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Human Metabolome Database Version 2.5

 

Showing metabocard for ADP (HMDB01341)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-01-20 12:04:58
Accession Number HMDB01341
Secondary Accession Numbers Not Available
Common Name ADP
Description Adenosine diphosphate, abbreviated ADP, is a nucleotide. It is an ester of pyrophosphoric acid with the nucleotide adenine. ADP consists of the pyrophosphate group, the pentose sugar ribose, and the nucleobase adenine. ADP is the product of ATP dephosphorylation by ATPases. ADP is converted back to ATP by ATP synthases.
Synonyms
  1. adenosindiphosphorsaeure
  2. adenosine 5'-pyrophosphate
  3. adenosine diphosphate
  4. adenosine pyrophosphate
  5. adenosine-5'-diphosphate
  6. adenosine-5-diphosphate
  7. adenosine-diphosphate
  8. adp
Chemical IUPAC Name [[5-(6-aminopurin-9-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxyphosphonic acid
Chemical Formula C10H15N5O10P2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide diphosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-diol
  • primary amine
  • primary aromatic amine
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Alanine and aspartate metabolism
  • Component of Aminosugars metabolism
  • Component of Arginine and proline metabolism
  • Component of C5-Branched dibasic acid metabolism
  • Component of Folate biosynthesis
  • Component of Fructose and mannose metabolism
  • Component of Galactose metabolism
  • Component of Glutamate metabolism
  • Component of Glutathione metabolism
  • Component of Glycerolipid metabolism
  • Component of Glycerophospholipid metabolism
  • Component of Glycine, serine and threonine metabolism
  • Component of Glycosphingolipid metabolism
  • Component of Glyoxylate and dicarboxylate metabolism
  • Component of Inositol phosphate metabolism
  • Component of Nicotinate and nicotinamide metabolism
  • Component of Nitrogen metabolism
  • Component of Pantothenate and CoA biosynthesis
  • Component of Peptidoglycan biosynthesis
  • Component of Propanoate metabolism
  • Component of Purine metabolism
  • Component of Pyrimidine metabolism
  • Component of Pyruvate metabolism
  • Component of Riboflavin metabolism
  • Component of Starch and sucrose metabolism
  • Component of Streptomycin biosynthesis
  • Component of Tetracycline biosynthesis
  • Component of Vitamin B6 metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 427.201
Monoisotopic Molecular Weight 427.029419
Isomeric SMILES NC1=NC=NC2=C1N=CN2[C@@H]1O[C@H](COP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1O
Canonical SMILES NC1=NC=NC2=C1N=CN2C1OC(COP(O)(=O)OP(O)(O)=O)C(O)C1O
KEGG Compound ID C00008 Link Image
BioCyc ID ADP Link Image
BiGG ID 33496 Link Image
Wikipedia Link ADP Link Image
NuGOwiki Link HMDB01341 Link Image
Metagene Link HMDB01341 Link Image
METLIN ID 6175 Link Image
PubChem Compound 6022 Link Image
PubChem Substance 10322523 Link Image
ChEBI ID 32889 Link Image
CAS Registry Number 58-64-0
InChI Identifier InChI=1/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
Synthesis Reference Yamagata, Yukio. Prebiotic formation of ADP and ATP from AMP, calcium phosphates and cyanate in aqueous solution. Origins of Life and Evolution of the Biosphere (1999), 29(5), 511-520.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 18.4 mg/mL [MEYLAN,WM et al. (1996)]; 3.27 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -3
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.65 [Predicted by ALOGPS]; -4.3 [Predicted by PubChem via XLOGP]; -2.64 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 13PK Link Image
Experimental PDB File Show
Experimental PDB Structure
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm
  • Nucleus
  • endoplasmic reticulum
  • Extracellular
  • mitochondria
  • peroxisome
Biofluid Location
  • Blood
  • Cellular Cytoplasm
  • Cerebrospinal Fluid
Tissue Location
Tissue References
All Tissues —
Concentrations (Normal)
Biofluid Blood
Value 160.0 +/- 14.0 uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Biofluid Cellular Cytoplasm
Value 270 (150-390) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed Link Image]
Biofluid CSF
Value 1.90 +/- 0.025 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid CSF
Value 1.10 +/- 0.60 uM
Age Adult:>18 yrs old
Sex Both
Condition Rachialgia
Comments Not Available
References
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Biofluid CSF
Value 0.91 +/- 0.46 uM
Age Adult:>18 yrs old
Sex Both
Condition Subarachnoid hemorrhage
Comments Not Available
References
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Biofluid CSF
Value 0.63 +/- 0.37 uM
Age Adult:>18 yrs old
Sex Both
Condition Epilepsy
Comments Not Available
References
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Biofluid CSF
Value 1.86 +/- 1.67 uM
Age Adult:>18 yrs old
Sex Both
Condition Stroke
Comments Cerebral stroke
References
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Biofluid CSF
Value 1.62 +/- 0.96 uM
Age Adult:>18 yrs old
Sex Both
Condition Neuroinfection
Comments Not Available
References
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Associated Disorders
Condition References
Epilepsy
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Neuroinfection
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Rachialgia
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Stroke
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
Subarachnoid hemorrhage
  • Czarnecka J, Cieslak M, Michal K: Application of solid phase extraction and high-performance liquid chromatography to qualitative and quantitative analysis of nucleotides and nucleosides in human cerebrospinal fluid. J Chromatogr B Analyt Technol Biomed Life Sci. 2005 Aug 5;822(1-2):85-90. [PubMed Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Amino Sugar Metabolism SMP00045 Link Image map00520 Link Image
Ammonia Recycling SMP00009 Link Image map00910 Link Image
Citric Acid Cycle SMP00057 Link Image map00020 Link Image
Folate Metabolism SMP00053 Link Image map00670 Link Image
Gluconeogenesis SMP00128 Link Image map00010 Link Image
Glycerolipid Metabolism SMP00039 Link Image map00561 Link Image
Glycine and Serine Metabolism SMP00004 Link Image map00260 Link Image
Glycolysis SMP00040 Link Image map00010 Link Image
Histidine Metabolism SMP00044 Link Image map00340 Link Image
Inositol Phosphate Metabolism SMP00462 Link Image map00562 Link Image
Lactose Degradation SMP00457 Link Image
Lactose Synthesis SMP00444 Link Image
Mitochondrial Electron Transport Chain SMP00355 Link Image map00190 Link Image
Phosphatidylinositol Phosphate Metabolism SMP00463 Link Image map00562 Link Image
Phytanic Acid Peroxisomal Oxidation SMP00450 Link Image
Purine Metabolism SMP00050 Link Image map00230 Link Image
Threonine and 2-Oxobutanoate Degradation SMP00452 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. Quinton TM, Kim S, Jin J, Kunapuli SP: Lipid rafts are required in Galpha(i) signaling downstream of the P2Y12 receptor during ADP-mediated platelet activation. J Thromb Haemost. 2005 May;3(5):1036-41. [PubMed Link Image]
  2. Saxena R, Gupta M, Gupta S, Kannan M, Ahmed RP, Choudhry VP: Inherited heterogenous defect in platelet aggregation selectively with ADP and epinephrine--a series of 25 cases. Indian J Pathol Microbiol. 2005 Jul;48(3):345-8. [PubMed Link Image]
  3. Corsonello A, Malara A, De Domenico D, Damiano MC, Mirone S, Loddo S, Ientile R, Corica F: Effects of magnesium sulphate on leptin-dependent platelet aggregation: an ex vivo study. Magnes Res. 2005 Mar;18(1):7-11. [PubMed Link Image]
  4. Cuisset T, Frere C, Quilici J, Barbou F, Morange PE, Hovasse T, Bonnet JL, Alessi MC: High post-treatment platelet reactivity identified low-responders to dual antiplatelet therapy at increased risk of recurrent cardiovascular events after stenting for acute coronary syndrome. J Thromb Haemost. 2006 Mar;4(3):542-9. Epub 2005 Dec 22. [PubMed Link Image]
  5. Imura Y, Stassen JM, Bunting S, Stockmans F, Collen D: Antithrombotic properties of L-cysteine, N-(mercaptoacetyl)-D-Tyr-Arg-Gly-Asp-sulfoxide (G4120) in a hamster platelet-rich femoral vein thrombosis model. Blood. 1992 Sep 1;80(5):1247-53. [PubMed Link Image]
  6. Cuisset T, Frere C, Quilici J, Morange PE, Nait-Saidi L, Carvajal J, Lehmann A, Lambert M, Bonnet JL, Alessi MC: Benefit of a 600-mg loading dose of clopidogrel on platelet reactivity and clinical outcomes in patients with non-ST-segment elevation acute coronary syndrome undergoing coronary stenting. J Am Coll Cardiol. 2006 Oct 3;48(7):1339-45. Epub 2006 Sep 12. [PubMed Link Image]
  7. Vigue C, Vigue L, Huszar G: Adenosine triphosphate (ATP) concentrations and ATP/adenosine diphosphate ratios in human sperm of normospermic, oligospermic, and asthenospermic specimens and in their swim-up fractions: lack of correlation between ATP parameters and sperm creatine kinase concentrations. J Androl. 1992 Jul-Aug;13(4):305-11. [PubMed Link Image]
  8. Smith SM, Judge HM, Peters G, Storey RF: Multiple antiplatelet effects of clopidogrel are not modulated by statin type in patients undergoing percutaneous coronary intervention. Platelets. 2004 Dec;15(8):465-74. [PubMed Link Image]
  9. Ji Q, Ghaly M, Hjemdahl P, Tornvall P, Li N: Contrast medium attenuates platelet activation and platelet-leukocyte cross-talk. Thromb Haemost. 2005 May;93(5):922-6. [PubMed Link Image]
  10. Nakayama Y, Kinoshita A, Tomita M: Dynamic simulation of red blood cell metabolism and its application to the analysis of a pathological condition. Theor Biol Med Model. 2005 May 9;2(1):18. [PubMed Link Image]
  11. Morshedi M, Oehninger S, Blackmore P, Bocca S, Coddington C, Hodgen G: Investigation of some biochemical and functional effects of cryopreservation of human spermatozoa using an automated freezing-quick-thawing method. Int J Androl. 1995 Dec;18(6):279-86. [PubMed Link Image]
  12. Hua J, Suguro S, Iwabuchi K, Tsutsumi-Ishii Y, Sakamoto K, Nagaoka I: Glucosamine, a naturally occurring amino monosaccharide, suppresses the ADP-mediated platelet activation in humans. Inflamm Res. 2004 Dec;53(12):680-8. [PubMed Link Image]
  13. Shabanova EY, Mindukshev IV, Malakhovskaya EA, Vivulanets EV, Petrishchev NN, Krivchenko AI: Cooperative type of platelet hypersensitivity to ADP. Bull Exp Biol Med. 2005 Sep;140(3):282-4. [PubMed Link Image]
  14. Wikipedia Link Image
Metabolic Enzymes
  1. Deoxycytidine kinase
  2. ATP-citrate synthase
  3. Acetyl-CoA carboxylase 2
  4. Pyruvate carboxylase, mitochondrial precursor
  5. Acetyl-CoA carboxylase 1
  6. Thymidylate kinase
  7. Ectonucleoside triphosphate diphosphohydrolase 1
  8. Soluble calcium-activated nucleotidase 1
  9. Thymidine kinase, cytosolic
  10. Nucleoside diphosphate kinase, mitochondrial precursor
  11. Ribonucleoside-diphosphate reductase large subunit
  12. Nucleoside diphosphate kinase A
  13. Nucleoside diphosphate kinase 7
  14. Ribonucleoside-diphosphate reductase M2 subunit
  15. Nucleoside diphosphate kinase B
  16. Nucleoside diphosphate kinase 3
  17. Nucleoside diphosphate kinase 6
  18. Glucokinase
  19. Hexokinase-3
  20. Hexokinase-2
  21. Diacylglycerol kinase alpha
  22. Diacylglycerol kinase delta
  23. Diacylglycerol kinase iota
  24. Diacylglycerol kinase zeta
  25. L-fucose kinase
  26. Propionyl-CoA carboxylase beta chain, mitochondrial precursor
  27. Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1
  28. Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 2
  29. Carbamoyl-phosphate synthase [ammonia], mitochondrial precursor
  30. ADP-dependent glucokinase
  31. Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial precursor
  32. Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial precursor
  33. Glutamate--cysteine ligase catalytic subunit
  34. Adenylate kinase isoenzyme 1
  35. GTP:AMP phosphotransferase mitochondrial
  36. Putative adenylate kinase 7
  37. Bis(5'-adenosyl)-triphosphatase
  38. ADP-ribose pyrophosphatase, mitochondrial precursor
  39. Adenosine kinase
  40. Adenylate kinase isoenzyme 5
  41. CTP synthase 1
  42. Creatine kinase, sarcomeric mitochondrial precursor
  43. Creatine kinase, ubiquitous mitochondrial precursor
  44. Creatine kinase M-type
  45. 6-phosphofructokinase type C
  46. 6-phosphofructokinase, liver type
  47. 6-phosphofructokinase, muscle type
  48. Pyruvate kinase isozymes R/L
  49. Deoxyguanosine kinase, mitochondrial precursor
  50. Choline kinase alpha
  51. Glutathione synthetase
  52. 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3
  53. 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4
  54. 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1
  55. 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2
  56. Glycerol kinase, testis specific 2
  57. Folylpolyglutamate synthase, mitochondrial precursor
  58. Delta 1-pyrroline-5-carboxylate synthetase
  59. 5-oxoprolinase
  60. Ethanolamine kinase 1
  61. Ectonucleoside triphosphate diphosphohydrolase 4
  62. Ectonucleoside triphosphate diphosphohydrolase 6
  63. Ectonucleoside triphosphate diphosphohydrolase 5 precursor
  64. Multifunctional protein ADE2 [Includes: Phosphoribosylaminoimidazole- succinocarboxamide synthase
  65. ADP-ribosyl cyclase 1
  66. Guanylate kinase
  67. Inositol-trisphosphate 3-kinase B
  68. Inositol-trisphosphate 3-kinase A
  69. Diphosphomevalonate decarboxylase
  70. Phosphomevalonate kinase
  71. Pantothenate kinase 4
  72. Pantothenate kinase 1
  73. Pantothenate kinase 3
  74. N-acetylglucosamine kinase
  75. Pyridoxal kinase
  76. Riboflavin kinase
  77. Sphingosine kinase 2
  78. Ribokinase
  79. cGMP-dependent protein kinase 1, alpha isozyme
  80. cGMP-dependent protein kinase 2
  81. Microtubule-associated serine/threonine-protein kinase 1
  82. Probable phospholipid-transporting ATPase IG
  83. Probable phospholipid-transporting ATPase IH
  84. Serine/threonine-protein kinase RIO2
  85. Mitogen-activated protein kinase kinase kinase 1
  86. Mitogen-activated protein kinase 12
  87. Cell division protein kinase 3
  88. Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing gamma polypeptide
  89. Mitogen-activated protein kinase kinase kinase kinase 3
  90. Mitogen-activated protein kinase kinase kinase 3
  91. Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta isoform
  92. Death-associated protein kinase 3
  93. Tyrosine-protein kinase TXK
  94. Epithelial discoidin domain-containing receptor 1 precursor
  95. Proto-oncogene tyrosine-protein kinase Src
  96. Receptor-interacting serine/threonine-protein kinase 3
  97. BDNF/NT-3 growth factors receptor precursor
  98. Activin receptor type-2B precursor
  99. Death-associated protein kinase 2
  100. Plasma membrane calcium-transporting ATPase 3
  101. RAF proto-oncogene serine/threonine-protein kinase
  102. Macrophage-stimulating protein receptor precursor
  103. Vascular endothelial growth factor receptor 3 precursor
  104. Glycogen synthase kinase-3 beta
  105. Katanin p60 ATPase-containing subunit A1
  106. Dual specificity protein kinase CLK4
  107. Vacuolar ATP synthase subunit G 3
  108. Receptor tyrosine-protein kinase erbB-3 precursor
  109. Ephrin type-A receptor 5 precursor
  110. Probable phospholipid-transporting ATPase VA
  111. Cell division protein kinase 10
  112. Serine/threonine-protein kinase Nek1
  113. Activin receptor type-1 precursor
  114. Mitogen-activated protein kinase kinase kinase 14
  115. Tyrosine-protein kinase transmembrane receptor ROR2 precursor
  116. MAP/microtubule affinity-regulating kinase 3
  117. Tyrosine-protein kinase-like 7 precursor
  118. Mitotic checkpoint serine/threonine-protein kinase BUB1
  119. Serine/threonine-protein kinase 38
  120. Ephrin type-B receptor 1 precursor
  121. Vacuolar ATP synthase subunit G 1
  122. Insulin-like growth factor 1 receptor precursor
  123. FL cytokine receptor precursor
  124. Mitogen-activated protein kinase 1
  125. Cell division protein kinase 8
  126. Probable phospholipid-transporting ATPase IC
  127. Phosphorylase b kinase gamma catalytic chain, skeletal muscle isoform
  128. Tyrosine-protein kinase JAK2
  129. Serine/threonine-protein kinase N2
  130. Sodium/potassium-transporting ATPase subunit beta-3
  131. Plasma membrane calcium-transporting ATPase 1
  132. Maternal embryonic leucine zipper kinase
  133. Mitogen-activated protein kinase 7
  134. Ketohexokinase
  135. ATP synthase epsilon chain, mitochondrial
  136. cAMP-dependent protein kinase, gamma-catalytic subunit
  137. Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta isoform
  138. Bone morphogenetic protein receptor type IA precursor
  139. Cyclin-dependent kinase-like 5
  140. Wee1-like protein kinase
  141. Myosin light chain kinase 2, skeletal/cardiac muscle
  142. ATP synthase delta chain, mitochondrial precursor
  143. Tyrosine-protein kinase 6
  144. Serine/threonine-protein kinase PINK1, mitochondrial precursor
  145. Tyrosine-protein kinase receptor TYRO3 precursor
  146. A-Raf proto-oncogene serine/threonine-protein kinase
  147. Probable phospholipid-transporting ATPase IIA
  148. Serine/threonine-protein kinase receptor R3 precursor
  149. ALK tyrosine kinase receptor precursor
  150. Sodium/potassium-transporting ATPase subunit beta-2
  151. Plasma membrane calcium-transporting ATPase 2
  152. Ribosomal protein S6 kinase alpha-4
  153. Sodium/potassium-transporting ATPase subunit beta-1
  154. Proto-oncogene tyrosine-protein kinase Yes
  155. Serine-protein kinase ATM
  156. Dual specificity tyrosine-phosphorylation-regulated kinase 1B
  157. Fibroblast growth factor receptor 4 precursor
  158. MAP kinase-interacting serine/threonine-protein kinase 2
  159. Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
  160. Cytoplasmic tyrosine-protein kinase BMX
  161. Probable phospholipid-transporting ATPase VD
  162. Serine/threonine-protein kinase Pim-3
  163. Hormonally up-regulated neu tumor-associated kinase
  164. Serine/threonine-protein kinase 38-like
  165. MAP/microtubule affinity-regulating kinase 4
  166. Transient receptor potential cation channel subfamily M member 6
  167. Insulin receptor-related protein precursor
  168. Ephrin type-A receptor 2 precursor
  169. Serine/threonine-protein kinase Chk2
  170. Dual specificity protein kinase CLK1
  171. Sarcoplasmic/endoplasmic reticulum calcium ATPase 3
  172. Tyrosine-protein kinase HCK
  173. Vacuolar ATP synthase subunit C 1
  174. Serine/threonine-protein kinase Sgk1
  175. Homeodomain-interacting protein kinase 3
  176. Serine/threonine-protein kinase Nek6
  177. Discoidin domain-containing receptor 2 precursor
  178. Serine/threonine-protein kinase 10
  179. Serine/threonine-protein kinase PAK 4
  180. Cell division cycle 2-like protein kinase 5
  181. Serine/threonine-protein kinase VRK1
  182. Vascular endothelial growth factor receptor 2 precursor
  183. Vacuolar ATP synthase subunit G 2
  184. FYVE finger-containing phosphoinositide kinase
  185. BR serine/threonine-protein kinase 2
  186. Serine/threonine-protein kinase MARK1
  187. Serine/threonine-protein kinase Pim-2
  188. Serine/threonine-protein kinase Nek3
  189. Focal adhesion kinase 1
  190. ATP synthase coupling factor 6, mitochondrial precursor
  191. Bifunctional polynucleotide phosphatase/kinase
  192. Inositol polyphosphate multikinase
  193. Serine/threonine-protein kinase PRP4 homolog
  194. Serine/threonine-protein kinase PLK4
  195. Polyribonucleotide nucleotidyltransferase 1, mitochondrial precursor
  196. Non-receptor tyrosine-protein kinase TNK1
  197. Beta-adrenergic receptor kinase 2
  198. Cell division cycle 2-related protein kinase 7
  199. Vacuolar ATP synthase subunit B, kidney isoform
  200. Calcium/calmodulin-dependent protein kinase type 1G
  201. Ephrin type-B receptor 4 precursor
  202. Serine/threonine-protein kinase Nek9
  203. Potassium-transporting ATPase alpha chain 2
  204. Inhibitor of nuclear factor kappa-B kinase subunit beta
  205. Fibroblast growth factor receptor 2 precursor
  206. Serine/threonine-protein kinase ATR
  207. Tyrosine-protein kinase JAK1
  208. X/potassium-transporting ATPase subunit beta-m
  209. Macrophage colony-stimulating factor 1 receptor precursor
  210. ATP synthase protein 8
  211. Calcium/calmodulin-dependent protein kinase kinase 1
  212. Serine/threonine-protein kinase 6
  213. Proto-oncogene serine/threonine-protein kinase mos
  214. RAC-beta serine/threonine-protein kinase
  215. Dual specificity tyrosine-phosphorylation-regulated kinase 2
  216. Serine/threonine-protein kinase VRK2
  217. DNA-dependent protein kinase catalytic subunit
  218. Ephrin type-A receptor 7 precursor
  219. Mitogen-activated protein kinase 13
  220. Tyrosine-protein kinase ABL2
  221. Serine/threonine-protein kinase ULK1
  222. Proto-oncogene tyrosine-protein kinase MER precursor
  223. Citron Rho-interacting kinase
  224. ATP synthase e chain, mitochondrial
  225. Serine/threonine-protein kinase Sgk2
  226. Serine/threonine-protein kinase Nek2
  227. ATP synthase gamma chain, mitochondrial precursor
  228. Serine/threonine-protein kinase MAK
  229. Ephrin type-A receptor 1 precursor
  230. Calcium/calmodulin-dependent protein kinase kinase 2
  231. Vacuolar ATP synthase subunit d 1
  232. Activated CDC42 kinase 1
  233. cAMP-dependent protein kinase, alpha-catalytic subunit
  234. Testis-specific serine/threonine-protein kinase 4
  235. Phosphatidylinositol-4-phosphate 5-kinase type-2 beta
  236. Alpha platelet-derived growth factor receptor precursor
  237. Proto-oncogene tyrosine-protein kinase LCK
  238. Tyrosine-protein kinase JAK3
  239. Cell division protein kinase 9
  240. Muscle, skeletal receptor tyrosine protein kinase precursor
  241. Fibroblast growth factor receptor 3 precursor
  242. RAC-gamma serine/threonine-protein kinase
  243. Dual specificity mitogen-activated protein kinase kinase 4
  244. Ephrin type-A receptor 3 precursor
  245. Tyrosine-protein kinase Tec
  246. Mitogen-activated protein kinase kinase kinase 10
  247. Protein kinase C beta type
  248. Non-receptor tyrosine-protein kinase TYK2
  249. Receptor tyrosine-protein kinase erbB-4 precursor
  250. Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase
  251. Galactokinase
  252. Calcium/calmodulin-dependent protein kinase type IV
  253. Glycogen synthase kinase-3 alpha
  254. Mitogen-activated protein kinase kinase kinase 12
  255. Sodium/potassium-transporting ATPase alpha-1 chain precursor
  256. Cell division protein kinase 7
  257. Proto-oncogene tyrosine-protein kinase FGR
  258. Mitogen-activated protein kinase kinase kinase kinase 2
  259. Calcium-transporting ATPase type 2C member 1
  260. Phosphorylase b kinase gamma catalytic chain, testis/liver isoform
  261. Cell division protein kinase 5
  262. Serine/threonine-protein kinase PRKY
  263. Cell division protein kinase 4
  264. Ceramide kinase
  265. Serine/threonine-protein kinase LATS2
  266. Activin receptor type 1B precursor
  267. 5-formyltetrahydrofolate cyclo-ligase
  268. Phosphatidylinositol 4-kinase alpha
  269. Sodium/potassium-transporting ATPase alpha-3 chain
  270. Myosin light chain kinase, smooth muscle
  271. Rhodopsin kinase precursor
  272. ATP synthase B chain, mitochondrial precursor
  273. Tyrosine-protein kinase BTK
  274. Serine/threonine-protein kinase 12
  275. Serine/threonine-protein kinase 16
  276. Vesicle-fusing ATPase
  277. Protein tyrosine kinase 2 beta
  278. Ribosomal protein S6 kinase beta-1
  279. Mitogen-activated protein kinase kinase kinase kinase 5
  280. Ephrin type-A receptor 4 precursor
  281. 3-phosphoinositide-dependent protein kinase 1
  282. STE20/SPS1-related proline-alanine-rich protein kinase
  283. Serine/threonine-protein kinase Nek7
  284. Casein kinase II subunit alpha
  285. Serine/threonine-protein kinase PLK2
  286. Beta platelet-derived growth factor receptor precursor
  287. Protein kinase C iota type
  288. Tyrosine-protein kinase BLK
  289. Serine/threonine-protein kinase tousled-like 2
  290. Cyclin-dependent kinase-like 1
  291. Ribosomal protein S6 kinase alpha-3
  292. Mitogen-activated protein kinase kinase kinase 4
  293. Tyrosine-protein kinase receptor Tie-1 precursor
  294. ATP synthase subunit alpha, mitochondrial precursor
  295. Microtubule-associated serine/threonine-protein kinase 2
  296. Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
  297. Probable phospholipid-transporting ATPase IIB
  298. Tyrosine-protein kinase RYK precursor
  299. Rho-associated protein kinase 1
  300. Epidermal growth factor receptor precursor
  301. Potassium-transporting ATPase alpha chain 1
  302. Integrin-linked protein kinase
  303. Bone morphogenetic protein receptor type-2 precursor
  304. Probable phospholipid-transporting ATPase IM
  305. Calcium/calmodulin-dependent protein kinase type II delta chain
  306. Serine/threonine-protein kinase D1
  307. Receptor tyrosine-protein kinase erbB-2 precursor
  308. Serine/threonine-protein kinase Chk1
  309. Casein kinase II subunit alpha'
  310. BR serine/threonine-protein kinase 1
  311. Tyrosine-protein kinase FRK
  312. Protein kinase C gamma type
  313. Proto-oncogene tyrosine-protein kinase ROS precursor
  314. Vacuolar ATP synthase 16 kDa proteolipid subunit
  315. Cell division cycle 2-like protein kinase 6
  316. Probable phospholipid-transporting ATPase IF
  317. Serine/threonine-protein kinase PCTAIRE-3
  318. Probable phospholipid-transporting ATPase IK
  319. Ribosomal protein S6 kinase alpha-5
  320. Serine/threonine-protein kinase Nek8
  321. Mitogen-activated protein kinase kinase kinase kinase 4
  322. Serine/threonine-protein kinase PRKX
  323. Serine/threonine-protein kinase LATS1
  324. Serine/threonine-protein kinase MARK2
  325. Phosphoglycerate kinase, testis specific
  326. Receptor-interacting serine/threonine-protein kinase 2
  327. ATP synthase D chain, mitochondrial
  328. Ephrin type-B receptor 3 precursor
  329. [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 3, mitochondrial precursor
  330. Tyrosine-protein kinase Srms
  331. Mast/stem cell growth factor receptor precursor
  332. Serine/threonine-protein kinase PLK1
  333. Tyrosine-protein kinase ZAP-70
  334. Mitogen-activated protein kinase 14
  335. Serine/threonine-protein kinase 17B
  336. Rho-associated protein kinase 2
  337. Transient receptor potential cation channel subfamily M member 7
  338. Insulin receptor precursor
  339. PITSLRE serine/threonine-protein kinase CDC2L1
  340. Anti-Muellerian hormone type-2 receptor precursor
  341. Serine/threonine-protein kinase DCAMKL2
  342. Proto-oncogene tyrosine-protein kinase receptor ret precursor
  343. Mitogen-activated protein kinase 6
  344. Serine/threonine-protein kinase 17A
  345. Serine/threonine-protein kinase N1
  346. ATP synthase f chain, mitochondrial
  347. Mitogen-activated protein kinase 10
  348. Sodium/potassium-transporting ATPase alpha-2 chain precursor
  349. Ephrin type-B receptor 2 precursor
  350. LIM domain kinase 1
  351. Serine/threonine-protein kinase H1
  352. Protein kinase C delta type
  353. Serine/threonine-protein kinase D3
  354. Protein kinase C theta type
  355. Protein kinase C eta type
  356. Bifunctional coenzyme A synthase
  357. 5'-AMP-activated protein kinase catalytic subunit alpha-1
  358. 5'-AMP-activated protein kinase catalytic subunit alpha-2
  359. Breakpoint cluster region protein
  360. Inhibitor of nuclear factor kappa-B kinase subunit alpha
  361. P2Y purinoceptor 12
  362. Poly(ADP-ribose) glycohydrolase ARH3
  363. Dihydroxyacetone kinase
  364. Uridine-cytidine kinase 2
  365. Copper-transporting ATPase 2
  366. Xylulose kinase
  367. Ectonucleoside triphosphate diphosphohydrolase 2
  368. MAP kinase-activated protein kinase 2
  369. Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2
  370. ATP synthase lipid-binding protein, mitochondrial precursor
  371. Sodium/potassium-transporting ATPase alpha-4 chain
  372. ATP synthase lipid-binding protein, mitochondrial precursor
  373. Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma
