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Human Metabolome Database Version 2.5

 

Showing metabocard for Estrone (HMDB00145)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2011-06-13 12:40:12
Accession Number HMDB00145
Secondary Accession Numbers HMDB04449
Common Name Estrone
Description Estrone is a major mammalian estrogen. The conversion of the natural C19 steroids, testosterone and androstenedione into estrone is dependent on a complex key reaction catalyzed by the cytochrome P450 aromatase (EC 1.14.14.1, unspecific monooxygenase), which is expressed in many tissues of the adult human (e.g. ovary, fat tissue), but not in the liver. The ovaries after menopause continue to produce androstenedione and testosterone in significant amounts and these androgens are converted in fat, muscle, and skin into estrone. When women between the ages of 45 and 64 years have prophylactic oophorectomy (when hysterectomy is performed for benign disease to prevent the development of ovarian cancer), evidence suggests that oophorectomy increases the subsequent risk of coronary heart disease (CHD) and osteoporosis. Whereas 14,000 women die of ovarian cancer every year nearly 490,000 women die of heart disease and 48,000 women die within 1 year after hip fracture. Therefore, the decision to perform prophylactic oophorectomy should be approached with great caution for the majority of women who are at low risk of developing ovarian cancer. Steroid sulfatase (EC 3.1.6.2, STS) hydrolyzes steroid sulfates, such as estrone sulfate to estrone which can be converted to steroids with potent estrogenic properties, that is, estradiol; STS activity is much higher in breast tumors and high levels of STS mRNA expression in tumors are associated with a poor prognosis. The biological roles of estrogens in tumorigenesis are certainly different between the endometrium and breast, although both are considered "estrogen-dependent tissues". 17beta-hydroxysteroid dehydrogenases (EC 1.1.1.62, 17-HSDs) are enzymes involved in the formation of active sex steroids. estrone is interconverted by two enzymes 17-HSD types. Type 1 converts estrone to estradiol and Type 2 catalyzes the reverse reaction. (PMID: 17653961, 17513923, 17470679, 17464097)
Synonyms
  1. (+)-Estrone
  2. 1,3,5(10)-Estratrien-3-ol-17-one
  3. 3-Hydroxy-17-keto-estra-1,3,5-triene
  4. 3-Hydroxyestra-1,3,5(10)-trien-17-one
  5. 3-Hydroxyestra-1,3,5(10)-triene-17-one
  6. 3-Hydroxyoestra-1,3,5(10)-trien-17-one
  7. D1,3,5(10)-Estratrien-3-ol-17-one
Chemical IUPAC Name 3-hydroxy-Estra-1,3,5(10)-trien-17-one
Chemical Formula C18H22O2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Cholesterols and derivatives
Class
  • Steroids and Steroid Derivatives
Sub Class
  • Ketosteroids
Family
  • Mammalian Metabolite
Species
  • ketone
  • phenol or hydroxyhetarene
  • aromatic compound
Biofunction
  • Component of Androgen and estrogen metabolism
  • Component of Sulfur metabolism
Application
Source
  • Endogenous
Average Molecular Weight 270.366
Monoisotopic Molecular Weight 270.161987
Isomeric SMILES C[C@]12CC[C@H]3[C@@H](CCC4=C3C=CC(O)=C4)[C@@H]1CCC2=O
Canonical SMILES CC12CCC3C(CCC4=C3C=CC(O)=C4)C1CCC2=O
KEGG Compound ID C00468 Link Image
BioCyc ID ESTRONE Link Image
BiGG ID 35059 Link Image
Wikipedia Link Estrone Link Image
NuGOwiki Link HMDB00145 Link Image
Metagene Link HMDB00145 Link Image
METLIN ID 264 Link Image
PubChem Compound 5870 Link Image
PubChem Substance 7988426 Link Image
ChEBI ID 17263 Link Image
CAS Registry Number 53-16-7
InChI Identifier InChI=1/C18H22O2/c1-18-9-8-14-13-5-3-12(19)10-11(13)2-4-15(14)16(18)6-7-17(18)20/h3,5,10,14-16,19H,2,4,6-9H2,1H3/t14-,15-,16+,18+/m1/s1
Synthesis Reference Kocovsky, Paved; Baines, Richard S. Synthesis of estrone via a thallium(III)-mediated fragmentation of a 19-hydroxyandrost-5-ene precursor. Tetrahedron Letters (1993), 34(38), 6139-40.
Melting Point (Experimental) 258-260oC
Experimental Water Solubility 0.03 mg/mL [MERCK INDEX (1996)] Source: PhysProp
Predicted Water Solubility 3.94e-03 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity 3.13 [HANSCH,C ET AL. (1995)] Source: PhysProp
Predicted LogP/Hydrophobicity 4.03 [Predicted by ALOGPS]; 3.6 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download FID (Varian)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Membrane (Predicted from LogP)
  • Cytoplasm
  • endoplasmic reticulum
Biofluid Location
  • Blood
  • Urine
Tissue Location
Tissue References
Liver
Concentrations (Normal)
Biofluid Blood
Value 0.00020 (0.00011-0.00030) uM
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Not Available
References
  • The Merck Manual, 17th ed. Mark H. Beers, MD, Robert Berkow, MD, eds. Whitehouse Station, NJ: Merck Research Labs, 1999.
Biofluid Blood
Value 0.00017 +/- 0.000071 uM
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Reichman ME, Judd JT, Longcope C, Schatzkin A, Clevidence BA, Nair PP, Campbell WS, Taylor PR: Effects of alcohol consumption on plasma and urinary hormone concentrations in premenopausal women. J Natl Cancer Inst. 1993 May 5;85(9):722-7. [PubMed Link Image]
Biofluid Urine
Value 0.0013 +/- 0.00085 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Female
Patient information Normal
Comments Not Available
References
  • Reichman ME, Judd JT, Longcope C, Schatzkin A, Clevidence BA, Nair PP, Campbell WS, Taylor PR: Effects of alcohol consumption on plasma and urinary hormone concentrations in premenopausal women. J Natl Cancer Inst. 1993 May 5;85(9):722-7. [PubMed Link Image]
Concentrations (Abnormal)
Biofluid Blood
Value 0.00035 (0.00014-0.00056) uM
Age Adult:>18 yrs old
Sex Female
Condition Menstrual cycle
Comments Not Available
References
  • The Merck Manual, 17th ed. Mark H. Beers, MD, Robert Berkow, MD, eds. Whitehouse Station, NJ: Merck Research Labs, 1999.
Biofluid Blood
Value 0.00050 (0.00028-0.00074) uM
Age Adult:>18 yrs old
Sex Female
Condition Menstrual cycle
Comments Not Available
References
  • The Merck Manual, 17th ed. Mark H. Beers, MD, Robert Berkow, MD, eds. Whitehouse Station, NJ: Merck Research Labs, 1999.
Biofluid Blood
Value 0.00030 (0.00018-0.00042) uM
Age Adult:>18 yrs old
Sex Female
Condition Menstrual cycle
Comments Not Available
References
  • The Merck Manual, 17th ed. Mark H. Beers, MD, Robert Berkow, MD, eds. Whitehouse Station, NJ: Merck Research Labs, 1999.
Biofluid Blood
Value 0.00012 (0.0-0.00024) uM
Age Adult:>18 yrs old
Sex Female
Condition Normal
Comments Not Available
References
  • The Merck Manual, 17th ed. Mark H. Beers, MD, Robert Berkow, MD, eds. Whitehouse Station, NJ: Merck Research Labs, 1999.
Biofluid Blood
Value 0.00022 (0.00013-0.00038) uM
Age Adult:>18 yrs old
Sex Male
Comments Not Available
References
  • Zumoff B, Troxler RG, O'Connor J, Rosenfeld RS, Kream J, Levin J, Hickman JR, Sloan AM, Walker W, Cook RL, Fukushima DK: Abnormal hormone levels in men with coronary artery disease. Arteriosclerosis. 1982 Jan-Feb;2(1):58-67. [PubMed Link Image]
Biofluid Blood
Value 0.00021 (0.00011-0.00037) uM
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
  • Zumoff B, Troxler RG, O'Connor J, Rosenfeld RS, Kream J, Levin J, Hickman JR, Sloan AM, Walker W, Cook RL, Fukushima DK: Abnormal hormone levels in men with coronary artery disease. Arteriosclerosis. 1982 Jan-Feb;2(1):58-67. [PubMed Link Image]
Associated Disorders
Condition References
Menstrual cycle
  • The Merck Manual, 17th ed. Mark H. Beers, MD, Robert Berkow, MD, eds. Whitehouse Station, NJ: Merck Research Labs, 1999.
Normal
  • The Merck Manual, 17th ed. Mark H. Beers, MD, Robert Berkow, MD, eds. Whitehouse Station, NJ: Merck Research Labs, 1999.
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Androgen and Estrogen Metabolism SMP00068 Link Image map00150 Link Image
Sulfate/Sulfite Metabolism SMP00041 Link Image map00920 Link Image
General References
  1. Czernik PJ, Little JM, Barone GW, Raufman JP, Radominska-Pandya A: Glucuronidation of estrogens and retinoic acid and expression of UDP-glucuronosyltransferase 2B7 in human intestinal mucosa. Drug Metab Dispos. 2000 Oct;28(10):1210-6. [PubMed Link Image]
  2. Pfeiffer E, Graf E, Gerstner S, Metzler M: Stimulation of estradiol glucuronidation: a protective mechanism against estradiol-mediated carcinogenesis? Mol Nutr Food Res. 2006 Apr;50(4-5):385-9. [PubMed Link Image]
  3. Wikipedia Link Image
Metabolic Enzymes
  1. Arylsulfatase D
  2. Arylsulfatase E
  3. Estrogen sulfotransferase
  4. Estradiol 17-beta-dehydrogenase 2
  5. UDP-glucuronosyltransferase 2B28
  6. Estradiol 17-beta-dehydrogenase 8
  7. Solute carrier organic anion transporter family member 1B1
  8. UDP-glucuronosyltransferase 2B4
  9. UDP-glucuronosyltransferase 1-4
  10. UDP-glucuronosyltransferase 2B7
  11. UDP-glucuronosyltransferase 2B15
  12. UDP-glucuronosyltransferase 2A1
  13. UDP-glucuronosyltransferase 1-1
  14. UDP-glucuronosyltransferase 1-9
  15. UDP-glucuronosyltransferase 1-3
  16. UDP-glucuronosyltransferase 2B17
  17. UDP-glucuronosyltransferase 1-6
  18. UDP-glucuronosyltransferase 1-5
  19. UDP-glucuronosyltransferase 2B11
  20. Steryl-sulfatase
  21. Estradiol 17-beta-dehydrogenase 11
  22. Estradiol 17-beta-dehydrogenase 1
  23. 3-keto-steroid reductase
  24. Cytochrome P450 3A4
  25. Cytochrome P450 2C9
  26. Cytochrome P450 2C19
  27. Cytochrome P450 2E1
  28. Cytochrome P450 1B1
  29. Cytochrome P450 2C18
  30. Cytochrome P450 2F1
  31. Cytochrome P450 2B6
  32. Cytochrome P450 3A5
  33. Cytochrome P450 1A1
  34. Cytochrome P450 2A13
  35. Cytochrome P450 3A7
  36. Cytochrome P450 4B1
  37. Cytochrome P450 4Z1
  38. Cytochrome P450 1A2
  39. Cytochrome P450 19A1
  40. Cytochrome P450 2C8
  41. Cytochrome P450 2S1
  42. Cytochrome P450 2J2
  43. Cytochrome P450 2A7
  44. Cytochrome P450 2A6
  45. Sex hormone-binding globulin
  46. Serum albumin
  47. Estrogen receptor
  48. 17-beta-hydroxysteroid dehydrogenase type 6
  49. UDP-glucuronosyltransferase 2A3
  50. Cytochrome P450, family 1, subfamily A, polypeptide 1
  51. Estradiol 17-beta-dehydrogenase 12
  52. Solute carrier family 22 member 7
  53. HCG2039726, isoform CRA_f
  54. HCG2039726, isoform CRA_e
  55. UDP glycosyltransferase 1 family polypeptide A7
  56. cDNA FLJ76966, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B10 (UGT2B10), mRNA (UDP glucuronosyltransferase 2 family, polypeptide B10, isoform CRA_b)
  57. Cytochrome P450, family 3, subfamily A, polypeptide 7
  58. Cytochrome P450 2D6
  59. Cytochrome P450, family 3, subfamily A, polypeptide 5 (Cytochrome P450, family 3, subfamily A, polypeptide 5, isoform CRA_a)
  60. Cytochrome P450
  61. Cytochrome P450, family 3, subfamily A, polypeptide 43, isoform CRA_e
  62. cDNA FLJ77672
  63. cDNA, FLJ93689, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B7 (UGT2B7), mRNA
  64. cDNA, FLJ93424, highly similar to Homo sapiens cytochrome P450, family 2, subfamily A, polypeptide 6 (CYP2A6), mRNA (Cytochrome P450, family 2, subfamily A, polypeptide 6)
  65. cDNA, FLJ93938, Homo sapiens cytochrome P450, family 2, subfamily C, polypeptide 18(CYP2C18), mRNA (HCG39167, isoform CRA_b)
  66. cDNA FLJ45935 fis, clone PLACE7003985, highly similar to Estradiol 17-beta-dehydrogenase 1 (Hydroxysteroid (17-beta) dehydrogenase 1)
  67. cDNA, FLJ93594, Homo sapiens hydroxysteroid (17-beta) dehydrogenase 2 (HSD17B2),mRNA (Hydroxysteroid (17-beta) dehydrogenase 2)
Enzyme 1 [top]
Enzyme 1 ID 5551
Enzyme 1 Name Arylsulfatase D
Enzyme 1 Synonyms
  1. ASD
Enzyme 1 Gene Name ARSD
Enzyme 1 Protein Sequence >Arylsulfatase D
MRSAARRGRAAPAARDSLPVLLFLCLLLKTCEPKTANAFKPNILLIMADDLGTGDLGCYG
NNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRALQWNA
GSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHHPLNHGFDYFYGMPFTL
TNDCDPGRPPEVDAALRAQLWGYTQFLALGILTLAAGQTCGFFSVSARAVTGMAGVGCLF
FISWYSSFGFVRRWNCILMRNHDVTEQPMVLEKTASLMLKEAVSYIERHKHGPFLLFLSL
LHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYFTSDHGGH
LEARDGHSQLGGWNGIYKGGKGMGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPT
VVQLVGGEVPQDRVIDGHSLVPLLQGAEARSAHEFLFHYCGQHLHAARWHQKDSGSVWKV
HYTTPQFHPEGAGACYGRGVCPCSGEGVTHHRPPLLFDLSRDPSEARPLTPDSEPLYHAV
IARVGAAVSEHRQTLSPVPQQFSMSNILWKPWLQPCCGHFPFCSCHEDGDGTP
Enzyme 1 Number of Residues 593
Enzyme 1 Molecular Weight 64859.3
Enzyme 1 Theoretical pI 7.24
Enzyme 1 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • sulfuric ester hydrolase activity
Process
  • metabolic process
Component
Enzyme 1 General Function Involved in catalytic activity
Enzyme 1 Specific Function Not Available
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions Not Available
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-33
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 791002 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P51689 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ARSD_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1782 bp
ATGCGATCCGCCGCGCGGAGGGGACGCGCCGCGCCCGCCGCCAGGGACTCTTTGCCGGTG
CTACTGTTTTTATGCTTGCTTCTGAAGACGTGTGAACCTAAAACTGCAAATGCCTTTAAA
CCAAATATCCTACTGATCATGGCGGATGATCTAGGCACTGGGGATCTCGGTTGCTACGGG
AACAATACACTGAGAACGCCGAATATTGACCAGCTTGCAGAGGAAGGTGTGAGGCTCACT
CAGCACCTGGCGGCCGCCCCGCTCTGCACCCCAAGCCGAGCTGCATTCCTCACAGGGAGA
CATTCCTTCAGATCAGGCATGGACGCCAGCAATGGATACCGGGCCCTTCAGTGGAACGCA
GGCTCAGGTGGACTCCCTGAGAACGAAACCACTTTTGCAAGAATCTTGCAGCAGCATGGC
TATGCAACCGGCCTCATAGGAAAATGGCACCAGGGTGTGAATTGTGCATCCCGCGGGGAT
CACTGCCACCACCCCCTGAACCACGGATTTGACTATTTCTACGGCATGCCCTTCACGCTC
ACAAACGACTGTGACCCAGGCAGGCCCCCCGAAGTGGACGCCGCCCTGAGGGCGCAGCTC
TGGGGTTACACCCAGTTCCTGGCGCTGGGGATTCTCACCCTGGCTGCCGGCCAGACCTGC
GGTTTCTTCTCTGTCTCCGCGAGAGCAGTCACCGGCATGGCCGGCGTGGGCTGCCTGTTT
TTCATCTCTTGGTACTCCTCCTTCGGGTTTGTGCGACGCTGGAACTGTATCCTGATGAGA
AACCATGACGTCACGGAGCAACCCATGGTTCTGGAGAAAACAGCGAGTCTTATGCTAAAG
GAAGCTGTTTCCTATATTGAAAGACACAAGCATGGGCCATTTCTCCTCTTCCTTTCTTTG
CTGCATGTGCACATTCCCCTTGTGACCACGAGTGCATTCCTGGGGAAAAGTCAGCATGGC
TTATATGGTGATAATGTGGAGGAGATGGACTGGCTCATAGGTAAGGTTCTTAATGCCATC
GAAGACAATGGTTTAAAGAACTCAACATTCACGTATTTCACCTCTGACCATGGAGGACAT
TTAGAGGCAAGAGATGGACACAGCCAGTTAGGGGGATGGAACGGAATTTACAAAGGTGGG
AAGGGCATGGGAGGATGGGAAGGTGGGATCCGAGTGCCCGGGATCTTCCACTGGCCGGGG
GTGCTCCCGGCCGGCCGAGTGATTGGAGAGCCCACGAGCCTGATGGACGTGTTCCCTACT
GTGGTCCAGCTGGTGGGTGGCGAGGTGCCCCAGGACAGGGTGATTGATGGCCACAGCCTG
GTACCCTTGCTGCAGGGAGCTGAGGCACGCTCGGCACATGAGTTCCTGTTTCATTACTGT
GGGCAGCATCTTCACGCAGCACGCTGGCACCAGAAGGACAGTGGAAGCGTCTGGAAGGTT
CATTACACGACCCCGCAGTTCCACCCCGAGGAGCGGGGCCTGCTAACGGCCGAGGCGTCT
GCCCATGCTGAATGGGGAGGCGTGACCCATCACAGACCCCCTTTGCTCTTTGACCTCTCC
AGGGACCCCTCCGAGGCACGGCCCCTGACCCCCGACTCCGAGCCCCTGTACCACGCCGTG
ATAGCAAGGGTAGGTGCCGCGGTGTCGGAGCATCGGCAGACCCTGAGTCCTGTGCCCCAG
CAGTTTTCCATGAGCAACATCCTGTGGAAGCCGTGGCTGCAGCCGTGCTGCGGACATTTC
CCGTTCTGTTCATGCCACGAGGATGGGGATGGCACCCCCTGA
Enzyme 1 GenBank Gene ID X83572 Link Image
Enzyme 1 GeneCard ID ARSD Link Image
Enzyme 1 GenAtlas ID ARSD Link Image
Enzyme 1 HGNC ID HGNC:717 Link Image
Enzyme 1 Chromosome Location Not Available
Enzyme 1 Locus Not Available
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Franco B, Meroni G, Parenti G, Levilliers J, Bernard L, Gebbia M, Cox L, Maroteaux P, Sheffield L, Rappold GA, et al.: A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy. Cell. 1995 Apr 7;81(1):15-25. [PubMed Link Image]
  2. Urbitsch P, Salzer MJ, Hirschmann P, Vogt PH: Arylsulfatase D gene in Xp22.3 encodes two protein isoforms. DNA Cell Biol. 2000 Dec;19(12):765-73. [PubMed Link Image]
  3. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5560
Enzyme 2 Name Arylsulfatase E
Enzyme 2 Synonyms
  1. ASE
Enzyme 2 Gene Name ARSE
Enzyme 2 Protein Sequence >Arylsulfatase E
MLHLHHSCLCFRSWLPAMLAVLLSLAPSASSDISASRPNILLLMADDLGIGDIGCYGNNT
MRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTGASG
GLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDHFYGMPFSLMGD
CARWELSEKRVNLEQKLNFLFQVLALVALTLVAGKLTHLIPVSWMPVIWSALSAVLLLAS
SYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLILQEVASFLKRNKHGPFLLFVSFLHV
HIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLEN
QLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVR
LAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFV
TPVFQPEGAGACYGRKVCPCFGEKVVHHDPPLLFDLSRDPSETHILTPASEPVFYQVMER
VQQAVWEHQRTLSPVPLQLDRLGNIWRPWLQPCCGPFPLCWCLREDDPQ
Enzyme 2 Number of Residues 589
Enzyme 2 Molecular Weight 65668.4
Enzyme 2 Theoretical pI 6.96
Enzyme 2 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • sulfuric ester hydrolase activity
Process
  • metabolic process
Component
Enzyme 2 General Function Involved in catalytic activity
Enzyme 2 Specific Function May be essential for the correct composition of cartilage and bone matrix during development. Has no activity toward steroid sulfates
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-31
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 62897927 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P51690 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name ARSE_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1770 bp
ATGTTACATCTGCACCATTCTTGTTTGTGTTTCAGGAGCTGGCTGCCAGCGATGCTCGCT
GTACTGCTAAGTTTGGCACCATCAGCTTCCAGCGACATTTCCGCCTCCCGACCGAACATC
CTTCTTCTGATGGCGGACGACCTTGGCATTGGGGACATTGGCTGCTATGGCAACAACACC
ATGAGGACTCCGAATATTGACCGCCTTGCAGAGGACGGCGTGAAGCTGACCCAACACATC
TCTGCCGCATCTTTGTGCACCCCAAGCAGAGCCGCCTTCCTCACGGGCAGATACCCTGTG
CGATCAGGGATGGTTTCCAGCATTGGTTACCGTGTTCTTCAGTGGACCGGAGCATCTGGA
GGTCTTCCAACAAATGAGACAACTTTTGCAAAAATACTGAAAGAGAAAGGCTATGCCACT
GGACTCATTGGAAAATGGCATCTGGGTCTCAACTGTGAGTCAGCCAGTGATCATTGCCAC
CACCCTCTCCATCACGGCTTTGACCATTTCTACGGAATGCCTTTCTCCTTGATGGGTGAT
TGCGCCCGCTGGGAACTCTCAGAGAAGCGTGTCAACCTGGAACAAAAACTCAACTTCCTC
TTCCAAGTCCTGGCCTTGGTTGCCCTCACACTGGTAGCAGGGAAGCTCACACACCTGATA
CCCGTCTCGTGGATGCCGGTCATCTGGTCAGCCCTTTCGGCCGTCCTCCTCCTCGCAAGC
TCCTATTTTGTGGGTGCTCTGATTGTCCATGCCGATTGCTTTCTGATGAGAAACCACACC
ATCACGGAGCAGCCCATGTGCTTCCAAAGAACGACACCCCTTATTCTGCAGGAGGTTGCG
TCCTTTCTCAAAAGGAATAAGCATGGGCCTTTCCTCCTCTTTGTTTCCTTTCTACACGTT
CACATCCCTCTTATCACTATGGAGAACTTCCTCGGGAAGAGTCTCCACGGGCTGTATGGG
GACAACGTAGAGGAGATGGACTGGATGGTAGGACGGATCCTTGACACTTTGGACGTGGAG
GGTTTGAGCAACAGCACCCTCATTTATTTTACGTCGGATCACGGCGGTTCCCTAGAGAAT
CAACTTGGAAACACCCAGTATGGTGGCTGGAATGGAATTTATAAAGGTGGGAAGGGCATG
GGAGGATGGGAAGGTGGGATCCGCGTGCCCGGGATCTTCCGCTGGCCCGGGGTGCTCCCG
GCCGGCCGAGTGATTGGCGAGCCCACGAGTCTGATGGACGTGTTCCCCACCGTGGTCCGG
CTGGCGGGCAGCGAGGTGCCCCAGGACAGAGTGATTGACGGCCAAGACCTTCTGCCCTTG
CTCCTGGGGACAGCCCAACACTCAGACCACGAGTTCCTGATGCATTATTGTGAGAGGTTT
CTGCACGCAGCCAGGTGGCATCAACGGGACAGAGGAACAATGTGGAAAGTCCACTTTGTG
ACGCCTGTGTTCCAGCCAGAGGGAGCCGGTGCCTGCTATGGAAGAAAGGTCTGCCCGTGC
TTTGGGGAAAAAGTAGTCCACCACGATCCACCTTTGCTCTTTGACCTCTCAAGAGACCCT
TCTGAGACCCACATCCTCACACCAGCCTCAGAGCCCGTGTTCTATCAGGTGATGGAACGA
GTCCAGCAGGCGGTGTGGGAACACCAGCGGACACTCAGCCCAGTTCCTCTGCAGCTGGAC
AGGCTGGGCAATATCTGGAGACCGTGGCTGCAGCCCTGCTGTGGCCCGTTCCCCCTCTGC
TGGTGCCTTAGGGAAGATGACCCACAATAA
Enzyme 2 GenBank Gene ID AK223183 Link Image
Enzyme 2 GeneCard ID ARSE Link Image
Enzyme 2 GenAtlas ID ARSE Link Image
Enzyme 2 HGNC ID HGNC:719 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Franco B, Meroni G, Parenti G, Levilliers J, Bernard L, Gebbia M, Cox L, Maroteaux P, Sheffield L, Rappold GA, et al.: A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy. Cell. 1995 Apr 7;81(1):15-25. [PubMed Link Image]
  2. Daniele A, Parenti G, d'Addio M, Andria G, Ballabio A, Meroni G: Biochemical characterization of arylsulfatase E and functional analysis of mutations found in patients with X-linked chondrodysplasia punctata. Am J Hum Genet. 1998 Mar;62(3):562-72. [PubMed Link Image]
  3. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  4. Parenti G, Buttitta P, Meroni G, Franco B, Bernard L, Rizzolo MG, Brunetti-Pierri N, Ballabio A, Andria G: X-linked recessive chondrodysplasia punctata due to a new point mutation of the ARSE gene. Am J Med Genet. 1997 Dec 12;73(2):139-43. [PubMed Link Image]
  5. Brunetti-Pierri N, Andreucci MV, Tuzzi R, Vega GR, Gray G, McKeown C, Ballabio A, Andria G, Meroni G, Parenti G: X-linked recessive chondrodysplasia punctata: spectrum of arylsulfatase E gene mutations and expanded clinical variability. Am J Med Genet A. 2003 Mar 1;117A(2):164-8. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5582
Enzyme 3 Name Estrogen sulfotransferase
Enzyme 3 Synonyms
  1. EST-1
  2. Sulfotransferase 1E1
  3. ST1E1
  4. Sulfotransferase, estrogen-preferring
Enzyme 3 Gene Name SULT1E1
Enzyme 3 Protein Sequence >Estrogen sulfotransferase
MNSELDYYEKFEEVHGILMYKDFVKYWDNVEAFQARPDDLVIATYPKSGTTWVSEIVYMI
YKEGDVEKCKEDVIFNRIPFLECRKENLMNGVKQLDEMNSPRIVKTHLPPELLPASFWEK
DCKIIYLCRNAKDVAVSFYYFFLMVAGHPNPGSFPEFVEKFMQGQVPYGSWYKHVKSWWE
KGKSPRVLFLFYEDLKEDIRKEVIKLIHFLERKPSEELVDRIIHHTSFQEMKNNPSTNYT
TLPDEIMNQKLSPFMRKGITGDWKNHFTVALNEKFDKHYEQQMKESTLKFRTEI
Enzyme 3 Number of Residues 294
Enzyme 3 Molecular Weight 35126.2
Enzyme 3 Theoretical pI 6.61
Enzyme 3 GO Classification
Function
  • catalytic activity
  • sulfotransferase activity
  • transferase activity
  • transferase activity, transferring sulfur-containing groups
Process
Component
Enzyme 3 General Function Involved in sulfotransferase activity
Enzyme 3 Specific Function May control the level of the estrogen receptor by sulfurylating free estradiol. Maximally sulfates beta-estradiol and estrone at concentrations of 20 nM. Also sulfates dehydroepiandrosterone, pregnenolone, ethinylestradiol, equalenin, diethylstilbesterol and 1-naphthol, at significantly higher concentrations; however, cortisol, testosterone and dopamine are not sulfated
Enzyme 3 Pathways
Enzyme 3 Reactions
  • 3'-phosphoadenylyl sulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate [RN:R02350]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID P49888 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ST1E1_HUMAN Link Image
Enzyme 3 PDB ID 1G3M Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >885 bp
ATGAATTCTGAACTTGACTATTATGAAAAGTTTGAAGAAGTCCATGGGATTCTAATGTAT
AAAGATTTTGTCAAATATTGGGATAATGTGGAAGCGTTCCAGGCAAGACCAGATGATCTT
GTCATTGCCACCTACCCTAAATCTGGTACAACCTGGGTTAGTGAAATTGTGTATATGATC
TATAAAGAGGGTGATGTGGAAAAGTGCAAAGAAGATGTAATTTTTAATCGAATACCTTTC
CTGGAATGCAGAAAAGAAAACCTCATGAATGGAGTAAAACAATTAGATGAGATGAATTCT
CCTAGAATTGTGAAGACTCATTTGCCACCTGAACTTCTTCCTGCCTCATTTTGGGAAAAG
GATTGTAAGATAATCTATCTTTGCCGGAATGCAAAGGATGTGGCTGTTTCCTTTTATTAT
TTCTTTCTAATGGTGGCTGGTCATCCAAATCCTGGATCCTTTCCAGAGTTTGTGGAGAAA
TTCATGCAAGGACAGGTTCCTTATGGTTCCTGGTATAAACATGTAAAATCTTGGTGGGAA
AAGGGAAAGAGTCCACGTGTACTATTTCTTTTCTACGAAGACCTGAAAGAGGATATCAGA
AAAGAGGTGATAAAATTGATACATTTCCTGGAAAGGAAGCCATCAGAGGAGCTTGTGGAC
AGGATTATACATCATACTTCGTTCCAAGAGATGAAGAACAATCCATCCACAAATTACACA
ACACTGCCAGACGAAATTATGAACCAGAAATTGTCGCCCTTCATGAGAAAGGGAATTACA
GGAGACTGGAAAAATCACTTTACAGTAGCCCTGAATGAAAAATTTGATAAACATTATGAG
CAGCAAATGAAGGAATCTACACTGAAGTTTCGAACTGAGATCTAA
Enzyme 3 GenBank Gene ID U08098 Link Image
Enzyme 3 GeneCard ID SULT1E1 Link Image
Enzyme 3 GenAtlas ID SULT1E1 Link Image
Enzyme 3 HGNC ID HGNC:11377 Link Image
Enzyme 3 Chromosome Location 4
Enzyme 3 Locus 4q13.1
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Aksoy IA, Wood TC, Weinshilboum R: Human liver estrogen sulfotransferase: identification by cDNA cloning and expression. Biochem Biophys Res Commun. 1994 May 16;200(3):1621-9. [PubMed Link Image]
  2. Her C, Aksoy IA, Kimura S, Brandriff BF, Wasmuth JJ, Weinshilboum RM: Human estrogen sulfotransferase gene (STE): cloning, structure, and chromosomal localization. Genomics. 1995 Sep 1;29(1):16-23. [PubMed Link Image]
  3. Falany CN, Krasnykh V, Falany JL: Bacterial expression and characterization of a cDNA for human liver estrogen sulfotransferase. J Steroid Biochem Mol Biol. 1995 Jun;52(6):529-39. [PubMed Link Image]
  4. Rubin GL, Harrold AJ, Mills JA, Falany CN, Coughtrie MW: Regulation of sulphotransferase expression in the endometrium during the menstrual cycle, by oral contraceptives and during early pregnancy. Mol Hum Reprod. 1999 Nov;5(11):995-1002. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Pedersen LC, Petrotchenko E, Shevtsov S, Negishi M: Crystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Ser137 in the sulfuryl transfer reaction. J Biol Chem. 2002 May 17;277(20):17928-32. Epub 2002 Mar 7. [PubMed Link Image]
  7. Shevtsov S, Petrotchenko EV, Pedersen LC, Negishi M: Crystallographic analysis of a hydroxylated polychlorinated biphenyl (OH-PCB) bound to the catalytic estrogen binding site of human estrogen sulfotransferase. Environ Health Perspect. 2003 Jun;111(7):884-8. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5685
Enzyme 4 Name Estradiol 17-beta-dehydrogenase 2
Enzyme 4 Synonyms
  1. 17-beta-hydroxysteroid dehydrogenase type 2
  2. 17-beta-HSD 2
  3. 20 alpha-hydroxysteroid dehydrogenase
  4. 20-alpha-HSD
  5. E2DH
  6. Microsomal 17-beta-hydroxysteroid dehydrogenase
  7. Testosterone 17-beta-dehydrogenase
Enzyme 4 Gene Name HSD17B2
Enzyme 4 Protein Sequence >Estradiol 17-beta-dehydrogenase 2
MSTFFSDTAWICLAVPTVLCGTVFCKYKKSSGQLWSWMVCLAGLCAVCLLILSPFWGLIL
FSVSCFLMYTYLSGQELLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPG
AEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQDRGLWAVINNAGVLGFPTDGELL
LMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAVT
MFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLPAEVQEDYGQDYI
LAQRNFLLLINSLASKDFSPVLRDIQHAILAKSPFAYYTPGKGAYLWICLAHYLPIGIYD
YFAKRHFGQDKPMPRALRMPNYKKKAT
Enzyme 4 Number of Residues 387
Enzyme 4 Molecular Weight 42784.8
Enzyme 4 Theoretical pI 8.62
Enzyme 4 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 4 General Function Involved in oxidoreductase activity
Enzyme 4 Specific Function Capable of catalyzing the interconversion of testosterone and androstenedione, as well as estradiol and estrone. Also has 20-alpha-HSD activity. Uses NADH while EDH17B3 uses NADPH
Enzyme 4 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 4 Reactions
  • testosterone + NAD+ = androst-4-ene-3,17-dione + NADH + H+ [RN:R01836]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 4-24
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID P37059 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name DHB2_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1164 bp
ATGAGCACTTTCTTCTCGGACACAGCATGGATCTGCCTGGCTGTCCCCACAGTACTATGT
GGGACAGTATTTTGCAAATACAAGAAGAGCTCAGGGCAGCTGTGGAGCTGGATGGTCTGC
CTGGCAGGCCTCTGTGCAGTCTGCCTGCTCATCCTGTCCCCTTTTTGGGGCTTGATCCTC
TTCTCGGTGTCATGCTTCCTCATGTATACTTACTTATCTGGCCAAGAATTGTTACCTGTG
GATCAGAAGGCAGTCCTGGTGACAGGTGGTGATTGCGGGCTTGGCCATGCTTTGTGCAAG
TATCTGGATGAGCTGGGCTTCACGGTATTTGCCGGAGTTTTGAATGAAAATGGCCCAGGA
GCTGAGGAATTGCGAAGAACCTGCTCTCCGCGCCTCTCGGTGCTCCAAATGGACATCACG
AAGCCAGTGCAGATAAAAGATGCTTACAGCAAGGTTGCAGCAATGCTGCAGGACAGAGGA
CTGTGGGCTGTGATCAACAATGCTGGGGTGCTTGGCTTTCCAACTGATGGGGAGCTTCTT
CTTATGACTGACTACAAACAATGCATGGCCGTGAACTTCTTTGGAACTGTGGAGGTCACA
AAGACGTTTTTGCCTCTTCTTAGAAAATCCAAAGGGAGGCTGGTGAATGTCAGCAGCATG
GGAGGAGGGGCCCCAATGGAAAGGCTGGCATCTTATGGCTCATCAAAGGCGGCTGTGACC
ATGTTCTCATCAGTTATGAGACTGGAGCTTTCCAAGTGGGGAATTAAAGTTGCTTCCATC
CAACCTGGAGGCTTCCTAACAAATATCGCAGGCACCAGTGACAAGTGGGAAAAGCTGGAG
AAGGACATTCTGGACCACCTCCCCGCTGAGGTACAGGAAGACTACGGCCAGGACTACATC
TTAGCACAGCGGAATTTCCTCCTATTGATCAACTCGTTAGCCAGCAAGGACTTCTCTCCG
GTGCTGCGGGACATCCAGCATGCTATCTTGGCGAAGAGCCCTTTTGCCTATTACACGCCA
GGGAAAGGCGCTTACTTGTGGATCTGCCTTGCTCACTATTTGCCTATTGGCATATATGAT
TACTTTGCTAAAAGACATTTTGGCCAAGACAAGCCCATGCCCAGAGCTCTAAGAATGCCT
AACTACAAGAAAAAGGCCACCTAG
Enzyme 4 GenBank Gene ID L11708 Link Image
Enzyme 4 GeneCard ID HSD17B2 Link Image
Enzyme 4 GenAtlas ID HSD17B2 Link Image
Enzyme 4 HGNC ID HGNC:5211 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 16q24.1-q24.2
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Wu L, Einstein M, Geissler WM, Chan HK, Elliston KO, Andersson S: Expression cloning and characterization of human 17 beta-hydroxysteroid dehydrogenase type 2, a microsomal enzyme possessing 20 alpha-hydroxysteroid dehydrogenase activity. J Biol Chem. 1993 Jun 15;268(17):12964-9. [PubMed Link Image]
  2. Labrie Y, Durocher F, Lachance Y, Turgeon C, Simard J, Labrie C, Labrie F: The human type II 17 beta-hydroxysteroid dehydrogenase gene encodes two alternatively spliced mRNA species. DNA Cell Biol. 1995 Oct;14(10):849-61. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5687
Enzyme 5 Name UDP-glucuronosyltransferase 2B28
Enzyme 5 Synonyms
  1. UDPGT 2B28
Enzyme 5 Gene Name UGT2B28
Enzyme 5 Protein Sequence >UDP-glucuronosyltransferase 2B28
MALKWTSVLLLIHLGCYFSSGSCGKVLVWTGEYSHWMNMKTILKELVQRGHEVTVLASSA
SILFDPNDAFTLKLEVYPTSLTKTEFENIIMQQVKRWSDIQKDSFWLYFSQEQEILWEFH
DIFRNFCKDVVSNKKVMKKLQESRFDIIFADAFFPCGELLAALLNIPFVYSLCFTPGYTI
ERHSGGLIFPPSYIPVVMSKLSDQMTFMERVKNMIYVLYFDFWFQMCDMKKWDQFYSEVL
GRPTTLFETMGKADIWLMRNSWSFQFPHPFLPNIDFVGGLHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSVISNMTAERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQN
DLLGLPKTRAFITHGGANGIYEAIYHGIPMVGIPLFWDQPDNIAHMKAKGAAVRLDFHTM
SSTDLLNALKTVINDPSYKENVMKLSIIQHDQPVKPLHRAVFWIEFVMCHKGAKHLRVAA
RDLTWFQYHSLDVIGFLLACVATVIFVVTKFCLFCFWKFARKGKKGKRD
Enzyme 5 Number of Residues 529
Enzyme 5 Molecular Weight 60905.8
Enzyme 5 Theoretical pI 8.80
Enzyme 5 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 5 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 5 Specific Function UDPGTs are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme has glucuronidating capacity with steroid substrates such as 5-beta-androstane 3-alpha,17-beta- diol, estradiol, ADT, eugenol and bile acids. Only isoform 1 seems to be active
Enzyme 5 Pathways
Enzyme 5 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-24
Enzyme 5 Transmembrane Regions
  • 495-517
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 13603476 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q9BY64 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name UDB28_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1590 bp
ATGGCTCTGAAGTGGACTTCAGTTCTTCTGCTGATACATCTCGGTTGTTACTTTAGCTCT
GGGAGTTGTGGAAAGGTGCTGGTGTGGACCGGTGAATACAGCCATTGGATGAATATGAAG
ACAATCCTGAAAGAGCTTGTTCAGAGAGGTCATGAGGTGACTGTACTGGCATCTTCAGCT
TCCATTCTTTTTGATCCCAATGACGCATTCACTCTTAAACTCGAAGTTTATCCTACATCT
TTAACTAAAACTGAATTTGAGAATATCATCATGCAACAGGTTAAGAGATGGTCAGACATT
CAAAAAGATAGCTTTTGGTTATATTTTTCACAAGAACAAGAAATCCTGTGGGAATTTCAT
GACATATTTAGAAACTTCTGTAAAGATGTAGTTTCAAATAAGAAAGTTATGAAAAAACTA
CAAGAGTCAAGATTTGACATCATTTTTGCAGATGCTTTTTTTCCTTGTGGTGAGCTGCTG
GCTGCGCTACTTAACATACCGTTTGTGTACAGTCTCTGCTTCACTCCTGGCTACACAATT
GAAAGGCACAGTGGAGGACTGATTTTCCCTCCTTCCTACATACCTGTTGTTATGTCAAAA
TTAAGTGATCAAATGACTTTCATGGAGAGGGTAAAAAACATGATCTATGTGCTTTATTTT
GACTTTTGGTTCCAAATGTGTGATATGAAGAAGTGGGATCAGTTTTACAGTGAAGTTTTA
GGAAGACCCACTACCTTATTTGAGACAATGGGGAAAGCTGACATATGGCTTATGCGAAAC
TCCTGGAGTTTTCAATTTCCTCATCCATTCTTACCAAACATTGATTTTGTTGGAGGACTC
CACTGCAAACCTGCCAAACCCCTACCTAAGGAAATGGAGGAATTTGTACAGAGCTCTGGT
GAAAATGGTGTTGTGGTGTTTTCTCTGGGGTCAGTGATAAGTAACATGACAGCAGAAAGG
GCCAACGTAATTGCAACAGCCCTTGCCAAGATCCCACAAAAGGTTCTGTGGAGATTTGAT
GGGAATAAACCAGATGCCTTAGGTCTCAATACTCGGCTGTATAAGTGGATACCCCAGAAT
GACCTTCTAGGTCTTCCAAAAACCAGAGCTTTTATAACTCATGGTGGAGCCAATGGCATC
TATGAGGCAATCTACCATGGGATCCCTATGGTAGGCATTCCATTGTTTTGGGATCAACCT
GATAACATTGCTCACATGAAGGCCAAGGGAGCAGCTGTTAGACTGGACTTCCACACAATG
TCGAGTACAGACCTGCTGAATGCACTGAAGACAGTAATTAATGATCCTTCATATAAAGAG
AATGTTATGAAATTATCAATAATTCAACATGATCAACCAGTAAAGCCCCTGCATCGAGCA
GTCTTCTGGATTGAATTTGTGATGTGCCACAAAGGAGCCAAACACCTTCGAGTTGCAGCC
CGTGACCTCACCTGGTTCCAGTACCACTCTTTGGATGTGATTGGGTTTCTGCTGGCCTGT
GTGGCAACTGTGATATTTGTCGTCACAAAGTTTTGTCTGTTTTGTTTCTGGAAGTTTGCT
AGAAAAGGGAAGAAGGGAAAAAGAGATTAG
Enzyme 5 GenBank Gene ID AF177272 Link Image
Enzyme 5 GeneCard ID UGT2B28 Link Image
Enzyme 5 GenAtlas ID UGT2B28 Link Image
Enzyme 5 HGNC ID HGNC:13479 Link Image
Enzyme 5 Chromosome Location 4
Enzyme 5 Locus 4q13.2
