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Human Metabolome Database Version 2.5

 

Showing metabocard for Water (HMDB02111)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-05-22 15:17:36
Update Date 2009-07-15 13:34:32
Accession Number HMDB02111
Secondary Accession Numbers Not Available
Common Name Water
Description Water is a chemical substance that is essential to all known forms of life. It appears colorless to the naked eye in small quantities, though it is actually slightly blue in color. It covers 71% of Earth's surface. Current estimates suggest that there are 1.4 billion cubic kilometers (330 million m3) of it available on Earth, and it exists in many forms. It appears mostly in the oceans (saltwater) and polar ice caps, but it is also present as clouds, rain water, rivers, freshwater aquifers, lakes, and sea ice. Water in these bodies perpetually moves through a cycle of evaporation, precipitation, and runoff to the sea. Clean water is essential to human life. In many parts of the world, it is in short supply. From a biological standpoint, water has many distinct properties that are critical for the proliferation of life that set it apart from other substances. It carries out this role by allowing organic compounds to react in ways that ultimately allow replication. All known forms of life depend on water. Water is vital both as a solvent in which many of the body's solutes dissolve and as an essential part of many metabolic processes within the body. Metabolism is the sum total of anabolism and catabolism. In anabolism, water is removed from molecules (through energy requiring enzymatic chemical reactions) in order to grow larger molecules (e.g. starches, triglycerides and proteins for storage of fuels and information). In catabolism, water is used to break bonds in order to generate smaller molecules (e.g. glucose, fatty acids and amino acids to be used for fuels for energy use or other purposes). Water is thus essential and central to these metabolic processes. Water is also central to photosynthesis and respiration. Photosynthetic cells use the sun's energy to split off water's hydrogen from oxygen. Hydrogen is combined with CO2 (absorbed from air or water) to form glucose and release oxygen. All living cells use such fuels and oxidize the hydrogen and carbon to capture the sun's energy and reform water and CO2 in the process (cellular respiration). Water is also central to acid-base neutrality and enzyme function. An acid, a hydrogen ion (H+, that is, a proton) donor, can be neutralized by a base, a proton acceptor such as hydroxide ion (OH-) to form water. Water is considered to be neutral, with a pH (the negative log of the hydrogen ion concentration) of 7. Acids have pH values less than 7 while bases have values greater than 7. Stomach acid (HCl) is useful to digestion. However, its corrosive effect on the esophagus during reflux can temporarily be neutralized by ingestion of a base such as aluminum hydroxide to produce the neutral molecules water and the salt aluminum chloride. Human biochemistry that involves enzymes usually performs optimally around a biologically neutral pH of 7.4. (Wikipedia)
Synonyms
  1. Dihydrogen oxide
  2. Steam
Chemical IUPAC Name water
Chemical Formula H2O
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Inorganic
Super Class
  • Inorganic compounds
Class
  • Inorganic Ions and Gases
Sub Class
  • Non metals
Family
  • Mammalian Metabolite
Species
—
Biofunction
  • Osmolyte, enzyme cofactor, signalling
Application
—
Source
  • Exogenous
Average Molecular Weight 18.015
Monoisotopic Molecular Weight 18.010559
Isomeric SMILES O
Canonical SMILES O
KEGG Compound ID C00001 Link Image
BioCyc ID Not Available
BiGG ID 33474 Link Image
Wikipedia Link Water Link Image
NuGOwiki Link HMDB02111 Link Image
Metagene Link HMDB02111 Link Image
METLIN ID 3194 Link Image
PubChem Compound 962 Link Image
PubChem Substance 3303 Link Image
ChEBI ID 15377 Link Image
CAS Registry Number 7732-18-5
InChI Identifier InChI=1/H2O/h1H2
Synthesis Reference Not Available
Melting Point (Experimental) 0 oC
Experimental Water Solubility 55.5 mol/L [Theoretical Calculation] Source: PhysProp
Predicted Water Solubility 1000 mg/mL at 25 oC [MEYLAN,WM et al. (1996)] Calculated using ALOGPS
Physiological Charge 0
State Liquid
Experimental LogP/Hydrophobicity -1.38 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity Not Available 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
  • Endoplasmic reticulum
  • Extracellular
  • Golgi apparatus
  • lysosome
  • mitochondria
  • nucleus
  • peroxisome
Biofluid Location
  • Amniotic Fluid
  • Aqueous Humour
  • Ascites Fluid
  • Blood
  • Breast Milk
  • Cerebrospinal Fluid
  • Lymph
  • Saliva
  • Sweat
  • Tears
  • Urine
Tissue Location
Tissue References
All Tissues —
Concentrations (Normal)
Biofluid Amniotic Fluid
Value 55,000,000 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Parsons DS: Salt and water absorption by the intestinal tract. Br Med Bull. 1967 Sep;23(3):252-7. [PubMed Link Image]
  • [No authors listed]Tissue electrolytes in dehydrated children. Nutr Rev. 1967 Jul;25(7):205-7. [PubMed Link Image]
  • Fishman RA: Cell volume, pumps, and neurologic function: brain's adaptation to osmotic stress. Res Publ Assoc Res Nerv Ment Dis. 1974;53:159-71. [PubMed Link Image]
Biofluid Aqueous Humour
Value 55,000,000 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Parsons DS: Salt and water absorption by the intestinal tract. Br Med Bull. 1967 Sep;23(3):252-7. [PubMed Link Image]
  • [No authors listed]Tissue electrolytes in dehydrated children. Nutr Rev. 1967 Jul;25(7):205-7. [PubMed Link Image]
  • Fishman RA: Cell volume, pumps, and neurologic function: brain's adaptation to osmotic stress. Res Publ Assoc Res Nerv Ment Dis. 1974;53:159-71. [PubMed Link Image]
Biofluid Ascites Fluid
Value 55,000,000 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Parsons DS: Salt and water absorption by the intestinal tract. Br Med Bull. 1967 Sep;23(3):252-7. [PubMed Link Image]
  • [No authors listed]Tissue electrolytes in dehydrated children. Nutr Rev. 1967 Jul;25(7):205-7. [PubMed Link Image]
  • Fishman RA: Cell volume, pumps, and neurologic function: brain's adaptation to osmotic stress. Res Publ Assoc Res Nerv Ment Dis. 1974;53:159-71. [PubMed Link Image]
Biofluid Blood
Value 55,000,000 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Ohira Y, Ito A, Ikawa S: Correction of water content and solute concentration in blood during hemoconcentration. J Appl Physiol. 1977 May;42(5):739-43. [PubMed Link Image]
  • Parsons DS: Salt and water absorption by the intestinal tract. Br Med Bull. 1967 Sep;23(3):252-7. [PubMed Link Image]
  • [No authors listed]Tissue electrolytes in dehydrated children. Nutr Rev. 1967 Jul;25(7):205-7. [PubMed Link Image]
  • Fishman RA: Cell volume, pumps, and neurologic function: brain's adaptation to osmotic stress. Res Publ Assoc Res Nerv Ment Dis. 1974;53:159-71. [PubMed Link Image]
Biofluid Breast Milk
Value 55,000,000 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Parsons DS: Salt and water absorption by the intestinal tract. Br Med Bull. 1967 Sep;23(3):252-7. [PubMed Link Image]
  • [No authors listed]Tissue electrolytes in dehydrated children. Nutr Rev. 1967 Jul;25(7):205-7. [PubMed Link Image]
  • Fishman RA: Cell volume, pumps, and neurologic function: brain's adaptation to osmotic stress. Res Publ Assoc Res Nerv Ment Dis. 1974;53:159-71. [PubMed Link Image]
Biofluid CSF
Value 55,000,000 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Parsons DS: Salt and water absorption by the intestinal tract. Br Med Bull. 1967 Sep;23(3):252-7. [PubMed Link Image]
  • [No authors listed]Tissue electrolytes in dehydrated children. Nutr Rev. 1967 Jul;25(7):205-7. [PubMed Link Image]
  • Fishman RA: Cell volume, pumps, and neurologic function: brain's adaptation to osmotic stress. Res Publ Assoc Res Nerv Ment Dis. 1974;53:159-71. [PubMed Link Image]
Biofluid Lymph
Value 55,000,000 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Parsons DS: Salt and water absorption by the intestinal tract. Br Med Bull. 1967 Sep;23(3):252-7. [PubMed Link Image]
  • [No authors listed]Tissue electrolytes in dehydrated children. Nutr Rev. 1967 Jul;25(7):205-7. [PubMed Link Image]
  • Fishman RA: Cell volume, pumps, and neurologic function: brain's adaptation to osmotic stress. Res Publ Assoc Res Nerv Ment Dis. 1974;53:159-71. [PubMed Link Image]
Biofluid Saliva
Value 55,000,000 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Parsons DS: Salt and water absorption by the intestinal tract. Br Med Bull. 1967 Sep;23(3):252-7. [PubMed Link Image]
  • [No authors listed]Tissue electrolytes in dehydrated children. Nutr Rev. 1967 Jul;25(7):205-7. [PubMed Link Image]
  • Fishman RA: Cell volume, pumps, and neurologic function: brain's adaptation to osmotic stress. Res Publ Assoc Res Nerv Ment Dis. 1974;53:159-71. [PubMed Link Image]
Biofluid Sweat
Value 55,000,000 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Parsons DS: Salt and water absorption by the intestinal tract. Br Med Bull. 1967 Sep;23(3):252-7. [PubMed Link Image]
  • [No authors listed]Tissue electrolytes in dehydrated children. Nutr Rev. 1967 Jul;25(7):205-7. [PubMed Link Image]
  • Fishman RA: Cell volume, pumps, and neurologic function: brain's adaptation to osmotic stress. Res Publ Assoc Res Nerv Ment Dis. 1974;53:159-71. [PubMed Link Image]
Biofluid Tears
Value 55,000,000 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Parsons DS: Salt and water absorption by the intestinal tract. Br Med Bull. 1967 Sep;23(3):252-7. [PubMed Link Image]
  • [No authors listed]Tissue electrolytes in dehydrated children. Nutr Rev. 1967 Jul;25(7):205-7. [PubMed Link Image]
  • Fishman RA: Cell volume, pumps, and neurologic function: brain's adaptation to osmotic stress. Res Publ Assoc Res Nerv Ment Dis. 1974;53:159-71. [PubMed Link Image]
Biofluid Urine
Value 55,000,000 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Parsons DS: Salt and water absorption by the intestinal tract. Br Med Bull. 1967 Sep;23(3):252-7. [PubMed Link Image]
  • [No authors listed]Tissue electrolytes in dehydrated children. Nutr Rev. 1967 Jul;25(7):205-7. [PubMed Link Image]
  • Fishman RA: Cell volume, pumps, and neurologic function: brain's adaptation to osmotic stress. Res Publ Assoc Res Nerv Ment Dis. 1974;53:159-71. [PubMed Link Image]
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Amino Sugar Metabolism SMP00045 Link Image map00520 Link Image
Ammonia Recycling SMP00009 Link Image map00910 Link Image
Arachidonic Acid Metabolism SMP00075 Link Image map00590 Link Image
Carnitine Synthesis SMP00465 Link Image
Catecholamine Biosynthesis SMP00012 Link Image map00350 Link Image
Citric Acid Cycle SMP00057 Link Image map00020 Link Image
D-Arginine and D-Ornithine Metabolism SMP00036 Link Image map00472 Link Image
Degradation of Superoxides SMP00468 Link Image
Ethanol Degradation SMP00449 Link Image
Folate Metabolism SMP00053 Link Image map00670 Link Image
Gluconeogenesis SMP00128 Link Image map00010 Link Image
Glucose-Alanine Cycle SMP00127 Link Image
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
Glycolysis SMP00040 Link Image map00010 Link Image
Homocysteine Degradation SMP00455 Link Image
Lactose Degradation SMP00457 Link Image
Mitochondrial Beta-Oxidation of Long Chain Saturated Fatty Acids SMP00482 Link Image
Mitochondrial Beta-Oxidation of Medium Chain Saturated Fatty Acids SMP00481 Link Image
Mitochondrial Beta-Oxidation of Short Chain Saturated Fatty Acids SMP00480 Link Image
Mitochondrial Electron Transport Chain SMP00355 Link Image map00190 Link Image
Phenylalanine and Tyrosine Metabolism SMP00008 Link Image map00360 Link Image
Plasmalogen Synthesis SMP00479 Link Image
Pterine Biosynthesis SMP00005 Link Image map00790 Link Image
Pyruvaldehyde Degradation SMP00459 Link Image
Spermidine and Spermine Biosynthesis SMP00445 Link Image
Transfer of Acetyl Groups into Mitochondria SMP00466 Link Image
Trehalose Degradation SMP00467 Link Image
Urea Cycle SMP00059 Link Image map00330 Link Image
General References
  1. Wikipedia Link Image
Metabolic Enzymes
  1. Cytosolic 5'-nucleotidase 1B
  2. Cytosolic 5'-nucleotidase 1A
  3. 5'(3')-deoxyribonucleotidase, cytosolic type
  4. 5'(3')-deoxyribonucleotidase, mitochondrial precursor
  5. Fatty acid synthase
  6. Hydroxymethylglutaryl-CoA synthase, mitochondrial precursor
  7. Citrate synthase, mitochondrial precursor
  8. Acyl-protein thioesterase 1
  9. Calcium-dependent phospholipase A2 precursor
  10. Group IIF secretory phospholipase A2 precursor
  11. Cytosolic phospholipase A2
  12. Phospholipase A2 precursor
  13. Group XIIB secretory phospholipase A2-like protein precursor
  14. Group 10 secretory phospholipase A2 precursor
  15. Group IIE secretory phospholipase A2 precursor
  16. Acyl-protein thioesterase 2
  17. Eosinophil lysophospholipase
  18. Group IID secretory phospholipase A2 precursor
  19. Phospholipase D2
  20. Ectonucleoside triphosphate diphosphohydrolase 1
  21. Soluble calcium-activated nucleotidase 1
  22. Tyrosinase precursor
  23. Alkaline phosphatase, placental type precursor
  24. Alkaline phosphatase, tissue-nonspecific isozyme precursor
  25. Tartrate-resistant acid phosphatase type 5 precursor
  26. Prostatic acid phosphatase precursor
  27. Alkaline phosphatase, placental-like precursor
  28. Ribonucleoside-diphosphate reductase large subunit
  29. Ribonucleoside-diphosphate reductase M2 subunit
  30. Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
  31. Aldehyde oxidase
  32. Lathosterol oxidase
  33. Dimethylaniline monooxygenase [N-oxide-forming] 5
  34. Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial precursor
  35. Acyl-coenzyme A oxidase 2, peroxisomal
  36. Dimethylaniline monooxygenase [N-oxide-forming] 4
  37. Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 precursor
  38. Amine oxidase [flavin-containing] A
  39. Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase
  40. Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
  41. Heme oxygenase 1
  42. Retinal dehydrogenase 1
  43. Dimethylglycine dehydrogenase, mitochondrial precursor
  44. Retinal dehydrogenase 2
  45. Glucosamine-6-phosphate isomerase
  46. Pancreatic triacylglycerol lipase precursor
  47. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 1
  48. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 4
  49. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 2
  50. Lysosomal acid lipase/cholesteryl ester hydrolase precursor
  51. Pancreatic lipase-related protein 1 precursor
  52. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma 2
  53. Lipid phosphate phosphohydrolase 2
  54. Adiponutrin
  55. Gastric triacylglycerol lipase precursor
  56. Lipid phosphate phosphohydrolase 1
  57. Pancreatic lipase-related protein 2 precursor
  58. Succinate semialdehyde dehydrogenase, mitochondrial precursor
  59. Dopamine beta-hydroxylase precursor
  60. Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
  61. Tyrosine 3-monooxygenase
  62. Thyroid peroxidase precursor
  63. Lactoperoxidase precursor
  64. Phenylalanine-4-hydroxylase
  65. Eosinophil peroxidase precursor
  66. Sucrase-isomaltase, intestinal [Contains: Sucrase
  67. 4-trimethylaminobutyraldehyde dehydrogenase
  68. Alpha-aminoadipic semialdehyde dehydrogenase
  69. Aldehyde dehydrogenase 1A3
  70. Aldehyde dehydrogenase, mitochondrial precursor
  71. Fatty aldehyde dehydrogenase
  72. Aldehyde dehydrogenase X, mitochondrial precursor
  73. Arginase-1
  74. Acyl-CoA desaturase
  75. Monoglyceride lipase
  76. Galactocerebrosidase precursor
  77. Arylsulfatase D precursor
  78. Sialidase-2
  79. Arylsulfatase A precursor
  80. Arylsulfatase B precursor
  81. Sialidase-4
  82. Arylsulfatase E precursor
  83. 6-phosphogluconolactonase
  84. GDH/6PGL endoplasmic bifunctional protein precursor [Includes: Glucose 1-dehydrogenase
  85. Carbamoyl-phosphate synthase [ammonia], mitochondrial precursor
  86. Type I inositol-1,4,5-trisphosphate 5-phosphatase
  87. Inositol polyphosphate 1-phosphatase
  88. Lactase-phlorizin hydrolase precursor
  89. Neutral alpha-glucosidase AB precursor
  90. Glycogen debranching enzyme
  91. Trehalase precursor
  92. Glucose-6-phosphatase
  93. GDP-mannose 4,6 dehydratase
  94. Enoyl-CoA hydratase, mitochondrial precursor
  95. Amiloride-sensitive amine oxidase [copper-containing] precursor
  96. Membrane copper amine oxidase
  97. Retina-specific copper amine oxidase precursor
  98. Cytochrome P450 4A11 precursor
  99. S-adenosylmethionine synthetase isoform type-1
  100. Inosine triphosphate pyrophosphatase
  101. Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial precursor
  102. Alpha-N-acetylgalactosaminidase precursor
  103. Cytochrome P450 11B1, mitochondrial precursor
  104. Aminopeptidase N
  105. Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1 precursor
  106. Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 precursor
  107. Tryptophan 5-hydroxylase 1
  108. Ferritin, mitochondrial precursor
  109. Tryptophan 5-hydroxylase 2
  110. Beta-Ala-His dipeptidase precursor
  111. Peroxisomal multifunctional enzyme type 2
  112. Steryl-sulfatase precursor
  113. Liver carboxylesterase 1 precursor
  114. Carboxylesterase 2 precursor
  115. Cytochrome P450 7A1
  116. Acetylcholinesterase precursor
  117. Cholinesterase precursor
  118. Platelet-activating factor acetylhydrolase IB subunit gamma
  119. Platelet-activating factor acetylhydrolase IB subunit beta
  120. Hormone-sensitive lipase
  121. Group 3 secretory phospholipase A2 precursor
  122. Acyloxyacyl hydrolase precursor
  123. Cystathionine gamma-lyase
  124. Cytidine deaminase
  125. Aldehyde dehydrogenase 3B2
  126. Dihydropyrimidinase
  127. Bile acid CoA:amino acid N-acyltransferase
  128. Acylphosphatase-2
  129. Aminoacylase-1
  130. Aspartoacylase
  131. Aspartoacylase-2
  132. Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
  133. Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
  134. High-affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A
  135. Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
  136. cGMP-inhibited 3',5'-cyclic phosphodiesterase B
  137. Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'
  138. Asparagine synthetase [glutamine-hydrolyzing]
  139. AMP deaminase 2
  140. cGMP-inhibited 3',5'-cyclic phosphodiesterase A
  141. Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
  142. cAMP-specific 3',5'-cyclic phosphodiesterase 4B
  143. Bis(5'-adenosyl)-triphosphatase
  144. High-affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A
  145. cGMP-dependent 3',5'-cyclic phosphodiesterase
  146. Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]
  147. Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
  148. High-affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B
  149. Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta precursor
  150. cAMP-specific 3',5'-cyclic phosphodiesterase 4D
  151. Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
  152. Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
  153. cAMP-specific 3',5'-cyclic phosphodiesterase 4A
  154. Selenide, water dikinase 1
  155. cGMP-specific 3',5'-cyclic phosphodiesterase
  156. AMP deaminase 1
  157. Selenide, water dikinase 2
  158. Putative adenosylhomocysteinase 3
  159. Putative adenosylhomocysteinase 2
  160. Adenosine deaminase
  161. Glutamate dehydrogenase 2, mitochondrial precursor
  162. Protein-arginine deiminase type-4
  163. Pyridoxine-5'-phosphate oxidase
  164. CTP synthase 1
  165. Protein-arginine deiminase type-3
  166. Glutaminase kidney isoform, mitochondrial precursor
  167. Protein-arginine deiminase type-2
  168. Glutamate dehydrogenase 1, mitochondrial precursor
  169. Protein-lysine 6-oxidase precursor
  170. Alpha-galactosidase A precursor
  171. Aconitate hydratase, mitochondrial precursor
  172. Iron-responsive element-binding protein 1
  173. Gamma-glutamyltranspeptidase 1 precursor
  174. NG,NG-dimethylarginine dimethylaminohydrolase 2
  175. Sphingomyelin phosphodiesterase precursor
  176. Alcohol dehydrogenase class 3
  177. Alcohol dehydrogenase 1B
  178. Alcohol dehydrogenase 1C
  179. Serine hydroxymethyltransferase, mitochondrial precursor
  180. Serine hydroxymethyltransferase, cytosolic
  181. 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3
  182. 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4
  183. 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1
  184. Fructose-1,6-bisphosphatase isozyme 2
  185. Fructose-1,6-bisphosphatase 1
  186. 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2
  187. Glutathione S-transferase Mu 2
  188. Glutathione peroxidase 7 precursor
  189. Epididymal secretory glutathione peroxidase precursor
  190. Glutathione S-transferase Mu 1
  191. Hydroxyacylglutathione hydrolase
  192. Glutathione S-transferase Mu 3
  193. Glutathione S-transferase A1
  194. Glutathione S-transferase theta-2
  195. Glutathione S-transferase Mu 5
  196. Microsomal glutathione S-transferase 2
  197. Glutathione transferase omega-1
  198. Glutathione S-transferase A5
  199. Glutathione S-transferase A2
  200. Glutathione peroxidase 6 precursor
  201. Glutathione peroxidase 1
  202. Phospholipid hydroperoxide glutathione peroxidase, mitochondrial precursor
  203. Glutathione peroxidase 3 precursor
  204. Glutathione transferase omega-2
  205. Glutathione S-transferase theta-1
  206. Glutathione peroxidase 2
  207. Glutathione S-transferase P
  208. Beta-glucuronidase precursor
  209. Beta-galactosidase precursor
  210. 3-keto-steroid reductase
  211. 5-oxoprolinase
  212. Cytosol aminopeptidase
  213. Alpha-mannosidase 2
  214. Mannosyl-oligosaccharide 1,2-alpha-mannosidase IB
  215. Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
  216. Mannosyl-oligosaccharide 1,2-alpha-mannosidase IA
  217. Beta-hexosaminidase beta chain precursor
  218. Beta-hexosaminidase alpha chain precursor
  219. Tissue alpha-L-fucosidase precursor
  220. Plasma alpha-L-fucosidase precursor
  221. Inosine-5'-monophosphate dehydrogenase 2
  222. Bifunctional purine biosynthesis protein PURH [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase
  223. dTDP-D-glucose 4,6-dehydratase
  224. UDP-glucose 6-dehydrogenase
  225. Probable urocanate hydratase
  226. ADP-ribosyl cyclase 1
  227. 10-formyltetrahydrofolate dehydrogenase
  228. GTP cyclohydrolase I
  229. Arachidonate 5-lipoxygenase
  230. Prostaglandin G/H synthase 1 precursor
  231. Methylglutaconyl-CoA hydratase, mitochondrial precursor
  232. Cytochrome P450 4F2
  233. Cytochrome P450 4F3
  234. Leukotriene A-4 hydrolase
  235. Cytochrome P450 3A4
  236. Protoporphyrinogen oxidase
  237. Acidic mammalian chitinase precursor
  238. Chitotriosidase-1 precursor
  239. Cytochrome P450 2C9
  240. Cytochrome P450 2C19
  241. 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial precursor
  242. Cytochrome P450 17A1
  243. Cytosolic acyl coenzyme A thioester hydrolase
  244. Acyl-coenzyme A thioesterase 2
  245. Acyl-coenzyme A thioesterase 8
  246. Palmitoyl-protein thioesterase 1 precursor
  247. Sulfite oxidase, mitochondrial precursor
  248. Inorganic pyrophosphatase
  249. mRNA-capping enzyme
  250. Beta-enolase
  251. Gamma-enolase
  252. Alpha-enolase
  253. Ectonucleotide pyrophosphatase/phosphodiesterase family member 7 precursor
  254. Sphingomyelin phosphodiesterase 2
  255. Uridine diphosphate glucose pyrophosphatase
  256. Peptide deformylase, mitochondrial precursor
  257. Probable phospholipid-transporting ATPase IG
  258. Probable phospholipid-transporting ATPase IH
  259. Plasma membrane calcium-transporting ATPase 3
  260. Katanin p60 ATPase-containing subunit A1
  261. Vacuolar ATP synthase subunit G 3
  262. Probable phospholipid-transporting ATPase VA
  263. Vacuolar ATP synthase subunit G 1
  264. Probable phospholipid-transporting ATPase IC
  265. Sodium/potassium-transporting ATPase subunit beta-3
  266. Plasma membrane calcium-transporting ATPase 1
  267. ATP synthase epsilon chain, mitochondrial
  268. ATP synthase delta chain, mitochondrial precursor
  269. Probable phospholipid-transporting ATPase IIA
  270. Sodium/potassium-transporting ATPase subunit beta-2
  271. Plasma membrane calcium-transporting ATPase 2
  272. Sodium/potassium-transporting ATPase subunit beta-1
  273. Probable phospholipid-transporting ATPase VD
  274. Sarcoplasmic/endoplasmic reticulum calcium ATPase 3
  275. Vacuolar ATP synthase subunit C 1
  276. Vacuolar ATP synthase subunit G 2
  277. ATP synthase coupling factor 6, mitochondrial precursor
  278. Bifunctional polynucleotide phosphatase/kinase
  279. Vacuolar ATP synthase subunit B, kidney isoform
  280. Potassium-transporting ATPase alpha chain 2
  281. X/potassium-transporting ATPase subunit beta-m
  282. ATP synthase protein 8
  283. ATP synthase e chain, mitochondrial
  284. ATP synthase gamma chain, mitochondrial precursor
  285. Vacuolar ATP synthase subunit d 1
  286. Sodium/potassium-transporting ATPase alpha-1 chain precursor
  287. Calcium-transporting ATPase type 2C member 1
  288. Sodium/potassium-transporting ATPase alpha-3 chain
  289. ATP synthase B chain, mitochondrial precursor
  290. Vesicle-fusing ATPase
  291. ATP synthase subunit alpha, mitochondrial precursor
  292. Probable phospholipid-transporting ATPase IIB
  293. Potassium-transporting ATPase alpha chain 1
  294. Probable phospholipid-transporting ATPase IM
  295. Vacuolar ATP synthase 16 kDa proteolipid subunit
  296. Probable phospholipid-transporting ATPase IF
  297. Probable phospholipid-transporting ATPase IK
  298. ATP synthase D chain, mitochondrial
  299. ATP synthase f chain, mitochondrial
  300. Sodium/potassium-transporting ATPase alpha-2 chain precursor
  301. Cytochrome P450 2E1
  302. Cytochrome P450 1B1
  303. Cytochrome P450 2F1
  304. Cytochrome P450 2B6
  305. Cytochrome P450 2A13
  306. Cytochrome P450 4B1
  307. Cytochrome P450 4Z1
  308. Cytochrome P450 1A2
  309. Cytochrome P450 19A1
  310. Cytochrome P450 2C8
  311. Cytochrome P450 2S1
  312. Cytochrome P450 2J2
  313. Cytochrome P450 2A7
  314. Inositol polyphosphate 5-phosphatase OCRL-1
  315. Synaptojanin-2
  316. 72 kDa inositol polyphosphate 5-phosphatase
  317. Synaptojanin-1
  318. Thiamine-triphosphatase
  319. Catalase
  320. Phosphatidylinositol-glycan-specific phospholipase D precursor
  321. Alpha-L-iduronidase precursor
  322. Iduronate 2-sulfatase precursor
  323. Alpha-N-acetylglucosaminidase precursor
  324. N-acetylglucosamine-6-sulfatase precursor
  325. Cytochrome c oxidase subunit 1
  326. Epoxide hydrolase 1
  327. Glucosylceramidase precursor
  328. Type II inositol-1,4,5-trisphosphate 5-phosphatase precursor
  329. Elongation factor 1-alpha 1
  330. Laforin
  331. Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
  332. Proline oxidase, mitochondrial precursor
  333. Peptidoglycan recognition protein precursor
  334. Carbonic anhydrase 1
  335. Salivary alpha-amylase precursor
  336. Pancreatic alpha-amylase precursor
  337. Natriuretic peptides B precursor [Contains: Gamma-brain natriuretic peptide; Brain natriuretic peptide 32
  338. N-acetylgalactosamine-6-sulfatase precursor
  339. Cytochrome c oxidase polypeptide VIIa-heart, mitochondrial precursor
  340. L-glutaminase
  341. 2',3'-cyclic-nucleotide 3'-phosphodiesterase
  342. Probable ubiquitin carboxyl-terminal hydrolase CYLD
  343. Peroxiredoxin-5, mitochondrial precursor
  344. Carbonic anhydrase 3
  345. Aquaporin-3
  346. Leukocyte common antigen precursor
  347. Kynurenine 3-monooxygenase
  348. Copper-transporting ATPase 2
  349. Probable peptidyl-tRNA hydrolase
  350. Agmatinase, mitochondrial precursor
  351. Receptor-type tyrosine-protein phosphatase alpha precursor
  352. Myotubularin
  353. Ectonucleoside triphosphate diphosphohydrolase 2
  354. Dual specificity protein phosphatase 2
  355. Pterin-4-alpha-carbinolamine dehydratase
  356. Aquaporin-2
  357. Thioesterase domain containing 1
  358. Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2
  359. Peroxiredoxin-2
  360. Cytochrome c oxidase polypeptide VIIa-liver/heart, mitochondrial precursor
  361. AID
  362. Cytosolic beta-glucosidase
  363. Thioredoxin-dependent peroxide reductase, mitochondrial precursor
  364. Maltase-glucoamylase, intestinal [Includes: Maltase
  365. Carbonic anhydrase 12 precursor
  366. Phosphoethanolamine/phosphocholine phosphatase
  367. ATP synthase lipid-binding protein, mitochondrial precursor
  368. Cytochrome P450, family 39, subfamily A, polypeptide 1
  369. Carbonic anhydrase 4 precursor
  370. Sodium/potassium-transporting ATPase alpha-4 chain
