGTCTGGAGAAGTTCGCCCGTGATGTGCCCGAGGACCGCTGCTTCTCCATTGTC
TTCAAGGACCAGCGCAATACACTAGACCTCATCGCCCCATCGCCAGCTGATGCCCAGCAC
TGGGTGCTGGGGCTGCACAAGATCATCCACCACTCAGGCTCCATGGACCAGCGTCAGAAG
CTACAGCACTGGATTCACTCCTGCTTGCGAAAAGCTGACAAAAACAAGGACAACAAGATG
AGCTTCAAGGAGCTGCAGAACTTCCTGAAGGAGCTCAACATCCAGGTGGACGACAGCTAT
GCCCGGAAGATCTTCAGGGAGTGTGACCACTCCCAGACAGACTCCCTGGAGGACGAGGAG
ATTGAGGCCTTCTACAAGATGCTGACCCAGCGGGTGGAGATCGACCGCACCTTCGCCGAG
GCCGCGGGCCCAGGGGAGACTCTGTCGGTGGATCAGTTAGTGACGTTCCTGCAGCACCAG
CAGCGGGAGGAGGCGGCAGGGCCTGCGCTGGCCCTCTCCCTCATTGAGCGCTACGAGCCC
AGCGAGACTACCAAGGCGCAGCGGCAGATGACCAAGGACGGCTTCCTCATGTACTTACTG
TCGGCTGACGGCAGCGCCTTCAGCCTGGCACACCGCCGTGTCTACCAGGACATGGGCCAG
CCACTTAGCCACTACCTGGTGTCCTCTTCACACAACACCTACCTGCTGGAGGACCAGCTA
GCCGGGCCCAGCAGCACTGAAGCCTACATCCGGGCACTGTGCAAAGGCTGCCGATGCCTG
GAGCTTGACTGCTGGGACGGGCCCAACCAGGAACCAATCATCTACCACGGCTATACTTTC
ACTTCCAAGATCCTCTTCTGCGATGTGCTCAGGGCCATCCGGGACTATGCCTTCAAGGCG
TCCCCCTACCCTGTCATCCTATCCCTGGAGAACCACTGCACACTGGAGCAGCAGCGCGTG
ATGGCGCGGCACCTGCATGCCATCCTGGGCCCCATGCTGTTGAACCGACCACTGGATGGG
GTCACCAACAGCCTGCCCTCCCCTGAGCAACTGAAGGGGAAGATCCTGCTGAAGGGGAAG
AAGCTCGGGGGGCTCCTCCCCCCTGGAGGGGAGGGTGGCCCTGAGGCCACTGTGGTGTCA
GACGAAGACGAGGCTGCTGAGATGGAGGATGAGGCAGTGAGGAGCCGTGTGCAGCACAAG
CCCAAGGAGGACAAGCTCAGGCTAGCACAGGAGCTCTCTGACATGGTCATTTACTGCAAG
AGTGTCCACTTTGGGGGCTTCTCCAGTCCTGGCACCCCTGGACAGGCCTTCTACGAGATG
GCGTCCTTCTCTGAGAACCGTGCCCTTCGACTGCTCCAAGAATCAGGAAACGGCTTTGTC
CGCCACAACGTGGGGCACCTGAGCAGAATATACCCGGCTGGATGGAGAACAGACTCCTCC
AACTACAGCCCCGTGGAGATGTGGAATGGGGGCTGCCAGATCGTGGCCCTGAATTTCCAG
ACACCTGGGCCAGAGATGGACGTGTACCAGGACCGCTTCCAGGACAACGGGGCCTGTGGG
TACGTGCTGAAGCCCGCCTTCCTGCGAGACCCCAACGGCACCTTTAACCCCCGCGCCCTG
GCTCAGGGGCCCTGGTGGGCACGGAAGCGGCTCAACATCAGGGTCATTTCGGGGCAGCAG
CTGCCAAAAGTCAACAAGAATAAGAATTCAATTGTGGACCCCAAAGTGACAGTGGAGATC
CATGGCGTGAGCCGGGACGTGGCCAGCCGCCAGACTGCTGTCATCACCAACAATGGTTTC
AACCCATGGTGGGACACGGAGTTTGCGTTTGAGGTAGTTGTGCCTGACCTTGCCCTCATC
CGCTTCTTGGTGGAAGATTATGATGCCTCCTCCAAGAATGACTTCATTGGCCAGAGTACC
ATCCCCTTGAACAGCCTCAAGCAAGGATACCGCCATGTCCACCTCATGTCTAAGAACGGG
GACCAGCATCCATCAGCCACCCTCTTTGTGAAGATCTCCCTCCAGGACTAG
Enzyme 24 GenBank Gene ID U09117 Link Image
Enzyme 24 GeneCard ID PLCD1 Link Image
Enzyme 24 GenAtlas ID PLCD1 Link Image
Enzyme 24 HGNC ID HGNC:9060 Link Image
Enzyme 24 Chromosome Location 3
Enzyme 24 Locus 3p22-p21.3
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 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]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 5508
Enzyme 25 Name Thyroid peroxidase precursor
Enzyme 25 Synonyms
  1. TPO
Enzyme 25 Gene Name TPO
Enzyme 25 Protein Sequence >Thyroid peroxidase precursor 
MRALAVLSVTLVMACTEAFFPFISRGKELLWGKPEESRVSSVLEESKRLVDTAMYATMQR
NLKKRGILSPAQLLSFSKLPEPTSGVIARAAEIMETSIQAMKRKVNLKTQQSQHPTDALS
EDLLSIIANMSGCLPYMLPPKCPNTCLANKYRPITGACNNRDHPRWGASNTALARWLPPV
YEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHD
IAFTPQSTSKAAFGGGADCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGD
QGALFGNLSTANPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAEGLLRVHARLRDSG
RAYLPFVPPRAPAACAPEPGIPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAA
LKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPT
VSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIR
GLLARPAKLQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGL
PRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQ
MKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFES
CDSIPGMNLEAWRETFPQDDKCGFPESVENGDFVHCEESGRRVLVYSCRHGYELQGREQL
TCTQEGWDFQPPLCKDVNECADGAHPPCHASARCRNTKGGFQCLCADPYELGDDGRTCVD
SGRLPRATWISMSLAALLIGGFAGLTSTVICRWTRTGTKSTLPISETGGGTPELRCGKHQ
AVGTSPQRAAAQDSEQESAGMEGRDTHRLPRAL
Enzyme 25 Number of Residues 933
Enzyme 25 Molecular Weight 102932
Enzyme 25 Theoretical pI 6.75
Enzyme 25 GO Classification
Function
  • antioxidant activity
  • binding
  • calcium ion binding
  • cation binding
  • ion binding
  • peroxidase activity
Process
  • cellular metabolism
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
—
Enzyme 25 General Function Not Available
Enzyme 25 Specific Function Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4)
Enzyme 25 Pathways
Enzyme 25 Reactions
  • iodide + H2O2 = iodine + 2 H2O
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • 1-14
Enzyme 25 Transmembrane Regions
  • 847-871
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 339867 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID P07202 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name PERT_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 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 25 GenBank Gene ID J02969 Link Image
Enzyme 25 GeneCard ID TPO Link Image
Enzyme 25 GenAtlas ID TPO Link Image