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Levesque E, Turgeon D, Carrier JS, Montminy V, Beaulieu M, Belanger A: Isolation and characterization of the UGT2B28 cDNA encoding a novel human steroid conjugating UDP-glucuronosyltransferase. Biochemistry. 2001 Apr 3;40(13):3869-81. [PubMed Link Image]
  2. Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5691
Enzyme 6 Name Estradiol 17-beta-dehydrogenase 8
Enzyme 6 Synonyms
  1. 17-beta-hydroxysteroid dehydrogenase 8
  2. 17-beta-HSD 8
  3. 3-oxoacyl-[acyl-carrier-protein] reductase
  4. Protein Ke6
  5. Ke-6
  6. Really interesting new gene 2 protein
  7. Testosterone 17-beta-dehydrogenase 8
Enzyme 6 Gene Name HSD17B8
Enzyme 6 Protein Sequence >Estradiol 17-beta-dehydrogenase 8
MASQLQNRLRSALALVTGAGSGIGRAVSVRLAGEGATVAACDLDRAAAQETVRLLGGPGS
KEGPPRGNHAAFQADVSEARAARCLLEQVQACFSRPPSVVVSCAGITQDEFLLHMSEDDW
DKVIAVNLKGTFLVTQAAAQALVSNGCRGSIINISSIVGKVGNVGQTNYAASKAGVIGLT
QTAARELGRHGIRCNSVLPGFIATPMTQKVPQKVVDKITEMIPMGHLGDPEDVADVVAFL
ASEDSGYITGTSVEVTGGLFM
Enzyme 6 Number of Residues 261
Enzyme 6 Molecular Weight 26973.6
Enzyme 6 Theoretical pI 6.50
Enzyme 6 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 6 General Function Involved in oxidoreductase activity
Enzyme 6 Specific Function NAD-dependent 17-beta-hydroxysteroid dehydrogenase with highest activity towards estradiol. Has very low activity towards testosterone. The heteroteramer with CBR4 has NADH-dependent 3- ketoacyl-acyl carrier protein reductase activity. May play a role in biosynthesis of fatty acids in mitochondria
Enzyme 6 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 6 Reactions
  • testosterone + NAD+ = androst-4-ene-3,17-dione + NADH + H+ [RN:R01836]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein Not Available
Enzyme 6 UniProtKB/Swiss-Prot ID Q92506 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name DHB8_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >786 bp
ATGGCGTCTCAGCTCCAGAACCGACTCCGCTCCGCACTGGCCTTGGTCACAGGTGCGGGG
AGCGGCATCGGCCGAGCGGTCAGTGTACGCCTGGCCGGAGAGGGGGCCACCGTAGCTGCC
TGCGACCTGGACCGGGCAGCGGCACAGGAGACGGTGCGGCTGCTGGGCGGGCCAGGGAGC
AAGGAGGGGCCGCCCCGAGGGAACCATGCTGCCTTCCAGGCTGACGTGTCTGAGGCCAGG
GCCGCCAGGTGCCTGCTGGAACAAGTGCAGGCCTGCTTTTCTCGCCCACCATCTGTCGTT
GTGTCCTGTGCGGGCATCACCCAGGATGAGTTTCTGCTGCACATGTCTGAGGATGACTGG
GACAAAGTCATAGCTGTCAACCTCAAGGGCACCTTCCTAGTCACTCAGGCTGCAGCACAA
GCCCTGGTGTCCAATGGTTGTCGTGGTTCCATCATCAACATCAGTAGCATCGTAGGAAAG
GTGGGGAACGTGGGGCAGACAAACTATGCAGCATCCAAGGCTGGAGTGATTGGGCTGACC
CAGACCGCAGCCCGGGAGCTTGGACGACATGGGATCCGCTGTAACTCTGTCCTCCCAGGG
TTCATTGCAACACCCATGACACAGAAAGTGCCACAGAAAGTGGTGGACAAGATTACTGAA
ATGATCCCGATGGGACACTTGGGGGACCCTGAGGATGTGGCAGATGTGGTCGCATTCTTG
GCATCTGAAGATAGTGGATACATCACAGGGACCTCAGTGGAAGTCACTGGAGGTCTTTTC
ATGTAG
Enzyme 6 GenBank Gene ID BT007239 Link Image
Enzyme 6 GeneCard ID HSD17B8 Link Image
Enzyme 6 GenAtlas ID HSD17B8 Link Image
Enzyme 6 HGNC ID HGNC:3554 Link Image
Enzyme 6 Chromosome Location 6
Enzyme 6 Locus 6p21.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Ando A, Kikuti YY, Shigenari A, Kawata H, Okamoto N, Shiina T, Chen L, Ikemura T, Abe K, Kimura M, Inoko H: cDNA cloning of the human homologues of the mouse Ke4 and Ke6 genes at the centromeric end of the human MHC region. Genomics. 1996 Aug 1;35(3):600-2. [PubMed Link Image]
  4. Ohno S, Nishikawa K, Honda Y, Nakajin S: Expression in E. coli and tissue distribution of the human homologue of the mouse Ke 6 gene, 17beta-hydroxysteroid dehydrogenase type 8. Mol Cell Biochem. 2008 Feb;309(1-2):209-15. Epub 2007 Nov 3. [PubMed Link Image]
  5. Chen Z, Kastaniotis AJ, Miinalainen IJ, Rajaram V, Wierenga RK, Hiltunen JK: 17beta-hydroxysteroid dehydrogenase type 8 and carbonyl reductase type 4 assemble as a ketoacyl reductase of human mitochondrial FAS. FASEB J. 2009 Nov;23(11):3682-91. Epub 2009 Jul 1. [PubMed Link Image]
  6. Rotinen M, Celay J, Alonso MM, Arrazola A, Encio I, Villar J: Estradiol induces type 8 17beta-hydroxysteroid dehydrogenase expression: crosstalk between estrogen receptor alpha and C/EBPbeta. J Endocrinol. 2009 Jan;200(1):85-92. Epub 2008 Oct 13. [PubMed Link Image]
  7. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5692
Enzyme 7 Name Solute carrier organic anion transporter family member 1B1
Enzyme 7 Synonyms
  1. Liver-specific organic anion transporter 1
  2. LST-1
  3. OATP-C
  4. Sodium-independent organic anion-transporting polypeptide 2
  5. OATP-2
  6. Solute carrier family 21 member 6
Enzyme 7 Gene Name SLCO1B1
Enzyme 7 Protein Sequence >Solute carrier organic anion transporter family member 1B1
MDQNQHLNKTAEAQPSENKKTRYCNGLKMFLAALSLSFIAKTLGAIIMKSSIIHIERRFE
ISSSLVGFIDGSFEIGNLLVIVFVSYFGSKLHRPKLIGIGCFIMGIGGVLTALPHFFMGY
YRYSKETNINSSENSTSTLSTCLINQILSLNRASPEIVGKGCLKESGSYMWIYVFMGNML
RGIGETPIVPLGLSYIDDFAKEGHSSLYLGILNAIAMIGPIIGFTLGSLFSKMYVDIGYV
DLSTIRITPTDSRWVGAWWLNFLVSGLFSIISSIPFFFLPQTPNKPQKERKASLSLHVLE
TNDEKDQTANLTNQGKNITKNVTGFFQSFKSILTNPLYVMFVLLTLLQVSSYIGAFTYVF
KYVEQQYGQPSSKANILLGVITIPIFASGMFLGGYIIKKFKLNTVGIAKFSCFTAVMSLS
FYLLYFFILCENKSVAGLTMTYDGNNPVTSHRDVPLSYCNSDCNCDESQWEPVCGNNGIT
YISPCLAGCKSSSGNKKPIVFYNCSCLEVTGLQNRNYSAHLGECPRDDACTRKFYFFVAI
QVLNLFFSALGGTSHVMLIVKIVQPELKSLALGFHSMVIRALGGILAPIYFGALIDTTCI
KWSTNNCGTRGSCRTYNSTSFSRVYLGLSSMLRVSSLVLYIILIYAMKKKYQEKDINASE
NGSVMDEANLESLNKNKHFVPSAGADSETHC
Enzyme 7 Number of Residues 691
Enzyme 7 Molecular Weight 76448.0
Enzyme 7 Theoretical pI 8.68
Enzyme 7 GO Classification
Function
  • transporter activity
Process
  • establishment of localization
  • transport
Component
  • cell part
  • membrane
Enzyme 7 General Function Involved in transporter activity
Enzyme 7 Specific Function Mediates the Na(+)-independent transport of organic anions such as pravastatin, taurocholate, methotrexate, dehydroepiandrosterone sulfate, 17-beta-glucuronosyl estradiol, estrone sulfate, prostaglandin E2, thromboxane B2, leukotriene C3, leukotriene E4, thyroxine and triiodothyronine. May play an important role in the clearance of bile acids and organic anions from the liver
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • 97-117 207-227 259-279 336-356 376-396 410-430 575-595
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 5006265 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q9Y6L6 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name SO1B1_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >2076 bp
ATGGACCAAAATCAACATTTGAATAAAACAGCAGAGGCACAACCTTCAGAGAATAAGAAA
ACAAGATACTGCAATGGATTGAAGATGTTCTTGGCAGCTCTGTCACTCAGCTTTATTGCT
AAGACACTAGGTGCAATTATTATGAAAAGTTCCATCATTCATATAGAACGGAGATTTGAG
ATATCCTCTTCTCTTGTTGGTTTTATTGACGGAAGCTTTGAAATTGGAAATTTGCTTGTG
ATTGTATTTGTGAGTTACTTTGGATCCAAACTACATAGACCAAAGTTAATTGGAATCGGT
TGTTTCATTATGGGAATTGGAGGTGTTTTGACTGCTTTGCCACATTTCTTCATGGGATAT
TACAGGTATTCTAAAGAAACTAATATCAATTCATCAGAAAATTCAACATCGACCTTATCC
ACTTGTTTAATTAATCAAATTTTATCACTCAATAGAGCATCACCTGAGATAGTGGGAAAA
GGTTGTTTAAAGGAATCTGGGTCATACATGTGGATATATGTGTTCATGGGTAATATGCTT
CGTGGAATAGGGGAGACTCCCATAGTACCACTGGGGCTTTCTTACATTGATGATTTCGCT
AAAGAAGGACATTCTTCTTTGTATTTAGGTATATTGAATGCAATAGCAATGATTGGTCCA
ATCATTGGCTTTACCCTGGGATCTCTGTTTTCTAAAATGTACGTGGATATTGGATATGTA
GATCTAAGCACTATCAGGATAACTCCTACTGATTCTCGATGGGTTGGAGCTTGGTGGCTT
AATTTCCTTGTGTCTGGACTATTCTCCATTATTTCTTCCATACCATTCTTTTTCTTGCCC
CAAACTCCAAATAAACCACAAAAAGAAAGAAAAGCTTCACTGTCTTTGCATGTGCTGGAA
ACAAATGATGAAAAGGATCAAACAGCTAATTTGACCAATCAAGGAAAAAATATTACCAAA
AATGTGACTGGTTTTTTCCAGTCTTTTAAAAGCATCCTTACTAATCCCCTGTATGTTATG
TTTGTGCTTTTGACGTTGTTACAAGTAAGCAGCTATATTGGTGCTTTTACTTATGTCTTC
AAATACGTAGAGCAACAGTATGGTCAGCCTTCATCTAAGGCTAACATCTTATTGGGAGTC
ATAACCATACCTATTTTTGCAAGTGGAATGTTTTTAGGAGGATATATCATTAAAAAATTC
AAACTGAACACCGTTGGAATTGCCAAATTCTCATGTTTTACTGCTGTGATGTCATTGTCC
TTTTACCTATTATATTTTTTCATACTCTGTGAAAACAAATCAGTTGCCGGACTAACCATG
ACCTATGATGGAAATAATCCAGTGACATCTCATAGAGATGTACCACTTTCTTATTGCAAC
TCAGACTGCAATTGTGATGAAAGTCAATGGGAACCAGTCTGTGGAAACAATGGAATAACT
TACATCTCACCCTGTCTAGCAGGTTGCAAATCTTCAAGTGGCAATAAAAAGCCTATAGTG
TTTTACAACTGCAGTTGTTTGGAAGTAACTGGTCTCCAGAACAGAAATTACTCAGCCCAT
TTGGGTGAATGCCCAAGAGATGATGCTTGTACAAGGAAATTTTACTTTTTTGTTGCAATA
CAAGTCTTGAATTTATTTTTCTCTGCACTTGGAGGCACCTCACATGTCATGCTGATTGTT
AAAATTGTTCAACCTGAATTGAAATCACTTGCACTGGGTTTCCACTCAATGGTTATACGA
GCACTAGGAGGAATTCTAGCTCCAATATATTTTGGGGCTCTGATTGATACAACGTGTATA
AAGTGGTCCACCAACAACTGTGGCACACGTGGGTCATGTAGGACATATAATTCCACATCA
TTTTCAAGGGTCTACTTGGGCTTGTCTTCAATGTTAAGAGTCTCATCACTTGTTTTATAT
ATTATATTAATTTATGCCATGAAGAAAAAATATCAAGAGAAAGATATCAATGCATCAGAA
AATGGAAGTGTCATGGATGAAGCAAACTTAGAATCCTTAAATAAAAATAAACATTTTGTC
CCTTCTGCTGGGGCAGATAGTGAAACACATTGTTAA
Enzyme 7 GenBank Gene ID AB026257 Link Image
Enzyme 7 GeneCard ID SLCO1B1 Link Image
Enzyme 7 GenAtlas ID SLCO1B1 Link Image
Enzyme 7 HGNC ID HGNC:10959 Link Image
Enzyme 7 Chromosome Location 1
Enzyme 7 Locus 12p
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Abe T, Kakyo M, Tokui T, Nakagomi R, Nishio T, Nakai D, Nomura H, Unno M, Suzuki M, Naitoh T, Matsuno S, Yawo H: Identification of a novel gene family encoding human liver-specific organic anion transporter LST-1. J Biol Chem. 1999 Jun 11;274(24):17159-63. [PubMed Link Image]
  2. Hsiang B, Zhu Y, Wang Z, Wu Y, Sasseville V, Yang WP, Kirchgessner TG: A novel human hepatic organic anion transporting polypeptide (OATP2). Identification of a liver-specific human organic anion transporting polypeptide and identification of rat and human hydroxymethylglutaryl-CoA reductase inhibitor transporters. J Biol Chem. 1999 Dec 24;274(52):37161-8. [PubMed Link Image]
  3. Konig J, Cui Y, Nies AT, Keppler D: A novel human organic anion transporting polypeptide localized to the basolateral hepatocyte membrane. Am J Physiol Gastrointest Liver Physiol. 2000 Jan;278(1):G156-64. [PubMed Link Image]
  4. Konig J, Cui Y, Nies AT, Keppler D: Localization and genomic organization of a new hepatocellular organic anion transporting polypeptide. J Biol Chem. 2000 Jul 28;275(30):23161-8. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Tirona RG, Leake BF, Merino G, Kim RB: Polymorphisms in OATP-C: identification of multiple allelic variants associated with altered transport activity among European- and African-Americans. J Biol Chem. 2001 Sep 21;276(38):35669-75. Epub 2001 Jul 26. [PubMed Link Image]
  8. Michalski C, Cui Y, Nies AT, Nuessler AK, Neuhaus P, Zanger UM, Klein K, Eichelbaum M, Keppler D, Konig J: A naturally occurring mutation in the SLC21A6 gene causing impaired membrane localization of the hepatocyte uptake transporter. J Biol Chem. 2002 Nov 8;277(45):43058-63. Epub 2002 Aug 23. [PubMed Link Image]
  9. Nozawa T, Nakajima M, Tamai I, Noda K, Nezu J, Sai Y, Tsuji A, Yokoi T: Genetic polymorphisms of human organic anion transporters OATP-C (SLC21A6) and OATP-B (SLC21A9): allele frequencies in the Japanese population and functional analysis. J Pharmacol Exp Ther. 2002 Aug;302(2):804-13. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5696
Enzyme 8 Name UDP-glucuronosyltransferase 2B4
Enzyme 8 Synonyms
  1. UDPGT 2B4
  2. HLUG25
  3. Hyodeoxycholic acid-specific UDPGT
  4. UDPGTh-1
Enzyme 8 Gene Name UGT2B4
Enzyme 8 Protein Sequence >UDP-glucuronosyltransferase 2B4
MSMKWTSALLLIQLSCYFSSGSCGKVLVWPTEFSHWMNIKTILDELVQRGHEVTVLASSA
SISFDPNSPSTLKFEVYPVSLTKTEFEDIIKQLVKRWAELPKDTFWSYFSQVQEIMWTFN
DILRKFCKDIVSNKKLMKKLQESRFDVVLADAVFPFGELLAELLKIPFVYSLRFSPGYAI
EKHSGGLLFPPSYVPVVMSELSDQMTFIERVKNMIYVLYFEFWFQIFDMKKWDQFYSEVL
GRPTTLSETMAKADIWLIRNYWDFQFPHPLLPNVEFVGGLHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSMVSNTSEERANVIASALAKIPQKVLWRFDGNKPDTLGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGVPLFADQPDNIAHMKAKGAAVSLDFHTM
SSTDLLNALKTVINDPLYKENAMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAA
HDLTWFQYHSLDVTGFLLACVATVIFIITKCLFCVWKFVRTGKKGKRD
Enzyme 8 Number of Residues 528
Enzyme 8 Molecular Weight 60512.0
Enzyme 8 Theoretical pI 8.75
Enzyme 8 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 8 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 8 Specific Function UDPGTs are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme is active on polyhydroxylated estrogens (such as estriol, 4-hydroxyestrone and 2-hydroxyestriol) and xenobiotics (such as 4-methylumbelliferone, 1-naphthol, 4- nitrophenol, 2-aminophenol, 4-hydroxybiphenyl and menthol). It is capable of 6 alpha-hydroxyglucuronidation of hyodeoxycholic acid
Enzyme 8 Pathways
Enzyme 8 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-23
Enzyme 8 Transmembrane Regions
  • 493-509
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 37589 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P06133 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name UD2B4_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1587 bp
ATGTCTATGAAATGGACTTCAGCTCTTCTGCTGATACAGCTGAGCTGTTACTTTAGCTCT
GGGAGTTGTGGAAAGGTGCTGGTGTGGCCCACAGAATTCAGCCACTGGATGAATATAAAG
ACAATCCTGGATGAACTTGTCCAGAGAGGTCATGAGGTGACTGTATTGGCATCTTCAGCT
TCCATTTCTTTCGATCCCAACAGCCCATCTACTCTTAAATTTGAAGTTTATCCTGTATCT
TTAACTAAAACTGAGTTTGAGGATATTATCAAGCAGCTGGTTAAGAGATGGGCAGAACTT
CCAAAAGACACATTTTGGTCATATTTTTCACAAGTACAAGAAATCATGTGGACATTTAAT
GACATACTTAGAAAGTTCTGTAAGGATATAGTTTCAAATAAGAAACTTATGAAGAAACTA
CAGGAGTCAAGATTTGATGTTGTTCTTGCAGATGCTGTTTTCCCCTTTGGTGAGCTGCTG
GCCGAGTTACTTAAAATACCCTTTGTCTACAGGCCTCGCTTCTCTCCTGGCTACGCAATT
GAAAAGCATAGTGGAGGACTTCTGTTCCCTCCTTCCTATGTGCCTGTTGTTATGTCAGAA
CTAAGTGACCAAATGACTTTCATAGAGAGGGTAAAAAATATGATCTATGTGCTTTATTTT
GAATTTTGGTTCCAAATATTTGACATGAAGAAGTGGGATCAGTTCTACAGTGAAGTTCTA
GGAAGACCCACTACGTTATCTGAGACAATGGCAAAAGCTGACATATGGCTTATTCGAAAC
TACTGGGATTTTCAATTTCCTCACCCACTCTTACCAAATGTTGAGTTCGTTGGAGGACTC
CACTGCAAACCTGCCAAACCCCTACCGAAGGAAATGGAAGAGTTTGTCCAGAGCTCTGGA
GAAAATGGTGTTGTGGTGTTTTCTCTGGGGTCGATGGTCAGTAACACGTCAGAAGAAAGG
GCCAATGTAATTGCATCAGCCCTTGCCAAGATCCCACAAAAGGTTCTGTGGAGATTTGAT
GGGAATAAACCAGATACTTTAGGACTCAATACTCGGCTGTACAAGTGGATACCCCAGAAT
GATCTTCTTGGTCACCCAAAAACCAGAGCTTTTATAACTCATGGTGGAGCCAATGGCATC
TATAAGGCAATCTCTCCTAGAATCCCTATGGTGGGCGTTCCATTGTTTGCAGATCAACCT
GATAACATTGCACACATGAAGGCCAAGGGAGCAGCTGTTAGTTTGGACTTCCACACAATG
TCGAGTACAGACTTACTCAATGCACTGAAGACAGTAATTAATGATCCTTTATATAAAGAG
AATGCTATGAAATTATCAAGAATTCATCATGATCAACCAGTGAAGCCCCTTGATCGAGCA
GTCTTCTGGATTGAATTTGTCATGCGCCATAAAGGAGCCAAGCACCTTCGGGTTGCAGCC
CACGACCTCACCTGGTTCCAGTACCACTCTTTGGATGTGACTGGGTTCCTGCTGGCCTGT
GTGGCAACTGTGATATTCATCATCACAAAATGTCTGTTTTGTGTCTGGAAGTTTGTTAGA
ACAGGAAAGAAGGGGAAAAGAGATTAA
Enzyme 8 GenBank Gene ID Y00317 Link Image
Enzyme 8 GeneCard ID UGT2B4 Link Image
Enzyme 8 GenAtlas ID UGT2B4 Link Image
Enzyme 8 HGNC ID HGNC:12553 Link Image
Enzyme 8 Chromosome Location 4
Enzyme 8 Locus 4q13
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Jackson MR, McCarthy LR, Harding D, Wilson S, Coughtrie MW, Burchell B: Cloning of a human liver microsomal UDP-glucuronosyltransferase cDNA. Biochem J. 1987 Mar 1;242(2):581-8. [PubMed Link Image]
  2. Jin CJ, Miners JO, Lillywhite KJ, Mackenzie PI: cDNA cloning and expression of two new members of the human liver UDP-glucuronosyltransferase 2B subfamily. Biochem Biophys Res Commun. 1993 Jul 15;194(1):496-503. [PubMed Link Image]
  3. Levesque E, Beaulieu M, Hum DW, Belanger A: Characterization and substrate specificity of UGT2B4 (E458): a UDP-glucuronosyltransferase encoded by a polymorphic gene. Pharmacogenetics. 1999 Apr;9(2):207-16. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5719
Enzyme 9 Name UDP-glucuronosyltransferase 1-4
Enzyme 9 Synonyms
  1. UDPGT 1-4
  2. UGT1*4
  3. UGT1-04
  4. UGT1.4
  5. Bilirubin-specific UDPGT isozyme 2
  6. hUG-BR2
  7. UDP-glucuronosyltransferase 1-D
  8. UGT-1D
  9. UGT1D
  10. UDP-glucuronosyltransferase 1A4
Enzyme 9 Gene Name UGT1A4
Enzyme 9 Protein Sequence >UDP-glucuronosyltransferase 1-4
MARGLQVPLPRLATGLLLLLSVQPWAESGKVLVVPTDGSPWLSMREALRELHARGHQAVV
LTPEVNMHIKEEKFFTLTAYAVPWTQKEFDRVTLGYTQGFFETEHLLKRYSRSMAIMNNV
SLALHRCCVELLHNEALIRHLNATSFDVVLTDPVNLCGAVLAKYLSIPAVFFWRYIPCDL
DFKGTQCPNPSSYIPKLLTTNSDHMTFLQRVKNMLYPLALSYICHTFSAPYASLASELFQ
REVSVVDLVSYASVWLFRGDFVMDYPRPIMPNMVFIGGINCANGKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 9 Number of Residues 534
Enzyme 9 Molecular Weight 60024.5
Enzyme 9 Theoretical pI 8.68