  374. CAD protein [Includes: Glutamine-dependent carbamoyl-phosphate synthase
  375. Phosphatidylinositol 4-kinase, catalytic, beta polypeptide
  376. Phosphatidylinositol 3-kinase catalytic subunit type 3
  377. Vacuolar ATP synthase subunit d 2
  378. Vacuolar ATP synthase subunit E 2
  379. Vacuolar ATP synthase subunit C 2
  380. Phosphatidylinositol-5-phosphate 4-kinase type-2 gamma
  381. Diacylglycerol kinase eta
  382. 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial precursor
  383. Sedoheptulokinase
  384. Serine/threonine-protein kinase D2
  385. cDNA FLJ78469, highly similar to Homo sapiens creatine kinase, brain
  386. cDNA FLJ78616, highly similar to Homo sapiens phosphoribosylglycinamide formyltransferase, phosphoribosylglycinamide synthetase, phosphoribosylaminoimidazole synthetase
  387. C1-tetrahydrofolate synthase
  388. Methylenetetrahydrofolate dehydrogenase
  389. Glutamine synthetase
  390. Glycerate kinase
  391. Choline kinase beta
  392. Inositol-tetrakisphosphate 1-kinase
  393. cDNA FLJ78307, highly similar to Homo sapiens NAD kinase
  394. Propionyl-CoA carboxylase alpha subunit
  395. Ribonucleoside-diphosphate reductase subunit M2 B
  396. LOC129607 protein
  397. Uridine/cytidine kinase-like 1
  398. Ectonucleoside triphosphate diphosphohydrolase 8
  399. Tau-tubulin kinase 1
  400. Serine/threonine-protein kinase OSR1
  401. Serine/threonine-protein kinase WNK1
  402. Leucine-rich repeat serine/threonine-protein kinase 1
  403. Serine/threonine-protein kinase MRCK gamma
  404. Serine/threonine-protein kinase PAK 1
  405. Eukaryotic translation initiation factor 2-alpha kinase 1
  406. Activin receptor type-1C precursor
  407. PITSLRE serine/threonine-protein kinase CDC2L2
  408. Peripheral plasma membrane protein CASK
  409. Myotonin-protein kinase
  410. Dual specificity tyrosine-phosphorylation-regulated kinase 3
  411. Dual specificity tyrosine-phosphorylation-regulated kinase 4
  412. Serine/threonine-protein kinase/endoribonuclease IRE1 precursor
  413. Serine/threonine-protein kinase/endoribonuclease IRE2 precursor
  414. Interleukin-1 receptor-associated kinase 1
  415. Interleukin-1 receptor-associated kinase 3
  416. Mitogen-activated protein kinase kinase kinase 11
  417. Mitogen-activated protein kinase kinase kinase 2
  418. Mitogen-activated protein kinase kinase kinase 5
  419. Mitogen-activated protein kinase kinase kinase 6
  420. Mitogen-activated protein kinase kinase kinase 9
  421. Microtubule-associated serine/threonine-protein kinase 3
  422. Mitogen-activated protein kinase kinase kinase MLT
  423. Dual specificity mitogen-activated protein kinase kinase 5
  424. Putative myosin light chain kinase 3
  425. Putative nucleoside diphosphate kinase
  426. Serine/threonine-protein kinase Nek11
  427. Serine/threonine-protein kinase Nek5
  428. NUAK family SNF1-like kinase 2
  429. Probable 7,8-dihydro-8-oxoguanine triphosphatase NUDT15
  430. Putative nucleoside diphosphate-linked moiety X motif 17, mitochondrial precursor
  431. Nucleoside diphosphate-linked moiety X motif 18
  432. Nucleoside diphosphate-linked moiety X motif 8, mitochondrial precursor
  433. Serine/threonine-protein kinase SRPK1
  434. Serine/threonine-protein kinase SRPK2
  435. Serine/threonine-protein kinase 32A
  436. Serine/threonine-protein kinase 32B
  437. Serine/threonine-protein kinase 32C
  438. Serine/threonine-protein kinase 36
  439. Dual specificity testis-specific protein kinase 1
  440. Serine/threonine-protein kinase WNK3
  441. Phosphoinositide 3-kinase regulatory subunit 4
  442. cDNA FLJ78442, highly similar to Homo sapiens phosphoglycerate kinase 1 (PGK1), mRNA (Phosphoglycerate kinase 1, isoform CRA_c)
  443. Thymidine kinase
  444. cDNA FLJ78347, highly similar to Homo sapiens adenylate kinase 2 (AK2), transcript variant AK2A, mRNA (Adenylate kinase 2, isoform CRA_d)
  445. cDNA FLJ76131, highly similar to Homo sapiens non-metastatic cells 7, protein expressed in (nucleoside-diphosphate kinase) (NME7), transcript variant 1, mRNA (Non-metastatic cells 7, protein expressed in (Nucleoside-diphosphate kinase), isoform CRA_a)
  446. Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
  447. cDNA FLJ78173, highly similar to Homo sapiens hexokinase 1 (HK1) mRNA
  448. Galactokinase 2 variant
  449. cDNA FLJ75059, highly similar to Homo sapiens phosphoribosylformylglycinamidine synthase (FGAR amidotransferase) (PFAS), mRNA
  450. ETNK2 protein (Ethanolamine kinase 2, isoform CRA_b) (Ethanolamine kinase 2)
  451. Putative uncharacterized protein TTL (Tubulin tyrosine ligase)
  452. Sphingosine kinase 1 (Sphingosine kinase 1, isoform CRA_c)
  453. 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)
  454. Diacylglycerol kinase, beta 90kDa (Diacylglycerol kinase, beta 90kDa, isoform CRA_b)
  455. Diacylglycerol kinase, theta 110kDa
  456. Diacylglycerol kinase, epsilon 64kDa (cDNA FLJ75840, highly similar to Homo sapiens diacylglycerol kinase, epsilon 64kDa (DGKE), mRNA)
  457. Calcium/calmodulin-dependent protein kinase ID (Calcium/calmodulin- dependent protein kinase ID, isoform CRA_b) (cDNA FLJ76987, highly similar to Homo sapiens calcium/calmodulin-dependent protein kinase ID (CAMK1D), transcript variant 1, mRNA)
  458. cDNA FLJ75193, highly similar to Homo sapiens calcium/calmodulin- dependent protein kinase II alpha-B subunit mRNA (Calcium/calmodulin- dependent protein kinase (CaM kinase) II alpha, isoform CRA_b)
  459. Calcium/calmodulin-dependent protein kinase (CaM kinase) II beta
  460. Calcium/calmodulin-dependent protein kinase isoform A (Fragment)
  461. cDNA FLJ75328, highly similar to Homo sapiens ATPase, Ca++ transporting, cardiac muscle, fast twitch1 (ATP2A1), transcript variant b, mRNA
  462. Putative uncharacterized protein DKFZp686I0955
  463. cDNA FLJ76965, highly similar to Homo sapiens phosphatidylinositol-4- phosphate 5-kinase, type I, beta (PIP5K1B), transcript variant 2, mRNA (Phosphatidylinositol-4-phosphate 5-kinase, type I, beta, isoform CRA_a)
  464. Putative uncharacterized protein FLJ10842 (Multiple substrate lipid kinase, isoform CRA_a)
  465. Phosphoinositide-3-kinase, catalytic, gamma polypeptide (Phosphoinositide-3-kinase, catalytic, gamma polypeptide, isoform CRA_a)
  466. Phosphoinositide-3-kinase, class 2, beta polypeptide (Phosphoinositide-3-kinase, class 2, beta polypeptide, isoform CRA_b)
  467. Inositol-pentakisphosphate 2-kinase
  468. Inositol hexaphosphate kinase 3 (Inositol hexaphosphate kinase 3, isoform CRA_a)
  469. Uncharacterized protein IHPK1
  470. EPH receptor A8
  471. Ephrin type-B receptor 6
  472. cDNA FLJ75121, highly similar to Homo sapiens fibroblast growth factor receptor 1 (fms-related tyrosine kinase 2, Pfeiffer syndrome) (FGFR1), transcript variant 2, mRNA
  473. Lemur tyrosine kinase 2 (Lemur tyrosine kinase 2, isoform CRA_c)
  474. Ephrin type-A receptor 10
  475. Met proto-oncogene (Hepatocyte growth factor receptor) (Met proto- oncogene (Hepatocyte growth factor receptor), isoform CRA_c)
  476. Tyrosine-protein kinase receptor (EC 2.7.10.1)
  477. Neurotrophic tyrosine kinase, receptor, type 3 (Neurotrophic tyrosine kinase, receptor, type 3, isoform CRA_e)
  478. ROR1 protein (Receptor tyrosine kinase-like orphan receptor 1, isoform CRA_b) (Receptor tyrosine kinase-like orphan receptor 1)
  479. AXL receptor tyrosine kinase
  480. cDNA FLJ75731, highly similar to Homo sapiens TEK tyrosine kinase, endothelial (venous malformations, multiple cutaneous and mucosal) (TEK), mRNA (TEK tyrosine kinase, endothelial (Venous malformations, multiple cutaneous and mucosal), isoform CRA_a)
  481. cDNA FLJ78579, highly similar to Homo sapiens c-src tyrosine kinase (CSK), mRNA
  482. V-abl Abelson murine leukemia viral oncogene homolog 1 (V-abl Abelson murine leukemia viral oncogene homolog 1, isoform CRA_b)
  483. LYN protein (Fragment)
  484. Spleen tyrosine kinase (Spleen tyrosine kinase, isoform CRA_b)
  485. Uncharacterized protein MAP4K1 (Mitogen-activated protein kinase kinase kinase kinase 1, isoform CRA_b)
  486. Leucine-rich repeat serine/threonine-protein kinase 2
  487. cDNA FLJ75471, highly similar to Homo sapiens U2AF homology motif (UHM) kinase 1 (UHMK1), mRNA (U2AF homology motif (UHM) kinase 1, isoform CRA_b)
  488. Myosin-IIIB
  489. CSNK1A1 protein (Fragment)
  490. Casein kinase I isoform delta
  491. Casein kinase I isoform epsilon
  492. Casein kinase I isoform gamma-3
  493. Putative uncharacterized protein (Fragment)
  494. Mixed lineage kinase domain-like protein
  495. Homeodomain interacting protein kinase 1
  496. AP2-associated protein kinase 1
  497. TRAF2 and NCK interacting kinase (TRAF2 and NCK interacting kinase, isoform CRA_g)
  498. PASK protein
  499. Testis-specific serine kinase 2 (HCG1641087)
  500. cDNA FLJ75495, highly similar to Homo sapiens serum/glucocorticoid regulated kinase family, member 3 (SGK3), transcript variant 1, mRNA (Serum/glucocorticoid regulated kinase family, member 3, isoform CRA_a)
  501. Receptor-interacting serine/threonine-protein kinase 5
  502. Cyclin G-associated kinase
  503. Serine/threonine-protein kinase ULK3
  504. SFRS protein kinase 3
  505. Homeodomain-interacting protein kinase 2
  506. Myosin light chain kinase family member 4
  507. Interleukin-1 receptor-associated kinase-like 2
  508. Serine/threonine-protein kinase SBK1
  509. LIM domain kinase 2 (LIM domain kinase 2, isoform CRA_b)
  510. Eukaryotic translation initiation factor 2-alpha kinase 4
  511. Misshapen/NIKs-related kinase isoform beta
  512. cDNA FLJ75088, highly similar to Homo sapiens p21 (CDKN1A)-activated kinase 2 (PAK2), mRNA
  513. cDNA FLJ78276, highly similar to Homo sapiens p21 (CDKN1A)-activated kinase 3 (PAK3), mRNA (P21 (CDKN1A)-activated kinase 3, isoform CRA_b)
  514. Interleukin-1 receptor-associated kinase 4 variant (Interleukin-1 receptor-associated kinase 4)
  515. Uncharacterized protein VRK3
  516. Serine/threonine-protein kinase TAO3
  517. Serine/threonine protein kinase MST4a (Mst3 and SOK1-related kinase, isoform CRA_b)
  518. Pim-1 oncogene (Pim-1 oncogene, isoform CRA_a)
  519. Putative uncharacterized protein DKFZp547K1617 (Casein kinase 1, gamma 1) (HCG2004507, isoform CRA_a)
  520. Protein kinase
  521. RING finger and WD repeat domain-containing protein 3
  522. Putative uncharacterized protein BMP2K (cDNA FLJ78410, highly similar to Homo sapiens BMP2 inducible kinase (BMP2K), transcript variant 2, mRNA)
  523. cDNA FLJ78089, highly similar to Homo sapiens eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2), mRNA
  524. cDNA FLJ75021, highly similar to Homo sapiens p21(CDKN1A)-activated kinase 6 (PAK6), mRNA (P21(CDKN1A)-activated kinase 6, isoform CRA_a)
  525. TAO kinase 1 (TAO kinase 1, isoform CRA_a)
  526. Uncharacterized protein RPS6KA1
  527. Uncharacterized protein RPS6KA2
  528. Uncharacterized protein WNK2
  529. V-raf murine sarcoma viral oncogene homolog B1
  530. NEK4 protein
  531. Aurora/Ipl1-related kinase 3 transcript variant 1
  532. Testis-specific serine kinase 3 (Testis-specific serine kinase 3, isoform CRA_b)
  533. Cell division cycle 7-related protein kinase
  534. Testis-specific serine kinase 1
  535. Serine/threonine kinase 24 (STE20 homolog, yeast) (Serine/threonine kinase 24 (STE20 homolog, yeast), isoform CRA_c)
  536. Microtubule-associated serine/threonine-protein kinase-like
  537. Serine/threonine-protein kinase H2
  538. MAP kinase interacting serine/threonine kinase 1 (MAP kinase interacting serine/threonine kinase 1, isoform CRA_d)
  539. Receptor-interacting serine/threonine-protein kinase 1
  540. U4/U6 small nuclear ribonucleoprotein Prp4
  541. TAOK2 protein (Fragment)
  542. Eukaryotic translation initiation factor 2-alpha kinase 3
  543. Serine/threonine-protein kinase ULK2
  544. STE20-like serine/threonine-protein kinase
  545. NUAK family, SNF1-like kinase, 1 (NUAK family, SNF1-like kinase, 1, isoform CRA_a) (cDNA FLJ77269, highly similar to Homo sapiens NUAK family, SNF1-like kinase, 1 (NUAK1), mRNA)
  546. cDNA FLJ75644, highly similar to Homo sapiens pyruvate dehydrogenase kinase, isoenzyme 2 (PDK2), mRNA (Pyruvate dehydrogenase kinase, isozyme 2, isoform CRA_a)
  547. Pyruvate dehydrogenase kinase, isoenzyme 4 (Pyruvate dehydrogenase kinase, isozyme 4, isoform CRA_a)
  548. Uncharacterized protein BCKDK (Branched chain ketoacid dehydrogenase kinase, isoform CRA_c)
  549. cDNA FLJ77336, highly similar to Homo sapiens serine/threonine kinase 3 (STE20 homolog, yeast) (STK3), mRNA (Serine/threonine kinase 3) (STE20 homolog, yeast)
  550. cDNA FLJ77586, highly similar to Homo sapiens Fas-activated serine/threonine kinase (FASTK), transcript variant 1, mRNA (Fas- activated serine/threonine kinase, isoform CRA_g)
  551. cDNA FLJ75314, highly similar to Homo sapiens TANK binding kinase TBK1 (TBK1) mRNA (TANK-binding kinase 1)
  552. Inhibitor of nuclear factor kappa-B kinase subunit epsilon
  553. Serine/threonine-protein kinase N3
  554. Uncharacterized protein PRKCZ
  555. G protein-coupled receptor kinase 7
  556. Polo-like kinase 3 (Drosophila)
  557. cDNA FLJ76907, highly similar to Homo sapiens cyclin-dependent kinase 2 (CDK2), transcript variant 1, mRNA (Cyclin-dependent kinase 2, isoform CRA_b)
  558. Cyclin-dependent kinase 6 (HCG19542)
  559. cDNA FLJ75758, highly similar to Homo sapiens serine/threonine kinase 25 (STE20 homolog, yeast) (STK25), mRNA (Serine/threonine kinase 25 (STE20 homolog, yeast), isoform CRA_a)
  560. Intestinal cell (MAK-like) kinase (Intestinal cell (MAK-like) kinase, isoform CRA_a)
  561. Cell cycle-related kinase
  562. Cyclin-dependent kinase-like 4
  563. Cyclin-dependent kinase-like 3
  564. cDNA FLJ75610, highly similar to Homo sapiens PCTAIRE protein kinase 1 (PCTK1), transcript variant 1, mRNA (PCTAIRE protein kinase 1, isoform CRA_c)
  565. PFTAIRE protein kinase 1 (PFTAIRE protein kinase 1, isoform CRA_c) (cDNA FLJ75582, highly similar to Homo sapiens PFTAIRE protein kinase 1 (PFTK1), mRNA)
  566. MAPK/MAK/MRK overlapping kinase
  567. cDNA FLJ77382, highly similar to Homo sapiens amyotrophic lateral sclerosis 2 (juvenile) chromosome region, candidate 7 (ALS2CR7), mRNA (Amyotrophic lateral sclerosis 2 (Juvenile) chromosome region, candidate 7, isoform CRA_a)
  568. Mitogen-activated protein kinase 15
  569. Extracellular signal-related kinase 1b
  570. Mitogen-activated protein kinase 4
  571. cDNA FLJ78064, highly similar to Human proto-oncogene protein (Mitogen-activated protein kinase kinase kinase 8, isoform CRA_a)
  572. Tau-tubulin kinase 2
  573. TGFBR1 protein
  574. Dual specificity tyrosine-phosphorylation-regulated kinase 1A
  575. Lymphokine-activated killer T-cell-originated protein kinase
  576. Mitogen-activated protein kinase kinase 1 (Mitogen-activated protein kinase kinase 1, isoform CRA_a) (cDNA FLJ76051, highly similar to Homo sapiens mitogen-activated protein kinase kinase 1 (MAP2K1), mRNA)
  577. Dual specificity mitogen-activated protein kinase kinase 2
  578. cDNA FLJ75671, highly similar to Homo sapiens mitogen-activated protein kinase kinase 6 (MAP2K6), transcript variant 1, mRNA (Mitogen- activated protein kinase kinase 6, isoform CRA_b)
  579. ATP8A1 protein (ATPase, aminophospholipid transporter (APLT), Class I, type 8A, member 1, isoform CRA_a)
  580. CDNA FLJ45330 fis, clone BRHIP3007195, highly similar to Potential phospholipid-transporting ATPase IB (EC 3.6.3.13)
  581. ATPase, class I, type 8B, member 2
  582. 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)
  583. cDNA FLJ76372, highly similar to Homo sapiens ATP synthase, H+ transporting, mitochondrial F0 complex, subunit G, mRNA (HCG2043599, isoform CRA_b)
  584. V-type proton ATPase subunit e 2
  585. 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)
  586. ATPase, H+ transporting, lysosomal V0 subunit a isoform 4 (ATPase, H+ transporting, lysosomal V0 subunit a4, isoform CRA_a)
  587. Uncharacterized protein ATP6V1E1
  588. Uncharacterized protein ATP6V0B (ATPase, H+ transporting, lysosomal 21kDa, V0 subunit b, isoform CRA_b)
  589. Vacuolar-type H(+)-ATPase
  590. 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
  591. ATPase, H+ transporting, lysosomal 14kDa, V1 subunit F (ATPase, H+ transporting, lysosomal 14kDa, V1 subunit F, isoform CRA_a)
  592. cDNA FLJ77987, highly similar to Homo sapiens katanin p60 subunit A- like 1, mRNA (Katanin p60 subunit A-like 1, isoform CRA_a)
  593. cDNA, FLJ94180, Homo sapiens adenylate kinase 3 (AK3), mRNA (AK3L2 protein)
  594. cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
  595. cDNA FLJ43342 fis, clone NT2RI3007978, highly similar to CTP synthase 2 (EC 6.3.4.2)
  596. cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
  597. cDNA, FLJ93716, Homo sapiens glycerol kinase (GK), mRNA
  598. Putative uncharacterized protein
  599. Pantothenate kinase 2 (Hallervorden-Spatz syndrome) (HCG39342, isoform CRA_c)
  600. cDNA, FLJ96772, Homo sapiens mevalonate kinase (mevalonic aciduria) (MVK), mRNA (Mevalonate kinase (Mevalonic aciduria), isoform CRA_c)
  601. Calcium/calmodulin-dependent protein kinase type 1 (Calcium/calmodulin-dependent protein kinase I, isoform CRA_a) (cDNA, FLJ95825, Homo sapiens calcium/calmodulin-dependent protein kinase I (CAMK1),mRNA)
  602. ATPase, Ca++ transporting, plasma membrane 4 (ATPase, Ca++ transporting, plasma membrane 4, isoform CRA_a)
  603. Phosphatidylinositol-4-phosphate 5-kinase type-2 alpha variant 1 (Phosphatidylinositol-4-phosphate 5-kinase, type II, alpha, isoform CRA_a) (Phosphatidylinositol-4-phosphate 5-kinase type-2 alpha variant 2)
  604. Phosphoinositide-3-kinase, class 2, alpha polypeptide
  605. cDNA FLJ13983 fis, clone Y79AA1001827, highly similar to Inositol hexakisphosphate kinase 2 (EC 2.7.4.21)
  606. Tyrosine-protein kinase receptor
  607. cDNA FLJ35246 fis, clone PROST2003324, highly similar to Ephrin type-A receptor 6 (EC 2.7.10.1)
  608. cDNA, FLJ96234, highly similar to Homo sapiens fer (fps/fes related) tyrosine kinase (phosphoprotein NCP94) (FER), mRNA (Fer (Fps/fes related) tyrosine kinase (Phosphoprotein NCP94), isoform CRA_b)
  609. cDNA, FLJ92916, Homo sapiens feline sarcoma oncogene (FES), mRNA (Feline sarcoma oncogene, isoform CRA_b)
  610. Protein-tyrosine kinase fyn isoform a (FYN oncogene related to SRC, FGR, YES, isoform CRA_a)
  611. cDNA, FLJ93288, Homo sapiens IL2-inducible T-cell kinase (ITK), mRNA (IL2-inducible T-cell kinase)
  612. cDNA FLJ30833 fis, clone FEBRA2002027, highly similar to Megakaryocyte-associated tyrosine-protein kinase (EC 2.7.10.2)
  613. cDNA, FLJ94543 (Serine/threonine/tyrosine kinase 1)
  614. cDNA FLJ39183 fis, clone OCBBF2004273, highly similar to TP53-regulating kinase (EC 2.7.11.1)
  615. cDNA, FLJ95588, Homo sapiens serine/threonine kinase 35 (STK35), mRNA (Serine/threonine kinase 35)
  616. Casein kinase 1 isoform gamma-2 (Casein kinase 1, gamma 2, isoform CRA_e)
  617. Casein kinase 2, beta polypeptide (Casein kinase 2, beta polypeptide, isoform CRA_b) (cDNA, FLJ92126, Homo sapiens casein kinase 2, beta polypeptide (CSNK2B), mRNA)
  618. V-akt murine thymoma viral oncogene homolog 1 (V-akt murine thymoma viral oncogene homolog 1, isoform CRA_a)
  619. cDNA, FLJ93745, Homo sapiens ribosomal protein S6 kinase, 90kDa, polypeptide 6(RPS6KA6), mRNA (Ribosomal protein S6 kinase, 90kDa, polypeptide 6)
  620. Myosin IIIA
  621. cDNA, FLJ95149, highly similar to Homo sapiens SNF-1 related kinase (SNRK), mRNA (SNF related kinase, isoform CRA_a)
  622. cDNA, FLJ79469, highly similar to Serine/threonine-protein kinase PAK 7 (EC2.7.11.1)
  623. Ribosomal protein S6 kinase, 70kDa, polypeptide 2 (Ribosomal protein S6 kinase, 70kDa, polypeptide 2, isoform CRA_c)
  624. WNK lysine deficient protein kinase 4 (WNK lysine deficient protein kinase 4, isoform CRA_a)
  625. Mitogen-activated protein kinase-activated protein kinase 3
  626. cDNA, FLJ95270, Homo sapiens RIO kinase 1 (yeast) (RIOK1), transcript variant 1,mRNA (RIO kinase 1) (Yeast)
  627. Testis-specific serine kinase 6, isoform CRA_a
  628. cDNA FLJ16306 fis, clone PUAEN2003954, highly similar to MAP kinase-activated protein kinase 5 (EC 2.7.11.1)
  629. cDNA FLJ32730 fis, clone TESTI2001099, highly similar to Serine/threonine-protein kinase RIO3 (EC 2.7.11.1)
  630. cDNA FLJ33460 fis, clone BRAMY2000653, highly similar to Serine/threonine-protein kinase tousled-like 1 (EC 2.7.11.1)
  631. cDNA, FLJ93099, Homo sapiens pyruvate dehydrogenase kinase, isoenzyme 1 (PDK1), nuclear gene encoding mitochondrial protein, mRNA (Pyruvate dehydrogenase kinase, isozyme 1, isoform CRA_a)
  632. cDNA, FLJ96240, Homo sapiens serine/threonine kinase 4 (STK4), mRNA (Serine/threonine kinase 4, isoform CRA_a)
  633. cDNA FLJ39535 fis, clone PUAEN2005502, highly similar to Goodpasture antigen-binding protein (EC 2.7.11.9)
  634. cDNA, FLJ95757, Homo sapiens serine/threonine kinase 11 (Peutz-Jeghers syndrome)(STK11), mRNA (Serine/threonine kinase 11, isoform CRA_c)
  635. Putative uncharacterized protein
  636. Protein kinase C alpha type (Protein kinase C, alpha)
  637. Protein kinase C, epsilon (Protein kinase C, epsilon, isoform CRA_b)
  638. Adrenergic, beta, receptor kinase 1
  639. cDNA, FLJ96208, highly similar to Homo sapiens PCTAIRE protein kinase 2 (PCTK2), mRNA (PCTAIRE protein kinase 2, isoform CRA_a)
  640. Cyclin-dependent kinase-like 2 (CDC2-related kinase), isoform CRA_a
  641. Mitogen-activated protein kinase 8 isoform JNK1 alpha1 (Mitogen-activated protein kinase 8, isoform CRA_c)
  642. Mitogen-activated protein kinase 11 (Mitogen-activated protein kinase 11, isoform CRA_a)
  643. Mitogen-activated protein kinase 9 isoform JNK2 gamma
  644. cDNA, FLJ96888, Homo sapiens mitogen-activated protein kinase kinase kinase 7(MAP3K7), transcript variant A, mRNA (Mitogen-activated protein kinase kinase kinase 7, isoform CRA_a)
  645. cDNA, FLJ93116, Homo sapiens mitogen-activated protein kinase kinase kinase 13 (MAP3K13), mRNA (Mitogen-activated protein kinase kinase kinase 13, isoform CRA_a)
  646. cDNA, FLJ94217, Homo sapiens bone morphogenetic protein receptor, type IB (BMPR1B),mRNA (Bone morphogenetic protein receptor, type IB)
  647. cDNA FLJ53920, highly similar to TGF-beta receptor type-2 (Transforming growth factor, beta receptor II (70/80kDa), isoform CRA_c)
  648. cDNA, FLJ94821, Homo sapiens activin A receptor, type II (ACVR2), mRNA (Activin A receptor, type IIA, isoform CRA_a)
  649. cDNA FLJ14667 fis, clone NT2RP2003164, highly similar to Dual specificity testis-specific protein kinase 2 (EC 2.7.12.1)
  650. CDC-like kinase 2
  651. cDNA FLJ34373 fis, clone FEBRA2017333, highly similar to Dual specificity protein kinase CLK3 (EC 2.7.12.1)
  652. cDNA FLJ36519 fis, clone TRACH2002092, highly similar to Dual specificity mitogen-activated proteinkinase kinase 3 (EC 2.7.12.2)
  653. cDNA, FLJ94535, Homo sapiens mitogen-activated protein kinase kinase 7 (MAP2K7),transcript variant B, mRNA (Mitogen-activated protein kinase kinase 7, isoform CRA_c)
  654. ATPase, Cu++ transporting, alpha polypeptide (Menkes syndrome) (ATPase, Cu++ transporting, alpha polypeptide (Menkes syndrome), isoform CRA_a)
  655. ATPase, H+/K+ exchanging, beta polypeptide (ATPase, H+/K+ exchanging, beta polypeptide, isoform CRA_b)
  656. 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)
  657. cDNA FLJ12283 fis, clone MAMMA1001754, highly similar to Vacuolar ATP synthase subunit H (EC 3.6.3.14)
  658. 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)
  659. 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)
  660. Putative uncharacterized protein
  661. 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)
  662. Poly(ADP-ribose) glycohydrolase
  663. [Protein ADP-ribosylarginine] hydrolase
  664. Nucleoside diphosphate kinase
Enzyme 1 [top]
Enzyme 1 ID 5235
Enzyme 1 Name Deoxycytidine kinase
Enzyme 1 Synonyms
  1. dCK
Enzyme 1 Gene Name DCK
Enzyme 1 Protein Sequence >Deoxycytidine kinase 
MATPPKRSCPSFSASSEGTRIKKISIEGNIAAGKSTFVNILKQLCEDWEVVPEPVARWCN
VQSTQDEFEELTMSQKNGGNVLQMMYEKPERWSFTFQTYACLSRIRAQLASLNGKLKDAE
KPVLFFERSVYSDRYIFASNLYESECMNETEWTIYQDWHDWMNNQFGQSLELDGIIYLQA
TPETCLHRIYLRGRNEEQGIPLEYLEKLHYKHESWLLHRTLKTNFDYLQEVPILTLDVNE
DFKDKYESLVEKVKEFLSTL
Enzyme 1 Number of Residues 260
Enzyme 1 Molecular Weight 30519
Enzyme 1 Theoretical pI 4.88
Enzyme 1 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
—
Enzyme 1 General Function Nucleotide transport and metabolism
Enzyme 1 Specific Function Required for the phosphorylation of several deoxyribonucleosides and certain nucleoside analogs widely employed as antiviral and chemotherapeutic agents
Enzyme 1 Pathways
Enzyme 1 Reactions
  • NTP + deoxycytidine = NDP + dCMP
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 181510 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P27707 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name DCK_HUMAN Link Image
Enzyme 1 PDB ID 1P62 Link Image
Enzyme 1 PDB File Show
Enzyme 1 3D Structure
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >783 bp 
ATGGCCACCCCGCCCAAGAGAAGCTGCCCGTCTTTCTCAGCCAGCTCTGAGGGGACCCGC
ATCAAGAAAATCTCCATCGAAGGGAACATCGCTGCAGGGAAGTCAACATTTGTGAATATC
CTTAAACAATTGTGTGAAGATTGGGAAGTGGTTCCTGAACCTGTTGCCAGATGGTGCAAT
GTTCAAAGTACTCAAGATGAATTTGAGGAACTTACAATGTCTCAGAAAAATGGTGGGAAT
GTTCTTCAGATGATGTATGAGAAACCTGAACGATGGTCTTTTACCTTCCAAACATATGCC
TGTCTCAGTCGAATAAGAGCTCAGCTTGCCTCTCTGAATGGCAAGCTCAAAGATGCAGAG
AAACCTGTATTATTTTTTGAACGATCTGTGTATAGTGACAGGTATATTTTTGCATCTAAT
TTGTATGAATCTGAATGCATGAATGAGACAGAGTGGACAATTTATCAAGACTGGCATGAC
TGGATGAATAACCAATTTGGCCAAAGCCTTGAATTGGATGGAATCATTTATCTTCAAGCC
ACTCCAGAGACATGCTTACATAGAATATATTTACGGGGAAGAAATGAAGAGCAAGGCATT
CCTCTTGAATATTTAGAGAAGCTTCATTATAAACATGAAAGCTGGCTCCTGCATAGGACA
CTGAAAACCAACTTCGATTATCTTCAAGAGGTGCCTATCTTAACACTGGATGTTAATGAA
GACTTTAAAGACAAATATGAAAGTCTGGTTGAAAAGGTCAAAGAGTTTTTGAGTACTTTG
TGA
Enzyme 1 GenBank Gene ID M60527 Link Image
Enzyme 1 GeneCard ID DCK Link Image
Enzyme 1 GenAtlas ID DCK Link Image
Enzyme 1 HGNC ID HGNC:2704 Link Image
Enzyme 1 Chromosome Location 4
Enzyme 1 Locus 4q13.3-q21.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Chottiner EG, Shewach DS, Datta NS, Ashcraft E, Gribbin D, Ginsburg D, Fox IH, Mitchell BS: Cloning and expression of human deoxycytidine kinase cDNA. Proc Natl Acad Sci U S A. 1991 Feb 15;88(4):1531-5. [PubMed Link Image]
  2. Eriksson S, Cederlund E, Bergman T, Jornvall H, Bohman C: Characterization of human deoxycytidine kinase. Correlation with cDNA sequences. FEBS Lett. 1991 Mar 25;280(2):363-6. [PubMed Link Image]
  3. Johansson M, Brismar S, Karlsson A: Human deoxycytidine kinase is located in the cell nucleus. Proc Natl Acad Sci U S A. 1997 Oct 28;94(22):11941-5. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5239
Enzyme 2 Name ATP-citrate synthase
Enzyme 2 Synonyms
  1. ATP-citrate
  2. pro-S--lyase
  3. Citrate cleavage enzyme
Enzyme 2 Gene Name ACLY
Enzyme 2 Protein Sequence >ATP-citrate synthase 
MSAKAISEQTGKELLYKFICTTSAIQNRFKYARVTPDTDWARLLQDHPWLLSQNLVVKPD
QLIKRRGKLGLVGVNLTLDGVKSWLKPRLGQEATVGKATGFLKNFLIEPFVPHSQAEEFY
VCIYATREGDYVLFHHEGGVDVGDVDAKAQKLLVGVDEKLNPEDIKKHLLVHAPEDKKEI
LASFISGLFNFYEDLYFTYLEINPLVVTKDGVYVLDLAAKVDATADYICKVKWGDIEFPP
PFGREAYPEEAYIADLDAKSGASLKLTLLNPKGRIWTMVAGGGASVVYSDTICDLGGVNE
LANYGEYSGAPSEQQTYDYAKTILSLMTREKHPDGKILIIGGSIANFTNVAATFKGIVRA
IRDYQGPLKEHEVTIFVRRGGPNYQEGLRVMGEVGKTTGIPIHVFGTETHMTAIVGMALG
HRPIPNQPPTAAHTANFLLNASGSTSTPAPSRTASFSESRADEVAPAKKAKPAMPQDSVP
SPRSLQGKSTTLFSRHTKAIVWGMQTRAVQGMLDFDYVCSRDEPSVAAMVYPFTGDHKQK
FYWGHKEILIPVFKNMADAMRKHPEVDVLINFASLRSAYDSTMETMNYAQIRTIAIIAEG
IPEALTRKLIKKADQKGVTIIGPATVGGIKPGCFKIGNTGGMLDNILASKLYRPGSVAYV
SRSGGMSNELNNIISRTTDGVYEGVAIGGDRYPGSTFMDHVLRYQDTPGVKMIVVLGEIG
GTEEYKICRGIKEGRLTKPIVCWCIGTCATMFSSEVQFGHAGACANQASETAVAKNQALK
EAGVFVPRSFDELGEIIQSVYEDLVANGVIVPAQEVPPPTVPMDYSWARELGLIRKPASF
MTSICDERGQELIYAGMPITEVFKEEMGIGGVLGLLWFQKRLPKYSCQFIEMCLMVTADH
GPAVSGAHNTIICARAGKDLVSSLTSGLLTIGDRFGGALDAAAKMFSKAFDSGIIPMEFV
NKMKKEGKLIMGIGHRVKSINNPDMRVQILKDYVRQHFPATPLLDYALEVEKITTSKKPN
LILNVDGLIGVAFVDMLRNCGSFTREEADEYIDIGALNGIFVLGRSMGFIGHYLDQKRLK
QGLYRHPWDDISYVLPEHMSM
Enzyme 2 Number of Residues 1101
Enzyme 2 Molecular Weight 120841