Enzyme 25 HGNC ID HGNC:12015 Link Image
Enzyme 25 Chromosome Location 2
Enzyme 25 Locus 2p25
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 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. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. 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]
  17. 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]
  18. 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]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 5511
Enzyme 26 Name Lactoperoxidase precursor
Enzyme 26 Synonyms
  1. LPO
  2. Salivary peroxidase
  3. SPO
Enzyme 26 Gene Name LPO
Enzyme 26 Protein Sequence >Lactoperoxidase precursor 
MRVLLHLPALLASLILLQAAASTTRAQTTRTSAISDTVSQAKVQVNKAFLDSRTRLKTAM
SSETPTSRQLSEYLKHAKGRTRTAIRNGQVWEESLKRLRQKASLTNVTDPSLDLTSLSLE
VGCGAPAPVVRCDPCSPYRTITGDCNNRRKPALGAANRALARWLPAEYEDGLSLPFGWTP
GKTRNGFPLPLAREVSNKIVGYLNEEGVLDQNRSLLFMQWGQIVDHDLDFAPDTELGSSE
YSKAQCDEYCIQGDNCFPIMFPPNDPKAGTQGKCMPFFRAGFVCPTPPYKSLAREQINAL
TSFLDASFVYSSEPSLASRLRNLSSPLGLMAVNQEVSDHGLPYLPYDSKKPSPCEFINTT
ARVPCFLAGDSRASEHILLATSHTLFLREHNRLARELKRLNPQWDGEKLYQEARKILGAF
VQIITFRDYLPILLGDHMQKWIPPYQGYSESVDPRISNVFTFAFRFGHLEVPSSMFRLDE
NYQPWGPEPELPLHTLFFNTWRMVKDGGIDPLVRGLLAKKSKLMKQNKMMTGELRNKLFQ
PTHRIHGFDLAAINTQRCRDHGQPGYNSWRAFCDLSQPQTLEELNTVLKSKMLAKKLLGL
YGTPDNIDIWIGAIAEPLVERGRVGPLLACLLGKQFQQIRDGDRFWWENPGVFTNEQKDS
LQKMSFSRLVCDNTRITKVPRDPFWANSYPYDFVDCSAIDKLDLSPWASVKN
Enzyme 26 Number of Residues 712
Enzyme 26 Molecular Weight 80289
Enzyme 26 Theoretical pI 8.76
Enzyme 26 GO Classification
Function
  • antioxidant activity
  • peroxidase activity
Process
  • cellular metabolism
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
—
Enzyme 26 General Function Not Available
Enzyme 26 Specific Function Donor + H(2)O(2) = oxidized donor + 2 H(2)O
Enzyme 26 Pathways
Enzyme 26 Reactions
  • donor + H2O2 = oxidized donor + 2 H2O
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • 1-26
Enzyme 26 Transmembrane Regions Not Available
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 1209685 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P22079 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name PERL_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 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 26 GenBank Gene ID U39573 Link Image
Enzyme 26 GeneCard ID LPO Link Image
Enzyme 26 GenAtlas ID LPO Link Image
Enzyme 26 HGNC ID HGNC:6678 Link Image
Enzyme 26 Chromosome Location 17
Enzyme 26 Locus 17q23.1
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 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. 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]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 5514
Enzyme 27 Name Myeloperoxidase precursor
Enzyme 27 Synonyms
  1. MPO[Contains: 89 kDa myeloperoxidase
  2. 84 kDa myeloperoxidase
  3. Myeloperoxidase light chain
  4. Myeloperoxidase heavy chain]
Enzyme 27 Gene Name MPO
Enzyme 27 Protein Sequence >Myeloperoxidase precursor 
MGVPFFSSLRCMVDLGPCWAGGLTAEMKLLLALAGLLAILATPQPSEGAAPAVLGEVDTS
LVLSSMEEAKQLVDKAYKERRESIKQRLRSGSASPMELLSYFKQPVAATRTAVRAADYLH
VALDLLERKLRSLWRRPFNVTDVLTPAQLNVLSKSSGCAYQDVGVTCPEQDKYRTITGMC
NNRRSPTLGASNRAFVRWLPAEYEDGFSLPYGWTPGVKRNGFPVALARAVSNEIVRFPTD
QLTPDQERSLMFMQWGQLLDHDLDFTPEPAARASFVTGVNCETSCVQQPPCFPLKIPPND
PRIKNQADCIPFFRSCPACPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNMSNQL
GLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLL
REHNRLATELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPTYR
SYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLSRVFFASWRVVLE
GGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYN
AWRRFCGLPQPETVGQLGTVLRNLKLARKLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPL
LACIIGTQFRKLRDGDRFWWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMS
NSYPRDFVNCSTLPALNLASWREAS
Enzyme 27 Number of Residues 745
Enzyme 27 Molecular Weight 83870
Enzyme 27 Theoretical pI 9.14
Enzyme 27 GO Classification
Function
  • antioxidant activity
  • peroxidase activity
Process
  • cellular metabolism
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
—
Enzyme 27 General Function Not Available
Enzyme 27 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 27 Pathways
Enzyme 27 Reactions
  • donor + H2O2 = oxidized donor + 2 H2O
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 189040 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID P05164 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name PERM_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 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 27 GenBank Gene ID J02694 Link Image
Enzyme 27 GeneCard ID MPO Link Image
Enzyme 27 GenAtlas ID MPO Link Image