  371. Cytochrome c oxidase polypeptide VIa-heart, mitochondrial precursor
  372. Cytochrome c oxidase subunit 7C, mitochondrial precursor
  373. Cytochrome c oxidase subunit 5B, mitochondrial precursor
  374. Carbonic anhydrase 9 precursor
  375. Cytochrome c oxidase subunit VIb isoform 1
  376. Cytosolic 5'-nucleotidase III
  377. CDNA PSEC0079 fis, clone NT2RP2004049, highly similar to Group XII secretory phospholipase A2
  378. Cytochrome c oxidase polypeptide VIIb2, mitochondrial precursor
  379. ENTPD4 protein
  380. Cytochrome c oxidase subunit VIb isoform 2
  381. Glutamine-dependent NAD(+) synthetase
  382. Carbonic anhydrase 13
  383. Inositol polyphosphate 5-phosphatase
  384. ATP synthase lipid-binding protein, mitochondrial precursor
  385. Cytochrome c oxidase polypeptide VIII-liver/heart, mitochondrial precursor
  386. Type II inositol-3,4-bisphosphate 4-phosphatase
  387. OTTHUMP00000017001
  388. Cytochrome c oxidase subunit VIIa-related protein, mitochondrial precursor
  389. CAD protein [Includes: Glutamine-dependent carbamoyl-phosphate synthase
  390. Cytochrome c oxidase polypeptide 8 isoform 3, mitochondrial precursor
  391. CGI-14 protein
  392. Pyridoxal phosphate phosphatase
  393. Vacuolar ATP synthase subunit d 2
  394. Vacuolar ATP synthase subunit E 2
  395. Vacuolar ATP synthase subunit C 2
  396. Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11A
  397. Uncharacterized protein ENSP00000330918
  398. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-4
  399. 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
  400. 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial precursor
  401. Cytochrome P450 46A1
  402. Inorganic pyrophosphatase 2, mitochondrial precursor
  403. Glucose-6-phosphatase 2
  404. Mannosyl-oligosaccharide 1,2-alpha-mannosidase IC
  405. Hydroxyacylglutathione hydrolase-like protein
  406. Neutral alpha-glucosidase C
  407. Type I inositol-3,4-bisphosphate 4-phosphatase
  408. Sphingomyelin phosphodiesterase 3
  409. Cytochrome c oxidase subunit 2
  410. Cytochrome c oxidase polypeptide VIa-liver, mitochondrial precursor
  411. Cytochrome c oxidase subunit 4 isoform 2, mitochondrial precursor
  412. Cytochrome P450 4A22 [Precursor]
  413. Lysophosphatidic acid phosphatase type 6 precursor
  414. Gamma-glutamyltransferase 6 homolog
  415. Epoxide hydrolase 2, cytoplasmic (Epoxide hydrolase 2, cytoplasmic, isoform CRA_b)
  416. UPB1 protein
  417. Carboxyl ester lipase
  418. cDNA FLJ76781, highly similar to Homo sapiens cytochrome P450, family 27, subfamily A, polypeptide 1
  419. cDNA FLJ75261, highly similar to Human class I alcohol dehydrogenase
  420. Putative uncharacterized protein DKFZp686B0215
  421. Enoyl-Coenzyme A, hydratase/3-hydroxyacyl Coenzyme A dehydrogenase
  422. cDNA FLJ76435, highly similar to Homo sapiens cytochrome P450, family 11, subfamily A, polypeptide 1
  423. Fumarate hydratase (Fumarate hydratase, isoform CRA_c) (cDNA, FLJ92753, Homo sapiens fumarate hydratase (FH), nuclear gene encodingmitochondrial protein, mRNA)
  424. cDNA FLJ75824, highly similar to Homo sapiens serine dehydratase
  425. Putative uncharacterized protein
  426. cDNA FLJ76259, highly similar to Homo sapiens aminomethyltransferase
  427. cDNA FLJ78616, highly similar to Homo sapiens phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase
  428. C1-tetrahydrofolate synthase
  429. Methylenetetrahydrofolate dehydrogenase
  430. Uncharacterized protein GAA
  431. cDNA FLJ78123, highly similar to Homo sapiens phosphoribosyl pyrophosphate amidotransferase
  432. cDNA FLJ75406, highly similar to Homo sapiens guanine monphosphate synthetase
  433. Glycerophosphodiester phosphodiesterase 1
  434. Multiple inositol polyphosphate phosphatase 1 precursor
  435. MIOX protein
  436. Protein-tyrosine phosphatase mitochondrial 1, mitochondrial precursor
  437. 2-aminoadipic 6-semialdehyde dehydrogenase
  438. Aminoadipate-semialdehyde synthase
  439. cDNA FLJ76252, highly similar to Homo sapiens S-adenosylhomocysteine hydrolase
  440. cDNA FLJ78177, highly similar to Homo sapiens carbonic anhydrase VB, mitochondrial
  441. cDNA FLJ77936, highly similar to Homo sapiens VNN1 protein
  442. cDNA FLJ76234, highly similar to Homo sapiens coproporphyrinogen oxidase
  443. cDNA FLJ76077, highly similar to Homo sapiens hydroxymethylbilane synthase
  444. cDNA FLJ76398, highly similar to Homo sapiens nudix
  445. Ribonucleoside-diphosphate reductase subunit M2 B
  446. IMP
  447. DCMP deaminase
  448. N-acylsphingosine amidohydrolase 3-like
  449. cDNA FLJ78026
  450. cDNA FLJ75757, highly similar to Homo sapiens PAP-inositol-1,4- phosphatase
  451. Cytochrome P450, family 1, subfamily A, polypeptide 1
  452. Kynureninase
  453. Uncharacterized protein GSTZ1
  454. Ectonucleoside triphosphate diphosphohydrolase 8
  455. Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
  456. Serine/threonine-protein phosphatase with EF-hands 1
  457. Serine/threonine-protein phosphatase with EF-hands 2
  458. Protein tyrosine phosphatase type IVA protein 3
  459. Tyrosine-protein phosphatase non-receptor type 7
  460. Sulfhydryl oxidase 1 precursor
  461. Sulfhydryl oxidase 2 precursor
  462. Dynamin-1
  463. Dynamin-2
  464. Elongation factor G 1, mitochondrial precursor
  465. Elongation factor G 2, mitochondrial precursor
  466. Elongation factor Tu, mitochondrial precursor
  467. Elongation factor Tu GTP-binding domain-containing protein 1
  468. Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
  469. Serine/threonine-protein phosphatase 4 catalytic subunit
  470. Serine/threonine-protein phosphatase 5
  471. Serine/threonine-protein phosphatase 6
  472. Enolase-phosphatase E1
  473. Eyes absent homolog 1
  474. Eyes absent homolog 2
  475. Sphingomyelin phosphodiesterase 4
  476. Diphosphoinositol polyphosphate phosphohydrolase 3 beta
  477. Diphosphoinositol polyphosphate phosphohydrolase 2
  478. Protein phosphatase 1D
  479. Protein phosphatase 1E
  480. Protein phosphatase 1F
  481. Protein phosphatase 1G
  482. Protein phosphatase 1M
  483. Ubiquitin-like domain-containing CTD phosphatase 1
  484. PH domain leucine-rich repeat protein phosphatase-like
  485. PH domain leucine-rich repeat-containing protein phosphatase
  486. RNA polymerase II subunit A C-terminal domain phosphatase
  487. Dual specificity protein phosphatase 10
  488. Dual specificity protein phosphatase 12
  489. Dual specificity protein phosphatase 16
  490. Dual specificity protein phosphatase 19
  491. Dual specificity protein phosphatase 1
  492. Dual specificity protein phosphatase 3
  493. Dual specificity protein phosphatase 5
  494. Dual specificity protein phosphatase 6
  495. Dual specificity protein phosphatase 7
  496. Dual specificity protein phosphatase 8
  497. M-phase inducer phosphatase 1
  498. M-phase inducer phosphatase 3
  499. Tyrosine-protein phosphatase non-receptor type 14
  500. Tyrosine-protein phosphatase non-receptor type 18
  501. Tyrosine-protein phosphatase non-receptor type 21
  502. Tyrosine-protein phosphatase non-receptor type 22
  503. Tyrosine-protein phosphatase non-receptor type 2
  504. Tyrosine-protein phosphatase non-receptor type 3
  505. Tyrosine-protein phosphatase non-receptor type 4
  506. Tyrosine-protein phosphatase non-receptor type 9
  507. Receptor-type tyrosine-protein phosphatase N2 precursor
  508. Receptor-type tyrosine-protein phosphatase epsilon precursor
  509. Receptor-type tyrosine-protein phosphatase F precursor
  510. Receptor-type tyrosine-protein phosphatase O precursor
  511. Receptor-type tyrosine-protein phosphatase zeta precursor
  512. Putative tyrosine-protein phosphatase TPTE
  513. Cytosolic phospholipase A2 beta
  514. Deoxyhypusine hydroxylase
  515. cDNA FLJ75877, highly similar to Homo sapiens 5'-nucleotidase, cytosolic II (NT5C2), mRNA
  516. Cytochrome P450, family 21, subfamily A, polypeptide 2
  517. Aldehyde dehydrogenase 3B1 (Aldehyde dehydrogenase 3 family, member B1, isoform CRA_c) (cDNA FLJ77312, highly similar to Homo sapiens aldehyde dehydrogenase 3 family, member B1 (ALDH3B1),mRNA)
  518. Paraoxonase 2 (cDNA FLJ78444, highly similar to Homo sapiens paraoxonase 2, transcript variant 1, mRNA)
  519. Paraoxonase 3 (HCG2023324, isoform CRA_a)
  520. Platelet-activating factor acetylhydrolase 2, 40kDa (Platelet- activating factor acetylhydrolase 2, 40kDa, isoform CRA_a)
  521. cDNA FLJ76635, highly similar to Homo sapiens phosphatidylinositol glycan, class L (PIGL), mRNA (Phosphatidylinositol glycan, class L, isoform CRA_b)
  522. Uncharacterized protein PAM
  523. 3',5'-cyclic nucleotide phosphodiesterase 10A2
  524. Adenosine monophosphate deaminase (Isoform E) (Adenosine monophosphate deaminase (Isoform E), isoform CRA_b) (cDNA FLJ76195, highly similar to Homo sapiens adenosine monophosphate deaminase (isoform E) (AMPD3),mRNA)
  525. CDNA FLJ14389 fis, clone HEMBA1002876
  526. Peptidyl arginine deiminase, type I
  527. Peptidyl arginine deiminase-like protein
  528. Guanine deaminase (Guanine deaminase, isoform CRA_b)
  529. Glucosamine-6-phosphate isomerase 2
  530. Cytochrome P450, family 3, subfamily A, polypeptide 7
  531. Cytochrome P450, family 2, subfamily D, polypeptide 6 (Cytochrome P450 2D6)
  532. Cytochrome P450, family 3, subfamily A, polypeptide 5 (Cytochrome P450, family 3, subfamily A, polypeptide 5, isoform CRA_a)
  533. Cytochrome P450, family 4, subfamily X, polypeptide 1 (Cytochrome P450, family 4, subfamily X, polypeptide 1, isoform CRA_b) (Cytochrome P450)
  534. Putative uncharacterized protein CYP3A43 (Cytochrome P450, family 3, subfamily A, polypeptide 43, isoform CRA_e)
  535. GGTL3 protein (Fragment)
  536. Gamma-glutamyltransferase-like activity 1
  537. cDNA FLJ77091, highly similar to Homo sapiens alcohol dehydrogenase 4 (class II), pi polypeptide (ADH4), mRNA
  538. Alcohol dehydrogenase 7 (Class IV), mu or sigma polypeptide
  539. Phospholipase D1 variant (Fragment)
  540. cDNA FLJ78566, highly similar to Homo sapiens glucosidase I, mRNA (Glucosidase I, isoform CRA_b)
  541. Glutathione S-transferase A3 (Glutathione S-transferase A3, isoform CRA_b)
  542. cDNA FLJ75746, highly similar to Homo sapiens glutathione S- transferase M4 (GSTM4), transcript variant 1, mRNA (Glutathione S- transferase M4, isoform CRA_d)
  543. LOC51064 protein (Glutathione S-transferase kappa 1, isoform CRA_d) (Glutathione S-transferase kappa 1) (cDNA FLJ78056)
  544. cDNA FLJ76401, highly similar to Homo sapiens microsomal glutathione S-transferase 1 (MGST1), transcript variant 1b, mRNA (Microsomal glutathione S-transferase 1, isoform CRA_a)
  545. Cytochrome P450, family 51, subfamily A, polypeptide 1 (Cytochrome P450, family 51, subfamily A, polypeptide 1, isoform CRA_a)
  546. AFMID protein
  547. cDNA FLJ75059, highly similar to Homo sapiens phosphoribosylformylglycinamidine synthase (FGAR amidotransferase) (PFAS), mRNA
  548. Myeloperoxidase (Myeloperoxidase, isoform CRA_a)
  549. cDNA FLJ76595, highly similar to Homo sapiens peroxiredoxin 6 (PRDX6), mRNA (Peroxiredoxin 6, isoform CRA_a)
  550. cDNA FLJ77866, highly similar to Homo sapiens peptidoglycan recognition protein L (PGLYRP) mRNA (Peptidoglycan recognition protein 2, isoform CRA_a)
  551. Peptidoglycan recognition protein I-alpha
  552. Peptidoglycan recognition protein 4 (PGLYRP4 protein)
  553. Putative uncharacterized protein DKFZp761J1915 (Ectonucleoside triphosphate diphosphohydrolase 6 (Putative function), isoform CRA_a)
  554. Ectonucleoside triphosphate diphosphohydrolase 5 (Ectonucleoside triphosphate diphosphohydrolase 5, isoform CRA_d)
  555. Acyl-CoA thioesterase 4
  556. Hyaluronidase-1
  557. Sperm adhesion molecule 1 (PH-20 hyaluronidase, zona pellucida binding) (Sperm adhesion molecule 1 (PH-20 hyaluronidase, zona pellucida binding), isoform CRA_c)
  558. Hyaluronidase-2
  559. cDNA FLJ77934, highly similar to Homo sapiens flavin containing monooxygenase 1 (FMO1), mRNA (Flavin containing monooxygenase 1, isoform CRA_a)
  560. Flavin containing monooxygenase 2
  561. Nitric oxide synthase 2A (Inducible, hepatocytes)
  562. Uncharacterized protein SC4MOL
  563. Uncharacterized protein ZNF554 (Zinc finger protein 554, isoform CRA_c)
  564. Sialidase 1 (Lysosomal sialidase) (Sialidase 1 (Lysosomal sialidase), isoform CRA_a) (NEU1 protein)
  565. Testicular acid phosphatase
  566. cDNA FLJ78014, highly similar to Homo sapiens aminolevulinate, delta-, dehydratase (ALAD), transcript variant 1, mRNA
  567. ASAH1 protein
  568. UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (EC 5.1.3.14) (Glucosamine (UDP-N-acetyl)-2-epimerase/N- acetylmannosamine kinase, isoform CRA_a)
  569. 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)
  570. CDKN3 protein (Cyclin-dependent kinase inhibitor 3 (CDK2-associated dual specificity phosphatase), isoform CRA_c)
  571. Dual specificity protein phosphatase 14
  572. Uncharacterized protein DUSP15
  573. Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit beta
  574. PPM1B beta isoform variant 4
  575. Serine/threonine protein phosphatase (EC 3.1.3.16)
  576. 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)
  577. Serine/threonine protein phosphatase (EC 3.1.3.16)
  578. Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1
  579. Dual specificity protein phosphatase 21
  580. Uncharacterized protein CDC14C
  581. cDNA FLJ75328, highly similar to Homo sapiens ATPase, Ca++ transporting, cardiac muscle, fast twitch1 (ATP2A1), transcript variant b, mRNA
  582. Putative uncharacterized protein DKFZp686I0955
  583. ATP8A1 protein (ATPase, aminophospholipid transporter (APLT), Class I, type 8A, member 1, isoform CRA_a)
  584. CDNA FLJ45330 fis, clone BRHIP3007195, highly similar to Potential phospholipid-transporting ATPase IB (EC 3.6.3.13)
  585. ATPase, class I, type 8B, member 2
  586. T-cell, immune regulator 1, ATPase, H+ transporting, lysosomal V0 subunit A3 (T-cell, immune regulator 1, ATPase, H+ transporting, lysosomal V0 subunit A3, isoform CRA_c)
  587. cDNA FLJ76372, highly similar to Homo sapiens ATP synthase, H+ transporting, mitochondrial F0 complex, subunit G, mRNA (HCG2043599, isoform CRA_b)
  588. V-type proton ATPase subunit e 2
  589. cDNA FLJ76178, highly similar to Homo sapiens ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide (ATP5B), mRNA (ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide)
  590. ATPase, H+ transporting, lysosomal V0 subunit a isoform 4 (ATPase, H+ transporting, lysosomal V0 subunit a4, isoform CRA_a)
  591. Uncharacterized protein ATP6V1E1
  592. Uncharacterized protein ATP6V0B (ATPase, H+ transporting, lysosomal 21kDa, V0 subunit b, isoform CRA_b)
  593. Vacuolar-type H(+)-ATPase
  594. ATPase, H+ transporting, lysosomal accessory protein 1 (ATPase, H+ transporting, lysosomal accessory protein 1, isoform CRA_d) (cDNA FLJ78461, highly similar to Homo sapiens ATPase, H+ transporting, lysosomal accessory protein 1 (ATP6AP1), mRNA) (Fragment
  595. ATPase, H+ transporting, lysosomal 14kDa, V1 subunit F (ATPase, H+ transporting, lysosomal 14kDa, V1 subunit F, isoform CRA_a)
  596. cDNA FLJ77987, highly similar to Homo sapiens katanin p60 subunit A- like 1, mRNA (Katanin p60 subunit A-like 1, isoform CRA_a)
  597. CP protein (Ceruloplasmin (Ferroxidase), isoform CRA_a)
  598. Peroxisomal N1-acetyl-spermine/spermidine oxidase (PAO) (Polyamine oxidase (Exo-N4-amino), isoform CRA_a)
  599. cDNA FLJ78072, highly similar to Homo sapiens amidohydrolase domain containing 1, mRNA (Amidohydrolase domain containing 1, isoform CRA_a)
  600. cDNA FLJ75807, highly similar to Homo sapiens pyruvate dehydrogenase phosphatase isoenzyme 2 (PDP2), mRNA (HCG1774842)
  601. cDNA FLJ75306, highly similar to Homo sapiens prostaglandin- endoperoxide synthase 2 (prostaglandin G/H synthase and cyclooxygenase), mRNA (Prostaglandin-endoperoxide synthase 2) (Prostaglandin G/H synthase and cyclooxygenase)
  602. cDNA FLJ76814, highly similar to Homo sapiens dynamin 1-like (DNM1L), transcript variant 3, mRNA
  603. cDNA FLJ77981, highly similar to Homo sapiens carbonic anhydrase 14 (Carbonic anhydrase XIV, isoform CRA_d)
  604. Carbonic anhydrase 6
  605. Carbonic anhydrase VII short form (Carbonic anhydrase VII, isoform CRA_d)
  606. cDNA FLJ78193, highly similar to Homo sapiens carbonic anhydrase VIII (CA8), mRNA (Carbonic anhydrase VIII, isoform CRA_c)
  607. Receptor protein tyrosine phosphatase hPTP-J precursor
  608. Protein tyrosine phosphatase domain-containing protein 1
  609. cDNA FLJ75567, highly similar to Homo sapiens protein tyrosine phosphatase, non-receptor type 23 (PTPN23), mRNA (Protein tyrosine phosphatase, non-receptor type 23, isoform CRA_b)
  610. cDNA FLJ75657, highly similar to Homo sapiens protein tyrosine phosphatase, non-receptor type 1 (PTPN1), mRNA (Protein tyrosine phosphatase, non-receptor type 1, isoform CRA_c)
  611. cDNA FLJ77053, highly similar to Homo sapiens protein tyrosine phosphatase, non-receptor type 6 (PTPN6), transcript variant 1, mRNA (Protein tyrosine phosphatase, non-receptor type 6, isoform CRA_d)
  612. cDNA FLJ75588, highly similar to Homo sapiens protein tyrosine phosphatase, non-receptor type 11 (Noonan syndrome 1) (PTPN11), mRNA (Protein tyrosine phosphatase, non-receptor type 11 (Noonan syndrome 1), isoform CRA_b)
  613. CDNA FLJ44133 fis, clone THYMU2008725, highly similar to PROTEIN- TYROSINE PHOSPHATASE BETA (EC 3.1.3.48)
  614. Protein tyrosine phosphatase receptor type D
  615. Receptor-type tyrosine-protein phosphatase H
  616. PTPRJ protein
  617. PTPRM protein
  618. Receptor-type tyrosine-protein phosphatase-like N
  619. Protein tyrosine phosphatase, receptor type, sigma isoform 3 variant (Fragment)
  620. cDNA FLJ76461, highly similar to Homo sapiens protein tyrosine phosphatase type IVA, member 2 (PTP4A2), transcript variant 1, mRNA (Protein tyrosine phosphatase type IVA, member 2, isoform CRA_a)
  621. Myotubularin related protein 3 (Myotubularin related protein 3, isoform CRA_f)
  622. Phospholipase C, beta 3 (Phosphatidylinositol-specific) (Phospholipase C, beta 3 (Phosphatidylinositol-specific), isoform CRA_a)
  623. Phospholipase C, gamma 1 (Phospholipase C, gamma 1, isoform CRA_b)
  624. Carboxylesterase 7
  625. Peroxiredoxin-4
  626. Lipase, hepatic
  627. Carboxymethylenebutenolidase homolog
  628. Ubiquitin carboxyl-terminal hydrolase 16
  629. STAM-binding protein
  630. Ubiquitin carboxyl-terminal hydrolase (EC 3.1.2.15)
  631. Ubiquitin carboxyl-terminal hydrolase (EC 3.1.2.15)
  632. Ubiquitin carboxyl-terminal hydrolase 51
  633. Ubiquitin carboxyl-terminal hydrolase 33
  634. Ubiquitin carboxyl-terminal hydrolase 22
  635. Ubiquitin carboxyl-terminal hydrolase (EC 3.1.2.15)
  636. Ubiquitin carboxyl-terminal hydrolase (EC 3.1.2.15)
  637. Ubiquitin carboxyl-terminal hydrolase 47
  638. Ubiquitin carboxyl-terminal hydrolase 40
  639. Ubiquitin carboxyl-terminal hydrolase 35
  640. Ubiquitin carboxyl-terminal hydrolase 36
  641. Ubiquitin carboxyl-terminal hydrolase 29
  642. Ubiquitin carboxyl-terminal hydrolase (EC 3.1.2.15)
  643. Ubiquitin carboxyl-terminal hydrolase 46
  644. Ubiquitin carboxyl-terminal hydrolase (EC 3.1.2.15)
  645. Ubiquitin carboxyl-terminal hydrolase 1
  646. Ubiquitin carboxyl-terminal hydrolase 7
  647. Ubiquitin carboxyl-terminal hydrolase 5
  648. Probable ubiquitin carboxyl-terminal hydrolase FAF-X
  649. Probable ubiquitin carboxyl-terminal hydrolase FAF-Y
  650. Ubiquitin carboxyl-terminal hydrolase 26
  651. Ubiquitin carboxyl-terminal hydrolase (EC 3.1.2.15)
  652. Ubiquitin carboxyl-terminal hydrolase 32
  653. Ubiquitin carboxyl-terminal hydrolase 30
  654. Ubiquitin carboxyl-terminal hydrolase 13
  655. Ubiquitin carboxyl-terminal hydrolase (EC 3.1.2.15)
  656. Ubiquitin carboxyl-terminal hydrolase 6
  657. Ubiquitin carboxyl-terminal hydrolase 10
  658. Ubiquitin carboxyl-terminal hydrolase 8
  659. Ubiquitin carboxyl-terminal hydrolase 15
  660. Ubiquitin carboxyl-terminal hydrolase 3
  661. Lysozyme-like protein 1
  662. Pterin-4-alpha-carbinolamine dehydratase 2
  663. cDNA, FLJ95508, highly similar to Homo sapiens 5'-nucleotidase, ecto (CD73) (NT5E), mRNA
  664. Mitochondrial cytochrome P450, family 11, subfamily B, polypeptide 2 (Cytochrome P450, family 11, subfamily B, polypeptide 2)
  665. cDNA, FLJ93072, Homo sapiens monoamine oxidase B (MAOB), nuclear gene encoding mitochondrial protein, mRNA (Monoamine oxidase B, isoform CRA_a)
  666. cDNA, FLJ93758, Homo sapiens biotinidase (BTD), mRNA (Biotinidase, isoform CRA_a)
  667. cDNA, FLJ93559, Homo sapiens platelet-activating factor acetylhydrolase, isoformIb, alpha subunit 45kDa (PAFAH1B1), mRNA (Platelet-activating factor acetylhydrolase, isoform Ib, alpha subunit 45kDa)
  668. cDNA FLJ31531 fis, clone NT2RI2000585, highly similar to Sialate O-acetylesterase (EC 3.1.1.53)
  669. cDNA FLJ16680 fis, clone TLIVE2008221, highly similar to Acyl-coenzyme A thioesterase 12 (EC 3.1.2.1)
  670. cDNA, FLJ92383, Homo sapiens acylphosphatase 1, erythrocyte (common) type (ACYP1), mRNA (Acylphosphatase 1, erythrocyte (Common) type)
  671. cDNA, FLJ93151, Homo sapiens procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3 (PLOD3), mRNA (Procollagen-lysine, 2-oxoglutarate 5-dioxygenase 3)
  672. cDNA, FLJ92898, Homo sapiens aminoadipate-semialdehydedehydrogenase-phosphopantetheinyl transferase (AASDHPPT), mRNA (Aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase, isoform CRA_b)
  673. Phosphodiesterase 7B (Phosphodiesterase 7B, isoform CRA_b)
  674. cDNA FLJ38065 fis, clone CTONG2015316, highly similar to cAMP-specific 3',5'-cyclic phosphodiesterase 4C (EC 3.1.4.17)
  675. cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
  676. cDNA FLJ40747 fis, clone TRACH2000502, highly similar to Peroxisomal NADH pyrophosphatase NUDT12 (EC 3.6.1.22)
  677. cDNA, FLJ93456, highly similar to Homo sapiens D-amino-acid oxidase (DAO), mRNA (D-amino-acid oxidase, isoform CRA_c)
  678. cDNA FLJ34575 fis, clone KIDNE2008362, highly similar to Homo sapiens asparaginase like 1 (ASRGL1), mRNA
  679. cDNA FLJ43342 fis, clone NT2RI3007978, highly similar to CTP synthase 2 (EC 6.3.4.2)
  680. cDNA, FLJ93424, highly similar to Homo sapiens cytochrome P450, family 2, subfamily A, polypeptide 6 (CYP2A6), mRNA (Cytochrome P450, family 2, subfamily A, polypeptide 6)
  681. cDNA, FLJ93938, Homo sapiens cytochrome P450, family 2, subfamily C, polypeptide 18(CYP2C18), mRNA (HCG39167, isoform CRA_b)
  682. cDNA, FLJ94596, Homo sapiens fumarylacetoacetate hydrolase (fumarylacetoacetase)(FAH), mRNA (Fumarylacetoacetate hydrolase (Fumarylacetoacetase), isoform CRA_a)
  683. Cholesterol 25-hydroxylase
  684. cDNA FLJ14592 fis, clone NT2RM4002063, highly similar to Peroxisomal sarcosine oxidase (EC 1.5.3.1)
  685. cDNA FLJ10843 fis, clone NT2RP4001345, highly similar to 1-O-acylceramide synthase (EC 2.3.1.-)
  686. cDNA FLJ61209, highly similar to NG,NG-dimethylarginine dimethylaminohydrolase 1 (EC 3.5.3.18)
  687. cDNA FLJ35449 fis, clone SMINT2004144, highly similar to ALCOHOL DEHYDROGENASE 6 (EC 1.1.1.1)
  688. cDNA, FLJ94281, Homo sapiens cystathionine-beta-synthase (CBS), mRNA (Cystathionine-beta-synthase, isoform CRA_b)
  689. Sarcosine dehydrogenase
  690. cDNA, FLJ96415, Homo sapiens glutathione S-transferase A4 (GSTA4), mRNA (Glutathione S-transferase A4, isoform CRA_b)
  691. cDNA, FLJ92385, Homo sapiens microsomal glutathione S-transferase 3 (MGST3), mRNA (Microsomal glutathione S-transferase 3, isoform CRA_a)
  692. cDNA, FLJ92616, Homo sapiens lipoprotein lipase (LPL), mRNA (Lipoprotein lipase)
  693. cDNA, FLJ94587, Homo sapiens annexin A3 (ANXA3), mRNA (Annexin A3, isoform CRA_a)
  694. Putative uncharacterized protein
  695. cDNA, FLJ96235, Homo sapiens phosphoserine phosphatase (PSPH), mRNA (Phosphoserine phosphatase, isoform CRA_a)
  696. cDNA, FLJ93260, Homo sapiens inositol(myo)-1(or 4)-monophosphatase 1 (IMPA1), mRNA (Inositol(Myo)-1(Or 4)-monophosphatase 1, isoform CRA_a)
  697. Inositol monophosphatase 2 variant 1 (Inositol(Myo)-1(Or 4)-monophosphatase 2, isoform CRA_b)
  698. cDNA, FLJ92843, Homo sapiens arginase, type II (ARG2), nuclear gene encodingmitochondrial protein, mRNA (Arginase, type II, isoform CRA_a)
  699. cDNA FLJ46063 fis, clone TBAES2007428, highly similar to N-acetylglucosamine-1-phosphodiesteralpha-N- acetylglucosaminidase (EC 3.1.4.45)
  700. cDNA, FLJ93696, highly similar to Homo sapiens flavin containing monooxygenase 3 (FMO3), mRNA (Flavin containing monooxygenase 3, isoform CRA_b)
  701. NOS1 mutant (Nitric oxide synthase 1 (Neuronal), isoform CRA_c)
  702. Cytochrome P450, family 7, subfamily B, polypeptide 1
  703. cDNA, FLJ92858, highly similar to Homo sapiens bone marrow stromal cell antigen 1 (BST1), mRNA (Bone marrow stromal cell antigen 1)
  704. Palmitoyl-protein thioesterase 2 (HCG1999928, isoform CRA_a)
  705. cDNA, FLJ96858, Homo sapiens N-acetylneuraminic acid synthase (sialic acid synthase) (NANS), mRNA (N-acetylneuraminic acid synthase (Sialic acid synthase), isoform CRA_b)
  706. cDNA FLJ30910 fis, clone FEBRA2006270, highly similar to N-acylneuraminate-9-phosphatase (EC 3.1.3.29)
  707. Putative uncharacterized protein ACP1
  708. Methionine adenosyltransferase II, beta, isoform CRA_a
  709. cDNA FLJ30970 fis, clone HEART2000444, highly similar to Homo sapiens phospholysine phosphohistidine inorganic pyrophosphate phosphatase (LHPP), mRNA
  710. cDNA, FLJ92787, highly similar to Homo sapiens phosphatidic acid phosphatase type 2B (PPAP2B), mRNA (Phosphatidic acid phosphatase type 2B, isoform CRA_a)
  711. cDNA FLJ60951, highly similar to Probable allantoicase (Allantoicase, isoform CRA_a)
  712. Phospholipase A2, group VI (Cytosolic, calcium-independent) (Phospholipase A2, group VI (Cytosolic, calcium-independent), isoform CRA_a)
  713. cDNA FLJ31512 fis, clone NT2RI1000048, highly similar to Dual specificity protein phosphatase 18 (EC 3.1.3.48)
  714. cDNA, FLJ95698, Homo sapiens dual specificity phosphatase 4 (DUSP4), transcript variant 1, mRNA (Dual specificity phosphatase 4, isoform CRA_a)
  715. cDNA, FLJ94996, highly similar to Homo sapiens dual specificity phosphatase 9 (DUSP9), mRNA
  716. cDNA FLJ45992 fis, clone SKMUS2008585, highly similar to Homo sapiens dual specificity phosphatase 13 (DUSP13), transcript variant 3, mRNA
  717. Protein phosphatase 1A isoform 1 (Protein phosphatase 1A (Formerly 2C), magnesium-dependent, alpha isoform, isoform CRA_a)
  718. cDNA, FLJ92643, Homo sapiens protein phosphatase 1, catalytic subunit, beta isoform(PPP1CB), mRNA (Protein phosphatase 1, catalytic subunit, beta isoform, isoform CRA_a)
  719. Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
  720. Serine/threonine protein phosphatase
  721. cDNA FLJ41117 fis, clone BRACE2006821, highly similar to Dopamine- and cAMP-regulated neuronalphospho protein
  722. CDC14 cell division cycle 14 homolog A (S. cerevisiae)
  723. ATPase, Ca++ transporting, plasma membrane 4 (ATPase, Ca++ transporting, plasma membrane 4, isoform CRA_a)
  724. cDNA, FLJ93898, Homo sapiens ADP-ribosylarginine hydrolase (ADPRH), mRNA (ADP-ribosylarginine hydrolase, isoform CRA_b)
  725. ATPase, Cu++ transporting, alpha polypeptide (Menkes syndrome) (ATPase, Cu++ transporting, alpha polypeptide (Menkes syndrome), isoform CRA_a)
  726. ATPase, H+/K+ exchanging, beta polypeptide (ATPase, H+/K+ exchanging, beta polypeptide, isoform CRA_b)
  727. cDNA, FLJ96900, Homo sapiens ATPase, H+ transporting, lysosomal 34kDa, V1 subunit D(ATP6V1D), mRNA (ATPase, H+ transporting, lysosomal 34kDa, V1 subunit D, isoform CRA_a)
  728. cDNA FLJ12283 fis, clone MAMMA1001754, highly similar to Vacuolar ATP synthase subunit H (EC 3.6.3.14)
  729. cDNA, FLJ95649, Homo sapiens ATPase, H+ transporting, lysosomal 70kDa, V1 subunit A(ATP6V1A), mRNA (ATPase, H+ transporting, lysosomal 70kDa, V1 subunit A, isoform CRA_a)
  730. cDNA, FLJ92695, Homo sapiens ATPase, H+ transporting, lysosomal 56/58kDa, V1subunit B, isoform 2 (ATP6V1B2), mRNA (ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B2, isoform CRA_a)
  731. Putative uncharacterized protein
  732. cDNA, FLJ92349, Homo sapiens ATPase, H+ transporting, lysosomal 9kDa, V0 subunit e(ATP6V0E), mRNA (ATPase, H+ transporting, lysosomal 9kDa, V0 subunit e, isoform CRA_a)
  733. cDNA, FLJ94145, Homo sapiens phosphatase and tensin homolog (mutated in multipleadvanced cancers 1) (PTEN), mRNA (Phosphatase and tensin homolog (Mutated in multiple advanced cancers 1), isoform CRA_c)
  734. cDNA, FLJ95254, highly similar to Homo sapiens prenylcysteine lyase (PCL1), mRNA (Prenylcysteine oxidase 1)
  735. cDNA FLJ30254 fis, clone BRACE2002441, highly similar to Ferritin heavy chain (Ferritin, heavy polypeptide 1, isoform CRA_a)