Enzyme 2 Theoretical pI 7.34
Enzyme 2 GO Classification
Function
  • catalytic activity
Process
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Energy production and conversion
Enzyme 2 Specific Function ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 28935 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P53396 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ACLY_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >3318 bp 
ATGTCGGCCAAGGCAATTTCAGAGCAGACGGGCAAAGAACTCCTTTACAAGTTCATCTGT
ACCACCTCAGCCATCCAGAATCGGTTCAAGTATGCTCGGGTCACTCCTGACACAGACTGG
GCCCGCTTGCTGCAGGACCACCCCTGGCTGCTCAGCCAGAACTTGGTAGTCAAGCCAGAC
CAGCTGATCAAACGTCGTGGAAAACTTGGTCTCGTTGGGGTCGACCTCACTCTGGATGGG
GTCAAGTCCTGGCTGAAGCCACGGCTGGGACAGGAAGCCACAGTTGGCAAGGCCACAGGC
TTCCTCAAGAACTTTCTGATCGAGCCCTTCGCCCCCCACAGTCAGGCTGAGGAGTTCTAT
GTCTGCATCTATGCCACCCGAGAAGGGGACTACGTCCTGTTCCACCACGAGGGGGGTGTG
GACGTGGGTGATGTGGACGCCAAGGCCCAGAAGCTGCTTGTTGGCGTGGATGAGAAACTG
AATCCTGAGGACATCAAAAAACACCTGTTGGTCCACGCCCCTGACGACAAGAAAGAAATT
CTGGCCAGTTTTATCTCCGGCCTCTTCAATTTCTACGAGGACTTGTACTTCACCTACCTC
GAGATCAATCCCCTTGTAGTGACCAAAGATGGAGTCTATGTCCTTGACTTGGCGGCCAAG
GTGGACGCCACTGCCGACTACATCTGCAAAGTGAAGTGGGGTGACATCGAGTTCCCTCCC
CCCTTCGGGCGGGTGGCATATCCAGAGGAAGCCTACATTGCAGACCTCGATGCCAAAAGT
GGGGCAAGCCTGAAGCTGACCTTGCTGAACCCCAAAGGGAGGATCTGGACCATGGTGGCC
GGGGGTGGCGCCTCTGTCGTGTACAGCGATACCATCTGTGATCTAGGGGGTGTCAACGAG
CTGGCAAACTATGGGGAGTACTCAGGCGCCCCCAGCGAGCAGCAGACCTATGACTATGCC
AAGACTATCCTCTCCCTCATGACCCGAGAGAAGCACCCAGATGGCAAGATCCTCATCATT
GGAGGCAGCATCGCAAACTTCACCAACGTGGCTGCCACGTTCAAGGGCATCGTGAGAGCA
ATTCGAGATTACCAGGGCCCCCTGAAGGAGCACGAAGTCACAATCTTTGTCCGAAGAGGT
GGCCCCAACTATCAGGAGGGCTTACGGGTGATGGGAGAAGTCGGGAAGACCACTGGGATC
CCCATCCATGTCTTTGGCACAGAGACTCACATGACGGCCATTGTGGGCATGGCCTGGGCA
CCGGCCATCCCCAACCAGCCACCCACAGCGGCCCACACTGCAAACTTTCTCCTCAACGCC
CAGCGGGAGACATCGACTCCAGCCCCCAGCAGGACAGCATCTTTTTATGAGTCCATGGTC
GATGAGGTCAGGGCCGATGAGGTGGCGCCTGCAAAGAAGGCCAAGCCTGCCATGCCACAA
GATTCAGTCCCAAGTCCAAGATCCCTGCAAGGAAAGAGCACCACCCTCTTCAGCCGCCAC
ACCAAGGCCATTGTGTGGGGCATGCAGACCCGGGCCGTGCAAGGCATGCTGGACTTTGAC
TATGTCTGCTCCCGAGACGAGCCCTCAGTGGCTGCCATGGTCTATCCTTTCACTGGGGAC
CACAAGCAGAAGTTTTACTGGGGGCACAAAGAGATCCTGATCCCTGTCTTCAAGAACATG
GCTGATGCCATGAGGAAGCACCCGGAGGTAGATGTGCTCATCAACTTTGCCTCTCTCCGC
TCTGCCTATGACAGCACCATGGAGACCATGAACTATGCCCAGATCCGGACCATCGCCATC
ATAGCTGAAGGCATCCCTGAGGCCCTCACGAGAAAGCTGATCAAGAAGGCGGACCAGAAG
GGAGTGACCATCATCGGACCTGCCACTGTTGGAGGCATCAAGCCTGGGTGCTTTAAGATT
GGCAACACAGGTGGGATGCTGGACAACATCCTGGCCTCCAAACTGTACCCCCAGGCAGCT
GTGGCCTATGTCTCACGTTCCGGAGGCATGTCCAACGAGCTCAACAATATCATCTCTCGG
ACCACGGATGGCGTCTATGAGGGCGTGGCCATTGGTGGGGACAGGTACCCGGGCTCCACA
TTCATGGATCATGTGTTACGCTATCAGGACACTCCAGGAGTCAAAATGATTGTGGTTCTT
GGAGAGATTGGGGGCACTGAGGAATATAAGATTTCCCGGGGCATCAAGGAGGGCCGCCTC
ACTAAGCCCATCGTCTGCTGGTGCATCGGGACGTGTGCCACCATGTTCTCCTCTGAGGTC
CAGTTTGGCCATGCTGGAGCTTGTGCCAACCAGGCTTCTGAAACTGCAGTAGCCAAGAAC
CAGGCTTTGAAGGAAGCAGGAGTGTTTGTGCCCCGGAGCTTTGATGAGCTTGGAGAGATC
ATCCAGTCTGTATACGAAGATCTCGTGGCCAATGGAGTCATTGTACCTGCCCAGGAGGTG
CCGCCCCCAACCGTGCCCATGGACTACTCCTGGGCCAGGGAGCTTGGTTTGATCCGCAAA
CCTGCCTCGTTCATGACCAGCATCTGCGATGAGCGAGGACAGGAGCTCATCTACGCGGGC
ATGCCCATCACTGAGGTCTTCAAGGAAGAGATGGGCATTGGCGGGGCCCTCGGCCTCCTC
TGGTTCCAGAAAAGGTTGCCTAAGTACTCTTGCCAGTTCATTGAGATGTGTCTGATGGTG
ACAGCTGATCACGGGCCAGCCGTCTCTGGAGCCCACAACACCATCATTTGTGCGCGCACC
GCGGTGGAGCTGGTCTCCAGCCTCACCTCGGGGCTGCTCACCATCGGGGATCGGTTTGGG
GGTGCCTTGGATGCAGCAGCCAAGATGTTCAGTAAAGCCTTTGACAGTGGCATTATCCCC
ATGGAGTTTGTGAACAAGATGAAGAAGGAAGGGAAGCTGATCATGGGCATTGGTCACCGA
GTGAAGTCGATAAACAACCCAGACATGCGAGTGCAGATCCTCAAAGATTACGTCAGGCAG
CACTTCCCTGCCACTCCTCTGCTCGATTATGCACTGGAAGTAGAGAAGATTACCACCTCG
AAGAAGCCAAATCTTATCCTGAATGTAGATGGTCTCATCGGAGTCGCATTTGTAGACATG
CTTAGAAACTGTGGGTCCTTTACTCGGGAGGAAGCTGATGAATATATTGACATTGGAGCC
CTCAATGGCATCTTTGTGCTGGGAAGGAGTATGGGGTTCATTGGACACTATCTTGATCAG
AAGAGGCTGAAGCAGGGGCTGTATCGTCATCCGTGGGATGATATTTCATATGTTCTTCCG
GAACACATGAGCATGTAA
Enzyme 2 GenBank Gene ID X64330 Link Image
Enzyme 2 GeneCard ID ACLY Link Image
Enzyme 2 GenAtlas ID ACLY Link Image
Enzyme 2 HGNC ID HGNC:115 Link Image
Enzyme 2 Chromosome Location 17
Enzyme 2 Locus 17q12-q21
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Elshourbagy NA, Near JC, Kmetz PJ, Wells TN, Groot PH, Saxty BA, Hughes SA, Franklin M, Gloger IS: Cloning and expression of a human ATP-citrate lyase cDNA. Eur J Biochem. 1992 Mar 1;204(2):491-9. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5247
Enzyme 3 Name Acetyl-CoA carboxylase 2
Enzyme 3 Synonyms
  1. ACC-beta[Includes: Biotin carboxylase
Enzyme 3 Gene Name ACACB
Enzyme 3 Protein Sequence >Acetyl-CoA carboxylase 2 
MVLLLCLSCLIFSCLTFSWLKIWGKMTDSKPITKSKSEANLIPSQEPFPASDNSGETPQR
NGEGHTLPKTPSQAEPASHKGPKDAGRRRNSLPPSHQKPPRNPLSSSDAAPSPELQANGT
GTQGLEATDTNGLSSSARPQGQQAGSPSKEDKKQANIKRQLMTNFILGSFDDYSSDEDSV
AGSSRESTRKGSRASLGALSLEAYLTTGEAETRVPTMRPSMSGLHLVKRGREHKKLDLHR
DFTVASPAEFVTRFGGDRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVT
PEDLKANAEYIKMADHYVPVPGGPNNNNYANVELIVDIAKRIPVQAVWAGWGHASENPKL
PELLCKNGVAFLGPPSEAMWALGDKIASTVVAQTLQVPTLPWSGSGLTVEWTEDDLQQGK
RISVPEDVYDKGCVKDVDEGLEAAERIGFPLMIKASEGGGGKGIRKAESAEDFPILFRQV
QSEIPGSPIFLMKLAQHARHLEVQILADQYGNAVSLFGRDCSIQRRHQKIVEEAPATIAP
LAIFEFMEQCAIRLAKTVGYVSAGTVEYLYSQDGSFHFLELNPRLQVEHPCTEMIADVNL
PAAQLQIAMGVPLHRLKDIRLLYGESPWGVTPISFETPSNPPLARGHVIAARITSENPDE
GFKPSSGTVQELNFRSSKNVWGYFSVAATGGLHEFADSQFGHCFSWGENREEAISNMVVA
LKELSIRGDFRTTVEYLINLLETESFQNNDIDTGWLDYLIAEKVQAEKPDIMLGVVCGAL
NVADAMFRTCMTDFLHSLERGQVLPADSLLNLVDVELIYGGVKYILKVARQSLTMFVLIM
NGCHIEIDAHRLNDGGLLLSYNGNSYTTYMKEEVDSYRITIGNKTCVFEKENDPTVLRSP
SAGKLTQYTVEDGGHVEAGSSYAEMEVMKMIMTLNVQERGRVKYIKRPGAVLEAGCVVAR
LELDDPSKVHPAEPFTGELPAQQTLPILGEKLHQVFHSVLENLTNVMSGFCLPEPVFSIK
LKEWVQKLMMTLRHPSLPLLELQEIMTSVAGRIPAPVEKSVRRVMAQYASNITSVLCQFP
SQQIATILDCHAATLQRKADREVFFINTQSIVQLVQRYRSGIRGYMKTVVLDLLRRYLRV
EHHFQQAHYDKCVINLREQFKPDMSQVLDCIFSHAQVAKKNQLVIMLIDELCGPDPSLSD
ELISILNELTQLSKSEHCKVALRARQILIASHLPSYELRHNQVESIFLSAIDMYGHQFCP
ENLKKLILSETTIFDVLPTFFYHANKVVCMASLEVYVRRGYIAYELNSLQHRQLPDGTCV
VEFQFMLPSSHPNRMTVPISITNPDLLRHSTELFMDSGFSPLCQRMGAMVAFRRFEDFTR
NFDEVISCFANVPKDTPLFSEARTSLYSEDDCKSLREEPIHILNVSIQCADHLEDEALVP
ILRTFVQSKKNILVDYGLRRITFLIAQEKEFPKFFTFRARDEFAEDRIYRHLEPALAFQL
ELNRMRNFDLTAVPCANHKMHLYLGAAKVKEGVEVTDHRFFIRAIIRHSDLITKEASFEY
LQNEGERLLLEAMDELEVAFNNTSVRTDCNHIFLNFVPTVIMDPFKIEESVRYMVMRYGS
RLWKLRVLQAEVKINIRQTTTGSAVPIRLFITNESGYYLDISLYKEVTDSRSGNIMFHSF
GNKQGPQHGMLINTPYVTKDLLQAKRFQAQTLGTTYIYDFPEMFRQALFKLWGSPDKYPK
DILTYTELVLDSQGQLVEMNRLPGGNEVGMVAFKMRFKTQEYPEGRDVIVIGNDITFRIG
SFGPGEDLLYLRASEMARAEGIPKIYVAANSGARIGMAEEIKHMFHVAWVDPEDPHKGFK
YLYLTPQDYTRISSLNSVHCKHIEEGGESRYMITDIIGKDDGLGVENLRGSGMIAGESSL
AYEEIVTISLVTCRAIGIGAYLVRLGQRVIQVENSHIILTGASALNKVLGREVYTSNNQL
GGVQIMHYNGVSHITVPDDFEGVYTILEWLSYMPKDNHSPVPIITPTDPIDREIEFLPSR
APYDPRWMLAGRPHPTLKGTWQSGFFDHGSFKEIMAPWAQTVVTGRARLGGIPVGVIAVE
TRTVEVAVPADPANLDSEAKIIQQAGQVWFPDSAYKTAQAIKDFNREKLPLMIFANWRGF
SGGMKDMYDQVLKFGAYIVDGLRQYKQPILIYIPPYAELRGGSWVVIDATINPLCIEMYA
DKESRGGVLEPEGTVEIKFRKKDLIKSMRRIDPAYKKLMEQLGEPDLSDKDRKDLEGRLK
AREDLLLPIYHQVAVQFADFHDTPGRMLEKGVISDILEWKTARTFLYWRLRRLLLEDQVK
QEILQASGELSHVHIQSMLRRWFVETEGAVKAYLWDNNQVVVQWLEQHWQAGDGPRSTIR
ENITYLKHDSVLKTIRGLVEENPEVAVDCVIYLSQHISPAERAQVVHLLSTMDSPAST
Enzyme 3 Number of Residues 2458
Enzyme 3 Molecular Weight 276558
Enzyme 3 Theoretical pI 6.46
Enzyme 3 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ligase activity
  • nucleotide binding
  • purine nucleotide binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Lipid transport and metabolism
Enzyme 3 Specific Function ACC-beta may be involved in the provision of malonyl-CoA or in the regulation of fatty acid oxidation, rather than fatty acid biosynthesis. Carries out three functions:biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-24
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 2138330 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O00763 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name COA2_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >7452 bp 
ATGGTCTTGCTTCTTTGTCTATCTTGTCTGATTTTCTCCTGTCTGACCTTTTCCTGGTTA
AAAATCTGGGAGAAAATGACGGACTCCAAGCCGATCACCAAGAGTAAATCAGAAGCAAAC
CTCATCCCGAGCCAGGAGCCCTTTCCAGCCTCTGATAACTCAGGGGAGACACCGCAGAGA
AATGGGGAGGGCCACACTCTGCACAAAGACACCCAGCCAGGCCGAGCCCAGCCTCCCACA
AAGGCCCAAAGATCCGGTCGGCGGAGAAACTCCCTACCACCCTCCCGCCAGAAGCCCCCA
AGAAACCCCCTTTCTTCCAGTGACGCAGCACCCTCCCCAGAGCTTCAAGCCAACGGGACT
GGGACACAAGGTCTGGAGGCCACAGATACCAATGGCCTGTCCTCCTCAGCCAGGCCCCAG
GGCAGCAAGCTGGTCCCCTCCAAAGAAGACAAGAAGCAGGCAAACATCAAGAGGCAGCTG
ATGACCAACTTCATCCTGGGCTCTTTTGATGACTACTCCTCCGACGAGGACTCTGTTGCT
GGCTCATCTCGTGAGTCTACCCGGAAGGGCAGCCGGGCCAGCTTGGGGGCCCTGTCCCTG
GAGGCTTATCTGACCACAGGTGAAGCTGAGACCCGCGTCCCCACTATGAGGCCGAGCATG
TCGGGACTCCACCTGGTGAAGAGGGGACGGGAACACAAGAAGCTGGACCTGCACAGAGAC
TTTACCGTGGCTTCTCCCGCTGAGTTTGTCACACGCTTTGGGGGGGATCGGGTCATCGAG
AAGGTGCTTATTGCCAACAACGGGATTGCCGCTGTGAAGTGCATGCGCTCCATCCGCAGG
TGGGCCTATGAGATGTTCCGCAACGAGCGGGCCATCCGGTTTGTTCGCATGGTGACCCCC
GAGGACCTTAAGGCCAACGCAGAGTACATCAAGATGGCGGATCATTACGGGCCCGCCCCA
GGAGGGCCCAATAACAACAACTATGCCAACGTGGAGCTGATTGTGGACATTGCCAAGAGA
ATCCCGTTGCAGGCGGTGTGGGCTGGCTGGGGCCATGCTTTAGAAAACCCTAAACTTCCG
GAGCTGCTGTGCAAGAATGGAGTTGCTTTCTTAGGCCCTCCCAGGTTGAGGCCAATGGTG
GGTCTAGGAGATAAGATCGCCTCCACCGTTGTCGCCCAGACGCTACAGGTCCCAACCCTG
CCCAGGAGTGGAAGCGCCCTGACAGTGGAGTGGACAGAAGATGATCTGCAGCAGGGAAAA
AGAATCAGTGTCCCAGAAGATGTTTATGACAAGGGTTGCGTGAAAGACGTAGATGAGGGC
TTGGAGGCAGCAGAAAGAATTGGTTTTCCATTGATGATCAAAGCTTCTGAAGGTGGCGGA
GGGAAGGGAATCCGGGAAACTGAGAGTGCGGAGGACTTCCCGATCCTTTTCAGACAAGTA
CAGAGTGAGATCCCAGGCTCGCCCATCTTTCTCATGAAGCTGGCCCAGCACGCCCGTCAC
CTGGAAGTTCAGATCCTCGCTGACCAGTATGGGAATGCTGTGTCTCTGTTTGGTCGCGAC
TGCTCCATCCAGCGGCGGCATCAGAAGATCGTTGAGGAAGCACCGGCCACCATCGCGCCG
CTGGCCATATTCGAGTTCATGGAGCAGTGTGCCATTCGCCTGGCCAAGACCGTGGGCTAT
GTGAGTGCAGGGACAGTGGAATACCTCTATAGTCAGGATGGTAGCTTCCACTTCTTGGAG
CTGAATCCTCGCTTGCAGGTGGAACATCCCTGCACAGAAATGATTGCTGACGTTAATCTG
CCGGCCGCCCAGCTACAGATCGCCATGGGTGCCCCACTGCACCGGCTGAAAGATATCCGG
CTTCTGTATGGAGAGTCACCCTGGGGAGACTCCCCAATTTCTTTTGAAAACTCAGCTCAT
CTCCCCTGCCCCCGAGGCCACGTCATTGCCACCAGAATCACCAGCGAAAACCCAGACGAG
GGTTTTAAGCCGAGCTCCGGGACTGTCCAGGAACTGAATTTCCGGAGCAGCAAGAACGTC
TGGGGTTACTTCACGGTGGCCGCTACTGGAGGCCTGCACGAGTTTGCGATTTCCCAGTTT
GGGCACTGCTTCTCCTGGGGAGAGAACCGGAAAGAGGCCATTTCGAACATGGTGGTGGCT
TTGAAGGAACTGTCCCTCCGAGGCGACTTTAGGACTACCGTGGAATACCTCATTAACCTC
CTGGAGACCGAGAGCTTCCAGAACAACTACATCGACACCGGGTGGTTGGACTACCTCATT
GCTGAGAAAGTGCAAAAGAAACCGAATATCATGCTTGGGGTGGTATGCGGGGCCCTTGAA
CGTGGAGATGCGATGTTCAGAACGTGCATGACAGATTTCTTACACTCCCTGGAAAGGGGC
CAGGTCCTCCCAGCGGATTCACTACTGAACCTCGTAGATGTGGAATTAATTTACGAGGGT
GTAAAGTACATTCTAAAGGTGACCCGGCAGTCTCTGACCATGTTCGTTCTCATCATGAAT
GGCTGCCACATCGAGATTGATGCCCACCGGCTGAATGATGGGGGGCTCCTGCTCTCCTAC
AATGGGAACAGCTACACCACCTACATGAAGGAAGAGGTTGACAGTTACCGTACCATCGGC
AATAAGACGTGTGTTTTTGAGAAGGAGAACGATCCTACAGTCCTGAGATCCCCCTCGGCT
GGGAAGCTGACACAGATCACAGTGGAGGATGGGGGCCACGTTGAGGCTGGGAGACGCTAC
GCTGAGATGGAGGTGATGAAGATGATCATGACCCTGAACGTTCAGGAAAGAGGCCGGGTG
AAGTACATCAAGCGTCCAGGTGCGGTGCTGGAAGCAGGCTGCGTGGTGGCCAGGCTGGAG
CTCGATGACCCTTCTAAAGTCCACCCGGCTGAACCGTTCACAGGAGAACTCCCTGCCCAG
CAGAACACTGCCGACCTCGGAAAGAAACTGCACAGGGTCTTCCACAGCGTCCTGGGAAGC
CTCACCAACGTCATGAGTGGCTTTTGTCTGCCAGAGCCGTTTTTTAGCATAAAGCTGAAG
GAGTGGGTGCAGAAGCTCATGATGACCCTCCGGCACCCGTCACTGCTGCTGGACGTGCAG
GAGATCATGACCAGTCGTGCAGGCCGCATCCCCCCCCCTGTTGAGAAGTCTGTCCGCAAG
GTGATGGCCCAGTATGCCAGCAACATCACCTCGGTGCTGTGCCAGTTCCCCAGCCAGCAG
ATAGCCACCATCCTGGACTGCCATGCAGCCACCCTGCAGCGGAAGGCTGATCGAGAGGTC
TTCTTCATCAACACCCAGAGCATGGTGCAGTTGGTCCAGAGGTACCGAAGTGGAATCCGC
GGTCATATGAAAACAGTGGTGATCGATCTCTTGAGAAGATACTTGCGTGTTGAGACCATT
TTCGGCAAGGCAAGAGATGCTGATGCCAACTCCAGTGGGATGGTGGGGGGCGTGAGGAGC
CTGAGCTTTACCTCTGTGTGGGTGGTTTTGTCTCCCCCAGCCCACTACGACAAGTGTGTG
ATAAACCTCAGGGAACAGTTCAAGCCAGACATGTCCCAGGTGCTGGACTGCATCTTCTCC
CACGCACAGGTGACCAAGAAGAACCAGCTGGTGATCATGTTGATCGATGAGCTGTGTGGC
CCAGACCCTTCCCTGTCGGACGAGCTGATCTCCATCCTCAACGAGCTCACTCAGCTGAGC
AAAAGCGAGCACTGCAAAGTGGCCCTCAGAGCCCGGCAGATCCTGATCGCCTCCCCCTCC
TACGAGCTGCGGCATAACCAGGTGGAGTCCATTTTCCTGTCTGCCATTGACATGTACGGC
CACCAGTTCTGCCCCGAGAACCTCCAGAAATTAATACTTTCGGAAACAACCATCTTCGAC
GTCCTGAATACTTTCTTCTATCACGCAAACAAAGTCGTGTGCATGGCGTCCTTGGAGGTT
TACGTGGGGGGGGCTTACATCGCCTATGTGTTAAACAGCCTGCAGCACCGGCAGCTCCCG
GACGGCACCTGCGTGGTAGAATTCCAGTTCATGCTGCCGTCCTCCCACCCAAACCGGATG
ACCGTGCCCATCAGCATCACCAACCCTGACCTGCTGAGGCACACGACAGAGCTCTTCATG
GACAGCGGCTTCTCCCCACTGTGCCAGCGCATGGGAGCCATGGTAGCCTTCAGGAGATTC
GAGGACTTCACCAGAAATTTTGATGAAGTCATCTCTTGCTTCGCCAACGTGCCGAAAGAC
CCCCCCCTCTTCAGCGAGGCCCGCACCTCCCTATACTCCGAGGATGACTGCAAGAGCCTC
AGAGAAGAGCCCATCCACATTCTGAATGTGTCCATCCAGTGTGCGGACCACCTGGAGGAT
GAGGCACTGGTGCCGATTTTACGTACATTCGTACAGTCCAAGAAAAATATCCTTGTGGAT
TATGGACTCCGACGAATCCCATTCTTGATTGCCCAAGAGAAAGAATTTCCCAAGTTTTTC
ACATTCAGAGCAAGAGATGAGTTTGCAGAAGATCGCATTTACCGTCACTTGGAACCTGCC
CTGGCTTTCCAGCTGGAACTCAACCGGATGCGTAACTTCGATCTGACCGCCGTGCCCTGT
GCCAACCACAAGATGCACCTTTACCTGGGTGCTGCCAAGGTGGAAGGAAGGTATGAAGTG
ACGGACCATAGGTTCTTCATCCGTGCCATCATCAGGCACTCTGACCTGATCACAAAGGAA
GCCTCCTTCGAATACCTGCAGAACGAGGGTGAGCGGCTGCTCCTGGAGGCCATGGACGAG
CTGGAGGTGGCGTTCAATAACACCAACGTGCGCACCGACTGCAACCACATCTTCCTCAAC
TTCGTGCCCACTGTCATCATGGACCCCAACAAGATCGAGGAGTCCGTGCGCTACATGGTT
ATGCGCTACGGCAGCCGGCTGTGGAAACTCCGTGTGCTACAGGCTGAGGTCAAGATCAAC
ATCCGCCAGACCACCACCGGCAGTGCCGTTCCCATCCGCCTGTTCATCACCAATGAGTCG
GGCTACTACCTGGACATCAGCCTCTACAAAGAAGTGACTGACTCCAGATCTGGAAATATC
ATGTTTCACTCCTTCGGCAACAAGCAAGGGCCCCAGCACGGGATGCTGATCAATACTCCC
TACGTCACCAAGGATCTGCTCCAGGCCAAGCGATTCCAGGCCCAGACCCTGGGAACCACC
TACATCTATGACTTCCCGGAAATGTTCAGGCAGGCTCTCTTTAAACTGTGGGGCTCCCCA
GACAAGTATCCCAAAGACATCCTGACATACACTGAATTAGTGTTGGACTCTCAGGGCCAG
CTGGTGGAGATGAACCGACTTCCTGGTGGAAATGAGGTGGGCATGGTGGCCTTCAAAATG
AGGTTTAAGACCCAGGAGTACCCGGAAGGACGGGATGTGATCGTCATCGGCAATGACATC
ACCTTTCGCATTGGATCCTTTGGCCCTGGAGAGGACCTTCTGTACCTGCGGGCATCCGAG
ATGGCCCGGGCAGAGGCGATTCCCAAAATTTACGTGGCAGCCAACAGTGGCGCCCGTATT
GGCATGGCAGAGGAGATCAAACACATGTTCCACGTGGCTTGGGTGGACCCAGAAGACCCC
CACAAAGGATTTAAATACCTGTACCTGACTCCCCAAGACTACACCAGAATCAGCTCCCTG
AACTCCGTCCACTGTAAACACATCGAGGAAGGAGGAGAGTCCAGATACATGATCACGGAT
ATCATCGGGAAGGATGATGGCTTGGGCGTGGAGAATCTGAGGGGCTCAGGCATGATTGCT
GGGGAGTCCTCTCTGGCTTACGAAGAGATCGTCACCATTAGCTTGGTGACCTGCCGAGCC
ATTGGGATTGGGGCCTACTTGGTGAGGCTGGGCCAGCGAGTGATCCAGGTGGAGAATTCC
CACATCATCCTCACAGGAGCAAGTGCTCTCAACAAGGTCCTGGGAAGAGAGGTCTACACA
TCCAACAACCAGCTGGGTGGCGTTCAGATCATGCATTACAATGGTGTCTCCCACATCACC
GTGCCAGATGACTTTGAGGGGGTTTATACCATCCTGGAGTGGCTGTCCTATATGCCAAAG
GATAATCACAGCCCTGTCCCTATCATCACACCCACTGACCCCATTGACAGAGAAATTGAA
TTCCTCCCATCCAGAGCTCCCTACGACCCCCGGTGGATGCTTGCAGGAAGGCCTCACCCA
ACTCTGAAGGGAACGTGGCAGAGCGGATTCTTTGACCACGGCAGTTTCAAGGAAATCATG
GCACCCTGGGCGCAGACCGTGGTGACAGGACGAGCAAGGCTTGGGGGGATTCCCGTGGGA
GTGATTGCTGTGGAGACACGGACTGTGGAGGTGGCAGTCCCTGCAGACCCTGCCAACCTG
GATTCTGAGGCCAAGATAATTCAGCAGGCAGGACAGGTGTGGTTCCCAGACTCAGCCTAC
AAAACCGCCCAGGCCATCAAGGACTTCAACCGGGAGAAGTTGCCCCTGATGATCTTTGCC
AACTGGAGGGGGTTCTCCGGTGGCATGAAAGACATGTATGACCAGGTGCTGAAGTTTGGA
GCCTACATCGTGGACGGCCTTAGACAATACAAACAGCCCATCCTGATCTATATCCGCCCT
ATGCGGGAGCTCCGGGGAGGCTCCTGGGTGGTCATAGATGCCACCATCAACCCGCTGTGC
ATAGAAATGTATGCAGACAAAGAGAGCAGGGGTGGTGTTCTGGAACCAGAGGGGACAGTG
GAGATTAAGTTCCGAAAGGAAGATCTGATAAAGTCCATGAGAAGGATCGATCCAGCTTAC
AAGAAGCTCATGGAACAGCTAGGGGAACCTGATCTCTCCGACAAGGACCGAAAGGACCTG
GAGGGCCGGCTAAAGGCTCGCGAGGACCTGCTGCTCCCCATCTACCACCAGGTGGCGGTG
CAGTTCGCCGACTTCCATGACACACCCGGCCGGATGCTGGAGAAGGGCGTCATATCTGAC
ATCCTGGAGTGGAAGACCGCACGCACCTTCCTGTATTGGCGTCTGCGCCGCCTCCTCCTG
GAGGACCAGGTCAAGCAGGAGATCCTGCAGGCCAGCGGGGAGCTGAGTCACGTGCATATC
CAGTCCATGCTGCGTCGCTGGTTCGTGGAGACGGAGGGGGCTGTCAAGGCCTACTTGTGG
GACAACAACCAGGTGGTTGTGCAGTGGCTGGAACAGCACTGGCAGGCAGGGGATGGCCCG
CGCTCCACCATCCGTGAGAACATCACGTACCTGAAGCACGACTCTGTCCTCAAGACCATC
CGAGGCCTGGTTGAAGAAAACCCCGAGGTGGCCGTGGACTGTGTGATATACCTGAGCCAG
CACATCAGCCCAGCTGAGCGGGCGCAGGTCGTTCACCTGCTGTCTACCATGGACAGCCCG
GCCTCCACCTGA
Enzyme 3 GenBank Gene ID U89344 Link Image
Enzyme 3 GeneCard ID ACACB Link Image
Enzyme 3 GenAtlas ID ACACB Link Image
Enzyme 3 HGNC ID HGNC:85 Link Image
Enzyme 3 Chromosome Location 12
Enzyme 3 Locus 12q24.11
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Abu-Elheiga L, Almarza-Ortega DB, Baldini A, Wakil SJ: Human acetyl-CoA carboxylase 2. Molecular cloning, characterization, chromosomal mapping, and evidence for two isoforms. J Biol Chem. 1997 Apr 18;272(16):10669-77. [PubMed Link Image]
  2. Widmer J, Fassihi KS, Schlichter SC, Wheeler KS, Crute BE, King N, Nutile-McMenemy N, Noll WW, Daniel S, Ha J, Kim KH, Witters LA: Identification of a second human acetyl-CoA carboxylase gene. Biochem J. 1996 Jun 15;316 ( Pt 3):915-22. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5248
Enzyme 4 Name Pyruvate carboxylase, mitochondrial precursor
Enzyme 4 Synonyms
  1. Pyruvic carboxylase
  2. PCB
Enzyme 4 Gene Name PC
Enzyme 4 Protein Sequence >Pyruvate carboxylase, mitochondrial precursor 
MLKFRTVHGGLRLLGIRRTSTAPAASPNVRRLEYKPIKKVMVANRGEIAIRVFRACTELG
IRTVAIYSEQDTGQMHRQKADEAYLIGRGLAPVQAYLHIPDIIKVAKENNVDAVHPGYGF
LSERADFAQACQDAGVRFIGPSPEVVRKMGDKVEARAIAIAAGVPVVPGTDAPITSLHEA
HEFSNTYGFPIIFKAAYGGGGRGMRVVHSYEELEENYTRAYSEALAAFGNGALFVEKFIE
KPRHIEVQILGDQYGNILHLYERDCSIQRRHQKVVEIAPAAHLDPQLRTRLTSDSVKLAK
QVGYENAGTVEFLVDRHGKHYFIEVNSRLQVEHTVTEEITDVDLVHAQIHVAEGRSLPDL
GLRQENIRINGCAIQCRVTTEDPARSFQPDTGRIEVFRSGEGMGIRLDNASAFQGAVISP
HYDSLLVKVIAHGKDHPTAATKMSRALAEFRVRGVKTNIAFLQNVLNNQQFLAGTVDTQF
IDENPELFQLRPAQNRAQKLLHYLGHVMVNGPTTPIPVKASPSPTDPVVPAVPIGPPPAG
FRDILLREGPEGFARAVRNHPGLLLMDTTFRDAHQSLLATRVRTHDLKKIAPYVAHNFSK
LFSMENWGGATFDVAMRFLYECPWRRLQELRELIPNIPFQMLLRGANAVGYTNYPDNVVF
KFCEVAKENGMDVFRVFDSLNYLPNMLLGMEAAGSAGGVVEAAISYTGDVADPSRTKYSL
QYYMGLAEELVRAGTHILCIKDMAGLLKPTACTMLVSSLRDRFPDLPLHIHTHDTSGAGV
AAMLACAQAGADVVDVAADSMSGMTSQPSMGALVACTRGTPLDTEVPMERVFDYSEYWEG
ARGLYAAFDCTATMKSGNSDVYENEIPGGQYTNLHFQAHSMGLGSKFKEVKKAYVEANQM
LGDLIKVTPSSKIVGDLAQFMVQNGLSRAEAEAQAEELSFPRSVVEFLQGYIGVPHGGFP
EPFRSKVLKDLPRVEGRPGASLPPLDLQALEKELVDRHGEEVTPEDVLSAAMYPDVFAHF
KDFTATFGPLDSLNTRLFLQGPKIAEEFEVELERGKTLHIKALAVSDLNRAGQRQVFFEL
NGQLRSILVKDTQAMKEMHFHPKALKDVKGQIGAPMPGKVIDIKVVAGAKVAKGQPLCVL
SAMKMETVVTSPMEGTVRKVHVTKDMTLEGDDLILEIE
Enzyme 4 Number of Residues 1178
Enzyme 4 Molecular Weight 129635
Enzyme 4 Theoretical pI 6.83
Enzyme 4 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • biotin binding
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-carbon bonds
  • nucleotide binding
  • purine nucleotide binding
  • pyruvate carboxylase activity
  • vitamin binding
Process
  • alcohol metabolism
  • cellular metabolism
  • gluconeogenesis
  • glucose metabolism
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-21
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 458236 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P11498 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name PYC_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >3537 bp 
ATGCTGAAGTTCCGAACAGTCCATGGGGGCCTGAGGCTCCTGGGAATCCGCCGAACCTCC
ACCGCCCCCGCTGCCTCCCCAAATGTCCGGCGCCTGGAGTATAAGCCCATCAAGAAAGTC
ATGGTGGCCAACAGAGGTGAGATTGCCATCCGTGTGTTCCGGGCCTGCACGGAGCTGGGC
ATCCGCACCGTAGCCATCTACTCTGAGCAGGACACGGGCCAGATGCACCGGCAGAAAGCA
GATGAAGCCTATCTCATCGGCCGCGGCCTGGCCCCCGTGCAGGCCTACCTGCACATCCCA
GACATCATCAAGGTGGCCAAGGAGAACAACGTAGATGCAGTGCACCCTGGCTACGGGTTC
CTCTCTGAGCGAGCGGACTTCGCCCAGGCCTGCCAGGATGCAGGGGTCCGGTTTATTGGG
CCAAGCCCAGAAGTGGTCCGCAAGATGGGAGACAAGGTGGAGGCCCGGGCCATCGCCATT
GCTGCGGGTGTTCCCGTTGTCCCTGGCACAGATGCCCCCATCACGTCCCTGCATGAGGCC
CACGAGTTCTCCAACACCTACGGCTTCCCCATCATCTTCAAGGCGGCCTATGGGGGTGGA
GGGCGTGGCATGAGGGTGGTGCACAGCTACGAGGAGCTGGAGGAGAATTACACCCGGGCC
TACTCAGAGGCTCTGGCCGCCTTTGGGAATGGGGCGCTGTTTGTGGAGAAGTTCATCGAG
AAGCCACGGCACATCGAGGTGCAGATCTTGGGGGACCAGTATGGGAACATCCTGCACCTG
TACGAGCGAGACTGCTCCATCCAGCGGCGGCACCAGAAGGTGGTCGAGATTGCCCCCGCC
GCCCACCTGGACCCGCAGCTTCGGACTCGGCTCACCAGCGACTCTGTGAAACTCGCTAAA
CAGGTGGGCTACGAGAACGCAGGCACCGTGGAGTTCCTGGTGGACAGGCACGGCAAGCAC
TACTTCATCGAGGTCAACTCCCGCCTGCAGGTGGAGCACACGGTCACAGAGGAGATCACC
GACGTAGACCTGGTCCATGCTCAGATCCACGTGGCTGAGGGCAGGAGCCTACCCGACCTG
GGCCTGCGGCAGGAGAACATCCGCATCAACGGGTGTGCCATCCAGTGCCGGGTCACCACC
GAGGACCCCGCGCGCAGCTTCCAGCCGGACACCGGCCGCATTGAGGTGTTCCGGAGCGGA
GAGGGCATGGGCATCCGCCTGGATAATGCTTCCGCCTTCCAAGGAGCCGTCATCTCGCCC
CACTACGACTCCCTGCTGGTCAAAGTCATTGCCCACGGCAAAGACCACCCCACGGCCGCC
ACCAAGATGAGCAGGGCCCTTGCGGAGTTCCGCGTCCGAGGTGTGAAGACCAACATCGCC
TTCCTGCAGAATGTGCTCAACAACCAGCAGTTCCTGGCAGGCACTGTGGACACCCAGTTC
ATCGACGAGAACCCAGAGCTGTTCCAGCTGCGGCCTGCACAGAACCGGGCCCAAAAGCTG
TTGCACTACCTCGGCCATGTCATGGTAAACGGTCCAACCACCCCGATTCCCGTCAAGGCC
AGCCCCAGCCCCACGGACCCCGTTGTCCCTGCAGTGCCCATAGGCCCGCCCCCGGCTGGT
TTCAGAGACATCCTGCTGCGAGAGGGGCCTGAGGGCTTTGCTCGAGCTGTGCGGAACCAC
CCGGGGCTGCTGCTGATGGACACGACCTTCAGGGACGCCCACCAGTCACTGCTGGCCACT
CGTGTGCGCACCCACGATCTCAAAAAGATCGCCCCCTATGTTGCCCACAACTTCAGCAAG
CTCTTCAGCATGGAGAACTGGGGAGGAGCCACGTTTGACGTCGCCATGCGCTTCCTGTAT
GAGTGCCCCTGGCGGCGGCTGCAGGAGCTCCGGGAGCTCATCCCCAACATCCCTTTCCAG
ATGCTGCTGCGGGGGGCCAATGCTGTGGGCTACACCAACTACCCAGACAACGTGGTCTTC
AAGTTCTGTGAAGTGGCCAAAGAGAATGGCATGGATGTCTTCCGTGTGTTTGACTCCCTC
AACTACTTGCCCAACATGCTGCTGGGCATGGAGGCGGCAGGAAGTGCCGGAGGCGTGGTG
GAGGCTGCCATCTCATACACGGGCGACGTGGCCGACCCCAGCCGCACCAAGTACTCACTG
CAGTACTACATGGGCTTGGCCGAAGAGCTGGTGCGAGCTGGCACCCACATCCTGTGCATC
AAGGACATGGCCGGGCTGCTGAAGCCCACGGCCTGCACCATGCTGGTCAGCTCCCTCCGG
GACCGCTTCCCCGACCTCCCACTGCACATCCACACCCACGACACGTCAGGGGCAGGCGTG
GCAGCCATGCTGGCCTGTGCCCAGGCTGGAGCTGATGTGGTGGATGTGGCAGCTGATTCC
ATGTCTGGGATGACTTCACAGCCCAGCATGGGGGCCCTGGTGGCCTGTACCAGAGGGACT
CCCCTGGACACAGAGGTGCCCATGGAGCGCGTGTTTGACTACAGTGAGTACTGGGAGGGG
GCTCGGGGACTGTACGCGGCCTTCGACTGCACGGCCACCATGAAGTCTGGCAACTCGGAC
GTGTATGAAAATGAGATCCCAGGGGGCCAGTACACCAACCTGCACTTCCAGGCCCACAGC
ATGGGGCTTGGCTCCAAGTTCAAGGAGGTCAAGAAGGCCTATGTGGAGGCCAACCAGATG
CTGGGCGATCTCATCAAGGTGACGCCCTCCTCCAAGATCGTGGGGGACCTGGCCCAGTTT
ATGGTGCAGAATGGATTGAGCCGGGCAGAGGCCGAAGCTCAGGCGGAAGAGCTGTCCTTT
CCCCGCTCCGTGGTGGAGTTCCTGCAGGGCTACATCGGTGTCCCCCATGGGGGGTTCCCC
GAACCCTTTCGCTCTAAGGTACTGAAGGACCTGCCAAGGGTGGAGGGGCGGCCTGGAGCC
TCCCTCCCTCCCCTGGATCTGCAGGCACTGGAGAAGGAGCTGGTAGACCGGCATGGGGAG
GAGGTGACGCCGGAAGATGTGCTCTCAGCAGCTATGTACCCCGATGTGTTTGCCCACTTC
AAGGACTTCACTGCCACCTTTGGCCCCCTGGATAGCCTGAATACTCGCCTCTTCCTGCAG
GGACCCAAGATCGCAGAGGAGTTTGAGGTGGAGCTGGAGCGGGGCAAGACGCTGCACATC
AAAGCCCTGGCCGTGAGCGACCTGAACCGGGCCGGCCAGAGGCAGGTCTTCTTTGAGCTC
AATGGGCAGCTGCGGTCCATCTTGGTCAAGGACACCCAGGCCATGAAGGAGATGCACTTC
CACCCCAAGGCCCTAAAGGACGTGAAGGGCCAGATCGGGGCGCCCATGCCTGGGAAGGTG
ATAGACATCAAAGTGGTGGCAGGGGCCAAGGTGGCCAAGGGCCAGCCCCTGTGTGTGCTC
AGTGCCATGAAGATGGAGACTGTGGTGACCTCACCCATGGAGGGTACTGTCCGCAAGGTT
CATGTGACCAAGGACATGACACTGGAAGGTGACGACCTCATCCTGGAGATCGAGTGA
Enzyme 4 GenBank Gene ID U04641 Link Image
Enzyme 4 GeneCard ID PC Link Image
Enzyme 4 GenAtlas ID PC Link Image
Enzyme 4 HGNC ID HGNC:8636 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Wexler ID, Du Y, Lisgaris MV, Mandal SK, Freytag SO, Yang BS, Liu TC, Kwon M, Patel MS, Kerr DS: Primary amino acid sequence and structure of human pyruvate carboxylase. Biochim Biophys Acta. 1994 Oct 21;1227(1-2):46-52. [PubMed Link Image]
  2. MacKay N, Rigat B, Douglas C, Chen HS, Robinson BH: cDNA cloning of human kidney pyruvate carboxylase. Biochem Biophys Res Commun. 1994 Jul 29;202(2):1009-14. [PubMed Link Image]
  3. Lamhonwah AM, Quan F, Gravel RA: Sequence homology around the biotin-binding site of human propionyl-CoA carboxylase and pyruvate carboxylase. Arch Biochem Biophys. 1987 May 1;254(2):631-6. [PubMed Link Image]
  4. Freytag SO, Collier KJ: Molecular cloning of a cDNA for human pyruvate carboxylase. Structural relationship to other biotin-containing carboxylases and regulation of mRNA content in differentiating preadipocytes. J Biol Chem. 1984 Oct 25;259(20):12831-7. [PubMed Link Image]
  5. Carbone MA, MacKay N, Ling M, Cole DE, Douglas C, Rigat B, Feigenbaum A, Clarke JT, Haworth JC, Greenberg CR, Seargeant L, Robinson BH: Amerindian pyruvate carboxylase deficiency is associated with two distinct missense mutations. Am J Hum Genet. 1998 Jun;62(6):1312-9. [PubMed Link Image]
  6. Wexler ID, Kerr DS, Du Y, Kaung MM, Stephenson W, Lusk MM, Wappner RS, Higgins JJ: Molecular characterization of pyruvate carboxylase deficiency in two consanguineous families. Pediatr Res. 1998 May;43(5):579-84. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5276
Enzyme 5 Name Acetyl-CoA carboxylase 1
Enzyme 5 Synonyms
  1. ACC-alpha[Includes: Biotin carboxylase
Enzyme 5 Gene Name ACACA
Enzyme 5 Protein Sequence >Acetyl-CoA carboxylase 1 
MDEPSPLAQPLELNQHSRFIIGSVSEDNSEDEISNLVKLDLLEEKEGSLSPASVGSDTLS
DLGISSLQDGLALHIRSSMSGLHLVKQGRDRKKIDSQRDFTVASPAEFVTRFGGNKVIEK
VLIANNGIAAVKCMRSIRRWSYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPVPG
GPNNNNYANVELILDIAKRIPVQAVWAGWGHASENPKLPELLLKNGIAFMGPPSQAMWAL
GDKIASSIVAQTAGIPTLPWSGSGLRVDWQENDFSKRILNVPQELYEKGYVKDVDDGLQA
AEEVGYPVMIKASEGGGGKGIRKVNNADDFPNLFRQVQAEVPGSPIFVMRLAKQSRHLEV
QILADQYGNAISLFGRDCSVQRRHQKIIEEAPATIATPAVFEHMEQCAVKLAKMVGYVSA
GTVEYLYSQDGSFYFLELNPRLQVEHPCTEMVADVNLPAAQLQIAMGIPLYRIKDIRMMY
GVSPWGDSPIDFEDSAHVPCPRGHVIAARITSENPDEGFKPSSGTVQELNFRSNKNVWGY
FSVAAAGGLHEFADSQFGHCFSWGENREEAISNMVVALKELSIRGDFRTTVEYLIKLLET
ESFQMNRIDTGWLDRLIAEKVQAERPDTMLGVVCGALHVADVSLRNSVSNFLHSLERGQV
LPAHTLLNTVDVELIYEGVKYVLKVTRQSPNSYVVIMNGSCVEVDVHRLSDGGLLLSYDG
SSYTTYMKEEVDRYRITIGNKTCVFEKENDPSVMRSPSAGKLIQYIVEDGGHVFAGQCYA
EIEVMKMVMTLTAVESGCIHYVKRPGAALDPGCVLAKMQLDNPSKVQQAELHTGSLPRIQ
STALRGEKLHRVFHYVLDNLVNVMNGYCLPDPFFSSKVKDWVERLMKTLRDPSLPLLELQ
DIMTSVSGRIPPNVEKSIKKEMAQYASNITSVLCQFPSQQIANILDSHAATLNRKSEREV
FFMNTQSIVQLVQRYRSGIRGHMKAVVMDLLRQYLRVETQFQNGHYDKCVFALREENKSD
MNTVLNYIFSHAQVTKKNLLVTMLIDQLCGRDPTLTDELLNILTELTQLSKTTNAKVALR
ARQVLIASHLPSYELRHNQVESIFLSAIDMYGHQFCIENLQKLILSETSIFDVLPNFFYH
SNQVVRMAALEVYVRRAYIAYELNSVQHRQLKDNTCVVEFQFMLPTSHPNRGNIPTLNRM
SFSSNLNHYGMTHVASVSDVLLDNSFTPPCQRMGGMVSFRTFEDFVRIFDEVMGCFSDSP
PQSPTFPEAGHTSLYDEDKVPRDEPIHILNVAIKTDCDIEDDRLAAMFREFTQQNKATLV
DHGIRRLTFLVAQKDFRKQVNYEVDRRFHREFPKFFTFRARDKFEEDRIYRHLEPALAFQ
LELNRMRNFDLTAIPCANHKMHLYLGAAKVEVGTEVTDYRFFVRAIIRHSDLVTKEASFE
YLQNEGERLLLEAMDELEVAFNNTNVRTDCNHIFLNFVPTVIMDPSKIEESVRSMVMRYG
SRLWKLRVLQAELKINIRLTPTGKAIPIRLFLTNESGYYLDISLYKEVTDSRTAQIMFQA
YGDKQGPLHGMLINTPYVTKDLLQSKRFQAQSLGTTYIYDIPEMFRQSLIKLWESMSTQA
FLPSPPLPSDMLTYTELVLDDQGQLVHMNRLPGGNEIGMVAWKMTFKSPEYPEGRDIIVI
GNDITYRIGSFGPQEDLLFLRASELARAEGIPRIYVSANSGARIGLAEEIRHMFHVAWVD
PEDPYKGYRYLYLTPQDYKRVSALNSVHCEHVEDEGESRYKITDIIGKEEGIGPENLRGS
GMIAGESSLAYNEIITISLVTCRAIGIGAYLVRLGQRTIQVENSHLILTGAGALNKVLGR
EVYTSNNQLGGIQIMHNNGVTHCTVCDDFEGVFTVLHWLSYMPKSVHSSVPLLNSKDPID
RIIEFVPTKTPYDPRWMLAGRPHPTQKGQWLSGFFDYGSFSEIMQPWAQTVVVGRARLGG
IPVGVVAVETRTVELSIPADPANLDSEAKIIQQAGQVWFPDSAFKTYQAIKDFNREGLPL
MVFANWRGFSGGMKDMYDQVLKFGAYIVDGLRECCQPVLVYIPPQAELRGGSWVVIDSSI
NPRHMEMYADRESRGSVLEPEGTVEIKFRRKDLVKTMRRVDPVYIHLAERLGTPELSTAE
RKELENKLKEREEFLIPIYHQVAVQFADLHDTPGRMQEKGVISDILDWKTSRTFFYWRLR
RLLLEDLVKKKIHNANPELTDGQIQAMLRRWFVEVEGTVKAYVWDNNKDLAEWLEKQLTE
EDGVHSVIEENIKCISRDYVLKQIRSLVQANPEVAMDSIIHMTQHISPTQRAEVIRILST
MDSPST
Enzyme 5 Number of Residues 2346
Enzyme 5 Molecular Weight 265557
Enzyme 5 Theoretical pI 6.32
Enzyme 5 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • biotin binding
  • catalytic activity
  • ligase activity
  • nucleotide binding
  • purine nucleotide binding
  • vitamin binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 5 General Function Lipid transport and metabolism
Enzyme 5 Specific Function Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions:biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 849083 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q13085 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name COA1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >7041 bp 
ATGGATGAACCATCTCCCTTGGCCCAACCTCTGGAGCTGAACCAGCACTCTCGATTCATA
ATAGGTTCTGTGTCAGAAGATAACTCAGAGGATGAGATCAGCAACCTGGTGAAGCTGGAC
CTACTGGAGGAGAAGGAGGGCTCCTTGTCACCTGCTTCTGTTGGCTCAGATACACTCTCT
GATTTGGGGATCTCTGCCCTACAGGATGGCTTGGCCTTGCACATAAGGTCCAGCTGGTCT
GGCTTGCACCTAGTAAAGCAGGGCGGAGACAGAAAGAAAATAGATTCTCAACGAGATTTC
ACTGTGGCTTCTCCAGCAGAATTTGTTACTCGCTTTGGGGGAAATAAAGTGATTGAGAAG
GTTCTCATCGCTAACAATGGCATTGCAGCAGTGAAATGCATGCGGTCTATCCGTAGGTGG
TCTTATGAAATGTTTCGAAATGAACGTGCAATTAGATTCGTTGTCATGGTCACACCTGAA
GACCTTAAAGCCAATGCAGAATACATTAAGATGGCAGATCACTATGTGCCGGTGCCTGGA
GGAGCAAACAACAACAACTATGCAAATGTGGAATTAATTCTTGATATTGCTAAAAGGATC
CCAGTGCAAGCAGTGTGGGCTGGCTGGGGTCATGCTTCTGAGAATCCCAAACTACCGGAA
CTTCTCTTGAAAAATGGCATTGCCTTCATGGGTCCTCCAAACCAGGCCATGTGGGCTTTA
GGGGATAAGATTGCATCTTCCATAGTGGCTCAAACTGCAGGTATCCCAACTCTTCCCTGG
AGCGGCAGTGGTCTTCGTGTGGACTGGCAGGAAAATGATTTTTCAAAACGTATCTTAAAT
GTTCCCCAGGAGCTATATGAAAAAGGTTATGTGAAAGATGTGGATGATGGGCTAAAGGCA
GCTGAGAAGGTTGGATATCCAGTAATGATCAAGGCCTCAGAGGGAGGAGGAGGGAAGGGA
ATTAGAAAAGTTAACAATGCAGATGACTTCCCTAATCTCTTCAGACAGGTTCAAGCTGAA
GTTCCTGGATCTCCCATATTTGTGATGAGACTAGCCAAACAATCTCGTCATCTGGAGGTG
CAGATCTTAGCGGACCAATATGGCAATGCTATCTCTTTGTTTGGTCGTGATTGCTCTGTA