Enzyme 27 HGNC ID HGNC:7218 Link Image
Enzyme 27 Chromosome Location 17
Enzyme 27 Locus 17q23.1
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 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. 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]
  4. 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]
  5. 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]
  6. 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]
  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. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. 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]
  17. 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]
  18. 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]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 5517
Enzyme 28 Name Eosinophil peroxidase precursor
Enzyme 28 Synonyms
  1. EPO[Contains: Eosinophil peroxidase light chain
  2. Eosinophil peroxidase heavy chain]
Enzyme 28 Gene Name EPX
Enzyme 28 Protein Sequence >Eosinophil peroxidase precursor 
MHLLPALAGVLATLVLAQPCEGTDPASPGAVETSVLRDCIAEAKLLVDAAYNWTQKSIKQ
RLRSGSASPMDLLSYFKQPVAATRTVVRAADYMHVALGLLEEKLQPQRSGPFNVTDVLTE
PQLRLLSQASGCALRDQAERCSDKYRTITGRCNNKRRPLLGASNQALARWLPAEYEDGLS
LPFGWTPSRRRNGFLLPLVRAVSNQIVRFPNERLTSDRGRALMFMQWGQFIDHDLDFSPE
SPARVAFTAGVDCERTCAQLPPCFPIKIPPNDPRIKNQRDCIPFFRSAPSCPQNKNRVRN
QINALTSFVDASMVYGSEVSLSLRLRNRTNYLGLLAINQRFQDNGRALLPFDNLHDDPCL
LTNRSARIPCFLAGDTRSTETPKLAAMHTLFMREHNRLATELRRLNPRWNGDKLYNEARK
IMGAMVQIITYRDFLPLVLGKARARRTLGHYRGYCSNVDPRVANVFTLAFRFGHTMLQPF
MFRLDSQYRASAPNSHVPLSSAFFASWRIVYEGGIDPILRGLMATPAKLNRQDAMLVDEL
RDRLFRQVRRIGLDLAALNMQRSRDHGLPGYNAWRRFCGLSQPRNLAQLSRVLKNQDLAR
KFLNLYGTPDNIDIWIGAIAEPLLPGARVGPLLACLFENQFRRARDGDRFWWQKRGVFTK
RQRKALSRISLSRIICDNTGITTVSRDIFRANIYPRGFVNCSRIPRLNLSAWRGT
Enzyme 28 Number of Residues 715
Enzyme 28 Molecular Weight 81042
Enzyme 28 Theoretical pI 10.81
Enzyme 28 GO Classification
Function
  • antioxidant activity
  • peroxidase activity
Process
  • cellular metabolism
  • metabolism
  • oxygen and reactive oxygen species metabolism
  • physiological process
  • response to oxidative stress
Component
—
Enzyme 28 General Function Not Available
Enzyme 28 Specific Function Donor + H(2)O(2) = oxidized donor + 2 H(2)O
Enzyme 28 Pathways
Enzyme 28 Reactions
  • donor + H2O2 = oxidized donor + 2 H2O
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • 1-17
Enzyme 28 Transmembrane Regions Not Available
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 182146 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID P11678 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name PERE_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 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 28 GenBank Gene ID M29913 Link Image
Enzyme 28 GeneCard ID EPX Link Image
Enzyme 28 GenAtlas ID EPX Link Image
Enzyme 28 HGNC ID HGNC:3423 Link Image
Enzyme 28 Chromosome Location 17
Enzyme 28 Locus 17q23.1
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 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. 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]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 5551
Enzyme 29 Name Arylsulfatase D precursor
Enzyme 29 Synonyms
  1. ASD
Enzyme 29 Gene Name ARSD
Enzyme 29 Protein Sequence >Arylsulfatase D precursor 
MRSAARRGRAAPAARDSLPVLLFLCLLLKTCEPKTANAFKPNILLIMADDLGTGDLGCYG
NNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRALQWNA
GSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHHPLNHGFDYFYGMPFTL
TNDCDPGRPPEVDAALRAQLWGYTQFLALGILTLAAGQTCGFFSVSARAVTGMAGVGCLF
FISWYSSFGFVRRWNCILMRNHDVTEQPMVLEKTASLMLKEAVSYIERHKHGPFLLFLSL
LHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYFTSDHGGH
LEARDGHSQLGGWNGIYKGGKGMGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPT
VVQLVGGEVPQDRVIDGHSLVPLLQGAEARSAHEFLFHYCGQHLHAARWHQKDSGSVWKV
HYTTPQFHPEERGLLTAEASAHAEWGGVTHHRPPLLFDLSRDPSEARPLTPDSEPLYHAV
IARVGAAVSEHRQTLSPVPQQFSMSNILWKPWLQPCCGHFPFCSCHEDGDGTP
Enzyme 29 Number of Residues 593
Enzyme 29 Molecular Weight 65072
Enzyme 29 Theoretical pI 7.10
Enzyme 29 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • sulfuric ester hydrolase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 29 General Function Inorganic ion transport and metabolism
Enzyme 29 Specific Function Not Available
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions Not Available
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • 1-33
Enzyme 29 Transmembrane Regions
  • 206-225
  • 229-251
  • 292-314
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 791002 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID P51689 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name ARSD_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 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 29 GenBank Gene ID X83572 Link Image