  736. Stearoyl-CoA desaturase 5 (Stearoyl-CoA desaturase 5, isoform CRA_c)
  737. cDNA FLJ35540 fis, clone SPLEN2002493, highly similar to Phosphatidylinositol 4,5-bisphosphate5-phosphatase A (EC 3.1.3.56)
  738. cDNA, FLJ92960, Homo sapiens skeletal muscle and kidney enriched inositolphosphatase (SKIP), transcript variant 2, mRNA (Skeletal muscle and kidney enriched inositol phosphatase, isoform CRA_a)
  739. cDNA FLJ44914 fis, clone BRAMY3009782, highly similar to Pyruvate dehydrogenase (lipoamide)-phosphatase 1 (Protein phosphatase 2C, magnesium-dependent, catalytic subunit, isoform CRA_a)
  740. cDNA, FLJ93658, highly similar to Homo sapiens alkaline phosphatase, intestinal (ALPI), mRNA (Alkaline phosphatase, intestinal, isoform CRA_a)
  741. cDNA, FLJ95799, Homo sapiens uroporphyrinogen III synthase (congenitalerythropoietic porphyria) (UROS), mRNA (Uroporphyrinogen III synthase (Congenital erythropoietic porphyria), isoform CRA_a)
  742. Eukaryotic translation elongation factor 1 alpha 2
  743. EEF2 protein (Eukaryotic translation elongation factor 2, isoform CRA_a)
  744. cDNA, FLJ96671, Homo sapiens 3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1 (soluble) (HMGCS1), mRNA (3-hydroxy-3-methylglutaryl-Coenzyme A synthase 1 (Soluble), isoform CRA_a)
  745. cDNA, FLJ93439, Homo sapiens carbonic anhydrase II (CA2), mRNA (Carbonic anhydrase II)
  746. Carbonic anhydrase VA, mitochondrial (Carbonic anhydrase VA, mitochondrial, isoform CRA_b)
  747. cDNA, FLJ92112, Homo sapiens cytochrome c oxidase subunit IV isoform 1 (COX4I1),mRNA (Cytochrome c oxidase subunit IV isoform 1, isoform CRA_b)
  748. cDNA, FLJ92052, Homo sapiens cytochrome c oxidase subunit VIc (COX6C), mRNA (Cytochrome c oxidase subunit VIc, isoform CRA_a)
  749. cDNA, FLJ92145, Homo sapiens cytochrome c oxidase subunit VIIb (COX7B), nucleargene encoding mitochondrial protein, mRNA (Cytochrome c oxidase subunit VIIb)
  750. cDNA FLJ76224, highly similar to Homo sapiens eyes absent homolog 3 (Drosophila) (EYA3), transcript variant 1, mRNA
  751. cDNA FLJ51710, highly similar to Tyrosine-protein phosphatase non-receptor type 12 (EC 3.1.3.48)
  752. Protein tyrosine phosphatase, receptor type, G
  753. PTPRK protein
  754. cDNA, FLJ92701, Homo sapiens protein tyrosine phosphatase, receptor type, R(PTPRR), transcript variant 1, mRNA
  755. cDNA, FLJ92892, Homo sapiens protein tyrosine phosphatase type IVA, member 1(PTP4A1), mRNA (Protein tyrosine phosphatase type IVA, member 1, isoform CRA_a)
  756. cDNA FLJ45381 fis, clone BRHIP3021019, highly similar to Homo sapiens protein tyrosine phosphatase, non-receptor type 5 (striatum-enriched) (PTPN5), transcript variant 3, mRNA
  757. cDNA FLJ35394 fis, clone SKNSH2002768, highly similar to M-PHASE INDUCER PHOSPHATASE 2 (EC 3.1.3.48)
  758. cDNA, FLJ96083, Homo sapiens TcD37 homolog (HTCD37), mRNA
  759. Dolichyl pyrophosphate phosphatase 1 (Dolichyl pyrophosphate phosphatase 1, isoform CRA_d) (cDNA FLJ60437, highly similar to Dolichyldiphosphatase 1)
  760. Nudix (Nucleoside diphosphate linked moiety X)-type motif 3
  761. cDNA FLJ33455 fis, clone BRAMY2000354, highly similar to 1-phosphatidylinositol-4,5-bisphosphatephosphodiesterase delta 1 (EC 3.1.4.11)
  762. Vitamin K epoxide reductase complex, subunit 1, isoform CRA_d
  763. Peroxiredoxin 1 (Peroxiredoxin 1, isoform CRA_a)
  764. Lipase, endothelial (Lipase, endothelial, isoform CRA_a)
  765. cDNA FLJ40900 fis, clone UTERU2003411, highly similar to Peptidyl-tRNA hydrolase 2, mitochondrial (Peptidyl-tRNA hydrolase 2)
  766. Ubiquitin carboxyl-terminal hydrolase
  767. Ubiquitin specific peptidase 11
  768. cDNA FLJ44996 fis, clone BRAWH3010657, highly similar to Ubiquitin carboxyl-terminal hydrolase 38 (EC 3.1.2.15)
  769. Ubiquitin carboxyl-terminal hydrolase
  770. cDNA FLJ45104 fis, clone BRAWH3032930, highly similar to Alpha-amylase 2B (EC 3.2.1.1)
  771. Aquaporin-1
  772. Aquaporin-4
  773. Aquaporin-10
Enzyme 1 [top]
Enzyme 1 ID 5232
Enzyme 1 Name Cytosolic 5'-nucleotidase 1B
Enzyme 1 Synonyms
  1. Cytosolic 5'-nucleotidase IB
  2. cN1B
  3. cN-IB
  4. Autoimmune infertility-related protein
Enzyme 1 Gene Name NT5C1B
Enzyme 1 Protein Sequence >Cytosolic 5'-nucleotidase 1B 
MSQTSLKQKKNEPGMRSSKESLEAEKRKESDKTGVRLSNQMRRAVNPNHSLRCCPFQGHS
SCRRCLCAAEGTALGPCHTIRIYIHMCLLWEQGQQITMMRGSQESSLRKTDSRGYLVRSQ
WSRISRSPSTKAPSIDEPRSRNTSAKLPSSSTSSRTPSTSPSLHDSSPPPLSGQPSLQPP
ASPQLPRSLDSRPPTPPEPDPGSRRSTKMQENPEAWAQGIVREIRQTRDSQPLEYSRTSP
TEWKSSSQRRGIYPASTQLDRNSLSEQQQQQREDEDDYEAAYWASMRSFYEKNPSCSRPW
PPKPKNAITIALSSCALFNMVDGRKIYEQEGLEKYMEYQLTNENVILTPGPAFRFVKALQ
YVNARLRDLYPDEQDLFDIVLMTNNHAQVGVRLINSVNHYGLLIDRFCLTGGKDPIGYLK
AYLTNLYIAADSEKVQEAIQEGIASATMFDGAKDMAYCDTQLRVAFDGDAVLFSDESEHF
TKEHGLDKFFQYDTLCESKPLAQGPLKGFLEDLGRLQKKFYAKNERLLCPIRTYLVTARS
AASSGARVLKTLRRWGLEIDEALFLAGAPKSPILVKIRPHIFFDDHMFHIEGAQRLGSIA
AYGFNKKFSS
Enzyme 1 Number of Residues 610
Enzyme 1 Molecular Weight 68804
Enzyme 1 Theoretical pI 9.03
Enzyme 1 GO Classification
Function
  • 5'-nucleotidase activity
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleotidase activity
  • nucleotide binding
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Helps to regulate adenosine levels
Enzyme 1 Pathways
Enzyme 1 Reactions
  • A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 13774961 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q96P26 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name 5NT1B_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1699 bp 
GGGCAAAAATGTGGATAACAACAAAAGAATTTCAACAGGTAAAAAAATGAGTCAAACATC
TCTCAAACAGAAAAAGAATGAGCCCGGAATGAGGTCCTCAAAAGAGAGTCTAGAAGCAGA
AAAAAGAAAGGAATCTGACAAAACAGGAGTTCGTCTGAGCAATCAGGGATCACAAGAATC
ATCACTGCGGAAGACAGACTCTCGAGGGTACCTTGTGCGCAGTCAATGGTCTAGAATATC
CCGGAGCCCATCCACCAAGGCTCCATCCATAGATGAGCCTAGAAGCAGGAACACCAGTGC
TAAGCTCCCCAGCAGCTCCACGAGCTCCCGGACTCCATCCACCTCCCCAAGCCTGCATGA
CTCCTCACCGCCGCCGCTGTCCGGGCAGCCCTCGCTCCAGCCACCCGCGTCGCCCCAGCT
GCCCCGGTCGCTGGACTCGCGGCCTCCCACGCCCCCAGAGCCCGATCCTGGCTCCCGGCG
CAGCACCAAAATGCAAGAAAATCCGGAGGCCTGGGCCCAAGGCATCGTGCGGGAAATCCG
CCAGACCCGGGACTCGCAGCCGCTGGAATATTCGCGCACGTCCCCCACCGAGTGGAAGTC
CTCCAGCCAGCGCAGGGGGATCTACCCCGCCTCCACCCAGCTGGACCGCAACTCTCTGTC
CGAGCAGCAGCAGCAGCAGCGGGAGGACGAAGACGACTACGAAGCTGCCTACTGGGCATC
CATGAAGTCGTTCTACGAAAAGAACCCGAGCTGCTGGCGCCCCTGGCCGCCCAAACCCAA
GAACGCCATCACCATTGCTCTCTCATCCTGCGCGCTCTTCAACATGGTGGACGGCAGGAA
AATCTACGAGCAAGAGGGTCTGGAAAAGTACATGGAGTATCAGCTCACCAATGAGAACGT
CATCCTGACCCCGGGCCCGGCGTTCCGTTTCGTCAAGGCACTACAGTATGTCAATGCTAG
ACTCCGTGATCTATATCCTGATGAACAGGACTTATTTGATATTGTACTGATGACTAATAA
CCATGCCCAAGTGGGAGTGCGGCTTATAAACAGCGTCAATCACTACGGCTTACTGATTGA
CCGCTTCTGTCTGACCGGGGGAAAAGACCCCATTGGCTATTTGAAGGCATATCTTACCAA
CTTGTATATTGCTGCAGATTCTGAAAAAGTGCAAGAGGCAATACAAGAAGGTATTGCCTC
TGCGACAATGTTTGATGGAGCCAAAGACATGGCTTACTGTGACACTCAGCTCCGTGTAGC
CTTTGATGGGGATGCTGTCCTCTTCTCTGATGAGTCTGAACATTTTACCAAGGAGCATGG
GCTGGACAAATTCTTCCAGTATGATACATTATGTGAAAGTAAGCCTCTTGCTCAGGGTCC
CCTAAAAGGCTTTCTGGAAGATTTAGGCAGACTGCAAAAGAAGTTCTATGCCAAAAATGA
ACGGTTACTTTGTCCTATCAGGACCTACCTGGTTACAGCTAGGAGTGCAGCCAGTTCAGG
CGCCCGTGTGCTGAAAACCTTCCGACGCTGGGGTCTAGAGATAGACGAAGCTCTTTTCCT
TGCTGGAGCCCCCAAAAGTCCCATCTTGGTGAAGATCCGGCCCCACATCTTCTTTGATGA
CCACATGTTCCACATTGAAGGGGCACAGAGGTTAGGTTCCATCGCAGCTTATGGCTTTAA
TAAAAAATTCAGTAGTTAG
Enzyme 1 GenBank Gene ID AF356185 Link Image
Enzyme 1 GeneCard ID NT5C1B Link Image
Enzyme 1 GenAtlas ID NT5C1B Link Image
Enzyme 1 HGNC ID HGNC:17818 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2p24.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Sala-Newby GB, Newby AC: Cloning of a mouse cytosolic 5'-nucleotidase-I identifies a new gene related to human autoimmune infertility-related protein. Biochim Biophys Acta. 2001 Oct 31;1521(1-3):12-8. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5233
Enzyme 2 Name Cytosolic 5'-nucleotidase 1A
Enzyme 2 Synonyms
  1. Cytosolic 5'-nucleotidase IA
  2. cN1A
  3. cN-IA
  4. cN-I
Enzyme 2 Gene Name NT5C1A
Enzyme 2 Protein Sequence >Cytosolic 5'-nucleotidase 1A 
MEPGQPREPQEPREPGPGAETAAAPVWEEAKIFYDNLAPKKKPKSPKPQNAVTIAVSSRA
LFRMDEEQQIYTEQGVEEYVRYQLEHENEPFSPGPAFPFVKALEAVNRRLRELYPDSEDV
FDIVLMTNNHAQVGVRLINSINHYDLFIERFCMTGGNSPICYLKAYHTNLYLSADAEKVR
EAIDEGIAAATIFSPSRDVVVSQSQLRVAFDGDAVLFSDESERIVKAHGLDRFFEHEKAH
ENKPLAQGPLKGFLEALGRLQKKFYSKGLRLECPIRTYLVTARSAASSGARALKTLRSWG
LETDEALFLAGAPKGPLLEKIRPHIFFDDQMFHVAGAQEMGTVAAHVPYGVAQTPRRTAP
AKQAPSAQ
Enzyme 2 Number of Residues 368
Enzyme 2 Molecular Weight 41021
Enzyme 2 Theoretical pI 6.52
Enzyme 2 GO Classification
Function
  • 5'-nucleotidase activity
  • binding
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleotidase activity
  • nucleotide binding
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides and has a broad substrate specificity. Helps to regulate adenosine levels in heart during ischemia and hypoxia
Enzyme 2 Pathways
Enzyme 2 Reactions
  • A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 12659324 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9BXI3 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name 5NT1A_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1107 bp 
ATGGAACCTGGGCAGCCCCGGGAGCCCCAGGAGCCCCGCGAGCCCGGGCCAGGAGCGGAG
ACCGCTGCGGCCCCGGTCTGGGAGGAAGCCAAGATTTTCTACGACAACCTCGCGCCCAAG
AAGAAACCCAAATCGCCCAAGCCTCAGAATGCAGTCACCATCGCTGTGTCCTCCCGAGCC
TTGTTTCGCATGGACGAGGAGCAGCAGATCTACACGGAGCAGGGCGTGGAGGAGTACGTG
CGCTACCAGCTGGAACATGAGAACGAACCCTTCAGTCCCGGGCCAGCCTTCCCTTTTGTG
AAGGCTCTGGAGGCCGTGAACAGGCGGCTGCGGGAGCTGTACCCTGATAGTGAGGACGTC
TTCGACATCGTCCTCATGACTAACAACCATGCTCAAGTGGGTGTCCGCCTCATCAACAGT
ATCAACCACTATGACCTGTTCATCGAGAGGTTCTGCATGACAGGTGGGAACAGCCCGATC
TGCTACCTCAAGGCCTATCACACCAACCTCTACTTGTCAGCCGATGCGGAAAAAGTGCGA
GAAGCCATTGATGAGGGGATCGCAGCTGCCACCATCTTCAGCCCCAGCAGGGATGTGGTT
GTGTCCCAGAGTCAGCTGCGCGTGGCCTTCGATGGGGACGCCGTGCTCTTCTCGGACGAG
TCGGAGCGCATCGTCAAGGCCCACGGGCTGGACCGATTCTTCGAGCATGAGAAGGCCCAC
GAGAACAAGCCTCTGGCTCAGGGCCCCTTAAAGGGCTTTCTGGAGGCACTGGGTAGGTTG
CAGAAGAAGTTCTACTCCAAAGGCCTGCGGCTGGAGTGCCCAATTCGTACCTACTTGGTG
ACAGCACGCAGTGCAGCCAGTTCCGGGGCCCGGGCTCTCAAGACCCTGCGCAGCTGGGGC
CTGGAGACAGATGAAGCCTTGTTCCTTGCTGGAGCGCCCAAGGGCCCTCTCCTTGAGAAG
ATCCGCCCACACATCTTCTTTGATGACCAGATGTTCCATGTGGCTGGGGCTCAGGAGATG
GGCACTGTGGCCGCCCATGTGCCTTATGGTGTGGCACAGACACCCCGGCGGACTGCACCT
GCAAAGCAGGCCCCATCTGCACAGTAG
Enzyme 2 GenBank Gene ID AF331801 Link Image
Enzyme 2 GeneCard ID NT5C1A Link Image
Enzyme 2 GenAtlas ID NT5C1A Link Image
Enzyme 2 HGNC ID HGNC:17819 Link Image
Enzyme 2 Chromosome Location 1
Enzyme 2 Locus 1p34.3-p33
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Hunsucker SA, Spychala J, Mitchell BS: Human cytosolic 5'-nucleotidase I: characterization and role in nucleoside analog resistance. J Biol Chem. 2001 Mar 30;276(13):10498-504. Epub 2000 Dec 22. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5234
Enzyme 3 Name 5'(3')-deoxyribonucleotidase, cytosolic type
Enzyme 3 Synonyms
  1. Cytosolic 5',3'-pyrimidine nucleotidase
  2. Deoxy-5'-nucleotidase 1
  3. dNT-1
Enzyme 3 Gene Name NT5C
Enzyme 3 Protein Sequence >5'(3')-deoxyribonucleotidase, cytosolic type 
MARSVRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRALRPDLADK
VASVYEAPGFFLDLEPIPGALDAVREMNDLPDTQVFICTSPLLKYHHCVGEKYRWVEQHL
GPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSWEHILFTCCHNRHLVLPPTRRRL
LSWSDNWREILDSKRGAAQRE
Enzyme 3 Number of Residues 201
Enzyme 3 Molecular Weight 23383
Enzyme 3 Theoretical pI 6.63
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 7524492 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q8TCD5 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name NT5C_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >606 bp 
ATGGCGCGGAGCGTGCGCGTGCTGGTGGACATGGACGGCGTCCTGGCCGACTTCGAGGCC
GGCCTCCTGCGGGGCTTCCGCCGCCGCTTCCCTGAGGAGCCGCACGTGCCGCTGGAGCAA
CGCCGCGGCTTCCTGGCCCGCGAGCAGTACCGCGCCCTGCGGCCCGACCTGGCGGATAAA
GTGGCCAGTGTGTACGAAGCCCCGGGCTTTTTCCTGGACCTGGAGCCCATCCCGGGAGCC
TTGGACGCTGTGCGGGAGATGAACGACCTACCGGACACGCAGGTCTTCATCTGCACCAGC
CCCCTGCTGAAGTACCACCACTGTGTGGGTGAGAAGTACCGCTGGGTGGAGCAGCACCTG
GGGCCCCAGTTCGTAGAACGAATTATCCTGACAAGGGACAAGACGGTGGTCTTGGGGGAC
CTGCTCATTGATGACAAGGACACAGTTCGAGGCCAGGAGGAGACCCCAAGCTGGGAGCAC
ATCTTGTTCACCTGCTGCCACAATCGGCACCTGGTCCTGCCCCCGACAAGGAGACGGCTG
CTCTCCTGGAGTGACAACTGGAGGGAGATCTTAGATAGCAAGCGCGGAGCTGCGCAGCGG
GAATGA
Enzyme 3 GenBank Gene ID AF154829 Link Image
Enzyme 3 GeneCard ID NT5C Link Image
Enzyme 3 GenAtlas ID NT5C Link Image
Enzyme 3 HGNC ID HGNC:17144 Link Image
Enzyme 3 Chromosome Location 17
Enzyme 3 Locus 17q25.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Rampazzo C, Johansson M, Gallinaro L, Ferraro P, Hellman U, Karlsson A, Reichard P, Bianchi V: Mammalian 5'(3')-deoxyribonucleotidase, cDNA cloning, and overexpression of the enzyme in Escherichia coli and mammalian cells. J Biol Chem. 2000 Feb 25;275(8):5409-15. [PubMed Link Image]
  2. Rampazzo C, Kost-Alimova M, Ruzzenente B, Dumanski JP, Bianchi V: Mouse cytosolic and mitochondrial deoxyribonucleotidases: cDNA cloning of the mitochondrial enzyme, gene structures, chromosomal mapping and comparison with the human orthologs. Gene. 2002 Jul 10;294(1-2):109-17. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5236
Enzyme 4 Name 5'(3')-deoxyribonucleotidase, mitochondrial precursor
Enzyme 4 Synonyms
  1. 5',3'-nucleotidase, mitochondrial
  2. Deoxy-5'-nucleotidase 2
  3. dNT-2
Enzyme 4 Gene Name NT5M
Enzyme 4 Protein Sequence >5'(3')-deoxyribonucleotidase, mitochondrial precursor 
MIRLGGWCARRLCSAAVPAGRRGAAGGLGLAGGRALRVLVDMDGVLADFEGGFLRKFRAR
FPDQPFIALEDRRGFWVSEQYGRLRPGLSEKAISIWESKNFFFELEPLPGAVEAVKEMAS
LQNTDVFICTSPIKMFKYCPYEKYAWVEKYFGPDFLEQIVLTRDKTVVSADLLIDDRPDI
TGAEPTPSWEHVLFTACHNQHLQLQPPRRRLHSWADDWKAILDSKRPC
Enzyme 4 Number of Residues 228
Enzyme 4 Molecular Weight 25862
Enzyme 4 Theoretical pI 8.12
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Dephosphorylates specifically the 5' and 2'(3')- phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-15
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 9408106 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9NPB1 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name NT5M_HUMAN Link Image
Enzyme 4 PDB ID 1Q92 Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >687 bp 
ATGATCCGGCTGGGCGGCTGGTGTGCGCGGCGGCTCTGCAGCGCGGCGGTTCCCGCGGGG
CGGCGCGGGGCGGCGGGCGGGCTGGGCCTGGCGGGAGGCCGCGCCCTACGGGTGCTGGTG
GACATGGACGGCGTGCTGGCTGACTTCGAGGGCGGATTCCTCAGGAAGTTCCGCGCGCGC
TTTCCCGACCAGCCCTTCATCGCGCTGGAGGACCGGCGCGGCTTCTGGGTGTCGGAGCAG
TACGGCCGCCTGCGGCCAGGGCTGAGCGAGAAGGCCATCAGCATTTGGGAGTCAAAGAAT
TTCTTTTTTGAACTTGAGCCTCTGCCAGGGGCCGTGGAAGCTGTCAAGGAGATGGCCAGC
CTACAAAACACTGACGTCTTCATCTGCACAAGCCCCATCAAGATGTTCAAGTACTGTCCC
TATGAGAAGTATGCCTGGGTGGAGAAGTACTTTGGCCCTGACTTTCTGGAGCAGATTGTG
CTGACCAGAGACAAGACCGTGGTCTCTGCTGACCTTCTCATAGACGACCGGCCGGACATC
ACAGGGGCCGAGCCAACCCCCAGCTGGGAGCATGTCCTCTTCACCGCCTGCCACAACCAG
CACCTGCAGCTGCAGCCCCCCCGCCGCAGGCTGCACTCGTGGGCGGACGACTGGAAGGCC
ATTCTGGACAGCAAGCGGCCCTGCTGA
Enzyme 4 GenBank Gene ID AJ277557 Link Image
Enzyme 4 GeneCard ID NT5M Link Image
Enzyme 4 GenAtlas ID NT5M Link Image
Enzyme 4 HGNC ID HGNC:15769 Link Image
Enzyme 4 Chromosome Location 17
Enzyme 4 Locus 17p11.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Rampazzo C, Gallinaro L, Milanesi E, Frigimelica E, Reichard P, Bianchi V: A deoxyribonucleotidase in mitochondria: involvement in regulation of dNTP pools and possible link to genetic disease. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8239-44. [PubMed Link Image]
  2. Rinaldo-Matthis A, Rampazzo C, Reichard P, Bianchi V, Nordlund P: Crystal structure of a human mitochondrial deoxyribonucleotidase. Nat Struct Biol. 2002 Oct;9(10):779-87. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5264
Enzyme 5 Name Fatty acid synthase
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name FASN
Enzyme 5 Protein Sequence >Fatty acid synthase 
MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRWKAGLYGLPRRSGKLKDLSRF
DASFFGVHPKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEAL
SRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQC
PAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLAR
RVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVG
DPQELNGITRALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFH
SPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNVHIILRPNTQPPPAPAPHATL
PRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGP
EVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSILRSDEAVKPFGLKVSQLLLS
TDESTFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAV
LAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVTISGPQAPVFE
FVEQLRKEGVFAKEVRTGGMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEA
QWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLEIAPHALLQAVLKRGLKPSCT
IIPLMKKDHRDNLEFFLAGIGRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSL
AWDVPAAEDFPNGSGSPSAAIYNIDTSSESPDHYLVDHTLDGRVLFPATGYLSIVWKTLA
RALGLGVEQLPVVFEDVVLHQATILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQ
WDDPDPRLFDHPESPTPNPTEPLFLAQAEVYKELRLRGYDYGPHFQGILEASLEGDSGRL
LWKDNWVSFMDTMLQMSILGSAKHGLYLPTRVTAIHIDPATHRQKLYTLQDKAQVADVVV
SRWLRVTVAGGVHISGLHTESAPRRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQL
CKGLVQALQTTVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQ
VLAQERPKLPEDPLLSGLLDSPALKACLDTAVENMPSLKMKVVEVLAGHGHLYSRIPGLL
SPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSADLLVCNCAVA
ALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVAFLTSTEPQYGQGILSQDAWESL
FSRVSLRLVGLKKSFYGSTLFLCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSSRP
VWLKAINCATSGVVGLVNCLRREPGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKVLQGD
LVMNVYRDGAWGAFRHFLLEEDKPEEPTAHAFVSTLTRGDLSSIRWVCSSLRHAQPTCPG
AQLCTVYYASLNFRDIMLATGKLSPDAIPGKWTSQDSLLGMEFSGRDASGKRVMGLVPAK
GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGV
GQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSRDTSFEQHVLWHTGGKG
VDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFF
NESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQVLAEE
PEAVLKGAKPKLMSAISKTFCPAHKSYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGI
RTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLL
ENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSA
MERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLN
QPHMVLSSFVLAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSV
EVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELACPTPKEDGLAQQQTQLNLR
SLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLD
SIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGS
PTYVLAYTQSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAA
VDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGA
DYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEPRVSVREG
Enzyme 5 Number of Residues 2511
Enzyme 5 Molecular Weight 273403
Enzyme 5 Theoretical pI 6.39
Enzyme 5 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • oxidoreductase activity
  • phosphopantetheine binding
  • transferase activity
  • vitamin binding
Process
  • biosynthesis
  • carboxylic acid metabolism
  • cellular metabolism
  • fatty acid biosynthesis
  • fatty acid metabolism
  • metabolism
  • organic acid metabolism
  • physiological process
Component
—
Enzyme 5 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 5 Specific Function Fatty acid synthetase catalyzes the formation of long- chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein
Enzyme 5 Pathways
Enzyme 5 Reactions
  • (3R)-3-hydroxypalmitoyl-[acyl-carrier protein] = 2-hexadecenoyl-[acyl-carrier protein] + H2O
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 1049053 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P49327 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name FAS_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >7515 bp 
ATGGAGGAGGTGGTGATTGCCGGCATGTTCGGGAAGCTGCCAGAGTCGGAGAACTTGCAG
GAGTTCTGGGACAACCTCATCGGCGGTGTGGACATGGTCACGGACGATGACCGTCGCTGG
AAGGCTGGGCTCTACGGCCTGCCCCGGCGGTCCGGCAAGCTGAAGGACCTGTCTAGGTTT
GATGCCTCCTTCTTCGGAGTCCACCCCAAGCAGGCACACACGATGGACCCTCAGCTGCGG
CTGCTGCTGGAAGCTACCTATGAAGCCATCGTGGACGGAGGCATCAACCCAGATTCACTC
CGAGGAACACACACTGGCGTCTGGGTGGGCGTGAGCGGCTCTGAGACCTCGGAGGCCCTG
AGCCGAGACCCCGAGACACTCGTGGGCTACAGCATGGTGGGCTGCCAGCGAGCGATGATG
GCCAACCGGCTCTCCTTCTTCTTCGACTTCAGAGGGCCCAGCATCGCACTGGACACAGCC
TGCTCCTCCAGCCTGATGGCCCTGCAGAACGCCTACCAGGCCATCCACAGCGGGCAGTGC
CCTGCCGCCATCGTGGGGGGCATCAACGTCCTGCTGAAGCCCAACACCTCCGTGCAGTTC
TTGAGGCTGGGGATGCTCAGCCCCGAGGGCACCTGCAAGGCCTTCGACACAGCGGGGAAT
GGGTACTGCCGCTCGGAGGGTGTGGTGGCTGTCCTGCTGACCAAGAAGTCCCTGGCCCGG
AAGGTCTACACCACCATCCTGAACAAAGGCACCAATACAGATGGCTTCAAGGAGCAAGGC
GTGACCTTCCCTCAGGATATCCAGGAGCAGCCTATCCGCTCGTTGTACCAGTCGGCCGGA
GTGGCCCCTGAGTCATTTGAATACATCGAAGCCCACGGACCAGGCACCAAGGTGGGCGAC
CCCCAGGAGCGTAATGGCATCACCCGAGCCCTGTGCGCCACCCGCCAGGAGCCGCTGCTC
ATCGGCTCCACCAAGTCCAACATGGGGCACCCGGAGCCAGCCTCGGGGCTCGACGCCCTG
GCCAAGGTGCTGCTGTCCCTGGAGCACGGGCTCTGGGCCCCCAACCTGCACTTCCATAGC
CCCAACCCTGAGATCCCAGCGCTGTTGGATGGGCGGCTGCAGGTGGTGGACCAGCCCCTG
CCCGTCCGTGGCGGCAACGTGGGCATCAACTCCTTTGGCTTCGGGGGCTCCAACATGCAC
ATCATCCTGAGGCCCAACACGCAGTCCGCCCCCGCACCCGCCCCACATGCCACCCTGCCC
CGTCTGCTGCGGGCCAGCGGACGCACCCCTGAGGCCGTGCAGAAGCTGCTGGAGCAGGGC
CTCCGGCACAGCCAGGGCCTGGCTTTCCTGAGCATGCTGAACGACATCGCGGCTGTCCCC
GCCACCGCCATGCCCTTCCGTGGCTACGCTGTGCTGGGTGGTGAGACGCGGTGGCCCAGA
GTGCAGCAGGTGCCCGCTGGCGAGCGCCCGCTCTGGTTCATCTGCTCTGGGATGGGCACA
CAGTGGCGTGGAATGGGGCTGAGCCTTATGCGCCTGGACCGCTTCCGAGATTCCATCCTA
CGCTCCGATGAGGCTGTGAACCGATTCGGCCTGAAGGTGTCACAGCTGCTGCTGAGCACA
GACGAGAGCACCTTTGATGACATCGTCCATTCGTTTGTGAGCCTGACTGCCATCCAGATA
GGCCTCATAGACCTGCTGAGCTGCATGGGACCTGAGGCAGATGGCATCGTCGGCCACTCC
CTGGGGGAGTGGCTGTCGGTACGCGACGGCTGCCTGTCCCAGGAGGAGGCCGTCCTCGCT
GCCTACTGGAGGGGACAGTGCATCAAAGAAGCCCCACTTCCCGCCGGCGCCATGGCAGCC
GTGGGCTTGTCCTGGGAGGAGTGTAAACAGCGCTGCCCCCCTGCGGTGGTGCCCGCCTGC
CACAACTCCAAGGACACAGTCACCATCTCGGGACCTCAGGCCCCGGTGTTTGAGTTCGTG
GAGCAGCTGAGGAAGGAGGGTGTGTTTGCCAAGGAGGTGCGGACCGGCGGTATGGCCTTC
CACTCCTACTTCATGGAGGCCATCGCACCCCCACTGCTGCAGGAGCTCAAGAAGGTGATC
CGGGAGCCGAAGCCACGTTCAGCCCGCTGGCTCAGCACCTCTATCCCCGAGGCCCAGTGG
CACAGCAGCCTGGCACGCACGTCTTCCGCCGAGTACAATGTCAACAACCTGGTGAGCCCT
GTGCTGTTCCAGGAGGCCCTGTGGCACGTGCCTGAGCACGCGGTGGTGCTGGAGATCGCC
CCGACCCCGTGCCCTCAGGCTGTCCTGAAGCGGGTCCGTAAGCCGAGCTGCACCATCATC
CCCCGTATGAAGAAGGATCACAGGGACAACCTGGAGTTCTTCCTGGCCGGCATCGGCAGG
CTGCACCTCTCAGGCATCGACGCCAACCCCAATGCCTTGTTCCCACCTGTGGAGTCCCCA
GCTCCCCGAGGAACTCCCCTCATCTCCCCACTCATCAAGTGGGACCACAGCCTGGCCTGG
GACGCGCCGGCCGCCGAGGACTTCCCCAACGGTTCAGGTTCCCCCTCAGCCACCATCTAC
ACATGCACACCAAGCTCCGAGTCTCCTGACCGCTACCTGGTGGACCACACCATCGACGGT
CGCGTCCTCTTCCCCGCCACTGGCTACCTGAGCATAGTGTGGAAGACGCTGGCCCGCGCC
TGGGCTGGGCTCGAGCAGCTGCCTGTGGTGTTTGAGGATGTGGTGCAGCACCAGGCCACC
ATCCTGCCCAAGACTGGGACAGTGTCCTTGGAGGTACGGCTCCTGGAGGCCACCGGTGCC
TTCGAGGTGTCAGAGAACGGCAACCTGGTAGTGAGTGGGAAGGTGTACCAGTGGGATGAC
CCTGACCCCAGGCTCTTCGACCACCCGGAAAGTCCCCACCCCAATTCCCCACGGAGTCCC
CTCTTCCTGGCCCAGGCAGAAGTTTACAAGGAGCTGCGTCTGCGTGGCTACGACTACGGC
CCTCATTTCCAGGGCATCCTGGAGGCCAGCCTGGAAGGTGACTCGGGGAGGCTGCTGTGG
AAGGATAACTGGGTGAGCTTCATGGACACCATGCTGCAGATGTCCATCCTGGGCTCGGCC
AAGCACGGCCTGTACCTACCCACCCGTGTCACCGCCATCCACATCGACCCTGCCACCCAC
AGGCAGAAGCTGTACACACTGCAGGACAAGGCCCAAGTGGCTGACGTGGTGGTGAGCAGG
TGGCCGAGGGTCACAGTGGCGGGAGGCGTCCACATCTCCGGGCTCCACACTGAGTCGGCC
CCGCGGCGGCACGAGGAGCAGCAGGTGCCCATCCTGGAGAAGTTTTGCTTCACTCCCCAC
ACGGAGGAGGGGTGCCTGTCTGAGCACGCTGCCCTCGAGGAGGAGCTGCAACTGTGCAAG
GGGCTGGTCGAGGCACTCGAGACCAAGGTGACCCAGCAGGGGCTGAAGATGGTGGTGCCG
GACTGGACGGGGCCCAGATCCCCCCGGGACCCCTCACAGCAGGAACTGCCCCGGCTGTTG
TCGGCTGCCTGCAGGCTTCAGCTCAACGGGAACCTGCAGCTGGAGCTGGCGCAGGTGCTG
GCCCAGGAGAGGCCCAAGCTGCCAGAGGACCCTCTGCTCAGCGGCCTCCTGGACTCCCCG
GCACTCAAGGCCTGCCTGGACACTGCCGTGGAGAACATGCCCAGCCTGAAGATGAAGGTG
GTGGAGGTGCTGGCCGGCCACGGTCACCTGTATTCCCGCATCCCAGGCCTGCTCAGCCCC
CATCCCCTGCTGCAGCTGAGCTACACGGCCACCGACCGCCACCCCCAGGCCCTGGAGGCT
GCCCAGGCCGAGCTGCAGCAGCACGACGTTGCCCAGGGCCAGTGGGATCCCGCAGACCCT
GCCCCCAGCGCCCTGGGCAGCGCGGACCTCCTGGTGTGCAACTGTGCTGTGGCTGCCCTC
GGGGACCCGGCCTCAGCTCTCAGCAACATGGTGGCTGCCCTGAGAGAAGGGGGCTTTCTG
CTCCTGCACACACTGCTCCGGGGGCACCCTCGGGACATCGTGGCCTTCCTCACCTCCACT
GAGCCGCAGTATGGCCAGGGCATCCTGAGCCAGGACGCGTGGGAGAGCCTCTTCTCCAGG
GTGTCGCTGCGCCTGGTGGGCCTGAAGAAGTCCTTCTACGGCGCCACGCTCTTCCTGTGC
CGCCGGCCCACCCCGCAGGACAGCCCCATCTTCCTGCCGGTGGACGATACCAGCTTCCGC
TGGGTGGAGTCTCTGAAGGGCATCCTGGCTGACGAAGACTCTTCCCGGCCTGTGTGGCTG
AAGGCCATCAACTGTGCCACCTCGGGCGTGGTGGGCTTGGTGAACTGTCTCCGCCGAGAG
CCCGGCGGAACCGTCCGGTGTGTGCTGCTCTCCAACCTCAGCAGCACCTCCCACGTCCCG
GAGGTGGACCCGGGCTCCGCAGAACTGCAGAAGGTGTTGCAGGGAGACCTGGTGATGAAC
GTCTACCGCGACGGGGCCTGGGGGGTTTTCCGCCACTTCCTGCTGGAGGACAAGCCTGAG
GAGCCGACGGCACATGCCTTTGTGAGCACCCTCACCCGGGGGGACCTGTCCTCCATCCGC
TGGGTCTGCTCCTCGCTGCGCCATGCCCAGCCCACCTGCCCTGGCGCCCAGCTCTGCACG
GTCTACTACGCCTCCCTCAACTTCCGCGACATCATGCTGGCCACTGGCAAGCTGTCCCCT
GATGCCATCCCAGGGAAGTGGACCTCCCAGGACAGCCTGCTAGGTATGGAGTTCTCGGGC
CGAGACGCCAGCGGCAAGCGTGTGATGGGACTGGTGCCTGCCAAGGGCCTGGCCACCTCT
GTCCTGCTGTCACCGGACTTCCTCTGGGATGTGCCTTCCAACTGGACGCTGGAGGAGGCG
GCCTCGGTGCCTGTCGTCTACAGCACGGCCTACTACGCGCTGGTGGTGCGTGGGCGGGTG
CGCCCCGGGGAGACGCTGCTCATCCACTCGGGCTCGGGCGGCGTGGGCCAGGCCGCCATC
GCCATCGCCCTCAGTCTGGGCTGCCGCGTCTTCACCACCGTGGGGTCGGCTGAGAAGCGG
GCGTACCTCCAGGCCAGGTTCCCCCAGCTCGACAGCACCAGCTTCGCCAACTCCCGGGAC
ACATCCTTCGAGCAGCATGTGCTGTGGCACACGGGCGGGAAGGGCGTTGACCTGGTCTTG
AACTCCTTGGCGGAAGAGAAGCTGCAGGCCAGCGTGAGGTGCTTCGGTACGCACGGTCGC
TTCCTGGAAATTGGCAAATTCGACCTTTCTCAGAACCACCCGCTCGGCATGGCTATCTTC
CTGAAGAACGTGACATTCCACGGGGTCCTACTGGATGCGTTCTTCAACGAGAGCAGTGCT
GACTGGCGGGAGGTGTGGGCGCTTGTCGAGGCCGCCATCCGGGATGGGGTGGTACGGCCC
CTCAAGTGCACGGTGTTCCATGGGGCCCAGGTGGAGGACGCCTTCCGCTACATGGCCCAA
GGGAAGCACATTGGCAAAGTCGTCGTGCAGGTGCTTGCGGAGGAGCCGGCAGTGCTGAAG
GGGGCCAAACCCAAGCTGATGTCGGCCATCTCCAAGACCTTCTGCCCGGCCCACAAGAGC
TACATCATCGCTGGTGGTCTGGGTGGCTTCGGCCTGGAGTTGGCGCAGTGGCTGATACAG
CGTGGGGTGCAGAAGCTCGTGTTGACTTCTCGCTCCGGGATCCGGACAGGCTACCAGGCC
AAGCAGGTCCGCCGGTGGAGGCGCCAGGGGCTACAGGTGCAGGTGTCCACCAGCAACATC
AGCTCACTGGAGGGGGCCCGGGGCCTCATTGCCGAGGCGGCGCAGCTTGGGCCCGTGGGG
GGCGTCTTCAACCTGGCCGTGGTCTTGAGAGATGGCTTGCTGGAGAACCAGACCCCAGAG
TTCTTCCAGGACGTCTGCAAGCCCAAGTACAGCGGCACCCTGAACCTGGACAGGGTGACC
CGAGAGGCGTGCCCTGAGCTGGACTACTTTGTGGTCTTCTCCTCTGTGAGCTGCGGGCGT
GGCAATGCGGGACAGAGCAACTACGGCTTTGCCAATTCCGCCATGGAGCGTATCTGTGAG
AAACGCCGGCACGAAGGCCTCCCAGGCCTGGCCGTGCAGTGGGGCGCCATCGGCACCGTG
GGCATTTTGGTGGAGACGATGAGCACCAACGACACGATCGTCAGTGGCACGCTGCCCACG
CGCATTGGCGTCCTTGGCCTGGAGGTGCTGGACCTCTTCCTGAACCAGCCCCACATGGTC
CTGAGCAGCTTTGTGCTGGCTGAGAAGGCTGCGGCCTATAGGGACAGGGACAGCCAGCGG
GACCTGGTGGAGGCCGTGGCACACATCCTGGGCATCCGCGACTTGGCTGCTGTCAACCTG
GGCGGCTCACTGGCGGACCTGGGCCTGGACTCGCTCATGAGCGCGCCGGTGCGCCAGACG
CTGGAGCGTGAGCTCAACCTGGTGCTGTCCGTGCGCGAGGTGCGGCAACTCACGCTCCGG
AAACTGCAGGAGCTGTCCTCAAAGGCGGATGAAGCCAGCGAGCTGGCATGCCCCACGCCC
AAGGAGGATGGTCTGGCCCAGCAGCAGACTCAGCTGAACCTGCGCTCCCTGCTGGTGAAA
CCGGAGGGCCCCACCCTGATGCGGCTCAACTCCGTGCAGAGCTCGGAGCGGCCCCTGTTC
CTGGTGCACCCAATCGAGGCTACCACCGTGTTCCACAGCCTCGGTCCCGGTCTCAGCATC
CCCACCTATGGCCTGCAGTGCACCCCGGCTGCGCCCCTTGACAGCATCCACAGCCTGGCT
GCCTACTACATCGACTGCATCAGGCAGGTGCAGCCCGAGGGCCCCTACCGCGTGGCCGGC
TACTCCTACGGGGCCTGCGTGGCCTTTGAAATGTGCTCCCAGCTGCAGGCCCAGCAGAGC
CCAGCCCCCACCCACAACAGCCTCTTCCTGTTCGACGGCTCGCCCACCTACGTACTGGCC
TACACCCAGAGCTACCGGGCAAAGCTGACCCCAGGCTGTAAGGCTGAGGCTGAGACGGAG
GCCATATGCTTCTTCGTGCAGCAGTTCACGGACATGGAGCACAACAGGGTGCTGGAGGCG
CTGCTGCCGCTGAAGGGCCTAGAGGAGCGTGTGGCAGCCGCCGTGGACCTGATCATCAAG
AGCCACCAGGGCCTGGACCGCCAGGAGCTGAGCTTTGCGGCCCGGTCCTTCTACTACAGG
CTGCGTGCCGCTGACCAGTATACACCCAAGGCCAAGTACAGTGGCAACGTGATGCTACTG
CGGGCCAAGACGGGTGGCCGCTACGGCGAGGACCTGGGCGCGGACTACAACCTCTCCCAG
GTATGCGACGGGAAAGTATCCGTCCATATCATCGAGGGTGACCACCGCACGCTGCTGGAG
GGCAGCGGCCTGGAGTCCATCATCAGCATCATCCACAGCTCCCTGGCTGAGCCACGTGTG
AGTCGGGAGGGCTAG
Enzyme 5 GenBank Gene ID U26644 Link Image
Enzyme 5 GeneCard ID FASN Link Image
Enzyme 5 GenAtlas ID FASN Link Image
Enzyme 5 HGNC ID HGNC:3594 Link Image
Enzyme 5 Chromosome Location 17
Enzyme 5 Locus 17q25
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Jayakumar A, Tai MH, Huang WY, al-Feel W, Hsu M, Abu-Elheiga L, Chirala SS, Wakil SJ: Human fatty acid synthase: properties and molecular cloning. Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8695-9. [PubMed Link Image]
  2. Kuhajda FP, Jenner K, Wood FD, Hennigar RA, Jacobs LB, Dick JD, Pasternack GR: Fatty acid synthesis: a potential selective target for antineoplastic therapy. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6379-83. [PubMed Link Image]
  3. Semenkovich CF, Coleman T, Fiedorek FT Jr: Human fatty acid synthase mRNA: tissue distribution, genetic mapping, and kinetics of decay after glucose deprivation. J Lipid Res. 1995 Jul;36(7):1507-21. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5269
Enzyme 6 Name Hydroxymethylglutaryl-CoA synthase, mitochondrial precursor
Enzyme 6 Synonyms
  1. HMG-CoA synthase
  2. 3-hydroxy-3-methylglutaryl coenzyme A synthase
Enzyme 6 Gene Name HMGCS2
Enzyme 6 Protein Sequence >Hydroxymethylglutaryl-CoA synthase, mitochondrial precursor 
MQRLLTPVKRILQLTRAVQETSLTPARLLPVAHQRFSTASAVPLAKTDTWPKDVGILALE
VYFPAQYVDQTDLEKYNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERIQLP
WDSVGRLEVGTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWM
ESSSWDGRYAMVVCGDIAVYPSGNARPTGGAGAVAMLIGPKAPLALERGLRGTHMENVYD