CAACGCAGGCATCAGAAGATTATTGAAGAAGCACCTGCTACTATTGCTACTCCAGCAGTA
TTTGAACACATGGAACAGTGTGCGGTGAAACTTGCCAAAATGGTGGGTTATGTGAGTGCT
GGGACTGTGGAATACCTGTACAGCCAGGATGGCAGCTTCTACTTTCTAGAATTGAACCCT
CGGCTACAGGTTGAACAACCTTGTACAGAGATGGTGGCTGATGTCAATCTCCCCGCAGCA
CAGCTCCAGATTGCCATGGGGATTCCTCTATATAGAATCAAGGATATCCGTATGATGTAT
GGGGTATCTCCTTGGGGTGATTCTCCCATTGATTTTGAAAATTCTGCTCACGTTCCTTGT
CCAAGGGGCCATGTTATTGCTGCTCGGATCACTAGTGAAAATCCAGATGAGGGTTTTAAG
CCCAGCTCAGGAACAGTTCAGGAGCTAAATTTCCGCAGCAATAAGAATGTTTGGGGATAT
TTCAGTGTTGCTGCTGCAGGGGGACTTCATGAATTTGCTGGTTCTCAGTTTGGTCACTGC
TTTTCTTGGGGAGAAAACAGAGAAGAAGCAATTTCAAACATGGTGGTGGCATTGAAGGAG
CTGTCTATTCGGGGTGACTTTCGAACTACAGTTGAATACCTGATCAAATTGTTAGAGACT
GAAAGCTTTCAAATGAACAGAATTGATACTGGCTGGCTGGACAGACTGATAGCAGAAAAA
GTACGGGCTGAGCGTCCTGACACCATGTTGGGGGTTGTGTGTGGTGCCCTCCACGTCGGA
GATGTGAGCCTGCGAAATAGCGTCTCTAACTTCCTTCACTCCTTAGAAAGGGGTCAAGTC
CTTCCGGCTCATACACTTCTGAATACAGTAGATGTTGAACTTATCTATGAGGGAGTCAAG
TATGTACTTAAGGTGACTCGACAGTCCCCCAACTCCTATGTGGTGATCATGAATGGCTCA
TGTGTAGAAGTAGATGTACATCGGCTGAGTGACGGTGGACTGCTCTTGTCCTATGATGGC
AGCAGTTACACCACGTATATGAAGGAGGAAGTAGACAGATATCGCATCACAATTGGCAAT
AAAACCTGTGTGTTTGAGAAGGAAAATGACCCATCGGTGATGCGCTCACCTTCTGCTGGG
AAGTTAATCCAGTACATTGTAGAAGATGGAGGTCATGTGTTTGCCGGCCAGTGCTATGCA
GAGATTGAGGTAATGAAGATGGTAATGACTTTGACAGCTGTGGAGTCTGGCTGTATCCAT
TACGTCAAGCGTCCTGGAGCAGCTCTTGACCCTGGCTGTGTACTCGCCAAAATGCAACTG
GACAACCCCAGCAAGGTTCAGCAGGCTGAACTTCACACAGGTAGTCTGCCACGGATCCAG
AGCACCGCTCTCCGAGGCGAGAAGCTCCATCGAGTGTTCCACTATGTCCTGGATAATCTG
GTCAATGTAATGAATGGATACTGCCTTCCAGATCCTTTCTTTAGCAGCAAGGTAAAAGAC
TGGGTAGAACGATTGATGAAAACCCTCAGAGATCCCTCCCTGCCTCTCCTAGAATTGCAA
GATATTATGACCAGTGTGTCTGGCCGCATTCCCCCCAATGTGGAGAAGTCTATCAAGAAG
GAAATGGCTCAGTATGCTAGCAACATCACATCAGTCCTCTGTCAGTTTCCCAGCCAGCAG
ATTGCAAACATCCTAGATAGCCATGCAGCTACATTGAACCGGAAATCTGAACGGGAAGTC
TTCTTTATGAATACTCAGAGCATTGTCCAGCTGGTACAGAGGTACCGAAGTGGCATCCGA
GGCCACATGAAGGCTGTGGTGATGGATCTGCTCCGGCAGTACCTGCGAGTAGAGACACAA
TTCCAGAATGGTCACTATGACAAATGTGTATTCGCCCTTCGAGAAGAGAATAAGAGTGAC
ATGAACACTGTACTGAACTACATCTTCTCTCACGCTCAAGTCACCAAGAAGAATCTTCTG
GTCACAATGCTTATTGATCAGTTGTGTGGCCGGGACCCTACTCTAACTGATGAGCTGCTG
AGTATTCTCACAGAGCTAACTCAACTCAGTAAGACCACCAATGCCAAAGTAGCACTTCGA
GCACGCCAGGTTCTTATTGCCTCCCATTTGCCATCATATGACGTTCGCCATAACCAAGTA
GAGTCTATCTTCCTATCAGCTATTGACATGTATGGACATCAATTTTGCATTGAGAACCTG
CAGAAACTCATCCTATCAGAAACATCTATTTTTGATGTCCTACCAAACTTCTTCTATCAC
AGCAACCAAGTAGTGAGGATGGCAGCTCTGGAGGTGTACGTTCGAAGGGCTTATATTGCC
TATGAACTTAACAGCGTACAACACCGCCAGCTTAAGGACAACACCTGCGTGGTGGAATTC
CAGTTCATGCTGCCCACATCTCATCCAAACAGAGGGAACATCCCTACGCTAAACAGAATG
TCCTTCTCCTCCAACCTCAACCACTATGGCATGACCCATGTAGCTAGTGTCAGCGATGTT
CTGTTGGACAACGCCTTCACACCACCTTGTCAACGCATGGGCGGAATGGTCTCTTTTCGG
ACTTTTGAAGATTTTGTCAGGATCTTTGATGAAGTAATGGGCTGCTTCTGTGACTCCCCA
CCCCAGAGTCCCACATTCCCTGAGGCAGGTCACACGTCTCTTTATGATGAGGATAAGGTT
CCCAGGGATGAACCAATTCACATTCTCAATGTGGCTATCAAGACTGACGGTGATATTGAG
GATGACAGGCTGGCAGCTATGTTCAGAGAATTCACCCAGCAAAATAAAGCTACCCTGGCT
GACCATGGGATCCGGCGCCTGACTTTCCTGGTTGCACAAAAGGATTTCAGAAAGCAGGTC
AACTATGAGGTGGATCGGAGATTTCATAGAGAATTCCCTAAATTTTTTACATTCCGAGCA
AGGGATAAGTTTGAGGAGGATCGTATCTATCGTCATCTGGAGCCTGCTCTGGCTTTCCAG
TTAGAGCTGAACCGGATGAGAAATTTTGACCTCACTGCCATTCCATGTGCTAATCACAAG
ATGCACCTGTATCTCGGGGCAGCCAAGGTGGAAGTGGGCACAGAAGTGACAGACTACAGG
TTCTTTGTTCGTGCAATCATCAGGCATTCTGATCTGGTCACCAAGGAAGCTTCTTTTGAA
TATCTGCAAAGTGAAGGGGAGCGGCTACTCCTGGAAGCCATGGATGAGTTGGAAGTTGCT
TTTAACAATACAAATGTCCGCACTGACTGTAACCACATCCTCCTCAACTTTGTGCCCACG
GTTATCATGGACCCATCAAAGATTGAGGAATCCGTGCGGAGCATGGTAATGCGGTATGGA
AGTCGCCTGTGGAAATTGCGCGTCCTCCAGGCAGAACTGAAAATCAACATTCGCCTGACG
CCAACTGGAAAAGCAATTCCCATCCGCCTTTTCCTGACAAACGAGTCTGGCTATTACTTG
GATATCAGCCTATACAAGGAAGTGACTGACTCCAGGACAGCACAGATCATGTTTCAGGCA
TATGGAGACAAGCAGGGACCACTGCATGGAATGTTAATCAATACTCCATATGTGACCAAA
GACCTGCTGCAATCAAAGAGGTTCCAGGCACAATCCTTAGGGACAACGTACATATATGAT
ATCCCAGAGATGTTTCGGCAGTCCCTGATCAAACTCTGGGAGTCTATGTCAACTCAAGCA
TTTCTTCCATCTCCCCCTCTGCCTTCTGACATGCTGACTTACACTGAACTGGTACTGGAT
GATCAAGGTCAGCTGGTCCACATGAACAGGCTTCCAGGAGGAAATGAGATTGGCATGGTA
GCTTGGAAAATGAGCCTTAAAAGTCCTGAATATCCAGAAGGCCGAGATGTTATTGTTATT
GGCAATGACATTACATACCGAATTGGGTCCTTTGGGCCTCAAGAAGATTTGTTATTTCTC
AGAGCTTCCGAACTTGCTAGGGCCGAAGGCATTCCACGCATCTATGTATCAGCCAACAGT
GGAGCAAGAATCGGACTGGCAGAAGAAATTCGCCATATGTTTCATGTGGCCTGGGTAGAT
TCTGAGGATCCTTACAAGGGATACAGGTATTTATATCTGACTCCTCAAGATTATAAGAGA
GTCGGTGCTCTCAACTCTGTCCATTGTGAACACGTGGAAGATGAAGGAGAATCCAGGTAC
AAGATAACAGATATTATTGGGAAAGAAGAGGGAATTGGACCCGAGAACCTTCGAGGTTCT
GGAATGATCGCTGGAGAATCCTCATTGGCCTATAATGAGATCATTACCATCAGCCTGGTG
ACGTCCCGGGCCATTGGGATTGGGGCTTACCTTGTCCGGCTGGGACAGAGAACCATCCAG
GTTGAGAATTCTCACTTGATTCTAACAGGAGCTGGAGCCCTCAACAAAGTCCTCGGGCGG
GAAGTGTACACCTCCAATAACCAGCTGGGGGGCATCCAGATTACGCACAACAATGGGGTG
ACCCACTGCACTGTGTGTGACGGCTTTGAAGGGGTTTTCACTGTCCTGCACTGGCTGTCT
TACATGCCCAAGAGCGTACACAGTTCAGTTCCTCTTCTGAACTCAAAGGATCCTATAGAC
AGAATCATCGAGTTTGTTCCCACAAAGACCCCATATGATCCTCGATGGATGCTAGCAGGC
CGCCCTCACCCAACCCAAAAAGGTCAGTGGTTGAGTGGCTTTTTTGACTATGGATCTTTC
TCAGAGATTATGCAGCCCTGGGCACAGACGGTGGTGGTTGGTAGAGCCAGGTTAGGGGGA
ATACCTGTGGGAGTTGTTGCTGTAGAAACCCGGACAGTAGAACTAAGTGTACCAGCTGAT
CCAGCAAACCTGGATTCTGAAGCCAAGATAATCCAGCACGCCGGCCAAGTTTGGTTTCCG
GATTCTGCGTTTAAGACGTATCAGGCCATCAAGGACTTCAACCGGGAAGGGCTACCTCTA
ATGGTCTTTGCCAACTGGAGAGGCTTCTCTGGTGGAATGAAAGATATGTATCACCAAGTG
CTGAAGTTTGGTGCTTACATTGTGGATGGCTTGCGGGAATGTTCCCAGCCTGTGCTGGTC
TACATTCCTCCCCAGGCTGAGCTGCGGGGTGGCTCCTGGGTGGTGATCGACCCAACCATC
AATCCTCGGCACATGGAGATGTATGCTGACCGAGAAAGCAGGGGATCTGTTCTGGAGCCA
GAAGGGACGGTAGAAATCAAATTCCGCAGAAAGGATCTGGTGAAAACCATGCGTCGGGTG
GACCCAGTCTACATCCACTTGGCTGAGCGATTGGGGACCCCAGAGCTGAGCCCAACTGAG
CGGAAGGAGTTGGAGAGCAAGTTGAAGGAGCGGGAGGAATTCCTAATTCCAATTTACCAT
CAGGTAGCCGTGCAGTTTGCTGACTTGCACGACACTCCAGGCCGGATGCAGGAGAAGGGT
GTTATTAGCGATATCCTGGATTGGAAAACATCCCGTACCTTCTTCTACTGGCGACTGAGG
CGTCTTCTGCTGGAGGACCTGGTCAAGAAGAAAATCCACAGTGCCAACCCTGAGCTGACT
GATGGCCAGATTCAAGCCATGTTAAGACGCTGGTTTGTGGAAGTGGAAGGAACAGTGAAG
GCTTATGTTTGGGACAATAATAAGGATCTGGCGGAGTGGCTAGAGAAACAGCTGACAGAG
GAGGATGGTGTTCACTCGGTAATAGAGGAAAACATCAAATGCATCAGCAGAGACTACGTC
CTCAAGCAAATCCGCAGCTTGGTCCAGGCCAATCCAGAGGTTGCCATGGATTCCATCATC
CATATGACGCAGCACATATCACCCACTCAGCGGGCAGAAGTCATAAGGATCCTTTCCACT
ATGGACTCCCCTTCTACGTAG
Enzyme 5 GenBank Gene ID U19822 Link Image
Enzyme 5 GeneCard ID ACACA Link Image
Enzyme 5 GenAtlas ID ACACA Link Image
Enzyme 5 HGNC ID HGNC:84 Link Image
Enzyme 5 Chromosome Location 17
Enzyme 5 Locus 17q21
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Abu-Elheiga L, Jayakumar A, Baldini A, Chirala SS, Wakil SJ: Human acetyl-CoA carboxylase: characterization, molecular cloning, and evidence for two isoforms. Proc Natl Acad Sci U S A. 1995 Apr 25;92(9):4011-5. [PubMed Link Image]
  2. Mao J, Chirala SS, Wakil SJ: Human acetyl-CoA carboxylase 1 gene: presence of three promoters and heterogeneity at the 5'-untranslated mRNA region. Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):7515-20. Epub 2003 Jun 16. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5312
Enzyme 6 Name Thymidylate kinase
Enzyme 6 Synonyms
  1. dTMP kinase
Enzyme 6 Gene Name DTYMK
Enzyme 6 Protein Sequence >Thymidylate kinase 
MAARRGALIVLEGVDRAGKSTQSRKLVEALCAAGHRAELLRFPERSTEIGKLLSSYLQKK
SDVEDHSVHLLFSANRWEQVPLIKEKLSQGVTLVVDRYAFSGVAFTGAKENFSLDWCKQP
DVGLPKPDLVLFLQLQLADAAKRGAFGHERYENGAFQERALRCFHQLMKDTTLNWKMVDA
SKSIEAVHEDIRVLSEDAIRTATEKPLGELWK
Enzyme 6 Number of Residues 212
Enzyme 6 Molecular Weight 23820
Enzyme 6 Theoretical pI 8.49
Enzyme 6 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • thymidylate kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • dTDP biosynthesis
  • dTTP biosynthesis
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • pyrimidine deoxyribonucleoside diphosphate biosynthesis
  • pyrimidine deoxyribonucleoside triphosphate biosynthesis
  • pyrimidine nucleoside diphosphate biosynthesis
  • pyrimidine nucleoside triphosphate biosynthesis
  • pyrimidine nucleotide biosynthesis
  • pyrimidine nucleotide metabolism
Component
—
Enzyme 6 General Function Nucleotide transport and metabolism
Enzyme 6 Specific Function Catalyzes the conversion of dTMP to dTDP
Enzyme 6 Pathways
Enzyme 6 Reactions
  • ATP + dTMP = ADP + dTDP
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 37206 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P23919 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name DTYMK_HUMAN Link Image
Enzyme 6 PDB ID 1E9A Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >636 bp 
ATGGCGGCCCGGCGCGGGGCTCTCATAGTGCTGGAGGGCGTGGACCGCGCCGGGAAGAGC
ACGCAGAGCCGCAAGCTGGTGGAAGCGCTGTCGCGCGGGCCACCGCCCGAACTGCTCCGG
TTCCCGGAAAGATCAACTGAAATCGGCAAACTTCTGAGTTCCTACTTGCAAAAGAAAAGT
GACGTGGAGGATCACTCGGTGCACCTGCTTTTTTCTGCAAATCGCTGGGAACAAGTGCCG
TTAATTAAGGAAAAGTTGAGCCAGGGCGTGACCCTCGTCGTGGACAGATACGCATTTTCT
GGTGTGGCCTTCACCGGTGCCAAGGAGAATTTTTCCCTAGACTGGTGTAAACAGCCAGAC
GTGGGCCTTCCCAAACCCGACCTGGTCCTGTTCCTCCAGTTACAGCTGGCGGATGCTGCC
AAGCGGGGAGCGTTTGGCCATGAGCGCTATGAGAACGGGGCTTTCCAGGAGCGGGCGCTC
CGGTGTTTCCACCAGCTCATGAAAGACACGACTTTGAACTGGAAGATGGTGGATGCTTCC
AAAAGACTCGAAGCTGTCCATGAGGAACTCCGCGTGCTCTCTGAGGACGCCATCCGCACT
GCCACAGAGAAGCCGCTGGGGGAGCTATGGAAGTGA
Enzyme 6 GenBank Gene ID X54729 Link Image
Enzyme 6 GeneCard ID DTYMK Link Image
Enzyme 6 GenAtlas ID DTYMK Link Image
Enzyme 6 HGNC ID HGNC:3061 Link Image
Enzyme 6 Chromosome Location 2
Enzyme 6 Locus 2q37.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Su JY, Sclafani RA: Molecular cloning and expression of the human deoxythymidylate kinase gene in yeast. Nucleic Acids Res. 1991 Feb 25;19(4):823-7. [PubMed Link Image]
  2. Huang SH, Tang A, Drisco B, Zhang SQ, Seeger R, Li C, Jong A: Human dTMP kinase: gene expression and enzymatic activity coinciding with cell cycle progression and cell growth. DNA Cell Biol. 1994 May;13(5):461-71. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5313
Enzyme 7 Name Ectonucleoside triphosphate diphosphohydrolase 1
Enzyme 7 Synonyms
  1. NTPDase 1
  2. Ecto-ATP diphosphohydrolase
  3. ATPDase
  4. Lymphoid cell activation antigen
  5. Ecto-apyrase
  6. CD39 antigen
Enzyme 7 Gene Name ENTPD1
Enzyme 7 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 1 
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
Enzyme 7 Number of Residues 510
Enzyme 7 Molecular Weight 57965
Enzyme 7 Theoretical pI 6.29
Enzyme 7 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 7 General Function Not Available
Enzyme 7 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 7 Pathways
Enzyme 7 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 17-37 479-499
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 765256 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P49961 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name ENTP1_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 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 7 GenBank Gene ID S73813 Link Image
Enzyme 7 GeneCard ID ENTPD1 Link Image
Enzyme 7 GenAtlas ID ENTPD1 Link Image
Enzyme 7 HGNC ID HGNC:3363 Link Image
Enzyme 7 Chromosome Location 10
Enzyme 7 Locus 10q24
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5314
Enzyme 8 Name Soluble calcium-activated nucleotidase 1
Enzyme 8 Synonyms
  1. SCAN-1
  2. Apyrase homolog
  3. Putative NF-kappa-B-activating protein 107
  4. Putative MAPK-activating protein PM09
Enzyme 8 Gene Name CANT1
Enzyme 8 Protein Sequence >Soluble calcium-activated nucleotidase 1 
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
Enzyme 8 Number of Residues 401
Enzyme 8 Molecular Weight 44840
Enzyme 8 Theoretical pI 5.98
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Not Available
Enzyme 8 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 8 Pathways
Enzyme 8 Reactions
  • A nucleoside diphosphate + H2O = a nucleotide + phosphate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • 45-62
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 22218108 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q8WVQ1 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name CANT1_HUMAN Link Image
Enzyme 8 PDB ID 1S1D Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1116 bp 
ATGACCAAGGCCGCGGACCCCCGCTTCCGCCCCCGCTGGAAGGTGATCCTGACGTTCTTT
GTGGGTGCTGCCATCCTCTGGCTGCTCTGCTCCCACCGCCCGGCCCCCGGCAGGCCCCCC
ACCCACAATGCACACAACTGGAGGCTCGGCCAGGCGCCCGCCAACTGGTACAATGACACC
TACCCCCTGTCTCCCCCACAAAGGACACCGGCTGGGATTCGGTATCGAATCGCAGTTATC
GCAGACCTGGACACAGAGTCAAGGGCCCAAGAGGAAAACACCTGGTTCAGTTACCTGAAA
AAGGGCTACCTGACCCTGTCAGACAGTGGGGACAAGGTGGCCGTGGAATGGGACAAAGAC
CATGGGGTCCTGGAGTCCCACCTGGCGGAGAAGGGGAGAGGCATGGAGCTATCCGACCTG
ATTGTTTTCAATGGGAAACTCTACTCCGTGGATGACCGGACGGGGGTCGTCTACCAGATC
GAAGGCAGCAAAGCCGTGCCCTGGGTGATTCTGTCCGACGGCGACGGCACCGTGGAGAAA
GGCTTCAAGGCCGAATGGCTGGCAGTGAAGGACGAGCGTCTGTACGTGGGCGGCCTGGGC
AAGGAGTGGACGACCACTACGGGTGATGTGGTGAACGAGAACCCGGAGTGGGTGAAGGTG
GTGGGCTACAAGGGCAGCGTGGACCACGAGAACTGGGTGTCCAACTACAACGCCCTGCGG
GCTGCTGCCGGCATCCAGCCGCCAGGCTACCTCATCCATGAGTCTGCCTGCTGGAGTGAC
ACGCTGCAGCGCTGGTTCTTCCTGCCGCGCCGCGCCAGCCAGGAGCGCTACAGCGAGAAG
GACGACGAGCGCAAGGGCGCCAACCTGCTGCTGAGCGCCTCCCCTGACTTCGGCGACATC
GCTGTGAGCCACGTCGGGGCGGTGGTCCCCACTCACGGCTTCTCGTCCTTCAAGTTCATC
CCCAACACCGACGACCAGATCATTGTGGCCCTCAAATCCGAGGAGGACAGCGGCAGAGTC
GCCTCCTACATCATGGCCTTCACGCTGGACGGGCGCTTCCTGTTGCCGGAGACCAAGATC
GGAAGCGTGAAATACGAAGGCATCGAGTTCATTTAA
Enzyme 8 GenBank Gene ID AF328554 Link Image
Enzyme 8 GeneCard ID CANT1 Link Image
Enzyme 8 GenAtlas ID CANT1 Link Image
Enzyme 8 HGNC ID HGNC:19721 Link Image
Enzyme 8 Chromosome Location 17
Enzyme 8 Locus 17q25.3
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5317
Enzyme 9 Name Thymidine kinase, cytosolic
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name TK1
Enzyme 9 Protein Sequence >Thymidine kinase, cytosolic 
MSCINLPTVLPGSPSKTRGQIQVILGPMFSGKSTELMRRVRRFQIAQYKCLVIKYAKDTR
YSSSFCTHDRNTMEALPACLLRDVAQEALGVAVIGIDEGQFFPDIVEFCEAMANAGKTVI
VAALDGTFQRKPFGAILNLVPLAESVVKLTAVCMECFREAAYTKRLGTEKEVEVIGGADK
YHSVCRLCYFKKASGQPAGPDNKENCPVPGKPGEAVAARKLFAPQQILQCSPAN
Enzyme 9 Number of Residues 234
Enzyme 9 Molecular Weight 25469
Enzyme 9 Theoretical pI 8.61
Enzyme 9 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • deoxynucleoside kinase activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleoside kinase activity
  • nucleotide binding
  • purine nucleotide binding
  • thymidine kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
—
Component
—
Enzyme 9 General Function Nucleotide transport and metabolism
Enzyme 9 Specific Function ATP + thymidine = ADP + thymidine 5'- phosphate
Enzyme 9 Pathways
Enzyme 9 Reactions
  • ATP + thymidine = ADP + thymidine 5'-phosphate
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 339709 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P04183 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name KITH_HUMAN Link Image
Enzyme 9 PDB ID 1XBT Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >705 bp 
ATGAGCTGCATTAACCTGCCCACTGTGCTGCCCGGCTCCCCCAGCAAGACCCGGGGGCAG
ATCCAGGTGATTCTCGGGCCGATGTTCTCAGGAAAAAGCACAGAGTTGATGAGACGCGTC
CGTCGCTTCCAGATTGCTCAGTACAAGTGCCTGGTGATCAAGTATGCCAAAGACACTCGC
TACAGCAGCAGCTTCTGCACACATGACCGGAACACCATGGAGGCGCTGCCCGCCTGCCTG
CTCCGAGACGTGGCCCAGGAGGCCCTGGGCGTGGCTGTCATAGGCATCGACGAGGGGCAG
TTTTTCCCTGACATCATGGAGTTCTGCGAGGCCATGGCCAACGCCGGGAAGACCGTAATT
GTGGCTGCACTGGATGGGACCTTCCAGAGGAAGCCATTTGGGGCCATCCTGAACCTGGTG
CCGCTGGCCGAGAGCGTGGTGAAGCTGACGGCGGTGTGCATGGAGTGCTTCCGGGAAGCC
GCCTATACCAAGAGGCTCGGCACAGAGAAGGAGGTCGAGGTGATTGGGGGAGCAGACAAG
TACCACTCCGTGTGTCGGCTCTGCTACTTCAAGAAGGCCTCAGGCCAGCCTGCCGGGCCG
GACAACAAAGAGAACTGCCCAGTGCCAGGAAAGCCAGGGGAAGCCGTGGCTGCCAGGAAG
CTCTTTGCCCCACAGCAGATTCTGCAATGCAGCCCTGCCAACTGA
Enzyme 9 GenBank Gene ID K02581 Link Image
Enzyme 9 GeneCard ID TK1 Link Image
Enzyme 9 GenAtlas ID TK1 Link Image
Enzyme 9 HGNC ID HGNC:11830 Link Image
Enzyme 9 Chromosome Location 17
Enzyme 9 Locus 17q23.2-q25.3
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Bradshaw HD Jr, Deininger PL: Human thymidine kinase gene: molecular cloning and nucleotide sequence of a cDNA expressible in mammalian cells. Mol Cell Biol. 1984 Nov;4(11):2316-20. [PubMed Link Image]
  2. Flemington E, Bradshaw HD Jr, Traina-Dorge V, Slagel V, Deininger PL: Sequence, structure and promoter characterization of the human thymidine kinase gene. Gene. 1987;52(2-3):267-77. [PubMed Link Image]
  3. Chang ZF, Huang DY, Chi LM: Serine 13 is the site of mitotic phosphorylation of human thymidine kinase. J Biol Chem. 1998 May 15;273(20):12095-100. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5338
Enzyme 10 Name Nucleoside diphosphate kinase, mitochondrial precursor
Enzyme 10 Synonyms
  1. NDP kinase, mitochondrial
  2. NDK
  3. nm23-H4
  4. Nucleoside diphosphate kinase D
  5. NDPKD
Enzyme 10 Gene Name NME4
Enzyme 10 Protein Sequence >Nucleoside diphosphate kinase, mitochondrial precursor 
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
Enzyme 10 Number of Residues 187
Enzyme 10 Molecular Weight 20659
Enzyme 10 Theoretical pI 10.75
Enzyme 10 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
—
Enzyme 10 General Function Nucleotide transport and metabolism
Enzyme 10 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP
Enzyme 10 Pathways
Enzyme 10 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-15
Enzyme 10 Transmembrane Regions Not Available
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 1945762 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID O00746 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name NDKM_HUMAN Link Image
Enzyme 10 PDB ID 1EHW Link Image
Enzyme 10 PDB File Show
Enzyme 10 3D Structure
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >564 bp 
ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCA
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
Enzyme 10 GenBank Gene ID Y07604 Link Image
Enzyme 10 GeneCard ID NME4 Link Image
Enzyme 10 GenAtlas ID NME4 Link Image
Enzyme 10 HGNC ID HGNC:7852 Link Image
Enzyme 10 Chromosome Location 16
Enzyme 10 Locus 16p13.3
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Milon L, Rousseau-Merck MF, Munier A, Erent M, Lascu I, Capeau J, Lacombe ML: nm23-H4, a new member of the family of human nm23/nucleoside diphosphate kinase genes localised on chromosome 16p13. Hum Genet. 1997 Apr;99(4):550-7. [PubMed Link Image]
  2. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  3. Milon L, Meyer P, Chiadmi M, Munier A, Johansson M, Karlsson A, Lascu I, Capeau J, Janin J, Lacombe ML: The human nm23-H4 gene product is a mitochondrial nucleoside diphosphate kinase. J Biol Chem. 2000 May 12;275(19):14264-72. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5340
Enzyme 11 Name Ribonucleoside-diphosphate reductase large subunit
Enzyme 11 Synonyms
  1. Ribonucleoside-diphosphate reductase M1 subunit
  2. Ribonucleotide reductase large chain
Enzyme 11 Gene Name RRM1
Enzyme 11 Protein Sequence >Ribonucleoside-diphosphate reductase large subunit 
MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLA
AETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKST
LDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHK
EDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCAL
ISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIY
LEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLD
EVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNL
GTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKI
IDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGAL
EASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIA
PMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQII
ACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKL
TSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCS
LENRDECLMCGS
Enzyme 11 Number of Residues 792
Enzyme 11 Molecular Weight 90071
Enzyme 11 Theoretical pI 7.16
Enzyme 11 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 11 General Function Nucleotide transport and metabolism
Enzyme 11 Specific Function Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides
Enzyme 11 Pathways
Enzyme 11 Reactions
  • 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 36065 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P23921 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name RIR1_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 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 11 GenBank Gene ID X59543 Link Image
Enzyme 11 GeneCard ID RRM1 Link Image
Enzyme 11 GenAtlas ID RRM1 Link Image
Enzyme 11 HGNC ID HGNC:10451 Link Image
Enzyme 11 Chromosome Location 11
Enzyme 11 Locus 11p15.5
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 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 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5341
Enzyme 12 Name Nucleoside diphosphate kinase A
Enzyme 12 Synonyms
  1. NDK A
  2. NDP kinase A
  3. Tumor metastatic process-associated protein
  4. Metastasis inhibition factor nm23
  5. nm23-H1
  6. Granzyme A-activated DNase
  7. GAAD
Enzyme 12 Gene Name NME1
Enzyme 12 Protein Sequence >Nucleoside diphosphate kinase A 
MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
Enzyme 12 Number of Residues 152
Enzyme 12 Molecular Weight 17149
Enzyme 12 Theoretical pI 6.11
Enzyme 12 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
—
Enzyme 12 General Function Nucleotide transport and metabolism
Enzyme 12 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP
Enzyme 12 Pathways
Enzyme 12 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • None
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 35068 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P15531 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name NDKA_HUMAN Link Image
Enzyme 12 PDB ID 1JXV Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >543 bp 
TGCTGCGAACCACGTGGGTCCCGGGCGCGTTTCGGGTGCTGGCGGCTGCAGCCGGAGTTC
AAACCTAAGCAGCTGGAAGGAACCATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAA
CCAGATGGGGTCCAGCGGGGTCTTGTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGA
TTCCGCCTTGTTGGTCTGAAATTCATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTAC
GTTGACCTGAAGGACCGTCCATTCTTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCG
GTAGTTGCCATGGTCTGGGAGGGGCTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGG
GAGACCAACCCTGCAGACTCCAAGCCTGGGACCATCCGTGGAGACTTCTGCATACAAGTT
GGCAGGAACATTATACATGGCAGTGATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTG
TGGTTTCACCCTGAGGAACTGGTAGATTACACGAGCTGTGCTCAGAACTGGATCTATGAA
TGA
Enzyme 12 GenBank Gene ID X17620 Link Image
Enzyme 12 GeneCard ID NME1 Link Image
Enzyme 12 GenAtlas ID NME1 Link Image
Enzyme 12 HGNC ID HGNC:7849 Link Image
Enzyme 12 Chromosome Location 17
Enzyme 12 Locus 17q21.3
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Rosengard AM, Krutzsch HC, Shearn A, Biggs JR, Barker E, Margulies IM, King CR, Liotta LA, Steeg PS: Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development. Nature. 1989 Nov 9;342(6246):177-80. [PubMed Link Image]
  2. Dooley S, Seib T, Engel M, Theisinger B, Janz H, Piontek K, Zang KD, Welter C: Isolation and characterization of the human genomic locus coding for the putative metastasis control gene nm23-H1. Hum Genet. 1994 Jan;93(1):63-6. [PubMed Link Image]
  3. Wang L, Patel U, Ghosh L, Chen HC, Banerjee S: Mutation in the nm23 gene is associated with metastasis in colorectal cancer. Cancer Res. 1993 Feb 15;53(4):717-20. [PubMed Link Image]
  4. Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed Link Image]
  5. Hailat N, Keim DR, Melhem RF, Zhu XX, Eckerskorn C, Brodeur GM, Reynolds CP, Seeger RC, Lottspeich F, Strahler JR, et al.: High levels of p19/nm23 protein in neuroblastoma are associated with advanced stage disease and with N-myc gene amplification. J Clin Invest. 1991 Jul;88(1):341-5. [PubMed Link Image]
  6. Manda R, Kohno T, Matsuno Y, Takenoshita S, Kuwano H, Yokota J: Identification of genes (SPON2 and C20orf2) differentially expressed between cancerous and noncancerous lung cells by mRNA differential display. Genomics. 1999 Oct 1;61(1):5-14. [PubMed Link Image]
  7. Min K, Song HK, Chang C, Kim SY, Lee KJ, Suh SW: Crystal structure of human nucleoside diphosphate kinase A, a metastasis suppressor. Proteins. 2002 Feb 15;46(3):340-2. [PubMed Link Image]
  8. Chen Y, Gallois-Montbrun S, Schneider B, Veron M, Morera S, Deville-Bonne D, Janin J: Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases. J Mol Biol. 2003 Sep 26;332(4):915-26. [PubMed Link Image]
  9. Fan Z, Beresford PJ, Oh DY, Zhang D, Lieberman J: Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Cell. 2003 Mar 7;112(5):659-72. [PubMed Link Image]
  10. Chang CL, Zhu XX, Thoraval DH, Ungar D, Rawwas J, Hora N, Strahler JR, Hanash SM, Radany E: Nm23-H1 mutation in neuroblastoma. Nature. 1994 Aug 4;370(6488):335-6. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5342
Enzyme 13 Name Nucleoside diphosphate kinase 7
Enzyme 13 Synonyms
  1. NDK 7
  2. NDP kinase 7
  3. nm23-H7
Enzyme 13 Gene Name NME7
Enzyme 13 Protein Sequence >Nucleoside diphosphate kinase 7 
MNHSERFVFIAEWYDPNASLLRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYDNLHLEDL
FIGNKVNVFSRQLVLIDYGDQYTARQLGSRKEKTLALIKPDAISKAGEIIEIINKAGFTI
TKLKMMMLSRKEALDFHVDHQSRPFFNELIQFITTGPIIAMEILRDDAICEWKRLLGPAN
SGVARTDASESIRALFGTDGIRNAAHGPDSFASAAREMELFFPSSGGCGPANTAKFTNCT
CCIVKPHAVSEGLLGKILMAIRDAGFEISAMQMFNMDRVNVEEFYEVYKGVVTEYHDMVT
EMYSGPCVAMEIQQNNATKTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLP
EDGLLEVQYFFKILDN
Enzyme 13 Number of Residues 376
Enzyme 13 Molecular Weight 42492
Enzyme 13 Theoretical pI 6.44
Enzyme 13 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
—
Enzyme 13 General Function Nucleotide transport and metabolism
Enzyme 13 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate
Enzyme 13 Pathways
Enzyme 13 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 4960169 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q9Y5B8 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name NDK7_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1131 bp 
ATGAATCATAGTGAAAGATTCGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
Enzyme 13 GenBank Gene ID AF153191 Link Image
Enzyme 13 GeneCard ID NME7 Link Image
Enzyme 13 GenAtlas ID NME7 Link Image
Enzyme 13 HGNC ID HGNC:20461 Link Image
Enzyme 13 Chromosome Location 1
Enzyme 13 Locus 1q24
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References Not Available
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5343
Enzyme 14 Name Ribonucleoside-diphosphate reductase M2 subunit
Enzyme 14 Synonyms
  1. Ribonucleotide reductase small subunit
  2. Ribonucleotide reductase small chain
Enzyme 14 Gene Name RRM2
Enzyme 14 Protein Sequence >Ribonucleoside-diphosphate reductase M2 subunit 
MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKT
KAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLK
PEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLI
DTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSF
ASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIE
QEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTN
FFEKRVGEYQRMGVMSSPTENSFTLDADF
Enzyme 14 Number of Residues 389
Enzyme 14 Molecular Weight 44878
Enzyme 14 Theoretical pI 5.05
Enzyme 14 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 14 General Function Nucleotide transport and metabolism
Enzyme 14 Specific Function Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides
Enzyme 14 Pathways
Enzyme 14 Reactions
  • 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • None
Enzyme 14 Transmembrane Regions
  • None
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 36155 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P31350 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name RIR2_HUMAN Link Image
Enzyme 14 PDB ID 1H0N Link Image
Enzyme 14 PDB File Show
Enzyme 14 3D Structure
Enzyme 14 Cellular Location Not Available
Enzyme 14 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 14 GenBank Gene ID X59618 Link Image
Enzyme 14 GeneCard ID RRM2 Link Image
Enzyme 14 GenAtlas ID RRM2 Link Image
Enzyme 14 HGNC ID HGNC:10452 Link Image
Enzyme 14 Chromosome Location 2
Enzyme 14 Locus 2p25-p24
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5344
Enzyme 15 Name Nucleoside diphosphate kinase B
Enzyme 15 Synonyms
  1. NDK B
  2. NDP kinase B
  3. nm23-H2
  4. C-myc purine-binding transcription factor PUF
Enzyme 15 Gene Name NME2
Enzyme 15 Protein Sequence >Nucleoside diphosphate kinase B 
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
Enzyme 15 Number of Residues 152
Enzyme 15 Molecular Weight 17298