Enzyme 29 GeneCard ID ARSD Link Image
Enzyme 29 GenAtlas ID ARSD Link Image
Enzyme 29 HGNC ID HGNC:717 Link Image
Enzyme 29 Chromosome Location X
Enzyme 29 Locus Xp22.3
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 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]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 5557
Enzyme 30 Name Arylsulfatase B precursor
Enzyme 30 Synonyms
  1. ASB
  2. N-acetylgalactosamine- 4-sulfatase
  3. G4S
Enzyme 30 Gene Name ARSB
Enzyme 30 Protein Sequence >Arylsulfatase B precursor 
MGPRGAASLPRGPGPRRLLLPVVLPLLLLLLLAPPGSGAGASRPPHLVFLLADDLGWNDV
GFHGSRIRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPS
CVPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYSHER
CTLIDALNVTRCALDFRDGEEVATGYKNMYSTNIFTKRAIALITNHPPEKPLFLYLALQS
VHEPLQVPEEYLKPYDFIQDKNRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTD
NGGQTLAGGNNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELIHISDWLPTLVKL
ARGHTNGTKPLDGFDVWKTISEGSPSPRIELLHNIDPNFVDSSPCPRNSMAPAKDDSSLP
EYSAFNTSVHAAIRHGNWKLLTGYPGCGYWFPPPSQYNVSEIPSSDPPTKTLWLFDIDRD
PEERHDLSREYPHIVTKLLSRLQFYHKHSVPVYFPAQDPRCDPKATGVWGPWM
Enzyme 30 Number of Residues 533
Enzyme 30 Molecular Weight 59688
Enzyme 30 Theoretical pI 8.31
Enzyme 30 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • sulfuric ester hydrolase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 30 General Function Inorganic ion transport and metabolism
Enzyme 30 Specific Function Hydrolysis of the 4-sulfate groups of the N- acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate
Enzyme 30 Pathways
Enzyme 30 Reactions
  • Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • 1-36
Enzyme 30 Transmembrane Regions Not Available
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 179077 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID P15848 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name ARSB_HUMAN Link Image
Enzyme 30 PDB ID 1FSU Link Image
Enzyme 30 PDB File Show
Enzyme 30 3D Structure
Enzyme 30 Cellular Location Not Available
Enzyme 30 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 30 GenBank Gene ID J05225 Link Image
Enzyme 30 GeneCard ID ARSB Link Image
Enzyme 30 GenAtlas ID ARSB Link Image
Enzyme 30 HGNC ID HGNC:714 Link Image
Enzyme 30 Chromosome Location 5
Enzyme 30 Locus 5p11-q13|5q11-q13
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 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. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. 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]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 5560
Enzyme 31 Name Arylsulfatase E precursor
Enzyme 31 Synonyms
  1. ASE
Enzyme 31 Gene Name ARSE
Enzyme 31 Protein Sequence >Arylsulfatase E precursor 
MLHLHHSCLCFRSWLPAMLAVLLSLAPSASSDISASRPNILLLMADDLGIGDIGCYGNNT
MRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTGASG
GLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDHFYGMPFSLMGD
CARWELSEKRVNLEQKLNFLFQVLALVALTLVAGKLTHLIPVSWMPVIWSALSAVLLLAS
SYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLILQEVASFLKRNKHGPFLLFVSFLHV
HIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLEN
QLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVR
LAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFV
TPVFQPEGAGACYGRKVCPCFGEKVVHHDPPLLFDLSRDPSETHILTPASEPVFYQVMER
VQQAVWEHQRTLSPVPLQLDRLGNIWRPWLQPCCGPFPLCWCLREDDPQ
Enzyme 31 Number of Residues 589
Enzyme 31 Molecular Weight 65670
Enzyme 31 Theoretical pI 6.96
Enzyme 31 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • sulfuric ester hydrolase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 31 General Function Inorganic ion transport and metabolism
Enzyme 31 Specific Function May be essential for the correct composition of cartilage and bone matrix during development. Has no activity toward steroid sulfates
Enzyme 31 Pathways Not Available
Enzyme 31 Reactions Not Available
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • 1-31
Enzyme 31 Transmembrane Regions
  • 200-222
  • 227-249
  • 289-311
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 791004 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID P51690 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name ARSE_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >1770 bp 
ATGTTACATCTGCACCATTCTTGTTTGTGTTTCAGGAGCTGGCTGCCAGCGATGCTCGCT
GTACTGCTAAGTTTGGCACCATCAGCTTCCAGCGACATTTCCGCCTCCCGACCGAACATC
CTTCTTCTGATGGCGGACGACCTTGGCATTGGGGACATTGGCTGCTATGGCAACAACACC
ATGAGGACTCCGAATATTGACCGCCTTGCAGAGGACGGCGTGAAGCTGACCCAACACATC