FYKPNLASEYPIVDGKLSIQCYLRALDRCYTSYRKKIQNQWKQAGSDRPFTLDDLQYMIF
HTPFCKMVQKSLARLMFNDFLSASSDTQTSLYKGLEAFGGLKLEDTYTNKDLDKALLKAS
QDMFDKKTKASLYLSTHNGNMYTSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASF
FSFRVSQDAAPGSPLDKLVSSTSDLPKRLASRKCVSPEEFTEIMNQREQFYHKVNFSPPG
DTNSLFPGTWYLERVDEQHRRKYARRPV
Enzyme 6 Number of Residues 508
Enzyme 6 Molecular Weight 56636
Enzyme 6 Theoretical pI 8.28
Enzyme 6 GO Classification
Function
  • catalytic activity
  • hydroxymethylglutaryl-CoA synthase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
Process
  • acetyl-CoA metabolism
  • cellular metabolism
  • coenzyme metabolism
  • cofactor metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 6 General Function Lipid transport and metabolism
Enzyme 6 Specific Function This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase
Enzyme 6 Pathways
  • Butyrate Metabolism (map00650 Link Image)
  • Synthesis and Degradation of Ketone Bodies (map00072 Link Image)
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 6 Reactions
  • acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-17
Enzyme 6 Transmembrane Regions Not Available
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 619877 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P54868 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name HMCS2_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1527 bp 
ATGCAGCGTCTGTTGACTCCAGTGAAGCGCATTCTGCAACTGACAAGAGCGGTGCAGGAA
ACCTCCCTCACACCTGCTCGCCTGCTCCCAGTAGCCCACCAAAGGTTTTCTACAGCCTCT
GCTGTCCCCCTGGCCAAAACAGATACTTGGCCAAAGGACGTGGGCATCCTGGCCCTGGAG
GTCTACTTCCCAGCCCAATATGTGGACCAAACTGACCTGGAGAAGTATAACAATGTGGAA
GCAGGAAAGTATACAGTGGGCTTGGGCCAGACCCGTATGGGCTTCTGCTCAGTCCAAGAG
GACATCAACTCCCTGTGCCTGACGGTGGTGCAACGGCTGATGGAGCGCATACAGCTCCCA
TGGGACTCTGTGGGCAGGCTGGAAGTAGGCACTGAGACCATCATTGACAAGTCCAAAGCT
GTCAAAACAGTGCTCATGGAACTCTTCCAGGATTCAGGCAATACTGATATTGAGGGCATA
GATACCACCAATGCCTGCTACGGTGGTACTGCCTCCCTCTTCAATGCTGCCAACTGGATG
GAGTCCAGTTCCTGGGATGGTCGTTATGCCATGGTGGTCTGTGGAGACATTGCCGTCTAT
CCCAGTGGTAATGCTCGTCCCACAGGTGGGGCCGGAGCTGTGGCTATGCTGATTGGCCCA
AAGGCCCCTCTGGCCCTGGAGCGAGGGCTGAGGGGAACCCATATGGAGAATGTGTATGAC
TTCTACAAACCAAATTTGGCCTCGGAGTACCCAATAGTGGATGGGAAGCTTTCCATCCAG
TGCTACTTGCGGGCCTTGGATCGATGTTACACATCATACCGTAAAAAAATCCAGAATCAG
TGGAAGCAAGCTGGCAGCGATCGACCCTTCACCCTTGACGATTTACAGTATATGATCTTT
CATACACCCTTTTGCAAGATGGTCCAGAAGTCTCTGGCTCGCCTGATGTTCAATGACTTC
CTGTCAGCCAGCAGTGACACACAAACCAGCTTATATAAGGGGCTGGAGGCTTTCGGGGGG
CTAAAGCTGGAAGACACCTACACCAACAAGGACCTGGATAAAGCACTTCTAAAGGCCTCT
CAGGACATGTTCGACAAGAAAACCAAGGCTTCCCTTTACCTCTCCACTCACAATGGGAAC
ATGTACACCTCATCCCTGTACGGGTGCCTGGCCTCGCTTCTGTCCCACCACTCTGCCCAA
GAACTGGCTGGCTCCAGGATTGGTGCCTTCTCTTATGGCTCTGGTTTAGCAGCAAGTTTC
TTTTCATTTCGAGTATCCCAGGATGCTGCTCCAGGCTCTCCCCTGGACAAGTTGGTGTCC
AGCACATCAGACCTGCCAAAACGCCTAGCCTCCCGAAAGTGTGTGTCTCCTGAGGAGTTC
ACAGAAATAATGAACCAAAGAGAGCAATTCTACCATAAGGTGAATTTCTCCCCACCTGGT
GACACAAACAGCCTTTTCCCAGGTACTTGGTACCTGGAGCGAGTGGACGAGCAGCATCGC
CGAAAGTATGCCCGGCGTCCCGTCTAA
Enzyme 6 GenBank Gene ID X83618 Link Image
Enzyme 6 GeneCard ID HMGCS2 Link Image
Enzyme 6 GenAtlas ID HMGCS2 Link Image
Enzyme 6 HGNC ID HGNC:5008 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 1p13-p12
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Mascaro C, Buesa C, Ortiz JA, Haro D, Hegardt FG: Molecular cloning and tissue expression of human mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase. Arch Biochem Biophys. 1995 Mar 10;317(2):385-90. [PubMed Link Image]
  2. Boukaftane Y, Mitchell GA: Cloning and characterization of the human mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase gene. Gene. 1997 Aug 22;195(2):121-6. [PubMed Link Image]
  3. Boukaftane Y, Duncan A, Wang S, Labuda D, Robert MF, Sarrazin J, Schappert K, Mitchell GA: Human mitochondrial HMG CoA synthase: liver cDNA and partial genomic cloning, chromosome mapping to 1p12-p13, and possible role in vertebrate evolution. Genomics. 1994 Oct;23(3):552-9. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5272
Enzyme 7 Name Citrate synthase, mitochondrial precursor
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name CS
Enzyme 7 Protein Sequence >Citrate synthase, mitochondrial precursor 
MALLTAAARLLGTKNASCLVLAARHASASSTNLKDILADLIPKEQARIKTFRQQHGKTVV
GQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAKGGEEPLPEGLF
WLLVTGHIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESN
FARAYAQGISRTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSGIGAIDSNLDWSHNF
TNMLGYTDHQFTELTRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPL
HGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQ
REFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYY
TVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDSKSG
Enzyme 7 Number of Residues 466
Enzyme 7 Molecular Weight 51713
Enzyme 7 Theoretical pI 8.53
Enzyme 7 GO Classification
Function
  • catalytic activity
  • citrate (Si)-synthase activity
  • transferase activity
  • transferase activity, transferring acyl groups
  • transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
Process
  • cellular metabolism
  • energy derivation by oxidation of organic compounds
  • generation of precursor metabolites and energy
  • main pathways of carbohydrate metabolism
  • metabolism
  • physiological process
  • tricarboxylic acid cycle
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 7 General Function Energy production and conversion
Enzyme 7 Specific Function Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA
Enzyme 7 Pathways
Enzyme 7 Reactions
  • acetyl-CoA + H2O + oxaloacetate = citrate + CoA
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-16
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 3288815 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID O75390 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name CISY_HUMAN Link Image
Enzyme 7 PDB ID 4CTS Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >1401 bp 
ATGGCTTTACTTACTGCGGCCGCCCGGCTCTTGGGAACCAAGAATGCATCTTGTCTTGTT
CTTGCAGCCCGGCATGCTAGTGCTTCCTCCACGAATTTGAAAGACATATTGGCTGACCTG
ATACCTAAGGAGCAGGCCAGAATTAAGACTTTCAGGCAGCAACATGGCAAGACGGTGGTG
GGCCAAATCACTGTGGACATGATGTATGGTGGCATGAGAGGCATGAAGGGATTGGTGTAT
GAAACATCAGTTCTTGATCCTGATGAGGGCATCCGTTTCCGAGGCTTTAGTATCCCTGAA
TGCCAGAAACTGCTACCCAAGGCTAAGGGTGGGGAAGAACCCCTGCCTGAGGGCTTATTT
TGGCTGCTGGTAACTGGATGTATCCCAACAGAGGAACAGGTATCTTGGCTCTCAAAAGAG
TGGGCAAAGAGGGCAGCTCTGCCTTCCCATGTGGTCACCATGCTGGACAACTTTCCCACC
AATCTACACCCCATGTCTCAGCTGAGTGCAGCTGTTACAGCCCTCAACAGTGAAAGTAAC
TTTGCCCAAGCATATGCACGGGGTATCAGCCGAACCAAGTACTGGGAGTTGATTTATGAA
GATTCTGTGGATCTAATAGCAAAGCTACCTTGTGTTGCAGCAAAGATCTACCGAAATCTC
TACTGGGAAGGCAGCGGTATTGGGGCCATTGACTCTAACCTGGACTGGTCTCACAATTTC
ACCAACATGTTAGGCTATACTGATCATCAGTTCACTGAGCTCATGCGCCTGTACCTCACC
ATCCACAGTGACCATGAGGGTGGCAATGTAAGTGCCCATACCAGCCACTTGGTGGGCAGT
GCCCTTTCCGACCCTTACCTGTCCTTTGCAGCAGCCATGAACGGGCTGGCAGGGCCTCTC
CATGGACTGGCAAATCAGGAAGTGCTTGTCTGGCTAACACAGCTGCAGAAGGAAGTTGGC
AAAGATGTGTCAGATGAGAAGTTACGAGACTACATCTGGAACACACTCAACTCAGGACGG
GTTGTTCCAGGCTATGGCCATGCAGTACTAAGGAAGACTGATCCGCGATATACCTGTCAG
CGAGAGTTTGCTCTGAAACACCTGCCTAATGACCCCATGTTTAAGTTGGTTGCTCAGCTG
TACAAGATTGTGCCCAATGTCCTCTTAGAGCAGGGTAAAGCCAAGAATCCTTGGCCCAAT
GTAGATGCTCACAGTGGGGTGCTGCTCCAGTATTATGGCATGACGGAGATGAATTACTAC
ACGGTCCTGTTTGGGGTGTCACGAGCATTGGGTGTACTGGCACAGCTCATCTGGAGCCGA
GCCTTAGGCTTCCCTCTAGAAAGGCCCAAGTCCATGAGCACAGAGGGTCTGATGAAGTTT
GTGGACTCTAAGTCAGGGTAA
Enzyme 7 GenBank Gene ID AF047042 Link Image
Enzyme 7 GeneCard ID CS Link Image
Enzyme 7 GenAtlas ID CS Link Image
Enzyme 7 HGNC ID HGNC:2422 Link Image
Enzyme 7 Chromosome Location 12
Enzyme 7 Locus 12q13.2-q13.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Goldenthal MJ, Marin-Garcia J, Ananthakrishnan R: Cloning and molecular analysis of the human citrate synthase gene. Genome. 1998 Oct;41(5):733-8. [PubMed Link Image]
  2. Liu Q, Yu L, Han XF, Fu Q, Zhang JX, Tang H, Zhao SY: [Cloning and tissue expression pattern analysis of the human citrate synthase cDNA] Shi Yan Sheng Wu Xue Bao. 2000 Sep;33(3):207-14. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5285
Enzyme 8 Name Acyl-protein thioesterase 1
Enzyme 8 Synonyms
  1. Lysophospholipase 1
  2. Lysophospholipase I
Enzyme 8 Gene Name LYPLA1
Enzyme 8 Protein Sequence >Acyl-protein thioesterase 1 
MCGNNMSTPLPAIVPAARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAPVRP
VTLNMNVAMPSWFDIIGLSPDSQEDESGIKQAAENIKALIDQEVKNGIPSNRIILGGFSQ
GGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIGGANRDISILQCHGDCDPLVPLM
FGSLTVEKLKTLVNPANVTFKTYEGMMHSSCQQEMMDVKQFIDKLLPPID
Enzyme 8 Number of Residues 230
Enzyme 8 Molecular Weight 24670
Enzyme 8 Theoretical pI 6.77
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Also has low lysophospholipase activity
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 3415123 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID O75608 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name LYPA1_HUMAN Link Image
Enzyme 8 PDB ID 1FJ2 Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >693 bp 
ATGTGCGGCAATAACATGTCAACCCCGCTGCCCGCCATCGTGCCCGCCGCCCGGAAGGCC
ACCGCTGCGGTGATTTTCCTGCATGGATTGGGAGATACTGGGCACGGATGGGCAGAAGCC
TTTGCAGGTATCAGAAGTTCACATATCAAATATATCTGCCCGCATGCGCCTGTTAGGCCT
GTTACATTAAATATGAACGTGGCTATGCCTTCATGGTTTGATATTATTGGGCTTTCACCA
GATTCACAGGAGGATGAATCTGGGATTAAACAGGCAGCAGAAAATATAAAAGCTTTGATT
GATCAAGAAGTGAAGAATGGCATTCCTTCTAACAGAATTATTTTGGGAGGGTTTTCTCAG
GGAGGAGCTTTATCTTTATATACTGCCCTTACCACACAGCAGAAACTGGCAGGTGTCACT
GCACTCAGTTGCTGGCTTCCACTTCGGGCTTCCTTTCCACAGGGTCCTATCGGTGGTGCT
AATAGAGATATTTCTATTCTCCAGTGCCACGGGGATTGTGACCCTTTGGTTCCCCTGATG
TTTGGTTCTCTTACGGTGGAAAAACTAAAAACATTGGTGAATCCAGCCAATGTGACCTTT
AAAACCTATGAAGGTATGATGCACAGTTCGTGTCAACAGGAAATGATGGATGTCAAGCAA
TTCATTGATAAACTCCTACCTCCAATTGATTGA
Enzyme 8 GenBank Gene ID AF081281 Link Image
Enzyme 8 GeneCard ID LYPLA1 Link Image
Enzyme 8 GenAtlas ID LYPLA1 Link Image
Enzyme 8 HGNC ID HGNC:6737 Link Image
Enzyme 8 Chromosome Location 8
Enzyme 8 Locus 8q11.23
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Devedjiev Y, Dauter Z, Kuznetsov SR, Jones TL, Derewenda ZS: Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A. Structure. 2000 Nov 15;8(11):1137-46. [PubMed Link Image]
  2. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5287
Enzyme 9 Name Calcium-dependent phospholipase A2 precursor
Enzyme 9 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase
  2. PLA2-10
  3. Group V phospholipase A2
Enzyme 9 Gene Name PLA2G5
Enzyme 9 Protein Sequence >Calcium-dependent phospholipase A2 precursor 
MKGLLPLAWFLACSVPAVQGGLLDLKSMIEKVTGKNALTNYGFYGCYCGWGGRGTPKDGT
DWCCWAHDHCYGRLEEKGCNIRTQSYKYRFAWGVVTCEPGPFCHVNLCACDRKLVYCLKR
NLRSYNPQYQYFPNILCS
Enzyme 9 Number of Residues 138
Enzyme 9 Molecular Weight 15674
Enzyme 9 Theoretical pI 8.48
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
—
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. 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 9 Pathways
Enzyme 9 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-20
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 460915 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P39877 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name PA2G5_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >417 bp 
ATGAAAGGCCTCCTCCCACTGGCTTGGTTCCTGGCTTGTAGTGTGCCTGCTGTGCAAGGA
GGCTTGCTGGACCTAAAATCAATGATCGAGAAGGTGACAGGGAAGAACGCCCTGACAAAC
TACGGCTTCTACGGCTGTTACTGCGGCTGGGGCGGCCGAGGAACCCCCAAGGATGGCACC
GATTGGTGCTGTTGGGCGCATGACCACTGCTATGGGCGGCTGGAGGAGAAGGGCTGCAAC
ATTCGCACACAGTCCTACAAATACAGATTCGCGTGGGGCGTGGTCACCTGCGAGCCCGGG
CCCTTCTGCCATGTGAACCTCTGTGCCTGTGACCGGAAGCTCGTCTACTGCCTCAAGAGA
AACCTACGGAGCTACAACCCACAGTACCAATACTTTCCCAACATCCTCTGCTCCTAG
Enzyme 9 GenBank Gene ID U03090 Link Image
Enzyme 9 GeneCard ID PLA2G5 Link Image
Enzyme 9 GenAtlas ID PLA2G5 Link Image
Enzyme 9 HGNC ID HGNC:9038 Link Image
Enzyme 9 Chromosome Location 1
Enzyme 9 Locus 1p36-p34
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 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 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5288
Enzyme 10 Name Group IIF secretory phospholipase A2 precursor
Enzyme 10 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase GIIF
  2. GIIF sPLA2
  3. sPLA(2-IIF
Enzyme 10 Gene Name PLA2G2F
Enzyme 10 Protein Sequence >Group IIF secretory phospholipase A2 precursor 
MKKFFTVAILAGSVLSTAHGSLLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEV
DWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTEIVCSDLNKTECDKQTCMCDKNMVLC
LMNQTYREEYRGFLNVYCQGPTPNCSIYEPPPEEVTCSHQSPAPPAPP
Enzyme 10 Number of Residues 168
Enzyme 10 Molecular Weight 18658
Enzyme 10 Theoretical pI 4.94
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 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 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 12276060 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q9BZM2 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name PA2GF_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >507 bp 
ATGAAGAAGTTCTTCACCGTGGCCATCCTTGCTGGCAGCGTTCTGTCCACAGCTCACGGC
AGCCTGCTCAACCTGAAGGCCATGGTGGAGGCCGTCACAGGGAGGAGCGCCATCCTGTCC
TTCGTGGGCTACGGTTGCTACTGTGGGCTGGGGGGCCGTGGCCAGCCCAAGGATGAGGTG
GACTGGTGCTGCCACGCCCACGACTGCTGCTACCAGGAACTCTTTGACCAAGGCTGTCAC
CCCTATGTGGACCACTATGATCACACCATCGAGAACAACACTGAGATAGTCTGCAGTGAC
CTCAACAAGACAGAGTGTGACAAGCAGACATGCATGTGTGACAAGAACATGGTTCTGTGC
CTCATGAACCAGACGTACCGAGAGGAGTACCGTGGCTTCCTCAATGTCTACTGCCAGGGC
CCCACGCCCAACTGCAGCATCTATGAACCGCCCCCTGAGGAGGTCACCTGCAGTCACCAA
TCCCCAGCGCCCCCCGCCCCTCCCTAG
Enzyme 10 GenBank Gene ID AF306566 Link Image
Enzyme 10 GeneCard ID PLA2G2F Link Image
Enzyme 10 GenAtlas ID PLA2G2F Link Image
Enzyme 10 HGNC ID HGNC:30040 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 1p35
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 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 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5289
Enzyme 11 Name Cytosolic phospholipase A2
Enzyme 11 Synonyms
  1. cPLA2
  2. Phospholipase A2 group IVA[Includes: Phospholipase A2
  3. Phosphatidylcholine 2- acylhydrolase
  4. Lysophospholipase
Enzyme 11 Gene Name PLA2G4A
Enzyme 11 Protein Sequence >Cytosolic phospholipase A2 
MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRT
RHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFTVSSMKVGEKKEV
PFIFNQVTEMVLEMSLEVCSCPDLRFSMALCDQEKTFRQQRKEHIRESMKKLLGPKNSEG
LHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSH
PDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIG
ETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYG
TFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSRGSTMEEE
LENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFN
TREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDV
KSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMN
KLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHFVLANINFRKYKAPGVPRETE
EEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRR
QNPSRCSVSLSNVEARRFFNKEFLSKPKA
Enzyme 11 Number of Residues 749
Enzyme 11 Molecular Weight 85212
Enzyme 11 Theoretical pI 5.03
Enzyme 11 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 11 General Function Not Available
Enzyme 11 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 11 Pathways
Enzyme 11 Reactions
  • 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 190007 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P47712 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name PA24A_HUMAN Link Image
Enzyme 11 PDB ID 1CJY Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 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 11 GenBank Gene ID M72393 Link Image
Enzyme 11 GeneCard ID PLA2G4A Link Image
Enzyme 11 GenAtlas ID PLA2G4A Link Image
Enzyme 11 HGNC ID HGNC:9035 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 1q25
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 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 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5290
Enzyme 12 Name Phospholipase A2 precursor
Enzyme 12 Synonyms
  1. Phosphatidylcholine 2- acylhydrolase
  2. Group IB phospholipase A2
Enzyme 12 Gene Name PLA2G1B
Enzyme 12 Protein Sequence >Phospholipase A2 precursor 
MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPV
DELDKCCQTHDNCYDQAKKLDSCKFLLDNPYTHTYSYSCSGSAITCSSKNKECEAFICNC
DRNAAICFSKAPYNKAHKNLDTKKYCQS
Enzyme 12 Number of Residues 148
Enzyme 12 Molecular Weight 16360
Enzyme 12 Theoretical pI 7.91
Enzyme 12 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 12 General Function Not Available
Enzyme 12 Specific Function PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides
Enzyme 12 Pathways
Enzyme 12 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-15
Enzyme 12 Transmembrane Regions Not Available
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 387025 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P04054 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name PA21B_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >447 bp 
ATGAAACTCCTTGTGCTAGCTGTGCTGCTCACAGTGGCCGCCGCCGACAGCGGCATCAGC
CCTCGGGCCGTGTGGCAGTTCCGCAAAATGATCAAGTGCGTGATCCCGGGGAGTGACCCC
TTCTTGGAATACAACAACTACGGCTGCTACTGTGGCTTGGGGGGCTCAGGCACCCCCGTG
GATGAACTGGACAAGTGCTGCCAGACACATGACAACTGCTACGACCAGGCCAAGAAGCTG
GACAGCTGTAAATTTCTGCTGGACAACCCGTACACCCACACCTATTCATACTCGTGCTCT
GGCTCGGCAATCACCTGTAGCAGCAAAAACAAAGAGTGTGAGGCCTTCATTTGCAACTGC
GACCGCAACGCTGCCATCTGCTTTTCAAAAGCTCCATATAACAAGGCACACAAGAACCTG
GACACCAAGAAGTATTGTCAGAGTTGA
Enzyme 12 GenBank Gene ID M21056 Link Image
Enzyme 12 GeneCard ID PLA2G1B Link Image
Enzyme 12 GenAtlas ID PLA2G1B Link Image
Enzyme 12 HGNC ID HGNC:9030 Link Image
Enzyme 12 Chromosome Location 12
Enzyme 12 Locus 12q23-q24.1
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 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 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5291
Enzyme 13 Name Group XIIB secretory phospholipase A2-like protein precursor
Enzyme 13 Synonyms
  1. Group XIII secretory phospholipase A2-like protein
  2. GXIII sPLA2-like
  3. GXIIB
Enzyme 13 Gene Name PLA2G12B
Enzyme 13 Protein Sequence >Group XIIB secretory phospholipase A2-like protein precursor 
MKLASGFLVLWLSLGGGLAQSDTSPDTEESYSDWGLRHLRGSFESVNSYFDSFLELLGGK
NGVCQYRCRYGKAPMPRPGYKPQEPNGCGSYFLGLKVPESMDLGIPAMTKCCNQLDVCYD
TCGANKYRCDAKFRWCLHSICSDLKRSLGFVSKVEAACDSLVDTVFNTVWTLGCRPFMNS
QRAACICAEEEKEEL
Enzyme 13 Number of Residues 195
Enzyme 13 Molecular Weight 21659
Enzyme 13 Theoretical pI 5.81
Enzyme 13 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 13 General Function Not Available
Enzyme 13 Specific Function Not known; does not seem to have catalytic activity
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions Not Available
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • 1-19
Enzyme 13 Transmembrane Regions Not Available
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 13560707 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q9BX93 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name PG12B_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >585 bp 
ATGAAGCTGGCCAGTGGCTTCTTGGTTTTGTGGCTCAGCCTTGGGGGTGGCCTGGCTCAG
AGCGACACGAGCCCTGACACGGAGGAGTCCTATTCAGACTGGGGCCTTCGGCACCTCCGG
GGAAGCTTTGAATCCGTCAATAGCTACTTCGATTCTTTTCTGGAGCTGCTGGGAGGGAAG
AATGGAGTCTGTCAGTACAGGTGCCGATATGGAAAGGCACCAATGCCCAGACCTGGCTAC
AAGCCCCAAGAGCCCAATGGCTGCGGCTCCTATTTCCTGGGTCTCAAGGTACCAGAAAGT
ATGGACTTGGGCATTCCAGCAATGACAAAGTGCTGCAACCAGCTGGATGTCTGTTATGAC
ACTTGCGGTGCCAACAAATATCGCTGTGATGCAAAATTCCGATGGTGTCTCCACTCGATC
TGCTCTGACCTTAAGCGGAGTCTGGGCTTTGTCTCCAAAGTGGAAGCCTGTGATTCCCTG
GTTGACACTGTGTTCAACACCGTGTGGACCTTGGGCTGCCGCCCCTTTATGAATAGTCAG
CGGGCAGCTTGCATCTGTGCAGAGGAGGAGAAGGAAGAGTTATGA
Enzyme 13 GenBank Gene ID AF349540 Link Image
Enzyme 13 GeneCard ID PLA2G12B Link Image
Enzyme 13 GenAtlas ID PLA2G12B Link Image
Enzyme 13 HGNC ID HGNC:18555 Link Image
Enzyme 13 Chromosome Location 10
Enzyme 13 Locus 10q22.1
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5292
Enzyme 14 Name Group 10 secretory phospholipase A2 precursor
Enzyme 14 Synonyms
  1. Group X secretory phospholipase A2
  2. Phosphatidylcholine 2-acylhydrolase GX
  3. GX sPLA2
  4. sPLA2-X
Enzyme 14 Gene Name PLA2G10
Enzyme 14 Protein Sequence >Group 10 secretory phospholipase A2 precursor 
MLLLLLPSLLLLLLLPGPGSGEASRILRVHRRGILELAGTVGCVGPRTPIAYMKYGCFCG
LGGHGQPRDAIDWCCHGHDCCYTRAEEAGCSPKTERYSWQCVNQSVLCGPAENKCQELLC
KCDQEIANCLAQTEYNLKYLFYPQFLCEPDSPKCD
Enzyme 14 Number of Residues 155
Enzyme 14 Molecular Weight 17132
Enzyme 14 Theoretical pI 6.46
Enzyme 14 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 14 General Function Not Available
Enzyme 14 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 14 Pathways
Enzyme 14 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-21
Enzyme 14 Transmembrane Regions Not Available
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 2289237 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID O15496 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name PA2GX_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >498 bp 
ATGGGGCCGCTACCTGTGTGCCTGCCAATCATGCTGCTCCTGCTACTGCCGTCGCTGCTG
CTGCTGCTGCTTCTACCTGGCCCCGGGTCCGGCGAGGCCTCCAGGATATTACGTGTGCAC
CGGCGTGGGATCCTGGAACTGGCAGGAACTGTGGGTTGTGTTGGTCCCCGAACCCCCATC
GCCTATATGAAATATGGTTGCTTTTGTGGCTTGGGAGGCCATGGCCAGCCCCGCGATGCC
ATTGACTGGTGCTGCCATGGCCACGACTGTTGTTACACTCGAGCTGAGGAGGCCGGCTGC
AGCCCCAAGACAGAGCGCTACTCCTGGCAGTGCGTCAATCAGAGCGTCCTGTGCGGACCG
GCAGAGAACAAATGCCAAGAACTGTTGTGCAAGTGTGACCAGGAGATTGCTAACTGCTTA
GCCCAAACTGAGTACAACTTAAAGTACCTCTTCTACCCCCAGTTCCTATGTGAGCCGGAC
TCGCCCAAGTGTGACTGA
Enzyme 14 GenBank Gene ID U95301 Link Image
Enzyme 14 GeneCard ID PLA2G10 Link Image
Enzyme 14 GenAtlas ID PLA2G10 Link Image
Enzyme 14 HGNC ID HGNC:9029 Link Image
Enzyme 14 Chromosome Location 16
Enzyme 14 Locus 16p13.1-p12
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5294
Enzyme 15 Name Group IIE secretory phospholipase A2 precursor
Enzyme 15 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase GIIE
  2. GIIE sPLA2
  3. sPLA(2-IIE
Enzyme 15 Gene Name PLA2G2E
Enzyme 15 Protein Sequence >Group IIE secretory phospholipase A2 precursor 
MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDW
CCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNL
GTYNRKYAHYPNKLCTGPTPPC
Enzyme 15 Number of Residues 142
Enzyme 15 Molecular Weight 15989
Enzyme 15 Theoretical pI 8.28
Enzyme 15 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 15 General Function Not Available
Enzyme 15 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 15 Pathways
Enzyme 15 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-19
Enzyme 15 Transmembrane Regions Not Available
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 7108923 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q9NZK7 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name PA2GE_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >429 bp 
ATGAAATCTCCCCACGTGCTGGTGTTCCTTTGCCTCCTGGTGGCTCTGGTCACCGGGAAC
CTGGTTCAGTTTGGGGTGATGATCGAGAAGATGACAGGCAAGTCCGCCCTGCAGTACAAC
GACTATGGCTGTTACTGCGGCATCGGTGGCTCCCACTGGCCGGTGGACCAGACTGACTGG
TGCTGCCACGCCCACGACTGCTGCTACGGGCGTCTGGAGAAGCTGGGCTGTGAGCCCAAA
CTGGAAAAGTATCTTTTCTCTGTCAGCGAACGTGGCATTTTCTGCGCCGGCAGGACCACC
TGCCAGCGGCTGACCTGCGAGTGTGACAAGAGGGCTGCCCTCTGCTTTCGCCGCAACCTG
GGCACCTACAACCGCAAATATGCCCATTATCCCAACAAGCTGTGCACCGGGCCCACCCCG
CCCTGCTGA
Enzyme 15 GenBank Gene ID AF189279 Link Image
Enzyme 15 GeneCard ID PLA2G2E Link Image
Enzyme 15 GenAtlas ID PLA2G2E Link Image
Enzyme 15 HGNC ID HGNC:13414 Link Image
Enzyme 15 Chromosome Location 1
Enzyme 15 Locus 1p36.13
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 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 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5295
Enzyme 16 Name Acyl-protein thioesterase 2
Enzyme 16 Synonyms
  1. Lysophospholipase II
  2. LPL- I
Enzyme 16 Gene Name LYPLA2
Enzyme 16 Protein Sequence >Acyl-protein thioesterase 2 
MCGNTMSVPLLTDAATVSGAERETAAVIFLHGLGDTGHSWADALSTIRLPHVKYICPHAP
RIPVTLNMKMVMPSWFDLMGLSPDAPEDEAGIKKAAENIKALIEHEMKNGIPANRIVLGG
FSQGGALSLYTALTCPHPLAGIVALSCWLPLHRAFPQAANGSAKDLAILQCHGELDPMVP
VRFGALTAEKLRSVVTPARVQFKTYPGVMHSSCPQEMAAVKEFLEKLLPPV
Enzyme 16 Number of Residues 231
Enzyme 16 Molecular Weight 24737
Enzyme 16 Theoretical pI 7.25
Enzyme 16 GO Classification Not Available
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function May hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has lysophospholipase activity
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 3859560 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID O95372 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name LYPA2_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >696 bp 
ATGTGTGGTAACACCATGTCTGTGCCCCTGCTCACCGATGCTGCCACCGTGTCTGGAGCT
GAGCGGGAAACGGCCGCGGTTATTTTTTTACATGGACTTGGAGACACAGGGCACAGCTGG
GCTGACGCCCTCTCCACCATCCGGCTCCCTCACGTCAAGTACATCTGTCCCCATGCGCCT
AGGATCCCTGTGACCCTCAACATGAAGATGGTGATGCCCTCCTGGTTTGACCTGATGGGG
CTGAGTCCAGATGCCCCAGAGGACGAGGCTGGCATCAAGAAGGCAGCAGAGAACATCAAG
GCCTTGATTGAGCATGAAATGAAGAACGGGATCCCTGCCAATCGAATCGTCCTGGGAGGC
TTTTCACAGGGCGGGGCCCTGTCCCTCTACACGGCCCTCACCTGCCCCCACCCTCTGGCT
GGCATCGTGGCGTTGAGCTGCTGGCTGCCTCTGCACCGGGCCTTCCCCCAGGCAGCTAAT
GGCAGTGCCAAGGACCTGGCCATACTCCAGTGCCATGGGGAGCTGGACCCCATGGTGCCC
GTACGGTTTGGGGCCCTGACGGCTGAGAAGCTCCGGTCTGTTGTCACACCTGCCAGGGTC
CAGTTCAAGACATACCCGGGTGTCATGCACAGCTCCTGTCCTCAGGAGATGGCAGCTGTG
AAGGAATTTCTTGAGAAGCTGCTGCCTCCTGTCTAA
Enzyme 16 GenBank Gene ID AF098668 Link Image
Enzyme 16 GeneCard ID LYPLA2 Link Image
Enzyme 16 GenAtlas ID LYPLA2 Link Image
Enzyme 16 HGNC ID HGNC:6738 Link Image
Enzyme 16 Chromosome Location 1
Enzyme 16 Locus 1p36.12-p35.1
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References Not Available
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5299
Enzyme 17 Name Eosinophil lysophospholipase
Enzyme 17 Synonyms
  1. Charcot-Leyden crystal protein
  2. Lysolecithin acylhydrolase
  3. CLC
  4. Galectin-10
Enzyme 17 Gene Name CLC
Enzyme 17 Protein Sequence >Eosinophil lysophospholipase 
MSLLPVPYTEAASLSTGSTVTIKGRPLVCFLNEPYLQVDFHTEMKEESDIVFHFQVCFGR
RVVMNSREYGAWKQQVESKNMPFQDGQEFELSISVLPDKYQVMVNGQSSYTFDHRIKPEA
VKMVQVWRDISLTKFNVSYLKR
Enzyme 17 Number of Residues 142
Enzyme 17 Molecular Weight 16481
Enzyme 17 Theoretical pI 7.50
Enzyme 17 GO Classification
Function
  • binding
  • carbohydrate binding
  • sugar binding
Process
—
Component
—
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function May have both lysophospholipase and carbohydrate-binding activities
Enzyme 17 Pathways
Enzyme 17 Reactions
  • 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 187274 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q05315 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name LPPL_HUMAN Link Image
Enzyme 17 PDB ID 1QKQ Link Image
Enzyme 17 PDB File Show
Enzyme 17 3D Structure
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >429 bp 
ATGTCCCTGCTACCCGTGCCATACACAGAGGCTGCCTCTTTGTCTACTGGTTCTACTGTG
ACAATCAAAGGGCGACCACTTGTCTGTTTCTTGAATGAACCATATCTGCAGGTGGATTTC
CACACTGAGATGAAGGAGGAATCAGACATTGTCTTCCATTTCCAAGTGTGCTTTGGTCGT
CGTGTGGTCATGAACAGCCGTGAGTATGGGGCCTGGAAGCAGCAGGTGGAATCCAAGAAC
ATGCCCTTTCAGGATGGCCAAGAATTTGAACTGAGCATCTCAGTGCTGCCAGATAAGTAC
CAGGTAATGGTCAATGGCCAATCCTCTTACACCTTTGACCATAGAATCAAGCCTGAGGCT
GTGAAGATGGTGCAAGTGTGGAGAGATATCTCCCTGACCAAATTTAATGTCAGCTATTTA
AAGAGATAA
Enzyme 17 GenBank Gene ID L01664 Link Image
Enzyme 17 GeneCard ID CLC Link Image
Enzyme 17 GenAtlas ID CLC Link Image
Enzyme 17 HGNC ID HGNC:2014 Link Image
Enzyme 17 Chromosome Location 19
Enzyme 17 Locus 19q13.1
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Ackerman SJ, Corrette SE, Rosenberg HF, Bennett JC, Mastrianni DM, Nicholson-Weller A, Weller PF, Chin DT, Tenen DG: Molecular cloning and characterization of human eosinophil Charcot-Leyden crystal protein (lysophospholipase). Similarities to IgE binding proteins and the S-type animal lectin superfamily. J Immunol. 1993 Jan 15;150(2):456-68. [PubMed Link Image]
  2. Mastrianni DM, Eddy RL, Rosenberg HF, Corrette SE, Shows TB, Tenen DG, Ackerman SJ: Localization of the human eosinophil Charcot-Leyden crystal protein (lysophospholipase) gene (CLC) to chromosome 19 and the human ribonuclease 2 (eosinophil-derived neurotoxin) and ribonuclease 3 (eosinophil cationic protein) genes (RNS2 and RNS3) to chromosome 14. Genomics. 1992 May;13(1):240-2. [PubMed Link Image]
  3. Dyer KD, Handen JS, Rosenberg HF: The genomic structure of the human Charcot-Leyden crystal protein gene is analogous to those of the galectin genes. Genomics. 1997 Mar 1;40(2):217-21. [PubMed Link Image]
  4. Leonidas DD, Elbert BL, Zhou Z, Leffler H, Ackerman SJ, Acharya KR: Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins. Structure. 1995 Dec 15;3(12):1379-93. [PubMed Link Image]
  5. Swaminathan GJ, Leonidas DD, Savage MP, Ackerman SJ, Acharya KR: Selective recognition of mannose by the human eosinophil Charcot-Leyden crystal protein (galectin-10): a crystallographic study at 1.8 A resolution. Biochemistry. 1999 Oct 19;38(42):13837-43. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5302