Enzyme 15 Theoretical pI 8.69
Enzyme 15 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
—
Enzyme 15 General Function Nucleotide transport and metabolism
Enzyme 15 Specific Function Acts as a transcriptional activator of the c-Myc gene; binds DNA nonspecifically (Ref.3)
Enzyme 15 Pathways
Enzyme 15 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 4467843 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P22392 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name NDKB_HUMAN Link Image
Enzyme 15 PDB ID 1NSK Link Image
Enzyme 15 PDB File Show
Enzyme 15 3D Structure
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >459 bp 
ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
Enzyme 15 GenBank Gene ID X58965 Link Image
Enzyme 15 GeneCard ID NME2 Link Image
Enzyme 15 GenAtlas ID NME2 Link Image
Enzyme 15 HGNC ID HGNC:7850 Link Image
Enzyme 15 Chromosome Location 17
Enzyme 15 Locus 17q21.3
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed Link Image]
  2. Stahl JA, Leone A, Rosengard AM, Porter L, King CR, Steeg PS: Identification of a second human nm23 gene, nm23-H2. Cancer Res. 1991 Jan 1;51(1):445-9. [PubMed Link Image]
  3. Postel EH, Berberich SJ, Flint SJ, Ferrone CA: Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis. Science. 1993 Jul 23;261(5120):478-80. [PubMed Link Image]
  4. Webb PA, Perisic O, Mendola CE, Backer JM, Williams RL: The crystal structure of a human nucleoside diphosphate kinase, NM23-H2. J Mol Biol. 1995 Aug 25;251(4):574-87. [PubMed Link Image]
  5. Morera S, Lacombe ML, Xu Y, LeBras G, Janin J: X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution. Structure. 1995 Dec 15;3(12):1307-14. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5345
Enzyme 16 Name Nucleoside diphosphate kinase 3
Enzyme 16 Synonyms
  1. NDK 3
  2. NDP kinase 3
  3. Nucleoside diphosphate kinase C
  4. NDPKC
  5. nm23-H3
  6. DR-nm23
Enzyme 16 Gene Name NME3
Enzyme 16 Protein Sequence >Nucleoside diphosphate kinase 3 
MICLVLTIFANLFPAACTGAHERTFLAVKPDGVQRRLVGEIVRRFERKGFKLVALKLVQA
SEELLREHYAELRERPFYGRLVKYMASGPVVAMVWQGLDVVRTSRALIGATNPADAPPGT
IRGDFCIEVGKNLIHGSDSVESARREIALWFRADELLCWEDSAGHWLYE
Enzyme 16 Number of Residues 169
Enzyme 16 Molecular Weight 19015
Enzyme 16 Theoretical pI 7.97
Enzyme 16 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
—
Enzyme 16 General Function Nucleotide transport and metabolism
Enzyme 16 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Probably has a role in normal hematopoiesis by inhibition of granulocyte differentiation and induction of apoptosis
Enzyme 16 Pathways
Enzyme 16 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-19
Enzyme 16 Transmembrane Regions Not Available
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 1051256 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q13232 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name NDK3_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >507 bp 
ATGATCTGCCTGGTGCTGACCATCTTCGCTAACCTCTTCCCCGCGGCCTGCACCGGCGCA
CACGAACGCACCTTCCTGGCCGTGAAGCCGGACGGCGTGCAGCGGCGGCTGGTGGGCGAG
ATTGTGCGGCGCTTCGAGAGGAAGGGCTTCAAGTTGGTGGCGCTGAAGCTGGTGCAGTCC
TCCGAGGAGCTGCTGCGTGAGCACTACGCCGAGCTGCGTGAACGCCCGTTCTACGGCCGC
CTTGTCAAGTATATGGCCTCCGGGCCGGTGGTGGCCATGGTTTGGCAGGGGCTGGACGTG
GTGCGCACCTCGCGGGCGCTCATCGGAGCCACGAACCCGGCCGACGCCCCGCCCGGCACC
ATCCGCGGGGATTTCTGCATCGAGGTTGGCAACCTGATTCACGGCAGCGACTCGGTGGAG
AGTGCCCGCCGCGAGATCGCTCTCTGGTTCCGCGCAGACGAGCTCCTCTGCTGGGAGGAC
AGCGCTGGGCACTGGCTGTATGAGTAG
Enzyme 16 GenBank Gene ID U29656 Link Image
Enzyme 16 GeneCard ID NME3 Link Image
Enzyme 16 GenAtlas ID NME3 Link Image
Enzyme 16 HGNC ID HGNC:7851 Link Image
Enzyme 16 Chromosome Location 16
Enzyme 16 Locus 16q13
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Venturelli D, Martinez R, Melotti P, Casella I, Peschle C, Cucco C, Spampinato G, Darzynkiewicz Z, Calabretta B: Overexpression of DR-nm23, a protein encoded by a member of the nm23 gene family, inhibits granulocyte differentiation and induces apoptosis in 32Dc13 myeloid cells. Proc Natl Acad Sci U S A. 1995 Aug 1;92(16):7435-9. [PubMed Link Image]
  2. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5346
Enzyme 17 Name Nucleoside diphosphate kinase 6
Enzyme 17 Synonyms
  1. NDK 6
  2. NDP kinase 6
  3. nm23-H6
  4. Inhibitor of p53-induced apoptosis-alpha
  5. IPIA-alpha
Enzyme 17 Gene Name NME6
Enzyme 17 Protein Sequence >Nucleoside diphosphate kinase 6 
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA
Enzyme 17 Number of Residues 186
Enzyme 17 Molecular Weight 21142
Enzyme 17 Theoretical pI 8.49
Enzyme 17 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
—
Enzyme 17 General Function Nucleotide transport and metabolism
Enzyme 17 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Inhibitor of p53-induced apoptosis
Enzyme 17 Pathways
Enzyme 17 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-24
Enzyme 17 Transmembrane Regions Not Available
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 3228530 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID O75414 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name NDK6_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >561 bp 
ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA
Enzyme 17 GenBank Gene ID AF051941 Link Image
Enzyme 17 GeneCard ID NME6 Link Image
Enzyme 17 GenAtlas ID NME6 Link Image
Enzyme 17 HGNC ID HGNC:20567 Link Image
Enzyme 17 Chromosome Location 3
Enzyme 17 Locus 3p21
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Mehus JG, Deloukas P, Lambeth DO: NME6: a new member of the nm23/nucleoside diphosphate kinase gene family located on human chromosome 3p21.3. Hum Genet. 1999 Jun;104(6):454-9. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5442
Enzyme 18 Name Glucokinase
Enzyme 18 Synonyms
  1. Hexokinase-4
  2. Hexokinase type IV
  3. HK IV
  4. HK4
  5. Hexokinase-D
Enzyme 18 Gene Name GCK
Enzyme 18 Protein Sequence >Glucokinase 
MLDDRARMEAAKKEKVEQILAEFQLQEEDLKKVMRRMQKEMDRGLRLETHEEASVKMLPT
YVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEEGQWSVKTKHQMYSIPEDAMTGTAE
MLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNN
VVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDHQCEVGMIVGTGCNACYMEEMQN
VELVEGDEGRMCVNTEWGAFGDSGELDEFLLEYDRLVDESSANPGQQLYEKLIGGKYMGE
LVRLVLLRLVDENLLFHGEASEQLRTRGAFETRFVSQVESDTGDRKQIYNILSTLGLRPS
TTDCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFK
ERFHASVRRLTPSCEITFIESEEGSGRGAALVSAVACKKACMLGQ
Enzyme 18 Number of Residues 465
Enzyme 18 Molecular Weight 52192
Enzyme 18 Theoretical pI 4.85
Enzyme 18 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 18 General Function Not Available
Enzyme 18 Specific Function Catalyzes the initial step in utilization of glucose by the beta-cell and liver at physiological glucose concentration. Glucokinase has a high Km for glucose, and so it is effective only when glucose is abundant. The role of GCK is to provide G6P for the synthesis of glycogen. Pancreatic glucokinase plays an important role in modulating insulin secretion. Hepatic glucokinase helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage
Enzyme 18 Pathways
Enzyme 18 Reactions
  • ATP + D-glucose = ADP + D-glucose 6-phosphate
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 179427 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID P35557 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name HXK4_HUMAN Link Image
Enzyme 18 PDB ID 1V4T Link Image
Enzyme 18 PDB File Show
Enzyme 18 3D Structure
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1398 bp 
ATGCTGGACGACAGAGCCAGGATGGAGGCCGCCAAGAAGGAGAAGGTAGAGCAGATCCTG
GCAGAGTTCCAGCTGCAGGAGGAGGACCTGAAGAAGGTGATGAGACGGATGCAGAAGGAG
ATGGACCGCGGCCTGAGGCTGGAGACCCATGAAGAGGCCAGTGTGAAGATGCTGCCCACC
TACGTGCGCTCCACCCCAGAAGGCTCAGAAGTCGGGGACTTCCTCTCCCTGGACCTGGGT
GGCACTAACTTCAGGGTGATGCTGGTGAAGGTGGGAGAAGGTGAGGAGGGGCAGTGGAGC
GTGAAGACCAAACACCAGATGTACTCCATCCCCGAGGACGCCATGACCGGCACTGCTGAG
ATGCTCTTCGACTACATCTCTGAGTGCATCTCCGACTTCCTGGACAAGCATCAGATGAAA
CACAAGAAGCTGCCCCTGGGCTTCACCTTCTCCTTTCCTGTGAGGCACGAAGACATCGAT
AAGGGCATCCTTCTCAACTGGACCAAGGGCTTCAAGGCCTCAGGAGCAGAAGGGAACAAT
GTCGTGGGGCTTCTGCGAGACGCTATCAAACGGAGAGGGGACTTTGAAATGGATGTGGTG
GCAATGGTGAATGACACGGTGGCCACGATGATCTCCTGCTACTACGAAGACCATCAGTGC
GAGGTCGGCATGATCGTGGGCACGGGCTGCAATGCCTGCTACATGGAGGAGATGCAGAAT
GTGGAGCTGGTGGAGGGGGACGAGGGCCGCATGTGCGTCAATACCGAGTGGGGCGCCTTC
GGGGACTCCGGCGAGCTGGACGAGTTCCTGCTGGAGTATGACCGCCTGGTGGACGAGAGC
TCTGCAAACCCCGGTCAGCAGCTGTATGAGAAGCTCATAGGTGGCAAGTACATGGGCGAG
CTGGTGCGGCTTGTGCTGCTCAGGCTCGTGGACGAAAACCTGCTCTTCCACGGGGAGGCC
TCCGAGCAGCTGCGCACACGCGGAGCCTTCGAGACGCGCTTCGTGTCGCAGGTGGAGAGC
GACACGGGCGACCGCAAGCAGATCTACAACATCCTGAGCACGCTGGGGCTGCGACCCTCG
ACCACCGACTGCGACATCGTGCGCCGCGCCTGCGAGAGCGTGTCTACGCGCGCTGCGCAC
ATGTGCTCGGCGGGGCTGGCGGGCGTCATCAACCGCATGCGCGAGAGCCGCAGCGAGGAC
GTAATGCGCATCACTGTGGGCGTGGATGGCTCCGTGTACAAGCTGCACCCCAGCTTCAAG
GAGCGGTTCCATGCCAGCGTGCGCAGGCTGACGCCCAGCTGCGAGATCACCTTCATCGAG
TCGGAGGAGGGCAGTGGCCGGGGCGCGGCCCTGGTCTCGGCGGTGGCCTGTAAGAAGGCC
TGTATGCTGGGCCAGTGA
Enzyme 18 GenBank Gene ID M88011 Link Image
Enzyme 18 GeneCard ID GCK Link Image
Enzyme 18 GenAtlas ID GCK Link Image
Enzyme 18 HGNC ID HGNC:4195 Link Image
Enzyme 18 Chromosome Location 7
Enzyme 18 Locus 7p15.3-p15.1
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Tanizawa Y, Matsutani A, Chiu KC, Permutt MA: Human glucokinase gene: isolation, structural characterization, and identification of a microsatellite repeat polymorphism. Mol Endocrinol. 1992 Jul;6(7):1070-81. [PubMed Link Image]
  2. Tanizawa Y, Koranyi LI, Welling CM, Permutt MA: Human liver glucokinase gene: cloning and sequence determination of two alternatively spliced cDNAs. Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):7294-7. [PubMed Link Image]
  3. Nishi S, Stoffel M, Xiang K, Shows TB, Bell GI, Takeda J: Human pancreatic beta-cell glucokinase: cDNA sequence and localization of the polymorphic gene to chromosome 7, band p 13. Diabetologia. 1992 Aug;35(8):743-7. [PubMed Link Image]
  4. Koranyi LI, Tanizawa Y, Welling CM, Rabin DU, Permutt MA: Human islet glucokinase gene. Isolation and sequence analysis of full-length cDNA. Diabetes. 1992 Jul;41(7):807-11. [PubMed Link Image]
  5. Stoffel M, Froguel P, Takeda J, Zouali H, Vionnet N, Nishi S, Weber IT, Harrison RW, Pilkis SJ, Lesage S, et al.: Human glucokinase gene: isolation, characterization, and identification of two missense mutations linked to early-onset non-insulin-dependent (type 2) diabetes mellitus. Proc Natl Acad Sci U S A. 1992 Aug 15;89(16):7698-702. [PubMed Link Image]
  6. Sakura H, Eto K, Kadowaki H, Simokawa K, Ueno H, Koda N, Fukushima Y, Akanuma Y, Yazaki Y, Kadowaki T: Structure of the human glucokinase gene and identification of a missense mutation in a Japanese patient with early-onset non-insulin-dependent diabetes mellitus. J Clin Endocrinol Metab. 1992 Dec;75(6):1571-3. [PubMed Link Image]
  7. St Charles R, Harrison RW, Bell GI, Pilkis SJ, Weber IT: Molecular model of human beta-cell glucokinase built by analogy to the crystal structure of yeast hexokinase B. Diabetes. 1994 Jun;43(6):784-91. [PubMed Link Image]
  8. Stoffel M, Patel P, Lo YM, Hattersley AT, Lucassen AM, Page R, Bell JI, Bell GI, Turner RC, Wainscoat JS: Missense glucokinase mutation in maturity-onset diabetes of the young and mutation screening in late-onset diabetes. Nat Genet. 1992 Oct;2(2):153-6. [PubMed Link Image]
  9. Chiu KC, Tanizawa Y, Permutt MA: Glucokinase gene variants in the common form of NIDDM. Diabetes. 1993 Apr;42(4):579-82. [PubMed Link Image]
  10. Stoffel M, Bell KL, Blackburn CL, Powell KL, Seo TS, Takeda J, Vionnet N, Xiang KS, Gidh-Jain M, Pilkis SJ, et al.: Identification of glucokinase mutations in subjects with gestational diabetes mellitus. Diabetes. 1993 Jun;42(6):937-40. [PubMed Link Image]
  11. Takeda J, Gidh-Jain M, Xu LZ, Froguel P, Velho G, Vaxillaire M, Cohen D, Shimada F, Makino H, Nishi S, et al.: Structure/function studies of human beta-cell glucokinase. Enzymatic properties of a sequence polymorphism, mutations associated with diabetes, and other site-directed mutants. J Biol Chem. 1993 Jul 15;268(20):15200-4. [PubMed Link Image]
  12. Gidh-Jain M, Takeda J, Xu LZ, Lange AJ, Vionnet N, Stoffel M, Froguel P, Velho G, Sun F, Cohen D, et al.: Glucokinase mutations associated with non-insulin-dependent (type 2) diabetes mellitus have decreased enzymatic activity: implications for structure/function relationships. Proc Natl Acad Sci U S A. 1993 Mar 1;90(5):1932-6. [PubMed Link Image]
  13. Hager J, Blanche H, Sun F, Vaxillaire NV, Poller W, Cohen D, Czernichow P, Velho G, Robert JJ, Cohen N, et al.: Six mutations in the glucokinase gene identified in MODY by using a nonradioactive sensitive screening technique. Diabetes. 1994 May;43(5):730-3. [PubMed Link Image]
  14. Velho G, Blanche H, Vaxillaire M, Bellanne-Chantelot C, Pardini VC, Timsit J, Passa P, Deschamps I, Robert JJ, Weber IT, Marotta D, Pilkis SJ, Lipkind GM, Bell GI, Froguel P: Identification of 14 new glucokinase mutations and description of the clinical profile of 42 MODY-2 families. Diabetologia. 1997 Feb;40(2):217-24. [PubMed Link Image]
  15. Hattersley AT, Beards F, Ballantyne E, Appleton M, Harvey R, Ellard S: Mutations in the glucokinase gene of the fetus result in reduced birth weight. Nat Genet. 1998 Jul;19(3):268-70. [PubMed Link Image]
  16. Glaser B, Kesavan P, Heyman M, Davis E, Cuesta A, Buchs A, Stanley CA, Thornton PS, Permutt MA, Matschinsky FM, Herold KC: Familial hyperinsulinism caused by an activating glucokinase mutation. N Engl J Med. 1998 Jan 22;338(4):226-30. [PubMed Link Image]
  17. Ng MC, Cockburn BN, Lindner TH, Yeung VT, Chow CC, So WY, Li JK, Lo YM, Lee ZS, Cockram CS, Critchley JA, Bell GI, Chan JC: Molecular genetics of diabetes mellitus in Chinese subjects: identification of mutations in glucokinase and hepatocyte nuclear factor-1alpha genes in patients with early-onset type 2 diabetes mellitus/MODY. Diabet Med. 1999 Nov;16(11):956-63. [PubMed Link Image]
  18. Nam JH, Lee HC, Kim YH, Cha BS, Song YD, Lim SK, Kim KR, Huh KB: Identification of glucokinase mutation in subjects with post-renal transplantation diabetes mellitus. Diabetes Res Clin Pract. 2000 Dec;50(3):169-76. [PubMed Link Image]
  19. Njolstad PR, Sovik O, Cuesta-Munoz A, Bjorkhaug L, Massa O, Barbetti F, Undlien DE, Shiota C, Magnuson MA, Molven A, Matschinsky FM, Bell GI: Neonatal diabetes mellitus due to complete glucokinase deficiency. N Engl J Med. 2001 May 24;344(21):1588-92. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5444
Enzyme 19 Name Hexokinase-3
Enzyme 19 Synonyms
  1. Hexokinase type III
  2. HK III
Enzyme 19 Gene Name HK3
Enzyme 19 Protein Sequence >Hexokinase-3 
MDSIGSSGLRQGEETLSCSEEGLPGPSDSSELVQECLQQFKVTRAQLQQIQASLLGSMEQ
ALRGQASPAPAVRMLPTYVGSTPHGTEQGDFVVLELGATGASLRVLWVTLTGIEGHRVEP
RSQEFVIPQEVMLGAGQQLFDFAAHCLSEFLDAQPVNKQGLQLGFSFSFPCHQTGLDRST
LISWTKGFRCSGVEGQDVVQLLRDAIRRQGAYNIDVVAVVNDTVGTMMGCEPGVRPCEVG
LVVDTGTNACYMEEARHVAVLDEDRGRVCVSVEWGSLSDDGALGPVLTTFDHTLDHESLN
PGAQRFEKMIGGLYLGELVRLVLAHLARCGVLFGGCTSPALLSQGSILLEHVAEMEDPST
GAARVHAILQDLGLSPGASDVELVQHVCAAVCTRAAQLCAAALAAVLSCLQHSREQQTLQ
VAVATGGRVCERHPRFCSVLQGTVMLLAPECDVSLIPSVDGGGRGVAMVTAVAARLAAHR
RLLEETLAPFRLNHDQLAAVQAQMRKAMAKGLRGEASSLRMLPTFVRATPDGSERGDFLA
LDLGGTNFRVLLVRVTTGVQITSEIYSIPETVAQGSGQQLFDHIVDCIVDFQQKQGLSGQ
SLPLGFTFSFPCRQLGLDQGILLNWTKGFKASDCEGQDVVSLLREAITRRQAVELNVVAI
VNDTVGTMMSCGYEDPRCEIGLIVGTGTNACYMEELRNVAGVPGDSGRMCINMEWGAFGD
DGSLAMLSTRFDASVDQASINPGKQRFEKMISGMYLGEIVRHILLHLTSLGVLFRGQQIQ
RLQTRDIFKTKFLSEIESDSLALRQVRAILEDLGLPLTSDDALMVLEVCQAVSQRAAQLC
GAGVAAVVEKIRGNRGLEELAVSVGVDGTLYKLHPRFSSLVAATVRELAPRCVVTFLQSE
DGSGKGAALVTAVACRLAQLTRV
Enzyme 19 Number of Residues 923
Enzyme 19 Molecular Weight 98921
Enzyme 19 Theoretical pI 5.11
Enzyme 19 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 19 Pathways
Enzyme 19 Reactions
  • ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 1255788 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID P52790 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name HXK3_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >2772 bp 
ATGGACTCCATTGGGTCTTCAGGGTTGCGGCAGGGGGAAGAAACCCTGAGTTGCTCTGAG
GAGGGCTTGCCCGGGCCCTCAGACAGCTCAGAGCTGGTGCAGGAGTGCCTGCAGCAGTTC
AAGGTGACAAGGGCACAGCTACAGCAGATCCAAGCCAGCCTCTTGGGTTCCATGGAGCAG
GCGCTGAGGGGACAGGCCAGCCCTGCCCCTGCGGTCCGGATGCTGCCTACATACGTGGGG
TCCACCCCACATGGCACTGAGCAAGGAGACTTCGTGGTGCTGGAGCTGGGGGCCACAGGG
GCCTCACTGCGTGTTTTGTGGGTGACTCTAACTGGCATTGAGGGGCATAGGGTGGAGCCC
AGAAGCCAGGAGTTTGTGATCCCCCAAGAGGTGATGCTGGGTGCTGGCCAGCAGCTCTTT
GACTTTGCTGCCCACTGCCTGTCTGAGTTCCTGGATGCGCAGCCTGTGAACAAACAGGGT
CTGCAGCTTGGCTTCAGCTTCTCTTTCCCTTGTCACCAGACGGGCTTGGACAGGAGCACC
CTCATTTCCTGGACCAAAGGTTTTAGGTGCAGTGGTGTGGAAGGCCAGGATGTGGTCCAG
CTGCTGAGAGATGCCATTCGGAGGCAGGGGGCCTACAACATCGACGTGGTTGCTGTGGTG
AACGACACAGTGGGCACCATGATGGGCTGTGAGCCGGGGGTCAGGCCGTGTGAGGTTGGG
CTAGTTGTAGACACGGGCACCAACGCGTGTTACATGGAGGAGGCACGGCATGTGGCAGTG
CTGGACGAAGACCGGGGCCGCGTCTGCGTCAGCGTCGAGTGGGGCTCCTTAAGCGATGAT
GGGGCGCTGGGACCAGTGCTGACCACCTTCGACCATACCCTGGACCATGAGTCCCTGAAT
CCTGGTGCTCAGAGGTTTGAGAAGATGATCGGAGGCCTGTACCTGGGTGAGCTGGTGCGG
CTGGTGCTGGCTCACTTGGCCCGGTGTGGGGTCCTCTTTGGTGGCTGCACCTCCCCTGCC
CTGCTGAGCCAAGGCAGCATCCTCCTGGAACACGTGGCTGAGATGGAGGACCCCTCTACT
GGGGCAGCCCGTGTCCATGCTATCCTGCAGGACTTGGGCCTGAGCCCTGGGGCTTCGGAT
GTTGAGCTTGTGCAGCACGTCTGTGCGGCCGTGTGCACGCGGGCTGCCCAGCTCTGTGCT
GCCGCCCTGGCCGCTGTTCTCTCCTGCCTCCAGCACAGCCGGGAGCAACAAACACTCCAG
GTTGCTGTGGCCACCGGAGGCCGAGTGTGTGAGCGGCACCCCAGGTTCTGCAGCGTCCTG
CAGGGGACAGTGATGCTCCTGGCCCCGGAATGCGATGTCTCCTTAATCCCCTCTGTGGAT
GGTGGTGGCCGGGGAGTGGCGATGGTGACTGCTGTGGCTGCCCGTCTGGCTGCCCACCGG
CGCCTGCTGGAGGAGACCCTGGCCCCATTCCGGTTGAACCATGATCAACTGGCTGCGGTT
CAGGCACAGATGCGGAAGGCCATGGCCAAGGGGCTCCGAGGGGAGGCCTCCTCCCTTCGC
ATGCTGCCCACTTTCGTCCGGGCCACCCCTGACGGCAGCGAGCGAGGGGATTTCCTGGCC
CTGGACCTCGGGGGCACGAACTTCCGTGTCCTCCTGGTACGTGTGACCACAGGCGTGCAG
ATCACCAGCGAGATCTACTCCATTCCCGAGACTGTGGCCCAGGGTTCTGGGCAGCAGCTC
TTTGACCACATCGTGGACTGCATCGTGGACTTCCAGCAGAAGCAGGGCCTGAGCGGGCAG
AGCCTCCCACTGGGTTTTACCTTCTCCTTCCCATGTAGGCAGCTTGGCCTAGACCAGGGC
ATCCTCCTGAACTGGACCAAGGGTTTCAAGGCATCAGACTGCGAGGGCCAAGATGTCGTG
AGTCTGTTGCGGGAAGCCATCACTCGCAGACAGGCAGTGGAGCTGAATGTGGTTGCCATT
GTCAATGACACGGTGGGGACCATGATGTCCTGTGGCTATGAGGACCCCCGTTGCGAGATA
GGCCTCATTGTCGGAACCGGCACCAATGCCTGCTACATGGAGGAGCTCCGGAATGTGGCG
GGCGTGCCTGGGGACTCAGGCCGCATGTGCATCAACATGGAGTGGGGCGCCTTTGGGGAC
GATGGCTCTCTGGCCATGCTCAGCACCCGCTTTGATGCAAGTGTGGACCAGGCGTCCATC
AACCCCGGCAAGCAGAGGTTTGAAAAGATGATCAGCGGCATGTACCTGGGGGAGATCGTC
CGCCACATCCTTTTACATTTAACCAGCCTTGGCGTTCTCTTCCGGGGCCAGCAGATCCAG
CGCCTTCAGACCAGGGACATCTTCAAGACCAAGTTCCTCTCTGAGATCGAAAGTGACAGC
CTGGCCCTGCGGCAGGTCCGAGCCATCCTAGAGGATCTGGGGCTACCCCTGACCTCAGAT
GACGCCCTGATGGTGCTAGAGGTGTGCCAGGCTGTGTCCCAGAGGGCTGCCCAGCTCTGT
GGGGCGGGTGTAGCTGCCGTGGTGGAGAAGATCCGGGGGAACCGGGGCCTGGAAGAGCTG
GCAGTGTCTGTGGGGGTGGATGGAACGCTCTACAAGCTGCACCCGCGCTTCTCCAGCCTG
GTGGCGGCCACAGTGCGGGAGCTGGCCCCTCGCTGTGTGGTCACGTTCCTGCAGTCAGAG
GATGGGTCCGGCAAAGGTGCGGCCCTGGTCACCGCTGTTGCCTGCCGCCTTGCGCAGTTG
ACTCGTGTCTGA
Enzyme 19 GenBank Gene ID U51333 Link Image
Enzyme 19 GeneCard ID HK3 Link Image
Enzyme 19 GenAtlas ID HK3 Link Image
Enzyme 19 HGNC ID HGNC:4925 Link Image
Enzyme 19 Chromosome Location 5
Enzyme 19 Locus 5q35.2
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Furuta H, Nishi S, Le Beau MM, Fernald AA, Yano H, Bell GI: Sequence of human hexokinase III cDNA and assignment of the human hexokinase III gene (HK3) to chromosome band 5q35.2 by fluorescence in situ hybridization. Genomics. 1996 Aug 15;36(1):206-9. [PubMed Link Image]
  2. Palma F, Agostini D, Mason P, Dacha M, Piccoli G, Biagiarelli B, Fiorani M, Stocchi V: Purification and characterization of the carboxyl-domain of human hexokinase type III expressed as fusion protein. Mol Cell Biochem. 1996 Feb 9;155(1):23-9. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5445
Enzyme 20 Name Hexokinase-2
Enzyme 20 Synonyms
  1. Hexokinase type II
  2. HK II
  3. Muscle form hexokinase
Enzyme 20 Gene Name HK2
Enzyme 20 Protein Sequence >Hexokinase-2 
MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLGATTHPTAA
VKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLWVKVTDNGLQKVEMENQIYAIPEDIMR
GSGTQLFDHIAECLANFMDKLQIKDKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGV
EGRDVVALIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDHNCEIGLIVGTGSNACYME
EMRHIDMVEGDEGRMCINMEWGAFGDDGSLNDIRTEFDQEIDMGSLNPGKQLFEKMISGM
YMGELVRLILVKMAKEELLFGGKLSPELLNTGRFETKDISDIEGEKDGIRKAREVLMRLG
LDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKH
PHFAKRLHKTVRRLVPGCDVRFLRSEDGSGKGAAMVTAVAYRLADQHRARQKTLEHLQLS
HDQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRV
LLVRVRNGKWGGVEMHNKIYAIPQEVMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGF
TFSFPCQQNSLDESILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVG
TMMTCGFEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNMEWGAFGDNGCLDD
FRTEFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRG
IFETKFLSQIESDCLALLQVRAILQHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAA
VVDRIRENRGLDALKVTVGVDGTLYKLHPHFAKVMHETVKDLAPKCDVSFLQSEDGSGKG
AALITAVACRIREAGQR
Enzyme 20 Number of Residues 917
Enzyme 20 Molecular Weight 102381
Enzyme 20 Theoretical pI 5.93
Enzyme 20 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 20 General Function Not Available
Enzyme 20 Specific Function ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 20 Pathways
Enzyme 20 Reactions
  • ATP + D-hexose = ADP + D-hexose 6-phosphate
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • None
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 587202 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P52789 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name HXK2_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >2754 bp 
ATGATTGCCTCGCATCTGCTTGCCTACTTCTTCACGGAGCTCAACCATGACCAAGTGCAG
AAGGTTGACCAGTATCTCTACCACATGCGCCTCTCTGATGAGACCCTCTTGGAGATCTCT
AAGCGGTTCCGCAAGGAGATGGAGAAAGGGCTTGGAGCCACCACTCACCCTACTGCAGCA
GTGAAGATGCTGCCCACCTTTGTGAGGTCCACTCCAGATGGGACAGAACACGGAGAGTTC
CTGGCTCTGGATCTTGGAGGGACCAACTTCCGTGTGCTTTGGGTGAAAGTAACGGACAAT
GGGCTCCAGAAGGTGGAGATGGAGAATCAGATCTATGCCATCCCTGAGGACATCATGCGA
GGCAGTGGCACCCAGCTGTTTGACCACATTGCCGAATGCCTGGCTAACTTCATGGATAAG
CTACAAATCAAAGACAAGAAGCTCCCACTGGGTTTTACCTTCTCGTTCCCCTGCCACCAG
ACTAAACTAGACGAGAGTTTCCTGGTCTCATGGACCAAGGGATTCAAGTCCAGTGGAGTG
GAAGGCAGAGACGTTGTGGCTCTGATCCGGAAGGCCATCCAGAGGAGAGGGGACTTTGAT
ATCGACATTGTGGCTGTGGTGAATGACACAGTTGGGACCATGATGACCTGTGGTTATGAT
GACCACAACTGTGAGATTGGTCTCATTGTGGGCACGGGCAGCAACGCCTGCTACATGGAA
GAGATGCGCCACATCGACATGGTGGAAGGCGATGAGGGGCGGATGTGTATCAATATGGAG
TGGGGGGCCTTCGGGGACGATGGCTCGCTCAACGACATTCGCACTGAGTTTGACCAGGAG
ATTGACATGGGCTCACTGAACCCGGGAAAGCAACTGTTTGAGAAGATGATCAGTGGGATG
TACATGGGGGAGCTGGTGAGGCTTATCCTGGTGAAGATGGCCAAGGAGGAGCTGCTCTTT
GGGGGGAAGCTCAGCCCAGAGCTTCTCAACACCGGTCGCTTTGAGACCAAAGACATCTCA
GACATTGAAGGGGAGAAGGATGGCATCCGGAAGGCCCGTGAGGTCCTGATGCGGTTGGGC
CTGGACCCGACTCAGGAGGACTGCGTGGCCACTCACCGGATCTGCCAGATCGTGTCCACA
CGCTCCGCCAGCCTGTGCGCAGCCACCCTGGCCGCCGTGCTGCAGCGCATCAAGGAGAAC
AAAGGCGAGGAGCGGCTGCGCTCTACTATTGGGGTCGACGGTTCCGTCTACAAGAAACAC
CCCCATTTTGCCAAGCGTCTACATAAGACCGTGCGGCGGCTGGTGCCCGGCTGCGATGTC
CGCTTCCTCCGCTCCGAGGATGGCAGTGGCAAAGGTGCAGCCATGGTGACAGCAGTGGCT
TACCGGCTGGCCGATCAACACCGTGCCCGCCAGAAGACATTAGAGCATCTGCAGCTGAGC
CATGACCAGCTGCTGGAGGTCAAGAGGAGGATGAAGGTAGAAATGGAGCGAGGTCTGAGC
AAGGAGACTCATGCCAGTGCCCCCGTCAAGATGCTGCCCACCTACGTGTGTGCTACCCCG
GACGGCACAGAGAAAGGGGACTTCTTGGCCTTGGACCTTGGAGGAACAAATTTCCGGGTC
CTGCTGGTCCGTGTTCGGAATGGGAAGTGGGGTGGAGTGGAGATGCACAACAAGATCTAC
GCCATCCCGCAGGAGGTCATGCACGGCACCGGGGACGAGCTCTTTGACCACATTGTCCAG
TGCATCGCGGACTTCCTCGAGTACATGGGCATGAAGGGCGTGTCCCTGCCTCTGGGTTTT
ACCTTCTCCTTCCCCTGCCAGCAGAACAGCCTGGACGAGAGCATCCTCCTCAAGTGGACA
AAAGGCTTCAAGGCATCTGGCTGCGAGGGCGAGGACGTGGTGACCCTGCTGAAGGAAGCG
ATCCACCGGCGAGAGGAGTTTGACCTGGATGTGGTTGCTGTGGTGAACGACACAGTCGGA
ACTATGATGACCTGTGGCTTTGAAGACCCTCACTGTGAAGTTGGCCTCATTGTTGGCACG
GGCAGCAATGCCTGCTACATGGAGGAGATGCGCAACGTGGAACTGGTGGAAGGAGAAGAG
GGGCGGATGTGTGTGAACATGGAATGGGGGGCCTTCGGGGACAATGGATGCCTAGATGAC
TTCCGCACAGAATTTGATGTGGCTGTGGATGAGCTTTCACTCAACCCCGGCAAGCAGAGG
TTCGAGAAAATGATCAGTGGAATGTACCTGGGTGAGATTGTCCGTAACATTCTCATCGAT
TTCACCAAGCGTGGACTACTCTTCCGAGGCCGCATCTCAGAGCGGCTCAAGACAAGGGGC
ATCTTTGAAACCAAGTTCTTGTCTCAGATTGAGAGTGACTGCCTGGCCCTGCTGCAAGTC
CGAGCCACCCTGCAACACTTAGGGCTTGAGAGCACCTGTGACGACAGCATCATTGTTAAG
GAGGTGTGCACTGTGGTGGCCCGGCGGGCAGCCCAGCTCTGTGGCGCAGGCATGGCCGCT
GTGGTGGACAGGATACGAGAAAACCGTGGGCTGGACGCTCTCAAAGTGACAGTGGGTGTG
GATGGGACCCTCTACAAGCTACATCCTCACTTTGCCAAAGTCATGCATGAGACAGTGAAG
GACCTGGCTCCGAAATGTGATGTGTCTTTCCTGCAGTCAGAGGATGGCAGCGGGAAGGGG
GCGGCGCTCATCACTGCTGTGGCCTGCCGCATCCGTGAGGCTGGACAGCGATAG
Enzyme 20 GenBank Gene ID Z46376 Link Image
Enzyme 20 GeneCard ID HK2 Link Image
Enzyme 20 GenAtlas ID HK2 Link Image
Enzyme 20 HGNC ID HGNC:4923 Link Image
Enzyme 20 Chromosome Location 2
Enzyme 20 Locus 2p13
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Lehto M, Huang X, Davis EM, Le Beau MM, Laurila E, Eriksson KF, Bell GI, Groop L: Human hexokinase II gene: exon-intron organization, mutation screening in NIDDM, and its relationship to muscle hexokinase activity. Diabetologia. 1995 Dec;38(12):1466-74. [PubMed Link Image]
  2. Deeb SS, Malkki M, Laakso M: Human hexokinase II: sequence and homology to other hexokinases. Biochem Biophys Res Commun. 1993 Nov 30;197(1):68-74. [PubMed Link Image]
  3. Shinohara Y, Yamamoto K, Kogure K, Ichihara J, Terada H: Steady state transcript levels of the type II hexokinase and type 1 glucose transporter in human tumor cell lines. Cancer Lett. 1994 Jul 15;82(1):27-32. [PubMed Link Image]
  4. Laakso M, Malkki M, Deeb SS: Amino acid substitutions in hexokinase II among patients with NIDDM. Diabetes. 1995 Mar;44(3):330-4. [PubMed Link Image]
  5. Vidal-Puig A, Printz RL, Stratton IM, Granner DK, Moller DE: Analysis of the hexokinase II gene in subjects with insulin resistance and NIDDM and detection of a Gln142-->His substitution. Diabetes. 1995 Mar;44(3):340-6. [PubMed Link Image]
  6. Echwald SM, Bjorbaek C, Hansen T, Clausen JO, Vestergaard H, Zierath JR, Printz RL, Granner DK, Pedersen O: Identification of four amino acid substitutions in hexokinase II and studies of relationships to NIDDM, glucose effectiveness, and insulin sensitivity. Diabetes. 1995 Mar;44(3):347-53. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5465
Enzyme 21 Name Diacylglycerol kinase alpha
Enzyme 21 Synonyms
  1. Diglyceride kinase alpha
  2. DGK-alpha
  3. DAG kinase alpha
  4. 80 kDa diacylglycerol kinase
Enzyme 21 Gene Name DGKA
Enzyme 21 Protein Sequence >Diacylglycerol kinase alpha 
MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAKYVQGDAIGYEGFQQFLKIY
LEVDNVPRHLSLALFQSFETGHCLNETNVTKDVVCLNDVSCYFSLLEGGRPEDKLEFTFK
LYDTDRNGILDSSEVDKIILQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSQAEW
VRAGATTVPLLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKY
TVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLTGLHC
VWCHLEIHDDCLQAVGHECDCGLLRDHILPPSSIYPSVLASGPDRKNSKTSQKTMDDLNL
STSEALRIDPVPNTHPLLVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRL
FKDVPDSRILVCGGDGTVGWILETIDKANLPVLPPVAVLPLGTGNDLARCLRWGGGYEGQ
NLAKILKDLEMSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIM
REKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVL
NIPSMHGGSNLWGDTRRPHGDIYGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLE
GAIEMGQIYTKLKNAGRRLAKCSEITFHTTKTLPMQIDVEPWMQTPCTIKITHKNQMPML
MGPPPRSTNFFGFLS
Enzyme 21 Number of Residues 735
Enzyme 21 Molecular Weight 82673
Enzyme 21 Theoretical pI 6.71
Enzyme 21 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • diacylglycerol kinase activity
  • ion binding
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • intracellular signaling cascade
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 21 General Function Not Available
Enzyme 21 Specific Function Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity
Enzyme 21 Pathways
Enzyme 21 Reactions
  • ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 30823 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID P23743 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name DGKA_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >2208 bp 
ATGGCCAAGGAGAGGGGCCTAATAAGCCCCAGTGATTTTGCCCAGCTGCAAAAATACATG
GAATACTCCACCAAAAAGGTCAGTGATGTCCTAAAGCTCTTCGAGGATGGCGAGATGGCT
AAATATGTCCAAGGAGATGCCATTGGGTACGAGGGATTCCAGCAATTCCTGAAAATCTAT