TCTGCCGCATCTTTGTGCACCCCAAGCAGAGCCGCCTTCCTCACGGGCAGATACCCTGTG
CGATCAGGGATGGTTTCCAGCATTGGTTACCGTGTTCTTCAGTGGACCGGAGCATCTGGA
GGTCTTCCAACAAATGAGACAACTTTTGCAAAAATACTGAAAGAGAAAGGCTATGCCACT
GGACTCATTGGAAAATGGCATCTGGGTCTCAACTGTGAGTCAGCCAGTGATCATTGCCAC
CACCCTCTCCATCATGGCTTTGAGCATTTCTACGGAATGCCTTTCTCCTTGATGGGTGAT
TGCGCCCGCTGGGAACTCTCAGAGAAGCGTGTCAACCTGGAACAAAAACTCAACTTCCTC
TTCCAAGTCCTGGCCTTGGTTGCCCTCACACTGGTAGCAGGGAAGCTCACACACCTGATA
CCCGTCTCGTGGATGCCGGTCATCTGGTCAGCCCTTTCGGCCGTCCTCCTCCTCGCAAGC
TCCTATTTTGTGGGTGCTCTGATTGTCCATGCCGATTGCTTTCTGATGAGAAACCACACC
ATCACGGAGCAGCCCATGTGCTTCCAAAGAACGACACCCCTTATTCTGCAGGAGGTTGCG
TCCTTTCTCAAAAGGAATAAGCATGGGCCTTTCCTCCTCTTTGTTTCCTTTCTACACGTT
CACATCCCTCTTATCACTATGGAGAACTTCCTCGGGAAGAGTCTCCACGGGCTGTATGGG
GACAACGTAGAGGAGATGGACTGGATGGTAGGACGGATCCTTGACACTTTGGACGTGGAG
GGTTTGAGCAACAGCACCCTCATTTATTTTACGTCGGATCACGGCGGTTCCCTAGAGAAT
CAACTTGGAAACACCCAGTATGGTGGCTGGAATGGAATTTATAAAGGTGGGAAGGGCATG
GGAGGATGGGAAGGTGGGATCCGCGTGCCCGGGATCTTCCGCTGGCCCGGGGTGCTCCCG
GCCGGCCGAGTGATTGGCGAGCCCACGAGTCTGATGGACGTGTTCCCCACCGTGGTCCGG
CTGGCGGGCGGCGAGGTGCCCCAGGACAGAGTGATTGACGGCCAAGACCTTCTGCCCTTG
CTCCTGGGGACAGCCCAACACTCAGACCACGAGTTCCTGATGCATTATTGTGAGAGGTTT
CTGCACGCAGCCAGGTGGCATCAACGGGACAGAGGAACAATGTGGAAAGTCCACTTTGTG
ACGCCTGTGTTCCAGCCAGAGGGAGCCGGTGCCTGCTATGGAAGAAAGGTCTGCCCGTGC
TTTGGGGAAAAAGTAGTCCACCACGATCCACCTTTGCTCTTTGACCTCTCAAGAGACCCT
TCTGAGACCCACATCCTCACACCAGCCTCAGAGCCCGTGTTCTATCAGGTGATGGAACGA
GTCCAGCAGGCGGTGTGGGAACACCAGCGGACACTCAGCCCAGTTCCTCTGCAGCTGGAC
AGGCTGGGCAACATCTGGAGACCGTGGCTGCAGCCCTGCTGTGGCCCGTTCCCCCTCTGC
TGGTGCCTTAGGGAAGATGACCCACAATAA
Enzyme 31 GenBank Gene ID X83573 Link Image
Enzyme 31 GeneCard ID ARSE Link Image
Enzyme 31 GenAtlas ID ARSE Link Image
Enzyme 31 HGNC ID HGNC:719 Link Image
Enzyme 31 Chromosome Location X
Enzyme 31 Locus Xp22.3
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 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. 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]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 5562
Enzyme 32 Name Annexin A3
Enzyme 32 Synonyms
  1. Annexin III
  2. Lipocortin III
  3. Placental anticoagulant protein III
  4. PAP-III
  5. 35-alpha calcimedin
  6. Inositol 1,2-cyclic phosphate 2-phosphohydrolase
Enzyme 32 Gene Name ANXA3
Enzyme 32 Protein Sequence >Annexin A3 
MASIWVGHRGTVRDYPDFSPSVDAEAIQKAIRGIGTDEKMLISILTERSNAQRQLIVKEY
QAAYGKELKDDLKGDLSGHFEHLMVALVTPPAVFDAKQLKKSMKGAGTNEDALIEILTTR
TSRQMKDISQAYYTVYKKSLGDDISSETSGDFRKALLTLADGRRDESLKVDEHLAKQDAQ
ILYKAGENRWGTDEDKFTEILCLRSFPQLKLTFDEYRNISQKDIVDSIKGELSGHFEDLL
LAIVNCVRNTPAFLAERLHRALKGIGTDEFTLNRIMVSRSEIDLLDIRTEFKKHYGYSLY
SAIKSDTSGDYEITLLKICGGDD
Enzyme 32 Number of Residues 323
Enzyme 32 Molecular Weight 36376
Enzyme 32 Theoretical pI 5.71
Enzyme 32 GO Classification
Function
  • binding
  • calcium ion binding
  • calcium-dependent phospholipid binding
  • cation binding
  • enzyme inhibitor activity
  • enzyme regulator activity
  • ion binding
  • lipid binding
  • phospholipase inhibitor activity
  • phospholipid binding
Process
—
Component
—
Enzyme 32 General Function Not Available
Enzyme 32 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 32 Pathways Not Available
Enzyme 32 Reactions Not Available
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 307115 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID P12429 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name ANXA3_HUMAN Link Image
Enzyme 32 PDB ID 1AII Link Image
Enzyme 32 PDB File Show
Enzyme 32 3D Structure
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >972 bp 
ATGGCATCTATCTGGGTTGGACACCGAGGAACAGTAAGAGATTATCCAGACTTTAGCCCA
TCAGTGGATGCTGAAGCTATTCAGAAAGCAATCAGAGGAATTGGAACTGATGAGAAAATG
CTCATCAGCATTCTGACTGAGAGGTCAAATGCACAGCGGCAGCTGATTGTTAAGGAATAT
CAAGCAGCATATGGAAAGGAGCTGAAAGATGACTTGAAGGGTGATCTCTCTGGCCACTTT
GAGCATCTCATGGTGGCCCTAGTGACTCCACCAGCAGTCTTTGATGCAAAGCAGCTAAAG
AAATCCATGAAGGGCGCGGGAACAAACGAAGATGCCTTGATTGAAATCTTAACTACCAGG
ACAAGCAGGCAAATGAAGGATATCTCTCAAGCCTATTATACAGTATACAAGAAGAGTCTT
GGAGATGACATTAGTTCCGAAACATCTGGTGACTTCCGGAAAGCTCTGTTGACTTTGGCA
GATGGCAGAAGAGATGAAAGTCTGAAAGTGGATGAGCATCTGGCCAAACAAGATGCCCAG
ATTCTCTATAAAGCTGGTGAGAACAGATGGGGCACGGATGAAGACAAATTCACTGAGATC
CTGTGTTTAAGGAGCTTTCCTCAATTAAAACTAACATTTGATGAATACAGAAATATCAGC
CAAAAGGACATTGTGGACAGCATAAAAGGAGAATTATCTGGGCATTTTGAAGACTTACTG
TTGGCCATAGTTAATTGTGTGAGGAACACGCCGGCCTTTTTAGCCGAAAGACTGCATCGA
GCCTTGAAGGGTATTGGAACTGATGAGTTTACTCTGAACCGAATAATGGTGTCCAGATCA
GAAATTGACCTTTTGGACATTCGAACAGAGTTCAAGAAGCATTATGGCTATTCCCTATAT
TCAGCAATTAAATCGGATACTTCTGGAGACTATGAAATCACACTCTTAAAAATCTGTGGT
GGAGATGACTGA
Enzyme 32 GenBank Gene ID M20560 Link Image
Enzyme 32 GeneCard ID ANXA3 Link Image
Enzyme 32 GenAtlas ID ANXA3 Link Image
Enzyme 32 HGNC ID HGNC:541 Link Image