Enzyme 18 Name Group IID secretory phospholipase A2 precursor
Enzyme 18 Synonyms
  1. Phosphatidylcholine 2-acylhydrolase GIID
  2. GIID sPLA2
  3. PLA2IID
  4. sPLA(2-IID
  5. Secretory-type PLA, stroma-associated homolog
Enzyme 18 Gene Name PLA2G2D
Enzyme 18 Protein Sequence >Group IID secretory phospholipase A2 precursor 
MELALLCGLVVMAGVIPIQGGILNLNKMVKQVTGKMPILSYWPYGCHCGLGGRGQPKDAT
DWCCQTHDCCYDHLKTQGCSIYKDYYRYNFSQGNIHCSDKGSWCEQQLCACDKEVAFCLK
RNLDTYQKRLRFYWRPHCRGQTPGC
Enzyme 18 Number of Residues 145
Enzyme 18 Molecular Weight 16546
Enzyme 18 Theoretical pI 8.28
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
  • ion binding
  • lipase activity
  • phospholipase A2 activity
  • phospholipase activity
Process
  • lipid catabolism
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
—
Enzyme 18 General Function Not Available
Enzyme 18 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 18 Pathways
Enzyme 18 Reactions
  • phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-20
Enzyme 18 Transmembrane Regions Not Available
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 5771420 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q9UNK4 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name PA2GD_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >438 bp 
ATGGAACTTGCACTGCTGTGTGGGCTGGTGGTGATGGCTGGTGTGATTCCAATCCAGGGC
GGGATCCTGAACCTGAACAAGATGGTCAAGCAAGTGACTGGGAAAATGCCCATCCTCTCC
TACTGGCCCTACGGCTGTCACTGCGGACTAGGTGGCAGAGGCCAACCCAAAGATGCCACG
GACTGGTGCTGCCAGACCCATGACTGCTGCTATGACCACCTGAAGACCCAGGGGTGCGGC
ATCTACAAGGACTATTACAGATACAACTTTTCCCAGGGGAACATCCACTGCTCTGACAAG
GGAAGCTGGTGTGAGCAGCAGCTGTGTGCCTGTGACAAGGAGGTGGCCTTCTGCCTGAAG
CGCAACCTGGACACCTACCAGAAGCGACTGCGTTTCTACTGGCGGCCCCACTGCCGGGGG
CAGACCCCTGGGTGCTAG
Enzyme 18 GenBank Gene ID AF112982 Link Image
Enzyme 18 GeneCard ID PLA2G2D Link Image
Enzyme 18 GenAtlas ID PLA2G2D Link Image
Enzyme 18 HGNC ID HGNC:9033 Link Image
Enzyme 18 Chromosome Location 1
Enzyme 18 Locus 1p36.12
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 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 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5309
Enzyme 19 Name Phospholipase D2
Enzyme 19 Synonyms
  1. PLD 2
  2. Choline phosphatase 2
  3. Phosphatidylcholine-hydrolyzing phospholipase D2
  4. PLD1C
  5. hPLD2
Enzyme 19 Gene Name PLD2
Enzyme 19 Protein Sequence >Phospholipase D2 
MTATPESLFPTGDELDSSQLQMESDEVDTLKEGEDPADRMHPFLAIYELQSLKVHPLVFA
PGVPVTAQVVGTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKKYRHFQELHRDLLRHKVL
MSLLPLARFAVAYSPARDAGNREMPSLPRAGPEGSTRHAASKQKYLENYLNRLLTMSFYR
NYHAMTEFLEVSQLSFIPDLGRKGLEGMIRKRSGGHRVPGLTCCGRDQVCYRWSKRWLVV
KDSFLLYMCLETGAISFVQLFDPGFEVQVGKRSTEARHGVRIDTSHRSLILKCSSYRQAR
WWAQEITELAQGPGRDFLQLHRHDSYAPPRPGTLARWFVNGAGYFAAVADAILRAQEEIF
ITDWWLSPEVYLKRPAHSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINSGYSKRAL
MLLHPNIKVMRHPDQVTLWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDLGDSSE
SAASQPPTPRPDSPATPDLSHNQFFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPW
RDVGVVVHGLPARDLARHFIQRWNFTKTTKAKYKTPTYPYLLPKSTSTANQLPFTLPGGQ
CTTVQVLRSVDRWSAGTLENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDE
IVDRILKAHKQGWCYRVYVLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEYSILHR
LKAAMGTAWRDYISICGLRTHGELGGHPVSELIYIHSKVLIADDRTVIIGSANINDRSLL
GKRDSELAVLIEDTETEPSLMNGAEYQAGRFALSLRKHCFGVILGANTRPDLDLRDPICD
DFFQLWQDMAESNANIYEQIFRCLPSNATRSLRTLREYVAVEPLATVSPPLARSELTQVQ
GHLVHFPLKFLEDESLLPPLGSKEGMIPLEVWT
Enzyme 19 Number of Residues 933
Enzyme 19 Molecular Weight 105988
Enzyme 19 Theoretical pI 7.68
Enzyme 19 GO Classification
Function
  • catalytic activity
Process
  • cell communication
  • cellular process
  • intracellular signaling cascade
  • metabolism
  • physiological process
  • signal transduction
Component
—
Enzyme 19 General Function Lipid transport and metabolism
Enzyme 19 Specific Function May have a role in signal-induced cytoskeletal regulation and/or endocytosis
Enzyme 19 Pathways
Enzyme 19 Reactions
  • A phosphatidylcholine + H2O = choline + a phosphatidate
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 2645858 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID O14939 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name PLD2_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >2802 bp 
ATGACGGCGACCCCTGAGAGCCTCTTCCCCACTGGGGACGAACTGGACTCCAGCCAGCTC
CAGATGGAGTCCGATGAGGTGGACACCCTGAAGGAGGGAGAGGACCCAGCCGACCGGATG
CACCCGTTTCTGGCCATCTATGAGCTTCAGTCTCTGAAAGTGCACCCCTTGGTGTTCGCA
CCTGGGGTCCCTGTCACAGCCCAGGTGGTGGGCACCGAAAGATATACCAGCGGATCCAAG
GTGGGAACCTGCACTCTGTATTCTGTCCGCTTGACTCACGGCGACTTTTCCTGGACAACC
AAGAAGAAATACCGTCATTTTCAGGAGCTGCATCGGGACCTCCTGAGACACAAAGTCTTG
ATGAGTCTGCTCCCTCTGGCTCGATTTGCCGTTGCCTATTCTCCAGCCCGAGATGCAGGC
AACAGAGAGATGCCCTCTCTACCCCGGGCAGGTCCTGAGGGCTCCACCAGACATGCAGCC
AGCAAACAGAAATACCTGGAGAATTACCTCAACTGTCTCTTGACCATGTCTTTCTATCGC
AACTACCATGCCATGACAGAGTTCCTGGAAGTCAGTCAGCTGTCCTTTATCCCGGACTTG
GGCCGCAAAGGACTGGAGGGGATGATCCGGAAGCGCTCAGGTGGCCACCGTGTTCCTGGC
CTCACCTGCTGTGGCCGAGACCAAGTTTGTTATCGCTGGTCCAAGAGGTGGCTGGTGGTG
AAGGACTCCTTCCTGCTGTACATGTGCCTCGAGACAGGTGCCATCTCATTTGTTCAGCTC
TTTGACCCTGGCTTTGAGGTGCAAGTGGGGAAAAGGAGCACGGAGGCACGGCACGGCGTG
CGGATCGATACCTCCCACAGGTCCTTGATTCTCAAGTGCAGCAGCTACCGGCAGGCACGG
TGGTGGGCCCAAGAGATCACTGAGCTGGCACAGGGCCCAGGCAGAGACTTCCTACAGCTG
CACCGGCATGACAGCTACGCCCCACCCCGGCCTGGGACCTTGGCCCGGTGGTTTGTGAAT
GGGGCAGGTTACTTTGCTGCTGTGGCAGATGCCATCCTTCGAGCTCAAGAGGAGATTTTC
ATCACAGACTGGTGGTTGAGTCCTGAGGTTTACCTGAAGCGTCCGGCCCATTCAGATGAC
TGGAGACTGGACATTATGCTCAAGAGGAAGGCGGAGGAAGGTGTCCGTGTGTCTATTCTG
CTGTTTAAAGAAGTGGAATTGGCCTTGGGCATCAACAGTGGCTATAGCAAGAGGGCGCTG
ATGCTGCTGCACCCCAACATAAAGGTGATGCGTCACCCAGACCAAGTGACGTTGTGGGCC
CATCATGAGAAGCTCCTGGTGGTGGACCAAGTGGTAGCATTCCTGGGGGGACTGGACCTT
GCCTATGGCCGCTGGGATGACCTGCACTACCGACTGACTGACCTTGGAGACTCCTCTGAA
TCAGCTGCCTCCCAGCCTCCCACCCCGCGCCCAGACTCACCAGCCACCCCAGACCTCTCT
CACAACCAATTCTTCTGGCTGGGCAAGGACTACAGCAATCTTATCACCAAGGACTGGGTG
CAGCTGGACCGGCCTTTCGAAGATTTCATTGACAGGGAGACGACCCCTCGGATGCCATGG
CGGGACGTTGGGGTGGTCGTCCATGGCCTACCGGCCCGGGACCTTGCCCGGCACTTCATC
CAGCGCTGGAACTTCACCAAGACCACCAAGGCCAAGTACAAGACTCCCACATACCCCTAC
CTGCTTCCCAAGTCTACCAGCACGGCCAATCAGCTCCCCTTCACACTTCCAGGAGGGCAG
TGCACCACCGTACAGGTCTTGCGATCAGTGGACCGCTGGTCAGCAGGGACTCTGGAGAAC
TCCATCCTCAATGCCTACCTGCACACCATCAGGGAGAGCCAGCACTTCCTCTACATTGAG
AATCAGTTCTTCATTAGCTGCTCAGATGGGCGGACGGTTCTGAACAAGGTGGGCGATGAG
ATTGTGGACAGAATCCTGAAGGCCCACAAACAGGGGTGGTGTTACCGAGTCTACGTGCTT
TTGCCCTTACTCCCTGGCTTCGAGGGTGACATCTCCACGGGCGGTGGCAACTCCATCCAG
GCCATTCTGCACTTTACTTACAGGACCCTGTGTCGTGGGGAGTATTCAATCCTGCATCGC
CTTAAAGCAGCCATGGGGACAGCATGGCGGGACTATATTTCCATCTGCGGGCTTCGTACA
CACGGAGAGCTGGGCGGGCACCCCGTCTCGGAGCTCATCTACATCCACAGCAAGGTGCTC
ATCGCAGATGACCGGACAGTCATCATTGGTTCTGCAAACATCAATGACCGGAGCTTGCTG
GGGAAGCGGGACAGTGAGCTGGCCGTGCTGATCGAGGACACAGAGACGGAACCATCCCTC
ATGAATGGGGCAGAGTATCAGGCGGGCAGGTTTGCCTTGAGTCTGCGGAAGCACTGCTTC
GGTGTGATTCTTGGAGCAAATACCCGGCCAGACTTGGATCTCCGAGACCCCATCTGTGAT
GACTTCTTCCAGTTGTGGCAAGACATGGCTGAGAGCAACGCCAATATCTATGAGCAGATC
TTCCGCTGCCTGCCATCCAATGCCACGCGTTCCCTGCGGACTCTCCGGGAGTACGTGGCC
GTGGAGCCCTTGGCCACGGTCAGTCCCCCCTTGGCTCGGTCTGAGCTCACCCAGGTCCAG
GGCCACCTGGTCCACTTCCCCCTCAAGTTCCTAGAGGATGAGTCTTTGCTGCCCCCGCTG
GGTAGCAAGGAGGGCATGATCCCCCTAGAAGTGTGGACATAG
Enzyme 19 GenBank Gene ID AF033850 Link Image
Enzyme 19 GeneCard ID PLD2 Link Image
Enzyme 19 GenAtlas ID PLD2 Link Image
Enzyme 19 HGNC ID HGNC:9068 Link Image
Enzyme 19 Chromosome Location 17
Enzyme 19 Locus 17p13.1
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Steed PM, Clark KL, Boyar WC, Lasala DJ: Characterization of human PLD2 and the analysis of PLD isoform splice variants. FASEB J. 1998 Oct;12(13):1309-17. [PubMed Link Image]
  2. Lopez I, Arnold RS, Lambeth JD: Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2. J Biol Chem. 1998 May 22;273(21):12846-52. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5313
Enzyme 20 Name Ectonucleoside triphosphate diphosphohydrolase 1
Enzyme 20 Synonyms
  1. NTPDase 1
  2. Ecto-ATP diphosphohydrolase
  3. ATPDase
  4. Lymphoid cell activation antigen
  5. Ecto-apyrase
  6. CD39 antigen
Enzyme 20 Gene Name ENTPD1
Enzyme 20 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 1 
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
Enzyme 20 Number of Residues 510
Enzyme 20 Molecular Weight 57965
Enzyme 20 Theoretical pI 6.29
Enzyme 20 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 20 General Function Not Available
Enzyme 20 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 20 Pathways
Enzyme 20 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • 17-37 479-499
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 765256 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P49961 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name ENTP1_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 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 20 GenBank Gene ID S73813 Link Image
Enzyme 20 GeneCard ID ENTPD1 Link Image
Enzyme 20 GenAtlas ID ENTPD1 Link Image
Enzyme 20 HGNC ID HGNC:3363 Link Image
Enzyme 20 Chromosome Location 10
Enzyme 20 Locus 10q24
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 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 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5314
Enzyme 21 Name Soluble calcium-activated nucleotidase 1
Enzyme 21 Synonyms
  1. SCAN-1
  2. Apyrase homolog
  3. Putative NF-kappa-B-activating protein 107
  4. Putative MAPK-activating protein PM09
Enzyme 21 Gene Name CANT1
Enzyme 21 Protein Sequence >Soluble calcium-activated nucleotidase 1 
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
Enzyme 21 Number of Residues 401
Enzyme 21 Molecular Weight 44840
Enzyme 21 Theoretical pI 5.98
Enzyme 21 GO Classification Not Available
Enzyme 21 General Function Not Available
Enzyme 21 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 21 Pathways
Enzyme 21 Reactions
  • A nucleoside diphosphate + H2O = a nucleotide + phosphate
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • 45-62
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 22218108 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q8WVQ1 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name CANT1_HUMAN Link Image
Enzyme 21 PDB ID 1S1D Link Image
Enzyme 21 PDB File Show
Enzyme 21 3D Structure
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1116 bp 
ATGACCAAGGCCGCGGACCCCCGCTTCCGCCCCCGCTGGAAGGTGATCCTGACGTTCTTT
GTGGGTGCTGCCATCCTCTGGCTGCTCTGCTCCCACCGCCCGGCCCCCGGCAGGCCCCCC
ACCCACAATGCACACAACTGGAGGCTCGGCCAGGCGCCCGCCAACTGGTACAATGACACC
TACCCCCTGTCTCCCCCACAAAGGACACCGGCTGGGATTCGGTATCGAATCGCAGTTATC
GCAGACCTGGACACAGAGTCAAGGGCCCAAGAGGAAAACACCTGGTTCAGTTACCTGAAA
AAGGGCTACCTGACCCTGTCAGACAGTGGGGACAAGGTGGCCGTGGAATGGGACAAAGAC
CATGGGGTCCTGGAGTCCCACCTGGCGGAGAAGGGGAGAGGCATGGAGCTATCCGACCTG
ATTGTTTTCAATGGGAAACTCTACTCCGTGGATGACCGGACGGGGGTCGTCTACCAGATC
GAAGGCAGCAAAGCCGTGCCCTGGGTGATTCTGTCCGACGGCGACGGCACCGTGGAGAAA
GGCTTCAAGGCCGAATGGCTGGCAGTGAAGGACGAGCGTCTGTACGTGGGCGGCCTGGGC
AAGGAGTGGACGACCACTACGGGTGATGTGGTGAACGAGAACCCGGAGTGGGTGAAGGTG
GTGGGCTACAAGGGCAGCGTGGACCACGAGAACTGGGTGTCCAACTACAACGCCCTGCGG
GCTGCTGCCGGCATCCAGCCGCCAGGCTACCTCATCCATGAGTCTGCCTGCTGGAGTGAC
ACGCTGCAGCGCTGGTTCTTCCTGCCGCGCCGCGCCAGCCAGGAGCGCTACAGCGAGAAG
GACGACGAGCGCAAGGGCGCCAACCTGCTGCTGAGCGCCTCCCCTGACTTCGGCGACATC
GCTGTGAGCCACGTCGGGGCGGTGGTCCCCACTCACGGCTTCTCGTCCTTCAAGTTCATC
CCCAACACCGACGACCAGATCATTGTGGCCCTCAAATCCGAGGAGGACAGCGGCAGAGTC
GCCTCCTACATCATGGCCTTCACGCTGGACGGGCGCTTCCTGTTGCCGGAGACCAAGATC
GGAAGCGTGAAATACGAAGGCATCGAGTTCATTTAA
Enzyme 21 GenBank Gene ID AF328554 Link Image
Enzyme 21 GeneCard ID CANT1 Link Image
Enzyme 21 GenAtlas ID CANT1 Link Image
Enzyme 21 HGNC ID HGNC:19721 Link Image
Enzyme 21 Chromosome Location 17
Enzyme 21 Locus 17q25.3
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 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 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5319
Enzyme 22 Name Tyrosinase precursor
Enzyme 22 Synonyms
  1. Monophenol monooxygenase
  2. Tumor rejection antigen AB
  3. SK29-AB
  4. LB24-AB
Enzyme 22 Gene Name TYR
Enzyme 22 Protein Sequence >Tyrosinase precursor 
MLLAVLYCLLWSFQTSAGHFPRACVSSKNLMEKECCPPWSGDRSPCGQLSGRGSCQNILL
SNAPLGPQFPFTGVDDRESWPSVFYNRTCQCSGNFMGFNCGNCKFGFWGPNCTERRLLVR
RNIFDLSAPEKDKFFAYLTLAKHTISSDYVIPIGTYGQMKNGSTPMFNDINIYDLFVWMH
YYVSMDALLGGSEIWRDIDFAHEAPAFLPWHRLFLLRWEQEIQKLTGDENFTIPYWDWRD
AEKCDICTDEYMGGQHPTNPNLLSPASFFSSWQIVCSRLEEYNSHQSLCNGTPEGPLRRN
PGNHDKSRTPRLPSSADVEFCLSLTQYESGSMDKAANFSFRNTLEGFASPLTGIADASQS
SMHNALHIYMNGTMSQVQGSANDPIFLLHHAFVDSIFEQWLRRHRPLQEVYPEANAPIGH
NRESYMVPFIPLYRNGDFFISSKDLGYDYSYLQDSDPDSFQDYIKSYLEQASRIWSWLLG
AAMVGAVLTALLAGLVSLLCRHKRKQLPEEKQPLLMEKEDYHSLYQSHL
Enzyme 22 Number of Residues 529
Enzyme 22 Molecular Weight 60394
Enzyme 22 Theoretical pI 6.05
Enzyme 22 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 22 General Function Not Available
Enzyme 22 Specific Function This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6-dihydroxyindole to indole-5,6 quinone
Enzyme 22 Pathways
Enzyme 22 Reactions
  • L-tyrosine + L-dopa + O2 = L-dopa + dopaquinone + H2O
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • 1-18
Enzyme 22 Transmembrane Regions
  • 477-497
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 340037 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID P14679 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name TYRO_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1590 bp 
ATGCTCCTGGCTGTTTTGTACTGCCTGCTGTGGAGTTTCCAGACCTCCGCTGGCCATTTC
CCTAGAGCCTGTGTCTCCTCTAAGAACCTGATGGAGAAGGAATGCTGTCCACCGTGGAGC
GGGGACAGGAGTCCCTGTGGCCAGCTTTCAGGCAGAGGTTCCTGTCAGAATATCCTTCTG
TCCAATGCACCACTTGGGCCTCAATTTCCCTTCACAGGGGTGGATGACCGGGAGTCGTGG
CCTTCCGTCTTTTATAATAGGACCTGCCAGTGCTCTGGCAACTTCATGGGATTCAACTGT
GGAAACTGCAAGTTTGGCTTTTGGGGACCAAACTGCACAGAGAGACGACTCTTGGTGAGA
AGAAACATCTTCGATTTGAGTGCCCCAGAGAAGGACAAATTTTTTGCCTACCTCACTTTA
GCAAAGCATACCATCAGCTCAGACTATGTCATCCCCATAGGGACCTATGGCCAAATGAAA
AATGGATCAACACCCATGTTTAACGACATCAATATTTATGACCTCTTTGTCTGGATGCAT
TATTATGTGTCAATGGATGCACTGCTTGGGGGATCTGAAATCTGGAGAGACATTGATTTT
GCCCATGAAGCACCAGCTTTTCTGCCTTGGCATAGACTCTTCTTGTTGCGGTGGGAACAA
GAAATCCAGAAGCTGACAGGAGATGAAAACTTCACTATTCCATATTGGGACTGGCGGGAT
GCAGAAAAGTGTGACATTTGCACAGATGAGTACATGGGAGGTCAGCACCCCACAAATCCT
AACTTACTCAGCCCAGCATCATTCTTCTCCTCTTGGCAGATTGTCTGTAGCCGATTGGAG
GAGTACAACAGCCATCAGTCTTTATGCAATGGAACGCCCGAGGGACCTTTACGGCGTAAT
CCTGGAAACCATGACAAATCCAGAACCCCAAGGCTCCCCTCTTCAGCTGATGTAGAATTT
TGCCTGAGTTTGACCCAATATGAATCTGGTTCCATGGATAAAGCTGCCAATTTCAGCTTT
AGAAATACACTGGAAGGATTTGCTAGTCCACTTACTGGGATAGCGGATGCCTCTCAAAGC
AGCATGCACAATGCCTTGCACATCTATATGAATGGAACAATGTCCCAGGTACAGGGATCT
GCCAACGATCCTATCTTCCTTCTTCACCATGCATTTGTTGACAGTATTTTTGAGCAGTGG
CTCCGAAGGCACCGTCCTCTTCAAGAAGTTTATCCAGAAGCCAATGCACCCATTGGACAT
AACCGGGAATCCTACATGGTTCCTTTTATACCACTGTACAGAAATGGTGATTTCTTTATT
TCATCCAAAGATCTGGGCTATGACTATAGCTATCTACAAGATTCAGACCCAGACTCTTTT
CAAGACTACATTAAGTCCTATTTGGAACAAGCGAGTCGGATCTGGTCATGGCTCCTTGGG
GCGGCGATGGTAGGGGCCGTCCTCACTGCCCTGCTGGCAGGGCTTGTGAGCTTGCTGTGT
CGTCACAAGAGAAAGCAGCTTCCTGAAGAAAAGCAGCCACTCCTCATGGAGAAAGAGGAT
TACCACAGCTTGTATCAGAGCCATTTATAA
Enzyme 22 GenBank Gene ID M27160 Link Image
Enzyme 22 GeneCard ID TYR Link Image
Enzyme 22 GenAtlas ID TYR Link Image
Enzyme 22 HGNC ID HGNC:12442 Link Image
Enzyme 22 Chromosome Location 11
Enzyme 22 Locus 11q14-q21
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Giebel LB, Strunk KM, Spritz RA: Organization and nucleotide sequences of the human tyrosinase gene and a truncated tyrosinase-related segment. Genomics. 1991 Mar;9(3):435-45. [PubMed Link Image]
  2. Kwon BS, Haq AK, Pomerantz SH, Halaban R: Isolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus. Proc Natl Acad Sci U S A. 1987 Nov;84(21):7473-7. [PubMed Link Image]
  3. Bouchard B, Fuller BB, Vijayasaradhi S, Houghton AN: Induction of pigmentation in mouse fibroblasts by expression of human tyrosinase cDNA. J Exp Med. 1989 Jun 1;169(6):2029-42. [PubMed Link Image]
  4. Chintamaneni CD, Halaban R, Kobayashi Y, Witkop CJ Jr, Kwon BS: A single base insertion in the putative transmembrane domain of the tyrosinase gene as a cause for tyrosinase-negative oculocutaneous albinism. Proc Natl Acad Sci U S A. 1991 Jun 15;88(12):5272-6. [PubMed Link Image]
  5. Brichard V, Van Pel A, Wolfel T, Wolfel C, De Plaen E, Lethe B, Coulie P, Boon T: The tyrosinase gene codes for an antigen recognized by autologous cytolytic T lymphocytes on HLA-A2 melanomas. J Exp Med. 1993 Aug 1;178(2):489-95. [PubMed Link Image]
  6. Martinez-Arias R, Comas D, Andres A, Abello MT, Domingo-Roura X, Bertranpetit J: The tyrosinase gene in gorillas and the albinism of 'Snowflake'. Pigment Cell Res. 2000 Dec;13(6):467-70. [PubMed Link Image]
  7. Kikuchi H, Miura H, Yamamoto H, Takeuchi T, Dei T, Watanabe M: Characteristic sequences in the upstream region of the human tyrosinase gene. Biochim Biophys Acta. 1989 Dec 22;1009(3):283-6. [PubMed Link Image]
  8. Takeda A, Tomita Y, Okinaga S, Tagami H, Shibahara S: Functional analysis of the cDNA encoding human tyrosinase precursor. Biochem Biophys Res Commun. 1989 Aug 15;162(3):984-90. [PubMed Link Image]
  9. Murphy WJ, Eizirik E, Johnson WE, Zhang YP, Ryder OA, O'Brien SJ: Molecular phylogenetics and the origins of placental mammals. Nature. 2001 Feb 1;409(6820):614-8. [PubMed Link Image]
  10. Oetting WS, King RA: Molecular basis of type I (tyrosinase-related) oculocutaneous albinism: mutations and polymorphisms of the human tyrosinase gene. Hum Mutat. 1993;2(1):1-6. [PubMed Link Image]
  11. Oetting WS, King RA: Molecular basis of albinism: mutations and polymorphisms of pigmentation genes associated with albinism. Hum Mutat. 1999;13(2):99-115. [PubMed Link Image]
  12. Spritz RA, Strunk KM, Giebel LB, King RA: Detection of mutations in the tyrosinase gene in a patient with type IA oculocutaneous albinism. N Engl J Med. 1990 Jun 14;322(24):1724-8. [PubMed Link Image]
  13. Giebel LB, Strunk KM, King RA, Hanifin JM, Spritz RA: A frequent tyrosinase gene mutation in classic, tyrosinase-negative (type IA) oculocutaneous albinism. Proc Natl Acad Sci U S A. 1990 May;87(9):3255-8. [PubMed Link Image]
  14. Giebel LB, Tripathi RK, Strunk KM, Hanifin JM, Jackson CE, King RA, Spritz RA: Tyrosinase gene mutations associated with type IB ("yellow") oculocutaneous albinism. Am J Hum Genet. 1991 Jun;48(6):1159-67. [PubMed Link Image]
  15. Tripathi RK, Strunk KM, Giebel LB, Weleber RG, Spritz RA: Tyrosinase gene mutations in type I (tyrosinase-deficient) oculocutaneous albinism define two clusters of missense substitutions. Am J Med Genet. 1992 Jul 15;43(5):865-71. [PubMed Link Image]
  16. Spritz RA, Strunk KM, Hsieh CL, Sekhon GS, Francke U: Homozygous tyrosinase gene mutation in an American black with tyrosinase-negative (type IA) oculocutaneous albinism. Am J Hum Genet. 1991 Feb;48(2):318-24. [PubMed Link Image]
  17. Giebel LB, Tripathi RK, King RA, Spritz RA: A tyrosinase gene missense mutation in temperature-sensitive type I oculocutaneous albinism. A human homologue to the Siamese cat and the Himalayan mouse. J Clin Invest. 1991 Mar;87(3):1119-22. [PubMed Link Image]
  18. King RA, Mentink MM, Oetting WS: Non-random distribution of missense mutations within the human tyrosinase gene in type I (tyrosinase-related) oculocutaneous albinism. Mol Biol Med. 1991 Feb;8(1):19-29. [PubMed Link Image]
  19. Oetting WS, King RA: Molecular analysis of type I-A (tyrosinase negative) oculocutaneous albinism. Hum Genet. 1992 Nov;90(3):258-62. [PubMed Link Image]
  20. Tripathi RK, Bundey S, Musarella MA, Droetto S, Strunk KM, Holmes SA, Spritz RA: Mutations of the tyrosinase gene in Indo-Pakistani patients with type I (tyrosinase-deficient) oculocutaneous albinism (OCA). Am J Hum Genet. 1993 Dec;53(6):1173-9. [PubMed Link Image]
  21. Gershoni-Baruch R, Rosenmann A, Droetto S, Holmes S, Tripathi RK, Spritz RA: Mutations of the tyrosinase gene in patients with oculocutaneous albinism from various ethnic groups in Israel. Am J Hum Genet. 1994 Apr;54(4):586-94. [PubMed Link Image]
  22. Breimer LH, Winder AF, Jay B, Jay M: Initiation codon mutation of the tyrosinase gene as a cause of human albinism. Clin Chim Acta. 1994 Jun;227(1-2):17-22. [PubMed Link Image]
  23. Summers CG, Oetting WS, King RA: Diagnosis of oculocutaneous albinism with molecular analysis. Am J Ophthalmol. 1996 Jun;121(6):724-6. [PubMed Link Image]
  24. Morell R, Spritz RA, Ho L, Pierpont J, Guo W, Friedman TB, Asher JH Jr: Apparent digenic inheritance of Waardenburg syndrome type 2 (WS2) and autosomal recessive ocular albinism (AROA). Hum Mol Genet. 1997 May;6(5):659-64. [PubMed Link Image]
  25. Spritz RA, Oh J, Fukai K, Holmes SA, Ho L, Chitayat D, France TD, Musarella MA, Orlow SJ, Schnur RE, Weleber RG, Levin AV: Novel mutations of the tyrosinase (TYR) gene in type I oculocutaneous albinism (OCA1). Hum Mutat. 1997;10(2):171-4. [PubMed Link Image]
  26. Passmore LA, Kaesmann-Kellner B, Weber BH: Novel and recurrent mutations in the tyrosinase gene and the P gene in the German albino population. Hum Genet. 1999 Sep;105(3):200-10. [PubMed Link Image]
  27. Tsai CH, Tsai FJ, Wu JY, Lin SP, Chang JG, Yang CF, Lee CC: Insertion/deletion mutations of type I oculocutaneous albinism in chinese patients from Taiwan. Hum Mutat. 1999 Dec;14(6):542. [PubMed Link Image]
  28. Camand O, Marchant D, Boutboul S, Pequignot M, Odent S, Dollfus H, Sutherland J, Levin A, Menasche M, Marsac C, Dufier JL, Heon E, Abitbol M: Mutation analysis of the tyrosinase gene in oculocutaneous albinism. Hum Mutat. 2001 Apr;17(4):352. [PubMed Link Image]
  29. Nakamura E, Miyamura Y, Matsunaga J, Kano Y, Dakeishi-Hara M, Tanita M, Kono M, Tomita Y: A novel mutation of the tyrosinase gene causing oculocutaneous albinism type 1 (OCA1). J Dermatol Sci. 2002 Feb;28(2):102-5. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5322
Enzyme 23 Name Alkaline phosphatase, placental type precursor
Enzyme 23 Synonyms
  1. PLAP-1
  2. Alkaline phosphatase Regan isozyme
Enzyme 23 Gene Name ALPP
Enzyme 23 Protein Sequence >Alkaline phosphatase, placental type precursor 
MLGPCMLLLLLLLGLRLQLSLGIIPVEEENPDFWNREAAEALGAAKKLQPAQTAAKNLII
FLGDGMGVSTVTAARILKGQKKDKLGPEIPLAMDRFPYVALSKTYNVDKHVPDSGATATA
YLCGVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAG
TYAHTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFRMGTPDPEYP
DDYSQGGTRLDGKNLVQEWLAKRQGARYVWNRTELMQASLDPSVTHLMGLFEPGDMKYEI
HRDSTLDPSLMEMTEAALRLLSRNPRGFFLFVEGGRIDHGHHESRAYRALTETIMFDDAI
ERAGQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPG
YVLKDGARPDVTESESGSPEYRQQSAVPLDEETHAGEDVAVFARGPQAHLVHGVQEQTFI
AHVMAFAACLEPYTACDLAPPAGTTDAAHPGRSVVPALLPLLAGTLLLLETATAP
Enzyme 23 Number of Residues 535
Enzyme 23 Molecular Weight 57954
Enzyme 23 Theoretical pI 6.24
Enzyme 23 GO Classification
Function
—
Process
  • metabolism
  • physiological process
Component
—
Enzyme 23 General Function Inorganic ion transport and metabolism
Enzyme 23 Specific Function A phosphate monoester + H(2)O = an alcohol + phosphate
Enzyme 23 Pathways
  • Folate and Pterine Biosynthesis (map00790 Link Image)
  • gamma-Hexachlorocyclohexane Degradation (map00361 Link Image)
Enzyme 23 Reactions
  • A phosphate monoester + H2O = an alcohol + phosphate
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • 1-22
Enzyme 23 Transmembrane Regions
  • 513-529
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 178474 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID P05187 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name PPB1_HUMAN Link Image
Enzyme 23 PDB ID 1EW2 Link Image
Enzyme 23 PDB File Show
Enzyme 23 3D Structure
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1608 bp 
ATGCTGGGGCCCTGCATGCTGCTGCTGCTGCTGCTGCTGGGCCTGAGGCTACAGCTCTCC
CTGGGCATCATCCCAGTTGAGGAGGAGAACCCGGACTTCTGGAACCGCGAGGCAGCCGAG
GCCCTGGGTGCCGCCAAGAAGCTGCAGCCTGCACAGACAGCCGCCAAGAACCTCATCATC
TTCCTGGGCGATGGGATGGGGGTGTCTACGGTGACAGCTGCCAGGATCCTAAAAGGGCAG
AAGAAGGACAAACTGGGGCCTGAGATACCCCTGGCCATGGACCGCTTCCCATATGTGGCT
CTGTCCAAGACATACAATGTAGACAAACATGTGCCAGACAGTGGAGCCACAGCCACGGCC
TACCTGTGCGGGGTCAAGGGCAACTTCCAGACCATTGGCTTGAGTGCAGCCGCCCGCTTT
AACCAGTGCAACACGACACGCGGCAACGAGGTCATCTCCGTGATGAATCGGGCCAAGAAA
GCAGGGAAGTCAGTGGGAGTGGTAACCACCACACGAGTGCAGCACGCCTCGCCAGCCGGC
ACCTACGCCCACACGGTGAACCGCAACTGGTACTCGGACGCCGACGTGCCTGCCTCGGCC
CGCCAGGAGGGGTGCCAGGACATCGCTACGCAGCTCATCTCCAACATGGACATTGACGTG
ATCCTAGGTGGAGGCCGAAAGTACATGTTTCCCATGGGAACCCCAGACCCTGAGTACCCA
GATGACTACAGCCAAGGTGGGACCAGGCTGGACGGGAAGAATCTGGTGCAGGAATGGCTG
GCGAAGCGCCAGGGTGCCCGGTATGTGTGGAACCGCACTGAGCTCATGCAGGCTTCCCTG
GACCCGTCTGTGACCCATCTCATGGGTCTCTTTGAGCCTGGAGACATGAAATACGAGATC
CACCGAGACTCCACACTGGACCCCTCCCTGATGGAGATGACAGAGGCTGCCCTGCGCCTG
CTGAGCAGGAACCCCCGCGGCTTCTTCCTCTTCGTGGAGGGTGGTCGCATCGACCATGGT
CATCATGAAAGCAGGGCTTACCGGGCACTGACTGAGACGATCATGTTCGACGACGCCATT
GAGAGGGCGGGCCAGCTCACCAGCGAGGAGGACACGCTGAGCCTCGTCACTGCCGACCAC
TCCCACGTCTTCTCCTTCGGAGGCTACCCCCTGCGAGGGAGCTCCATCTTCGGGCTGGCC
CCTGGCAAGGCCCGGGACAGGAAGGCCTACACGGTCCTCCTATACGGAAACGGTCCAGGC
TATGTGCTCAAGGACGGCGCCCGGCCGGATGTTACCGAGAGCGAGAGCGGGAGCCCCGAG
TATCGGCAGCAGTCAGCAGTGCCCCTGGACGAAGAGACCCACGCAGGCGAGGACGTGGCG
GTGTTCGCGCGCGGCCCGCAGGCGCACCTGGTTCACGGCGTGCAGGAGCAGACCTTCATA
GCGCACGTCATGGCCTTCGCCGCCTGCCTGGAGCCCTACACCGCCTGCGACCTGGCGCCC
CCCGCCGGCACCACCGACGCCGCGCACCCGGGGCGGTCCGTGGTCCCCGCGTTGCTTCCT
CTGCTGGCCGGGACCCTGCTGCTGCTGGAGACGGCCACTGCTCCCTGA
Enzyme 23 GenBank Gene ID M13077 Link Image
Enzyme 23 GeneCard ID ALPP Link Image
Enzyme 23 GenAtlas ID ALPP Link Image
Enzyme 23 HGNC ID HGNC:439 Link Image
Enzyme 23 Chromosome Location 2
Enzyme 23 Locus 2q37
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Knoll BJ, Rothblum KN, Longley M: Nucleotide sequence of the human placental alkaline phosphatase gene. Evolution of the 5' flanking region by deletion/substitution. J Biol Chem. 1988 Aug 25;263(24):12020-7. [PubMed Link Image]
  2. Millan JL: Molecular cloning and sequence analysis of human placental alkaline phosphatase. J Biol Chem. 1986 Mar 5;261(7):3112-5. [PubMed Link Image]
  3. Henthorn PS, Knoll BJ, Raducha M, Rothblum KN, Slaughter C, Weiss M, Lafferty MA, Fischer T, Harris H: Products of two common alleles at the locus for human placental alkaline phosphatase differ by seven amino acids. Proc Natl Acad Sci U S A. 1986 Aug;83(15):5597-601. [PubMed Link Image]
  4. Kam W, Clauser E, Kim YS, Kan YW, Rutter WJ: Cloning, sequencing, and chromosomal localization of human term placental alkaline phosphatase cDNA. Proc Natl Acad Sci U S A. 1985 Dec;82(24):8715-9. [PubMed Link Image]
  5. Ezra E, Blacher R, Udenfriend S: Purification and partial sequencing of human placental alkaline phosphatase. Biochem Biophys Res Commun. 1983 Nov 15;116(3):1076-83. [PubMed Link Image]
  6. Knoll BJ, Rothblum KN, Longley M: Two gene duplication events in the evolution of the human heat-stable alkaline phosphatases. Gene. 1987;60(2-3):267-76. [PubMed Link Image]
  7. Ovitt CE, Strauss AW, Alpers DH, Chou JY, Boime I: Expression of different-sized placental alkaline phosphatase mRNAs in placenta and choriocarcinoma cells. Proc Natl Acad Sci U S A. 1986 Jun;83(11):3781-5. [PubMed Link Image]
  8. Micanovic R, Bailey CA, Brink L, Gerber L, Pan YC, Hulmes JD, Udenfriend S: Aspartic acid-484 of nascent placental alkaline phosphatase condenses with a phosphatidylinositol glycan to become the carboxyl terminus of the mature enzyme. Proc Natl Acad Sci U S A. 1988 Mar;85(5):1398-402. [PubMed Link Image]
  9. Micanovic R, Gerber LD, Berger J, Kodukula K, Udenfriend S: Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan-anchored membrane proteins determined by site-specific mutagenesis at Asp-484 of placental alkaline phosphatase. Proc Natl Acad Sci U S A. 1990 Jan;87(1):157-61. [PubMed Link Image]
  10. Kozlenkov A, Manes T, Hoylaerts MF, Millan JL: Function assignment to conserved residues in mammalian alkaline phosphatases. J Biol Chem. 2002 Jun 21;277(25):22992-9. Epub 2002 Apr 5. [PubMed Link Image]
  11. Lowe ME: Site-specific mutations in the COOH-terminus of placental alkaline phosphatase: a single amino acid change converts a phosphatidylinositol-glycan-anchored protein to a secreted protein. J Cell Biol. 1992 Feb;116(3):799-807. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 5328
Enzyme 24 Name Alkaline phosphatase, tissue-nonspecific isozyme precursor
Enzyme 24 Synonyms
  1. AP-TNAP
  2. TNSALP
  3. Alkaline phosphatase liver/bone/kidney isozyme
Enzyme 24 Gene Name ALPL
Enzyme 24 Protein Sequence >Alkaline phosphatase, tissue-nonspecific isozyme precursor 
MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGD
GMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCG
VKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAH
SADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDE
KARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELN
RNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIG
QAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPG
YKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYV
PHVMAYAACIGANLGHCAPASSAGSLAAGPLLLALALYPLSVLF
Enzyme 24 Number of Residues 524