CTCGAAGTGGATAATGTTCCCAGACACCTAAGCCTGGCACTGTTTCAATCCTTTGAGACT
GGTCACTGCTTAAATGAGACAAATGTGACAAAAGATGTGGTGTGTCTCAATGATGTTTCC
TGCTACTTTTCCCTTCTGGAGGGTGGTCGGCCAGAAGACAAGTTAGAATTCACCTTCAAG
CTGTACGACACGGACAGAAATGGGATCCTGGACAGCTCAGAAGTGGACAAAATTATCCTA
CAGATGATGCGAGTGGCTGAATACCTGGATTGGGATGTGTCTGAGCTGAGGCCGATTCTT
CAGGAGATGATGAAAGAGATTGACTATGATGGCAGTGGCTCTGTCTCTCAAGCTGAGTGG
GTCCGGGCTGGGGCCACCACCGTGCCACTGCTAGTGCTGCTGGGTCTGGAGATGACTCTG
AAGGACGACGGACAGCACATGTGGAGGCCCAAGAGGTTCCCCAGACCAGTCTACTGCAAT
CTGTGCGAGTCAAGCATTGGTCTTGGCAAACAGGGACTGAGCTGTAACCTCTGTAAGTAC
ACTGTTCACGACCAGTGTGCCATGAAAGCCCTGCCTTGTGAAGTCAGCACCTATGCCAAG
TCTCGGAAGGACATTGGTGTCCAATCACATGTGTGGGTGCGAGGAGGCTGTGAGTCCGGG
CGCTGCGACCGCTGTCAGAAAAAGATCCGGATCTACCACAGTCTGACCGGGCTGCATTGT
GTATGGTGCCACCTAGAGATCCACGATGACTGCCTGCAAGCGGTGGGCCATGAGTGTGAC
TGTGGGCTGCTCCGGGATCACATCCTGCCTCCATCTTCCATCTATCCCAGTGTCCTGGCC
TCTGGACCGGATCGTAAAAATAGCAAAACAAGCCAGAAGACCATGGATGATTTAAATTTG
AGCACCTCTGAGGCTCTGCGGATTGACCCTGTTCCTAACACCCACCCACTTCTCGTCTTT
GTCAATCCTAAGAGTGGCGGGAAGCAGGGGCAGAGGGTGCTCTGGAAGTTCCAGTATATA
TTAAACCCTCGACAGGTGTTCAACCTCCTAAAGGATGGTCCTGAGATAGGGCTCCGATTA
TTCAAGGATGTTCCTGATAGCCGGATTTTGGTGTGTGGTGGAGACGGCACAGTAGGCTGG
ATTCTAGAGACCATTGACAAAGCTAACTTGCCAGTTTTGCCTCCTGTTGCTGTGTTGCCC
CTGGGTACTGGAAATGATCTGGCTCGATGCCTAAGATGGGGAGGAGGTTATGAAGGACAG
AATCTGGCAAAGATCCTCAAGGATTTAGAGATGAGTAAAGTGGTACATATGGATCGATGG
TCTGTGGAGGTGATACCTCAACAAACTGAAGAAAAAAGTGACCCAGTCCCCTTTCAAATC
ATCAATAACTACTTCTCTATTGGCGTGGATGCCTCTATTGCTCATCGATTCCACATCATG
CGAGAGAAATATCCGGAGAAGTTCAACAGCAGAATGAAGAACAAGCTATGGTACTTCGAA
TTTGCCACATCTGAATCCATCTTCTCAACATGCAAAAAGCTGGAGGAGTCTTTGACAGTT
GAGATCTGTGGGAAACCGCTGGATCTGAGCAACCTGTCCCTAGAAGGCATCGCAGTGCTA
AACATCCCTAGCATGCATGGTGGCTCCAACCTCTGGGGTGATACCAGGAGACCCCATGGG
GATATCTATGGGATCAACCAGGCCTTAGGTGCTACAGCTAAAGTCATCACCGACCCTGAT
ATCCTGAAAACCTGTGTACCAGACCTAAGTGACAAGAGACTGGAAGTGGTTGGGCTGGAG
GGTGCAATTGAGATGGGCCAAATCTATACCAAGCTCAAGAATGCTGGACGTCGGCTGGCC
AAGTGCTCTGAGATCACCTTCCACACCACAAAAACCCTTCCCATGCAAATTGACGTAGAA
CCCTGGATGCAGACGCCCTGTACAATCAAGATCACCCACAAGAACCAGATGCCCATGCTC
ATGGGCCCACCCCCCCGCTCCACCAATTTCTTTGGCTTCTTGAGCTAA
Enzyme 21 GenBank Gene ID X62535 Link Image
Enzyme 21 GeneCard ID DGKA Link Image
Enzyme 21 GenAtlas ID DGKA Link Image
Enzyme 21 HGNC ID HGNC:2849 Link Image
Enzyme 21 Chromosome Location 12
Enzyme 21 Locus 12q13.3
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Schaap D, de Widt J, van der Wal J, Vandekerckhove J, van Damme J, Gussow D, Ploegh HL, van Blitterswijk WJ, van der Bend RL: Purification, cDNA-cloning and expression of human diacylglycerol kinase. FEBS Lett. 1990 Nov 26;275(1-2):151-8. [PubMed Link Image]
  2. Hart TC, Champagne C, Zhou J, Van Dyke TE: Assignment of the gene for diacylglycerol kinase (DAGK) to human chromosome 12. Mamm Genome. 1994 Feb;5(2):123-4. [PubMed Link Image]
  3. Hart TC, Zhou J, Champagne C, Van Dyke TE, Rao PN, Pettenati MJ: Assignment of the human diacylglycerol kinase gene (DAGK) to 12q13.3 using fluorescence in situ hybridization analysis. Genomics. 1994 Jul 1;22(1):246-7. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5466
Enzyme 22 Name Diacylglycerol kinase delta
Enzyme 22 Synonyms
  1. Diglyceride kinase delta
  2. DGK-delta
  3. DAG kinase delta
  4. 130 kDa diacylglycerol kinase
Enzyme 22 Gene Name DGKD
Enzyme 22 Protein Sequence >Diacylglycerol kinase delta 
MAAAAGAPPPGPPQPPPPPPPEESSDSEPEAEPGSPQKLIRKVSTSGQIRQKTIIKEGML
TKQNNSFQRSKRRYFKLRGRTLYYAKTAKSIIFDEVDLTDASVAESSTKNVNNSFTVITP
CRKLILCADNRKEMEDWIAALKTVQNREHFEPTQYSMDHFSGMHNWYACSHARPTYCNVC
REALSGVTSHGLSCEVCKFKAHKRCAVRATNNCKWTTLASIGKDIIEDADGIAMPHQWLE
GNLPVSAKCTVCDKTCGSVLRLQDWRCLWCKAMVHTSCKESLLTKCPLGLCKVSVIPPTA
LNSIDSDGFWKASCPPSCTSPLLVFVNSKSGDNQGVKFLRRFKQLLNPAQVFDLMNGGPH
LGLRLFQKFDTFRILVCGGDGSVGWVLSEIDSLNLHKQCQLGVLPLGTGNDLARVLGWGS
ACDDDTQLPQILEKLERASTKMLDRWSVMAYEAKLPRQASSSTVTEDFSEDSEVQQILFY
EDSVAAHLSKILTSDQHSVVISSAKVLCETVKDFVARVGKAYEKTTESSEESEVMAKKCS
VLKEKLDSLLKTLDDESQASSSLPNPPPTIAEEAEDGDGSGSICGSTGDRLVASACPARP
QIFRPREQLMLRANSLKKAIRQIIEHTEKAVDEQNAQTQEQEGFVLGLSESEEKMDHRVC
PPLSHSESFGVPKGRSQRKVSKSPCEKLISKGSLSLGSSASLPPQPGSRDGLPALNTKIL
YPNVRAGMSGSLPGGSVISRLLINADPFNSEPETLEYYTEKCVMNNYFGIGLDAKISLDF
NNKRDEHPEKCRSRTKNMMWYGVLGTKELLHRTYKNLEQKVLLECDGRPIPLPSLQGIAV
LNIPSYAGGTNFWGGTKEDDTFAAPSFDDKILEVVAVFGSMQMAVSRVIRLQHHRIAQCR
TVKISILGDEGVPVQVDGEAWVQPPGYIRIVHKNRAQTLTRDRAFESTLKSWEDKQKCEL
PRPPSCSLHPEMLSEEEATQMDQFGQAAGVLIHSIREIAQSHRDMEQELAHAVNASSKSM
DRVYGKPRTTEGLNCSFVLEMVNNFRALRSETELLLSGKMALQLDPPQKEQLGSALAEMD
RQLRRLADTPWLCQSAEPGDEESVMLDLAKRSRSGKFRLVTKFKKEKNNKNKEAHSSLGA
PVHLWGTEEVAAWLEHLSLCEYKDIFTRHDIRGSELLHLERRDLKDLGVTKVGHMKRILC
GIKELSRSAPAVEA
Enzyme 22 Number of Residues 1214
Enzyme 22 Molecular Weight 134527
Enzyme 22 Theoretical pI 7.58
Enzyme 22 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • intracellular signaling cascade
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 22 General Function Not Available
Enzyme 22 Specific Function May function as signaling molecule. Isoform 2 may be involved in cell growth and tumorigenesis
Enzyme 22 Pathways
Enzyme 22 Reactions
  • ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 22773821 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q16760 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name DGKD_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >3645 bp 
ATGGCGGCGGCGGCGGGCGCCCCTCCGCCGGGTCCCCCGCAACCGCCTCCGCCGCCGCCG
CCCGAGGAGTCGTCCGACAGCGAGCCCGAGGCGGAGCCCGGCTCCCCACAGAAGCTCATC
CGCAAGGTGTCCACGTCGGGTCAGATCCGACAGAAGACCATCATCAAAGAGGGGATGCTG
ACCAAACAGAACAATTCATTCCAGCGATCAAAAAGGAGATACTTTAAGCTTCGAGGGCGA
ACGCTTTACTATGCCAAAACGGCAAAGTCAATCATATTTGATGAGGTGGATCTGACAGAT
GCCAGCGTAGCTGAATCCAGTACCAAAAACGTCAACAACAGTTTTACGGTCATAACTCCA
TGCAGGAAGCTCATCTTGTGTGCTGATAACAGAAAAGAAATGGAAGATTGGATTGCAGCA
TTAAAGACTGTGCAGAACAGGGAGCACTTTGAGCCCACCCAGTACAGCATGGACCACTTC
TCAGGGATGCACAATTGGTACGCCTGTTCCCACGCGAGGCCGACCTACTGCAATGTGTGC
CGTGAGGCTCTGTCTGGGGTCACGTCGCACGGGCTGTCCTGCGAGGTGTGCAAATTTAAG
GCCCACAAGCGCTGTGCTGTGCGTGCAACCAATAACTGCAAGTGGACCACACTGGCCTCG
ATCGGGAAGGACATCATTGAAGATGCAGATGGGATTGCAATGCCCCACCAGTGGTTGGAA
GGAAACCTACCTGTGAGCGCCAAGTGCACTGTGTGCGACAAGACCTGTGGCAGTGTGCTG
CGCCTGCAGGACTGGCGCTGCCTCTGGTGCAAGGCCATGGTTCACACATCGTGTAAAGAA
TCCTTGCTGACCAAGTGCCCACTTGGCCTGTGCAAAGTGTCAGTCATCCCACCCACGGCT
CTCAACAGCATCGACTCCGATGGGTTCTGGAAGGCCAGCTGTCCTCCTTCTTGCACAAGC
CCACTGTTGGTCTTCGTCAATTCAAAAAGTGGGGACAACCAGGGTGTGAAGTTCCTCAGA
AGATTCAAACAGCTACTAAACCCCGCCCAGGTCTTCGACCTCATGAACGGAGGCCCACAC
CTCGGCTTACGGTTATTCCAGAAGTTTGACACATTCCGGATTCTGGTTTGTGGCGGGGAT
GGAAGTGTTGGCTGGGTCCTCTCCGAAATCGACAGCCTCAACCTTCATAAACAGTGTCAG
CTGGGAGTGCTGCCGCTCGGCACAGGGAACGACTTGGCCCGAGTACTGGGCTGGGGCTCA
GCCTGCGATGACGACACCCAGCTCCCCCAGATCTTGGAGAAGTTGGAGAGAGCCAGCACC
AAGATGCTGGACAGGTGGAGCGTCATGGCATACGAGGCCAAGCTCCCCCGGCAGGCCTCC
TCCTCTACCGTCACCGAAGACTTCAGCGAGGATTCCGAGGTACAGCAGATTCTCTTCTAT
GAAGACTCGGTTGCAGCCCACCTTTCTAAAATCCTCACCTCGGACCAGCACTCGGTGGTC
ATCTCCTCGGCCAAAGTGCTCTGTGAGACGGTGAAGGACTTCGTGGCACGGGTGGGGAAG
GCCTATGAGAAGACGACCGAGAGCTCGGAGGAGTCAGAGGTCATGGCCAAGAAGTGCTCT
GTCCTGAAAGAGAAGCTGGATTCCCTTCTCAAGACCTTGGACGATGAGTCCCAGGCCTCG
TCCTCTCTGCCCAACCCGCCCCCCACCATTGCCGAGGAGGCTGAAGATGGAGATGGGTCG
GGCAGCATCTGCGGTTCCACCGGAGACCGCTTGGTGGCATCAGCTTGCCCGGCCCGGCCG
CAGATATTCCGGCCTCGAGAACAGCTCATGCTGAGAGCCAACAGCCTGAAGAAAGCAATT
CGTCAGATCATAGAACACACAGAAAAAGCTGTCGATGAGCAGAATGCCCAGACCCAGGAG
CAGGAGGGCTTCGTCCTGGGCCTCTCTGAGTCAGAGGAGAAGATGGACCACAGAGTGTGC
CCACCACTGTCCCACAGCGAGAGCTTCGGGGTCCCCAAGGGGAGGAGCCAGCGCAAAGTG
TCGAAATCTCCGTGTGAAAAGCTGATCAGCAAAGGGAGTCTGTCCCTAGGCAGTTCTGCT
TCCCTTCCGCCCCAGCCGGGAAGCCGGGACGGCCTGCCTGCGCTCAACACCAAGATCCTG
TACCCAAATGTCCGGGCTGGAATGTCTGGTTCCTTACCCGGTGGCTCAGTCATCAGTCGC
CTGTTAATTAATGCTGATCCCTTCAACTCTGAACCAGAAACCCTAGAGTATTACACGGAG
AAATGTGTCATGAACAACTATTTTGGCATTGGCCTGGATGCGAAGATATCCCTGGACTTT
AACAACAAGCGCGATGAGCACCCAGAGAAGTGCAGGAGCCGAACCAAGAACATGATGTGG
TATGGAGTTCTTGGAACCAAAGAGTTGCTGCACAGAACCTACAAGAACCTGGAGCAAAAG
GTCTTGCTGGAGTGTGACGGGCGACCCATCCCACTCCCCAGTCTTCAGGGAATTGCTGTC
CTTAACATTCCCAGCTATGCCGGAGGAACCAACTTCTGGGGGGGTACCAAGGAAGATGAT
ACTTTCGCAGCTCCATCATTCGATGACAAGATTCTGGAGGTGGTCGCCGTGTTCGGCAGC
ATGCAGATGGCCGTCTCTCGAGTCATCAGGCTACAGCATCATCGGATCGCCCAGTGTCGC
ACGGTGAAGATCTCCATCCTTGGGGATGAGGGCGTGCCTGTGCAGGTGGACGGAGAGGCC
TGGGTCCAGCCGCCAGGGTACATTCGGATTGTCCACAAGAACCGGGCACAGACACTGACC
AGAGACAGGGCATTTGAGAGCACCCTGAAGTCCTGGGAAGACAAGCAGAAGTGCGAGGTG
CCCCGCCCTCCATCCTGTTCCCTGCACCCGGAGATGCTGTCCGAGGAGGAGGCCACCCAG
ATGGACCAGTTTGGGCAGGCAGCAGGGGTCCTCATTCACAGTATCCGAGAAATAGCTCAG
TCTCACCGGGACATGGAGCAGGAACTGGCCCACGCCGTCAATGCCAGCTCCAAGTCCATG
GACCGTGTGTATGGCAAGCCCAGAACCACAGAGGGGCTCAACTGCAGCTTCGTCCTGGAA
ATGGTGAATAACTTCAGAGCTCTGCGCAGTGAGACGGAGCTGCTGCTGTCTGGGAAGATG
GCCCTGCAGCTGGATCCGCCTCAGAAGGAGCAGCTGGGGAGTGCTCTTGCCGAGATGGAC
CGACAGCTCAGGAGGCTGGCAGACACCCCGTGGCTCTGCCAGTCCGCAGAGCCCGGCGAC
GAAGAGAGTGTGATGCTGGATCTTGCCAAGCGCAGTCGCAGTGGTAAATTCCGCCTCGTG
ACCAAGTTTAAAAAGGAGAAAAACAACAAGAACAAAGAAGCTCACAGTAGCCTGGGAGCC
CCGGTTCACCTCTGGGGGACAGAGGAGGTTGCTGCCTGGCTGGAGCACCTCAGTCTCTGT
GAGTATAAGGACATCTTCACACGGCACGACATCCGGGGCTCTGAGCTCCTGCACCTGGAG
CGGAGGGACCTCAAGGACCTGGGCGTGACCAAGGTGGGCCACATGAAGAGGATCCTGTGT
GGCATCAAGGAGCTGAGCCGCAGCGCCCCCGCCGTCGAGGCCTAG
Enzyme 22 GenBank Gene ID AB078966 Link Image
Enzyme 22 GeneCard ID DGKD Link Image
Enzyme 22 GenAtlas ID DGKD Link Image
Enzyme 22 HGNC ID HGNC:2851 Link Image
Enzyme 22 Chromosome Location 2
Enzyme 22 Locus 2q37.1
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Sakane F, Imai S, Yamada K, Murakami T, Tsushima S, Kanoh H: Alternative splicing of the human diacylglycerol kinase delta gene generates two isoforms differing in their expression patterns and in regulatory functions. J Biol Chem. 2002 Nov 8;277(45):43519-26. Epub 2002 Aug 27. [PubMed Link Image]
  2. Nagase T, Seki N, Tanaka A, Ishikawa K, Nomura N: Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995 Aug 31;2(4):167-74, 199-210. [PubMed Link Image]
  3. Sakane F, Imai S, Kai M, Wada I, Kanoh H: Molecular cloning of a novel diacylglycerol kinase isozyme with a pleckstrin homology domain and a C-terminal tail similar to those of the EPH family of protein-tyrosine kinases. J Biol Chem. 1996 Apr 5;271(14):8394-401. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5472
Enzyme 23 Name Diacylglycerol kinase iota
Enzyme 23 Synonyms
  1. Diglyceride kinase iota
  2. DGK-iota
  3. DAG kinase iota
Enzyme 23 Gene Name DGKI
Enzyme 23 Protein Sequence >Diacylglycerol kinase iota 
MDAAGRGCHLLPLPAARGPARAPAAAAAAAASPPGPCSGAACAPSAAAGAGAMNPSSSAG
EEKGATGGSSSSGSGAGSCCLGAEGGADPRGAGSAAAAGAAALDEPAAAGQKEKDEALEE
KLRNLTFRKQVSYRKAISRAGLQHLAPAHPLSLPVANGPAKEPRATLDWSENAVNGEHLW
LETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGG
SRSPRENFVRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCF
MLHHIEEPCSLGAHAAVIVPPTWIIKVKKPQNSLKASNRKKKRTSFKRKASKRGMEQENK
GRPFVIKPISSPLMKPLLVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALEL
YRKVPNLRILACGGDGTVGWILSILDELQLSPQPPVGVLPLGTGNDLARTLNWGGGYTDE
PVSKILCQVEDGTVVQLDRWNLHVERNPDLPPEELEDGVCKLPLNVFNNYFSLGFDAHVT
LEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIQEL
KFQCIVFLNIPRYCAGTMPWGNPGDHHDFEPQRHDDGYIEVIGFTMASLAALQVGGHGER
LHQCREVMLLTYKSIPMQVDGEPCRLAPAMIRISLRNQANMVQKSKRRTSMPLLNDPQSV
PDRLRIRVNKISLQDYEGFHYDKEKLREASISDWLRTIAGELVQSFGAIPLGILVVRGDC
DLETCRMYIDRLQEDLQSVSSGSQRVHYQDHETSFPRALSAQRLSPRWCFLDDRSQEHLH
FVMEISQDEIFILDPDMVVSQPAGTPPGMPDLVVEQASGISDWWNPALRKRMLSDSGLGM
IAPYYEDSDLKDLSHSRVLQSPVSSEDHAILQAVIAGDLMKLIESYKNGGSLLIQGPDHC
SLLHYAAKTGNGEIVKYILDHGPSELLDMADSETGETALHKAACQRNRAVCQLLVDAGAS
LRKTDSKGKTPQERAQQAGDPDLAAYLESRQNYKVIGHEDLETAV
Enzyme 23 Number of Residues 1065
Enzyme 23 Molecular Weight 116998
Enzyme 23 Theoretical pI 7.81
Enzyme 23 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • intracellular signaling cascade
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 23 General Function Not Available
Enzyme 23 Specific Function ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl- sn-glycerol 3-phosphate
Enzyme 23 Pathways
Enzyme 23 Reactions
  • ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 3676530 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID O75912 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name DGKI_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >3198 bp 
ATGGATGCTGCGGGAAGGGGCTGCCATTTGCTGCCCCTGCCAGCGGCGCGCGGACCTGCC
CGCGCTCCTGCAGCCGCCGCCGCCGCCGCCGCCAGCCCGCCCGGCCCCTGCAGCGGCGCC
GCCTGCGCTCCCTCCGCGGCCGCCGGAGCGGGCGCCATGAACCCCAGCTCCTCGGCGGGA
GAGGAGAAAGGGGCGACGGGCGGCAGCAGCAGCAGCGGAAGCGGCGCCGGGAGCTGCTGC
CTGGGCGCCGAGGGCGGCGCGGACCCGCGGGGCGCAGGGTCAGCCGCGGCGGCGGGGGCC
GCTGCCCTGGACGAGCCCGCGGCCGCCGGCCAGAAGGAGAAGGACGAAGCGCTGGAGGAG
AAGCTGAGGAACTTAACTTTCCGGAAGCAGGTCTCGTACAGGAAAGCAATCTCCCGGGCA
GGCCTCCAGCATCTGGCTCCTGCACATCCCCTCAGCCTTCCTGTGGCAAATGGTCCAGCC
AAGGAGCCCAGAGCGACTTTGGACTGGAGTGAGAATGCCGTGAATGGAGAACACCTGTGG
CTGGAGACCAACGTCTCGGGAGACCTCTGCTACCTTGGAGAGGAGAACTGCCAAGTCAGA
TTTGCAAAATCAGCTCTCAGGAGGAAGTGTGCAGTCTGTAAAATCGTCGTCCACACCGCC
TGCATTGAGCAGCTAGAAAAGATTAATTTCAGATGTAAACCAACATTTCGAGAAGGAGGC
TCAAGGTCACCAAGAGAAAATTTTGTACGTCATCACTGGGTGCACAGGCGTCGGCAGGAG
GGGAAATGTAAGCAGTGTGGTAAGGGCTTCCAGCAAAAGTTCTCCTTCCACAGTAAAGAG
ATTGTGGCTATCAGCTGTTCCTGGTGCAAGCAGGCGTTTCACAATAAGGTGACCTGCTTC
ATGCTGCATCACATTGAAGAACCCTGCTCCCTGGGGGCTCATGCTGCTGTTATTGTCCCG
CCCACTTGGATCATTAAGGTGAAGAAACCTCAGAACTCCCTGAAGGCTTCAAATCGGAAG
AAGAAGAGAACAAGCTTTAAAAGAAAAGCCAGTAAAAGAGGGATGGAACAGGAAAACAAA
GGTCGTCCTTTTGTGATAAAACCCATCTCTTCTCCTCTCATGAAACCCTTGCTTGTATTT
GTGAATCCCAAGAGTGGAGGCAACCAGGGAACCAAAGTCCTGCAGATGTTCATGTGGTAC
CTGAATCCACGGCAAGTCTTTGATCTTTCTCAGGAAGGGCCAAAAGATGCGCTTGAATTG
TATAGGAAAGTACCAAATCTGCGAATTCTGGCCTGTGGTGGGGATGGAACGGTGGGCTGG
ATCCTTTCCATCCTGGATGAACTGCAGCTGAGCCCTCAGCCTCCTGTGGGGGTCCTTCCT
CTGGGGACTGGGAATGACCTGGCTCGAACTCTCAACTGGGGAGGGGGCTACACTGATGAA
CCTGTTTCTAAGATCCTGTGTCAAGTGGAAGATGGGACAGTTGTACAGCTAGATCGCTGG
AACCTCCATGTGGAAAGAAACCCCGACTTGCCTCCAGAAGAACTTGAAGATGGCGTATGT
AAGCTCCCTCTGAATGTTTTCAATAACTACTTCAGCCTTGGATTTGATGCCCATGTCACA
CTGGAGTTCCATGAATCCAGAGAAGCAAATCCAGAGAAATTCAACAGTCGTTTTCGAAAT
AAAATGTTCTATGCAGGGGCAGCTTTTTCTGACTTCCTACAGAGAAGTTCTAGAGATCTA
TCCAAACATGTTAAAGTTGTTTGTGATGGAACAGATCTCACCCCAAAGATTCAGGAACTG
AAGTTCCAGTGTATAGTATTTTTAAATATACCCAGATATTGTGCTGGCACAATGCCCTGG
GGAAACCCAGGTGATCACCATGATTTCGAACCTCAGCGTCATGATGATGGTTATATTGAA
GTCATTGGATTTACCATGGCCTCTTTGGCAGCCCTGCAAGTTGGGGGCCATGGAGAGAGG
CTACACCAGTGTCGAGAAGTCATGCTTCTAACTTACAAATCCATCCCCATGCAAGTGGAT
GGGGAGCCCTGTAGGTTGGCCCCAGCTATGATTCGGATCTCCCTGAGGAATCAGGCCAAC
ATGGTACAGAAGAGCAAGAGGAGAACATCCATGCCTTTACTCAATGATCCCCAGTCTGTC
CCAGATCGTCTGAGGATCCGGGTGAACAAAATCAGTTTACAAGACTATGAAGGATTCCAC
TATGACAAGGAGAAACTCCGAGAAGCTTCTATTTCAGACTGGTTAAGAACCATTGCTGGG
GAACTAGTGCAGTCATTTGGAGCGATACCTCTGGGTATTCTAGTTGTGCGTGGAGACTGT
GATTTGGAGACTTGCCGTATGTACATAGACCGCCTACAGGAGGACCTACAGTCAGTTTCT
TCTGGCTCCCAGAGAGTTCATTACCAGGACCATGAAACCTCCTTCCCCAGGGCTCTCTCA
GCACAGAGGCTCTCTCCTCGGTGGTGCTTCCTAGATGACAGATCTCAGGAACATTTGCAC
TTTGTGATGGAGATTTCCCAAGATGAGATTTTTATTCTGGACCCAGATATGGTGGTGTCA
CAGCCGGCGGGGACACCTCCGGGCATGCCTGACCTGGTGGTGGAACAAGCCTCGGGGATC
TCAGACTGGTGGAATCCTGCCCTGCGGAAACGCATGCTGAGTGACAGTGGGCTGGGGATG
ATAGCTCCCTATTATGAGGACTCAGATCTGAAAGATCTCAGCCACTCCCGCGTGCTACAG
TCACCAGTCTCTTCAGAAGATCATGCAATTTTGCAGGCAGTAATAGCTGGTGATCTTATG
AAGCTAATAGAAAGCTATAAAAATGGAGGCAGTCTGCTAATTCAGGGACCAGACCACTGT
TCACTCCTTCACTACGCAGCTAAAACCGGCAACGGGGAGATTGTGAAATATATCCTTGAC
CACGGACCTTCCGAGTTATTGGATATGGCAGACAGTGAAACGGGTGAGACTGCACTGCAC
AAGGCTGCCTGCCAGCGGAACCGGGCTGTGTGCCAGCTTCTGGTGGATGCAGGAGCATCT
CTGAGAAAGACGGACTCCAAGGGTAAGACACCTCAAGAAAGAGCACAGCAGGCTGGGGAC
CCAGACTTGGCTGCTTACCTAGAAAGCCGTCAGAACTATAAGGTCATTGGCCATGAGGAC
CTGGAAACTGCTGTTTGA
Enzyme 23 GenBank Gene ID AF061936 Link Image
Enzyme 23 GeneCard ID DGKI Link Image
Enzyme 23 GenAtlas ID DGKI Link Image
Enzyme 23 HGNC ID HGNC:2855 Link Image
Enzyme 23 Chromosome Location Not Available
Enzyme 23 Locus Not Available
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Ding L, Traer E, McIntyre TM, Zimmerman GA, Prescott SM: The cloning and characterization of a novel human diacylglycerol kinase, DGKiota. J Biol Chem. 1998 Dec 4;273(49):32746-52. [PubMed Link Image]
  2. Bowne SJ, Sullivan LS, Ding L, Traer E, Prescott SM, Birch DG, Kennan A, Humphries P, Daiger SP: Evaluation of human diacylglycerol kinase(iota), DGKI, a homolog of Drosophila rdgA, in inherited retinopathy mapping to 7q. Mol Vis. 2000 Feb 22;6:6-9. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 5478
Enzyme 24 Name Diacylglycerol kinase zeta
Enzyme 24 Synonyms
  1. Diglyceride kinase zeta
  2. DGK-zeta
  3. DAG kinase zeta
Enzyme 24 Gene Name DGKZ
Enzyme 24 Protein Sequence >Diacylglycerol kinase zeta 
METFFRRHFRGKVPGPGEGQRRPSSVGLPTGKARRRSPAGQASSSLAQRRRSSAQLQGCL
LSCGVRAQGSSRRRSSTVPPSCNPRFIVDKVLTPQPTTVGAQLLGAPLLLTGLVGMNEEE
GVQEDVVAEASSAIQPGTKTPGPPPPRGAQPLLPLPRYVRRASSHCCPADAVYDHALWGL
HGYYRRLSQRRPSGQHPGPGGRRASGTTAGTMLPTRVRPLSRRRQVALRRKAAGPQAWSA
LLAKAITKSGLQHLAPPPPTPGAPCSESERQIRSTVDWSESATYGEHIWFETNVSGDFCY
VGEQYCVARMLKSVSRRKCAACKIVVHTPCIEQLEKINFRCKPSFRESGSRNVREPTFVR
HHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCS
LGVHAAVVIPPTWILRARRPQNTLKASKKKKRASFKRKSSKKGPEEGRWRPFIIRPTPSP
LMKPLLVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPKEALEMYRKVHNLRILAC
GGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEG
NVVQLDRWDLHAEPNPEAGPEDRDEGATDRLPLDVFNNYFSLGFDAHVTLEFHESREANP
EKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIQDLKPQCVVFLNIP
RYCAGTMPWGHPGEHHDFEPQRHDDGYLEVIGFTMTSLAALQVGGHGERLTQCREVVLTT
SKAIPVQVDGEPCKLAASRIRIALRNQATMVQKAKRRSAAPLHSDQQPVPEQLRIQVSRV
SMHDYEALHYDKEQLKEASVPLGTVVVPGDSDLELCRAHIERLQQEPDGAGAKSPTCQKL
SPKWCFLDATTASRFYRIDRAQEHLNYVTEIAQDEIYILDPELLGASARPDLPTPTSPLP
TSPCSPTPRSLQGDAAPPQGEELIEAAKRNDFCKLQELHRAGGDLMHRDEQSRTLLHHAV
STGSKDVVRYLLDHAPPEILDAVEENGETCLHQAAALGQRTICHYIVEAGASLMKTDQQG
DTPRQRAEKAQDTELAAYLENRQHYQMIQREDQETAV
Enzyme 24 Number of Residues 1117
Enzyme 24 Molecular Weight 124124
Enzyme 24 Theoretical pI 9.27
Enzyme 24 GO Classification
Function
  • catalytic activity
  • diacylglycerol kinase activity
  • kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • G-protein coupled receptor protein signaling pathway
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
  • cell communication
  • cell surface receptor linked signal transduction
  • cellular process
  • intracellular signaling cascade
  • protein kinase C activation
  • signal transduction
Component
—
Enzyme 24 General Function Not Available
Enzyme 24 Specific Function Displays a strong preference for 1,2-diacylglycerols over 1,3-diacylglycerols, but lacks substrate specificity among molecular species of long chain diacylglycerols
Enzyme 24 Pathways
Enzyme 24 Reactions
  • ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 1293079 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q13574 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name DGKZ_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >2787 bp 
ATGGAGCCGCGGGACGGTAGCCCCGAGGCCCGGAGCAGCGACTCCGAGTCGGCTTCCGCC
TCGTCCAGCGGCTCCGAGCGCGACGCCGGTCCCGAGCCGGACAAGGCGCCGCGGCGACTC
AACAAGCGGCGCTTCCCGGGGCTGCGGCTCTTCGGGCACAGGAAAGCCATCACCAAGTCG
GGCCTCCAGCACCTGGCCCCCCCTCCGCCCACCCCTGGGGCCCCGTGCAGCGAGTCAGAG
CGGCAGATCCGGAGTACAGTGGACTGGAGCGAGTCAGCGACATATGGGGAGCACATCTGG
TTCGAGACCAACGTGTCCGGGGACTTCTGCTACGTTGGGGAGCAGTACTGTGTAGCCAGG
ATGCTGAAGTCAGTGTCTCGAAGAAAGTGCGCAGCCTGCAAGATTGTGGTGCACACGCCC
TGCATCGAGCAGCTGGAGAAGATAAATTTCCGCTGTAAGCCGTCCTTCCGTGAATCAGGC
TCCAGGAATGTCCGCGAGCCAACCTTTGTACGGCACCACTGGGTACACAGACGACGCCAG
GACGGCAAGTGTCGGCACTGTGGGAAGGGATTCCAGCAGAAGTTCACCTTCCACAGCAAG
GAGATTGTGGCCATCAGCTGCTCGTGGTGCAAGCAGGCATACCACAGCAAGGTGTCCTGC
TTCATGCTGCAGCAGATCGAGGAGCCGTGCTCGCTGGGGGTCCACGCAGCCGTGGTCATC
CCGCCCACCTGGATCCTCCGCGCCCGGAGGCCCCAGAATACTCTGAAAGCAAGCAAGAAG
AAGAAGAGGGCATCCTTCAAGAGGAAGTCCAGCAAGAAAGGGCCTGAGGAGGGCCGCTGG
AGACCCTTCATCATCAGGCCCACCCCCTCCCCGCTCATGAAGCCCCTGCTGGTGTTTGTG
AACCCCAAGAGTGGGGGCAACCAGGGTGCAAAGATCATCCAGTCTTTCCTCTGGTATCTC
AATCCCCGACAAGTCTTCGACCTGAGCCAGGGAGGGCCCAAGGAGGCGCTGGAGATGTAC
CGCAAAGTGCACAACCTGCGGATCCTGGCGTGCGGGGGCGACGGCACGGTGGGCTGGATC
CTCTCCACCCTGGACCAGCTACGCCTGAAGCCGCCACCCCCTGTTGCCATCCTGCCCCTG
GGTACTGGCAACGACTTGGCCCGAACCCTCAACTGGGGTGGGGGCTACACAGATGAGCCT
GTGTCCAAGATCCTCTCCCACGTGGAGGAGGGGAACGTGGTACAGCTGGACCGCTGGGAC
CTCCACGCTGAGCCCAACCCCGAGGCAGGGCCTGAGGACCGAGATGAAGGCGCCACCGAC
CGGTTGCCCCTGGATGTCTTCAACAACTACTTCAGCCTGGGCTTTGACGCCCACGTCACC
CTGGAGTTCCACGAGTCTCGAGAGGCCAACCCAGAGAAATTCAACAGCCGCTTTCGGAAT
AAGATGTTCTACGCCGGGACAGCTTTCTCTGACTTCCTGATGGGCAGCTCCAAGGACCTG
GCCAAGCACATCCGAGTGGTGTGTGATGGAATGGACTTGACTCCCAAGATCCAGGACCTG
AAACCCCAGTGTGTTGTTTTCCTGAACATCCCCAGGTACTGTGCGGGCACCATGCCCTGG
GGCCACCCTGGGGAGCACCACGACTTTGAGCCCCAGCGGCATGACGACGGCTACCTCGAG
GTCATTGGCTTCACCATGACGTCGTTGGCCGCGCTGCAGGTGGGCGGACACGGCGAGCGG
CTGACGCAGTGTCGCGAGGTGGTGCTCACCACATCCAAGGCCATCCCGGTGCAGGTGGAT
GGCGAGCCCTGCAAGCTTGCAGCCTCACGCATCCGCATCGCCCTGCGCAACCAGGCCACC
ATGGTGCAGAAGGCCAAGCGGCGGAGCGCCGCCCCCCTGCACAGCGACCAGCAGCCGGTG
CCAGAGCAGTTGCGCATCCAGGTGAGTCGCGTCAGCATGCACGACTATGAGGCCCTGCAC
TACGACAAGGAGCAGCTCAAGGAGGCCTCTGTGCCGCTGGGCACTGTGGTGGTCCCAGGA
GACAGTGACCTAGAGCTCTGCCGTGCCCACATTGAGAGACTCCAGCAGGAGCCCGATGGT
GCTGGAGCCAAGTCCCCGACATGCCAGAAACTGTCCCCCAAGTGGTGCTTCCTGGACGCC
ACCACTGCCAGCCGCTTCTACAGGATCGACCGAGCCCAGGAGCACCTCAACTATGTGACT
GAGATCGCACAGGATGAGATTTATATCCTGGACCCTGAGCTGCTGGGGGCATCGGCCCGG
CCTGACCTCCCAACCCCCACTTCCCCTCTCCCCACCTCACCCTGCTCACCCACGCCCCGG
TCACTGCAAGGGGATGCTGCACCCCCTCAAGGTGAAGAGCTGATTGAGGCTGCCAAGAGG
AACGACTTCTGTAAGCTCCAGGAGCTGCACCGAGCTGGGGGCGACCTCATGCACCGAGAC
GAGCAGAGTCGCACGCTCCTGCACCACGCAGTCAGCACTGGCAGCAAGGATGTGGTCCGC
TACCTGCTGGACCACGCCCCCCCAGAGATCCTTGATGCGGTGGAGGAAAACGGGGAGACC
TGTTTGCACCAAGCAGCGGCCCTGGGCCAGCGCACCATCTGCCACTACATCGTGGAGGCC
GGGGCCTCGCTCATGAAGACAGACCAGCAGGGCGACACTCCCCGGCAGCGGGCTGAGAAG
GCTCAGGACACCGAGCTGGCCGCCTACCTGGAGAACCGGCAGCACTACCAGATGATCCAG
CGGGAGGACCAGGAGACGGCTGTGTAG
Enzyme 24 GenBank Gene ID U51477 Link Image
Enzyme 24 GeneCard ID DGKZ Link Image
Enzyme 24 GenAtlas ID DGKZ Link Image
Enzyme 24 HGNC ID HGNC:2857 Link Image
Enzyme 24 Chromosome Location 11
Enzyme 24 Locus 11p11.2
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Bunting M, Tang W, Zimmerman GA, McIntyre TM, Prescott SM: Molecular cloning and characterization of a novel human diacylglycerol kinase zeta. J Biol Chem. 1996 Apr 26;271(17):10230-6. [PubMed Link Image]
  2. Ding L, Bunting M, Topham MK, McIntyre TM, Zimmerman GA, Prescott SM: Alternative splicing of the human diacylglycerol kinase zeta gene in muscle. Proc Natl Acad Sci U S A. 1997 May 27;94(11):5519-24. [PubMed Link Image]
  3. Topham MK, Bunting M, Zimmerman GA, McIntyre TM, Blackshear PJ, Prescott SM: Protein kinase C regulates the nuclear localization of diacylglycerol kinase-zeta. Nature. 1998 Aug 13;394(6694):697-700. [PubMed Link Image]
  4. Hogan A, Shepherd L, Chabot J, Quenneville S, Prescott SM, Topham MK, Gee SH: Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta. Regulation of nuclear localization by PDZ interactions. J Biol Chem. 2001 Jul 13;276(28):26526-33. Epub 2001 May 14. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 5487
Enzyme 25 Name L-fucose kinase
Enzyme 25 Synonyms
  1. Fucokinase
Enzyme 25 Gene Name FUK
Enzyme 25 Protein Sequence >L-fucose kinase 
MEQPKGVDWTVIILTCQYKDSVQVFQRELEVRQKREQIPAGTLLLAVEDPEKRVGSGGAT
LNALLVAAEHLSARAGFTVVTSDVLHSAWILILHMGRDFPFDDCGRAFTCLPVENPEAPV
EALVCNLDCLLDIMTYRLGPGSPPGVWVCSTDMLLSVPANPGISWDSFRGARVIALPGSP
AYAQNHGVYLTDPQGLVLDIYYQGTEAEIQRCVRPDGRVPLVSGVVFFSVETAERLLATH
VSPPLDACTYLGLDSGARPVQLSLFFDILHCMAENVTREDFLVGRPPELGQGDADVAGYL
QSARAQLWRELRDQPLTMAYVSSGSYSYMTSSASEFLLSLTLPGAPGAQIVHSQVEEQQL
LAAGSSVVSCLLEGPVQLGPGSVLQHCHLQGPIHIGAGCLVTGLDTAHSKALHGRELRDL
VLQGHHTRLHGSPGHAFTLVGRLDSWERQGAGTYLNVPWSEFFKRTGVRAWDLWDPETLP
AEYCLPSARLFPVLHPSRELGPQDLLWMLDHQEDGGEALRAWRASWRLSWEQLQPCLDRA
ATLASRRDLFFRQALHKARHVLEARQDLSLRPLIWAAVREGCPGPLLATLDQVAAGAGDP
GVAARALACVADVLGCMAEGRGGLRSGPAANPEWMRPFSYLECGDLAAGVEALAQERDKW
LSRPALLVRAARHYEGAGQILIRQAVMSAQHFVSTEQVELPGPGQWVVAECPARVDFSGG
WSDTPPLAYELGGAVLGLAVRVDGRRPIGARARRIPEPELWLAVGPRQDEMTVKIVCRCL
ADLRDYCQPHAPGALLKAAFICAGIVHVHSELQLSEQLLRTFGGGFELHTWSELPHGSGL
GTSSILAGTALAALQRAAGRVVGTEALIHAVLHLEQVLTTGGGWQDQVGGLMPGIKVGRS
RAQLPLKVEVEEVTVPEGFVQKLNDHLLLVYTGKTRLARNLLQDVLRSWYARLPAVVQNA
HSLVRQTEECAEGFRQGSLPLLGQCLTSYWEQKKLMAPGCEPLTVRRMMDVLAPHVHGQS
LAGAGGGGFLYLLTKEPQQKEALEAVLAKTEGLGNYSIHLVEVDTQGLSLKLLGTEASTC
CPFP
Enzyme 25 Number of Residues 1084
Enzyme 25 Molecular Weight 117624
Enzyme 25 Theoretical pI 6.21
Enzyme 25 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • phosphate metabolism
  • phosphorus metabolism
  • phosphorylation
  • physiological process
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 25 General Function Not Available
Enzyme 25 Specific Function Takes part in the salvage pathway for reutilization of fucose from the degradation of oligosaccharides
Enzyme 25 Pathways
Enzyme 25 Reactions
  • ATP + L-fucose = ADP + beta-L-fucose 1-phosphate
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 21212956 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q8N0W3 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name FUK_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >2973 bp 
ATGGGTCGAGACTTCCCCTTTGATGACTGTGGCAGGGCTTTCACCTGCCTCCCCGTGGAG
AACCCCGAGGCCCCCGTGGAAGCCTTGGTCTGCAACCTGGACTGCCTGCTGGACATCATG
ACCTATCGGCTGGGCCCGGGCTCCCCGCCAGGCGTGTGGGTCTGCAGCACCGACATGCTG
CTGTCTGTTCCTGCAAATCCTGGTATCAGCTGGGACAGCTTCCGGGGAGCCAGAGTGATC
GCCCTCCCAGGGAGCCCGGCCTACGCTCAGAATCATGGCGTCTACCTAACTGACCCCCAG
GGCCTTGTTTTGGACATTTACTACCAGGGCACTGAGGCAGAGATTCAGCGGTGTGTCAGG
CCTGATGGGCGGGTGCCACTGGTCTCTGGGGTTGTCTTCTTCTCTGTGGAGACTGCCGAG
CGCCTCCTAGCCACCCACGTGAGCCCGCCCCTGGATGCCTGCACCTACCTAGGCTTGGAC
TCCGGAGCCCGGCCTGTCCAGCTGTCTCTGTTTTTTGACATTCTCCACTGCATGGCTGAG
AACGTGACCAGGGAGGACTTCCTGGTGGGGAGGCCCCCAGAGTTGGGGCAAGGCGATGCA
GATGTAGCGGGTTATCTGCAGAGCGCCCGGGCCCAGCTGTGGAGGGAGCTTCGCGATCAG
CCCCTTACCATGGCCTATGTCTCCAGCGGCAGCTACAGCTACATGACCTCCTCAGCCAGT
GAGTTCCTGCTCAGCCTCACACTCCCCGGGGCTCCTGGGGCCCAGATTGTGCACTCCCAG
GTGGAGGAGCAGCAGCTTCTGGCGGCCGGGAGCTCTGTGGTCAGCTGCCTGCTGGAGGGC
CCTGTCCAGCTGGGTCCTGGGAGCGTCCTGCAGCACTGCCACCTGCAGGGCCCCATTCAC
ATAGGCGCTGGCTGCTTGGTGACTGGCCTGGATACAGCCCACTCCAAGGCCCTGCATGGC
CGGGAGCTGCGTGACCTTGTCCTGCAGGGACACCACACGCGGCTACACGGCTCCCCGGGC
CACGCCTTCACCCTCGTTGGCCGTCTGGACAGCTGGGAGAGACAGGGGGCAGGCACATAT
CTCAACGTGCCCTGGAGTGAATTCTTCAAGAGGACAGGTGTTCGAGCCTGGGACCTGTGG
GACCCCGAGACGCTGCCCGCAGAGTACTGCCTTCCCAGCGCCCGCCTCTTTCCTGTGCTC
CACCCCTCGAGGGAGCTGGGACCCCAGGACCTGCTGTGGATGCTGGACCACCAGGAGGAT
GGGGGCGAGGCCCTGCGAGCCTGGCGGGCCTCCTGGCGCCTGTCCTGGGAGCAGCTGCAG
CCGTGCCTGGATCGGGCTGCCACGCTGGCCTCTCGCCGGGACCTGTTCTTCCGCCAGGCC
CTGCATAAGGCGCGGCACGTGCTGGAGGCCCGGCAGGACCTCAGCCTGCGCCCGCTGATC
TGGGCTGCTGTCCGCGAGGGCTGCCCCGGGCCCCTGCTGGCCACGCTGGACCAGGTTGCA
GCTGGGGCAGGAGACCCTGGTGTGGCGGCACGGGCACTGGCCTGTGTGGCGGACGTCCTG
GGCTGCATGGCAGAGGGCCGTGGGGGCTTGCGGAGCGGGCCAGCTGCCAACCCTGAGTGG
ATGCGGCCCTTCTCATACCTGGAGTGTGGAGACCTGGCAGCGGGCGTGGAGGCGCTTGCC
CAGGAGAGGGACAAGTGGCTAAGCAGGCCAGCCTTGCTGGTGCGAGCGGCCCGCCACTAT
GAGGGGGCTGGTCAGATCCTGATCCGCCAGGCTGTGATGTCAGCCCAGCACTTTGTCTCC
ACAGAGCAGGTGGAACTGCCGGGACCTGGGCAGTGGGTGGTGGCTGAGTGCCCGGCCCGT
GTGGATTTCTCTGGGGGCTGGAGTGACACGCCACCCCTTGCCTATGAGCTTGGCGGGGCT
GTGCTGGGCCTGGCTGTGCGAGTGGACGGCCGCCGGCCCATCGGAGCCAGGGCACGCCGC
ATCCCGGAGCCTGAGCTGTGGCTGGCGGTGGGGCCTCGGCAGGATGAGATGACTGTGAAG
ATAGTGTGCCGGTGCCTGGCTGACCTGCGGGACTACTGCCAGCCTCATGCCCCAGGGGCC
CTGCTGAAGGCGGCCTTCATCTGTGCAGGGATCGTGCATGTCCACTCGGAACTCCAGCTG
AGTGAGCAGCTGCTCCGCACCTTCGGGGGCGGCTTTGAGCTGCACACCTGGTCTGAGCTG
CCCCACGGCTCTGGCCTGGGCACCAGCAGCATCCTGGCAGGCACTGCCCTGGCTGCCTTG
CAGCGAGCCGCAGGCCGGGTGGTGGGCACGGAAGCCCTGATCCACGCAGTGCTGCACCTG
GAGCAGGTGCTCACCACTGGAGGTGGCTGGCAGGACCAAGTAGGTGGCCTAATGCCTGGC
ATCAAGGTGGGGCGCTCCCGGGCTCAGCTGCCACTGAAGGTGGAGGTAGAAGAGGTCACG
GTGCCTGAGGGCTTTGTCCAGAAGCTCAATGACCACCTGCTCTTGGTGTACACTGGCAAG
ACCCGCCTGGCTCGGAACCTGCTGCAGGATGTGCTGAGGAGCTGGTATGCCCGACTTCCT
GCTGTGGTGCAGAATGCCCACAGCCTGGTACGGCAAACTGAGGAGTGTGCTGAAGGCTTC
CGCCAAGGAAGCCTGCCTCTGCTGGGCCAGTGCCTGACCTCGTACTGGGAGCAGAAGAAG
CTCATGGCTCCAGGCTGTGAGCCCCTGACTGTGCGGCGTATGATGGATGTCCTGGCCCCC
CACGTGCATGGCCAGAGCCTGGCTGGGGCAGGCGGTGGAGGCTTTCTCTATCTGTTGACC
AAGGAGCCACAGCAAAAGGAGGCCTTGGAGGCGGTGCTGGCCAAGACCGAGGGCCTTGGG
AATTACAGCATCCACCTGGTTGAAGTGGACACTCAGGGCCTGAGCCTGAAGCTGCTGGGG
ACCGAGGCCTCAACCTGTTGCCCTTTCCCATGA
Enzyme 25 GenBank Gene ID AJ441184 Link Image
Enzyme 25 GeneCard ID FUK Link Image
Enzyme 25 GenAtlas ID FUK Link Image
Enzyme 25 HGNC ID HGNC:29500 Link Image
Enzyme 25 Chromosome Location Not Available
Enzyme 25 Locus Not Available
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Hinderlich S, Berger M, Blume A, Chen H, Ghaderi D, Bauer C: Identification of human L-fucose kinase amino acid sequence. Biochem Biophys Res Commun. 2002 Jun 14;294(3):650-4. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 5490