Enzyme 32 Chromosome Location 4
Enzyme 32 Locus 4q13-q22
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 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. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 5597
Enzyme 33 Name Type I inositol-1,4,5-trisphosphate 5-phosphatase
Enzyme 33 Synonyms
  1. 5PTase
Enzyme 33 Gene Name INPP5A
Enzyme 33 Protein Sequence >Type I inositol-1,4,5-trisphosphate 5-phosphatase 
MAGKAAAPGTAVLLVTANVGSLFDDPENLQKNWLREFYQVVHTHKPHFMALHCQEFGGKN
YEASMSHVDKFVKELLSSDAMKEYNRARVYLDENYKSQEHFTALGSFYFLHESLKNIYQF
DFKAKKYRKVAGKEIYSDTLESTPMLEKEKFPQDYFPECKWSRKGFIRTRWCIADCAFDL
VNIHLFHDASNLVAWETSPSVYSGIRHKALGYVLDRIIDQRFEKVSYFVFGDFNFRLDSK
SVVETLCTKATMQTVRAADTNEVVKLIFRESDNDRKVMLQLEKKLFDYFNQEVFRDNNGT
ALLEFDKELSVFKDRLYELDISFPPSYPYSEDARQGEQYMNTRCPAWCDRILMSPSAKEL
VLRSESEEKVVTYDHIGPNVCMGDHKPVFLAFRIMPGAGKPHAHVHKCCVVQ
Enzyme 33 Number of Residues 412
Enzyme 33 Molecular Weight 47820
Enzyme 33 Theoretical pI 7.04
Enzyme 33 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • inositol or phosphatidylinositol phosphatase activity
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
—
Component
—
Enzyme 33 General Function Not Available
Enzyme 33 Specific Function Major isoenzyme hydrolyzing the calcium-mobilizing second messenger Ins(1,4,5)P3, this is a signal-terminating reaction
Enzyme 33 Pathways
Enzyme 33 Reactions
  • (1) D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate
  • (2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • 1-22
Enzyme 33 Transmembrane Regions Not Available
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 556769 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q14642 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name I5P1_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 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 33 GenBank Gene ID X77567 Link Image
Enzyme 33 GeneCard ID INPP5A Link Image
Enzyme 33 GenAtlas ID INPP5A Link Image
Enzyme 33 HGNC ID HGNC:6076 Link Image
Enzyme 33 Chromosome Location 10
Enzyme 33 Locus 10q26.3
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 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. 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 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 5627
Enzyme 34 Name Amiloride-sensitive amine oxidase [copper-containing] precursor
Enzyme 34 Synonyms
  1. Diamine oxidase
  2. DAO
  3. Amiloride-binding protein
  4. ABP
  5. Histaminase
  6. Kidney amine oxidase
  7. KAO
Enzyme 34 Gene Name ABP1
Enzyme 34 Protein Sequence >Amiloride-sensitive amine oxidase [copper-containing] precursor 
MPALGWAVAAILMLQTAMAEPSPGTLPRKAGVFSDLSNQELKAVHSFLWSKKELRLQPSS
TTTMAKNTVFLIEMLLPKKYHVLRFLDKGERHPVREARAVIFFGDQEHPNVTEFAVGPLP
GPCYMRALSPRPGYQSSWASRPISTAEYALLYHTLQEATKPLHQFFLNTTGFSFQDCHDR
CLAFTDVAPRGVASGQRRSWLIIQRYVEGYFLHPTGLELLVDHGSTDAGHWAVEQVWYNG
KFYGSPEELARKYADGEVDVVVLEDPLPGGKGHDSTEEPPLFSSHKPRGDFPSPIHVSGP
RLVQPHGPRFRLEGNAVLYGGWSFAFRLRSSSGLQVLNVHFGGERIAYEVSVQEAVALYG
GHTPAGMQTKYLDVGWGLGSVTHELAPGIDCPETATFLDTFHYYDADDPVHYPRALCLFE
MPTGVPLRRHFNSNFKGGFNFYAGLKGQVLVLRTTSTVYNYDYIWDFIFYPNGVMEAKMH
ATGYVHATFYTPEGLRHGTRLHTHLIGNIHTHLVHYRVDLDVAGTKNSFQTLQMKLENIT
NPWSPRHRVVQPTLEQTQYSWERQAAFRFKRKLPKYLLFTSPQENPWGHKRSYRLQIHSM
ADQVLPPGWQEEQAITWARYPLAVTKYRESELCSSSIYHQNDPWDPPVVFEQFLHNNENI
ENEDLVAWVTVGFLHIPHSEDIPNTATPGNSVGFLLRPFNFFPEDPSLASRDTVIVWPRD
NGPNYVQRWIPEDRDCSMPPPFSYNGTYRPV
Enzyme 34 Number of Residues 751
Enzyme 34 Molecular Weight 85342
Enzyme 34 Theoretical pI 7.01
Enzyme 34 GO Classification
Function
  • binding
  • cation binding
  • copper ion binding
  • ion binding
  • transition metal ion binding
Process
—
Component
—
Enzyme 34 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 34 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 34 Pathways
Enzyme 34 Reactions
  • RCH2NH2 + H2O + O2 = RCHO + ammonia + H2O2
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • 1-19
Enzyme 34 Transmembrane Regions Not Available
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 177960 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID P19801 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name ABP1_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >2142 bp 
ATGCCGGCCCTGGGCTGGGCCGTGGCTGCCATCCTGATGCTGCAGACGGCCATGGCGGAG
CCCTCCCCGGGGACTCTGCCCAGGAAGGCAGGGGTGTTTTCAGACCTAAGCAACCAAGAG
CTGAAGGCAGTGCACAGCTTCCTCTGGTCCAAGAAGGAGCTGAGGCTGCAGCCCTCCAGT
ACCACCACCATGGCCAAGAACACCGTGTTTCTCATCGAGATGCTGCTGCCCAAGAAGTAC
CATGTGCTGAGGTTTCTGGATAAAGGTGAAAGGCATCCTGTGCGGGAAGCCCGTGCCGTC
ATCTTCTTTGGTGACCAGGAGCATCCCAATGTCACCGAGTTTGCTGTGGGGCCCCTGCCA
GGGCCCTGCTACATGCGAGCACTGTCCCCCAGGCCTGGGTACCAGTCCTCCTGGGCATCG
AGGCCCATCTCCACAGCAGAGTATGCCCTCCTCTACCACACCCTGCAGGAAGCCACCAAG