Enzyme 24 Molecular Weight 57305
Enzyme 24 Theoretical pI 6.66
Enzyme 24 GO Classification
Function
—
Process
  • metabolism
  • physiological process
Component
—
Enzyme 24 General Function Inorganic ion transport and metabolism
Enzyme 24 Specific Function This isozyme may play a role in skeletal mineralization
Enzyme 24 Pathways
  • Folate and Pterine Biosynthesis (map00790 Link Image)
  • gamma-Hexachlorocyclohexane Degradation (map00361 Link Image)
Enzyme 24 Reactions
  • A phosphate monoester + H2O = an alcohol + phosphate
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • 1-17
Enzyme 24 Transmembrane Regions Not Available
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 28738 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID P05186 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name PPBT_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >1575 bp 
ATGATTTCACCATTCTTAGTACTGGCCATTGGCACCTGCCTTACTAACTCCTTAGTGCCA
GAGAAAGAGAAAGACCCCAAGTACTGGCGAGACCAAGCGCAAGAGACACTGAAATATGCC
CTGGAGCTTCAGAAGCTCAACACCAACGTGGCTAAGAATGTCATCATGTTCCTGGGAGAT
GGGATGGGTGTCTCCACAGTGACGGCTGCCCGCATCCTCAAGGGTCAGCTCCACCACAAC
CCTGGGGAGGAGACCAGGCTGGAGATGGACAAGTTCCCCTTCGTGGCCCTCTCCAAGACG
TACAACACCAAAGCCCAGGTCCCTGACAGCGCCGGCACCGCCACCGCCTACCTGTGTGGG
GTGAAGGCCAATGAGGGCACCGTGGGGGTAAGCGCAGCCACTGAGCGTTCCCGGTGCAAC
ACCACCCAGGGGAACGAGGTCACCTCCATCCTGCGCTGGGCCAAGGACGCTGGGAAATCT
GTGGGCATTGTGACCACCACGAGAGTGAACCATGCCACCCCCAGCGCCGCCTACGCCCAC
TCGGCTGACCGGGACTGGTACTCAGACAACGAGATGCCCCCTGAGGCCTTGAGCCAGGGC
TGTAAGGACATCGCCTACCAGCTCATGCATAACATCAGGGACATTGACGTGATCATGGGG
GGTGGCCGGAAATACATGTACCCCAAGAATAAAACTGATGTGGAGTATGAGAGTGACGAG
AAAGCCAGGGGCACGAGGCTGGACGGCCTGGACCTCGTTGACACCTGGAAGAGCTTCAAA
CCGAGACACAAGCACTCCCACTTCATCTGGAACCGCACGGAACTCCTGACCCTTGACCCC
CACAATGTGGACTACCTATTGGGTCTCTTCGAGCCGGGGGACATGCAGTACGAGCTGAAC
AGGAACAACGTGACGGACCCGTCACTCTCCGAGATGGTGGTGGTGGCCATCCAGATCCTG
CGGAAGAACCCCAAAGGCTTCTTCTTGCTGGTGGAAGGAGGCAGAATTGACCACGGGCAC
CATGAAGGAAAAGCCAAGCAGGCCCTGCATGAGGCGGTGGAGATGGACCGGGCCATCGGG
CAGGCAGGCAGCTTGACCTCCTCGGAAGACACTCTGACCGTGGTCACTGCGGACCATTCC
CACGTCTTCACATTTGGTGGATACACCCCCCGTGGCAACTCTATCTTTGGTCTGGCCCCC
ATGCTGAGTGACACAGACAAGAAGCCCTTCACTGCCATCCTGTATGGCAATGGGCCTGGC
TACAAGGTGGTGGGCGGTGAACGAGAGAATGTCTCCATGGTGGACTATGCTCACAACAAC
TACCAGGCGCAGTCTGCTGTGCCCCTGCGCCACGAGACCCACGGCGGGGAGGACGTGGCC
GTCTTCTCCAAGGGCCCCATGGCGCACCTGCTGCACGGCGTCCACGAGCAGAACTACGTC
CCCCACGTGATGGCGTATGCAGCCTGCATCGGGGCCAACCTCGGCCACTGTGCTCCTGCC
AGCTCGGCAGGCAGCCTTGCTGCAGGCCCCCTGCTGCTCGCGCTGGCCCTCTACCCCCTG
AGCGTCCTGTTCTGA
Enzyme 24 GenBank Gene ID X14174 Link Image
Enzyme 24 GeneCard ID ALPL Link Image
Enzyme 24 GenAtlas ID ALPL Link Image
Enzyme 24 HGNC ID HGNC:438 Link Image
Enzyme 24 Chromosome Location 1
Enzyme 24 Locus 1p36.1-p34
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Kishi F, Matsuura S, Kajii T: Nucleotide sequence of the human liver-type alkaline phosphatase cDNA. Nucleic Acids Res. 1989 Mar 11;17(5):2129. [PubMed Link Image]
  2. Weiss MJ, Henthorn PS, Lafferty MA, Slaughter C, Raducha M, Harris H: Isolation and characterization of a cDNA encoding a human liver/bone/kidney-type alkaline phosphatase. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7182-6. [PubMed Link Image]
  3. Weiss MJ, Ray K, Henthorn PS, Lamb B, Kadesch T, Harris H: Structure of the human liver/bone/kidney alkaline phosphatase gene. J Biol Chem. 1988 Aug 25;263(24):12002-10. [PubMed Link Image]
  4. Garattini E, Hua JC, Pan YC, Udenfriend S: Human liver alkaline phosphatase, purification and partial sequencing: homology with the placental isozyme. Arch Biochem Biophys. 1986 Mar;245(2):331-7. [PubMed Link Image]
  5. Weiss MJ, Cole DE, Ray K, Whyte MP, Lafferty MA, Mulivor RA, Harris H: A missense mutation in the human liver/bone/kidney alkaline phosphatase gene causing a lethal form of hypophosphatasia. Proc Natl Acad Sci U S A. 1988 Oct;85(20):7666-9. [PubMed Link Image]
  6. Henthorn PS, Raducha M, Fedde KN, Lafferty MA, Whyte MP: Different missense mutations at the tissue-nonspecific alkaline phosphatase gene locus in autosomal recessively inherited forms of mild and severe hypophosphatasia. Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9924-8. [PubMed Link Image]
  7. Greenberg CR, Taylor CL, Haworth JC, Seargeant LE, Philipps S, Triggs-Raine B, Chodirker BN: A homoallelic Gly317-->Asp mutation in ALPL causes the perinatal (lethal) form of hypophosphatasia in Canadian mennonites. Genomics. 1993 Jul;17(1):215-7. [PubMed Link Image]
  8. Ozono K, Yamagata M, Michigami T, Nakajima S, Sakai N, Cai G, Satomura K, Yasui N, Okada S, Nakayama M: Identification of novel missense mutations (Phe310Leu and Gly439Arg) in a neonatal case of hypophosphatasia. J Clin Endocrinol Metab. 1996 Dec;81(12):4458-61. [PubMed Link Image]
  9. Goseki-Sone M, Orimo H, Iimura T, Takagi Y, Watanabe H, Taketa K, Sato S, Mayanagi H, Shimada T, Oida S: Hypophosphatasia: identification of five novel missense mutations (G507A, G705A, A748G, T1155C, G1320A) in the tissue-nonspecific alkaline phosphatase gene among Japanese patients. Hum Mutat. 1998;Suppl 1:S263-7. [PubMed Link Image]
  10. Sugimoto N, Iwamoto S, Hoshino Y, Kajii E: A novel missense mutation of the tissue-nonspecific alkaline phosphatase gene detected in a patient with hypophosphatasia. J Hum Genet. 1998;43(3):160-4. [PubMed Link Image]
  11. Zurutuza L, Muller F, Gibrat JF, Taillandier A, Simon-Bouy B, Serre JL, Mornet E: Correlations of genotype and phenotype in hypophosphatasia. Hum Mol Genet. 1999 Jun;8(6):1039-46. [PubMed Link Image]
  12. Taillandier A, Zurutuza L, Muller F, Simon-Bouy B, Serre JL, Bird L, Brenner R, Boute O, Cousin J, Gaillard D, Heidemann PH, Steinmann B, Wallot M, Mornet E: Characterization of eleven novel mutations (M45L, R119H, 544delG, G145V, H154Y, C184Y, D289V, 862+5A, 1172delC, R411X, E459K) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with severe hypophosphatasia. Mutations in brief no. 217. Online. Hum Mutat. 1999;13(2):171-2. [PubMed Link Image]
  13. Mochizuki H, Saito M, Michigami T, Ohashi H, Koda N, Yamaguchi S, Ozono K: Severe hypercalcaemia and respiratory insufficiency associated with infantile hypophosphatasia caused by two novel mutations of the tissue-nonspecific alkaline phosphatase gene. Eur J Pediatr. 2000 May;159(5):375-9. [PubMed Link Image]
  14. Taillandier A, Cozien E, Muller F, Merrien Y, Bonnin E, Fribourg C, Simon-Bouy B, Serre JL, Bieth E, Brenner R, Cordier MP, De Bie S, Fellmann F, Freisinger P, Hesse V, Hennekam RC, Josifova D, Kerzin-Storrar L, Leporrier N, Zabot MT, Mornet E: Fifteen new mutations (-195C>T, L-12X, 298-2A>G, T117N, A159T, R229S, 997+2T>A, E274X, A331T, H364R, D389G, 1256delC, R433H, N461I, C472S) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with hypophosphatasia. Hum Mutat. 2000 Mar;15(3):293. [PubMed Link Image]
  15. Muller HL, Yamazaki M, Michigami T, Kageyama T, Schonau E, Schneider P, Ozono K: Asp361Val Mutant of alkaline phosphatase found in patients with dominantly inherited hypophosphatasia inhibits the activity of the wild-type enzyme. J Clin Endocrinol Metab. 2000 Feb;85(2):743-7. [PubMed Link Image]
  16. Lia-Baldini AS, Muller F, Taillandier A, Gibrat JF, Mouchard M, Robin B, Simon-Bouy B, Serre JL, Aylsworth AS, Bieth E, Delanote S, Freisinger P, Hu JC, Krohn HP, Nunes ME, Mornet E: A molecular approach to dominance in hypophosphatasia. Hum Genet. 2001 Jul;109(1):99-108. [PubMed Link Image]
  17. Taillandier A, Lia-Baldini AS, Mouchard M, Robin B, Muller F, Simon-Bouy B, Serre JL, Bera-Louville A, Bonduelle M, Eckhardt J, Gaillard D, Myhre AG, Kortge-Jung S, Larget-Piet L, Malou E, Sillence D, Temple IK, Viot G, Mornet E: Twelve novel mutations in the tissue-nonspecific alkaline phosphatase gene (ALPL) in patients with various forms of hypophosphatasia. Hum Mutat. 2001;18(1):83-4. [PubMed Link Image]
  18. Watanabe H, Hashimoto-Uoshima M, Goseki-Sone M, Orimo H, Ishikawa I: A novel point mutation (C571T) in the tissue-non-specific alkaline phosphatase gene in a case of adult-type hypophosphatasia. Oral Dis. 2001 Nov;7(6):331-5. [PubMed Link Image]
  19. Litmanovitz, Reish O, Dolfin T, Arnon S, Regev R, Grinshpan G, Yamazaki M, Ozono K: Glu274Lys/Gly309Arg mutation of the tissue-nonspecific alkaline phosphatase gene in neonatal hypophosphatasia associated with convulsions. J Inherit Metab Dis. 2002 Feb;25(1):35-40. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 5329
Enzyme 25 Name Tartrate-resistant acid phosphatase type 5 precursor
Enzyme 25 Synonyms
  1. TR- AP
  2. Tartrate-resistant acid ATPase
  3. TrATPase
  4. Acid phosphatase 5, tartrate resistant
Enzyme 25 Gene Name ACP5
Enzyme 25 Protein Sequence >Tartrate-resistant acid phosphatase type 5 precursor 
MDMWTALLILQALLLPSLADGATPALRFVAVGDWGGVPNAPFHTAREMANAKEIARTVQI
LGADFILSLGDNFYFTGVQDINDKRFQETFEDVFSDRSLRKVPWYVLAGNHDHLGNVSAQ
IAYSKISKRWNFPSPFYRLHFKIPQTNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDVKL
ARTQLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLATYGVTAYLCGH
DHNLQYLQDENGVGYVLSGAGNFMDPSKRHQRKVPNGYLRFHYGTEDSLGGFAYVEISSK
EMTVTYIEASGKSLFKTRLPRRARP
Enzyme 25 Number of Residues 325
Enzyme 25 Molecular Weight 36599
Enzyme 25 Theoretical pI 8.95
Enzyme 25 GO Classification
Function
  • acid phosphatase activity
  • binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • ion binding
  • iron ion binding
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
  • transition metal ion binding
Process
—
Component
—
Enzyme 25 General Function Not Available
Enzyme 25 Specific Function A phosphate monoester + H(2)O = an alcohol + phosphate
Enzyme 25 Pathways
Enzyme 25 Reactions
  • A phosphate monoester + H2O = an alcohol + phosphate
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • 1-21
Enzyme 25 Transmembrane Regions Not Available
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 178006 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID P13686 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name PPA5_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >972 bp 
ATGGACATGTGGACGGCGCTGCTCATCCTGCAAGCCTTGTTGCTACCCTCCCTGGCTGAT
GGTGCCACCCCTGCCCTGCGCTTTGTAGCCGTGGGTGACTGGGGAGGGGTCCCCAATGCC
CCATTCCACACGGGCCCGGAAATGGCCAATGCCAAGGAGATCGCTCGGACTGTGCAGATC
CTGGGTGCAGACTTCATCCTGTCTCTAGGGGACAATTTTTACTTCACTGGTGTGCAAGAC
ATCAATGACAAGAGGTTCCAGGAGACCTTTGAGGACGTATTCTCTGACCGCTCCCTTCGC
AAAGTGCCCTGGTACGTGCTAGCCGGAAACCATGACCACCTTGGCAATGTCTCTGCCCAG
ATTGCATACTCTAAGATCTCCAAGCGCTGGAACTTCCCCAGCCCTTTCTACCGCCTGCAC
TTCAAGATCCCACAGACCAATGTGTCTGTGGCCATTTTTATGCTGGACACAGTGACACTA
TGTGGCAACTCAGATGACTTCCTCAGCCAGCAGCCTGAGAGGCCCCGACTAACTGCCCGC
ACACAGCTGTCCTGGCTCAAGAAACAGCTGGCGGCGGCCAGGGAGGACTACGTGCTGGTG
GCTGGCCACTACCCCGTGTGGTCCATAGCCGAGCACGGGCCTACCCACTGCCTGGTCAAG
CAGCTACGGCCACTGCTGGCCACATACGGGGTCACTGCCTACCTGTGCGGCCACGATCAC
AATCTGCAGTACCTGCAAGATGAGAATGGCGTGGGCTACGTGCTGAGTGGGGCTGGGAAT
TTCATGGACCCCTCAAAGCGGCACCAGCGCAAGGTCCCCAACGGCTATCTGCGCTTCCAC
TATGGGACTGAAGACTCACTGGGTGGCTTTGCCTATGTGGAGATCAGCTCCAAAGAGATG
ACTGTCACTTACATCGAGGCCTCGGGCAAGTCCCTCTTTAAGACCAGGCTGCCGAGGCGA
GCCAGGCCCTGA
Enzyme 25 GenBank Gene ID J04430 Link Image
Enzyme 25 GeneCard ID ACP5 Link Image
Enzyme 25 GenAtlas ID ACP5 Link Image
Enzyme 25 HGNC ID HGNC:124 Link Image
Enzyme 25 Chromosome Location 19
Enzyme 25 Locus 19p13.3-p13.2
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Ketcham CM, Roberts RM, Simmen RC, Nick HS: Molecular cloning of the type 5, iron-containing, tartrate-resistant acid phosphatase from human placenta. J Biol Chem. 1989 Jan 5;264(1):557-63. [PubMed Link Image]
  2. Lord DK, Cross NC, Bevilacqua MA, Rider SH, Gorman PA, Groves AV, Moss DW, Sheer D, Cox TM: Type 5 acid phosphatase. Sequence, expression and chromosomal localization of a differentiation-associated protein of the human macrophage. Eur J Biochem. 1990 Apr 30;189(2):287-93. [PubMed Link Image]
  3. Cassady AI, King AG, Cross NC, Hume DA: Isolation and characterization of the genes encoding mouse and human type-5 acid phosphatase. Gene. 1993 Aug 25;130(2):201-7. [PubMed Link Image]
  4. Stepan JJ, Lau KH, Mohan S, Kraenzlin M, Baylink DJ: Purification and N-terminal sequence of two tartrate-resistant acid phosphatases type-5 from the hairy cell leukemia spleen. Biochem Biophys Res Commun. 1989 Dec 29;165(3):1027-34. [PubMed Link Image]
  5. Stepan JJ, Lau KH, Mohan S, Singer FR, Baylink DJ: Purification and N-terminal amino acid sequence of the tartrate-resistant acid phosphatase from human osteoclastoma: evidence for a single structure. Biochem Biophys Res Commun. 1990 Apr 30;168(2):792-800. [PubMed Link Image]
  6. Hayman AR, Warburton MJ, Pringle JA, Coles B, Chambers TJ: Purification and characterization of a tartrate-resistant acid phosphatase from human osteoclastomas. Biochem J. 1989 Jul 15;261(2):601-9. [PubMed Link Image]
  7. Hayman AR, Dryden AJ, Chambers TJ, Warburton MJ: Tartrate-resistant acid phosphatase from human osteoclastomas is translated as a single polypeptide. Biochem J. 1991 Aug 1;277 ( Pt 3):631-4. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 5330
Enzyme 26 Name Prostatic acid phosphatase precursor
Enzyme 26 Synonyms Not Available
Enzyme 26 Gene Name ACPP
Enzyme 26 Protein Sequence >Prostatic acid phosphatase precursor 
MRAAPLLLARAASLSLGFLFLLFFWLDRSVLAKELKFVTLVFRHGDRSPIDTFPTDPIKE
SSWPQGFGQLTQLGMEQHYELGEYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNL
AALFPPEGVSIWNPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKR
LHPYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTMTKLRELSE
LSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMYSAHDTTVSGLQMAL
DVYNGLLPPYASCHLTELYFEKGEYFVEMYYRNETQHEPYPLMLPGCSPSCPLERFAELV
GPVIPQDWSTECMTTNSHQGTEDSTD
Enzyme 26 Number of Residues 386
Enzyme 26 Molecular Weight 44567
Enzyme 26 Theoretical pI 6.19
Enzyme 26 GO Classification
Function
  • acid phosphatase activity
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • phosphoric ester hydrolase activity
  • phosphoric monoester hydrolase activity
Process
—
Component
—
Enzyme 26 General Function Not Available
Enzyme 26 Specific Function A phosphate monoester + H(2)O = an alcohol + phosphate
Enzyme 26 Pathways
Enzyme 26 Reactions
  • A phosphate monoester + H2O = an alcohol + phosphate
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • 1-32
Enzyme 26 Transmembrane Regions Not Available
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 189613 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P15309 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name PPAP_HUMAN Link Image
Enzyme 26 PDB ID 1ND6 Link Image
Enzyme 26 PDB File Show
Enzyme 26 3D Structure
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >1161 bp 
ATGAGAGCTGCACCCCTCCTCCTGGCCAGGGCAGCAAGCCTTAGCCTTGGCTTCTTGTTT
CTGCTTTTTTTCTGGCTAGACCGAAGTGTACTAGCCAAGGAGTTGAAGTTTGTGACTTTG
GTGTTTCGGCATGGAGACCGAAGTCCCATTGACACCTTTCCCACTGACCCCATAAAGGAA
TCCTCATGGCCACAAGGATTTGGCCAACTCACCCAGCTGGGCATGGAGCAGCATTATGAA
CTTGGAGAGTATATAAGAAAGAGATATAGAAAATTCTTGAATGAGTCCTATAAACATGAA
CAGGTTTATATTCGAAGCACAGACGTTGACCGGACTTTGATGAGTGCTATGACAAACCTG
GCAGCCCTGTTTCCCCCAGAAGGTGTCAGCATCTGGAATCCTATCCTACTCTGGCAGCCC
ATCCCGGTGCACACAGTTCCTCTTTCTGAAGATCAGTTGCTATACCTGCCTTTCAGGAAC
TGCCCTCGTTTTCAAGAACTTGAGAGTGAGACTTTGAAATCAGAGGAATTCCAGAAGAGG
CTGCACCCTTATAAGGATTTTATAGCTACCTTGGGAAAACTTTCAGGATTACATGGCCAG
GACCTTTTTGGAATTTGGAGTAAAGTCTACGACCCTTTATATTGTGAGAGTGTTCACAAT
TTCACTTTACCCTCCTGGGCCACTGAGGACACCATGACTAAGTTGAGAGAATTGTCAGAA
TTGTCCCTCCTGTCCCTCTATGGAATTCACAAGCAGAAAGAGAAATCTAGGCTCCAAGGG
GGTGTCCTGGTCAATGAAATCCTCAATCACATGAAGAGAGCAACTCAGATACCAAGCTAC
AAAAAACTTATCATGTATTCTGCGCATGACACTACTGTGAGTGGCCTACAGATGGCGCTA
GATGTTTACAACGGACTCCTTCCTCCCTATGCTTCTTGCCACTTGACGGAATTGTACTTT
GAGAAGGGGGAGTACTTTGTGGAGATGTACTACCGGAATGAGACGCAGCACGAGCCGTAT
CCCCTCATGCTACCTGGCTGCAGCCCCAGCTGTCCTCTGGAGAGGTTTGCTGAGCTGGTT
GGCCCTGTGATCCCTCAAGACTGGTCCACGGAGTGTATGACCACAAACAGCCATCAAGGT
ACTGAGGACAGTACAGATTAG
Enzyme 26 GenBank Gene ID M97589 Link Image
Enzyme 26 GeneCard ID ACPP Link Image
Enzyme 26 GenAtlas ID ACPP Link Image
Enzyme 26 HGNC ID HGNC:125 Link Image
Enzyme 26 Chromosome Location 3
Enzyme 26 Locus 3q21-q23
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Sharief FS, Li SS: Structure of human prostatic acid phosphatase gene. Biochem Biophys Res Commun. 1992 May 15;184(3):1468-76. [PubMed Link Image]
  2. Van Etten RL, Davidson R, Stevis PE, MacArthur H, Moore DL: Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase. J Biol Chem. 1991 Feb 5;266(4):2313-9. [PubMed Link Image]
  3. Sharief FS, Lee H, Leuderman MM, Lundwall A, Deaven LL, Lee CL, Li SS: Human prostatic acid phosphatase: cDNA cloning, gene mapping and protein sequence homology with lysosomal acid phosphatase. Biochem Biophys Res Commun. 1989 Apr 14;160(1):79-86. [PubMed Link Image]
  4. Vihko P, Virkkunen P, Henttu P, Roiko K, Solin T, Huhtala ML: Molecular cloning and sequence analysis of cDNA encoding human prostatic acid phosphatase. FEBS Lett. 1988 Aug 29;236(2):275-81. [PubMed Link Image]
  5. Tailor PG, Govindan MV, Patel PC: Nucleotide sequence of human prostatic acid phosphatase determined from a full-length cDNA clone. Nucleic Acids Res. 1990 Aug 25;18(16):4928. [PubMed Link Image]
  6. Sharief FS, Li SS: Nucleotide sequence of human prostatic acid phosphatase ACPP gene, including seven Alu repeats. Biochem Mol Biol Int. 1994 Jun;33(3):561-5. [PubMed Link Image]
  7. LaCount MW, Handy G, Lebioda L: Structural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase. J Biol Chem. 1998 Nov 13;273(46):30406-9. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 5331
Enzyme 27 Name Alkaline phosphatase, placental-like precursor
Enzyme 27 Synonyms
  1. Alkaline phosphatase Nagao isozyme
  2. Germ-cell alkaline phosphatase
  3. GCAP
  4. PLAP-like
  5. ALP-1
Enzyme 27 Gene Name ALPPL2
Enzyme 27 Protein Sequence >Alkaline phosphatase, placental-like precursor 
MQGPWVLLLLGLRLQLSLGIIPVEEENPDFWNRQAAEALGAAKKLQPAQTAAKNLIIFLG
DGMGVSTVTAARILKGQKKDKLGPETFLAMDRFPYVALSKTYSVDKHVPDSGATATAYLC
GVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAGAYA
HTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPDDY
SQGGTRLDGKNLVQEWLAKHQGARYVWNRTELLQASLDPSVTHLMGLFEPGDMKYEIHRD
STLDPSLMEMTEAALLLLSRNPRGFFLFVEGGRIDHGHHESRAYRALTETIMFDDAIERA
GQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPGYVL
KDGARPDVTESESGSPEYRQQSAVPLDGETHAGEDVAVFARGPQAHLVHGVQEQTFIAHV
MAFAACLEPYTACDLAPRAGTTDAAHPGPSVVPALLPLLAGTLLLLGTATAP
Enzyme 27 Number of Residues 532
Enzyme 27 Molecular Weight 57378
Enzyme 27 Theoretical pI 6.31
Enzyme 27 GO Classification
Function
—
Process
  • metabolism
  • physiological process
Component
—
Enzyme 27 General Function Inorganic ion transport and metabolism
Enzyme 27 Specific Function A phosphate monoester + H(2)O = an alcohol + phosphate
Enzyme 27 Pathways
  • Folate and Pterine Biosynthesis (map00790 Link Image)
  • gamma-Hexachlorocyclohexane Degradation (map00361 Link Image)
Enzyme 27 Reactions
  • A phosphate monoester + H2O = an alcohol + phosphate
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • 1-19
Enzyme 27 Transmembrane Regions Not Available
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 178428 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID P10696 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name PPBN_HUMAN Link Image
Enzyme 27 PDB ID 1EW2 Link Image
Enzyme 27 PDB File Show
Enzyme 27 3D Structure
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >1599 bp 
ATGCAGGGGCCCTGGGTGCTGCTCCTGCTGGGCCTGAGGCTACAGCTCTCCCTGGGCATC
ATCCCAGTTGAGGAGGAGAACCCGGACTTCTGGAACCGCCAGGCAGCCGAGGCCCTGGGT
GCCGCCAAGAAGCTGCAGCCTGCACAGACAGCCGCCAAGAACCTCATCATGTTCCTGGGT
GACGGGATGGGGGTGTCTACGGTGACAGCTGCCAGGATCCTAAAAGGGCAGAAGAAGGAC
AAACTGGGGCCTGAGACCTTCCTGGCCATGGACCGCTTCCCGTACGTGGCTCTGTCCAAG
ACATACAGTGTAGACAAGCATGTGCCAGACAGTGGAGCCACAGCCACGGCCTACCTGTGC
GGGGTCAAGGGCAACTTCCAGACCATTGGCTTGAGTGCAGCCGCCCGCTTTAACCAGTGC
AACACGACACGCGGCAACGAGGTCATCTCCGTGGTGAATCGGGCCAAGAAAGCAGGAAAG
TCAGTGGGAGTGGTAACCACCACACGGGTGCAGCATGCCTCGCCAGCCGGCACCTACGCC
CACACGGTGAACCGCAACTGGTACTCGGATGCCGACGTGCCTGCCTCGGCCCGCCAGGAG
GGGTGCCAGGACATCGCCACGCAGCTCATCTCCAACATGGACATTGATGTGATCCTAGGT
GGAGGCCGAAAGTACATGTTTCCCATGGGGACCCCAGACCCTGAGTACCCAGATGACTAC
AGCCAAGGTGGGACCAGGCTGGACGGGAAGAATCTGGTGCAGGAATGGCTGGCGAAGCAC
CAGGGTGCCCGGTACGTGTGGAACCGCACTGAGCTCCTGCAGGCTTCCCTGGACCCGTCT
GTGACCCATCTCATGGGTCTCTTTGAGCCTGGAGACATGAAATACGAGATCCACCGAGAC
TCCACACTGGACCCCTCCCTGATGGAGATGACAGAGGCTGCCCTGCTCCTGCTGAGCAGG
AACCCCCGCGGCTTCTTCCTCTTCGTGGAGGGTGGTCGCATCGACCATGGTCATCATGAA
AGCAGGGCTTACCGGGCACTGACTGAGACGATCATGTTCGACGACGCCATTGAGAGGGCG
GGCCAGCTCACCAGCGAGGAGGACACGCTGAGCCTCGTCACTGCCGACCACTCCCACGTC
TTCTCCTTCGGAGGCTACCCCCTGCGAGGGAGCTCCATCTTCGGGCTGGCCCCTGGCAAG
GCCCGGGACAGGAAGGCCTACACGGTCCTCCTATACGGAAACGGTCCAGGCTATGTGCTC
AAGGACGGCGCCCGGCCGGATGTTACGGAGAGCGAGAGCGGGAGCCCCGAGTATCGGCAG
CAGTCAGCAGTGCCCCTGGACGGAGAGACCCACGCAGGCGAGGACGTGGCGGTGTTCGCG
CGCGGCCCGCAGGCGCACCTGGTTCACGGCGTGCAGGAGCAGACCTTCATAGCGCACGTC
ATGGCCTTCGCCGCCTGCCTGGAGCCCTACACCGCCTGCGACCTGGCGCCCCCCGCCGGC
ACCACCGACGCCGCGCACCCGGGGCCGTCCGTGGTCCCCGCGTTGCTTCCTCTGCTGGCA
GGGACCTTGCTGCTGCTGGGGACGGCCACTGCTCCCTGA
Enzyme 27 GenBank Gene ID J03252 Link Image
Enzyme 27 GeneCard ID ALPPL2 Link Image
Enzyme 27 GenAtlas ID ALPPL2 Link Image
Enzyme 27 HGNC ID HGNC:441 Link Image
Enzyme 27 Chromosome Location 2
Enzyme 27 Locus 2q37
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Millan JL, Manes T: Seminoma-derived Nagao isozyme is encoded by a germ-cell alkaline phosphatase gene. Proc Natl Acad Sci U S A. 1988 May;85(9):3024-8. [PubMed Link Image]
  2. Watanabe S, Watanabe T, Li WB, Soong BW, Chou JY: Expression of the germ cell alkaline phosphatase gene in human choriocarcinoma cells. J Biol Chem. 1989 Jul 25;264(21):12611-9. [PubMed Link Image]
  3. Gum JR, Hicks JW, Sack TL, Kim YS: Molecular cloning of complementary DNAs encoding alkaline phosphatase in human colon cancer cells. Cancer Res. 1990 Feb 15;50(4):1085-91. [PubMed Link Image]
  4. Lowe ME, Strauss AW: Expression of a Nagao-type, phosphatidylinositol-glycan anchored alkaline phosphatase in human choriocarcinomas. Cancer Res. 1990 Jul 1;50(13):3956-62. [PubMed Link Image]
  5. Shen LP, Liu H, Kan YW, Kam W: 5' nucleotide sequence of a putative human placental alkaline phosphatase-like gene. Nucleic Acids Res. 1988 Jun 24;16(12):5694. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 5340
Enzyme 28 Name Ribonucleoside-diphosphate reductase large subunit
Enzyme 28 Synonyms
  1. Ribonucleoside-diphosphate reductase M1 subunit
  2. Ribonucleotide reductase large chain
Enzyme 28 Gene Name RRM1
Enzyme 28 Protein Sequence >Ribonucleoside-diphosphate reductase large subunit 
MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLA
AETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKST
LDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHK
EDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCAL
ISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIY
LEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLD
EVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNL
GTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKI
IDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGAL
EASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIA
PMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQII
ACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKL
TSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCS
LENRDECLMCGS
Enzyme 28 Number of Residues 792
Enzyme 28 Molecular Weight 90071
Enzyme 28 Theoretical pI 7.16
Enzyme 28 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH2 groups
  • oxidoreductase activity, acting on CH2 groups, disulfide as acceptor
  • ribonucleoside-diphosphate reductase activity
Process
  • DNA metabolism
  • DNA replication
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • protein complex
  • ribonucleoside-diphosphate reductase complex
Enzyme 28 General Function Nucleotide transport and metabolism
Enzyme 28 Specific Function Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides
Enzyme 28 Pathways
Enzyme 28 Reactions
  • 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 36065 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID P23921 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name RIR1_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >2379 bp 
ATGCATGTGATCAAGCGAGATGGCCGCCAAGAACGAGTCATGTTTGACAAAATTACATCT
CGAATCCAGAAGCTTTGTTATGGACTCAATATGGATTTTGTTGATCCTGCTCAGATCACC
ATGAAAGTAATCCAAGGCTTGTACAGTGGGGTCACCACAGTGGAACTAGATACTTTGGCT
GCTGAAACAGCTGCAACCTTGACTACTAAGCACCCTGACTATGCTATCCTGGCAGCCAGG
ATCGCTGTCTCTAACTTGCACAAAGAAACAAAGAAAGTGTTCAGTGATGTGATGGAAGAC
CTCTATAACTACATAAATCCACATAATGGCAAACACTCTCCCATGGTGGCCAAGTCAACA
TTGGATATTGTTCTGGCCAATAAAGATCGCCTGAATTCTGCTATTATCTATGACCGAGAT
TTCTCTTACAATTACTTCGGCTTTAAGACGCTAGAGCGGTCTTATTTGTTGAAGATCAAT
GGAAAAGTGGCTGAAAGACCACAACATATGTTGATGAGAGTATCTGTTGGGATCCACAAA
GAAGACATTGATGCAGCAATTGAAACATATAATCTTCTTTCTGAGAGGTGGTTTACTCAT
GCTTCGCCCACTCTCTTCAATGCTGGTACCAACCGCCCACAACTTTCTAGCTGTTTTCTT
CTGAGTATGAAAGATGACAGCATTGAAGGCATTTATGACACTCTAAAGCAATGTGCATTG
ATTTCTAAGTCTGCTGGAGGAATTGGTGTTGCTGTGAGTTGTATTCGGGCTACTGGCAGC
TACATTGCTGGGACTAATGGCAATTCCAATGGCCTTGTACCGATGCTGAGAGTATATAAC
AACACAGCTCGATATGTGGATCAAGGTGGGAACAAGCGTCCTGGGGCATTTGCTATTTAC
CTGGAGCCTTGGCATTTAGACATCTTTGAATTCCTTGATTTAAAGAAGAACACAGGAAAG
GAAGAGCAGCGTGCCAGAGATCTTTTCTTTGCTCTTTGGATTCCGGATCTCTTCATGAAA
CGAGTGGAGACTAATCAGGACTGGTCTTTGATGTGTCCAAATGAGTGTCCTGGTCTGGAT
GAGGTTTGGGGAGAGGAATTTGAGAAACTATATGCAAGTTATGAGAAACAAGGTCGTGTC
CGCAAAGTTGTAAAAGCTCAGCAGCTTTGGTATGCCATCATTGAGTCTCAGACGGAAACA
GGCACCCCGTATATGCTCTACAAAGATTCCTGTAATCGAAAGAGCAACCAGCAGAACCTG
GGAACCATCAAATGCAGCAACCTGTGCACAGAAATAGTGGAGTACACCAGCAAAGATGAG
GTTGCTGTTTGTAATTTGGCTTCCCTGGCCCTGAATATGTATGTCACATCAGAACACACA
TACGACTTTAAGAAGTTGGCTGAAGTCACTAAAGTCGTTGTCCGAAACTTGAATAAAATT
ATTGATATAAACTACTATCCTGTACCAGAGGCATGCCTATCAAATAAACGCCATCGCCCC
ATTGGAATTGGGGTACAAGGTCTGGCAGATGCTTTTATCCTGATGAGATACCCTTTTGAG
AGTGCAGAAGCCCAGTTACTGAATAAGCAGATCTTTGAAACTATTTATTATGGTGCTCTG
GAAGCCAGCTGTGACCTTGCCAAGGAGCAGGGCCCATACGAAACCTATGAGGGCTCTCCA
GTTAGCAAAGGAATTCTTCAGTATGATATGTGGAATGTTACTCCTACAGACCTATGGGAC
TGGAAGGTTCTCAAGGAGAAGATTGCAAAGTATGGTATAAGAAACAGTTTACTTATTGCC
CCGATGCCTACAGCTTCCACTGCTCAGATCCTGGGGAATAATGAGTCCATTGAACCTTAC
ACCAGCAACATCTATACTCGCAGAGTCTTGTCAGGAGAATTTCAGATTGTAAATCCTCAC
TTATTGAAAGATCTTACCGAGCGGGGCCTATGGCATGAAGAGATGAAAAACCAGATTATT
GCATGCAATGGCTCTATTCAGAGCATACCAGAAATTCCTGATGACCTGAAGCAACTTTAT
AAAACTGTGTGGGAAATCTCTCAGAAAACTGTTCTCAAGATGGCAGCTGAGAGAGGTGCT
TTCATTGATCAAAGCCAATCTTTGAACATCCACATTGCTGAGCCTAACTATGGCAAACTC
ACTAGTATGCACTTCTACGGCTGGAAGCAGGGTTTGAAGACTGGGATGTATTATTTAAGG
ACGAGACCAGCAGCTAATCCAATCCAGTTCACTCTAAATAAGGAGAAGCTAAAAGATAAA
GAAAAGGTATCAAAAGAGGAAGAAGAGAAGGAGAGGAACACAGCAGCCATGGTGTGCTCT
TTGGAGAATAGAGATGAATGTCTGATGTGTGGATCCTGA
Enzyme 28 GenBank Gene ID X59543 Link Image
Enzyme 28 GeneCard ID RRM1 Link Image
Enzyme 28 GenAtlas ID RRM1 Link Image
Enzyme 28 HGNC ID HGNC:10451 Link Image
Enzyme 28 Chromosome Location 11
Enzyme 28 Locus 11p15.5
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Parker NJ, Begley CG, Fox RM: Human M1 subunit of ribonucleotide reductase: cDNA sequence and expression in stimulated lymphocytes. Nucleic Acids Res. 1991 Jul 11;19(13):3741. [PubMed Link Image]
  2. Pavloff N, Rivard D, Masson S, Shen SH, Mes-Masson AM: Sequence analysis of the large and small subunits of human ribonucleotide reductase. DNA Seq. 1992;2(4):227-34. [PubMed Link Image]
  3. Bepler G, O'briant KC, Kim YC, Schreiber G, Pitterle DM: A 1.4-Mb high-resolution physical map and contig of chromosome segment 11p15.5 and genes in the LOH11A metastasis suppressor region. Genomics. 1999 Jan 15;55(2):164-75. [PubMed Link Image]
  4. Parker NJ, Begley CG, Fox RM: Human R1 subunit of ribonucleotide reductase (RRM1): 5' flanking region of the gene. Genomics. 1994 Jan 1;19(1):91-6. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 5343
Enzyme 29 Name Ribonucleoside-diphosphate reductase M2 subunit
Enzyme 29 Synonyms
  1. Ribonucleotide reductase small subunit
  2. Ribonucleotide reductase small chain
Enzyme 29 Gene Name RRM2
Enzyme 29 Protein Sequence >Ribonucleoside-diphosphate reductase M2 subunit 
MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKT
KAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLK
PEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLI
DTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSF
ASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIE
QEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTN
FFEKRVGEYQRMGVMSSPTENSFTLDADF
Enzyme 29 Number of Residues 389
Enzyme 29 Molecular Weight 44878
Enzyme 29 Theoretical pI 5.05
Enzyme 29 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH2 groups
  • oxidoreductase activity, acting on CH2 groups, disulfide as acceptor
  • ribonucleoside-diphosphate reductase activity
Process
  • cellular metabolism
  • deoxyribonucleoside diphosphate metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside diphosphate metabolism