Enzyme 26 Name Propionyl-CoA carboxylase beta chain, mitochondrial precursor
Enzyme 26 Synonyms
  1. PCCase subunit beta
  2. Propanoyl-CoA:carbon dioxide ligase subunit beta
Enzyme 26 Gene Name PCCB
Enzyme 26 Protein Sequence >Propionyl-CoA carboxylase beta chain, mitochondrial precursor 
MAAALRVAAVGARLSVLASGLRAAVRSLCSQATSVNERIENKRRTALLGGGQRRIDAQHK
RGKLTARERISLLLDPGSFVESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVY
VFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIF
LRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVT
QEELGGAKTHTTMSGVAHRAFENDVDALCNLRDFFNYLPLSSQDPAPVRECHDPSDRLVP
ELDTIVPLESTKAYNMVDIIHSVVDEREFFEIMPNYAKNIIVGFARMNGRTVGIVGNQPK
VASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFA
EATVPKVTVITRKAYGGAYDVMSSKHLCGDTNYAWPTAEIAVMGAKGAVEIIFKGHENVE
AAQAEYIEKFANPFPAAVRGFVDDIIQPSSTRARICCDLDVLASKKVQRPWRKHANIPL
Enzyme 26 Number of Residues 539
Enzyme 26 Molecular Weight 58216
Enzyme 26 Theoretical pI 7.69
Enzyme 26 GO Classification
Function
  • catalytic activity
  • ligase activity
Process
—
Component
—
Enzyme 26 General Function Not Available
Enzyme 26 Specific Function ATP + propanoyl-CoA + HCO(3)(-) = ADP + phosphate + (S)-methylmalonyl-CoA
Enzyme 26 Pathways
Enzyme 26 Reactions
  • ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • 1-23
Enzyme 26 Transmembrane Regions Not Available
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 312812 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P05166 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name PCCB_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >1620 bp 
ATGGCGGCGGCATTACGGGTGGCGGCGGTCGGGGCAAGGCTCAGCGTTCTGGCGAGCGGT
CTCCGCGCCGCGGTCCGCAGCCTTTGCAGCCAGGCCACCTCTGTTAACGAACGCATCGAA
AACAAGCGCCGGACCGCGCTGCTGGGAGGGGGCCAACGCCGTATTGACGCGCAGCACAAG
CGAGGAAAGCTAACAGCCAGGGAGAGGATCAGTCTCTTGCTGGACCCTGGCAGCTTTGTT
GAGAGCGACATGTTTGTGGAACACAGATGTGCAGATTTTGGAATGGCTGCTGACAAGAAT
AAGTTTCCTGGAGACAGCGTGGTCACTGGACGAGGCCGAATCAATGGAAGATTGGTTTAT
GTCTTCAGTCAGGATTTTACAGTTTTTGGAGGCAGTCTGTCAGGAGCACATGCCCAAAAG
ATCTGCAAAATCATGGACCAGGCCATAACGGTGGGGGCTCCAGTGATTGGGCTGAATGAC
TCTGGGGGAGCACGGATCCAAGAAGGAGTGGAGTCTTTGGCTGGCTATGCAGACATCTTT
CTGAGGAATGTTACGGCATCCGGAGTCATCCCTCAGATTTCTCTGATCATGGGCCCATGT
GCTGGTGGGGCCGTCTACTCCCCAGCCCTAACAGACTTCACGTTCATGGTAAAGGACACC
TCCTACCTGTTCATCACTGGCCCTGATGTTGTGAAGTCTGTCACCAATGAGGATGTTACC
CAGGAGGAGCTCGGTGGTGCCAAGACCCACACCACCATGTCAGGTGTGGCCCACAGAGCT
TTTGAAAATGATGTTGATGCCTTGTGTAATCTCCGGGATTTCTTCAACTACCTGCCCCTG
AGCAGTCAGGACCCGGCTTCCGTCCGTGAGTGCCACGATCCCAGTGACCGTCTGGTTCCT
GAGCTTGACACAATTGTCCCTTTGGAATCAACCAAAGCCTACAACATGGTGGACATCATA
CACTCTGTTGTTGATGAGCGTGAATTTTTTGAGATCATGCCCAATTATGCCAAGAACATC
ATTGTTGGTTTTGCAAGAATGAATGGGAGGACTGTTGGAATTGTTGGCAACCAACCTAAG
GTGGCCTCAGGATGCTTGGATATTAATTCATCTGTGAAAGGGGCTCGTTTTGTCAGATTC
TGTGATGCATTCAATATTCCACTCATCACTTTTGTTGATGTCCCTGGCTTTCTACCTGGC
ACAGCACAGGAATACGGGGGCATCATCCGGCATGGTGCCAAGCTTCTCTACGCATTTGCT
GAGGCAACTGTACCCAAAGTCACAGTCATCACCAGGAAGGCCTATGGAGGTGCCTATGAT
GTCATGAGCTCTAAGCACCTTTGTGGTGATACCAACTATGCCTGGCCCACCGCAGAGATT
GCAGTCATGGGAGCAAAGGGCGCTGTGGAGATCATCTTCAAAGGGCATGAGAATGTGGAA
GCTGCTCAGGCAGAGTACATCGAGAAGTTTGCCAACCCTTTCCCTGCAGCAGTGCGAGGG
TTTGTGGATGACATCATCCAACCTTCTTCCACACGTGCCCGAATCTGCTGTGACCTGGAT
GTCTTGGCCAGCAAGAAGGTACAACGTCCTTGGAGAAAACATGCAAATATTCCATTGTAA
Enzyme 26 GenBank Gene ID X73424 Link Image
Enzyme 26 GeneCard ID PCCB Link Image
Enzyme 26 GenAtlas ID PCCB Link Image
Enzyme 26 HGNC ID HGNC:8654 Link Image
Enzyme 26 Chromosome Location 3
Enzyme 26 Locus 3q21-q22
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Lamhonwah AM, Leclerc D, Loyer M, Clarizio R, Gravel RA: Correction of the metabolic defect in propionic acidemia fibroblasts by microinjection of a full-length cDNA or RNA transcript encoding the propionyl-CoA carboxylase beta subunit. Genomics. 1994 Feb;19(3):500-5. [PubMed Link Image]
  2. Ohura T, Ogasawara M, Ikeda H, Narisawa K, Tada K: The molecular defect in propionic acidemia: exon skipping caused by an 8-bp deletion from an intron in the PCCB allele. Hum Genet. 1993 Oct;92(4):397-402. [PubMed Link Image]
  3. Rodriguez-Pombo P, Hoenicka J, Muro S, Perez B, Perez-Cerda C, Richard E, Desviat LR, Ugarte M: Human propionyl-CoA carboxylase beta subunit gene: exon-intron definition and mutation spectrum in Spanish and Latin American propionic acidemia patients. Am J Hum Genet. 1998 Aug;63(2):360-9. [PubMed Link Image]
  4. Lamhonwah AM, Barankiewicz TJ, Willard HF, Mahuran DJ, Quan F, Gravel RA: Isolation of cDNA clones coding for the alpha and beta chains of human propionyl-CoA carboxylase: chromosomal assignments and DNA polymorphisms associated with PCCA and PCCB genes. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4864-8. [PubMed Link Image]
  5. Tahara T, Kraus JP, Rosenberg LE: An unusual insertion/deletion in the gene encoding the beta-subunit of propionyl-CoA carboxylase is a frequent mutation in Caucasian propionic acidemia. Proc Natl Acad Sci U S A. 1990 Feb;87(4):1372-6. [PubMed Link Image]
  6. Tahara T, Kraus JP, Ohura T, Rosenberg LE, Fenton WA: Three independent mutations in the same exon of the PCCB gene: differences between Caucasian and Japanese propionic acidaemia. J Inherit Metab Dis. 1993;16(2):353-60. [PubMed Link Image]
  7. Muro S, Rodriguez-Pombo P, Perez B, Perez-Cerda C, Desviat LR, Sperl W, Skladal D, Sass JO, Ugarte M: Identification of novel mutations in the PCCB gene in European propionic acidemia patients. Mutation in brief no. 253. Online. Hum Mutat. 1999;14(1):89-90. [PubMed Link Image]
  8. Ugarte M, Perez-Cerda C, Rodriguez-Pombo P, Desviat LR, Perez B, Richard E, Muro S, Campeau E, Ohura T, Gravel RA: Overview of mutations in the PCCA and PCCB genes causing propionic acidemia. Hum Mutat. 1999;14(4):275-82. [PubMed Link Image]
  9. Perez B, Desviat LR, Rodriguez-Pombo P, Clavero S, Navarrete R, Perez-Cerda C, Ugarte M: Propionic acidemia: identification of twenty-four novel mutations in Europe and North America. Mol Genet Metab. 2003 Jan;78(1):59-67. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 5581
Enzyme 27 Name Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1
Enzyme 27 Synonyms
  1. PAPS synthetase 1
  2. PAPSS 1
  3. Sulfurylase kinase 1
  4. SK1
  5. SK 1[Includes: Sulfate adenylyltransferase
  6. Sulfate adenylate transferase
  7. SAT
  8. ATP-sulfurylase
  9. Adenylyl-sulfate kinase
  10. Adenylylsulfate 3'-phosphotransferase
  11. APS kinase
  12. Adenosine-5'-phosphosulfate 3'-phosphotransferase
  13. 3'- phosphoadenosine-5'-phosphosulfate synthetase]
Enzyme 27 Gene Name PAPSS1
Enzyme 27 Protein Sequence >Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 
MEIPGSLCKKVKLSNNAQNWGMQRATNVTYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGL
SGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLF
ADAGLVCITSFISPYTQDRNNARQIHEGASLPFFEVFVDAPLHVCEQRDVKGLYKKARAG
EIKGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVPVDASYEVKELYVP
ENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGG
VINLSVPIVLTATHEDKERLDGCTAFALMYEGRRVAILRNPEFFEHRKEERCARQWGTTC
KNHPYIKMVMEQGDWLIGGDLQVLDRVYWNDGLDQYRLTPTELKQKFKDMNADAVFAFQL
RNPVHNGHALLMQDTHKQLLERGYRRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGV
LNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPS
HGAKVLTMAPGLITLEIVPFRVAAYNKKKKRMDYYDSEHHEDFEFISGTRMRKLAREGQK
PPEGFMAPKAWTVLTEYYKSLEKA
Enzyme 27 Number of Residues 624
Enzyme 27 Molecular Weight 70834
Enzyme 27 Theoretical pI 6.85
Enzyme 27 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • nucleotidyltransferase activity
  • purine nucleotide binding
  • sulfate adenylyltransferase (ATP) activity
  • sulfate adenylyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • physiological process
  • sulfate assimilation
  • sulfur metabolism
  • sulfur utilization
Component
—
Enzyme 27 General Function Inorganic ion transport and metabolism
Enzyme 27 Specific Function Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS:activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate- activation pathway. Also involved in the biosynthesis of sulfated L-selectin ligands in endothelial cells
Enzyme 27 Pathways
Enzyme 27 Reactions
  • ATP + sulfate = diphosphate + adenylylsulfate
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 2673862 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID O43252 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name PAPS1_HUMAN Link Image
Enzyme 27 PDB ID 1X6V Link Image
Enzyme 27 PDB File Show
Enzyme 27 3D Structure
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >1875 bp 
ATGGAGATCCCCGGGAGCTTGTGCAAGAAAGTCAAGCTGAGCAATAACGCGCAGAACTGG
GGAATGCAGAGAGCAACCAATGTCACCTACCAAGCCCATCATGTCAGCAGGAACAAGAGA
GGTCAGGTGGTGGGGACCAGAGGTGGCTTTCGTGGTTGCACAGTTTGGCTAACAGGCTTG
TCTGGAGCGGGAAAGACTACTGTGAGCATGGCCTTGGAGGAGTACCTGGTTTGTCATGGT
ATTCCATGCTACACTCTGGATGGTGACAATATTCGTCAAGGTCTCAATAAAAATCTTGGC
TTTAGTCCTGAAGACAGAGAAGAGAATGTTCGACGCATCGCAGAAGTTGCTAAACTGTTT
GCAGATGCTGGCTTAGTGTGCATCACAAGTTTCATATCACCTTACACTCAGGATCGCAAC
AATGCAAGGCAAATTCATGAAGGTGCAAGTTTACCGTTTTTTGAAGTATTTGTTGATGCT
CCTCTGCATGTTTGTGAACAGAGGGATGTCAAAGGACTCTACAAAAAAGCCCGGGCAGGA
GAAATTAAAGGTTTCACTGGGATCGATTCTGAATATGAAAAGCCAGAGGCCCCTGAGTTG
GTGCTGAAAACAGACTCCTGTGATGTAAATGACTGTGTCCAGCAAGTTGTGGAACTTCTA
CAGGAACGGGATATTGTACCTGTGGATGCATCTTATGAAGTAAAAGAACTATATGTGCCA
GAAAATAAACTTCATTTGGCAAAAACAGATGCGGAAACATTACCAGCACTGAAAATTAAT
AAAGTGGATATGCAGTGGGTGCAGGTTTTGGCAGAAGGTTGGGCAACCCCATTGAATGGC
TTTATGAGAGAGAGGGAGTACTTGCAGTGCCTTCATTTTGATTGTCTTCTGGATGGAGGT
GTCATTAACTTGTCAGTACCTATAGTTCTGACTGCGACTCATGAAGATAAAGAGAGGCTG
GACGGCTGTACAGCATTTGCTCTGATGTATGAGGGCCGCCGTGTGGCCATTCTTCGCAAT
CCAGAGTTTTTTGAGCACAGGAAAGAGGAGCGCTGTGCCAGACAGTGGGGAACGACATGC
AAGAACCACCCCTATATTAAGATGGTGATGGAACAAGGAGATTGGCTGATTGGAGGAGAT
CTTCAAGTCTTGGATCGAGTTTATTGGAATGATGGTCTTGATCAGTATCGTCTTACTCCT
ACTGAGCTAAAGCAGAAATTTAAAGATATGAATGCTGATGCTGTCTTTGCATTTCAACTA
CGCAACCCAGTGCACAATGGACATGCCCTGTTAATGCAGGATACCCATAAGCAACTTCTA
GAGAGGGGCTACCGGCGCCCTGTCCTCCTCCTCCACCCTCTGGGTGCTTGGACAAAGGAT
GACGATGTTCCTTTGATGTGGCGTATGAAGCAGCATGCTGCAGTGTTGGAGGAAGGAGTT
CTGAATCCTGAGACGACAGTGGTGGCCATCTTCCCATCTCCCATGATGTATGCTGGACCA
ACTGAGGTCCAGTGGCATTGCAGAGCACGGATGGTTGCAGGAGCCAACTTTTACATTGTT
GGACGAGACCCTGCTGGCATGCCTCATCCAGAAACAGGGAAGGATCTTTATGAGCCAAGT
CATGGTGCCAAAGTGCTGACGATGGCCCCTGGTTTAATCACTTTGGAAATAGTTCCCTTT
CGAGTTGCAGCTTACAACAAGAAAAAGAAGCGTATGGACTACTATGACTCTGAACACCAT
GAAGACTTTGAATTTATTTCAGGAACACGAATGCGCAAACTTGCTCGAGAAGGCCAGAAA
CCACCTGAAGGTTTCATGGCTCCCAAGGCTTGGACCGTGCTGACAGAATACTACAAATCC
TTGGAGAAAGCTTAG
Enzyme 27 GenBank Gene ID Y10387 Link Image
Enzyme 27 GeneCard ID PAPSS1 Link Image
Enzyme 27 GenAtlas ID PAPSS1 Link Image
Enzyme 27 HGNC ID HGNC:8603 Link Image
Enzyme 27 Chromosome Location 4
Enzyme 27 Locus 4q24
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Girard JP, Baekkevold ES, Amalric F: Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase. FASEB J. 1998 May;12(7):603-12. [PubMed Link Image]
  2. Venkatachalam KV, Akita H, Strott CA: Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains. J Biol Chem. 1998 Jul 24;273(30):19311-20. [PubMed Link Image]
  3. Yanagisawa K, Sakakibara Y, Suiko M, Takami Y, Nakayama T, Nakajima H, Takayanagi K, Natori Y, Liu MC: cDNA cloning, expression, and characterization of the human bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase enzyme. Biosci Biotechnol Biochem. 1998 May;62(5):1037-40. [PubMed Link Image]
  4. Xu ZH, Otterness DM, Freimuth RR, Carlini EJ, Wood TC, Mitchell S, Moon E, Kim UJ, Xu JP, Siciliano MJ, Weinshilboum RM: Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization. Biochem Biophys Res Commun. 2000 Feb 16;268(2):437-44. [PubMed Link Image]
  5. Venkatachalam KV, Fuda H, Koonin EV, Strott CA: Site-selected mutagenesis of a conserved nucleotide binding HXGH motif located in the ATP sulfurylase domain of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase. J Biol Chem. 1999 Jan 29;274(5):2601-4. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 5589
Enzyme 28 Name Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 2
Enzyme 28 Synonyms
  1. PAPS synthetase 2
  2. PAPSS 2
  3. Sulfurylase kinase 2
  4. SK2
  5. SK 2[Includes: Sulfate adenylyltransferase
  6. Sulfate adenylate transferase
  7. SAT
  8. ATP-sulfurylase
  9. Adenylyl-sulfate kinase
  10. Adenylylsulfate 3'-phosphotransferase
  11. APS kinase
  12. Adenosine-5'-phosphosulfate 3'-phosphotransferase
  13. 3'- phosphoadenosine-5'-phosphosulfate synthetase]
Enzyme 28 Gene Name PAPSS2
Enzyme 28 Protein Sequence >Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 2 
MSGIKKQKTENQQKSTNVVYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTISF
ALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITS
FISPFAKDRENARKIHESAGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDS
DYEKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVPYTIIKDIHELFVPENKLDHVRAE
AETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDGVINMSIPIVL
PVSAEDKTRLEGCSKFVLAHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVM
ESGDWLVGGDLQVLEKIRWNDGLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHAL
LMQDTRRRLLERGYKHPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLDPKSTIVAI
FPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAP
GLTSVEIIPFRVAAYNKAKKAMDFYDPARHNEFDFISGTRMRKLAREGENPPDGFMAPKA
WKVLTDYYRSLEKN
Enzyme 28 Number of Residues 614
Enzyme 28 Molecular Weight 69502
Enzyme 28 Theoretical pI 8.13
Enzyme 28 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleotide binding
  • nucleotidyltransferase activity
  • purine nucleotide binding
  • sulfate adenylyltransferase (ATP) activity
  • sulfate adenylyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • physiological process
  • sulfate assimilation
  • sulfur metabolism
  • sulfur utilization
Component
—
Enzyme 28 General Function Inorganic ion transport and metabolism
Enzyme 28 Specific Function Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS:activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate- activation pathway. May have a important role in skeletogenesis during postnatal growth
Enzyme 28 Pathways
Enzyme 28 Reactions
  • ATP + sulfate = diphosphate + adenylylsulfate
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 3769610 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID O95340 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name PAPS2_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >1845 bp 
ATGTCGGGGATCAAGAAGCAAAAGACGGAGAACCAGCAGAAATCCACCAATGTAGTCTAT
CAGGCCCACCATGTGAGCAGGAATAAGAGAGGGCAAGTGGTTGGAACAAGGGGTGGGTTC
CGAGGATGTACCGTGTGGCTAACAGGTCTCTCTGGTGCTGGAAAAACAACGATAAGTTTT
GCCCTGGAGGAGTACCTTGTCTCCCATGCCATCCCTTGTTACTCCCTGGATGGGGACAAT
GTCCGTCATGGCCTTAACAGAAATCTCGGATTCTCTCCTGGGGACAGAGAGGAAAATATC
CGCCGGATTGCTGAGGTGGCTAAGCTGTTTGCTGATGCTGGTCTGGTCTGCATTACCAGC
TTTATTTCTCCATTCGCAAAGGATCGTGAGAATGCCCGCAAAATACATGAATCAGCAGGG
CTGCCATTCTTTGAAATATTTGTAGATGCACCTCTAAATATTTGTGAAAGCAGAGACGTA
AAAGGCCTCTATAAAAGGGCCAGAGCTGGGGAGATTAAAGGATTTACAGGTATTGATTCT
GATTATGAGAAACCTGAAACTCCTGAGCGTGTGCTTAAAACCAATTTGTCCACAGTGAGT
GACTGTGTCCACCAGGTAGTGGAACTTCTGCAAGAGCAGAACATTGTACCCTATACTATA
ATCAAAGATATCCACGAACTCTTTGTGCCGGAAAACAAACTTGACCACGTCCGAGCTGAG
GCTGAAACTCTCCCTTCATTATCAATTACTAAGCTGGATCTCCAGTGGGTCCAGGTTTTG
AGCGAAGGCTGGGCCACTCCCCTCAAAGGTTTCATGCGGGAGAAGGAGTACTTACAGGTT
ATGCACTTTGACACCCTGCTAGATGATGGCGTGATCAACATGAGCATCCCCATTGTACTG
CCCGTCTCTGCAGAGGATAAGACACGGCTGGAAGGGTGCAGCAAGTTTGTCCTGGCACAT
GGTGGACGGAGGGTAGCTATCTTACGAGACGCTGAATTCTATGAACACAGAAAAGAGGAA
CGCTGTTCCCGTGTTTGGGGGACAACATGTACAAAACACCCCCATATCAAAATGGTGATG
GAAAGTGGGGACTGGCTGGTTGGTGGAGACCTTCAGGTGCTGGAGAAAATAAGATGGAAT
GATGGGCTGGACCAATACCGTCTGACACCTCTGGAGCTCAAACAGAAATGTAAAGAAATG
AATGCTGATGCGGTGTTTGCATTCCAGTTGCGCAATCCTGTCCACAATGGCCATGCCCTG
TTGATGCAGGACACCTGCCGCAGGCTCCTAGAGAGGGGCTACAAGCACCCGGTCCTCCTA
CTACACCCTCTGGGCGGCTGGACCAAGGATGACGATGTGCCTCTAGACTGGCGGATGAAG
CAGCACGCGGCTGTGCTCGAGGAAGGGGTCCTGGATCCCAAGTCAACCATTGTTGCCATC
TTTCCGTCTCCCATGTTATATGCTGGCCCCACAGAGGTCCAGTGGCACTGCAGGTCCCGG
ATGATTGCGGGTGCCAATTTCTACATTGTGGGGAGGGACCCTGCAGGAATGCCCCATCCT
GAAACCAAGAAGGATCTGTATGAACCCACTCATGGGGGCAAGGTCTTGAGCATGGCCCCT
GGCCTCACCTCTGTGGAAATCATTCCATTCCGAGTGGCTGCCTACAACAAAGCCAAAAAA
GCCATGGACTTCTATGATCCAGCAAGGCACAATGAGTTTGACTTCATCTCAGGAACTCGA
ATGAGGAAGCTCGCCCGGGAAGGAGAGAATCCCCCAGATGGCTTCATGGCCCCCAAAGCA
TGGAAGGTCCTGACAGATTATTACAGGTCCCTGGAGAAGAACTAA
Enzyme 28 GenBank Gene ID AF091242 Link Image
Enzyme 28 GeneCard ID PAPSS2 Link Image
Enzyme 28 GenAtlas ID PAPSS2 Link Image
Enzyme 28 HGNC ID HGNC:8604 Link Image
Enzyme 28 Chromosome Location 10
Enzyme 28 Locus 10q23-q24
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. ul Haque MF, King LM, Krakow D, Cantor RM, Rusiniak ME, Swank RT, Superti-Furga A, Haque S, Abbas H, Ahmad W, Ahmad M, Cohn DH: Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse. Nat Genet. 1998 Oct;20(2):157-62. [PubMed Link Image]
  2. Xu ZH, Otterness DM, Freimuth RR, Carlini EJ, Wood TC, Mitchell S, Moon E, Kim UJ, Xu JP, Siciliano MJ, Weinshilboum RM: Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization. Biochem Biophys Res Commun. 2000 Feb 16;268(2):437-44. [PubMed Link Image]
  3. Kurima K, Singh B, Schwartz NB: Genomic organization of the mouse and human genes encoding the ATP sulfurylase/adenosine 5'-phosphosulfate kinase isoform SK2. J Biol Chem. 1999 Nov 19;274(47):33306-12. [PubMed Link Image]
  4. Ahmad M, Haque MF, Ahmad W, Abbas H, Haque S, Krakow D, Rimoin DL, Lachman RS, Cohn DH: Distinct, autosomal recessive form of spondyloepimetaphyseal dysplasia segregating in an inbred Pakistani kindred. Am J Med Genet. 1998 Aug 6;78(5):468-73. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 5595
Enzyme 29 Name Carbamoyl-phosphate synthase [ammonia], mitochondrial precursor
Enzyme 29 Synonyms
  1. Carbamoyl-phosphate synthetase I
  2. CPSase I
Enzyme 29 Gene Name CPS1
Enzyme 29 Protein Sequence >Carbamoyl-phosphate synthase [ammonia], mitochondrial precursor 
MTRILTAFKVVRTLKTGFGFTNVTAHQKWKFSRPGIRLLSVKAQTAHIVLEDGTKMKGYS
FGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTTALDELGLSKY
LESNGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTML
GKIEFEGQPVDFVDPNKQNLIAEVSTKDVKVYGKGNPTKVVAVDCGIKNNVIRLLVKRGA
EVHLVPWNHDFTKMEYDGILIAGGPGNPALAEPLIQNVRKILESDRKEPLFGISTGNLIT
GLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALDNTLPAGWKPLFVNVNDQT
NEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIKKGKATTITSVLPKPALVASRV
EVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEVGLKQAD
TVYFLPITPQFVTEVIKAEQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVES
IMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAADTIGYPVMIRSAYALGGLGSGIC
PNRETLMDLSTKAFAMTNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMGVHT
GDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLS
RSSALASKATGYPLAFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDR
FHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSIEGFTPRLPMNKEWPSNLDLR
KELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGLNSESMT
EETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYV
TYNGQEHDVNFDDHGMMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETV
STDFDECDKLYFEELSLERILDIYHQEACGGCIISVGGQIPNNLAVPLYKNGVKIMGTSP
LQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMN
VVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAVGKDGRVISHAISEHVEDAG
VHSGDATLMLPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRA
SRSFPFVSKTLGVDFIDVATKVMIGENVDEKHLPTLDHPIIPADYVAIKAPMFSWPRLRD
ADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKGILIGIQQSFRPRFLGVAEQ
LHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSLSSIRKLIRDGSIDLVINLPN
NNTKFVHDNYVIRRTAVDSGIPLLTNFQVTKLFAEAVQKSRKVDSKSLFHYRQYSAGKAA
Enzyme 29 Number of Residues 1500
Enzyme 29 Molecular Weight 164941
Enzyme 29 Theoretical pI 6.71
Enzyme 29 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • carbamoyl-phosphate synthase activity
  • catalytic activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
  • nucleotide binding
  • purine nucleotide binding
Process
  • amino acid and derivative metabolism
  • amino acid metabolism
  • arginine biosynthesis
  • arginine metabolism
  • cellular metabolism
  • glutamine family amino acid metabolism
  • glutamine metabolism
  • metabolism
  • nitrogen compound metabolism
  • nucleobase metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
  • pyrimidine base biosynthesis
  • pyrimidine base metabolism
  • urea cycle intermediate metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 29 General Function Amino acid transport and metabolism
Enzyme 29 Specific Function Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell
Enzyme 29 Pathways
Enzyme 29 Reactions
  • 2 ATP + NH3 + CO2 + H2O = 2 ADP + phosphate + carbamoyl phosphate
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • 1-19
Enzyme 29 Transmembrane Regions Not Available
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 219553 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID P31327 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name CPSM_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >4503 bp 
ATGACGAGGATTTTGACAGCTTTCAAAGTGGTGAGGACACTGAAGACTGGTTTTGGCTTT
ACCAATGTGACTGCACACCAAAAATGGAAATTTTCAAGACCTGGCATCAGGCTCCTTTCT
GTCAAGGCACAGACAGCACACATTGTCCTGGAAGATGGAACTAAGATGAAAGGTTACTCC
TTTGGCCATCCATCCTCTGTTGCTGGTGAAGTGGTTTTTAATACTGGCCTGGGAGGGTAC
CCAGAAGCTATTACTGACCCTGCCTACAAAGGACAGATTCTCACAATGGCCAACCCTATT
ATTGGGAATGGTGGAGCTCCTGATACTACTTCTCTGGATGAACTGGGACTTAGCAAATAT
TTGGAGTCTAATGGAATCAAGGTTTCAGGTTTGCTGGTGCTGGATTATAGTAAAGACTAC
AACCACTGGCTGGCTACCAAGAGTTTAGGGCAATGGCTACAGGAAGAAAAGGTTCCTGCA
ATTTATGGAGTGGACACAAGAATGCTGACTAAAATAATTCGGGATAAGGGTACCATGCTT
GGGAAGATTGAATTTGAAGGTCAGCCTGTGGATTTTGTGGATCCAAATAAACAGAATTTG
ATTGCTGAGGTTTCAACCAAGGATGTCAAAGTGTACGGCAAAGGAAACCCCACAAAAGTG
GTAGCTGTAGACTGTGGGATTAAAAACAATGTAATCCGCCTGCTAGTAAAGCGAGGAGCT
GAAGTGCACTTAGTTCCCTGGAACCATGATTTCACCAAGATGGAGTATGATGGGATTTTG
ATCGCGGGAGGACCGGGGAACCCAGCTCTTGCAGAACCACTAATTCAGAATGTTCAGAAG
ATTTTGGAGAGTGATCGCAAGGAGCCATTGTTTGGAATCAGTACAGGAAACTTAATAACA
GGATTGGCTGCTGGTGCCAAAACCTACAAGATGTCCATGGCCAACAGAGGGCAGAATCAG
CCTGTTTTGAATATCACAAACAAACAGGCTTTCATTACTGCTCAGAATCATTGCTATGCC
TTGGACAACACCCTCCCTGCTGGCTGGAAACCACTTTTTGTGAATGTCAACGATCAAACA
AATGAGGGGATTATGCATGAGAGCAAACCCTTCTTCGCTGTGCAGTTCCACCCAGAGGTC
ACCCCGGGGCCAATAGACACTGAGTACCTGTTTGATTCCTTTTTCTCACTGATAAAGAAA
GGAAAAGCTACCACCATTACATCAGTCTTACCGAAGCCAGCACTAGTTGCATCTCGGGTT
GAGGTTTCCAAAGTCCTTATTCTAGGATCAGGAGGTCTGTCCATTGGTCAGGCTGGAGAA
TTTGATTACTCAGGATCTCAAGCTGTAAAAGCCATGAAGGAAGAAAATGTCAAAACTGTT
CTGATGAACCCAAACATTGCATCAGTCCAGACCAATGAGGTGGGCTTAAAGCAAGCGGAT
ACTGTCTACTTTCTTCCCATCACCCCTCAGTTTGTCACAGAGGTCATCAAGGCAGAACAG
CCAGATGGGTTAATTCTGGGCATGGGTGGCCAGACAGCTCTGAACTGTGGAGTAGAACTA
TTCAAGAGAGGTGTGCTCAAGGAATATGGTGTGAAAGTCCTGGGAACTTCAGTTGAGTCC
ATTATGGCTACGGAAGACAGGCAGCTGTTTTCAGATAAACTAAATGAGATCAATGAAAAG
ATTGCTCCAAGTTTTGCAGTGGAATCGATTGAGGATGCACTGAAGGCAGCAGACACCATT
GGCTACCCAGTGATGATCCGTTCCGCCTATGCACTGGGTGGGTTAGGCTCAGGCATCTGT
CCCAACAGAGAGACTTTGATGGACCTCAGCACAAAGGCCTTTGCTATGACCAACCAAATT
CTGGTGGAGAAGTCAGTGACAGGTTGGAAAGAAATAGAATATGAAGTGGTTCGAGATGCT
GATGACAATTGTGTCACTGTCTGTAACATGGAAAATGTTGATGCCATGGGTGTTCACACA
GGTGACTCAGTTGTTGTGGCTCCTGCCCAGACACTCTCCAATGCCGAGTTTCAGATGTTG
AGACGTACTTCAATCAATGTTGTTCGCCACTTGGGCATTGTGGGTGAATGCAACATTCAG
TTTGCCCTTCATCCTACCTCAATGGAATACTGCATCATTGAAGTGAATGCCAAGATGTCC
CCGAACTCTGCTCTGGCCTCCAAAACGACTGGCTACCCATTGGCATTCATTGCTGCAAAG
ATTGCCCTAGGAATCCCACTTCCAGGAATTAAGAACGTCGTATCCGGGAAGACATCAGCC
TGTTTTGAACCTAGCCTGGATTACATGGTCACCAAGATTCCCCGCTGGGATCTTGACCGT
TTTCATGGAACATCTAGCCGAATTGGTAGCTCTATGAAAAGTGTAGGAGAGGTCATGGCT
ATTGGTCGTACCTTTGAGGAGAGTTTCCAGAAAGCTTTACGGATGTGCCACCCATCTATA
GAGGGTTTCACTCCCCGTCTCCCAATGAACAAAGAATGGCCATCGAATTTAGATCTTAGA
AAAGAGTTGTCTGAACCAAGCAGCACGCGTATCTATGCCATTGCCAAGGCCATTGATGAC
AACATGTCCCTTGATGAGATTGAGAAGCTCACATACATTGACAAGTGGTTTTTGTATAAG
ATGCGTGATATTTTAAACATGGAAAAGACACTGAAAGGCCTCAACAGTGAGTCCATGACA
GAAGAAACCCTGAAAAGGGCAAAGGAGATTGGGTTCTCAGATAAGCAGATTTCAAAATGC
CTTGGGCTCACTGAGGCCCAGACAAGGGAGCTGAGGTTAAAGAAAAACATCCACCCTTGG
GTTAAACAGATTGATACACTGGCTGCAGAATACCCATCAGTAACAAACTATCTCTATGTT
ACCTACAATGGTCAGGAGCATGATGTCAATTTTGATGACCATGGAATGATGGTGCTAGGC
TGTGGTCCATATCACATTGGCAGCAGTGTGGAATTTGATTGGTGTGCTGTCTCTAGTATC
CGCACACTGCGTCAACTTGGCAAGAAGACGGTGGTGGTGAATTGCAATCCTGAGACTGTG
AGCACAGACTTTGATGAGTGTGACAAACTGTACTTTGAAGAGTTGTCCTTGGAGAGAATC
CTAGACATCTACCATCAGGAGGCATGTGGTGGCTGCATCATATCAGTTGGAGGCCAGATT
CCAAACAACCTGGCAGTTCCTCTATACAAGAATGGTGTCAAGATCATGGGCACAAGCCCC
CTGCAGATCGACAGGGCTGAGGATCGCTCCATCTTCTCAGCTGTCTTGGATGAGCTGAAG
GTGGCTCAGGCACCTTGGAAAGCTGTTAATACTTTGAATGAAGCACTGGAATTTGCAAAG
TCTGTGGACTACCCCTGCTTGTTGAGGCCTTCCTATGTTTTGAGTGGGTCTGCTATGAAT
GTGGTATTCTCTGAGGATGAGATGAAAAAATTCCTAGAAGAGGCGACTAGAGTTTCTCAG
GCCACGCCAGTGGTGCTGACAAAATTTGTTGAAGGGGCCCGAGAAGTAGAAATGGACGCT
GTTGGCAAAGATGGAAGGGTTATCTCTCATGCCATCTCTGAACATGTTGAAGATGCAGGT
GTCCACTCGGAGAATGCCACTCTGATGCTGCCCACACAAACCATCAGCCAAGGGGCCATT
GAAAAGGTGAAGGATGCTACCCGGAAGATTGCAAAGGCTTTTGCCATCTCTGGTCCATTC
AACGTCCAATTTCTTGTCAAAGGAAATGATGTCTTGGTGAATGAGTGTAACTTGAGAGCT
TCTCGATCCTTCCCCTCTGTTTCCAAGACTCTTGGGGTTGACTTCATTGATGTGGCCACC
AAGGTGTTGATTGGAGAGAATGTTGATGAGAAACATCTTCCAACATTGGACCATCCCATA
ATTCCTGTTGACTATGTTGCAATTAAGGCTCCCATGTTTTCCTGGCCCCGGTTGAGGGAT
GCTGACCCCATTCTGAGATGTGAGATGGCTTCCACTGGAGAGGTGGCTTGCTTTGGTGAA
GGTATTCATACAGCCTTCCTAAAGGCAATGCTTTCCACAGGATTTAAGATACCCCAGAAA
GGCATCCTGATAGGCATCCAGCAATCATTCCGGCCAAGATTCCTTGGTGTGGCTGAACAA
TTACACAATGAAGGTTTCAAGCTGTTTGCCACGGAAGCCACATCAGACTGGCTCAACGCC
AACAATGTCCCTGCCAACCCAGTGGCATGGCCGTCTCAAGAAGGACAGAATCCCAGCCTC
TCTTCCATCAGAAAATTGATTAGAGATGGCAGCATTGACCTAGTGATTAACCTTCCCAAC
AACAACACTAAATTTGTCCATGATAATTATGTGATTCGGAGGACAGCTGTTGATAGTGGA
ATCCCTCTCCTCACTAATTTTCAGGTGACCAAACTTTTTGCTGAAGCTGTGCAGAAATCT
CGCAAGGTGGACTCCAAGAGTCTTTTCCACTACAGGCAGTACAGTGCTGGAAAAGCAGCA
TAG
Enzyme 29 GenBank Gene ID D90282 Link Image
Enzyme 29 GeneCard ID CPS1 Link Image
Enzyme 29 GenAtlas ID CPS1 Link Image
Enzyme 29 HGNC ID HGNC:2323 Link Image
Enzyme 29 Chromosome Location 2
Enzyme 29 Locus 2q35
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Haraguchi Y, Uchino T, Takiguchi M, Endo F, Mori M, Matsuda I: Cloning and sequence of a cDNA encoding human carbamyl phosphate synthetase I: molecular analysis of hyperammonemia. Gene. 1991 Nov 15;107(2):335-40. [PubMed Link Image]
  2. Finckh U, Kohlschutter A, Schafer H, Sperhake K, Colombo JP, Gal A: Prenatal diagnosis of carbamoyl phosphate synthetase I deficiency by identification of a missense mutation in CPS1. Hum Mutat. 1998;12(3):206-11. [PubMed Link Image]
  3. Funghini S, Donati MA, Pasquini E, Zammarchi E, Morrone A: Structural organization of the human carbamyl phosphate synthetase I gene (CPS1) and identification of two novel genetic lesions. Hum Mutat. 2003 Oct;22(4):340-1. [PubMed Link Image]
  4. Aoshima T, Kajita M, Sekido Y, Kikuchi S, Yasuda I, Saheki T, Watanabe K, Shimokata K, Niwa T: Novel mutations (H337R and 238-362del) in the CPS1 gene cause carbamoyl phosphate synthetase I deficiency. Hum Hered. 2001;52(2):99-101. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 5605
Enzyme 30 Name ADP-dependent glucokinase
Enzyme 30 Synonyms
  1. ADPGK
  2. ADP-GK
  3. RbBP-35
Enzyme 30 Gene Name ADPGK
Enzyme 30 Protein Sequence >ADP-dependent glucokinase 
MALWRGSAYAGFLALAVGCVFLLEPELPGSALRSLWSSLCLGPAPAPPGPVSPEGRLAAA
WDALIVRPVRRWRRVAVGVNACVDVVLSGVKLLQALGLSPGNGKDHSILHSRNDLEEAFI
HFMGKGAAAERFFSDKETFHDIAQVASEFPGAQHYVGGNAALIGQKFAANSDLKVLLCGP
VGPKLHELLDDNVFVPPESLQEVDEFHLILEYQAGEEWGQLKAPHANRFIFSHDLSNGAM
NMLEVFVSSLEEFQPDLVVLSGLHMMEGQSKELQRKRLLEVVTSISDIPTGIPVHLELAS
MTNRELMSSIVHQQVFPAVTSLGLNEQELLFLTQSASGPHSSLSSWNGVPDVGMVSDILF
WILKEHGRSKSRASDLTRIHFHTLVYHILATVDGHWANQLAAVAAGARVAGTQACATETI
DTSRVSLRAPQEFMTSHSEAGSRIVLNPNKPVVEWHREGISFHFTPVLVCKDPIRTVGLG
DAISAEGLFYSEVHPHY
Enzyme 30 Number of Residues 497
Enzyme 30 Molecular Weight 54089
Enzyme 30 Theoretical pI 6.17
Enzyme 30 GO Classification
Function
  • catalytic activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • carbohydrate metabolism
  • cellular metabolism
  • glucose metabolism
  • hexose metabolism
  • macromolecule metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
—
Enzyme 30 General Function Not Available
Enzyme 30 Specific Function Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor. GDP and CDP can replace ADP, but with reduced efficiency
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions
  • ADP + D-glucose = AMP + D-glucose 6-phosphate
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • 1-22