CCCCTGCATCAGTTCTTCCTCAATACCACAGGCTTCTCATTCCAAGACTGCCATGACAGA
TGCCTGGCCTTCACCGATGTGGCCCCCCGGGGTGTGGCTTCTGGCCAGCGCCGCAGTTGG
CTTATCATACAGCGCTATGTAGAAGGCTACTTTCTGCACCCCACTGGGCTGGAGCTCCTC
GTGGATCATGGGAGCACAGATGCTGGGCACTGGGCCGTGGAGCAGGTGTGGTACAACGGG
AAGTTCTATGGGAGCCCAGAGGAACTGGCACGGAAGTATGCAGATGGAGAGGTGGACGTG
GTGGTCCTGGAGGACCGCTGCCTGGGGGCAAGGGGCATGACAGCACAGAGGAGCCGGCCC
TCTTCTCCTCCACAAGCCCCGCGGGACTTTCCCCAGCCCCATCCATGTGAGCGGCCCCCG
CTTGGTCCAGCCCCACGGCCCTCGCTTCAGGCTGGAGGGCAACGCTGTGCTCTACGGCGG
CTGGAGCTTTGCCTTCCGGTGCGCTCCTCCTCCGGGCTGCAGGTCCTGAACGTGCACTTC
GGCGGAGAGCGCATTGCCTATGAGGTCAGCGTGCAAGAGGCAGTGGCGCTGTATGGAGGA
CACACACCTGCAGGCATGCAGACCAAGTACCTCGATGTCGGCTGGGGCCTGGGCAGCGTC
ACTCATGAGTTAGCCCCCGGCATCGACTGCCCGGAGACCGCCACCTTCCTGGACACTTTC
CACTACTATGATGCCGATGACCCGGTCCATTATCCCCGAGCCCTCTGCCTCTTTGAAATG
CCCACAGGGGTGCCCCTTCGGCGGCACTTTAATTCCAACTTTAAAGGTGGCTTCAACTTC
TATGCAGGGCTGAAGGGCCAGGTGCTGGTGCTGCGGACAACTTCAACTGTCTACAATTAT
GATTACATTTGGGACTTTATCTTCTACCCCAACGGGGTGATGGAGGCCAAGATGCATGCC
ACTGGCTACGTCCACGCCACCTTCTACACCCCCGAGGGCTGCGCACGGCACTCGCCTGCA
CACCCACCTGATTGGCAACATACACACTCACTTGTGCACTACCGCGTAGACCTGGATGTG
GCAGGCACCAAGAACAGCTTCCAGACACTGCAGATGAAGCTAGAAAACATCACCAACCCC
TGGAGCCCGAGACACCGCGTGGTCCAGCCAACTCTGGAGCAGACGCAGTACTCCTGGGAG
CGCCAGGCGGCCTTCCGCTTCAAAAGGAGGCTGCCCAAGTACCTGCTCTTTACCAGCCCC
CAGGAGAACCCCTGGGGCCACAAGCGCAGCTACCGCCTGCAGATCCACTCCATGGCCGAC
CAGGTGCTGCCCCCAGGCTGGCAGGAGGAGCAGGCCATCACCTGGGCAAGGTACCCCCTG
GCAGTGACCAAGTACCGGGAGTCAGAGCTGTGCAGCAGCAGCATCTACCACCAGAACGAC
CCCTGGGACCCGCCCGTGGTCTTTGAGCAGTTTCTTCACAACAACGAGAACATTGAAAAT
GAGGACCTGGTGGCCTGGGTGACGGTGGGCTTCCTGCACATCCCCCACTCAGAGGACATT
CCCAACACAGCCACACCTGGGAACTCCGTGGGCTTCCTGCTCCGGCCATTCAACTTCTTC
CCAGAGGACCCCTCCCCTCCCTGGCATCCAGAGACACTGTGA
Enzyme 34 GenBank Gene ID M55602 Link Image
Enzyme 34 GeneCard ID ABP1 Link Image
Enzyme 34 GenAtlas ID ABP1 Link Image
Enzyme 34 HGNC ID HGNC:80 Link Image
Enzyme 34 Chromosome Location 7
Enzyme 34 Locus 7q34-q36
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 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. 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 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 5628
Enzyme 35 Name Glyoxylate reductase/hydroxypyruvate reductase
Enzyme 35 Synonyms Not Available
Enzyme 35 Gene Name GRHPR
Enzyme 35 Protein Sequence >Glyoxylate reductase/hydroxypyruvate reductase 
MRPVRLMKVFVTRRIPAEGRVALARAADCEVEQWDSDEPIPAKELERGVAGAHGLLCLLS
DHVDKRILDAAGANLKVISTMSVGIDHLALDEIKKRGIRVGYTPDVLTDTTAELAVSLLL
TTCRRLPEAIEEVKNGGWTSWKPLWLCGYGLTQSTVGIIGLGRIGQAIARRLKPFGVQRF
LYTGRQPRPEEAAEFQAEFVSTPELAAQSDFIVVACSLTPATEGLCNKDFFQKMKETAVF
INISRGDVVNQDDLYQALASGKIAAAGLDVTSPEPLPTNHPLLTLKNCVILPHIGSATHR
TRNTMSLLAANNLLAGLRGEPMPSELKL
Enzyme 35 Number of Residues 328
Enzyme 35 Molecular Weight 35669
Enzyme 35 Theoretical pI 7.44
Enzyme 35 GO Classification
Function
  • NAD binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor 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
  • L-serine biosynthesis
  • L-serine metabolism
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • metabolism
  • physiological process
  • serine family amino acid metabolism
Component
—
Enzyme 35 General Function Energy production and conversion
Enzyme 35 Specific Function Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities
Enzyme 35 Pathways
Enzyme 35 Reactions
  • glycolate + NADP+ = glyoxylate + NADPH + H+
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 6002730 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID Q9UBQ7 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name GRHPR_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >987 bp 
ATGAGACCGGTGCGACTCATGAAGGTGTTCGTCACCCGCAGGATACCCGCCGAGGGTAGG
GTCGCGCTCGCCCGGGCGGCAGACTGTGAGGTGGAGCAGTGGGACTCGGATGAGCCCATC
CCTGCCAAGGAGCTAGAGCGAGGTGTGGCGGGGGCCCACGGCCTGCTCTGCCTCCTCTCC
GACCACGTGGACAAGAGGATCCTGGATGCTGCAGGGGCCAATCTCAAAGTCATCAGCACC
ATGTCTGTGGGCATCGACCACTTGGCTTTGGATGAAATCAAGAAGCGTGGGATCCGAGTT
GGCTACACCCCAGATGTCCTGACAGATACCACCGCCGAACTCGCAGTCTCCCTGCTACTT
ACCACCTGCCGCCGGTTGCCGGAGGCCATCGAGGAAGTGAAGAATGGTGGCTGGACCTCG
TGGAAGCCCCTCTGGCTGTGTGGCTATGGACTCACGCAGAGCACTGTCGGCATCATCGGG
CTGGGGCGCATAGGCCAGGCCATTGCTCGGCGTCTGAAACCATTCGGTGTCCAGAGATTT
CTGTACACAGGGCGCCAGCCCAGGCCTGAGGAAGCAGCAGAATTCCAGGCAGAGTTTGTG
TCTACCCCTGAGCTGGCTGCCCAATCTGATTTCATCGTCGTGGCCTGCTCCTTAACACCT
GCAACCGAGGGACTCTGCAACAAGGACTTCTTCCAGAAGATGAAGGAAACAGCTGTGTTC
ATCAACATCAGCAGGGGCGACGTCGTAAACCAGGACGACCTGTACCAGGCCTTGGCCAGT
GGTAAGATTGCAGCTGCTGGACTGGATGTGACGAGCCCAGAACCACTGCCTACAAACCAC
CCTCTCCTGACCCTGAAGAACTGTGTGATTCTGCCCCACATTGGCAGTGCCACCCACAGA
ACCCGCAACACCATGTCCTTGTTGGCAGCTAACAACTTGCTGGCTGGCCTGAGAGGGGAG
CCGATGCCTAGTGAACTCAAGCTGTAG
Enzyme 35 GenBank Gene ID AF134895 Link Image