  • nucleotide metabolism
  • physiological process
Component
—
Enzyme 29 General Function Nucleotide transport and metabolism
Enzyme 29 Specific Function Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides
Enzyme 29 Pathways
Enzyme 29 Reactions
  • 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 36155 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID P31350 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name RIR2_HUMAN Link Image
Enzyme 29 PDB ID 1H0N Link Image
Enzyme 29 PDB File Show
Enzyme 29 3D Structure
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >1170 bp 
ATGCTCTCCCTCCGTGTCCCGCTCGCGCCCATCACGGACCCGCAGCAGCTGCAGCTCTCG
CCGCTGAAGGGGCTCAGCTTGGTCGACAAGGAGAACACGCCGCCGGCCCTGAGCGGGACC
CGCGTCCTGGCCAGCAAGACCGCGAGGAGGATCTTCCAGGAGCCCACGGAGCCGAAAACT
AAAGCAGCTGCCCCCGGCGTGGAGGATGAGCCGCTGCTGAGAGAAAACCCCCGCCGCTTT
GTCATCTTCCCCATCGAGTACCATGATATCTGGCAGATGTATAAGAAGGCAGAGGCTTCC
TTTTGGACCGCCGAGGAGGTTGACCTCTCCAAGGACATTCAGCACTGGGAATCCCTGAAA
CCCGAGGAGAGATATTTTATATCCCATGTTCTGGCTTTCTTTGCAGCAAGCGATGGCATA
GTAAATGAAAACTTGGTGGAGCGATTTAGCCAAGAAGTTCAGATTACAGAAGCCCGCTGT
TTCTATGGCTTCCAAATTGCCATGGAAAACATACATTCTGAAATGTATAGTCTTCTTATT
GACACTTACATAAAAGATCCCAAAGAAAGGGAATTTCTCTTCAATGCCATTGAAACGATG
CCTTGTGTCAAGAAGAAGGCAGACTGGGCCTTGCGCTGGATTGGGGACAAAGAGGCTACC
TATGGTGAACGTGTTGTAGCCTTTGCTGCAGTGGAAGGCATTTTCTTTTCCGGTTCTTTT
GCGTCGATATTCTGGCTCAAGAAACGAGGACTGATGCCTGGCCTCACATTTTCTAATGAA
CTTATTAGCAGAGATGAGGGTTTACACTGTGATTTTGCTTGCCTGATGTTCAAACACCTG
GTACACAAACCATCGGAGGAGAGAGTAAGAGAAATAATTATCAATGCTGTTCGGATAGAA
CAGGAGTTCCTCACTGAGGCCTTGCCTGTGAAGCTCATTGGGATGAATTGCACTCTAATG
AAGCAATACATTGAGTTTGTGGCAGACAGACTTATGCTGGAACTGGGTTTTAGCAAGGTT
TTCAGAGTAGAGAACCCATTTGACTTTATGGAGAATATTTCACTGGAAGGAAAGACTAAC
TTCTTTGAGAAGAGAGTAGGCGAGTATCAGAGGATGGGAGTGATGTCAAGTCCAACAGAG
AATTCTTTTACCTTGGATGCTGACTTCTAA
Enzyme 29 GenBank Gene ID X59618 Link Image
Enzyme 29 GeneCard ID RRM2 Link Image
Enzyme 29 GenAtlas ID RRM2 Link Image
Enzyme 29 HGNC ID HGNC:10452 Link Image
Enzyme 29 Chromosome Location 2
Enzyme 29 Locus 2p25-p24
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Pavloff N, Rivard D, Masson S, Shen SH, Mes-Masson AM: Sequence analysis of the large and small subunits of human ribonucleotide reductase. DNA Seq. 1992;2(4):227-34. [PubMed Link Image]
  2. Zhou B, Yen Y: Characterization of the human ribonucleotide reductase M2 subunit gene; genomic structure and promoter analyses. Cytogenet Cell Genet. 2001;95(1-2):52-9. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 5351
Enzyme 30 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Enzyme 30 Synonyms
  1. E- NPP 1
  2. Phosphodiesterase I/nucleotide pyrophosphatase 1
  3. Plasma-cell membrane glycoprotein PC-1[Includes: Alkaline phosphodiesterase I
  4. NPPase]
Enzyme 30 Gene Name ENPP1
Enzyme 30 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 1 
MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPL
EKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNC
RCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINY
SSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKK
CGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEW
YKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLP
KDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLIL
ISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSC
REPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNV
FSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVY
TPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYG
RPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPL
SPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTL
LRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKD
TSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSF
YQQRKEPVSDILKLKTHLPTFSQED
Enzyme 30 Number of Residues 925
Enzyme 30 Molecular Weight 104925
Enzyme 30 Theoretical pI 7.14
Enzyme 30 GO Classification
Function
  • binding
  • catalytic activity
  • endonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
—
Enzyme 30 General Function Not Available
Enzyme 30 Specific Function Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity
Enzyme 30 Pathways
Enzyme 30 Reactions
  • A dinucleotide + H2O = 2 mononucleotides
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • 77-97
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 189650 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID P22413 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name ENPP1_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >2622 bp 
ATGGACGTGGGGGAGGAGCCGCTGGAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCC
AACACCTATAAAGTACTCTCGCTGGTATTGTCAGTATGTGTGTTAACAACAATACTTGGT
TGTATATTTGGGTTGAAACCAAGCTGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGT
TTCGAGAGAACATTTGGGAACTGTCGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGC
TGTTTAGATTACCAGGAGACGTGCATAGAACCAGAACATATATGGACTTGCAACAAATTC
AGGTGTGGTGAGAAAAGGTTGACCAGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGAC
AAGGGCGACTGCTGCATCAACTACAGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAA
GAACCATGTGAGAGCATTAATGAGCCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACC
CTCTTATTTTCTTTGGATGGATTCAGGGCAGAATATTTACACACTTGGGGTGGACTTCTT
CCTGTTATTAGCAAACTAAAAAAATGTGGAACATATACTAAAAACATGAGACCGGTATAT
CCAACAAAAACTTTCCCCAATCACTACAGCATTGTCACCGGATTGTATCCAGAATCTCAT
GGCATAATCGACAATAAAATGTATGATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGT
AAAGAGAAATTTAATCCTGAGTGGTACAAAGGAGAACCAATTTGGGTCACAGCTAAGTAT
CAAGGCCTCAAGTCTGGCACATTTTTCTGGCCAGGATCAGATGTGGAAATTAACGGAATT
TTCCCAGACATCTATAAAATGTATAATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCT
GTTCTTCAGTGGCTACAGCTTCCTAAAGATGAAAGACCACACTTTTACACTCTGTATTTA
GAAGAACCAGATTCTTCAGGTCATTCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCC
TTGCAGAGGGTTGATGGTATGGTTGGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTG
CACAGATGCCTGAACCTCATCCTTATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAG
AAATACATATATCTGAATAAATATTTGGGGGATGTTAAAAATATTAAAGTTATCTATGGA
CCTGCAGCTCGATTGAGACCCTCTGATGTCCCAGATAAATACTATTCATTTAACTATGAA
GGCATTGCCCGAAATCTTTCTTGCCGGGAACCAAACCAGCACTTCAAACCTTACCTGAAA
CATTTCTTACCTAAGCGTTTGCACTTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTC
TATTTGGACCCTCAGTGGCAACTTGCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGT
GGATTTCATGGCTCTGACAATGTATTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGA
CCTGGATTCAAGCATGGCATTGAGGCTGACACCTTTGAAAACATTGAAGTCTATAACTTA
ATGTGTGATTTACTGAATTTGACACCGGCTCCTAATAACGGAACTCATGGAAGTCTTAAC
CACCTTCTAAAGAATCCTGTTTATACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTA
CAGTGCCCCTTCACAAGAAACCCCAGAGATAACCTTGGCTGCTCATGTAACCCTTCGATT
TTGCCGATTGAGGATTTTCAAACACAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATT
AAGCATGAAACTTTACCCTATGGAAGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGT
CTTCTTTCCCAGCACCAGTTTATGAGTGGATACAGCCAAGACATCTTAATGCCCCTTTGG
ACATCCTATACCGTGGACAGAAATGACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTG
TACCAGGACTTTAGAATTCCTCTTAGTCCTGTCCATAAATGTTCATTTTATAAAAATAAC
ACCAAAGTGAGTTACGGGTTCCTCTCCCCACCACAACTAAATAAAAATTCAAGTGGAATA
TATTCTGAAGCTTTGCTTACTACAAATATAGTGCCAATGTACCAGAGTTTTCAAGTTATA
TGGCGCTACTTTCATGACACCCTACTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAAT
GTCGTCAGTGGTCCTGTGTTTGACTTTGATTATGATGGACGTTGTGATTCCTTAGAGAAT
CTGAGGCAAAAAAGAAGAGTCATCCGTAACCAAGAAATTTTGATTCCAACTCACTTCTTT
ATTGTGCTAACAAGCTGTAAAGATACATCTCAGACGCCTTTGCACTGTGAAAACCTAGAC
ACCTTAGCTTTCATTTTGCCTCACAGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAG
CATGACTCCTCATGGGTTGAAGAATTGTTAATGTTACACAGAGCACGGATCACAGATGTT
GAGCACATCACTGGACTCAGCTTCTATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTA
AAGTTGAAAACACATTTGCCAACCTTTAGCCAAGAAGACTGA
Enzyme 30 GenBank Gene ID M57736 Link Image
Enzyme 30 GeneCard ID ENPP1 Link Image
Enzyme 30 GenAtlas ID ENPP1 Link Image
Enzyme 30 HGNC ID HGNC:3356 Link Image
Enzyme 30 Chromosome Location 6
Enzyme 30 Locus 6q22-q23
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Buckley MF, Loveland KA, McKinstry WJ, Garson OM, Goding JW: Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. J Biol Chem. 1990 Oct 15;265(29):17506-11. [PubMed Link Image]
  2. Funakoshi I, Kato H, Horie K, Yano T, Hori Y, Kobayashi H, Inoue T, Suzuki H, Fukui S, Tsukahara M, et al.: Molecular cloning of cDNAs for human fibroblast nucleotide pyrophosphatase. Arch Biochem Biophys. 1992 May 15;295(1):180-7. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  4. Pizzuti A, Frittitta L, Argiolas A, Baratta R, Goldfine ID, Bozzali M, Ercolino T, Scarlato G, Iacoviello L, Vigneri R, Tassi V, Trischitta V: A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding region is strongly associated with insulin resistance. Diabetes. 1999 Sep;48(9):1881-4. [PubMed Link Image]
  5. Belli SI, Goding JW: Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities. Eur J Biochem. 1994 Dec 1;226(2):433-43. [PubMed Link Image]
  6. Belli SI, Mercuri FA, Sali A, Goding JW: Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide pyrophosphatase) and analysis of the active site. Eur J Biochem. 1995 Mar 15;228(3):669-76. [PubMed Link Image]
  7. Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed Link Image]
  8. Nakamura I, Ikegawa S, Okawa A, Okuda S, Koshizuka Y, Kawaguchi H, Nakamura K, Koyama T, Goto S, Toguchida J, Matsushita M, Ochi T, Takaoka K, Nakamura Y: Association of the human NPPS gene with ossification of the posterior longitudinal ligament of the spine (OPLL). Hum Genet. 1999 Jun;104(6):492-7. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 5358
Enzyme 31 Name Aldehyde oxidase
Enzyme 31 Synonyms Not Available
Enzyme 31 Gene Name AOX1
Enzyme 31 Protein Sequence >Aldehyde oxidase 
MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTPYGCGGGGCGACTVMISRYN
PITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPG
MVMSIYPLLRNHPEPTLDQLTDALGGNLCRCHGYRPIIDACKTFCKTSGCCQSKENGVCC
LDQGINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMADKQSQRTRVFGSER
MMWFSPVTLKDLLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPGYNSPDRIEEPECCKPC
IYGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHII
SRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPISR
KWEFVSAFRQAQRQENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKL
IGRHWNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQILKKMDPV
HYPSLADKYESALEDLHSKHHCSTLKYQNIGPKQHPEDPIGHPIMHLSGVKHATGEAIYC
DDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDIMTAEHLSDVNSFCFFTEAE
KFLATDKVFCVGQLVCAVLADSEVQAKRAAKRVKIVYQDLEPLILTIEESIQHNSSFKPE
RKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKY
IQDIVASTLKLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGE
DMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLDESLFVIEMGLLKMDNAYKF
PNLRCRGWACRTNLPSNTAFRGFGFPQAVLITESCITEVAAKCGLSPEKVRIINMYKEID
QTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNAENYWKKKGLAMVPLKFPVGLAS
RAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETV
PNANISGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVG
YFRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAID
IGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTELHIALLPPSQNSN
TLYSSKGLGESGVFLGCSVFFAIHDAVSAARQERGLHGPLTLNSPLTPEKIRMACEDKFT
KMIPRDEPGSYVPWNVPI
Enzyme 31 Number of Residues 1338
Enzyme 31 Molecular Weight 147933
Enzyme 31 Theoretical pI 7.11
Enzyme 31 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron transporter activity
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 31 General Function Nucleotide transport and metabolism
Enzyme 31 Specific Function An aldehyde + H(2)O + O(2) = a carboxylic acid + H(2)O(2)
Enzyme 31 Pathways
Enzyme 31 Reactions
  • an aldehyde + H2O + O2 = a carboxylic acid + H2O2
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 438656 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q06278 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name ADO_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >4017 bp 
ATGGACCGGGCGTCCGAGCTGCTCTTCTACGTGAACGGCCGCAAGGTGATAGAAAAAAAT
GTCGATCCTGAAACAATGCTGTTGCCTTATTTGAGGAAGAAGCTTCGACTCACAGGAACT
CCGTATGGCTGTGGAGGAGGAGGCTGTGGTGCTTGTACAGTGATGATATCACGATACAAC
CCCATCACCAAGAGGATAAGGCATCACCCAGCCAATGCCTGTCTGATTCCCATCTGTTCT
CTGTATGGTGCTGCCGTCACCACAGTAGAAGGCATAGGAAGCACCCACACCAGAATTCAT
CCTGTTCAGGAGAGGATTGCCAAGTGTCATGGCACCCAGTGTGGCTTCTGCACACCTGGG
ATGGTGATGTCCATCTACCCCCTGCTCAGGAACCACCCAGAGCCCACTCTGGATCAGTTA
ACTGATGCCCTTGGTGGTAACCTGTGCCGTTGCCATGGATACAGGCCCATAATTGATGCA
TGCAAGACTTTCTGTAAAACTTCGGGCTGCTGTCAAAGTAAAGAAAATGGGGTTTGCTGT
TTGGATCAAGGAATCAATGGATTGCCAGAATTTGAGGAAGGAAGTAAGACAAGTCCAAAA
CTCTTCGCAGAAGAGGAGTTTCTGCCATTGGATCCAACCCAGGAACTGATATTTCCTCCT
GAGCTAATGATAATGGCTGATAAACAGTCGCAAAGGACCAGGGTGTTTGGCAGTGAGAGA
ATGATGTGGTTTTCCCCCGTGACCCTGAAGGACCTGCTGGAATTTAAATTCAAGTATCCC
CAGGCTCCTGTTATCATGGGAAACACCTCTGTGGGGCCTGAAGTGAAATTTAAAGGCGTC
TTTCACCCAGGTTATAATTCTCCTGATAGAATTGAAGAACCTGAGTGTTGTAAACCATGC
ATATATGGACTCACCCTTGGTGCTGGTCTCAGCCTAGCCCAGGTGAAGGACATTTTGGCT
GATGTAGTCCAGAAGCTTCCAGAGGAGAAGACACAGATGTACCATGCTCTCCTGAAGCAT
TTGGGAACTCTGGCTGGGTCCCAGATCAGGAACATGGCTTCTTTAGGGGGACACATCATT
AGCAGGCATCCAGATTCAGATCTGAATCCCATCCTGGCTGTGGGTAACTGTACCCTCAAC
TTGCTATCAAAAGAAGGAAAACGACAGATTCCTTTAAATGAGCAATTCCTCAGCAAGTGC
CCTAATGCAGATCTTAAGCCTCAAGAAATCTTGGTCTCAGTGAACATCCCCATCTCAAGG
AAGTGGGAATTTGTGTCAGCCTTCCGACAAGCCCAGCGACAGGAGAATGCGCTAGCGATA
GTCAATTCAGGAATGAGAGTCTTTTTTGGAGAAGGGGATGGCATTATTAGAGAGTTATGC
ATCTCATATGGAGGCGTTGGTCCAGCCACCATCTGTGCCAAGAATTCCTGCCAGAAACTC
ATTGGAAGGCACTGGAACGAACAGATGCTGGATATAGCCTGCAGGCTTATTCTGAATGAA
GTCTCCCTTTTGGGCTCGGCGCCAGGTGGGAAAGTGGAGTTCAAGAGGACTCTCATCATC
AGCTTCCTCTTCAAGTTCTACCTGGAAGTGTCACAGATTTTGAAAAAGATGGATCCAGTT
CACTATCCTAGCCTTGCAGACAAGTATGAAAGTGCTTTAGAAGATCTTCATTCCAAACAT
CACTGCAGTACATTAAAGTACCAGAATATAGGCCCAAAGCAGCATCCTGAAGACCCAATT
GGCCACCCCATCATGCATCTGTCTGGTGTGAAGCATGCCACGGGGGAGGCCATCTACTGT
GATGACATGCCTCTGGTGGACCAGGAACTTTTCTTGACTTTTGTGACTAGTTCAAGAGCT
CATGCTAAGATTGTGTCTATTGATCTGTCAGAAGCTCTCAGCATGCCCGGTGTGGTGGAC
ATCATGACAGCAGAACATCTTAGTGACGTCAACTCCTTCTGCTTTTTTACTGAAGCTGAG
AAATTTCTGGCGACAGATAAGGTGTTCTGTGTGGGTCAGCTTGTCTGTGCTGTGCTTGCC
GATTCTGAGGTTCAGGCAAAGCGAGCTGCTAAGCGAGTGAAGATTGTCTATCAAGACTTG
GAGCCGCTGATACTAACAATTGAGGAAAGTATACAACACAACTCCTCCTTCAAGCCAGAA
AGGAAACTGGAATATGGAAATGTTGACGAAGCATTTAAAGTGGTTGATCAAATTCTTGAA
GGTGAAATACATATGGGAGGTCAAGAACATTTTTATATGGAAACCCAAAGCATGCTTGTC
GTTCCCAAGGGAGAGGATCAAGAAATGGATGTCTACGTGTCCACACAGTTTCCCAAATAT
ATACAGGACATTGTTGCCTCAACCTTGAAGCTCCCAGCTAACAAGGTCATGTGCCATGTA
AGGCGTGTTGGTGGAGCGTTTGGAGGGAAGGTGTTAAAAACCGGAATCATTGCAGCCGTC
ACTGCATTTGCCGCAAACAAACATGGCCGTGCAGTTCGCTGTGTTCTGGAACGAGGAGAA
GACATGTTAATAACTGGAGGCCGCCATCCTTACCTTGGAAAGTACAAAGCTGGATTCATG
AACGATGGCAGAATCTTGGCCCTGGACATGGAGCATTACAGCAATGCAGGCGCCTCCTTG
GATGAATCATTATTCGTGATAGAAATGGGACTTCTGAAAATGGACAATGCTTACAAGTTT
CCCAATCTCCGCTGCCGGGGTTGGGCATGCAGAACCAACCTTCCATCCAACACAGCTTTT
CGTGGGTTTGGCTTTCCTCAGGCAGTGCTGATCACCGAATCTTGTATCACGGAAGTTGCA
GCCAAATGTGGACTATCCCCTGAGAAGGTGCGAATCATAAACATGTACAAGGAAATTGAT
CAAACACCCTACAAACAAGAGATCAATGCCAAGAACCTAATCCAGTGTTGGAGAGAATGT
ATGGCCATGTCTTCCTACTCCTTGAGGAAAGTTGCTGTGGAAAAGTTCAATGCAGAGAAT
TATTGGAAGAAGAAAGGACTGGCCATGGTCCCCCTGAAGTTTCCTGTTGGCCTTGCGTCA
CGTGCTGCTGGTCAGGCTGCTGCCTTGGTTCACATTTATCTTGATGGCTCTGTGCTGGTC
ACTCACGGTGGAATTGAAATGGGGCAGGGGGTCCACACTAAAATGATTCAGGTGGTCAGC
CGTGAATTAAGAATGCCAATGTCGAATGTCCACCTGCGTGGAACAAGCACAGAAACTGTC
CCTAATGCAAATATCTCTGGAGGTTCTGTGGTGGCAGATCTCAACGGTTTGGCAGTAAAG
GATGCCTGTCAAACTCTTCTAAAACGCCTCGAACCCATCATCAGCAAGAATCCTAAAGGA
ACTTGGAAAGACTGGGCACAGACTGCTTTTGATGAAAGCATTAACCTTTCAGCTGTTGGA
TACTTCAGAGGTTATGAGTCAGACATGAACTGGGAGAAAGGCGAAGGCCAGCCCTTCGAA
TACTTTGTTTATGGAGCTGCCTGTTCCGAGGTTGAAATAGACTGCCTGACGGGGGATCAT
AAGAACATCAGAACAGACATTGTCATGGATGTTGGCTGCAGTATAAATCCAGCCATTGAC
ATAGGCCAGATTGAAGGTGCATTTATTCAAGGCATGGGACTTTATACAATAGAGGAACTG
AATTATTCTCCCCAGGGCATTCTGCACACTCGTGGTCCAGACCAATATAAAATCCCTGCC
ATCTGTGACATGCCCACGGAGTTGCACATTGCTTTGTTGCCTCCTTCTCAAAACTCAAAT
ACTCTTTATTCATCTAAGGGTCTGGGAGAGTCGGGGGTGTTCCTGGGGTGTTCCGTGTTT
TTCGCTATCCATGACGCAGTGAGTGCAGCACGACAGGAGAGAGGCCTGCATGGACCCTTG
ACCCTTAATAGTCCACTGACCCCGGAGAAGATTAGGATGGCCTGTGAAGACAAGTTCACA
AAAATGATTCCGAGAGATGAACCTGGATCCTACGTTCCTTGGAATGTACCCATCTGA
Enzyme 31 GenBank Gene ID L11005 Link Image
Enzyme 31 GeneCard ID AOX1 Link Image
Enzyme 31 GenAtlas ID AOX1 Link Image
Enzyme 31 HGNC ID HGNC:553 Link Image
Enzyme 31 Chromosome Location 2
Enzyme 31 Locus 2q33
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Wright RM, Vaitaitis GM, Wilson CM, Repine TB, Terada LS, Repine JE: cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase. Proc Natl Acad Sci U S A. 1993 Nov 15;90(22):10690-4. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 5367
Enzyme 32 Name Lathosterol oxidase
Enzyme 32 Synonyms
  1. Lathosterol 5-desaturase
  2. Delta(7-sterol 5-desaturase
  3. C-5 sterol desaturase
  4. Sterol-C5- desaturase
Enzyme 32 Gene Name SC5DL
Enzyme 32 Protein Sequence >Lathosterol oxidase 
MDLVLRVADYYFFTPYVYPATWPEDDIFRQAISLLIVTNVGAYILYFFCATLSYYFVFDH
ALMKHPQFLKNQVRREIKFTVQALPWISILTVALFLLEIRGYSKLHDDLGEFPYGLFELV
VSIISFLFFTDMFIYWIHRGLHHRLVYKRLHKPHHIWKIPTPFASHAFHPIDGFLQSLPY
HIYPFIFPLHKVVYLSLYILVNIWTISIHDGDFRVPQILQPFINGSAHHTDHHMFFDYNY
GQYFTLWDRIGGSFKNPSSFEGKGPLSYVKEMTEGKRSSHSGNGCKNEKLFNGEFTKTE
Enzyme 32 Number of Residues 299
Enzyme 32 Molecular Weight 35301
Enzyme 32 Theoretical pI 8.24
Enzyme 32 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 32 General Function Lipid transport and metabolism
Enzyme 32 Specific Function Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions Not Available
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • 32-52 79-99 117-137 186-206
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 1906796 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID O75845 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name SC5D_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >711 bp 
ATGGATCTTGTACTCCGTGTTGCAGATTACTATTTTTTTACACCATACGTGTATCCAGCC
ACATGGCCAGAAGATGACATCTTCCGACAAGCTATTAGTCTTCTGATTGTAACAAATGTT
GGTGCTTACATCCTTTATTTCTTCTGTGCAACACTGAGCTATTATTTTGTCTTCGATCAT
GCATTAATGAAACATCCACAATTTTTAAAGAATCAAGTCCGTCGAGAGATTAAGTTTACT
GTCCAGGCATTGCCATGGATAAGTATTCTTACTGTTGCACTGTTCTTGCTGGAGATAAGA
GGTTACAGCAAATTACATGATGACCTAGGAGAGTTTCCATATGGATTGTTTGAACTTGTC
GTTAGTATAATATCTTTCCTCTTTTTCACTGACATGTTCATCTACTGGATTCACAGAGGC
CTTCATCATAGACTGGTATATAAGCGCCTACATAAACCTCACCATATTTGGAAGATTCCT
ACTCCATTTGCAAGTCATGCTTTTCACCCTATTGATGGCTTTCTTCAGAGTCTACCTTAC
CATATATACCCTTTTATCTTTCCATTACACAAGGTGGTTTATTTAAGTCTGTACATCTTG
GTTAATATCTGGACAATTTCCATTCATGACGGTGATTTTCGTGTAAGAATGAAAAATTAT
TCAATGGAGAGTTTACAAAGACTGAATAGATTATTGCCCAGTTATTCTTAA
Enzyme 32 GenBank Gene ID D85181 Link Image
Enzyme 32 GeneCard ID SC5DL Link Image
Enzyme 32 GenAtlas ID SC5DL Link Image
Enzyme 32 HGNC ID HGNC:10547 Link Image
Enzyme 32 Chromosome Location 11
Enzyme 32 Locus 11q23.3
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Matsushima M, Inazawa J, Takahashi E, Suzumori K, Nakamura Y: Molecular cloning and mapping of a human cDNA (SC5DL) encoding a protein homologous to fungal sterol-C5-desaturase. Cytogenet Cell Genet. 1996;74(4):252-4. [PubMed Link Image]
  2. Husselstein T, Schaller H, Gachotte D, Benveniste P: Delta7-sterol-C5-desaturase: molecular characterization and functional expression of wild-type and mutant alleles. Plant Mol Biol. 1999 Mar;39(5):891-906. [PubMed Link Image]
  3. Nishi S, Nishino H, Ishibashi T: cDNA cloning of the mammalian sterol C5-desaturase and the expression in yeast mutant. Biochim Biophys Acta. 2000 Jan 31;1490(1-2):106-8. [PubMed Link Image]
  4. Brunetti-Pierri N, Corso G, Rossi M, Ferrari P, Balli F, Rivasi F, Annunziata I, Ballabio A, Russo AD, Andria G, Parenti G: Lathosterolosis, a novel multiple-malformation/mental retardation syndrome due to deficiency of 3beta-hydroxysteroid-delta5-desaturase. Am J Hum Genet. 2002 Oct;71(4):952-8. Epub 2002 Aug 20. [PubMed Link Image]
  5. Krakowiak PA, Wassif CA, Kratz L, Cozma D, Kovarova M, Harris G, Grinberg A, Yang Y, Hunter AG, Tsokos M, Kelley RI, Porter FD: Lathosterolosis: an inborn error of human and murine cholesterol synthesis due to lathosterol 5-desaturase deficiency. Hum Mol Genet. 2003 Jul 1;12(13):1631-41. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 5375
Enzyme 33 Name Dimethylaniline monooxygenase [N-oxide-forming] 5
Enzyme 33 Synonyms
  1. Hepatic flavin-containing monooxygenase 5
  2. FMO 5
  3. Dimethylaniline oxidase 5
Enzyme 33 Gene Name FMO5
Enzyme 33 Protein Sequence >Dimethylaniline monooxygenase [N-oxide-forming] 5 
MTKKRIAVIGGGVSGLSSIKCCVEEGLEPVCFERTDDIGGLWRFQENPEEGRASIYKSVI
INTSKEMMCFSDYPIPDHYPNFMHNAQVLEYFRMYAKEFDLLKYIRFKTTVCSVKKQPDF
ATSGQWEVVTESEGKKEMNVFDGVMVCTGHHTNAHLPLESFPGIEKFKGQYFHSRDYKNP
EGFTGKRVIIIGIGNSGGDLAVEISQTAKQVFLSTRRGAWILNRVGDYGYPADVLFSSRL
THFIWKICGQSLANKYLEKKINQRFDHEMFGLKPKHRALSQHPTLNDDLPNRIISGLVKV
KGNVKEFTETAAIFEDGSREDDIDAVIFATGYSFDFPFLEDSVKVVKNKISLYKKVFPPN
LERPTLAIIGLIQPLGAIMPISELQGRWATQVFKGLKTLPSQSEMMAEISKAQEEIDKRY
VESQRHTIQGDYIDTMEELADLVGVRPNLLSLAFTDPKLALHLLLGPCTPIHYRVQGPGK
WDGARKAILTTDDRIRKPLMTRVVERSSSMTSTMTIGKFMLALAFFAIIIAYF
Enzyme 33 Number of Residues 533
Enzyme 33 Molecular Weight 60221
Enzyme 33 Theoretical pI 8.36
Enzyme 33 GO Classification
Function
  • FAD binding
  • NADP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
  • dimethylaniline monooxygenase (N-oxide-forming) activity
  • dimethylaniline monooxygenase (N-oxide-forming) activity
  • disulfide oxidoreductase activity
  • monooxygenase activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD or NADH as one donor, and incorporation of one atom of oxygen
  • purine nucleotide binding
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
  • cell
  • cell fraction
  • intrinsic to endoplasmic reticulum membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
  • membrane fraction
  • microsome
  • vesicular fraction
Enzyme 33 General Function Inorganic ion transport and metabolism
Enzyme 33 Specific Function In contrast with other forms of FMO it does not seem to be a drug-metabolizing enzyme
Enzyme 33 Pathways Not Available
Enzyme 33 Reactions
  • N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • 510-532
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 559046 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID P49326 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name FMO5_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >1602 bp 
ATGACTAAGAAAAGAATTGCTGTGATTGGGGGAGGAGTGAGCGGGCTCTCTTCCATCAAG
TGCTGCGTAGAAGAAGGCTTGGAACCTGTCTGCTTTGAAAGGACTGATGACATCGGAGGG
CTCTGGAGGTTCCAGGAAAATCCTGAAGAAGGAAGGGCCAGTATTTACAAATCAGTGATC
ATCAATACTTCTAAAGAGATGATGTGCTTCAGTGACTATCCAATCCCAGATCATTATCCC
AACTTCATGCATAATGCCCAGGTCCTGGAGTATTTCAGGATGTATGCCAAAGAATTTGAC
CTTCTAAAGTATATTCGATTTAAGACCACTGTGTGCAGTGTGAAGAAGCAGCCTGATTTT
GCCACTTCAGGCCAATGGGAAGTGGTCACTGAATCTGAAGGGAAAAAGGAGATGAATGTC
TTTGATGGAGTCATGGTTTGCACTGGCCATCACACCAATGCTCATCTACCTCTGGAAAGC
TTCCCTGGAATTGAGAAGTTCAAAGGGCAGTACTTCCACAGTCGAGACTATAAGAACCCA
GAGGGATTCACTGGAAAGAGAGTCATTATAATTGGCATTGGGAATTCTGGAGGGGATCTG
GCTGTAGAGATTAGCCAAACAGCCAAGCAGGTTTTCCTCAGCACCAGGAGAGGGGCTTGG
ATCCTGAATCGTGTAGGGGACTACGGATATCCTGCTGATGTGTTGTTCTCTTCTCGACTT
ACACATTTTATATGGAAGATCTGTGGCCAATCATTAGCAAACAAATATTTGGAAAAAAAG
ATAAACCAAAGGTTTGACCATGAAATGTTTGGCCTGAAGCCTAAACACAGAGCTCTGAGT
CAGCATCCAACCTTAAATGATGACCTGCCAAATCGTATCATTTCTGGCTTGGTGAAAGTG
AAAGGAAATGTGAAGGAATTCACGGAGACAGCTGCCATATTTGAGGATGGCTCCAGGGAG
GATGACATTGATGCTGTTATCTTTGCCACAGGCTATAGCTTTGACTTTCCATTTCTGGAA
GATTCCGTCAAAGTGGTCAAAAACAAGATATCCCTGTATAAAAAGGTCTTCCCTCCTAAC
CTGGAAAGGCCAACTCTTGCAATCATAGGCTTGATTCAGCCCTTAGGAGCCATTATGCCC
ATTTCAGAGCTCCAAGGACGCTGGGCCACTCAGGTATTTAAAGGTCTAAAGACATTGCCC
TCACAGAGTGAAATGATGGCAGAAATATCTAAAGCTCAAGAGGAAATTGACAAAAGGTAT
GTGGAGAGCCAACGCCATACCATTCAGGGAGACTACATAGATACCATGGAAGAGCTTGCT
GATTTGGTGGGGGTCAGGCCCAATCTGCTGTCTCTGGCCTTCACTGACCCCAAGCTGGCA
TTACACTTATTACTGGGACCCTGCACTCCAATCCACTATCGTGTACAGGGCCCTGGAAAG
TGGGATGGGGCTCGAAAAGCTATCCTCACCACAGATGATCGCATCAGGAAGCCTCTGATG
ACAAGAGTAGTTGAAAGGAGTAGTTCTATGACTTCAACAATGACAATAGGCAAGTTTATG
CTAGCTCTTGCCTTCTTTGCTATAATTATAGCTTACTTCTAG
Enzyme 33 GenBank Gene ID L37080 Link Image
Enzyme 33 GeneCard ID FMO5 Link Image
Enzyme 33 GenAtlas ID FMO5 Link Image
Enzyme 33 HGNC ID HGNC:3773 Link Image
Enzyme 33 Chromosome Location 1
Enzyme 33 Locus 1q21.1
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Overby LH, Buckpitt AR, Lawton MP, Atta-Asafo-Adjei E, Schulze J, Philpot RM: Characterization of flavin-containing monooxygenase 5 (FMO5) cloned from human and guinea pig: evidence that the unique catalytic properties of FMO5 are not confined to the rabbit ortholog. Arch Biochem Biophys. 1995 Feb 20;317(1):275-84. [PubMed Link Image]
  2. Furnes B, Feng J, Sommer SS, Schlenk D: Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans. Drug Metab Dispos. 2003 Feb;31(2):187-93. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 5388
Enzyme 34 Name Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial precursor
Enzyme 34 Synonyms
  1. P5C dehydrogenase
  2. Aldehyde dehydrogenase 4A1
Enzyme 34 Gene Name ALDH4A1
Enzyme 34 Protein Sequence >Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial precursor 
MLLPAPALRRALLSRPWTGAGLRWKHTSSLKVANEPVLAFTQGSPERDALQKALKDLKGR
MEAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKP
IADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVEL
EGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAML
ASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ
NLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSL
WPQIKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGK
CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDKYKETLQLVDSTTSYGLTG
AVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILR
WTSPQVIKETHKPLGDWSYAYMQ
Enzyme 34 Number of Residues 563
Enzyme 34 Molecular Weight 61720
Enzyme 34 Theoretical pI 8.20
Enzyme 34 GO Classification
Function
  • 1-pyrroline-5-carboxylate dehydrogenase activity
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-NH group of donors
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • cellular metabolism
  • glutamine family amino acid metabolism
  • metabolism
  • physiological process
  • proline biosynthesis
  • proline metabolism
Component
  • membrane-enclosed lumen
  • mitochondrial lumen
  • mitochondrial matrix
  • organelle lumen
Enzyme 34 General Function Energy production and conversion
Enzyme 34 Specific Function Irreversible conversion of delta-1-pyrroline-5- carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes
Enzyme 34 Pathways
Enzyme 34 Reactions
  • 1-pyrroline-5-carboxylate + NAD+ + H2O = L-glutamate + NADH + H+
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 1353250 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID P30038 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name AL4A1_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >1692 bp 
ATGCTGCTGCCGGCGCCCGCGCTCCGCCGCGCCCTGCTGTCCCGCCCCTGGACCGGGGCC
GGCCTGCGGTGGAAGCACACCTCCTCCCTGAAGGTGGCCAACGAGCCCGTCTTAGCCTTC
ACGCAGGGCAGCCCTGAGCGAGATGCCCTGCAAAAGGCCTTGAAGGACCTGAAGGGCCGG
ATGGAAGCCATCCCATGCGTGATGGGGGATGAGGAGGTGTGGACGTCGGACGTGCAGTAC
CAAGTGTCGCCTTTTAACCATGGACATAAGGTGGCCAAGTTCTGTTATGCAGACAAGAGC
CTGCTCAACAAAGCCATTGAGGCTGCCCTGGCTGCCCGGAAAGAGTGGGACCTGAAGCCT
ATTGCAGACCGGGCCCAGATCTTCCTGAAGGCGGCAGACATGCTGAGTGGGCCGCGCAGG
GCTGAGATCCTCGCCAAGACCATGGTGGGACAGGGTAAGACCGTGATCCAAGCGGAGATT
GACGCTGCAGCGGAACTCATCGACTTCTTCCGGTTCAATGCCAAGTATGCGGTGGAGCTG
GAGGGGCAGCAGCCCATCAGCGTGCCCCCGAGCACCAACAGCACGGTGTACCGGGGTCTG
GAGGGCTTCGTGGCGGCCATCTCGCCCTTTAACTTCACTGCAATCGGCGGCAACCTGGCG
GGGGCACCGGCCCTGATGGGCAACGTGGTCCTATGGAAGCCCAGTGACACTGCCATGCTG
GCCAGCTATGCTGTCTACCGCATCCTTCGGGAGGCTGGCCTGCCCCCCAACATCATCCAG
TTTGTGCCAGCTGATGGGCCCCTATTTGGGGACACTGTCACCAGCTCAGAGCACCTCTGT
GGCATCAACTTCACAGGCAGTGTGCCCACCTTCAAACACCTGTGGAAGCAGGTGGCCCAG
AACCTGGACCGGTTCCACACCTTCCCACGCCTGGCTGGAGAGTGCGGCGGAAAGAACTTC
CACTTCGTGCACCGCTCGGCCGACGTGGAGAGCGTGGTGAGCGGGACCCTCCGCTCAGCC
TTCGAGTACGGTGGCCAGAAGTGTTCCGCCTGCTCGCGTCTCTACGTGCCGCACTCGCTG
TGGCCGCAGATCAAAGGGCGGCTGCTGGAGGAGCACAGTCGGATCAAAGTGGGCGACCCT
GCAGAGGATTTTGGGACCTTCTTCTCTGCAGTGATTGATGCCAAGTCCTTTGCCCGTATC
AAGAAGTGGCTGGAGCACGCGCGCTCCTCGCCCAGCCTCACCATCCTGGCTGGGGGCAAG
TGTGATGACTCCGTGGGCTACTTTGTGGAGCCCTGCATCGTGGAGAGCAAGGACCCTCAG
GAGCCCATCATGAAGGAGGAGATCTTCGGGCCTGTACTGTCTGTGTACGTCTACCCGGAC
GACAAGTACAAGGAGACGCTGCAGCTGGTTGACAGCACCACCAGCTATGGCCTCACGGGG
GCAGTGTTCTCCCAGGATAAGGACGTCGTGCAGGAGGCCACAAAGGTGCTGAGGAATGCT
GCCGGCAACTTCTACATCAACGACAAGTCCACTGGCTCGATAGTGGGCCAGCAGCCCTTT
GGGGGGGCCCGAGCCTCTGGAACCAATGACAAGCCAGGGGGCCCACACTACATCCTGCGC
TGGACGTCGCCGCAGGTCATCAAGGAGACACATAAGCCCCTGGGGGACTGGAGCTACGCG
TACATGCAGTGA
Enzyme 34 GenBank Gene ID U24267 Link Image
Enzyme 34 GeneCard ID ALDH4A1 Link Image
Enzyme 34 GenAtlas ID ALDH4A1 Link Image
Enzyme 34 HGNC ID HGNC:406 Link Image
Enzyme 34 Chromosome Location 1
Enzyme 34 Locus 1p36
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Hu CA, Lin WW, Valle D: Cloning, characterization, and expression of cDNAs encoding human delta 1-pyrroline-5-carboxylate dehydrogenase. J Biol Chem. 1996 Apr 19;271(16):9795-800. [PubMed Link Image]
  2. Hempel J, Eckey R, Berie D, Romovacek H, Agarwal DP, Goedde HW: Human liver glutamic gamma-semialdehyde dehydrogenase: structural relationship to the yeast enzyme. Comp Biochem Physiol B. 1992 Aug;102(4):791-93. [PubMed Link Image]