Enzyme 9 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 9 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 9 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform glucuronidates bilirubin IX- alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate
Enzyme 9 Pathways
Enzyme 9 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-28
Enzyme 9 Transmembrane Regions
  • 492-508
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
Enzyme 9 UniProtKB/Swiss-Prot ID P22310 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name UD14_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1605 bp
ATGGCCAGAGGACTCCAGGTTCCCCTGCCGCGGCTGGCCACAGGACTGCTGCTCCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGAAAGGTGTTGGTGGTGCCCACTGATGGCAGCCCC
TGGCTCAGCATGCGGGAGGCCTTGCGGGAGCTCCATGCCAGAGGCCACCAGGCGGTGGTC
CTCACCCCAGAGGTGAATATGCACATCAAAGAAGAGAAATTTTTCACCCTGACAGCCTAT
GCTGTTCCATGGACCCAGAAGGAATTTGATCGCGTTACGCTGGGCTACACTCAAGGGTTC
TTTGAAACAGAACATCTTCTGAAGAGATATTCTAGAAGTATGGCAATTATGAACAATGTA
TCTTTGGCCCTTCATAGGTGTTGTGTGGAGCTACTGCATAATGAGGCCCTGATCAGGCAC
CTGAATGCTACTTCCTTTGATGTGGTTTTAACAGACCCCGTTAACCTCTGCGGGGCGGTG
CTGGCTAAGTACCTGTCGATTCCTGCTGTGTTTTTTTGGAGGTACATTCCATGTGACTTA
GACTTTAAGGGCACACAGTGTCCAAATCCTTCCTCCTATATTCCTAAGTTACTAACGACC
AATTCAGACCACATGACATTCCTGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACATTTGCCATACTTTTTCTGCCCCTTATGCAAGTCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATCTTGTCAGCTATGCATCCGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGACTACCCCAGGCCGATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACGGGAAGCCACTATCTCAGGAATTTGAAGCCTACATTAATGCTTCTGGAGAA
CATGGAATTGTGGTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCT
ATGGCAATTGCTGATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGA
ACCCGACCATCGAATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGAT
CTGCTTGGTCACCCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTAT
GAAAGCATATGCAATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGAC
AATGCAAAGCGCATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACT
TCTGAAGATTTAGAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAAC
ATCATGCGCCTCTCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTG
TTCTGGGTGGAGTTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCAC
GACCTCACCTGGTACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTG
CTGACAGTGGCCTTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGG
AAAAAAGGGCGAGTTAAGAAAGCCCACAAATCCAAGACCCATTGA
Enzyme 9 GenBank Gene ID M57951 Link Image
Enzyme 9 GeneCard ID UGT1A4 Link Image
Enzyme 9 GenAtlas ID UGT1A4 Link Image
Enzyme 9 HGNC ID HGNC:12536 Link Image
Enzyme 9 Chromosome Location 2
Enzyme 9 Locus 2q37
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Ritter JK, Crawford JM, Owens IS: Cloning of two human liver bilirubin UDP-glucuronosyltransferase cDNAs with expression in COS-1 cells. J Biol Chem. 1991 Jan 15;266(2):1043-7. [PubMed Link Image]
  2. Ritter JK, Chen F, Sheen YY, Tran HM, Kimura S, Yeatman MT, Owens IS: A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini. J Biol Chem. 1992 Feb 15;267(5):3257-61. [PubMed Link Image]
  3. Gong QH, Cho JW, Huang T, Potter C, Gholami N, Basu NK, Kubota S, Carvalho S, Pennington MW, Owens IS, Popescu NC: Thirteen UDPglucuronosyltransferase genes are encoded at the human UGT1 gene complex locus. Pharmacogenetics. 2001 Jun;11(4):357-68. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  6. Bosma PJ, Chowdhury JR, Huang TJ, Lahiri P, Elferink RP, Van Es HH, Lederstein M, Whitington PF, Jansen PL, Chowdhury NR: Mechanisms of inherited deficiencies of multiple UDP-glucuronosyltransferase isoforms in two patients with Crigler-Najjar syndrome, type I. FASEB J. 1992 Jul;6(10):2859-63. [PubMed Link Image]
  7. Aono S, Yamada Y, Keino H, Hanada N, Nakagawa T, Sasaoka Y, Yazawa T, Sato H, Koiwai O: Identification of defect in the genes for bilirubin UDP-glucuronosyl-transferase in a patient with Crigler-Najjar syndrome type II. Biochem Biophys Res Commun. 1993 Dec 30;197(3):1239-44. [PubMed Link Image]
  8. Moghrabi N, Clarke DJ, Boxer M, Burchell B: Identification of an A-to-G missense mutation in exon 2 of the UGT1 gene complex that causes Crigler-Najjar syndrome type 2. Genomics. 1993 Oct;18(1):171-3. [PubMed Link Image]
  9. Menard V, Girard H, Harvey M, Perusse L, Guillemette C: Analysis of inherited genetic variations at the UGT1 locus in the French-Canadian population. Hum Mutat. 2009 Apr;30(4):677-87. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5721
Enzyme 10 Name UDP-glucuronosyltransferase 2B7
Enzyme 10 Synonyms
  1. UDPGT 2B7
  2. 3,4-catechol estrogen-specific UDPGT
  3. UDP-glucuronosyltransferase 2B9
  4. UDPGT 2B9
  5. UDPGTh-2
Enzyme 10 Gene Name UGT2B7
Enzyme 10 Protein Sequence >UDP-glucuronosyltransferase 2B7
MSVKWTSVILLIQLSFCFSSGNCGKVLVWAAEYSHWMNIKTILDELIQRGHEVTVLASSA
SILFDPNNSSALKIEIYPTSLTKTELENFIMQQIKRWSDLPKDTFWLYFSQVQEIMSIFG
DITRKFCKDVVSNKKFMKKVQESRFDVIFADAIFPCSELLAELFNIPFVYSLSFSPGYTF
EKHSGGFIFPPSYVPVVMSELTDQMTFMERVKNMIYVLYFDFWFEIFDMKKWDQFYSEVL
GRPTTLSETMGKADVWLIRNSWNFQFPHPLLPNVDFVGGLHCKPAKPLPKEMEDFVQSSG
ENGVVVFSLGSMVSNMTEERANVIASALAQIPQKVLWRFDGNKPDTLGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFADQPDNIAHMKARGAAVRVDFNTM
SSTDLLNALKRVINDPSYKENVMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAA
HDLTWFQYHSLDVIGFLLVCVATVIFIVTKCCLFCFWKFARKAKKGKND
Enzyme 10 Number of Residues 529
Enzyme 10 Molecular Weight 60694.1
Enzyme 10 Theoretical pI 8.45
Enzyme 10 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 10 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 10 Specific Function Its unique specificity for 3,4-catechol estrogens and estriol suggests it may play an important role in regulating the level and activity of these potent and active estrogen metabolites
Enzyme 10 Pathways
Enzyme 10 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-23
Enzyme 10 Transmembrane Regions
  • 493-509
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein Not Available
Enzyme 10 UniProtKB/Swiss-Prot ID P16662 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name UD2B7_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1590 bp
ATGTCTGTGAAATGGACTTCAGTAATTTTGCTAATACAACTGAGCTTTTGCTTTAGCTCT
GGGAATTGTGGAAAGGTGCTGGTGTGGGCAGCAGAATACAGCCATTGGATGAATATAAAG
ACAATCCTGGATGAGCTTATTCAGAGAGGTCATGAGGTGACTGTACTGGCATCTTCAGCT
TCCATTCTTTTTGATCCCAACAACTCATCCGCTCTTAAAATTGAAATTTATCCCACATCT
TTAACTAAAACTGAGTTGGAGAATTTCATCATGCAACAGATTAAGAGATGGTCAGACCTT
CCAAAAGATACATTTTGGTTATATTTTTCACAAGTACAGGAAATCATGTCAATATTTGGT
GACATAACTAGAAAGTTCTGTAAAGATGTAGTTTCAAATAAGAAATTTATGAAAAAAGTA
CAAGAGTCAAGATTTGACGTCATTTTTGCAGATGCTATTTTTCCCTGTAGTGAGCTGCTG
GCTGAGCTATTTAACATACCCTTTGTGTACAGTCTCAGCTTCTCTCCTGGCTACACTTTT
GAAAAGCATAGTGGAGGATTTATTTTCCCTCCTTCCTACGTACCTGTTGTTATGTCAGAA
TTAACTGATCAAATGACTTTCATGGAGAGGGTAAAAAATATGATCTATGTGCTTTACTTT
GACTTTTGGTTCGAAATATTTGACATGAAGAAGTGGGATCAGTTTTATAGTGAAGTTCTA
GGAAGACCCACTACGTTATCTGAGACAATGGGGAAAGCTGACGTATGGCTTATTCGAAAC
TCCTGGAATTTTCAGTTTCCTCATCCACTCTTACCAAATGTTGATTTTGTTGGAGGACTC
CACTGCAAACCTGCCAAACCCCTGCCTAAGGAAATGGAAGACTTTGTACAGAGCTCTGGA
GAAAATGGTGTTGTGGTGTTTTCTCTGGGGTCAATGGTCAGTAACATGACAGAAGAAAGG
GCCAACGTAATTGCATCAGCCCTGGCCCAGATCCCACAAAAGGTTCTGTGGAGATTTGAT
GGGAATAAACCAGATACCTTAGGTCTCAATACTCGGCTGTATAAGTGGATACCCCAGAAT
GACCTTCTAGGTCATCCAAAGACCAGAGCTTTTATAACTCATGGTGGAGCCAATGGCATC
TACGAGGCAATCTACCATGGGATCCCTATGGTGGGGATTCCATTGTTTGCCGATCAACCT
GATAACATTGCTCACATGAAGGCCAGGGGAGCAGCTGTTAGAGTGGACTTCAACACAATG
TCGAGTACAGACTTGCTGAATGCATTGAAGAGAGTAATTAATGATCCTTCATATAAAGAG
AATGTTATGAAATTATCAAGAATTCAACATGATCAACCAGTGAAGCCCCTGGATCGAGCA
GTCTTCTGGATTGAATTTGTCATGCGCCACAAAGGAGCTAAACACCTTCGGGTTGCAGCC
CACGACCTCACCTGGTTCCAGTACCACTCTTTGGATGTGATTGGGTTCCTGCTGGTCTGT
GTGGCAACTGTGATATTTATCGTCACAAAATGTTGTCTGTTTTGTTTCTGGAAGTTTGCT
AGAAAAGCAAAGAAGGGAAAAAATGATTAG
Enzyme 10 GenBank Gene ID J05428 Link Image
Enzyme 10 GeneCard ID UGT2B7 Link Image
Enzyme 10 GenAtlas ID UGT2B7 Link Image
Enzyme 10 HGNC ID HGNC:12554 Link Image
Enzyme 10 Chromosome Location 4
Enzyme 10 Locus 4q13
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. Ritter JK, Sheen YY, Owens IS: Cloning and expression of human liver UDP-glucuronosyltransferase in COS-1 cells. 3,4-catechol estrogens and estriol as primary substrates. J Biol Chem. 1990 May 15;265(14):7900-6. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  6. Bhasker CR, McKinnon W, Stone A, Lo AC, Kubota T, Ishizaki T, Miners JO: Genetic polymorphism of UDP-glucuronosyltransferase 2B7 (UGT2B7) at amino acid 268: ethnic diversity of alleles and potential clinical significance. Pharmacogenetics. 2000 Nov;10(8):679-85. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5722
Enzyme 11 Name UDP-glucuronosyltransferase 2B15
Enzyme 11 Synonyms
  1. UDPGT 2B15
  2. HLUG4
  3. UDP-glucuronosyltransferase 2B8
  4. UDPGT 2B8
  5. UDPGTh-3
Enzyme 11 Gene Name UGT2B15
Enzyme 11 Protein Sequence >UDP-glucuronosyltransferase 2B15
MSLKWTSVFLLIQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVTVLTSSA
STLVNASKSSAIKLEVYPTSLTKNDLEDSLLKILDRWIYGVSKNTFWSYFSQLQELCWEY
YDYSNKLCKDAVLNKKLMMKLQESKFDVILADALNPCGELLAELFNIPFLYSLRFSVGYT
FEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIHMLYFDFWFQIYDLKKWDQFYSEV
LGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSS
GENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQ
NDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRT
MSSRDLLNALKSVINDPVYKENVMKLSRIHHDQPMKPLDRAVFWIEFVMRHKGAKHLRVA
AHNLTWIQYHSLDVIAFLLACVATVIFIITKFCLFCFRKLAKKGKKKKRD
Enzyme 11 Number of Residues 530
Enzyme 11 Molecular Weight 60987.7
Enzyme 11 Theoretical pI 9.04
Enzyme 11 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 11 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 11 Specific Function UDPGTs are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme displays activity toward several classes of xenobiotic substrates, including simple phenolic compounds, 7-hydroxylated coumarins, flavonoids, anthraquinones, and certain drugs and their hydroxylated metabolites. It also catalyzes the glucuronidation of endogenous estrogens and androgens
Enzyme 11 Pathways
Enzyme 11 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-23
Enzyme 11 Transmembrane Regions
  • 495-515
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 116517299 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P54855 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name UDB15_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >1593 bp
ATGTCTCTGAAATGGACGTCAGTCTTTCTGCTGATACAGCTCAGTTGTTACTTTAGCTCT
GGAAGCTGTGGAAAGGTGCTAGTGTGGCCCACAGAATACAGCCATTGGATAAATATGAAG
ACAATCCTGGAAGAGCTTGTTCAGAGGGGTCATGAGGTGACTGTGTTGACATCTTCGGCT
TCTACTCTTGTCAATGCCAGTAAATCATCTGCTATTAAATTAGAAGTTTATCCTACATCT
TTAACTAAAAATTATTTGGAAGATTCTCTTCTGAAAATTCTCGATAGATGGATATATGGT
GTTTCAAAAAATACATTTTGGTCATATTTTTCACAATTACAAGAATTGTGTTGGGAATAT
TATGACTACAGTAACAAGCTCTGTAAAGATGCAGTTTTGAATAAGAAACTTATGATGAAA
CTACAAGAGTCAAAGTTTGATGTCATTCTGGCAGATGCCCTTAATCCCTGTGGTGAGCTA
CTGGCTGAACTATTTAACATACCCTTTCTGTACAGTCTTCGATTCTCTGTTGGCTACACA
TTTGAGAAGAATGGTGGAGGATTTCTGTTCCCTCCTTCCTATGTACCTGTTGTTATGTCA
GAATTAAGTGATCAAATGATTTTCATGGAGAGGATAAAAAATATGATACATATGCTTTAT
TTTGACTTTTGGTTTCAAATTTATGATCTGAAGAAGTGGGACCAGTTTTATAGTGAAGTT
CTAGGAAGACCCACTACATTATTTGAGACAATGGGGAAAGCTGAAATGTGGCTCATTCGA
ACCTATTGGGATTTTGAATTTCCTCGCCCATTCTTACCAAATGTTGATTTTGTTGGAGGA
CTTCACTGTAAACCAGCCAAACCCCTGCCTAAGGAAATGGAAGAGTTTGTGCAGAGCTCT
GGAGAAAATGGTATTGTGGTGTTTTCTCTGGGGTCGATGATCAGTAACATGTCAGAAGAA
AGTGCCAACATGATTGCATCAGCCCTTGCCCAGATCCCACAAAAGGTTCTATGGAGATTT
GATGGCAAGAAGCCAAATACTTTAGGTTCCAATACTCGACTGTACAAGTGGTTACCCCAG
AATGACCTTCTTGGTCATCCCAAAACCAAAGCTTTTATAACTCATGGTGGAACCAATGGC
ATCTATGAGGCGATCTACCATGGGATCCCTATGGTGGGCATTCCCTTGTTTGCGGATCAA
CATGATAACATTGCTCACATGAAAGCCAAGGGAGCAGCCCTCAGTGTGGACATCAGGACC
ATGTCAAGTAGAGATTTGCTCAATGCATTGAAGTCAGTCATTAATGACCCTGTCTATAAA
GAGAATGTCATGAAATTATCAAGAATTCATCATGACCAACCAATGAAGCCCCTGGATCGA
GCAGTCTTCTGGATTGAGTTTGTCATGCGCCACAAAGGAGCCAAGCACCTTCGAGTCGCA
GCTCACAACCTCACCTGGATCCAGTACCACTCTTTGGATGTGATAGCATTCCTGCTGGCC
TGCGTGGCAACTGTGATATTTATCATCACAAAATTTTGCCTGTTTTGTTTCCGAAAGCTT
GCCAAAAAAGGAAAGAAGAAGAAAAGAGATTAG
Enzyme 11 GenBank Gene ID NM_001076.2 Link Image
Enzyme 11 GeneCard ID UGT2B15 Link Image
Enzyme 11 GenAtlas ID UGT2B15 Link Image
Enzyme 11 HGNC ID HGNC:12546 Link Image
Enzyme 11 Chromosome Location 4
Enzyme 11 Locus 4q13
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Chen F, Ritter JK, Wang MG, McBride OW, Lubet RA, Owens IS: Characterization of a cloned human dihydrotestosterone/androstanediol UDP-glucuronosyltransferase and its comparison to other steroid isoforms. Biochemistry. 1993 Oct 12;32(40):10648-57. [PubMed Link Image]
  2. Green MD, Oturu EM, Tephly TR: Stable expression of a human liver UDP-glucuronosyltransferase (UGT2B15) with activity toward steroid and xenobiotic substrates. Drug Metab Dispos. 1994 Sep-Oct;22(5):799-805. [PubMed Link Image]
  3. Levesque E, Beaulieu M, Green MD, Tephly TR, Belanger A, Hum DW: Isolation and characterization of UGT2B15(Y85): a UDP-glucuronosyltransferase encoded by a polymorphic gene. Pharmacogenetics. 1997 Aug;7(4):317-25. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Coffman BL, Tephly TR, Irshaid YM, Green MD, Smith C, Jackson MR, Wooster R, Burchell B: Characterization and primary sequence of a human hepatic microsomal estriol UDPglucuronosyltransferase. Arch Biochem Biophys. 1990 Aug 15;281(1):170-5. [PubMed Link Image]
  6. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  7. Toide K, Umeda S, Yamazaki H, Takahashi Y, Terauchi Y, Fujii T, Kamataki T: A major genotype in UDP-glucuronosyltransferase 2B15. Drug Metab Pharmacokinet. 2002;17(2):164-6. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5724
Enzyme 12 Name UDP-glucuronosyltransferase 2A1
Enzyme 12 Synonyms
  1. UDPGT 2A1
Enzyme 12 Gene Name UGT2A1
Enzyme 12 Protein Sequence >UDP-glucuronosyltransferase 2A1
MLNNLLLFSLQISLIGTTLGGNVLIWPMEGSHWLNVKIIIDELIKKEHNVTVLVASGALF
ITPTSNPSLTFEIYRVPFGKERIEGVIKDFVLTWLENRPSPSTIWRFYQEMAKVIKDFHM
VSQEICDGVLKNQQLMAKLKKSKFEVLVSDPVFPCGDIVALKLGIPFMYSLRFSPASTVE
KHCGKVPYPPSYVPAVLSELTDQMSFTDRIRNFISYHLQDYMFETLWKSWDSYYSKALGR
PTTLCETMGKAEIWLIRTYWDFEFPRPYLPNFEFVGGLHCKPAKPLPKEMEEFIQSSGKN
GVVVFSLGSMVKNLTEEKANLIASALAQIPQKVLWRYKGKKPATLGNNTQLFDWIPQNDL
LGHPKTKAFITHGGTNGIYEAIYHGVPMVGVPMFADQPDNIAHMKAKGAAVEVNLNTMTS
VDLLSALRTVINEPSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHD
LTWFQYHSLDVIGFLLVCVTTAIFLVIQCCLFSCQKFGKIGKKKKRE
Enzyme 12 Number of Residues 527
Enzyme 12 Molecular Weight 59925.7
Enzyme 12 Theoretical pI 9.29
Enzyme 12 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 12 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 12 Specific Function UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. Active on odorants and seems to be involved in olfaction; it could help clear lipophilic odorant molecules from the sensory epithelium
Enzyme 12 Pathways
Enzyme 12 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-20
Enzyme 12 Transmembrane Regions
  • 491-507
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 110611919 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q9Y4X1 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name UD2A1_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1584 bp
ATGTTAAACAACCTTCTGCTGTTCTCCCTTCAGATAAGTCTCATAGGAACCACTCTTGGT
GGGAATGTTTTGATTTGGCCAATGGAAGGTAGTCATTGGCTAAATGTTAAGATAATTATA
GATGAGCTCATTAAAAAGGAGCATAATGTGACTGTCCTAGTTGCCTCTGGTGCACTTTTC
ATCACACCAACCTCTAACCCATCTCTGACATTTGAAATATATAGGGTGCCCTTTGGCAAA
GAAAGAATAGAAGGAGTAATTAAGGACTTCGTTTTGACATGGCTGGAAAATAGACCATCT
CCTTCAACCATTTGGAGATTCTATCAGGAGATGGCCAAAGTAATCAAGGACTTCCACATG
GTGTCTCAGGAGATCTGTGATGGCGTTCTTAAAAACCAACAGCTGATGGCAAAGCTAAAG
AAAAGCAAGTTTGAAGTCCTGGTGTCTGATCCAGTATTTCCTTGTGGCGATATAGTAGCT
TTAAAACTTGGAATTCCATTTATGTACTCCTTGAGGTTTTCTCCAGCCTCAACAGTGGAA
AAGCACTGTGGGAAGGTACCATACCCTCCTTCCTATGTTCCTGCTGTTTTATCAGAACTC
ACCGACCAAATGTCTTTCACTGACAGAATAAGAAATTTCATCTCCTACCACCTACAGGAC