Enzyme 35 GeneCard ID GRHPR Link Image
Enzyme 35 GenAtlas ID GRHPR Link Image
Enzyme 35 HGNC ID HGNC:4570 Link Image
Enzyme 35 Chromosome Location 9
Enzyme 35 Locus 9q12
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 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. 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]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 5630
Enzyme 36 Name Membrane copper amine oxidase
Enzyme 36 Synonyms
  1. Semicarbazide-sensitive amine oxidase
  2. SSAO
  3. Vascular adhesion protein 1
  4. VAP-1
  5. HPAO
Enzyme 36 Gene Name AOC3
Enzyme 36 Protein Sequence >Membrane copper amine oxidase 
MNQKTILVLLILAVITIFALVCVLLVGRGGDGGEPSQLPHCPSVSPSAQPWTHPGQSQLF
ADLSREELTAVMRFLTQRLGPGLVDAAQARPSDNCVFSVELQLPPKAAALAHLDRGSPPP
AREALAIVFFGRQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLFQEYLDID
QMIFNRELPQASGLLHHCCFYKHRGRNLVTMTTAPRGLQSGDRATWFGLYYNISGAGFFL
HHVGLELLVNHKALDPARWTIQKVFYQGRYYDSLAQLEAQFEAGLVNVVLIPDNGTGGSW
SLKSPVPPGPAPPLQFYPQGPRFSVQGSRVASSLWTFSFGLGAFSGPRIFDVRFQGERLV
YEISLQEALAIYGGNSPAAMTTRYVDGGFGMGKYTTPLTRGVDCPYLATYVDWHFLLESQ
APKTIRDAFCVFEQNQGLPLRRHHSDLYSHYFGGLAETVLVVRSMSTLLNYDYVWDTVFH
PSGAIEIRFYATGYISSAFLFGATGKYGNQVSEHTLGTVHTHSAHFKVDLDVAGLENWVW
AEDMVFVPMAVPWSPEHQLQRLQVTRKLLEMEEQAAFLVGSATPRYLYLASNHSNKWGHP
RGYRIQMLSFAGEPLPQNSSMARGFSWERYQLAVTQRKEEEPSSSSVFNQNDPWAPTVDF
SDFINNETIAGKDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYNFFDEDPSFYSA
DSIYFRGDQDAGACEVNPLACLPQAAACAPDLPAFSHGGFSHN
Enzyme 36 Number of Residues 763
Enzyme 36 Molecular Weight 84623
Enzyme 36 Theoretical pI 6.51
Enzyme 36 GO Classification
Function
  • binding
  • cation binding
  • copper ion binding
  • ion binding
  • transition metal ion binding
Process
—
Component
—
Enzyme 36 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 36 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
Enzyme 36 Pathways
Enzyme 36 Reactions
  • RCH2NH2 + H2O + O2 = RCHO + ammonia + H2O2
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • 1-19
Enzyme 36 Transmembrane Regions Not Available
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 1399032 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q16853 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name AOC3_HUMAN Link Image
Enzyme 36 PDB ID 1PU4 Link Image
Enzyme 36 PDB File Show
Enzyme 36 3D Structure
Enzyme 36 Cellular Location Not Available
Enzyme 36 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 36 GenBank Gene ID U39447 Link Image
Enzyme 36 GeneCard ID AOC3 Link Image
Enzyme 36 GenAtlas ID AOC3 Link Image
Enzyme 36 HGNC ID HGNC:550 Link Image
Enzyme 36 Chromosome Location Not Available
Enzyme 36 Locus Not Available
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 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]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 5631
Enzyme 37 Name Retina-specific copper amine oxidase precursor
Enzyme 37 Synonyms
  1. RAO
  2. Amine oxidase [copper-containing]
Enzyme 37 Gene Name AOC2
Enzyme 37 Protein Sequence >Retina-specific copper amine oxidase precursor 
MHLKIVLAFLALSLITIFALAYVLLTSPGGSSQPPHCPSVSHRAQPWPHPGQSQLFADLS
REELTAVMRFLTQRLGPGLVDAAQAQPSDNCIFSVELQLPPKAAALAHLDRGSPPPAREA
LAIVLFGGQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLRAEFTQMWRHLK
EVELPKAPIFLSSTFNYNGSTLAAVHATPRGLRSGDRATWMALYHNISGVGLFLHPVGLE
LLLDHRALDPAHWTVQQVFYLGHYYADLGQLEREFKSGRLEVVRVPLPPPNGASSLRSRN
SPGPLPPLQFSPQGSQYSVQGNLVVSSLWSFTFGHGVFSGLRIFDVRFQGERIAYEVSVQ
ECVSIYGADSPKTMLTRYLDSSFGLGRNSRGLVRGVDCPYQATMVDIHILVGKGAVQLLP
GAVCVFEEAQGLPLRRHHNYLQNHFYGGLASSALVVRSVSSVGNYDYIWDFVLYPNGALE
GRVHATGYINTAFLKGGEEGLLFGNRVGERVLGTVHTHAFHFKLDLDVAGLKNWVVAEDV
VFKPVAAPWNPEHWLQRPQLTRQVLGKEDLTAFSLGSPLPRYLYLASNQTNAWGHQRGYR
IQIHSPLGIHIPLESDMERALSWGRYQLVVTQRKEEESQSSSIYHQNDIWTPTVTFADFI
NNETLLGEDLVAWVTASFLHIPHAEDIPNTVTLGNRVGFLLRPYNFFDEDPSIFSPGSVY
FEKGQDAGLCSINPVACLPDLAACVPDLPPFSYHGF
Enzyme 37 Number of Residues 756
Enzyme 37 Molecular Weight 83674
Enzyme 37 Theoretical pI 7.03
Enzyme 37 GO Classification
Function
  • binding
  • cation binding
  • copper ion binding
  • ion binding
  • transition metal ion binding
Process
—
Component
—
Enzyme 37 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 37 Specific Function May be a critical modulator of signal transmission in retina, possibly by degrading the biogenic amines dopamine, histamine, and putrescine
Enzyme 37 Pathways
  • Alkaloid biosynthesis II (map00960 Link Image)
  • Arginine and Proline Metabolism (map00330 Link Image)
  • Beta Alanine Metabolism (map00410 Link Image)
  • Glycine, Serine and Threonine Metabolism (map00260 Link Image)
  • Histidine Metabolism (map00340 Link Image)
  • Phenylalanine Metabolism (