Enzyme 30 Transmembrane Regions Not Available
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 16923351 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID Q9BRR6 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name ADPGK_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >1044 bp 
ATGGGGAAGGGAGCAGCTGCTGAGCGCTTCTTCAGTGATAAGGAAACTTTTCACGACATT
GCCCAGGTTGCGTCAGAGTTCCCAGGAGCCCAGCACTATGTAGGAGGAAATGCAGCTTTA
ATTGGACAGAAATTTGCAGCCAACTCAGATTTAAAGGTTCTTCTTTGCGGTCCAGTTGGT
CCAAAGCTACATGAGCTTCTTGATGACAATGTCTTTGTTCCACCAGAGTCATTGCAGGAA
GTGGATGAGTTCCACCTCATTTTAGAGTATCAAGCAGGGGAGGAGTGGGGCCAGTTAAAA
GCTCCCCATGCCAACCGATTCATCTTCTCTCACGACCTCTCCAACGGGGCCATGAATATG
CTGGAGGTGTTTGTGTCTAGCCTGGAGGAGTTTCAGCCAGACCTGGTGGTCCTCTCTGGA
TTGCACATGATGGAGGGACAAAGCAAGGAGCTCCAGAGGAAGAGACTCTTGGAGGTTGTA
ACCTCCATTTCTGACATCCCCACTGGTATTCCAGTTCACCTAGAGCTGGCCAGTATGACT
AACAGGGAGCTCATGAGCAGCATTGTCCATCAGCAGGTCTTTCCCGCGGTGACTTCCCTT
GGGCTGAATGAACAGGAGCTGTTATTTCTCACCCAGTCAGCCTCTGGACCTCACTCTTCT
CTCTCTTCCTGGAACGGTGTTCCTGATGTGGGCATGGTCAGTGACATCCTCTTCTGGATC
TTGAAAGAACATGGGAGGAGTAAAAGCAGAGCCTCGGATCTCACCAGGATCCATTTCCAC
ACGCTGGTCTACCACATCCTGGCAACTGTGGATGGACACTGGGCCAACCAGCTGGCAGCC
GTGTTAGGAAGCTCGTGTGGCTGGGACACAGGCCTGCGCCACAGAAACCATAGACACCAG
CCGAGTGTCTCTGAGGGCACCCCAAGAGTTCATGACTTCCCATTCGGAGGCAGGCTCCAG
GATTGTATTAAACCCAAACAAGCCAGTAGTAGAATGGCACAGAGAGGGAATATCCTTCCA
CTTCACACCAGTATTGGTGTGTAA
Enzyme 30 GenBank Gene ID AF204270 Link Image
Enzyme 30 GeneCard ID ADPGK Link Image
Enzyme 30 GenAtlas ID ADPGK Link Image
Enzyme 30 HGNC ID HGNC:25250 Link Image
Enzyme 30 Chromosome Location Not Available
Enzyme 30 Locus Not Available
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 5755
Enzyme 31 Name Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial precursor
Enzyme 31 Synonyms
  1. 3-methylcrotonyl-CoA carboxylase 2
  2. MCCase subunit beta
  3. 3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta
  4. 3- methylcrotonyl-CoA carboxylase non-biotin-containing subunit
Enzyme 31 Gene Name MCCC2
Enzyme 31 Protein Sequence >Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial precursor 
MWAVLRLALRPCARASPAGPRAYHGDSVASLGTQPDLGSALYQENYKQMKALVNQLHERV
EHIKLGGGEKARALHISRGKLLPRERIDNLIDPGSPFLELSQFAGYQLYDNEEVPGGGII
TGIGRVSGVECMIIANDATVKGGAYYPVTVKKQLRAQEIAMQNRLPCIYLVDSGGAYLPR
QADVFPDRDHFGRTFYNQAIMSSKNIAQIAVVMGSCTAGGAYVPAMADENIIVRKQGTIF
LAGPPLVKAATGEEVSAEDLGGADLHCRKSGVSDHWALDDHHALHLTRKVVRNLNYQKKL
DVTIEPSEEPLFPADELYGIVGANLKRSFDVREVIARIVDGSRFTEFKAFYGDTLVTGFA
RIFGYPVGIVGNNGVLFSESAKKGTHFVQLCCQRNIPLLFLQNITGFMVGREYEAEGIAK
DGAKMVAAVACAQVPKITLIIGGSYGAGNYGMCGRAYSPRFLYIWPNARISVMGGEQAAN
VLATITKDQRAREGKQFSSADEAALKEPIIKKFEEEGNPYYSSARVWDDGIIDPADTRLV
LGLSFSAALNAPIEKTDFGIFRM
Enzyme 31 Number of Residues 563
Enzyme 31 Molecular Weight 61334
Enzyme 31 Theoretical pI 7.75
Enzyme 31 GO Classification
Function
  • catalytic activity
  • ligase activity
Process
—
Component
—
Enzyme 31 General Function Not Available
Enzyme 31 Specific Function ATP + 3-methylcrotonoyl-CoA + HCO(3)(-) = ADP + phosphate + 3-methylglutaconyl-CoA
Enzyme 31 Pathways
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 31 Reactions
  • ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate + 3-methylglutaconyl-CoA
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • 1-15
Enzyme 31 Transmembrane Regions Not Available
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 10934059 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q9HCC0 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name MCCC2_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >1692 bp 
ATGTGGGCCGTCCTGAGGTTAGCCCTGCGGCCGTGTGCCCGCGCCTCTCCCGCCGGGCCG
CGCGCCTATCACGGGGACTCGGTGGCCTCGCTGGGCACCCAGCCGGACTTGGGCTCTGCC
CTCTACCAGGAGAACTACAAGCAGATGAAAGCACTAGTAAATCAGCTCCATGAACGAGTG
GAGCATATAAAACTAGGAGGTGGTGAGAAAGCCCGAGCACTTCACATATCAAGAGGAAAA
CTATTGCCCAGAGAAAGAATTGACAATCTCATAGACCCAGGGTCTCCATTTCTGGAATTA
TCCCAGTTTGCAGGTTACCAGTTATATGACAATGAGGAGGTGCCAGGAGGTGGCATTATT
ACAGGCATTGGAAGAGTATCAGGAGTAGAATGCATGATTATTGCCAATGATGCCACCGTC
AAAGGAGGTGCCTACTACCCAGTGACTGTGAAAAAACAATTACGGGCCCAAGAAATTGCC
ATGCAAAACAGGCTCCCCTGCATCTACTTAGTTGATTCGGGAGGAGCATACTTACCTCGA
CAAGCAGATGTGTTTCCAGATCGAGACCACTTTGGCCGTACATTCTATAATCAGGCAATT
ATGTCTTCTAAAAATATTGCACAGATCGCAGTGGTCATGGGCTCCTGCACCGCAGGAGGA
GCCTATGTGCCTGCCATGGCTGATGAAAACATCATTGTACGCAAGCAGGGTACCATTTTC
TTGGCAGGACCCCCCTTGGTTAAAGCGGCAACTGGGGAAGAAGTATCTGCTGAGGATCTT
GGAGGTGCTGATCTTCATTGCAGAAAGTCTGGAGTAAGTGACCACTGGGCTTTGGATGAT
CATCATGCCCTTCACTTAACTAGGAAGGTTGTGAGGAATCTAAATTATCAGAAGAAATTG
GATGTCACCATTGAACCTTCTGAAGAGCCTTTATTTCCTGCTGATGAATTGTATGGAATA
GTTGGTGCTAACCTTAAGAGGAGCTTTGATGTCCGAGAGGTCATTGCTAGAATCGTGGAT
GGAAGCAGATTCACTGAGTTCAAAGCCTTTTATGGAGACACATTAGTTACAGGATTTGCT
CGAATATTTGGGTACCCAGTAGGTATCGTTGGAAACAACGGAGTTCTCTTTTCTGAATCT
GCAAAAAAGGGTACTCACTTTGTCCAGTTATGCTGCCAAAGAAATATTCCTCTGCTGTTC
CTTCAAAACATTACTGGATTTATGGTTGGTAGAGAGTATGAAGCTGAAGGAATTGCCAAG
GATGGTGCCAAGATGGTGGCCGCTGTGGCCTGTGCCCAAGTGCCTAAGATAACCCTCATC
ATTGGGGGCTCCTATGGAGCCGGAAACTATGGGATGTGTGGCAGAGCGTATAGCCCAAGA
TTTCTCTACATTTGGCCAAATGCTCGTATCTCAGTGATGGGAGGAGAGCAGGCAGCCAAT
GTGTTGGCCACGATAACAAAGGACCAAAGAGCCCGGGAAGGAAAGCAGTTCTCCAGTGCT
GATGAAGCGGCTTTAAAAGAGCCCATCATTAAGAAGTTTGAAGAGGAAGGAAACCCTTAC
TATTCCAGCGCAAGGGTATGGGATGATGGGATCATTGATCCAGCAGACACCAGACTGGTC
TTGGGTCTCAGTTTTAGTGCAGCCCTCAACGCACCAATAGAGAAGACTGACTTCGGTATC
TTCAGGATGTAA
Enzyme 31 GenBank Gene ID AB050049 Link Image
Enzyme 31 GeneCard ID MCCC2 Link Image
Enzyme 31 GenAtlas ID MCCC2 Link Image
Enzyme 31 HGNC ID HGNC:6937 Link Image
Enzyme 31 Chromosome Location Not Available
Enzyme 31 Locus Not Available
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Holzinger A, Roschinger W, Lagler F, Mayerhofer PU, Lichtner P, Kattenfeld T, Thuy LP, Nyhan WL, Koch HG, Muntau AC, Roscher AA: Cloning of the human MCCA and MCCB genes and mutations therein reveal the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency. Hum Mol Genet. 2001 Jun 1;10(12):1299-306. [PubMed Link Image]
  2. Baumgartner MR, Almashanu S, Suormala T, Obie C, Cole RN, Packman S, Baumgartner ER, Valle D: The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency. J Clin Invest. 2001 Feb;107(4):495-504. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 5757
Enzyme 32 Name Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial precursor
Enzyme 32 Synonyms
  1. 3-methylcrotonyl-CoA carboxylase 1
  2. MCCase subunit alpha
  3. 3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha
  4. 3- methylcrotonyl-CoA carboxylase biotin-containing subunit
Enzyme 32 Gene Name MCCC1
Enzyme 32 Protein Sequence >Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial precursor 
MAAASAVSVLLVAAERNRWHRLPSLLLPPRTWVWRQRTMKYTTATGRNITKVLIANRGEI
ACRVMRTAKKLGVQTVAVYSEADRNSMHVDMADEAYSIGPAPSQQSYLSMEKIIQVAKTS
AAQAIHPGCGFLSENMEFAELCKQEGIIFIGPPPSAIRDMGIKSTSKSIMAAAGVPVVEG
YHGEDQSDQCLKEHARRIGYPVMIKAVRGGGGKGMRIVRSEQEFQEQLESARREAKKSFN
DDAMLIEKFVDTPRHVEVQVFGDHHGNAVYLFERDCSVQRRHQKIIEEAPAPGIKSEVRK
KLGEAAVRAAKAVNYVGAGTVEFIMDSKHNFCFMEMNTRLQVEHPVTEMITGTDLVEWQL
RIAAGEKIPLSQEEITLQGHAFEARIYAEDPSNNFMPVAGPLVHLSTPRADPSTRIETGV
RQGDEVSVHYDPMIAKLVVWAADRQAALTKLRYSLRQYNIVGLHTNIDFLLNLSGHPEFE
AGNVHTDFIPQHHKQLLLSRKAAAKESLCQAALGLILKEKAMTDTFTLQAHDQFSPFSSS
SGRRLNISYTRNMTLKDGKNNVAIAVTYNHDGSYSMQIEDKTFQVLGNLYSEGDCTYLKC
SVNGVASKAKLIILENTIYLFSKEGSIEIDIPVPKYLSSVSSQETQGGPLAPMTGTIEKV
FVKAGDKVKAGDSLMVMIAMKMEHTIKSPKDGTVKKVFYREGAQANRHTPLVEFEEEESD
KRESE
Enzyme 32 Number of Residues 725
Enzyme 32 Molecular Weight 80474
Enzyme 32 Theoretical pI 7.86
Enzyme 32 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • biotin binding
  • catalytic activity
  • ligase activity
  • nucleotide binding
  • purine nucleotide binding
  • vitamin binding
Process
  • metabolism
  • physiological process
Component
—
Enzyme 32 General Function Not Available
Enzyme 32 Specific Function ATP + 3-methylcrotonoyl-CoA + HCO(3)(-) = ADP + phosphate + 3-methylglutaconyl-CoA
Enzyme 32 Pathways
  • Valine, Leucine and Isoleucine Degradation (map00280 Link Image)
Enzyme 32 Reactions
  • ATP + 3-methylcrotonoyl-CoA + HCO3- = ADP + phosphate + 3-methylglutaconyl-CoA
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • 1-14
Enzyme 32 Transmembrane Regions Not Available
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 12382296 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID Q96RQ3 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name MCCA_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >2178 bp 
ATGGCGGCGGCCTCTGCGGTGTCGGTGCTGCTGGTGGCGGCGGAGAGGAACCGGTGGCAT
CGTCTCCCGAGCCTGCTCCTGCCGCCGAGGACATGGGTGTGGAGGCAAAGAACCATGAAG
TACACAACAGCCACAGGAAGAAACATTACCAAGGTCCTCATTGCAAACAGAGGAGAAATT
GCCTGCAGGGTGATGCGCACAGCCAAAAAACTGGGTGTACAGACTGTGGCGGTTTATAGT
GAGGCTGACAGAAATTCCATGCATGTAGATATGGCAGATGAAGCATATTCCATCGGCCCC
GCTCCCTCCCAGCAGAGCTACCTATCTATGGAGAAAATCATTCAAGTGGCCAAGACCTCT
GCTGCACAGGCTATCCATCCAGGATGCGGTTTTCTTTCAGAAAACATGGAATTTGCTGAA
CTTTGTAAGCAAGAAGGAATTATTTTTATAGGCCCTCCTCCATCTGCAATTAGAGACATG
GGTATAAAGAGCACATCCAAATCCATAATGGCTGCTGCTGGAGTACCTGTTGTGGAGGGT
TATCATGGTGAGGACCAATCAGACCAGTGCCTGAAGGAACACGCCAGGAGAATTGGCTAT
CCTGTCATGATTAAAGCCGTCCGGGGTGGAGGAGGAAAAGGAATGAGGATTGTTAGATCA
GAACAAGAATTTCAAGAACAGTTAGAGTCAGCACGGAGAGAAGCTAAGAAGTCTTTCAAT
GATGATGCTATGCTGATCGAGAAGTTTGTAGACACACCGAGGCATGTAGAAGTCCAGGTG
TTTGGTGATCACCATGGCAATGCTGTGTACTTGTTTGAAAGAGACTGTAGTGTGCAGAGG
CGACATCAGAAGATCATTGAGGAGGCCCCAGCGCCTGGTATTAAATCTGAAGTAAGAAAA
AAGCTGGGAGAAGCTGCAGTCAGAGCTGCTAAAGCTGTAAATTATGTTGGAGCAGGGACT
GTGGAGTTTATTATGGACTCAAAACATAATTTCTGTTTCATGGAGATGAATACAAGGCTG
CAAGTGGAACATCCTGTTACTGAGATGATCACAGGAACTGACTTGGTGGAGTGGCAGCTT
AGAATTGCAGCAGGAGAGAAGATTCCTTTGAGCCAGGAAGAAATAACTCTGCAGGGCCAT
GCCTTCGAAGCTAGAATATATGCAGAAGATCCTAGCAATAACTTCATGCCTGTGGCAGGC
CCATTAGTGCACCTCTCTACTCCTCGAGCAGACCCTTCCACCAGGATTGAAACTGGAGTA
CGGCAAGGAGACGAAGTTTCCGTGCATTATGACCCCATGATTGCGAAGCTGGTCGTGTGG
GCAGCAGATCGCCAGGCGGCATTGACAAAACTGAGGTACAGCCTTCGTCAGTACAATATT
GTTGGACTGCACACCAACATTGACTTCTTACTCAACCTGTCTGGCCACCCAGAGTTTGAA
GCTGGGAACGTGCACACTGATTTCATCCCTCAACACCACAAACAGTTGTTGCTCAGTCGG
AAGGCTGCAGCCAAAGAGTCTTTATGCCAGGCAGCCCTGGGTCTCATCCTCAAGGAGAAA
GCCATGACCGACACTTTCACTCTTCAGGCACATGATCAATTCTCTCCATTTTCGTCTAGC
AGTGGAAGAAGACTGAATATCTCGTATACCAGAAACATGACTCTTAAAGATGGTAAAAAC
AATGTAGCCATAGCTGTAACGTATAACCATGATGGGTCTTATAGCATGCAGATTGAAGAT
AAAACTTTCCAAGTCCTTGGTAATCTTTACAGCGAGGGAGACTGCACTTACCTGAAATGT
TCTGTTAATGGAGTTGCTAGTAAAGCGAAGCTGATTATCCTGGAAAACACTATTTACCTA
TTTTCCAAGGAAGGAAGTATTGAGATTGACATTCCAGTCCCCAAATACTTATCTTCTGTG
AGCTCACAAGAAACTCAGGGCGGCCCCTTAGCTCCTATGACTGGAACCATTGAAAAGGTG
TTTGTCAAAGCTGGAGACAAAGTGAAAGCGGGAGATTCCCTCATGGTTATGATCGCCATG
AAGATGGAGCATACCATAAAGTCTCCAAAGGATGGCACAGTAAAGAAAGTGTTCTACAGA
GAAGGTGCTCAGGCCAACAGACACACTCCTTTAGTCGAGTTTGAGGAGGAAGAATCAGAC
AAAAGGGAATCGGAATAA
Enzyme 32 GenBank Gene ID AF310972 Link Image
Enzyme 32 GeneCard ID MCCC1 Link Image
Enzyme 32 GenAtlas ID MCCC1 Link Image
Enzyme 32 HGNC ID HGNC:6936 Link Image
Enzyme 32 Chromosome Location 3
Enzyme 32 Locus 3q27
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Obata K, Fukuda T, Morishita R, Abe S, Asakawa S, Yamaguchi S, Yoshino M, Ihara K, Murayama K, Shigemoto K, Shimizu N, Kondo I: Human biotin-containing subunit of 3-methylcrotonyl-CoA carboxylase gene (MCCA): cDNA sequence, genomic organization, localization to chromosomal band 3q27, and expression. Genomics. 2001 Mar 1;72(2):145-52. [PubMed Link Image]
  2. Holzinger A, Roschinger W, Lagler F, Mayerhofer PU, Lichtner P, Kattenfeld T, Thuy LP, Nyhan WL, Koch HG, Muntau AC, Roscher AA: Cloning of the human MCCA and MCCB genes and mutations therein reveal the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency. Hum Mol Genet. 2001 Jun 1;10(12):1299-306. [PubMed Link Image]
  3. Baumgartner MR, Almashanu S, Suormala T, Obie C, Cole RN, Packman S, Baumgartner ER, Valle D: The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency. J Clin Invest. 2001 Feb;107(4):495-504. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 5759
Enzyme 33 Name Glutamate--cysteine ligase catalytic subunit
Enzyme 33 Synonyms
  1. Gamma- glutamylcysteine synthetase
  2. Gamma-ECS
  3. GCS heavy chain
Enzyme 33 Gene Name GCLC
Enzyme 33 Protein Sequence >Glutamate--cysteine ligase catalytic subunit 
MGLLSQGSPLSWEETKRHADHVRRHGILQFLHIYHAVKDRHKDVLKWGDEVEYMLVSFDH
ENKKVRLVLSGEKVLETLQEKGERTNPNHPTLWRPEYGSYMIEGTPGQPYGGTMSEFNTV
EANMRKRRKEATSILEENQALCTITSFPRLGCPGFTLPEVKPNPVEGGASKSLFFPDEAI
NKHPRFSTLTRNIRHRRGEKVVINVPIFKDKNTPSPFIETFTEDDEASRASKPDHIYMDA
MGFGMGNCCLQVTFQACSISEARYLYDQLATICPIVMALSAASPFYRGYVSDIDCRWGVI
SASVDDRTREERGLEPLKNNNYRISKSRYDSIDSYLSKCGEKYNDIDLTIDKEIYEQLLQ
EGIDHLLAQHVAHLFIRDPLTLFEEKIHLDDANESDHFENIQSTNWQTMRFKPPPPNSDI
GWRVEFRPMEVQLTDFENSAYVVFVVLLTRVILSYKLDFLIPLSKVDENMKVAQKRDAVL
QGMFYFRKDICKGGNAVVDGCGKAQNSTELAAEEYTLMSIDTIINGKEGVFPGLIPILNS
YLENMEVDVDTRCSILNYLKLIKKRASGELMTVARWMREFIANHPDYKQDSVITDEMNYS
LILKCNQIANELCECPELLGSAFRKVKYSGSKTDSSN
Enzyme 33 Number of Residues 637
Enzyme 33 Molecular Weight 72767
Enzyme 33 Theoretical pI 5.98
Enzyme 33 GO Classification
Function
  • acid-amino acid ligase activity
  • catalytic activity
  • glutamate-cysteine ligase activity
  • ligase activity
  • ligase activity, forming carbon-nitrogen bonds
Process
  • cellular metabolism
  • coenzyme metabolism
  • cofactor metabolism
  • glutathione biosynthesis
  • glutathione metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 33 General Function Not Available
Enzyme 33 Specific Function ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
Enzyme 33 Pathways
Enzyme 33 Reactions
  • ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 183039 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID P48506 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name GSH1_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >1914 bp 
ATGGGGCTGCTGTCCCAGGGCTCGCCGCTGAGCTGGGAGGAAACCAAGCGCCATGCCGAC
CACGTGCGGCGGCACGGGATCCTCCAGTTCCTGCACATCTACCACGCCGTCAAGGACCGG
CACAAGGACGTTCTCAAGTGGGGCGATGAGGTGGAATACATGTTGGTATCTTTTGATCAT
GAAAATAAAAAAGTCCGGTTGGTCCTGTCTGGGGAGAAAGTTCTTGAAACTCTGCAAGAG
AAGGGGGAAAGGACAAACCCAAACCATCCTACCCTTTGGAGACCAGAGTATGGGAGTTAC
ATGATTGAAGGGACACCAGGACAGCCCTACGGAGGAACAATGTCCGAGTTCAATACAGTT
GAGGCCAACATGCGAAAACGCCGGAAGGAGGCTACTTCTATATTAGAAGAAAATCAGGCT
CTTTGCACAATAACTTCATTTCCCAGATTAGGCTGTCCTGGGTTCACACTGCCCGAGGTC
AAACCCAACCCAGTGGAAGGAGGAGCTTCCAAGTCCCTCTTCTTTCCAGATGAAGCAATA
AACAAGCACCCTCGCTTCAGTACCTTAACAAGAAATATCCGACATAGGAGAGGAGAAAAG
GTTGTCATCAATGTACCAATATTTAAGGACAAGAATACACCATCTCCATTTATAGAAACA
TTTACTGAGGATGATGAAGCTTCAAGGGCTTCTAAGCCGGATCATATTTACATGGATGCC
ATGGGATTTGGAATGGGCAATTGCTGTCTCCAGGTGACATTCCAAGCCTGCAGTATATCT
GAGGCCAGATACCTTTATGATCAGTTGGCTACTATCTGTCCAATTGTTATGGCTTTGAGT
GCTGCATCTCCCTTTTACCGAGGCTATGTGTCAGACATTGATTGTCGCTGGGGAGTGATT
TCTGCATCTGTAGATGATAGAACTCGGGAGGAGCGAGGACTGGAGCCATTGAAGAACAAT
AACTATAGGATCAGTAAATCCCGATATGACTCAATAGACAGCTATTTATCTAAGTGTGGT
GAGAAATATAATGACATCGACTTGACGATAGATAAAGAGATCTACGAACAGCTGTTGCAG
GAAGGCATTGATCATCTCCTGGCCCAGCATGTTGCTCATCTCTTTATTAGAGACCCACTG
ACACTGTTTGAAGAGAAAATACACCTGGATGATGCTAATGAGTCTGACCATTTTGAGAAT
ATTCAGTCCACAAATTGGCAGACAATGAGATTTAAGCCCCCTCCTCCAAACTCAGACATT
GGATGGAGAGTAGAATTTCGACCCATGGAGGTGCAATTAACAGACTTTGAGAACTCTGCC
TATGTGGTGTTTGTGGTACTGCTCACCAGAGTGATCCTTTCCTACAAATTGGATTTTCTC
ATTCCACTGTCAAAGGTTGATGAGAACATGAAGGTAGCACAGAAAAGAGATGCTGTCTTG
CAGGGAATGTTTTATTTCAGGAAAGATATTTGCAAAGGTGGCAATGCAGTGGTGGATGGT
TGTGGCAAGGCCCAGAACAGCACGGAGCTCGCTGCAGAGGAGTACACCCTCATGAGCATA
GACACCATCATCAATGGGAAGGAAGGTGTGTTTCCTGGACTGATCCCAATTCTGAACTCT
TACCTTGAAAACATGGAAGTGGATGTGGACACCAGATGTAGTATTCTGAACTACCTAAAG
CTAATTAAGAAGAGAGCATCTGGAGAACTAATGACAGTTGCCAGATGGATGAGGGAGTTT
ATCGCAAACCATCCTGACTACAAGCAAGACAGTGTCATAACTGATGAAATGAATTATAGC
CTTATTTTGAAGTGTAACCAAATTGCAAATGAATTATGTGAATGCCCAGAGTTACTTGGA
TCAGCATTTAGGAAAGTAAAATATAGTGGAAGTAAAACTGACTCATCCAACTAG
Enzyme 33 GenBank Gene ID M90656 Link Image
Enzyme 33 GeneCard ID GCLC Link Image
Enzyme 33 GenAtlas ID GCLC Link Image
Enzyme 33 HGNC ID HGNC:4311 Link Image
Enzyme 33 Chromosome Location 6
Enzyme 33 Locus 6p12
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Gipp JJ, Chang C, Mulcahy RT: Cloning and nucleotide sequence of a full-length cDNA for human liver gamma-glutamylcysteine synthetase. Biochem Biophys Res Commun. 1992 May 29;185(1):29-35. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  3. Mulcahy RT, Gipp JJ: Identification of a putative antioxidant response element in the 5'-flanking region of the human gamma-glutamylcysteine synthetase heavy subunit gene. Biochem Biophys Res Commun. 1995 Apr 6;209(1):227-33. [PubMed Link Image]
  4. Beutler E, Gelbart T, Kondo T, Matsunaga AT: The molecular basis of a case of gamma-glutamylcysteine synthetase deficiency. Blood. 1999 Oct 15;94(8):2890-4. [PubMed Link Image]
  5. Ristoff E, Augustson C, Geissler J, de Rijk T, Carlsson K, Luo JL, Andersson K, Weening RS, van Zwieten R, Larsson A, Roos D: A missense mutation in the heavy subunit of gamma-glutamylcysteine synthetase gene causes hemolytic anemia. Blood. 2000 Apr 1;95(7):2193-6. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 5834
Enzyme 34 Name Adenylate kinase isoenzyme 1
Enzyme 34 Synonyms
  1. ATP-AMP transphosphorylase
  2. AK1
  3. Myokinase
Enzyme 34 Gene Name AK1
Enzyme 34 Protein Sequence >Adenylate kinase isoenzyme 1 
MEEKLKKTKIIFVVGGPGSGKGTQCEKIVQKYGYTHLSTGDLLRSEVSSGSARGKKLSEI
MEKGQLVPLETVLDMLRDAMVAKVNTSKGFLIDGYPREVQQGEEFERRIGQPTLLLYVDA
GPETMTQRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVD
SVFSQVCTHLDALK
Enzyme 34 Number of Residues 194
Enzyme 34 Molecular Weight 21635
Enzyme 34 Theoretical pI 8.99
Enzyme 34 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenylate kinase activity
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleotide binding
  • nucleotide kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • ATP metabolism
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate metabolism
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 34 General Function Nucleotide transport and metabolism
Enzyme 34 Specific Function This small ubiquitous enzyme is essential for maintenance and cell growth
Enzyme 34 Pathways
Enzyme 34 Reactions
  • ATP + AMP = 2 ADP
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 178322 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID P00568 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name KAD1_HUMAN Link Image
Enzyme 34 PDB ID 1Z83 Link Image
Enzyme 34 PDB File Show
Enzyme 34 3D Structure
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >585 bp 
ATGGAAGAGAAGCTGAAGAAAACCAAGATCATCTTTGTGGTGGGTGGGCCTGGCTCAGGG
AAGGGCACCCAGTGTGAGAAGATCGTGCAGAAGTATGGCTACACCCACCTCTCCACCGGG
GACCTCCTGCGGTCCGAGGTCAGCTCAGGCTCGGCCAGGGGCAAGAAGCTGTCGGAAATC
ATGGAGAAGGGGCAGCTGGTTCCACTGGAGACAGTGTTGGACATGCTCCGGGATGCCATG
GTGGCCAAAGTCAATACTTCCAAAGGCTTCCTGATTGATGGCTACCCGCGGGAGGTGCAG
CAAGGAGAAGAGTTTGAGCGACGGATTGGACAGCCCACACTGCTGCTGTATGTGGACGCA
GGCCCTGAGACCATGACCCAGCGGCTCTTGAAACGTGGAGAGACCAGCGGGCGTGTGGAC
GACAATGAGGAGACCATCAAAAAGCGGCTGGAGACCTATTACAAGGCCACAGAACCCGTC
ATCGCCTTCTATGAGAAACGTGGCATTGTGCGCAAGGTCAACGCTGAGGGCTCCGTGGAC
AGTGTCTTCTCCCAGGTCTGCACCCACCTGGACGCCCTAAAGTAG
Enzyme 34 GenBank Gene ID J04809 Link Image
Enzyme 34 GeneCard ID AK1 Link Image
Enzyme 34 GenAtlas ID AK1 Link Image
Enzyme 34 HGNC ID HGNC:361 Link Image
Enzyme 34 Chromosome Location 9
Enzyme 34 Locus 9q34.1
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Von Zabern I, Wittmann-Liebold B, Untucht-Grau R, Schirmer RH, Pai EF: Primary and tertiary structure of the principal human adenylate kinase. Eur J Biochem. 1976 Sep;68(1):281-90. [PubMed Link Image]
  2. Matsuura S, Igarashi M, Tanizawa Y, Yamada M, Kishi F, Kajii T, Fujii H, Miwa S, Sakurai M, Nakazawa A: Human adenylate kinase deficiency associated with hemolytic anemia. A single base substitution affecting solubility and catalytic activity of the cytosolic adenylate kinase. J Biol Chem. 1989 Jun 15;264(17):10148-55. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 5845
Enzyme 35 Name GTP:AMP phosphotransferase mitochondrial
Enzyme 35 Synonyms
  1. Adenylate kinase 3
  2. AK3
  3. Adenylate kinase 3 alpha-like 1
Enzyme 35 Gene Name AK3
Enzyme 35 Protein Sequence >GTP:AMP phosphotransferase mitochondrial 
MGASARLLRAVIMGAPGSGKGTVSSRITTHFELKHLSSGDLLRDNMLRGTEIGVLAKAFI
DQGKLIPDDVMTRLALHELKNLTQYSWLLDGFPRTLPQAEALDRAYQIDTVINLNVPFEV
IKQRLTARWIHPASGRVYNIEFNPPKTVGIDDLTGEPLIQREDDKPETVIKRLKAYEDQT
KPVLEYYQKKGVLETFSGTETNKIWPYVYAFLQTKVPQRSQKASVTP
Enzyme 35 Number of Residues 227
Enzyme 35 Molecular Weight 25566
Enzyme 35 Theoretical pI 9.64
Enzyme 35 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenylate kinase activity
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleotide binding
  • nucleotide kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
—
Enzyme 35 General Function Nucleotide transport and metabolism
Enzyme 35 Specific Function NTP + AMP = NDP + ADP
Enzyme 35 Pathways
Enzyme 35 Reactions
  • nucleoside triphosphate + AMP = nucleoside diphosphate + ADP
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 6518533 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID Q9UIJ7 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name KAD3_HUMAN Link Image
Enzyme 35 PDB ID 2AK3 Link Image
Enzyme 35 PDB File Show
Enzyme 35 3D Structure
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >684 bp 
ATGGGGGCGTCGGGGCGGCTGCTGCGAGCGGTGATCATGGGGGCCCCGGGCTCGGGCAAG
GGCACCGTGTCGTCCCGCATCACTACACACTTCGAGCTGAAGCACCTCTCCCGCGGGGAC
CTGCTCCGGGACAACATGCTGCGGGGCACAGAAATTGGCGTGTTAGCCCAGGCTTTCATT
GACCAAGGGAAACTCATCCCAGATTATGTCACGACTCGGCTGGCCCTTCATGAGCTGAAA
AACCTCACCCAGTATAGCTGGCTGTTGGATGGTTTTCCAAGGACACTTCCACAGGCAGAA
GCCCTAGATAGAGCTTATCAGATCGACACAGTGATTAACCTGAATGTGCCCTTTGAGGTC
ATTAAACAACGCCTTACTGCTCGCTGGATTCATCCCGCCAGTGGCCGAGTCTATAACATT
GAATTCAACCCTCCCAAAACTGTGGGCATTGATGACCTGACTGGGGAGCCTCTCATTCAG
CGTGAGGATGATAAACCAGAGACGGTTATCAAGAGACTAAAGGCTTATGAAGACCAAACA
AAGCCAGTCCTGGAATATTACCAGAAAAAAGGGGTGTTGGAAACATTCTCCGGAACAGAA
ACCAACAAGATTTGGCCCTATGTATATGCTTTCCTACAAACTAAAGTTCCACAAAGAAGC
CAGAAAGCTTCAGTTACTCCATGA
Enzyme 35 GenBank Gene ID AB021870 Link Image
Enzyme 35 GeneCard ID AK3 Link Image
Enzyme 35 GenAtlas ID AK3 Link Image
Enzyme 35 HGNC ID HGNC:17376 Link Image
Enzyme 35 Chromosome Location 9
Enzyme 35 Locus 9p24.1-p24.3
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References Not Available
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 5875
Enzyme 36 Name Putative adenylate kinase 7
Enzyme 36 Synonyms Not Available
Enzyme 36 Gene Name AK7
Enzyme 36 Protein Sequence >Putative adenylate kinase 7 
MAEEEETAALTEKVIRTQRVFINLLDSYSSGNIGKFLSNCVVGASLEEITEEEEEEDENK
SAMLEASSTKVKEGTFQIVGTLSKPDSPRPDFAVETYSAISREDLLMRLLECDVIIYNIT
ESSQQMEEAIWAVSALSEEVSHFEKRKLFILLSTVMTWARSKALDPEDSEVPFTEEDYRR
RKSHPNFLDHINAEKMVLKFGKKARKFAAYVVAAGLQYGAEGGMLHTFFKMAWLGEIPAL
PVFGDGTNVIPTIHVLDLAGVIQNVIDHVPKPHYLVAVDESVHTLEDIVKCISKNTGPGK
IQKIPRENAYLTKDLTQDCLDHLLVNLRMEALFVKENFNIRWAAQTGFVENINTILKEYK
QSRGLMPIKICILGPPAVGKSSIAKELAKYYKLHHIQLKDVISEAIAKLEAIVAPNDVGE
GEEEVEEEEEEENVEDAQELLDGIKESMEQNAGQLDDQYIIRFMKEKLKSMPCRNQGYIL
DGFPKTYDQAKDLFNQEDEEEEDDVRGRMFPFDKLIIPEFVCALDASDEFLKERVINLPE
SIVAGTHYSQDRFLRALSNYRDINIDDETVFNYFDELEIHPIHIDVGKLEDAQNRLAIKQ
LIKEIGEPRNYGLTDEEKAEEERKAAEERLAREAAEEAEREHQEAVEMAEKIARWEEWNK
RLEEVKREERELLEAQSIPLRNYLMTYVMPTLIQGLNECCNVRPEDPVDFLAEYLFKNNP
EAQ
Enzyme 36 Number of Residues 723
Enzyme 36 Molecular Weight 82673
Enzyme 36 Theoretical pI 4.40
Enzyme 36 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleotide binding
  • nucleotide kinase activity
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
—
Enzyme 36 General Function Not Available
Enzyme 36 Specific Function ATP + AMP = 2 ADP
Enzyme 36 Pathways
Enzyme 36 Reactions
  • ATP + AMP = 2 ADP
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 16553126 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q96M32 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name KAD7_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >2172 bp 
ATGGCTGAAGAAGAGGAAACTGCTGCTCTCACGGAGAAGGTTATCCGGACCCAGAGGGTG
TTTATAAACCTGTTGGATTCCTACAGCAGCGGAAACATCGGGAAGTTTCTATCTAACTGT
GTAGTTGGGGCTTCGCTTGAAGAAATTACAGAGGAAGAGGAAGAGGAAGATGAAAATAAG
TCAGCTATGCTGGAAGCTTCCTCAACCAAAGTGAAGGAAGGCACATTCCAGATTGTGGGC
ACGCTGTCCAAGCCTGACAGCCCGCGGCCTGACTTTGCGGTGGAGACGTACTCTGCCATC
TCTCAAGAAGACCTTCTCATGCGCCTGCTGGAGTGTGATGTTATTATTTATAACATCACT
GAGAGCTCACAGCAAATGGAGGAAGCCATCTGGGCAGTCTCTGCACTCAGTGAAGAAGTC
AGCCACTTTGAAAAGCGAAAGCTATTTATTTTACTGTCGACGGTGATGACTTGGGCGCGC
TCCAAAGCCCTGGACCCCGAGGATTCTGAGGTTCCATTCACTGAAGAAGATTATCGAAGA
AGAAAGTCTCATCCTAATTTTCTGGACCACATAAATGCTGAAAAAATGGTTCTCAAATTT
GGAAAAAAGGCCAGAAAATTTGCAGCATACGTAGTTGCTGCTGGACTCCAGTATGGAGCG
GAAGGAGGCATGTTACACACATTTTTTAAGATGGCTTGGTTGGGCGAGATTCCTGCATTA
CCAGTTTTTGGCGATGGAACAAATGTAATTCCAACAATCCATGTTCTTGATCTAGCAGGA
GTGATACAAAACGTCATAGATCACGTGCCAAAGCTTCACTACCTGGTTGCTGTGGATGAG
TCTGTTCATACCCTGGAAGACATAGTCAAGTGTATCAGTAAAAATACTGGCCCTGGGAAA
ATCCAGAAAATACCCAGAGAAAATGCATACCTAACCAAGGACTTAACGCAAGATTGTCTT
GACCATTTACTGGTCAACTTAAGAATGGAAGCGCTCTTTGTGAAGGAGAATTTTAATATT
CGATGGGCTGCCCAAACAGGATTTGTGGAAAATATCAACACTATCCTCAAGGAGTACAAG
CAAAGCAGAGGATTGATGCCAATCAAGATCTGCATTCTTGGTCCCCCTGCTGTGGGAAAA
TCCAGTATTGCTAAAGAATTGGCCAAGTACTACAAACTGCATCACATCCAACTGAAGGAT
GTCATTTCTGAAGCCATAGCAAAACTGGGGGCGATTGTTGCCCCTAACGATGTAGGGGAA
GGAGAAGAAGAAGTCGAAGAGGAAGAGGAGGAGGAGAATGTGGAAGATGCACAGGAGCTC
CTAGATGGCATCAAGGAGAGCATGGAGCAGAATGCAGGTCAACTAGACGATCAATATATA
ATTAGATTTATGAAAGAAAAGCTAAAATCAATGCCTTGCAGGAATCAAGGTTATATTTTG
GATGGATTCCCAAAGACCTATGATCAAGCAAAAGACCTGTTCAATCAGGAAGATGAGGAG
GAGGAAGATGATGTCAGAGGCAGAATGTTTCCCTTTGATAAATTAATTATACCTGAATTC
GTTTGTGCACTGGATGCTTCGGATGAGTTTCTGAAGGAGCGTGTGATAAACCTTCCTGAG
AGCATCGTGGCGGGGACCCACTACAGCCAAGACCGATTCCTCCGGGCTCTGAGCAACTAC
CGGGACATCAATATCGACGATGAGACTGTCTTCAACTATTTTGATGAACTTGAAATTCAC
CCGATACATATTGATGTAGGAAAACTTGAAGATGCTCAGAATAGACTTGCTATCAAACAG
CTCATCAAAGAGATTGGGGAGCCTCGAAATTATGGTTTAACAGACGAAGAAAAGGCAGAA
GAGGAGCGGAAGGCTGCGGAGGAGCGGCTGGCCAGGGAGGCTGCTGAGGAAGCAGAACGC
GAGCACCAGGAGGCCGTGGAGATGGCAGAGAAGATAGCTCGCTGGGAGGAGTGGAATAAA
CGACTGGAGGAAGTGAAAAGAGAAGAAAGAGAATTACTGGAGGCTCAGTCAATTCCCCTG
AGAAACTATTTAATGACCTATGTGATGCCAACTCTTATTCAGGGCCTGAATGAATGTTGC
AACGTCCGACCCGAAGACCCTGTTGATTTTCTGGCAGAATATCTCTTCAAGAACAATCCT
GAAGCACAGTGA
Enzyme 36 GenBank Gene ID AK057426 Link Image
Enzyme 36 GeneCard ID AK7 Link Image
Enzyme 36 GenAtlas ID AK7 Link Image
Enzyme 36 HGNC ID HGNC:20091 Link Image
Enzyme 36 Chromosome Location Not Available
Enzyme 36 Locus Not Available
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 5887
Enzyme 37 Name Bis(5'-adenosyl)-triphosphatase
Enzyme 37 Synonyms
  1. Diadenosine 5',5'''- P1,P3-triphosphate hydrolase
  2. Dinucleosidetriphosphatase
  3. AP3A hydrolase
  4. AP3AASE
  5. Fragile histidine triad protein
Enzyme 37 Gene Name FHIT
Enzyme 37 Protein Sequence >Bis(5'-adenosyl)-triphosphatase 
MSFRFGQHLIKPSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQ
TTQRVGTVVEKHFHGTSLTFSMQDGPEAGQTVKHVHVHVLPRKAGDFHRNDSIYEELQKH
DKEDFPASWRSEEEMAAEAAALRVYFQ
Enzyme 37 Number of Residues 147
Enzyme 37 Molecular Weight 16858
Enzyme 37 Theoretical pI 7.09
Enzyme 37 GO Classification Not Available
Enzyme 37 General Function Nucleotide transport and metabolism
Enzyme 37 Specific Function Cleaves A-5'-PPP-5'A to yield AMP and ADP. Possible tumor suppressor for specific tissues
Enzyme 37 Pathways
Enzyme 37 Reactions
  • P1-P3-bis(5'-adenosyl) triphosphate + H2O = ADP + AMP
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • 1-24
Enzyme 37 Transmembrane Regions Not Available
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 1203836 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID P49789 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name FHIT_HUMAN Link Image
Enzyme 37 PDB ID 1FHI Link Image
Enzyme 37 PDB File Show
Enzyme 37 3D Structure
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >444 bp 
ATGTCGTTCAGATTTGGCCAACATCTCATCAAGCCCTCTGTAGTGTTTCTCAAAACAGAA
CTGTCCTTCGCTCTTGTGAATAGGAAACCTGTGGTACCAGGACATGTCCTTGTGTGCCCG
CTGCGGCCAGTGGAGCGCTTCCATGACCTGCGTCCTGATGAAGTGGCCGATTTGTTTCAG
ACGACCCAGAGAGTCGGGACAGTGGTGGAAAAACATTTCCATGGGACCTCTCTCACCTTT
TCCATGCAGGATGGCCCCGAAGCCGGACAGACTGTGAAGCACGTTCACGTCCATGTTCTT
CCCAGGAAGGCTGGAGACTTTCACAGGAATGACAGCATCTATGAGGAGCTCCAGAAACAT
GACAAGGAGGACTTTCCTGCCTCTTGGAGATCAGAGGAGGAAATGGCAGCAGAAGCCGCA
GCTCTGCGGGTCTACTTTCAGTGA
Enzyme 37 GenBank Gene ID U46922 Link Image
Enzyme 37 GeneCard ID FHIT Link Image
Enzyme 37 GenAtlas ID FHIT Link Image
Enzyme 37 HGNC ID HGNC:3701 Link Image
Enzyme 37 Chromosome Location 3
Enzyme 37 Locus 3p14.2
Enzyme 37 SNPs SNPJam Report