TACATGTTTGAAACTCTTTGGAAATCATGGGATTCATACTATAGTAAAGCTTTAGGAAGA
CCCACTACGTTATGTGAGACTATGGGGAAAGCTGAAATTTGGTTAATCCGAACATATTGG
GATTTTGAATTTCCTCGTCCATACTTACCTAATTTTGAGTTTGTTGGAGGATTGCACTGC
AAACCTGCCAAACCTTTACCTAAGGAAATGGAAGAATTTATCCAGAGCTCAGGTAAAAAT
GGTGTTGTGGTGTTTTCTCTGGGATCAATGGTCAAAAACCTTACAGAAGAAAAGGCCAAT
CTTATTGCCTCAGCCCTTGCCCAGATTCCACAGAAGGTTTTATGGAGATACAAAGGAAAG
AAACCAGCCACATTAGGAAACAATACTCAGCTCTTTGATTGGATACCCCAGAATGATCTT
CTTGGACATCCCAAAACCAAAGCTTTTATCACTCATGGTGGAACTAATGGGATCTACGAA
GCTATTTACCACGGAGTCCCTATGGTGGGAGTTCCCATGTTTGCTGATCAGCCTGATAAC
ATTGCTCACATGAAGGCCAAAGGAGCAGCTGTGGAAGTGAACCTAAACACAATGACAAGT
GTGGATTTGCTTAGCGCTTTGAGAACAGTCATTAATGAACCTTCTTATAAAGAGAATGCT
ATGAGGTTATCAAGAATTCACCATGATCAACCTGTAAAGCCCCTGGATCGAGCAGTCTTC
TGGATCGAGTTTGTCATGCGCCACAAAGGAGCCAAGCACCTTCGGGTTGCAGCCCATGAC
CTCACCTGGTTCCAGTACCACTCTTTGGATGTAATTGGGTTCTTGCTGGTCTGTGTGACA
ACGGCTATATTTTTGGTCATACAATGTTGTTTGTTTTCCTGTCAAAAATTTGGTAAGATA
GGAAAGAAGAAAAAAAGAGAATAG
Enzyme 12 GenBank Gene ID NM_006798.2 Link Image
Enzyme 12 GeneCard ID UGT2A1 Link Image
Enzyme 12 GenAtlas ID UGT2A1 Link Image
Enzyme 12 HGNC ID HGNC:12542 Link Image
Enzyme 12 Chromosome Location 4
Enzyme 12 Locus 4q13
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Jedlitschky G, Cassidy AJ, Sales M, Pratt N, Burchell B: Cloning and characterization of a novel human olfactory UDP-glucuronosyltransferase. Biochem J. 1999 Jun 15;340 ( Pt 3):837-43. [PubMed Link Image]
  2. Sneitz N, Court MH, Zhang X, Laajanen K, Yee KK, Dalton P, Ding X, Finel M: Human UDP-glucuronosyltransferase UGT2A2: cDNA construction, expression, and functional characterization in comparison with UGT2A1 and UGT2A3. Pharmacogenet Genomics. 2009 Oct 24. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5725
Enzyme 13 Name UDP-glucuronosyltransferase 1-1
Enzyme 13 Synonyms
  1. UDPGT 1-1
  2. UGT1*1
  3. UGT1-01
  4. UGT1.1
  5. Bilirubin-specific UDPGT isozyme 1
  6. hUG-BR1
  7. UDP-glucuronosyltransferase 1-A
  8. UGT-1A
  9. UGT1A
  10. UDP-glucuronosyltransferase 1A1
Enzyme 13 Gene Name UGT1A1
Enzyme 13 Protein Sequence >UDP-glucuronosyltransferase 1-1
MAVESQGGRPLVLGLLLCVLGPVVSHAGKILLIPVDGSHWLSMLGAIQQLQQRGHEIVVL
APDASLYIRDGAFYTLKTYPVPFQREDVKESFVSLGHNVFENDSFLQRVIKTYKKIKKDS
AMLLSGCSHLLHNKELMASLAESSFDVMLTDPFLPCSPIVAQYLSLPTVFFLHALPCSLE
FEATQCPNPFSYVPRPLSSHSDHMTFLQRVKNMLIAFSQNFLCDVVYSPYATLASEFLQR
EVTVQDLLSSASVWLFRSDFVKDYPRPIMPNMVFVGGINCLHQNPLSQEFEAYINASGEH
GIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDL
LGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTS
EDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHD
LTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 13 Number of Residues 533
Enzyme 13 Molecular Weight 59590.9
Enzyme 13 Theoretical pI 8.09
Enzyme 13 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 13 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 13 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform glucuronidates bilirubin IX- alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate
Enzyme 13 Pathways
Enzyme 13 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • 1-25
Enzyme 13 Transmembrane Regions
  • 491-507
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein Not Available
Enzyme 13 UniProtKB/Swiss-Prot ID P22309 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name UD11_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1602 bp
ATGGCTGTGGAGTCCCAGGGCGGACGCCCACTTGTCCTGGGCCTGCTGCTGTGTGTGCTG
GGCCCAGTGGTGTCCCATGCTGGGAAGATACTGTTGATCCCAGTGGATGGCAGCCACTGG
CTGAGCATGCTTGGGGCCATCCAGCAGCTGCAGCAGAGGGGACATGAAATAGTTGTCCTA
GCACCTGACGCCTCGTTGTACATCAGAGACGGAGCATTTTACACCTTGAAGACGTACCCT
GTGCCATTCCAAAGGGAGGATGTGAAAGAGTCTTTTGTTAGTCTCGGGCATAATGTTTTT
GAGAATGATTCTTTCCTGCAGCGTGTGATCAAAACATACAAGAAAATAAAAAAGGACTCT
GCTATGCTTTTGTCTGGCTGTTCCCACTTACTGCACAACAAGGAGCTCATGGCCTCCCTG
GCAGAAAGCAGCTTTGATGTCATGCTGACGGACCCTTTCCTTCCTTGCAGCCCCATCGTG
GCCCAGTACCTGTCTCTGCCCACTGTATTCTTCTTGCATGCACTGCCATGCAGCCTGGAA
TTTGAGGCTACCCAGTGCCCCAACCCATTCTCCTACGTGCCCAGGCCTCTCTCCTCTCAT
TCAGATCACATGACCTTCCTGCAGCGGGTGAAGAACATGCTCATTGCCTTTTCACAGAAC
TTTCTGTGCGACGTGGTTTATTCCCCGTATGCAACCCTTGCCTCAGAATTCCTTCAGAGA
GAGGTGACTGTCCAGGACCTATTGAGCTCTGCATCTGTCTGGCTGTTTAGAAGTGACTTT
GTGAAGGATTACCCTAGGCCCATCATGCCCAATATGGTTTTTGTTGGTGGAATCAACTGC
CTTCACCAAAATCCACTATCCCAGGAATTTGAAGCCTACATTAATGCTTCTGGAGAACAT
GGAATTGTGGTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCTATG
GCAATTGCTGATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGAACC
CGACCATCGAATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGATCTG
CTTGGTCACCCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTATGAA
AGCATATGCAATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGACAAT
GCAAAGCGCATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACTTCT
GAAGATTTAGAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAACATC
ATGCGCCTCTCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTGTTC
TGGGTGGAGTTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCACGAC
CTCACCTGGTACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTGCTG
ACAGTGGCCTTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGGAAA
AAAGGGCGAGTTAAGAAAGCCCACAAATCCAAGACCCATTGA
Enzyme 13 GenBank Gene ID M57899 Link Image
Enzyme 13 GeneCard ID UGT1A1 Link Image
Enzyme 13 GenAtlas ID UGT1A1 Link Image
Enzyme 13 HGNC ID HGNC:12530 Link Image
Enzyme 13 Chromosome Location 2
Enzyme 13 Locus 2q37
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Ritter JK, Crawford JM, Owens IS: Cloning of two human liver bilirubin UDP-glucuronosyltransferase cDNAs with expression in COS-1 cells. J Biol Chem. 1991 Jan 15;266(2):1043-7. [PubMed Link Image]
  2. Ritter JK, Chen F, Sheen YY, Tran HM, Kimura S, Yeatman MT, Owens IS: A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini. J Biol Chem. 1992 Feb 15;267(5):3257-61. [PubMed Link Image]
  3. Gong QH, Cho JW, Huang T, Potter C, Gholami N, Basu NK, Kubota S, Carvalho S, Pennington MW, Owens IS, Popescu NC: Thirteen UDPglucuronosyltransferase genes are encoded at the human UGT1 gene complex locus. Pharmacogenetics. 2001 Jun;11(4):357-68. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Meunier L, Usherwood YK, Chung KT, Hendershot LM: A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol Biol Cell. 2002 Dec;13(12):4456-69. [PubMed Link Image]
  6. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  7. Bosma PJ, Chowdhury JR, Huang TJ, Lahiri P, Elferink RP, Van Es HH, Lederstein M, Whitington PF, Jansen PL, Chowdhury NR: Mechanisms of inherited deficiencies of multiple UDP-glucuronosyltransferase isoforms in two patients with Crigler-Najjar syndrome, type I. FASEB J. 1992 Jul;6(10):2859-63. [PubMed Link Image]
  8. Aono S, Yamada Y, Keino H, Hanada N, Nakagawa T, Sasaoka Y, Yazawa T, Sato H, Koiwai O: Identification of defect in the genes for bilirubin UDP-glucuronosyl-transferase in a patient with Crigler-Najjar syndrome type II. Biochem Biophys Res Commun. 1993 Dec 30;197(3):1239-44. [PubMed Link Image]
  9. Moghrabi N, Clarke DJ, Boxer M, Burchell B: Identification of an A-to-G missense mutation in exon 2 of the UGT1 gene complex that causes Crigler-Najjar syndrome type 2. Genomics. 1993 Oct;18(1):171-3. [PubMed Link Image]
  10. Ritter JK, Yeatman MT, Kaiser C, Gridelli B, Owens IS: A phenylalanine codon deletion at the UGT1 gene complex locus of a Crigler-Najjar type I patient generates a pH-sensitive bilirubin UDP-glucuronosyltransferase. J Biol Chem. 1993 Nov 5;268(31):23573-9. [PubMed Link Image]
  11. Labrune P, Myara A, Hadchouel M, Ronchi F, Bernard O, Trivin F, Chowdhury NR, Chowdhury JR, Munnich A, Odievre M: Genetic heterogeneity of Crigler-Najjar syndrome type I: a study of 14 cases. Hum Genet. 1994 Dec;94(6):693-7. [PubMed Link Image]
  12. Erps LT, Ritter JK, Hersh JH, Blossom D, Martin NC, Owens IS: Identification of two single base substitutions in the UGT1 gene locus which abolish bilirubin uridine diphosphate glucuronosyltransferase activity in vitro. J Clin Invest. 1994 Feb;93(2):564-70. [PubMed Link Image]
  13. Seppen J, Bosma PJ, Goldhoorn BG, Bakker CT, Chowdhury JR, Chowdhury NR, Jansen PL, Oude Elferink RP: Discrimination between Crigler-Najjar type I and II by expression of mutant bilirubin uridine diphosphate-glucuronosyltransferase. J Clin Invest. 1994 Dec;94(6):2385-91. [PubMed Link Image]
  14. Aono S, Adachi Y, Uyama E, Yamada Y, Keino H, Nanno T, Koiwai O, Sato H: Analysis of genes for bilirubin UDP-glucuronosyltransferase in Gilbert's syndrome. Lancet. 1995 Apr 15;345(8955):958-9. [PubMed Link Image]
  15. Seppen J, Steenken E, Lindhout D, Bosma PJ, Elferink RP: A mutation which disrupts the hydrophobic core of the signal peptide of bilirubin UDP-glucuronosyltransferase, an endoplasmic reticulum membrane protein, causes Crigler-Najjar type II. FEBS Lett. 1996 Jul 29;390(3):294-8. [PubMed Link Image]
  16. Ciotti M, Chen F, Rubaltelli FF, Owens IS: Coding defect and a TATA box mutation at the bilirubin UDP-glucuronosyltransferase gene cause Crigler-Najjar type I disease. Biochim Biophys Acta. 1998 Jul 1;1407(1):40-50. [PubMed Link Image]
  17. Yamamoto K, Soeda Y, Kamisako T, Hosaka H, Fukano M, Sato H, Fujiyama Y, Adachi Y, Satoh Y, Bamba T: Analysis of bilirubin uridine 5'-diphosphate (UDP)-glucuronosyltransferase gene mutations in seven patients with Crigler-Najjar syndrome type II. J Hum Genet. 1998;43(2):111-4. [PubMed Link Image]
  18. Maruo Y, Sato H, Yamano T, Doida Y, Shimada M: Gilbert syndrome caused by a homozygous missense mutation (Tyr486Asp) of bilirubin UDP-glucuronosyltransferase gene. J Pediatr. 1998 Jun;132(6):1045-7. [PubMed Link Image]
  19. Kadakol A, Ghosh SS, Sappal BS, Sharma G, Chowdhury JR, Chowdhury NR: Genetic lesions of bilirubin uridine-diphosphoglucuronate glucuronosyltransferase (UGT1A1) causing Crigler-Najjar and Gilbert syndromes: correlation of genotype to phenotype. Hum Mutat. 2000 Oct;16(4):297-306. [PubMed Link Image]
  20. Maruo Y, Nishizawa K, Sato H, Sawa H, Shimada M: Prolonged unconjugated hyperbilirubinemia associated with breast milk and mutations of the bilirubin uridine diphosphate- glucuronosyltransferase gene. Pediatrics. 2000 Nov;106(5):E59. [PubMed Link Image]
  21. Kadakol A, Sappal BS, Ghosh SS, Lowenheim M, Chowdhury A, Chowdhury S, Santra A, Arias IM, Chowdhury JR, Chowdhury NR: Interaction of coding region mutations and the Gilbert-type promoter abnormality of the UGT1A1 gene causes moderate degrees of unconjugated hyperbilirubinaemia and may lead to neonatal kernicterus. J Med Genet. 2001 Apr;38(4):244-9. [PubMed Link Image]
  22. Labrune P, Myara A, Chalas J, Le Bihan B, Capel L, Francoual J: Association of a homozygous (TA)8 promoter polymorphism and a N400D mutation of UGT1A1 in a child with Crigler-Najjar type II syndrome. Hum Mutat. 2002 Nov;20(5):399-401. [PubMed Link Image]
  23. Sutomo R, Laosombat V, Sadewa AH, Yokoyama N, Nakamura H, Matsuo M, Nishio H: Novel missense mutation of the UGT1A1 gene in Thai siblings with Gilbert's syndrome. Pediatr Int. 2002 Aug;44(4):427-32. [PubMed Link Image]
  24. Ohnishi A, Emi Y: Rapid proteasomal degradation of translocation-deficient UDP-glucuronosyltransferase 1A1 proteins in patients with Crigler-Najjar type II. Biochem Biophys Res Commun. 2003 Oct 24;310(3):735-41. [PubMed Link Image]
  25. Servedio V, d'Apolito M, Maiorano N, Minuti B, Torricelli F, Ronchi F, Zancan L, Perrotta S, Vajro P, Boschetto L, Iolascon A: Spectrum of UGT1A1 mutations in Crigler-Najjar (CN) syndrome patients: identification of twelve novel alleles and genotype-phenotype correlation. Hum Mutat. 2005 Mar;25(3):325. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5726
Enzyme 14 Name UDP-glucuronosyltransferase 1-9
Enzyme 14 Synonyms
  1. UDPGT 1-9
  2. UGT1*9
  3. UGT1-09
  4. UGT1.9
  5. UDP-glucuronosyltransferase 1-I
  6. UGT-1I
  7. UGT1I
  8. UDP-glucuronosyltransferase 1A9
  9. lugP4
Enzyme 14 Gene Name UGT1A9
Enzyme 14 Protein Sequence >UDP-glucuronosyltransferase 1-9
MACTGWTSPLPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMRSVVEKLILRGHEVVVVMP
EVSWQLGRSLNCTVKTYSTSYTLEDLDREFKAFAHAQWKAQVRSIYSLLMGSYNDIFDLF
FSNCRSLFKDKKLVEYLKESSFDAVFLDPFDNCGLIVAKYFSLPSVVFARGILCHYLEEG
AQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLLCHRFFKNALEIASEILQTPVT
EYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 14 Number of Residues 530
Enzyme 14 Molecular Weight 59940.5
Enzyme 14 Theoretical pI 7.96
Enzyme 14 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 14 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 14 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform has specificity for phenols
Enzyme 14 Pathways
Enzyme 14 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-25
Enzyme 14 Transmembrane Regions
  • 488-504
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 3025896 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID O60656 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name UD19_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1593 bp
ATGGCTTGCACAGGGTGGACCAGCCCCCTTCCTCTATGTGTGTGTCTGCTGCTGACCTGT
GGCTTTGCCGAGGCAGGGAAGCTACTGGTAGTGCCCATGGATGGGAGCCACTGGTTCACC
ATGAGGTCGGTGGTGGAGAAACTCATTCTCAGGGGGCATGAGGTGGTTGTAGTCATGCCA
GAGGTGAGTTGGCAACTGGGAAGATCACTGAATTGCACAGTGAAGACTTATTCAACTTCA
TATACCCTGGAGGATCTGGACCGGGAGTTCAAGGCTTTTGCCCATGCTCAATGGAAAGCA
CAAGTACGAAGTATATATTCTCTATTAATGGGTTCATACAATGACATTTTTGACTTATTT
TTTTCAAATTGCAGGAGTTTGTTTAAAGACAAAAAATTAGTAGAATACTTAAAGGAGAGT
TCTTTTGATGCAGTGTTTCTCGATCCTTTTGATAACTGTGGCTTAATTGTTGCCAAATAT
TTCTCCCTCCCCTCCGTGGTCTTCGCCAGGGGAATACTTTGCCACTATCTTGAAGAAGGT
GCACAGTGCCCTGCTCCTCTTTCCTATGTCCCCAGAATTCTCTTAGGGTTCTCAGATGCC
ATGACTTTCAAGGAGAGAGTACGGAACCACATCATGCACTTGGAGGAACATTTATTATGC
CACCGTTTTTTCAAAAATGCCCTAGAAATAGCCTCTGAAATTCTCCAAACACCTGTTACG
GAGTATGATCTCTACAGCCACACATCAATTTGGTTGTTGCGAACGGACTTTGTTTTGGAC
TATCCCAAACCCGTGATGCCCAACATGATCTTCATTGGTGGTATCAACTGCCATCAGGGA
AAGCCGTTGCCTATGGAATTTGAAGCCTACATTAATGCTTCTGGAGAACATGGAATTGTG
GTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCTATGGCAATTGCT
GATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGAACCCGACCATCG
AATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGATCTGCTTGGTCAC
CCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTATGAAAGCATATGC
AATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGACAATGCAAAGCGC
ATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACTTCTGAAGATTTA
GAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAACATCATGCGCCTC
TCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTGTTCTGGGTGGAG
TTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCACGACCTCACCTGG
TACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTGCTGACAGTGGCC
TTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGGAAAAAAGGGCGA
GTTAAGAAAGCCCACAAATCCAAGACCCATTGA
Enzyme 14 GenBank Gene ID AF056188 Link Image
Enzyme 14 GeneCard ID UGT1A9 Link Image
Enzyme 14 GenAtlas ID UGT1A9 Link Image
Enzyme 14 HGNC ID HGNC:12541 Link Image
Enzyme 14 Chromosome Location 2
Enzyme 14 Locus 2q37
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Wooster R, Sutherland L, Ebner T, Clarke D, Da Cruz e Silva O, Burchell B: Cloning and stable expression of a new member of the human liver phenol/bilirubin: UDP-glucuronosyltransferase cDNA family. Biochem J. 1991 Sep 1;278 ( Pt 2):465-9. [PubMed Link Image]
  2. Gong QH, Cho JW, Huang T, Potter C, Gholami N, Basu NK, Kubota S, Carvalho S, Pennington MW, Owens IS, Popescu NC: Thirteen UDPglucuronosyltransferase genes are encoded at the human UGT1 gene complex locus. Pharmacogenetics. 2001 Jun;11(4):357-68. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
  5. Menard V, Girard H, Harvey M, Perusse L, Guillemette C: Analysis of inherited genetic variations at the UGT1 locus in the French-Canadian population. Hum Mutat. 2009 Apr;30(4):677-87. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5728
Enzyme 15 Name UDP-glucuronosyltransferase 1-3
Enzyme 15 Synonyms