  3. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed Link Image]
  4. Geraghty MT, Vaughn D, Nicholson AJ, Lin WW, Jimenez-Sanchez G, Obie C, Flynn MP, Valle D, Hu CA: Mutations in the Delta1-pyrroline 5-carboxylate dehydrogenase gene cause type II hyperprolinemia. Hum Mol Genet. 1998 Sep;7(9):1411-5. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 5396
Enzyme 35 Name Acyl-coenzyme A oxidase 2, peroxisomal
Enzyme 35 Synonyms
  1. 3-alpha,7- alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase
  2. 3- alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase
  3. Trihydroxycoprostanoyl-CoA oxidase
  4. THCCox
  5. THCA-CoA oxidase
Enzyme 35 Gene Name ACOX2
Enzyme 35 Protein Sequence >Acyl-coenzyme A oxidase 2, peroxisomal 
MGSPVHRVSLGDTWSRQMHPDIESERYMQSFDVERLTNILDGGAQNTALRRKVESIIHSY
PEFSCKDNYFMTQNERYKAAMRRAFHIRLIARRLGWLEDGRELGYAYRALSGDVALNIHR
VFVRALRSLGSEEQIAKWDPLCKNIQIIATYAQTELGHGTYLQGLETEATYDAATQEFVI
HSPTLTATKWWPGDLGRSATHALVQAQLICSGARRGMHAFIVPIRSLQDHTPLPGIIIGD
IGPKMDFDQTDNGFLQLNHVRVPRENMLSRFAQVLPDGTYVKLGTAQSNYLPMVVVRVEL
LSGEILPILQKACVIAMRYSVIRRQSRLRPSDPEAKVLDYQTQQQKLFPQLAISYAFHFL
AVSLLEFFQHSYTAILNQDFSFLPELHALSTGMKAMMSEFCTQGAEMCRRACGGHGYSKL
SGLPSLVTKLSASCTYEGENTVLYLQVARFLVKSYLQTQMSPGSTPQRSLSPSVAYLTAP
DLARCPAQRAADFLCPELYTTAWAHVAVRLIKDSVQHLQTLTQSGADQHEAWNQTTVIHL
QAAKVHCYYVTVKGFTEALEKLENEPAIQQVLKRLCDLHAIHGILTNSGDFLHDAFLSGA
QVDMARTAYLDLLRLIRKDAILLTDAFDFTDQCLNSALGCYDGNVYERLFQWAQKSPTNT
QENPAYEEYIRPLLQSWRSKL
Enzyme 35 Number of Residues 681
Enzyme 35 Molecular Weight 76828
Enzyme 35 Theoretical pI 7.59
Enzyme 35 GO Classification
Function
  • FAD binding
  • acyl-CoA dehydrogenase activity
  • acyl-CoA oxidase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleotide binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on the CH-CH group of donors
  • oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
  • purine nucleotide binding
Process
  • carboxylic acid metabolism
  • cellular metabolism
  • electron transport
  • fatty acid beta-oxidation
  • fatty acid metabolism
  • fatty acid oxidation
  • generation of precursor metabolites and energy
  • metabolism
  • organic acid metabolism
  • physiological process
Component
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • microbody
  • organelle
  • peroxisome
Enzyme 35 General Function Lipid transport and metabolism
Enzyme 35 Specific Function Oxidizes the CoA esters of the bile acid intermediates di- and tri-hydroxycholestanoic acids
Enzyme 35 Pathways Not Available
Enzyme 35 Reactions Not Available
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 1780991 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID Q99424 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name ACOX2_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >2046 bp 
ATGGGCAGCCCAGTGCACCGAGTGTCATTGGGGGATACCTGGAGCAGGCAAATGCACCCC
GACATAGAGAGCGAGAGGTATATGCAGTCCTTTGACGTGGAACGGCTCACCAACATCCTT
GATGGAGGTGCCCAGAACACTGCACTCCGCAGGAAAGTTGAGAGCATCATCCACAGTTAC
CCGGAGTTTAGCTGTAAGGACAATTATTTCATGACCCAGAATGAGCGTTATAAGGCTGCC
ATGCGGAGGGCATTCCACATCCGGTTGATAGCTCGGCGCCTGGGTTGGTTAGAAGATGGT
CGTGAATTAGGCTACGCTTACAGAGCCCTTTCTGGAGACGTGGCCTTAAATATACACAGA
GTCTTCGTGAGAGCCCTCAGGAGCCTGGGCTCAGAGGAGCAGATTGCCAAATGGGACCCA
CTCTGCAAAAACATCCAGATCATCGCAACGTATGCACAGACAGAGTTGGGACATGGGACA
TATCTTCAGGGCCTGGAGACTGAAGCCACCTATGACGCAGCCACCCAGGAGTTTGTGATA
CACAGCCCCACGCTGACTGCCACCAAATGGTGGCCTGGAGACTTGGGACGGTCAGCCACC
CATGCCCTGGTCCAGGCCCAGCTGATCTGCTCAGGAGCCAGGCGGGGCATGCACGCTTTT
ATTGTGCCAATCCGGAGTCTTCAGGACCACACCCCACTGCCAGGAATCATCATTGGGGAC
ATCGGACCCAAGATGGACTTTGATCAAACAGACAATGGCTTCCTGCAGCTGAACCATGTG
CGGGTCCCCAGGGAGAACATGCTGAGTCGCTTTGCACAGGTCTTGCCAGATGGCACCTAC
GTCAAACTCGGTACAGCACAGAGCAACTACCTTCCCATGGTGGTGGTGCGGGTGGAGCTG
CTGTCAGGGGAGATCCTCCCTATACTGCAGAAGGCCTGTGTCATCGCCATGCGCTACTCG
GTCATCCGCCGCCAATCCCGGCTCCGGCCCAGTGACCCAGAGGCAAAGGTCCTGGACTAC
CAGACACAACAGCAGAAACTCTTTCCTCAGCTGGCCATCAGTTATGCCTTCCATTTCCTG
GCAGTCAGCCTCTTGGAGTTCTTCCAGCACTCCTACACTGCCATTCTGAACCAAGACTTC
AGCTTCCTGCCTGAGCTCCACGCGCTGAGCACGGGCATGAAGGCCATGATGTCAGAATTC
TGCACCCAGGGAGCTGAGATGTGCCGCAGGGCCTGTGGCGGACATGGCTACTCAAAGCTG
AGTGGCCTGCCATCACTGGTCACCAAATTGTCGGCCTCCTGCACCTACGAGGGTGAGAAC
ACAGTGCTCTACCTGCAGGTGGCCAGGTTCCTGGTGAAGAGCTACCTGCAGACTCAGATG
TCCCCTGGCTCCACGCCACAGAGATCTCTCTCTCCATCTGTCGCATATCTCACCGCACCT
GACCTGGCCAGGTGTCCAGCCCAGAGGGCAGCCGACTTCCTCTGCCCGGAGCTCTACACC
ACGGCCTGGGCACATGTGGCAGTAAGGCTCATAAAGGACTCAGTGCAGCATTTACAGACC
CTGACGCAATCCGGAGCTGACCAGCACGAGGCTTGGAACCAGACCACTGTCATACACCTC
CAGGCTGCTAAGGTGCACTGCTACTATGTCACTGTGAAGGGTTTTACAGAAGCTCTGGAG
AAACTAGAAAATGAACCAGCGATTCAGCAGGTGCTCAAGCGCCTCTGTGACCTCCATGCC
ATACATGGAATCTTGACTAACTCGGGTGACTTTCTCCATGACGCCTTCCTGTCTGGTGCC
CAAGTGGACATGGCAAGAACAGCCTACCTGGACCTGCTCCGCCTGATCCGGAAGGATGCC
ATCCTGTTAACTGATGCTTTTGACTTCACCGATCAGTGTTTAAATTCAGCCCTTGGCTGT
TATGATGGAAACGTCTACGAACGCCTGTTCCAGTGGGCTCAGAAGTCACCAACCAATACT
CAGGAGAACCCTGCCTATGAGGAATATATAAGACCACTTTTACAAAGTTGGAGATCCAAG
CTATGA
Enzyme 35 GenBank Gene ID X95190 Link Image
Enzyme 35 GeneCard ID ACOX2 Link Image
Enzyme 35 GenAtlas ID ACOX2 Link Image
Enzyme 35 HGNC ID HGNC:120 Link Image
Enzyme 35 Chromosome Location 3
Enzyme 35 Locus 3p14.3
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Baumgart E, Vanhooren JC, Fransen M, Marynen P, Puype M, Vandekerckhove J, Leunissen JA, Fahimi HD, Mannaerts GP, van Veldhoven PP: Molecular characterization of the human peroxisomal branched-chain acyl-CoA oxidase: cDNA cloning, chromosomal assignment, tissue distribution, and evidence for the absence of the protein in Zellweger syndrome. Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13748-53. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 5397
Enzyme 36 Name Dimethylaniline monooxygenase [N-oxide-forming] 4
Enzyme 36 Synonyms
  1. Hepatic flavin-containing monooxygenase 4
  2. FMO 4
  3. Dimethylaniline oxidase 4
Enzyme 36 Gene Name FMO4
Enzyme 36 Protein Sequence >Dimethylaniline monooxygenase [N-oxide-forming] 4 
MAKKVAVIGAGVSGLSSIKCCVDEDLEPTCFERSDDIGGLWKFTESSKDGMTRVYKSLVT
NVCKEMSCYSDFPFHEDYPNFMNHEKFWDYLQEFAEHFDLLKYIQFKTTVCSITKRPDFS
ETGQWDVVTETEGKQNRAVFDAVMVCTGHFLNPHLPLEAFPGIHKFKGQILHSQEYKIPE
GFQGKRVLVIGLGNTGGDIAVELSRTAAQVLLSTRTGTWVLGRSSDWGYPYNMMVTRRCC
SFIAQVLPSRFLNWIQERKLNKRFNHEDYGLSITKGKKAKFIVNDELPNCILCGAITMKT
SVIEFTETSAVFEDGTVEENIDVVIFTTGYTFSFPFFEEPLKSLCTKKIFLYKQVFPLNL
ERATLAIIGLIGLKGSILSGTELQARWVTRVFKGLCKIPPSQKLMMEATEKEQLIKRGVF
KDTSKDKFDYIAYMDDIAACIGTKPSIPLLFLKDPRLAWEVFFGPCTPYQYRLMGPGKWD
GARNAILTQWDRTLKPLKTRIVPDSSKPASMSHYLKAWGAPVLLASLLLICKSSLFLKLV
RDKLQDRMSPYLVSLWRG
Enzyme 36 Number of Residues 558
Enzyme 36 Molecular Weight 63343
Enzyme 36 Theoretical pI 8.59
Enzyme 36 GO Classification
Function
  • catalytic activity
  • dimethylaniline monooxygenase (N-oxide-forming) activity
  • disulfide oxidoreductase activity
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD or NADH as one donor, and incorporation of one atom of oxygen
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
  • cell
  • cell fraction
  • membrane fraction
  • microsome
  • vesicular fraction
Enzyme 36 General Function Inorganic ion transport and metabolism
Enzyme 36 Specific Function This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides
Enzyme 36 Pathways Not Available
Enzyme 36 Reactions
  • N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • 517-531
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 31430 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID P31512 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name FMO4_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >1677 bp 
ATGGCCAAGAAAGTTGCAGTGATTGGAGCTGGTGTGAGTGGCCTCTCCTCCATCAAATGC
TGTGTGGATGAGGACCTGGAGCCCACCTGCTTTGAGAGAAGTGATGACATTGGGGGATTA
TGGAAGTTTACTGAATCTTCCAAAGATGGGATGACCAGGGTCTATAAGTCATTAGTGACA
AATGTCTGTAAGGAAATGTCATGTTACAGTGACTTCCCTTTCCACGAAGATTATCCTAAT
TTCATGAACCATGAAAAATTTTGGGACTATCTCCAAGAATTTGCTGAGCACTTTGACCTC
CTGAAATACATTCAGTTTAAGACCACTGTGTGCAGCATAACGAAGCGTCCAGACTTCTCC
GAAACTGGTCAGTGGGATGTTGTCACAGAGACAGAGGGCAAGCAAAATAGAGCTGTCTTT
GATGCTGTTATGGTTTGCACTGGACATTTCCTGAATCCCCATTTACCTTTGGAAGCCTTT
CCTGGAATTCATAAGTTTAAAGGTCAGATCCTGCATAGTCAAGAGTACAAGATCCCAGAA
GGCTTTCAGGGCAAACGCGTCTTGGTGATTGGTCTTGGGAACACTGGAGGAGACATTGCT
GTGGAACTCAGTCGAACGGCAGCTCAGGTACTTCTCAGTACTAGAACTGGTACCTGGGTT
CTTGGGCGCTCTTCAGATTGGGGCTATCCTTATAATATGATGGTTACAAGAAGATGCTGT
AGTTTTATTGCACAAGTTCTGCCTTCACGTTTTCTAAACTGGATTCAAGAAAGGAAGTTG
AATAAGAGATTTAATCATGAGGATTATGGATTAAGTATTACCAAAGGGAAAAAAGCAAAA
TTCATTGTGAATGATGAGCTGCCAAACTGTATCCTCTGTGGGGCAATCACTATGAAAACC
AGCGTGATTGAATTTACAGAAACCTCTGCTGTCTTTGAAGATGGGACAGTGGAAGAAAAC
ATTGATGTTGTGATCTTCACTACAGGATATACATTTTCTTTTCCATTTTTTGAAGAACCT
CTTAAAAGCCTCTGTACAAAGAAGATATTTCTATACAAGCAAGTCTTTCCCTTAAACCTA
GAGAGAGCGACATTAGCCATCATCGGCCTTATCGGCCTTAAAGGATCCATCTTATCAGGC
ACAGAGCTCCAAGCACGATGGGTCACAAGAGTATTCAAAGGACTCTGTAAGATACCTCCA
TCCCAAAAATTGATGATGGAGGCTACTGAAAAGGAACAGCTCATTAAAAGGGGAGTGTTT
AAAGACACCAGCAAAGACAAATTTGACTACATTGCCTACATGGATGATATCGCTGCCTGC
ATAGGCACAAAGCCCAGCATCCCACTTCTGTTCCTCAAGGATCCCAGACTAGCTTGGGAA
GTTTTCTTTGGACCATGTACTCCTTATCAGTACCGCCTCATGGGCCCTGGAAAATGGGAT
GGAGCCAGAAATGCCATCCTGACCCAGTGGGACAGAACATTGAAACCTTTAAAAACTCGA
ATTGTCCCTGATTCCTCCAAGCCTGCCTCCATGTCACATTATTTAAAAGCCTGGGGGGCA
CCTGTCCTACTTGCCTCTCTTCTACTTATCTGTAAATCTTCACTTTTCTTGAAATTGGTG
AGAGATAAACTACAGGACAGAATGTCCCCTTACCTAGTAAGTCTTTGGCGAGGATGA
Enzyme 36 GenBank Gene ID Z11737 Link Image
Enzyme 36 GeneCard ID FMO4 Link Image
Enzyme 36 GenAtlas ID FMO4 Link Image
Enzyme 36 HGNC ID HGNC:3772 Link Image
Enzyme 36 Chromosome Location 1
Enzyme 36 Locus 1q23-q25
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Dolphin CT, Shephard EA, Povey S, Smith RL, Phillips IR: Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family. Biochem J. 1992 Oct 1;287 ( Pt 1):261-7. [PubMed Link Image]
  2. Furnes B, Feng J, Sommer SS, Schlenk D: Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans. Drug Metab Dispos. 2003 Feb;31(2):187-93. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 5399
Enzyme 37 Name Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 precursor
Enzyme 37 Synonyms
  1. E-NPP 2
  2. Extracellular lysophospholipase D
  3. LysoPLD
  4. Autotaxin
Enzyme 37 Gene Name ENPP2
Enzyme 37 Protein Sequence >Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 precursor 
MARRSSFQSCQIISLFTFAVGVNICLGFTAHRIKRAEGWEEGPPTVLSDSPWTNISGSCK
GRCFELQEAGPPDCRCDNLCKSYTSCCHDFDELCLKTARGWECTKDRCGEVRNEENACHC
SEDCLARGDCCTNYQVVCKGESHWVDDDCEEIKAAECPAGFVRPPLIIFSVDGFRASYMK
KGSKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDA
TFHLRGREKFNHRWWGGQPLWITATKQGVKAGTFFWSVVIPHERRILTILQWLTLPDHER
PSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDH
GMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRSKFSNNAKYDPKAIIANLTCKKPDQH
FKPYLKQHLPKRLHYANNRRIEDIHLLVERRWHVARKPLDVYKKPSGKCFFQGDHGFDNK
VNSMQTVFVGYGPTFKYKTKVPPFENIELYNVMCDLLGLKPAPNNGTHGSLNHLLRTNTF
RPTMPEEVTRPNYPGIMYLQSDFDLGCTCDDKVEPKNKLDELNKRLHTKGSTEERHLLYG
RPAVLYRTRYDILYHTDFESGYSEIFLMPLWTSYTVSKQAEVSSVPDHLTSCVRPDVRVS
PSFSQNCLAYKNDKQMSYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWNYFQRVL
VKKYASERNGVNVISGPIFDYDYDGLHDTEDKIKQYVEGSSIPVPTHYYSIITSCLDFTQ
PADKCDGPLSVSSFILPHRPDNEESCNSSEDESKWVEELMKMHTARVRDIEHLTSLDFFR
KTSRSYPEILTLKTYLHTYESEI
Enzyme 37 Number of Residues 863
Enzyme 37 Molecular Weight 99004
Enzyme 37 Theoretical pI 7.39
Enzyme 37 GO Classification
Function
  • binding
  • catalytic activity
  • endonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
Component
—
Enzyme 37 General Function Not Available
Enzyme 37 Specific Function Hydrolyzes lysophospholipids to produce lysophosphatidic acid (LPA) in extracellular fluids. Major substrate is lysophosphatidylcholine. Also can act on sphingosylphosphphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP. Involved in several motility- related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation. May have a role in induction of parturition. Possible involvement in cell proliferation and adipose tissue development Tumor cell motility-stimulating factor
Enzyme 37 Pathways Not Available
Enzyme 37 Reactions
  • 1-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • 1-27
Enzyme 37 Transmembrane Regions Not Available
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 537906 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q13822 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name ENPP2_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >2748 bp 
ATGGCAAGGAGGAGCTCGTTCCAGTCGTGTCAGATAATATCCCTGTTCACTTTTGCCGTT
GGAGTCAGTATCTGCTTAGGATTCACTGCACATCGAATTAAGAGAGCAGAAGGATGGGAG
GAAGGTCCTCCTACAGTGCTATCAGACTCCCCCTGGACCAACATCTCCGGATCTTGCAAG
GGCAGGTGCTTTGAACTTCAAGAGGCTGGACCTCCTGATTGTCGCTGTGACAACTTGTGT
AAGAGCTATACCAGTTGCTGCCATGACTTTGATGAGCTGTGTTTGAAGACAGCCCGTGGC
TGGGAGTGTACTAAGGACAGATGTGGAGAAGTCAGAAATGAAGAAAATGCCTGTCACTGC
TCAGAGGACTGCTTGGCCAGGGGAGACTGCTGTACCAATTACCAAGTGGTTTGCAAAGGA
GAGTCGCATTGGGTTGATGATGACTGTGAGGAAATAAAGGCCGCAGAATGCCCTGCAGGG
TTTGTTCGCCCTCCATTAATCATCTTCTCCGTGGATGGCTTCCGTGCATCATACATGAAG
AAAGGCAGCAAAGTCATGCCTAATATTGAAAAACTAAGGTCTTGTGGCACACACTCTCCC
TACATGAGGCCGGTGTACCCAACTAAAACCTTTCCTAACTTATACACTTTGGCCACTGGG
CTATATCCAGAATCACATGGAATTGTTGGCAATTCAATGTATGATCCTGTATTTGATGCC
ACTTTTCATCTGCGAGGGCGAGAGAAATTTAATCATAGATGGTGGGGAGGTCAACCGCTA
TGGATTACAGCCACCAAGCAAGGGGTGAAAGCTGGAACATTCTTTTGGTCTGTTGTCATC
CCTCACGAGCGGAGAATATTAACCATATTGCGGTGGCTCACCCTGCCAGATCATGAGAGG
CCTTCGGTCTATGCCTTCTATTCTGAGCAACCTGATTTCTCTGGACACAAATATGGCCCT
TTCGGCCCTGAGGAGAGTAGTTATGGCTCACCTTTTACTCCGGCTAAGAGACCTAAGAGG
AAAGTTGCCCCTAAGAGGAGACAGGAAAGACCAGTTGCTCCTCCAAAGAAAAGAAGAAGA
AAAATACATAGGATGGATCATTATGCTGCGGAAACTCGTCAGGACAAAATGACAAATCCT
CTGAGGGAAATCGACAAAATTGTGGGGCAATTAATGGATGGACTGAAACAACTAAAACTG
CGTCGGTGTGTCAACGTCATCTTTGTCGGAGACCATGGAATGGAAGATGTCACATGTGAT
AGAACTGAGTTCTTGAGTAATTACCTAACTAATGTGGATGATATTACTTTAGTGCCTGGA
ACTCTAGGAAGAATTCGATCCAAATTTAGCAACAATGCTAAATATGACCCCAAAGCCATT
ATTGCCAATCTCACGTGTAAAAAACCAGATCAGCACTTTAAGCCTTACTTGAAACAGCAC
CTTCCCAAACGTTTGCACTATGCCAACAACAGAAGAATTGAGGATATCCATTTATTGGTG
GAACGCAGATGGCATGTTGCAAGGAAACCTTTGGATGTTTATAAGAAACCATCAGGAAAA
TGCTTTTTCCAGGGAGACCACGGATTTGATAACAAGGTCAACAGCATGCAGACTGTTTTT
GTAGGTTATGGCCCAACATTTAAGTACAAGACTAAAGTGCCTCCATTTGAAAACATTGAA
CTTTACAATGTTATGTGTGATCTCCTGGGATTGAAGCCAGCTCCTAATAATGGGACCCAT
GGAAGTTTGAATCATCTCCTGCGCACTAATACCTTCAGGCCAACCATGCCAGAGGAAGTT
ACCAGACCCAATTATCCAGGGATTATGTACCTTCAGTCTGATTTTGACCTGGGCTGCACT
TGTGATGATAAGGTAGAGCCAAAGAACAAGTTGGATGAACTCAACAAACGGCTTCATACA
AAAGGGTCTACAGAAGAGAGACACCTCCTCTATGGGCGACCTGCAGTGCTTTATCGGACT
AGATATGATATCTTATATCACACTGACTTTGAAAGTGGTTATAGTGAAATATTCCTAATG
CTACTCTGGACATCATATACTGTTTCCAAACAGGCTGAGGTTTCCAGCGTTCCTGACCAT
CTGACCAGTTGCGTCCGGCCTGATGTCCGTGTTTCTCCGAGTTTCAGTCAGAACTGTTTG
GCCTACAAAAATGATAAGCAGATGTCCTACGGATTCCTCTTTCCTCCTTATCTGAGCTCT
TCACCAGAGGCTAAATATGATGCATTCCTTGTAACCAATATGGTTCCAATGTATCCTGCT
TTCAAACGGGTCTGGAATTATTTCCAAAGGGTATTGGTGAAGAAATATGCTTCGGAAAGA
AATGGAGTTAACGTGATAAGTGGACCAATCTTCGACTATGACTATGATGGCTTACATGAC
ACAGAAGACAAAATAAAACAGTACGTGGAAGGCAGTTCCATTCCTGTTCCAACTCACTAC
TACAGCATCATCACCAGCTGTCTGGATTTCACTCAGCCTGCCGACAAGTGTGACGGCCCT
CTCTCTGTGTCCTCCTTCATCCTGCCTCACCGGCCTGACAACGAGGAGAGCTGCAATAGC
TCAGAGGACGAATCAAAATGGGTAGAAGAACTCATGAAGATGCACACAGCTAGGGTGCGT
GACATTGAACATCTCACCAGCCTGGACTTCTTCCGAAAGACCAGCCGCAGCTACCCAGAA
ATCCTGACACTCAAGACATACCTGCATACATATGAGAGCGAGATTTAA
Enzyme 37 GenBank Gene ID L35594 Link Image
Enzyme 37 GeneCard ID ENPP2 Link Image
Enzyme 37 GenAtlas ID ENPP2 Link Image
Enzyme 37 HGNC ID HGNC:3357 Link Image
Enzyme 37 Chromosome Location 8
Enzyme 37 Locus 8q24.1
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Murata J, Lee HY, Clair T, Krutzsch HC, Arestad AA, Sobel ME, Liotta LA, Stracke ML: cDNA cloning of the human tumor motility-stimulating protein, autotaxin, reveals a homology with phosphodiesterases. J Biol Chem. 1994 Dec 2;269(48):30479-84. [PubMed Link Image]
  2. Lee HY, Murata J, Clair T, Polymeropoulos MH, Torres R, Manrow RE, Liotta LA, Stracke ML: Cloning, chromosomal localization, and tissue expression of autotaxin from human teratocarcinoma cells. Biochem Biophys Res Commun. 1996 Jan 26;218(3):714-9. [PubMed Link Image]
  3. Kawagoe H, Soma O, Goji J, Nishimura N, Narita M, Inazawa J, Nakamura H, Sano K: Molecular cloning and chromosomal assignment of the human brain-type phosphodiesterase I/nucleotide pyrophosphatase gene (PDNP2). Genomics. 1995 Nov 20;30(2):380-4. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 5401
Enzyme 38 Name Amine oxidase [flavin-containing] A
Enzyme 38 Synonyms
  1. Monoamine oxidase type A
  2. MAO-A
Enzyme 38 Gene Name MAOA
Enzyme 38 Protein Sequence >Amine oxidase [flavin-containing] A 
MENQEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHV
DYVDVGGAYVGPTQNRILRLSKELGIETYKVNVSERLVQYVKGKTYPFRGAFPPVWNPIA
YLDYNNLWRTIDNMGKEIPTDAPWEAQHADKWDKMTMKELIDKICWTKTARRFAYLFVNI
NVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKL
NHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPM
GAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPISITLDDTKPDGSLPAIMGFILARKADR
LAKLHKEIRKKKICELYAKVLGSQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYG
RVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLGKVTEKDIWVQEPESKD
VPAVEITHTFWERNLPSVSGLLKIIGFSTSVTALGFVLYKYKLLPRS
Enzyme 38 Number of Residues 527
Enzyme 38 Molecular Weight 59682
Enzyme 38 Theoretical pI 7.96
Enzyme 38 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 38 General Function Amino acid transport and metabolism
Enzyme 38 Specific Function Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine
Enzyme 38 Pathways
Enzyme 38 Reactions
  • RCH2NH2 + H2O + O2 = RCHO + ammonia + H2O2
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • 498-518
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 187353 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID P21397 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name AOFA_HUMAN Link Image
Enzyme 38 PDB ID 1O5W Link Image
Enzyme 38 PDB File Show
Enzyme 38 3D Structure
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >1584 bp 
ATGGAGAATCAAGAGAAGGCGAGTATCGCGGGCCACATGTTCGACGTAGTCGTGATCGGA
GGTGGCATTTCAGGACTATCTGCTGCCAAACTCTTGACTGAATATGGCGTTAGTGTTTTG
GTTTTAGAAGCTCGGGACAGGGTTGGAGGAAGAACATATACTATAAGGAATGAGCATGTT
GATTACGTAGATGTTGGTGGAGCTTATGTGGGACCAACCCAAAACAGAATCTTACGCTTG
TCTAAGGAGCTGGGCATAGAGACTTACAAAGTGAATGTCAGTGAGCGTCTCGTTCAATAT
GTCAAGGGGAAAACATATCCATTTCGGGGCGCCTTTCCACCAGTATGGAATCCCATTGCA
TATTTGGATTACAATAATCTGTGGAGGACAATAGATAACATGGGGAAGGAGATTCCAACT
GATGCACCCTGGGAGGCTCAACATGCTGACAAATGGGACAAAATGACCATGAAAGAGCTC
ATTGACAAAATCTGCTGGACAAAGACTGCTAGGCGGTTTGCTTATCTTTTTGTGAATATC
AATGTGACCTCTGAGCCTCACGAAGTGTCTGCCCTGTGGTTCTTGTGGTATGTGAAGCAG
TGCGGGGGCACCACTCGGATATTCTCTGTCACCAATGGTGGCCAGGAACGGAAGTTTGTA
GGTGGATCTGGTCAAGTGAGCGAACGGATAATGGACCTCCTCGGAGACCAAGTGAAGCTG
AACCATCCTGTCACTCACGTTGACCAGTCAAGTGACAACATCATCATAGAGACGCTGAAC
CATGAACATTATGAGTGCAAATACGTAATTAATGCGATCCCTCCGACCTTGACTGCCAAG
ATTCACTTCAGACCAGAGCTTCCAGCAGAGAGAAACCAGTTAATTCAGCGGCTTCCAATG
GGAGCTGTCATTAAGTGCATGATGTATTACAAGGAGGCCTTCTGGAAGAAGAAGGATTAC
TGTGGCTGCATGATCATTGAAGATGAAGATGCTCCAATTTCAATAACCTTGGATGACACC
AAGCCTGATGGGTCACTGCCTGCCATCATGGGCTTCATTCTTGCCCGGAAAGCTGATCGA
CTTGCTAAGCTACATAAGGAAATAAGGAAGAAGAAAATCTGTGAGCTCTATGCCAAAGTG
CTGGGATCCCAAGAAGCTTTACATCCAGTGCATTATGAAGAGAAGAACTGGTGTGAGGAG
CAGTACTCTGGGGGCTGCTACACGGCCTACTTCCCTCCTGGGATCATGACTCAATATGGA
AGGGTGATTCGTCAACCCGTGGGCAGGATTTTCTTTGCGGGCACAGAGACTGCCACAAAG
TGGAGCGGCTACATGGAAGGGGCAGTTGAGGCTGGAGAACGAGCAGCTAGGGAGGTCTTA
AATGGTCTCGGGAAGGTGACCGAGAAAGATATCTGGGTACAAGAACCTGAATCAAAGGAC
GTTCCAGCGGTAGAAATCACCCACACCTTCTGGGAAAGGAACCTGCCCTCTGTTTCTGGC
CTGCTGAAGATCATTGGATTTTCCACATCAGTAACTGCCCTGGGGTTTGTGCTGTACAAA
TACAAGCTCCTGCCACGGTCTTGA
Enzyme 38 GenBank Gene ID M68840 Link Image
Enzyme 38 GeneCard ID MAOA Link Image
Enzyme 38 GenAtlas ID MAOA Link Image
Enzyme 38 HGNC ID HGNC:6833 Link Image
Enzyme 38 Chromosome Location X
Enzyme 38 Locus Xp11.3
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Hsu YP, Weyler W, Chen S, Sims KB, Rinehart WB, Utterback MC, Powell JF, Breakefield XO: Structural features of human monoamine oxidase A elucidated from cDNA and peptide sequences. J Neurochem. 1988 Oct;51(4):1321-4. [PubMed Link Image]
  2. Bach AW, Lan NC, Johnson DL, Abell CW, Bembenek ME, Kwan SW, Seeburg PH, Shih JC: cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties. Proc Natl Acad Sci U S A. 1988 Jul;85(13):4934-8. [PubMed Link Image]
  3. Zhu QS, Grimsby J, Chen K, Shih JC: Promoter organization and activity of human monoamine oxidase (MAO) A and B genes. J Neurosci. 1992 Nov;12(11):4437-46. [PubMed Link Image]
  4. Denney RM: The promoter of the human monoamine oxidase A gene. Prog Brain Res. 1995;106:57-66. [PubMed Link Image]
  5. Denney RM, Sharma A, Dave SK, Waguespack A: A new look at the promoter of the human monoamine oxidase A gene: mapping transcription initiation sites and capacity to drive luciferase expression. J Neurochem. 1994 Sep;63(3):843-56. [PubMed Link Image]
  6. Chen SA, Weyler W: Partial amino acid sequence analysis of human placenta monoamine oxidase A and bovine liver monoamine oxidase B. Biochem Biophys Res Commun. 1988 Oct 14;156(1):445-50. [PubMed Link Image]
  7. Weyler W: Monoamine oxidase A from human placenta and monoamine oxidase B from bovine liver both have one FAD per subunit. Biochem J. 1989 Jun 15;260(3):725-9. [PubMed Link Image]
  8. Li M, Hubalek F, Newton-Vinson P, Edmondson DE: High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiae. Protein Expr Purif. 2002 Feb;24(1):152-62. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 5413
Enzyme 39 Name Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase
Enzyme 39 Synonyms
  1. XD
  2. Xanthine oxidase
  3. XO
  4. Xanthine oxidoreductase]
Enzyme 39 Gene Name XDH
Enzyme 39 Protein Sequence >Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase 
MTADKLVFFVNGRKVVEKNADPETTLLAYLRRKLGLSGTKLGCGEGGCGACTVMLSKYDR
LQNKIVHFSANACLAPICSLHHVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGI
VMSMYTLLRNQPEPTMEEIENAFQGNLCRCTGYRPILQGFRTFARDGGCCGGDGNNPNCC
MNQKKDHSVSLSPSLFKPEEFTPLDPTQEPIFPPELLRLKDTPRKQLRFEGERVTWIQAS
TLKELLDLKAQHPDAKLVVGNTEIGIEMKFKNMLFPMIVCPAWIPELNSVEHGPDGISFG
AACPLSIVEKTLVDAVAKLPAQKTEVFRGVLEQLRWFAGKQVKSVASVGGNIITASPISD
LNPVFMASGAKLTLVSRGTRRTVQMDHTFFPGYRKTLLSPEEILLSIEIPYSREGEYFSA
FKQASRREDDIAKVTSGMRVLFKPGTTEVQELALCYGGMANRTISALKTTQRQLSKLWKE
ELLQDVCAGLAEELHLPPDAPGGMVDFRCTLTLSFFFKFYLTVLQKLGQENLEDKCGKLD
PTFASATLLFQKDPPADVQLFQEVPKGQSEEDMVGRPLPHLAADMQASGEAVYCDDIPRY
ENELSLRLVTSTRAHAKIKSIDTSEAKKVPGFVCFISADDVPGSNITGICNDETVFAKDK
VTCVGHIIGAVVADTPEHTQRAAQGVKITYEELPAIITIEDAIKNNSFYGPELKIEKGDL
KKGFSEADNVVSGEIYIGGQEHFYLETHCTIAVPKGEAGEMELFVSTQNTMKTQSFVAKM
LGVPANRIVVRVKRMGGGFGGKETRSTVVSTAVALAAYKTGRPVRCMLDRDEDMLITGGR
HPFLARYKVGFMKTGTVVALEVDHFSNVGNTQDLSQSIMERALFHMDNCYKIPNIRGTGR
LCKTNLPSNTAFRGFGGPQGMLIAECWMSEVAVTCGMPAEEVRRKNLYKEGDLTHFNQKL
EGFTLPRCWEECLASSQYHARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGA
LLHVYTDGSVLLTHGGTEMGQGLHTKMVQVASRALKIPTSKIYISETSTNTVPNTSPTAA
SVSADLNGQAVYAACQTILKRLEPYKKKNPSGSWEDWVTAAYMDTVSLSATGFYRTPNLG
YSFETNSGNPFHYFSYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAF
VQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPIEFRVSLLRDCPNKKAIYASKAV
GEPPLFLAASIFFAIKDAIRAARAQHTGNNVKELFRLDSPATPEKIRNACVDKFTTLCVT
GVPENCKPWSVRV
Enzyme 39 Number of Residues 1333
Enzyme 39 Molecular Weight 146426
Enzyme 39 Theoretical pI 7.70
Enzyme 39 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron transporter activity
  • ion binding
  • iron ion binding
  • metal ion binding
  • oxidoreductase activity
  • transition metal ion binding
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
—
Enzyme 39 General Function Nucleotide transport and metabolism
Enzyme 39 Specific Function This enzyme can be converted from the dehydrogenase form (D) to the oxidase form (O) irreversibly by proteolysis or reversibly through the oxidation of sulfhydryl groups
Enzyme 39 Pathways
Enzyme 39 Reactions
  • xanthine + H2O + O2 = urate + H2O2
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 10336525 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID P47989 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name XDH_HUMAN Link Image
Enzyme 39 PDB ID 1V97 Link Image
Enzyme 39 PDB File Show
Enzyme 39 3D Structure
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >4002 bp 
ATGACAGCAGACAAATTGGTTTTCTTTGTGAATGGCAGAAAGGTGGTGGAGAAAAATGCA
GATCCAGAGACAACCCTTTTGGCCTACCTGAGAAGAAAGTTGGGGCTGAGTGGAACCAAG
CTCGGCTGTGGAGAGGGGGGCTGCGGGGCTTGCACAGTGATGCTCTCCAAGTATGATCGT
CTGCAGAACAAGATCGTCCACTTTTCTGCCAATGCCTGCCTGGCCCCCATCTGCTCCTTG
CACCATGTTGCAGTGACAACTGTGGAAGGAATAGGAAGCACCAAGACGAGGCTGCATCCT
GTGCAGGAGAGAATTGCCAAAAGCCACGGCTCCCAGTGCGGGTTCTGCACCCCTGGCATC
GTCATGAGTATGTACACACTGCTCCGGAATCAGCCCGAGCCCACCATGGAGGAGATTGAG
AATGCCTTCCAAGGAAATCTGTGCCGCTGCACAGGCTACAGACCCATCCTCCAGGGCTTC
CGGACCTTTGCCAGGGATGGTGGATGCTGTGGAGGAGATGGGAATAATCCAAATTGCTGC
ATGAACCAGAAGAAAGACCACTCAGTCAGCCTCTCGCCATCTTTATTCAAACCAGAGGAG
TTCACGCCCCTGGATCCAACCCAGGAGCCCATTTTTCCCCCAGAGTTGCTGAGGCTGAAA
GACACTCCTCGGAAGCAGCTGCGATTTGAAGGGGAGCGTGTGACGTGGATACAGGCCTCA
ACCCTCAAGGAGCTGCTGGACCTCAAGGCTCAGCACCCTGACGCCAAGCTGGTCGTGGGG
AACACGGAGATTGGCATTGAGATGAAGTTCAAGAATATGCTGTTTCCTATGATTGTCTGC
CCAGCCTGGATCCCTGAGCTGAATTCGGTAGAACATGGACCCGACGGTATCTCCTTTGGA
GCTGCTTGCCCCCTGAGCATTGTGGAAAAAACCCTGGTGGATGCTGTTGCTAAGCTTCCT
GCCCAAAAGACAGAGGTGTTCAGAGGGGTCCTGGAGCAGCTGCGCTGGTTTGCTGGGAAG
CAAGTCAAGTCTGTGGCGTCCGTTGGAGGGAACATCATCACTGCCAGCCCCATCTCCGAC
CTCAACCCCGTGTTCATGGCCAGTGGGGCCAAGCTGACACTTGTGTCCAGAGGCACCAGG
AGAACTGTCCAGATGGACCACACCTTCTTCCCTGGCTACAGAAAGACCCTGCTGAGCCCG
GAGGAGATACTGCTCTCCATAGAGATCCCCTACAGCAGGGAGGGGGAGTATTTCTCAGCA
TTCAAGCAGGCCTCCCGGAGAGAAGATGACATTGCCAAGGTAACCAGTGGCATGAGAGTT
TTATTCAAGCCAGGAACCACAGAGGTACAGGAGCTGGCCCTTTGCTATGGTGGAATGGCC
AACAGAACCATCTCAGCCCTCAAGACCACTCAGAGGCAGCTTTCCAAGCTCTGGAAGGAG
GAGCTGCTGCAGGACGTGTGTGCAGGACTGGCAGAGGAGCTGCATCTGCCTCCCGATGCC
CCTGGTGGCATGGTGGACTTCCGGTGCACCCTCACCCTCAGCTTCTTCTTCAAGTTCTAC
CTGACAGTCCTTCAGAAGCTGGGCCAAGAGAACCTGGAAGACAAGTGTGGTAAACTGGAC
CCCACTTTCGCCAGTGCAACTTTACTGTTTCAGAAAGACCCCCCAGCCGATGTCCAGCTC
TTCCAAGAGGTGCCCAAGGGTCAGTCTGAGGAGGACATGGTGGGCCGGCCCCTGCCCCAC
CTGGCAGCGGACATGCAGGCCTCTGGTGAGGCCGTGTACTGTGACGACATTCCTCGCTAC
GAGAATGAGCTGTCTCTCCGGCTGGTCACCAGCACCCGGGCCCACGCCAAGATCAAGTCC
ATAGATACATCAGAAGCTAAGAAGGTTCCAGGGTTTGTTTGTTTCATTTCCGCTGATGAT
GTTCCTGGGAGTAACATAACTGGAATTTGTAATGATGAGACAGTCTTTGCGAAGGATAAG
GTTACTTGTGTTGGGCATATCATTGGTGCTGTGGTTGCTGACACCCCGGAACACACACAG
AGAGCTGCCCAAGGGGTGAAAATCACCTATGAAGAACTACCAGCCATTATCACAATTGAG
GATGCTATAAAGAACAACTCCTTTTATGGACCTGAGCTGAAGATCGAGAAAGGGGACCTA
AAGAAGGGGTTTTCCGAAGCAGATAATGTTGTGTCAGGGGAGATATACATCGGTGGCCAA
GAGCACTTCTACCTGGAGACTCACTGCACCATTGCTGTTCCAAAAGGCGAGGCAGGGGAG
ATGGAGCTCTTTGTGTCTACACAGAACACCATGAAGACCCAGAGCTTTGTTGCAAAAATG
TTGGGGGTTCCAGCAAACCGGATTGTGGTTCGAGTGAAGAGAATGGGAGGAGGCTTTGGA
GGCAAGGAGACCCGGAGCACTGTGGTGTCCACGGCAGTGGCCCTGGCTGCATATAAGACC
GGCCGCCCTGTGCGATGCATGCTGGACCGTGATGAGGACATGCTGATAACTGGTGGCAGA
CATCCCTTCCTGGCCAGATACAAGGTTGGCTTCATGAAGACTGGGACAGTTGTGGCTCTT
GAGGTGGACCACTTCAGCAATGTGGGGAACACCCAGGATCTCTCTCAGAGTATTATGGAA
CGAGCTTTATTCCACATGGACAACTGCTATAAAATCCCCAACATCCGGGGCACTGGGCGG
CTGTGCAAAACCAACCTTCCCTCCAACACGGCCTTCCGGGGCTTTGGGGGGCCCCAGGGG
ATGCTCATTGCCGAGTGCTGGATGAGTGAAGTTGCAGTGACCTGTGGGATGCCTGCAGAG
GAGGTGCGGAGAAAAAACCTGTACAAAGAAGGGGACCTGACACACTTCAACCAGAAGCTT
GAGGGTTTCACCTTGCCCAGATGCTGGGAAGAATGCCTAGCAAGCTCTCAGTATCATGCT
CGGAAGAGTGAGGTTGACAAGTTCAACAAGGAGAATTGTTGGAAAAAGAGAGGATTGTGC
ATAATTCCCACCAAGTTTGGAATAAGCTTCACAGTTCCTTTTCTGAATCAGGCAGGAGCC
CTACTTCATGTGTACACAGATGGCTCTGTGCTGCTGACCCACGGGGGGACTGAGATGGGC
CAAGGCCTTCATACCAAAATGGTCCAGGTGGCCAGTAGAGCTCTGAAAATCCCCACCTCT
AAGATTTATATCAGCGAGACAAGCACTAACACTGTGCCCAACACCTCTCCCACGGCTGCC
TCTGTCAGCGCTGACCTCAATGGACAGGCCGTCTATGCGGCTTGTCAGACCATCTTGAAA
AGGCTGGAACCCTACAAGAAGAAGAATCCCAGTGGCTCCTGGGAAGACTGGGTCACAGCT
GCCTACATGGACACAGTGAGCTTGTCTGCCACTGGGTTTTATAGAACACCCAATCTGGGC
TACAGCTTTGAGACTAACTCAGGGAACCCCTTCCACTACTTCAGCTATGGGGTGGCTTGC
TCTGAAGTAGAAATCGACTGCCTAACAGGAGATCATAAGAACCTCCGCACAGATATTGTC
ATGGATGTTGGCTCCAGTCTAAACCCTGCCATTGATATTGGACAGGTGGAAGGGGCATTT
GTCCAGGGCCTTGGCCTCTTCACCCTAGAGGAGCTACACTATTCCCCCGAGGGGAGCCTG
CACACCCGTGGCCCTAGCACCTACAAGATCCCGGCATTTGGCAGCATCCCCATTGAGTTC
AGGGTGTCCCTGCTCCGCGACTGCCCCAACAAGAAGGCCATCTATGCATCGAAGGCTGTT
GGAGAGCCGCCCCTCTTCCTGGCTGCTTCTATCTTCTTTGCCATCAAAGATGCCATCCGT
GCAGCTCGAGCTCAGCACACAGGTAATAACGTGAAGGAACTCTTCCGGCTAGACAGCCCT
GCCACCCCGGAGAAGATCCGCAATGCCTGCGTGGACAAGTTCACCACCCTGTGTGTCACT
GGTGTCCCAGAAAACTGCAAACCCTGGTCTGTGAGGGTCTAA
Enzyme 39 GenBank Gene ID D11456 Link Image
Enzyme 39 GeneCard ID XDH Link Image
Enzyme 39 GenAtlas ID XDH Link Image
Enzyme 39 HGNC ID HGNC:12805 Link Image
Enzyme 39 Chromosome Location 2
Enzyme 39 Locus 2p23.1
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Ichida K, Amaya Y, Noda K, Minoshima S, Hosoya T, Sakai O, Shimizu N, Nishino T: Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene. Gene. 1993 Nov 15;133(2):279-84. [PubMed Link Image]
  2. Xu P, Huecksteadt TP, Harrison R, Hoidal JR: Molecular cloning, tissue expression of human xanthine dehydrogenase. Biochem Biophys Res Commun. 1994 Mar 15;199(2):998-1004. [