  1. UDPGT 1-3
  2. UGT1*3
  3. UGT1-03
  4. UGT1.3
  5. UDP-glucuronosyltransferase 1-C
  6. UGT-1C
  7. UGT1C
  8. UDP-glucuronosyltransferase 1A3
Enzyme 15 Gene Name UGT1A3
Enzyme 15 Protein Sequence >UDP-glucuronosyltransferase 1-3
MATGLQVPLPWLATGLLLLLSVQPWAESGKVLVVPIDGSHWLSMREVLRELHARGHQAVV
LTPEVNMHIKEENFFTLTTYAISWTQDEFDRHVLGHTQLYFETEHFLKKFFRSMAMLNNM
SLVYHRSCVELLHNEALIRHLNATSFDVVLTDPVNLCAAVLAKYLSIPTVFFLRNIPCDL
DFKGTQCPNPSSYIPRLLTTNSDHMTFMQRVKNMLYPLALSYICHAFSAPYASLASELFQ
REVSVVDILSHASVWLFRGDFVMDYPRPIMPNMVFIGGINCANRKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 15 Number of Residues 534
Enzyme 15 Molecular Weight 60337.8
Enzyme 15 Theoretical pI 8.28
Enzyme 15 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 15 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 15 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds
Enzyme 15 Pathways
Enzyme 15 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-28
Enzyme 15 Transmembrane Regions
  • 492-508
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 11118746 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P35503 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name UD13_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1605 bp
ATGGCCACAGGACTCCAGGTTCCCCTGCCGCAGCTGGCCACAGGACTGCTGCTTCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGGAAGGTGCTGGTGGTGCCCACTGATGGCAGCCAC
TGGCTCAGCATGCGGGAGGCCTTGCGGGACCTCCATGCGAGAGGCCACCAGGTGGTGGTC
CTCACCCTGGAGGTGAATATGTACATCAAAGAAGAGAACTTTTTCACCCTGACAACGTAT
GCCATTTCATGGACCCAGGACGAATTTGATCGCCTTTTGCTGGGTCACACTCAATCGTTC
TTTGAAACAGAACATCTTCTGATGAAATTTTCTAGAAGAATGGCAATTATGAACAATATG
TCTTTGATCATACATAGGTCTTGTGTGGAGCTACTGCATAATGAGGCCCTGATCAGGCAC
CTGCATGCTACTTCCTTTGATGTGGTTCTAACAGACCCCTTTCACCTCTGCGCGGCGGTG
CTGGCTAAGTACCTGTCGATTCCTGCTGTGTTTTTCTTGAGGAACATTCCATGTGATTTA
GACTTTAAGGGCACACAGTGTCCAAACCCTTCCTCCTATATTCCTAGATTACTAACGACC
AATTCAGACCACATGACATTCCTGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACCTTTGCCATGCTGTTTCTGCTCCTTATGCAAGCCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATCTTGTCAGCCATGCATCTGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGATTACCCCAGGCCGATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACGGGAAGCCACTATCTCAGGAATTTGAAGCCTACATTAATGCTTCTGGAGAA
CATGGAATTGTGGTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCT
ATGGCAATTGCTGATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGA
ACCCGACCATCGAATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGAT
CTGCTTGGTCACCCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTAT
GAAAGCATATGCAATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGAC
AATGCAAAGCGCATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACT
TCTGAAGATTTAGAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAAC
ATCATGCGCCTCTCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTG
TTCTGGGTGGAGTTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCAC
GACCTCACCTGGTACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTG
CTGACAGTGGCCTTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGG
AAAAAAGGGCGAGTTAAGAAAGCCCACAAATCCAAGACCCATTGA
Enzyme 15 GenBank Gene ID AF297093 Link Image
Enzyme 15 GeneCard ID UGT1A3 Link Image
Enzyme 15 GenAtlas ID UGT1A3 Link Image
Enzyme 15 HGNC ID HGNC:12535 Link Image
Enzyme 15 Chromosome Location 2
Enzyme 15 Locus 2q37
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Ritter JK, Chen F, Sheen YY, Tran HM, Kimura S, Yeatman MT, Owens IS: A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini. J Biol Chem. 1992 Feb 15;267(5):3257-61. [PubMed Link Image]
  2. Gong QH, Cho JW, Huang T, Potter C, Gholami N, Basu NK, Kubota S, Carvalho S, Pennington MW, Owens IS, Popescu NC: Thirteen UDPglucuronosyltransferase genes are encoded at the human UGT1 gene complex locus. Pharmacogenetics. 2001 Jun;11(4):357-68. [PubMed Link Image]
  3. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  4. Menard V, Girard H, Harvey M, Perusse L, Guillemette C: Analysis of inherited genetic variations at the UGT1 locus in the French-Canadian population. Hum Mutat. 2009 Apr;30(4):677-87. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5731
Enzyme 16 Name UDP-glucuronosyltransferase 2B17
Enzyme 16 Synonyms
  1. UDPGT 2B17
  2. C19-steroid-specific UDP-glucuronosyltransferase
  3. C19-steroid-specific UDPGT
Enzyme 16 Gene Name UGT2B17
Enzyme 16 Protein Sequence >UDP-glucuronosyltransferase 2B17
MSLKWMSVFLLMQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVIVLTSSA
SILVNASKSSAIKLEVYPTSLTKNDLEDFFMKMFDRWTYSISKNTFWSYFSQLQELCWEY
SDYNIKLCEDAVLNKKLMRKLQESKFDVLLADAVNPCGELLAELLNIPFLYSLRFSVGYT
VEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIYMLYFDFWFQAYDLKKWDQFYSEV
LGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSS
GENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQ
NDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRT
MSSRDLLNALKSVINDPIYKENIMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVA
AHNLTWIQYHSLDVIAFLLACVATMIFMITKCCLFCFRKLAKTGKKKKRD
Enzyme 16 Number of Residues 530
Enzyme 16 Molecular Weight 61094.9
Enzyme 16 Theoretical pI 8.73
Enzyme 16 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 16 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 16 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. The major substrates of this isozyme are eugenol > 4-methylumbelliferone > dihydrotestosterone (DHT) > androstane-3-alpha,17-beta-diol (3-alpha-diol) > testosterone > androsterone (ADT)
Enzyme 16 Pathways
Enzyme 16 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-23
Enzyme 16 Transmembrane Regions
  • 495-515
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein Not Available
Enzyme 16 UniProtKB/Swiss-Prot ID O75795 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name UDB17_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1593 bp
ATGTCTCTGAAATGGATGTCAGTCTTTCTGCTGATGCAGCTCAGTTGTTACTTTAGCTCT
GGGAGTTGTGGAAAGGTGCTGGTGTGGCCCACAGAATACAGCCATTGGATAAATATGAAG
ACAATCCTGGAAGAGCTTGTTCAGAGGGGTCATGAGGTGATTGTGTTGACATCTTCGGCT
TCTATTCTTGTCAATGCCAGTAAATCATCTGCTATTAAATTAGAAGTTTATCCTACATCT
TTAACTAAAAATGATTTGGAAGATTTTTTTATGAAAATGTTCGATAGATGGACATATAGT
ATTTCAAAAAATACATTTTGGTCATATTTTTCACAACTACAAGAATTGTGTTGGGAATAT
TCTGACTATAATATAAAGCTCTGTGAAGATGCAGTTTTGAACAAGAAACTTATGAGAAAA
CTACAAGAGTCAAAATTTGATGTCCTTCTGGCAGATGCCGTTAATCCCTGTGGTGAGCTG
CTGGCTGAACTACTTAACATACCCTTTCTGTACAGTCTCCGCTTCTCTGTTGGCTACACA
GTTGAGAAGAATGGTGGAGGATTTCTGTTCCCTCCTTCCTATGTACCTGTTGTTATGTCA
GAATTAAGTGATCAAATGATTTTCATGGAGAGGATAAAAAATATGATATATATGCTTTAT
TTTGACTTTTGGTTTCAAGCATATGATCTGAAGAAGTGGGACCAGTTTTATAGTGAAGTT
CTAGGAAGACCCACTACATTATTTGAGACAATGGGGAAAGCTGAAATGTGGCTCATTCGA
ACCTATTGGGATTTTGAATTTCCTCGCCCATTCTTACCAAATGTTGATTTTGTTGGAGGA
CTTCACTGTAAACCAGCCAAACCCTTGCCTAAGGAAATGGAAGAGTTTGTGCAGAGCTCT
GGAGAAAATGGTATTGTGGTGTTTTCTCTGGGGTCGATGATCAGTAACATGTCAGAAGAA
AGTGCCAACATGATTGCATCAGCCCTTGCCCAGATCCCACAAAAGGTTCTATGGAGATTT
GATGGCAAGAAGCCAAATACTTTAGGTTCCAATACTCGACTGTATAAGTGGTTACCCCAG
AATGACCTTCTTGGTCATCCCAAAACCAAAGCTTTTATAACTCATGGTGGAACCAATGGC
ATCTATGAGGCGATCTACCATGGGATCCCTATGGTGGGCATTCCCTTGTTTGCGGATCAA
CATGATAACATTGCTCACATGAAAGCCAAGGGAGCAGCCCTCAGTGTGGACATCAGGACC
ATGTCAAGTAGAGATTTGCTCAATGCATTGAAGTCAGTCATTAATGACCCTATCTATAAA
GAGAATATCATGAAATTATCAAGAATTCATCATGATCAACCGGTGAAGCCCCTGGATCGA
GCAGTCTTCTGGATTGAGTTTGTCATGCGCCATAAAGGAGCCAAGCACCTTCGGGTCGCA
GCCCACAACCTCACCTGGATCCAGTACCACTCTTTGGATGTGATAGCATTCCTGCTGGCC
TGCGTGGCAACTATGATATTTATGATCACAAAATGTTGCCTGTTTTGTTTCCGAAAGCTT
GCCAAAACAGGAAAGAAGAAGAAAAGGGATTAG
Enzyme 16 GenBank Gene ID U59209 Link Image
Enzyme 16 GeneCard ID UGT2B17 Link Image
Enzyme 16 GenAtlas ID UGT2B17 Link Image
Enzyme 16 HGNC ID HGNC:12547 Link Image
Enzyme 16 Chromosome Location 4
Enzyme 16 Locus 4q13
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Beaulieu M, Levesque E, Hum DW, Belanger A: Isolation and characterization of a novel cDNA encoding a human UDP-glucuronosyltransferase active on C19 steroids. J Biol Chem. 1996 Sep 13;271(37):22855-62. [PubMed Link Image]
  2. Beaulieu M, Levesque E, Tchernof A, Beatty BG, Belanger A, Hum DW: Chromosomal localization, structure, and regulation of the UGT2B17 gene, encoding a C19 steroid metabolizing enzyme. DNA Cell Biol. 1997 Oct;16(10):1143-54. [PubMed Link Image]
  3. Yang TL, Chen XD, Guo Y, Lei SF, Wang JT, Zhou Q, Pan F, Chen Y, Zhang ZX, Dong SS, Xu XH, Yan H, Liu X, Qiu C, Zhu XZ, Chen T, Li M, Zhang H, Zhang L, Drees BM, Hamilton JJ, Papasian CJ, Recker RR, Song XP, Cheng J, Deng HW: Genome-wide copy-number-variation study identified a susceptibility gene, UGT2B17, for osteoporosis. Am J Hum Genet. 2008 Dec;83(6):663-74. Epub 2008 Nov 6. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5732
Enzyme 17 Name UDP-glucuronosyltransferase 1-6
Enzyme 17 Synonyms
  1. UDPGT 1-6
  2. UGT1*6
  3. UGT1-06
  4. UGT1.6
  5. Phenol-metabolizing UDP-glucuronosyltransferase
  6. UDP-glucuronosyltransferase 1-F
  7. UGT-1F
  8. UGT1F
  9. UDP-glucuronosyltransferase 1A6
Enzyme 17 Gene Name UGT1A6
Enzyme 17 Protein Sequence >UDP-glucuronosyltransferase 1-6
MACLLRSFQRISAGVFFLALWGMVVGDKLLVVPQDGSHWLSMKDIVEVLSDRGHEIVVVV
PEVNLLLKESKYYTRKIYPVPYDQEELKNRYQSFGNNHFAERSFLTAPQTEYRNNMIVIG
LYFINCQSLLQDRDTLNFFKESKFDALFTDPALPCGVILAEYLGLPSVYLFRGFPCSLEH
TFSRSPDPVSYIPRCYTKFSDHMTFSQRVANFLVNLLEPYLFYCLFSKYEELASAVLKRD
VDIITLYQKVSVWLLRYDFVLEYPRPVMPNMVFIGGINCKKRKDLSQEFEAYINASGEHG
IVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLL
GHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSE
DLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDL
TWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 17 Number of Residues 532
Enzyme 17 Molecular Weight 60750.2
Enzyme 17 Theoretical pI 8.55
Enzyme 17 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 17 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 17 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform has specificity for phenols
Enzyme 17 Pathways
Enzyme 17 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-26
Enzyme 17 Transmembrane Regions
  • 490-506
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 45827765 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID P19224 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name UD16_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1599 bp
ATGGCCTGCCTCCTTCGCTCATTTCAGAGAATTTCTGCAGGGGTTTTCTTCTTAGCACTT
TGGGGCATGGTTGTAGGTGACAAGCTGCTGGTGGTCCCTCAGGACGGAAGCCACTGGCTT
AGTATGAAGGATATAGTTGAGGTTCTCAGTGACCGGGGTCATGAGATTGTAGTGGTGGTG
CCTGAAGTTAATTTGCTTTTGAAAGAATCCAAATACTACACAAGAAAAATCTATCCAGTG
CCGTATGACCAAGAAGAGCTGAAGAACCGTTACCAATCATTTGGAAACAATCACTTTGCT
GAGCGATCATTCCTAACTGCTCCTCAGACAGAGTACAGGAATAACATGATTGTTATTGGC
CTGTACTTCATCAACTGCCAGAGCCTCCTGCAGGACAGGGACACCCTGAACTTCTTTAAG
GAGAGCAAGTTTGATGCTCTTTTCACAGACCCAGCCTTACCCTGTGGGGTGATCCTGGCT
GAGTATTTGGGCCTACCATCTGTGTACCTCTTCAGGGGTTTTCCGTGTTCCCTGGAGCAT
ACATTCAGCAGAAGCCCAGACCCTGTGTCCTACATTCCCAGGTGCTACACAAAGTTTTCA
GACCACATGACTTTTTCCCAACGAGTGGCCAACTTCCTTGTTAATTTGTTGGAGCCCTAT
CTATTTTATTGTCTGTTTTCAAAGTATGAAGAACTCGCATCAGCTGTCCTCAAGAGAGAT
GTGGATATAATCACCTTATATCAGAAGGTCTCTGTTTGGCTGTTAAGATATGACTTTGTG
CTTGAATATCCTAGGCCGGTCATGCCCAACATGGTCTTCATTGGAGGTATCAACTGTAAG
AAGAGGAAAGACTTGTCTCAGGAATTTGAAGCCTACATTAATGCTTCTGGAGAACATGGA
ATTGTGGTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCTATGGCA
ATTGCTGATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGAACCCGA
CCATCGAATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGATCTGCTT
GGTCACCCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTATGAAAGC
ATATGCAATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGACAATGCA
AAGCGCATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACTTCTGAA
GATTTAGAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAACATCATG
CGCCTCTCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTGTTCTGG
GTGGAGTTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCACGACCTC
ACCTGGTACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTGCTGACA
GTGGCCTTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGGAAAAAA
GGGCGAGTTAAGAAAGCCCACAAATCCAAGACCCATTGA
Enzyme 17 GenBank Gene ID NM_001072.3 Link Image
Enzyme 17 GeneCard ID UGT1A6 Link Image
Enzyme 17 GenAtlas ID UGT1A6 Link Image
Enzyme 17 HGNC ID HGNC:12538 Link Image
Enzyme 17 Chromosome Location 2
Enzyme 17 Locus 2q37
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Ritter JK, Chen F, Sheen YY, Tran HM, Kimura S, Yeatman MT, Owens IS: A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini. J Biol Chem. 1992 Feb 15;267(5):3257-61. [PubMed Link Image]
  2. Harding D, Fournel-Gigleux S, Jackson MR, Burchell B: Cloning and substrate specificity of a human phenol UDP-glucuronosyltransferase expressed in COS-7 cells. Proc Natl Acad Sci U S A. 1988 Nov;85(22):8381-5. [PubMed Link Image]
  3. Gong QH, Cho JW, Huang T, Potter C, Gholami N, Basu NK, Kubota S, Carvalho S, Pennington MW, Owens IS, Popescu NC: Thirteen UDPglucuronosyltransferase genes are encoded at the human UGT1 gene complex locus. Pharmacogenetics. 2001 Jun;11(4):357-68. [PubMed Link Image]
  4. Munzel PA, Lehmkoster T, Bruck M, Ritter JK, Bock KW: Aryl hydrocarbon receptor-inducible or constitutive expression of human UDP glucuronosyltransferase UGT1A6. Arch Biochem Biophys. 1998 Feb 1;350(1):72-8. [PubMed Link Image]
  5. Ciotti M, Marrone A, Potter C, Owens IS: Genetic polymorphism in the human UGT1A6 (planar phenol) UDP-glucuronosyltransferase: pharmacological implications. Pharmacogenetics. 1997 Dec;7(6):485-95. [PubMed Link Image]
  6. Nagar S, Zalatoris JJ, Blanchard RL: Human UGT1A6 pharmacogenetics: identification of a novel SNP, characterization of allele frequencies and functional analysis of recombinant allozymes in human liver tissue and in cultured cells. Pharmacogenetics. 2004 Aug;14(8):487-99. [PubMed Link Image]
  7. Menard V, Girard H, Harvey M, Perusse L, Guillemette C: Analysis of inherited genetic variations at the UGT1 locus in the French-Canadian population. Hum Mutat. 2009 Apr;30(4):677-87. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5733
Enzyme 18 Name UDP-glucuronosyltransferase 1-5
Enzyme 18 Synonyms
  1. UDPGT 1-5
  2. UGT1*5
  3. UGT1-05
  4. UGT1.5
  5. UDP-glucuronosyltransferase 1-E
  6. UGT-1E
  7. UGT1E
  8. UDP-glucuronosyltransferase 1A5
Enzyme 18 Gene Name UGT1A5
Enzyme 18 Protein Sequence >UDP-glucuronosyltransferase 1-5
MATGLQVPLPQLATGLLLLLSVQPWAESGKVLVVPTDGSHWLSMREALRDLHARGHQVVV
LTLEVNMYIKEENFFTLTTYAISWTQDEFDRLLLGHTQSFFETEHLLMKFSRRMAIMNNM
SLIIHRSCVELLHNEALIRHLHATSFDVVLTDPFHLCAAVLAKYLSIPAVFFLRNIPCDL
DFKGTQCPNPSSYIPRLLTTNSDHMTFLQRVKNMLYPLALSYLCHAVSAPYASLASELFQ
REVSVVDLVSHASVWLFRGDFVMDYPRPIMPNMVFIGGINCANGKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 18 Number of Residues 534
Enzyme 18 Molecular Weight 60070.6
Enzyme 18 Theoretical pI 8.14
Enzyme 18 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 18 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 18 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds
Enzyme 18 Pathways
Enzyme 18 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-28
Enzyme 18 Transmembrane Regions
  • 492-508
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 11118746 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID P35504 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name UD15_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1605 bp
ATGGCCACAGGACTCCAGGTTCCCCTGCCGCAGCTGGCCACAGGACTGCTGCTTCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGGAAGGTGCTGGTGGTGCCCACTGATGGCAGCCAC
TGGCTCAGCATGCGGGAGGCCTTGCGGGACCTCCATGCGAGAGGCCACCAGGTGGTGGTC
CTCACCCTGGAGGTGAATATGTACATCAAAGAAGAGAACTTTTTCACCCTGACAACGTAT
GCCATTTCATGGACCCAGGACGAATTTGATCGCCTTTTGCTGGGTCACACTCAATCGTTC
TTTGAAACAGAACATCTTCTGATGAAATTTTCTAGAAGAATGGCAATTATGAACAATATG
TCTTTGATCATACATAGGTCTTGTGTGGAGCTACTGCATAATGAGGCCCTGATCAGGCAC
CTGCATGCTACTTCCTTTGATGTGGTTCTAACAGACCCCTTTCACCTCTGCGCGGCGGTG
CTGGCTAAGTACCTGTCGATTCCTGCTGTGTTTTTCTTGAGGAACATTCCATGTGATTTA
GACTTTAAGGGCACACAGTGTCCAAACCCTTCCTCCTATATTCCTAGATTACTAACGACC
AATTCAGACCACATGACATTCCTGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACCTTTGCCATGCTGTTTCTGCTCCTTATGCAAGCCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATCTTGTCAGCCATGCATCTGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGATTACCCCAGGCCGATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACGGGAAGCCACTATCTCAGGAATTTGAAGCCTACATTAATGCTTCTGGAGAA
CATGGAATTGTGGTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCT
ATGGCAATTGCTGATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGA
ACCCGACCATCGAATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGAT
CTGCTTGGTCACCCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTAT
GAAAGCATATGCAATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGAC
AATGCAAAGCGCATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACT
TCTGAAGATTTAGAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAAC
ATCATGCGCCTCTCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTG
TTCTGGGTGGAGTTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCAC
GACCTCACCTGGTACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTG
CTGACAGTGGCCTTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGG
AAAAAAGGGCGAGTTAAGAAAGCCCACAAATCCAAGACCCATTGA
Enzyme 18 GenBank Gene ID AF297093 Link Image
Enzyme 18 GeneCard ID UGT1A5 Link Image
Enzyme 18 GenAtlas ID UGT1A5 Link Image
Enzyme 18 HGNC ID HGNC:12537 Link Image
Enzyme 18 Chromosome Location 2
Enzyme 18 Locus 2q37
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. Ritter JK, Chen F, Sheen YY, Tran HM, Kimura S, Yeatman MT, Owens IS: A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini. J Biol Chem. 1992 Feb 15;267(5):3257-61. [PubMed Link Image]
  2. Gong QH, Cho JW, Huang T, Potter C, Gholami N, Basu NK, Kubota S, Carvalho S, Pennington MW, Owens IS, Popescu NC: Thirteen UDPglucuronosyltransferase genes are encoded at the human UGT1 gene complex locus. Pharmacogenetics. 2001 Jun;11(4):357-68. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5734
Enzyme 19 Name UDP-glucuronosyltransferase 2B11
Enzyme 19 Synonyms
  1. UDPGT 2B11
Enzyme 19 Gene Name UGT2B11
Enzyme 19 Protein Sequence >UDP-glucuronosyltransferase 2B11
MTLKWTSVLLLIHLSCYFSSGSCGKVLVWAAEYSHWMNMKTILKELVQRGHEVTVLASSA
SILFDPNDASTLKFEVYPTSLTKTEFENIIMQQVKRWSDIRKDSFWLYFSQEQEILWELY
DIFRNFCKDVVSNKKVMKKLQESRFDIVFADAVFPCGELLAALLNIRFVYSLRFTPGYTI
ERHSGGLIFPPSYIPIVMSKLSDQMTFMERVKNMIYVLYFDFWFQMSDMKKWDQFYSEVL
GRPTTLFETMGKADIWLMRNSWSFQFPHPFLPNVDFVGGFHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSVISNMTAERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFFDQPDNIAHMKAKGAAVRLDFNTM
SSTDLLNALKTVINDPLYKENIMKLSRIQHDQPVKPLDRAVFWIEFVMPHKGAKHLRVAA
HDLTWFQYHSLDVIGFLLACVATVIFIITKFCLFCFWKFARKGKKGKRD
Enzyme 19 Number of Residues 529
Enzyme 19 Molecular Weight 61037.8
Enzyme 19 Theoretical pI 9.29
Enzyme 19 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 19 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 19 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds
Enzyme 19 Pathways
Enzyme 19 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • 1-21
Enzyme 19 Transmembrane Regions
  • 493-513
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 3360273 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID O75310 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name UDB11_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >1590 bp
ATGACTCTGAAATGGACTTCAGTTCTTCTGCTGATACATCTCAGTTGTTACTTTAGCTCT
GGGAGTTGTGGAAAAGTGCTGGTGTGGGCCGCAGAATACAGCCATTGGATGAATATGAAG
ACAATCCTGAAAGAGCTTGTTCAGAGAGGTCATGAGGTGACTGTACTGGCATCTTCAGCT
TCCATTCTTTTTGATCCCAATGATGCATCCACTCTTAAATTTGAAGTTTATCCTACATCT
TTAACTAAAACTGAATTTGAGAATATCATCATGCAACAGGTTAAGAGATGGTCAGACATT
CGAAAAGATAGCTTTTGGTTATATTTTTCACAAGAACAAGAAATCCTGTGGGAATTATAT
GACATATTTAGAAACTTCTGTAAAGATGTAGTTTCAAATAAGAAAGTTATGAAAAAACTA
CAAGAGTCAAGATTTGACATCGTTTTTGCAGATGCTGTTTTTCCCTGTGGTGAGCTGCTG
GCTGCGCTACTTAACATACGGTTTGTGTACAGTCTCCGCTTTACTCCTGGCTACACAATT
GAAAGGCACAGTGGAGGACTGATTTTCCCTCCTTCCTACATACCTATTGTTATGTCAAAA
TTAAGTGATCAAATGACTTTCATGGAGAGGGTAAAAAATATGATCTATGTGCTTTATTTT
GACTTTTGGTTCCAAATGTCTGATATGAAGAAGTGGGATCAGTTTTACAGTGAAGTTTTA
GGAAGACCCACTACCTTATTTGAGACAATGGGAAAAGCTGACATATGGCTTATGCGAAAC
TCCTGGAGTTTTCAATTTCCTCATCCATTCTTACCAAACGTTGATTTTGTTGGAGGATTC
CACTGCAAACCTGCCAAACCCCTACCTAAGGAAATGGAGGAGTTTGTACAGAGCTCTGGA
GAAAATGGTGTTGTGGTGTTTTCTCTGGGGTCAGTGATAAGTAACATGACAGCAGAAAGG
GCCAATGTAATTGCAACAGCCCTTGCCAAGATCCCACAAAAGGTTCTGTGGAGATTTGAC
GGGAATAAACCAGATGCCTTAGGTCTCAATACTCGGCTGTACAAGTGGATACCCCAGAAT
GACCTTCTAGGTCATCCAAAAACCAGAGCTTTTATAACTCATGGTGGAGCCAATGGCATC
TATGAGGCAATCTACCATGGGATCCCTATGGTGGGCATTCCATTGTTTTTTGATCAACCT
GATAACATTGCTCACATGAAGGCCAAGGGAGCAGCTGTTAGATTGGACTTCAACACAATG
TCGAGTACAGACCTGCTGAATGCACTGAAGACAGTAATTAATGATCCTTTATATAAAGAG
AATATTATGAAATTATCAAGAATTCAACATGATCAACCAGTAAAGCCCCTGGATCGAGCA
GTCTTCTGGATTGAATTTGTCATGCCCCACAAAGGAGCCAAACACCTTCGAGTTGCAGCC
CATGACCTCACCTGGTTCCAGTACCACTCTTTGGATGTGATTGGGTTTCTGCTGGCCTGT
GTGGCAACTGTGATATTTATCATCACAAAGTTTTGTCTGTTTTGTTTCTGGAAGTTTGCT
AGAAAAGGGAAGAAGGGAAAAAGAGATTAG
Enzyme 19 GenBank Gene ID AF016492 Link Image
Enzyme 19 GeneCard ID UGT2B11 Link Image
Enzyme 19 GenAtlas ID UGT2B11 Link Image
Enzyme 19 HGNC ID HGNC:12545 Link Image
Enzyme 19 Chromosome Location 4
Enzyme 19 Locus 4q13.2
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Beaulieu M, Levesque E, Hum DW, Belanger A: Isolation and characterization of a human orphan UDP-glucuronosyltransferase, UGT2B11. Biochem Biophys Res Commun. 1998 Jul 9;248(1):44-50. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5740
Enzyme 20 Name Steryl-sulfatase
Enzyme 20 Synonyms
  1. Arylsulfatase C
  2. ASC
  3. Steroid sulfatase
  4. Steryl-sulfate sulfohydrolase
Enzyme 20 Gene Name STS
Enzyme 20 Protein Sequence >Steryl-sulfatase
MPLRKMKIPFLLLFFLWEAESHAASRPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLAS
GGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTGVFLFTASSGGLPTDEITFAK
LLKDQGYSTALIGKWHLGMSCHSKTDFCHHPLHHGFNYFYGISLTNLRDCKPGEGSVFTT
GFKRLVFLPLQIVGVTLLTLAALNCLGLLHVPLGVFFSLLFLAALILTLFLGFLHYFRPL
NCFMMRNYEIIQQPMSYDNLTQRLTVEAAQFIQRNTETPFLLVLSYLHVHTALFSSKDFA
GKSQHGVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFTSDQGAHVEEVSSKGEIHGGS
NGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDRI
IDGRDLMPLLEGKSQRSDHEFLFHYCNAYLNAVRWHPQNSTSIWKAFFFTPNFNPVGSNG
CFATHVCFCFGSYVTHHDPPLLFDISKDPRERNPLTPASEPRFYEILKVMQEAADRHTQT
LPEVPDQFSWNNFLWKPWLQLCCPSTGLSCQCDREKQDKRLSR
Enzyme 20 Number of Residues 583
Enzyme 20 Molecular Weight 65491.7
Enzyme 20 Theoretical pI 7.71
Enzyme 20 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • sulfuric ester hydrolase activity
Process
  • metabolic process
Component
Enzyme 20 General Function Involved in catalytic activity
Enzyme 20 Specific Function Conversion of sulfated steroid precursors to estrogens during pregnancy
Enzyme 20 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 20 Reactions
  • 3beta-hydroxyandrost-5-en-17-one 3-sulfate + H2O = 3beta-hydroxyandrost-5-en-17-one + sulfate [RN:R03404]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • 1-21
Enzyme 20 Transmembrane Regions
  • 185-208 213-234
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 338565 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P08842 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name STS_HUMAN Link Image
Enzyme 20 PDB ID 1P49 Link Image
Enzyme 20 PDB File Show
Enzyme 20 3D Structure
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >1752 bp
ATGCCTTTAAGGAAGATGAAGATCCCTTTCCTCCTACTGTTCTTTCTGTGGGAAGCCGAG
AGCCACGCAGCATCAAGGCCGAACATCATCCTGGTGATGGCTGACGACCTCGGCATTGGA
GATCCTGGGTGCTATGGGAACAAAACTATCAGGACTCCCAATATCGACCGGTTGGCCAGT
GGGGGAGTGAAACTCACTCAGCACCTGGCAGCATCACCGCTGTGCACACCAAGCAGGGCA
GCCTTCATGACTGGCCGGTACCCTGTCCGATCAGGAATGGCATCTTGGTCCCGCACTGGA
GTTTTCCTCTTCACAGCCTCTTCGGGAGGACTTCCCACCGATGAGATTACCTTTGCTAAG
CTTCTGAAGGATCAAGGTTATTCAACAGCACTGATAGGGAAATGGCACCTTGGGATGAGC
TGTCACAGCAAGACTGACTTCTGTCACCACCCTTTACATCACGGCTTCAATTATTTCTAT
GGGATCTCTTTGACCAATCTGAGAGACTGCAAGCCCGGAGAGGGCAGTGTCTTCACCACG
GGCTTCAAGAGGCTGGTCTTCCTCCCCCTGCAGATCGTCGGGGTCACCCTCCTTACCCTT
GCTGCACTCAATTGTCTGGGGCTACTCCACGTGCCTCTAGGCGTTTTTTTCAGCCTTCTC
TTCCTAGCAGCCCTAATCCTGACCCTTTTCTTGGGCTTCCTTCATTACTTCCGGCCCCTG
AACTGCTTCATGATGAGGAACTACGAGATCATTCAGCAGCCCATGTCCTATGACAATCTC
ACCCAGAGGCTAACGGTGGAGGCGGCCCAGTTCATACAGCGGAACACTGAGACTCCGTTC
CTGCTTGTCTTGTCCTACCTCCACGTGCACACAGCCCTGTTCTCCAGCAAAGACTTTGCT
GGCAAAAGTCAACACGGAGTCTACGGGGATGCTGTTGAGGAAATGGACTGGAGTGTGGGG
CAGATCTTGAACCTTCTGGATGAGCTGAGATTGGCTAATGATACCCTCATCTACTTCACA
TCGGACCAGGGAGCACATGTAGAGGAGGTGTCTTCCAAAGGAGAAATTCATGGCGGAAGT
AATGGGATCTATAAAGGAGGAAAAGCAAACAACTGGGAAGGAGGTATCCGGGTTCCAGGC
ATCCTTCGTTGGCCCAGGGTGATACAGGCTGGCCAGAAGATTGATGAGCCCACTAGCAAC
ATGGACATATTTCCTACAGTAGCCAAGCTGGCTGGAGCTCCCTTGCCTGAGGACAGGATC
ATTGATGGACGTGATCTGATGCCCCTGCTTGAAGGAAAAAGCCAACGCTCCGATCATGAG
TTTCTCTTCCATTACTGCAACGCCTACTTAAATGCTGTGCGCTGGCACCCTCAGAACAGC
ACATCCATCTGGAAGGCCTTTTTCTTCACCCCCAACTTCAACCCCGTGGGTTCCAACGGA
TGCTTTGCCACACACGTGTGCTTCTGTTTCGGGAGTTATGTCACCCATCACGACCCACCT
TTACTCTTTGATATTTCCAAAGATCCCAGAGAGAGAAACCCACTAACTCCAGCATCCGAG
CCCCGGTTTTATGAAATCCTCAAAGTCATGCAGGAAGCTGCGGACAGACACACCCAGACC
CTGCCAGAGGTGCCCGATCAGTTTTCATGGAACAACTTTCTTTGGAAGCCCTGGCTTCAG
CTGTGCTGTCCTTCCACCGGCCTGTCTTGCCAGTGTGATAGAGAAAAACAGGATAAGAGA
CTGAGCCGCTAG
Enzyme 20 GenBank Gene ID J04964 Link Image
Enzyme 20 GeneCard ID STS Link Image
Enzyme 20 GenAtlas ID STS Link Image
Enzyme 20 HGNC ID HGNC:11425 Link Image
Enzyme 20 Chromosome Location Not Available
Enzyme 20 Locus Not Available
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Stein C, Hille A, Seidel J, Rijnbout S, Waheed A, Schmidt B, Geuze H, von Figura K: Cloning and expression of human steroid-sulfatase. Membrane topology, glycosylation, and subcellular distribution in BHK-21 cells. J Biol Chem. 1989 Aug 15;264(23):13865-72. [PubMed Link Image]
  2. Yen PH, Allen E, Marsh B, Mohandas T, Wang N, Taggart RT, Shapiro LJ: Cloning and expression of steroid sulfatase cDNA and the frequent occurrence of deletions in STS deficiency: implications for X-Y interchange. Cell. 1987 May 22;49(4):443-54. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Yen PH, Marsh B, Allen E, Tsai SP, Ellison J, Connolly L, Neiswanger K, Shapiro LJ: The human X-linked steroid sulfatase gene and a Y-encoded pseudogene: evidence for an inversion of the Y chromosome during primate evolution. Cell. 1988 Dec 23;55(6):1123-35. [PubMed Link Image]
  6. Kawano J, Kotani T, Ohtaki S, Minamino N, Matsuo H, Oinuma T, Aikawa E: Characterization of rat and human steroid sulfatases. Biochim Biophys Acta. 1989 Aug 31;997(3):199-205. [PubMed Link Image]
  7. Hernandez-Guzman FG, Higashiyama T, Pangborn W, Osawa Y, Ghosh D: Structure of human estrone sulfatase suggests functional roles of membrane association. J Biol Chem. 2003 Jun 20;278(25):22989-97. Epub 2003 Mar 25. [PubMed Link Image]
  8. Basler E, Grompe M, Parenti G, Yates J, Ballabio A: Identification of point mutations in the steroid sulfatase gene of three patients with X-linked ichthyosis. Am J Hum Genet. 1992 Mar;50(3):483-91. [PubMed Link Image]
  9. Alperin ES, Shapiro LJ: Characterization of point mutations in patients with X-linked ichthyosis. Effects on the structure and function of the steroid sulfatase protein. J Biol Chem. 1997 Aug 15;272(33):20756-63. [PubMed Link Image]
  10. Sugawara T, Shimizu H, Hoshi N, Fujimoto Y, Nakajima A, Fujimoto S: PCR diagnosis of X-linked ichthyosis: identification of a novel mutation (E560P) of the steroid sulfatase gene. Hum Mutat. 2000 Mar;15(3):296. [PubMed Link Image]
  11. Oyama N, Satoh M, Iwatsuki K, Kaneko F: Novel point mutations in the steroid sulfatase gene in patients with X-linked ichthyosis: transfection analysis using the mutated genes. J Invest Dermatol. 2000 Jun;114(6):1195-9. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5818
Enzyme 21 Name Estradiol 17-beta-dehydrogenase 11
Enzyme 21 Synonyms
  1. 17-beta-hydroxysteroid dehydrogenase 11
  2. 17-beta-HSD 11
  3. 17bHSD11
  4. 17betaHSD11
  5. 17-beta-hydroxysteroid dehydrogenase XI
  6. 17-beta-HSD XI
  7. 17betaHSDXI
  8. Cutaneous T-cell lymphoma-associated antigen HD-CL-03
  9. CTCL-associated antigen HD-CL-03
  10. Dehydrogenase/reductase SDR family member 8
  11. Retinal short-chain dehydrogenase/reductase 2
  12. retSDR2
Enzyme 21 Gene Name HSD17B11
Enzyme 21 Protein Sequence >Estradiol 17-beta-dehydrogenase 11
MKFLLDILLLLPLLIVCSLESFVKLFIPKRRKSVTGEIVLITGAGHGIGRLTAYEFAKLK
SKLVLWDINKHGLEETAAKCKGLGAKVHTFVVDCSNREDIYSSAKKVKAEIGDVSILVNN
AGVVYTSDLFATQDPQIEKTFEVNVLAHFWTTKAFLPAMTKNNHGHIVTVASAAGHVSVP
FLLAYCSSKFAAVGFHKTLTDELAALQITGVKTTCLCPNFVNTGFIKNPSTSLGPTLEPE
EVVNRLMHGILTEQKMIFIPSSIAFLTTLERILPERFLAVLKQKISVKFDAVIGYKMKAQ
Enzyme 21 Number of Residues 300
Enzyme 21 Molecular Weight 32935.5
Enzyme 21 Theoretical pI 9.56
Enzyme 21 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 21 General Function Involved in oxidoreductase activity
Enzyme 21 Specific Function Can convert androstan-3-alpha,17-beta-diol (3-alpha- diol) to androsterone in vitro, suggesting that it may participate in androgen metabolism during steroidogenesis. May act by metabolizing compounds that stimulate steroid synthesis and/or by generating metabolites that inhibit it. Has no activity toward DHEA (dehydroepiandrosterone), or A-dione (4-androste-3,17-dione), and only a slight activity toward testosterone to A-dione. Tumor- associated antigen in cutaneous T-cell lymphoma
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions
  • estradiol-17beta + NAD(P)+ = estrone + NAD(P)H + H+ [RN:R02352 R02353]
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • 1-19
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 142976729 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID Q8NBQ5 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name DHB11_HUMAN Link Image
Enzyme 21 PDB ID 1YB1 Link Image
Enzyme 21 PDB File Show
Enzyme 21 3D Structure
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >903 bp
ATGAAATTTCTTCTGGACATCCTCCTGCTTCTCCCGTTACTGATCGTCTGCTCCCTAGAG
TCCTTCGTGAAGCTTTTTATTCCTAAGAGGAGAAAATCAGTCACCGGCGAAATCGTGCTG
ATTACAGGAGCTGGGCATGGAATTGGGAGACTGACTGCCTATGAATTTGCTAAACTTAAA
AGCAAGCTGGTTCTCTGGGATATAAATAAGCATGGACTGGAGGAAACAGCTGCCAAATGC
AAGGGACTGGGTGCCAAGGTTCATACCTTTGTGGTAGACTGCAGCAACCGAGAAGATATT
TACAGCTCTGCAAAGAAGGTGAAGGCAGAAATTGGAGATGTTAGTATTTTAGTAAATAAT
GCTGGTGTAGTCTATACATCAGATTTGTTTGCTACACAAGATCCTCAGATTGAAAAGACT
TTTGAAGTTAATGTACTTGCACATTTCTGGACTACAAAGGCATTTCTTCCTGCAATGACG
AAGAATAACCATGGCCATATTGTCACTGTGGCTTCGGCAGCTGGACATGTCTCGGTCCCC
TTCTTACTGGCTTACTGTTCAAGCAAGTTTGCTGCTGTTGGATTTCATAAAACTTTGACA
GATGAACTGGCTGCCTTACAAATAACTGGAGTCAAAACAACATGTCTGTGTCCTAATTTC
GTAAACACTGGCTTCATCAAAAATCCAAGTACAAGTTTGGGACCCACTCTGGAACCTGAG
GAAGTGGTAAACAGGCTGATGCATGGGATTCTGACTGAGCAGAAGATGATTTTTATTCCA
TCTTCTATAGCTTTTTTAACAACATTGGAAAGGATCCTTCCTGAGCGTTTCCTGGCAGTT
TTAAAACAAAAAATCAGTGTTAAGTTTGATGCAGTTATTGGATATAAAATGAAAGCGCAA
TAA
Enzyme 21 GenBank Gene ID NM_016245.3 Link Image
Enzyme 21 GeneCard ID HSD17B11 Link Image
Enzyme 21 GenAtlas ID HSD17B11 Link Image
Enzyme 21 HGNC ID HGNC:22960 Link Image
Enzyme 21 Chromosome Location 4
Enzyme 21 Locus 4q22.1
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Haeseleer F, Palczewski K: Short-chain dehydrogenases/reductases in retina. Methods Enzymol. 2000;316:372-83. [PubMed Link Image]
  2. Hartmann TB, Thiel D, Dummer R, Schadendorf D, Eichmuller S: SEREX identification of new tumour-associated antigens in cutaneous T-cell lymphoma. Br J Dermatol. 2004 Feb;150(2):252-8. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed Link Image]
  5. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Li KX, Smith RE, Krozowski ZS: Cloning and expression of a novel tissue specific 17beta-hydroxysteroid dehydrogenase. Endocr Res. 1998 Aug-Nov;24(3-4):663-7. [PubMed Link Image]
  8. Brereton P, Suzuki T, Sasano H, Li K, Duarte C, Obeyesekere V, Haeseleer F, Palczewski K, Smith I, Komesaroff P, Krozowski Z: Pan1b (17betaHSD11)-enzymatic activity and distribution in the lung. Mol Cell Endocrinol. 2001 Jan 22;171(1-2):111-7. [PubMed Link Image]
  9. Chai Z, Brereton P, Suzuki T, Sasano H, Obeyesekere V, Escher G, Saffery R, Fuller P, Enriquez C, Krozowski Z: 17 beta-hydroxysteroid dehydrogenase type XI localizes to human steroidogenic cells. Endocrinology. 2003 May;144(5):2084-91. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 6128
Enzyme 22 Name Estradiol 17-beta-dehydrogenase 1
Enzyme 22 Synonyms
  1. 17-beta-hydroxysteroid dehydrogenase type 1
  2. 17-beta-HSD 1
  3. 20 alpha-hydroxysteroid dehydrogenase
  4. 20-alpha-HSD
  5. E2DH
  6. Placental 17-beta-hydroxysteroid dehydrogenase
Enzyme 22 Gene Name HSD17B1
Enzyme 22 Protein Sequence >Estradiol 17-beta-dehydrogenase 1
MARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSL
ETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTV
RMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVH
LSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEV
FLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGG
GAGPGAEDEAGRSAVGDPELGDPPAAPQ
Enzyme 22 Number of Residues 328
Enzyme 22 Molecular Weight 34979.7
Enzyme 22 Theoretical pI 5.42
Enzyme 22 GO Classification
Function
  • binding
  • catalytic activity
  • estradiol 17-beta-dehydrogenase activity
  • oxidoreductase activity
  • steroid dehydrogenase activity
  • steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
  • estrogen biosynthetic process
  • lipid metabolic process
  • metabolic process
  • oxidation reduction
  • primary metabolic process
  • steroid biosynthetic process
  • steroid metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 22 General Function Involved in estradiol 17-beta-dehydrogenase activity
Enzyme 22 Specific Function Favors the reduction of estrogens and androgens. Also has 20-alpha-HSD activity. Uses preferentially NADH
Enzyme 22 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 22 Reactions
  • estradiol-17beta + NAD(P)+ = estrone + NAD(P)H + H+ [RN:R02352 R02353]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 23365 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID P14061 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name DHB1_HUMAN Link Image
Enzyme 22 PDB ID 1QYX Link Image
Enzyme 22 PDB File Show
Enzyme 22 3D Structure
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >987 bp
ATGGCCCGCACCGTGGTGCTCATCACCGGCTGTTCCTCGGGCATCGGCCTGCACTTGGCC
GTACGTCTGGCTTCAGATCCATCCCAGAGCTTCAAAGTGTATGCCACGTTGAGGGACCTG
AAAACACAGGGCCGGCTGTGGGAGGCGGCCCGGGCCCTGGCATGCCCTCCGGGATCCCTG
GAGACGTTGCAGCTGGACGTAAGGGACTCAAAATCCGTGGCCGCTGCCCGGGAACGCGTG
ACTGAGGGCCGCGTGGACGTGCTGGTGTGTAACGCAGGCCTGGGCCTGCTGGGGCCGCTG
GAGGCGCTGGGGGAGGACGCCGTGGCCTCTGTGCTGGACGTGAATGTAGTAGGGACTGTG
CGGATGCTGCAGGCCTTCCTGCCAGACATGAAGAGGCGCGGTTCGGGACGCGTGTTGGTG
ACCGGGAGCGTGGGAGGATTGATGGGGCTGCCTTTCAATGACGTTTATTGCGCCAGCAAG
TTCGCGCTCGAAGGCTTATGCGAGAGTCTGGCGGTTCTGCTGCTGCCCTTTGGGGTCCAC
TTGAGCCTGATCGAGTGCGGCCCAGTGCACACCGCCTTCATGGAGAAGGTGTTGGGCAGC
CCAGAGGAGGTGCTGGACCGCACGGACATCCACACCTTCCACCGCTTCTACCAATACCTC
GCCCACAGCAAGCAAGTCTTTCGCGAGGCGGCGCAGAACCCTGAGGAGGTGGCGGAGGTC
TTCCTCACCGCTTTGCGCGCCCCGAAGCCGACCCTGCGCTACTTCACCACCGAGCGCTTC
CTGCCCCTGCTGCGGATGCGCCTGGACGACCCCAGCGGCTCCAACTACGTCACCGCCATG
CACCGGGAAGTGTTCGGCGACGTTCCGGCAAAGGCCGAGGCTGGGGCCGAGGCTGGGGGC
GGGGCCGGGCCTGGGGCAGAGGACGAGGCCGGGCGCAGTGCGGTGGGGGACCCTGAGCTC
GGCGATCCTCCGGCCGCCCCGCAGTAA
Enzyme 22 GenBank Gene ID X13440 Link Image
Enzyme 22 GeneCard ID HSD17B1 Link Image
Enzyme 22 GenAtlas ID HSD17B1 Link Image
Enzyme 22 HGNC ID HGNC:5210 Link Image
Enzyme 22 Chromosome Location 1
Enzyme 22 Locus 17q11-q21
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Peltoketo H, Isomaa V, Maentausta O, Vihko R: Complete amino acid sequence of human placental 17 beta-hydroxysteroid dehydrogenase deduced from cDNA. FEBS Lett. 1988 Oct 24;239(1):73-7. [PubMed Link Image]
  2. Luu The V, Labrie C, Zhao HF, Couet J, Lachance Y, Simard J, Leblanc G, Cote J, Berube D, Gagne R, et al.: Characterization of cDNAs for human estradiol 17 beta-dehydrogenase and assignment of the gene to chromosome 17: evidence of two mRNA species with distinct 5'-termini in human placenta. Mol Endocrinol. 1989 Aug;3(8):1301-9. [PubMed Link Image]
  3. Luu-The V, Labrie C, Simard J, Lachance Y, Zhao HF, Couet J, Leblanc G, Labrie F: Structure of two in tandem human 17 beta-hydroxysteroid dehydrogenase genes. Mol Endocrinol. 1990 Feb;4(2):268-75. [PubMed Link Image]
  4. Luu-The V, Labrie C, Zhao HF, Couet J, Lachance Y, Simard J, Cote J, Leblanc G, Lagace L, Berube D, et al.: Purification, cloning, complementary DNA structure, and predicted amino acid sequence of human estradiol 17 beta-dehydrogenase. Ann N Y Acad Sci. 1990;595:40-52. [PubMed Link Image]
  5. Peltoketo H, Isomaa V, Vihko R: Genomic organization and DNA sequences of human 17 beta-hydroxysteroid dehydrogenase genes and flanking regions. Localization of multiple Alu sequences and putative cis-acting elements. Eur J Biochem. 1992 Oct 1;209(1):459-66. [PubMed Link Image]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Burns DJ, Engel LL, Bethune JL: Amino acid composition and subunit structure. Human placental 17 -estradiol dehydrogenase. Biochemistry. 1972 Jul 4;11(14):2699-703. [PubMed Link Image]
  9. Nicolas JC, Harris JI: Human placental 17 -oestradiol dehydrogenase. Sequence of a tryptic peptide containing an essential cysteine. FEBS Lett. 1973 Jan 15;29(2):173-6. [PubMed Link Image]
  10. Murdock GL, Chin CC, Warren JC: Human placental estradiol 17 beta-dehydrogenase: sequence of a histidine-bearing peptide in the catalytic region. Biochemistry. 1986 Feb 11;25(3):641-6. [PubMed Link Image]
  11. Murdock GL, Chin CC, Offord RE, Bradshaw RA, Warren JC: Human placental estradiol 17 beta-dehydrogenase. Identification of a single histidine residue affinity-labeled by both 3-bromoacetoxyestrone and 12 beta-bromoacetoxy-4-estrene-3,17-dione. J Biol Chem. 1983 Oct 10;258(19):11460-4. [PubMed Link Image]
  12. Baker ME: Human placental 17 beta-hydroxysteroid dehydrogenase is homologous to NodG protein of Rhizobium meliloti. Mol Endocrinol. 1989 May;3(5):881-4. [PubMed Link Image]
  13. Ghosh D, Pletnev VZ, Zhu DW, Wawrzak Z, Duax WL, Pangborn W, Labrie F, Lin SX: Structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase at 2.20 A resolution. Structure. 1995 May 15;3(5):503-13. [PubMed Link Image]
  14. Azzi A, Rehse PH, Zhu DW, Campbell RL, Labrie F, Lin SX: Crystal structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase complexed with 17 beta-estradiol. Nat Struct Biol. 1996 Aug;3(8):665-8. [PubMed Link Image]
  15. Breton R, Housset D, Mazza C, Fontecilla-Camps JC: The structure of a complex of human 17beta-hydroxysteroid dehydrogenase with estradiol and NADP+ identifies two principal targets for the design of inhibitors. Structure. 1996 Aug 15;4(8):905-15. [PubMed Link Image]
  16. Mazza C, Breton R, Housset D, Fontecilla-Camps JC: Unusual charge stabilization of NADP+ in 17beta-hydroxysteroid dehydrogenase. J Biol Chem. 1998 Apr 3;273(14):8145-52. [PubMed Link Image]
  17. Sawicki MW, Erman M, Puranen T, Vihko P, Ghosh D: Structure of the ternary complex of human 17beta-hydroxysteroid dehydrogenase type 1 with 3-hydroxyestra-1,3,5,7-tetraen-17-one (equilin) and NADP+. Proc Natl Acad Sci U S A. 1999 Feb 2;96(3):840-5. [PubMed Link Image]
  18. Han Q, Campbell RL, Gangloff A, Huang YW, Lin SX: Dehydroepiandrosterone and dihydrotestosterone recognition by human estrogenic 17beta-hydroxysteroid dehydrogenase. C-18/c-19 steroid discrimination and enzyme-induced strain. J Biol Chem. 2000 Jan 14;275(2):1105-11. [PubMed Link Image]
  19. Qiu W, Campbell RL, Gangloff A, Dupuis P, Boivin RP, Tremblay MR, Poirier D, Lin SX: A concerted, rational design of type 1 17beta-hydroxysteroid dehydrogenase inhibitors: estradiol-adenosine hybrids with high affinity. FASEB J. 2002 Nov;16(13):1829-31. Epub 2002 Sep 5. [PubMed Link Image]
  20. Gangloff A, Shi R, Nahoum V, Lin SX: Pseudo-symmetry of C19 steroids, alternative binding orientations, and multispecificity in human estrogenic 17beta-hydroxysteroid dehydrogenase. FASEB J. 2003 Feb;17(2):274-6. Epub 2002 Dec 17. [PubMed Link Image]
  21. Shi R, Lin SX: Cofactor hydrogen bonding onto the protein main chain is conserved in the short chain dehydrogenase/reductase family and contributes to nicotinamide orientation. J Biol Chem. 2004 Apr 16;279(16):16778-85. Epub 2004 Feb 13. [PubMed Link Image]
  22. Normand T, Narod S, Labrie F, Simard J: Detection of polymorphisms in the estradiol 17 beta-hydroxysteroid dehydrogenase II gene at the EDH17B2 locus on 17q11-q21. Hum Mol Genet. 1993 Apr;2(4):479-83. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 6129
Enzyme 23 Name 3-keto-steroid reductase
Enzyme 23 Synonyms
  1. 17-beta-hydroxysteroid dehydrogenase 7
  2. 17-beta-HSD 7
  3. Estradiol 17-beta-dehydrogenase 7
Enzyme 23 Gene Name HSD17B7
Enzyme 23 Protein Sequence >3-keto-steroid reductase
MRKVVLITGASSGIGLALCKRLLAEDDELHLCLACRNMSKAEAVCAALLASHPTAEVTIV
QVDVSNLQSVFRASKELKQRFQRLDCIYLNAGIMPNPQLNIKALFFGLFSRKVIHMFSTA
EGLLTQGDKITADGLQEVFETNVFGHFILIRELEPLLCHSDNPSQLIWTSSRSARKSNFS
LEDFQHSKGKEPYSSSKYATDLLSVALNRNFNQQGLYSNVACPGTALTNLTYGILPPFIW
TLLMPAILLLRFFANAFTLTPYNGTEALVWLFHQKPESLNPLIKYLSATTGFGRNYIMTQ
KMDLDEDTAEKFYQKLLELEKHIRVTIQKTDNQARLSGSCL
Enzyme 23 Number of Residues 341
Enzyme 23 Molecular Weight 38205.8
Enzyme 23 Theoretical pI 8.21
Enzyme 23 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 23 General Function Involved in oxidoreductase activity
Enzyme 23 Specific Function Responsible for the reduction of the keto group on the C-3 of sterols
Enzyme 23 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 23 Reactions
  • 4alpha-methyl-5alpha-cholest-7-en-3beta-ol + NADP+ = 4alpha-methyl-5alpha-cholest-7-en-3-one + NADPH + H+ [RN:R05691]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • 230-250
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 6721095 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID P56937 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name DHB7_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1026 bp
ATGCGAAAGGTGGTTTTGATCACCGGGGCTAGCAGTGGCATTGGCCTGGCCCTCTGCAAG
CGGCTGCTGGCGGAAGATGATGAGCTTCATCTGTGTTTGGCGTGCAGGAACATGAGCAAG
GCAGAAGCTGTCTGTGCTGCTCTGCTGGCCTCTCACCCCACTGCTGAGGTCACCATTGTC
CAGGTGGATGTCAGCAACCTGCAGTCGGTCTTCCGGGCCTCCAAGGAACTTAAGCAAAGG
TTTCAGAGATTAGACTGTATATATCTAAATGCTGGGATCATGCCTAATCCACAACTAAAT
ATCAAAGCACTTTTCTTTGGCCTCTTTTCAAGAAAAGTGATTCATATGTTCTCCACAGCT
GAAGGCCTGCTGACCCAGGGTGATAAGATCACTGCTGATGGACTTCAGGAGGTGTTTGAG
ACCAATGTCTTTGGCCATTTTATCCTGATTCGGGAACTGGAGCCTCTCCTCTGTCACAGT
GACAATCCATCTCAGCTCATCTGGACATCATCTCGCAGTGCAAGGAAATCTAATTTCAGC
CTCGAGGACTTCCAGCACAGCAAAGGCAAGGAACCCTACAGCTCTTCCAAATATGCCACT
GACCTTTTGAGTGTGGCTTTGAACAGGAACTTCAACCAGCAGGGTCTCTATTCCAATGTG
GCCTGTCCAGGTACAGCATTGACCAATTTGACATATGGAATTCTGCCTCCGTTTATATGG
ACGCTGTTGATGCCGGCAATATTGCTACTTCGCTTTTTTGCAAATGCATTCACTTTGACA
CCATATAATGGAACAGAAGCTCTGGTATGGCTTTTCCACCAAAAGCCTGAATCTCTCAAT
CCTCTGATCAAATATCTGAGTGCCACCACTGGCTTTGGAAGAAATTATATTATGACCCAG
AAGATGGACCTAGATGAAGACACTGCTGAAAAATTTTATCAAAAGTTACTGGAACTGGAA
AAGCACATTAGGGTCACTATTCAAAAAACAGATAATCAGGCCAGGCTCAGTGGCTCATGC
CTATAA
Enzyme 23 GenBank Gene ID AF098786 Link Image
Enzyme 23 GeneCard ID HSD17B7 Link Image
Enzyme 23 GenAtlas ID HSD17B7 Link Image
Enzyme 23 HGNC ID HGNC:5215 Link Image
Enzyme 23 Chromosome Location 1
Enzyme 23 Locus 1q23
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Krazeisen A, Breitling R, Imai K, Fritz S, Moller G, Adamski J: Determination of cDNA, gene structure and chromosomal localization of the novel human 17beta-hydroxysteroid dehydrogenase type 7(1). FEBS Lett. 1999 Oct 29;460(2):373-9. [PubMed Link Image]
  2. Torn S, Nokelainen P, Kurkela R, Pulkka A, Menjivar M, Ghosh S, Coca-Prados M, Peltoketo H, Isomaa V, Vihko P: Production, purification, and functional analysis of recombinant human and mouse 17beta-hydroxysteroid dehydrogenase type 7. Biochem Biophys Res Commun. 2003 May 23;305(1):37-45. [PubMed Link Image]
  3. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Marijanovic Z, Laubner D, Moller G, Gege C, Husen B, Adamski J, Breitling R: Closing the gap: identification of human 3-ketosteroid reductase, the last unknown enzyme of mammalian cholesterol biosynthesis. Mol Endocrinol. 2003 Sep;17(9):1715-25. Epub 2003 Jun 26. [PubMed Link Image]
  8. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 6306
Enzyme 24 Name Cytochrome P450 3A4
Enzyme 24 Synonyms
  1. Albendazole monooxygenase
  2. Albendazole sulfoxidase
  3. CYPIIIA3
  4. CYPIIIA4
  5. Cytochrome P450 3A3
  6. Cytochrome P450 HLp
  7. Cytochrome P450 NF-25
  8. Cytochrome P450-PCN1
  9. Nifedipine oxidase
  10. Quinine 3-monooxygenase
  11. Taurochenodeoxycholate 6-alpha-hydroxylase
Enzyme 24 Gene Name CYP3A4
Enzyme 24 Protein Sequence >Cytochrome P450 3A4
MALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMF
DMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISI
AEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYS
MDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICV
FPREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSI
IFIFAGYETTSSVLSFIMYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVLQMEYLDMVV
NETLRLFPIAMRLERVCKKDVEINGMFIPKGVVVMIPSYALHRDPKYWTEPEKFLPERFS
KKNKDNIDPYIYTPFGSGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLSLG
GLLQPEKPVVLKVESRDGTVSGA
Enzyme 24 Number of Residues 503
Enzyme 24 Molecular Weight 57342.7
Enzyme 24 Theoretical pI 8.25
Enzyme 24 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 24 General Function Involved in monooxygenase activity
Enzyme 24 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It performs a variety of oxidation reactions (e.g. caffeine 8-oxidation, omeprazole sulphoxidation, midazolam 1'-hydroxylation and midazolam 4- hydroxylation) of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. The enzyme also hydroxylates etoposide
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions
  • (1) taurochenodeoxycholate + NADPH + H+ + O2 = taurohyocholate + NADP+ + H2O [RN:R07205]
  • (2) lithocholate + NADPH + H+ + O2 = hyodeoxycholate + NADP+ + H2O [RN:R07206]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • 2-22
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 6470135 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID P08684 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name CP3A4_HUMAN Link Image
Enzyme 24 PDB ID 1TQN Link Image
Enzyme 24 PDB File Show
Enzyme 24 3D Structure
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >1512 bp
ATGGCTCTCATCCCAGACTTGGCCATGGAAACCCGGCTTCTCCTGGCTGTCAGCCTGGTG
CTCCTCTATCTATATGGAACTCATTCACATGGACTTTTTAAGAAGCTTGGAATTCCAGGG
CCCACACCTCTGCCTTTTTTGGGAAATATTTTGTCCTACCATAAGGGCTTTTGTATGTTT
GACATGGAATGTCATAAAAAGTATGGAAAAGTGTGGGGCTTTTATGATGGTCAACAGCCT
GTGCTGGCTATCACAGATCCTGACATGATCAAAACAGTGCTAGTGAAAGAATGTTATTCT
GTCTTCACAAACCGGAGGCCTTTTGGTCCAGTGGGATTTATGAAAAGTGCCATCTCTATA
GCTGAGGATGAAGAATGGAAGAGATTACGATCATTGCTGTCTCCAACCTTCACCAGTGGA
AAACTCAAGGAGATGGTCCCTATCATTGCCCAGTATGGAGATGTGTTGGTGAGAAATCTG
AGGCGGGAAGCAGAGACAGGCAAGCCTGTCACCTTGAAAGACGTCTTTGGGGCCTACAGC
ATGGATGTGATCACTAGCACATCATTTGGAGTGAACATCGACTCTCTCAACAATCCACAA
GACCCCTTTGTGGAAAACACCAAGAAGCTTTTAAGATTTGATTTTTTGGATCCATTCTTT
CTCTCAATAACAGTCTTTCCATTCCTCATCCCAATTCTTGAAGTATTAAATATCTGTGTG
TTTCCAAGAGAAGTTACAAATTTTTTAAGAAAATCTGTAAAAAGGATGAAAGAAAGTCGC
CTCGAAGATACACAAAAGCACCGAGTGGATTTCCTTCAGCTGATGATTGACTCTCAGAAT
TCAAAAGAAACTGAGTCCCACAAAGCTCTGTCCGATCTGGAGCTCGTGGCCCAATCAATT
ATCTTTATTTTTGCTGGCTGTGAAACCACGAGCAGTGTTCTCTCCTTCATTATGTATGAA
CTGGCCACTCACCCTGATGTCCAGCAGAAACTGCAGGAGGAAATTGATGCAGTTTTACCC
AATAAGGCACCACCCACCTATGATACTGTGCTACAGATGGAGTATCTTGACATGGTGGTG
AATGAAACGCTCAGATTATTCCCAATTGCTATGAGACTTGAGAGGGTCTGCAAAAAAGAT
GTTGAGATCAATGGGATGTTCATTCCCAAAGGGGTGGTGGTGATGATTCCAAGCTATGCT
CTTCACCGTGACCCAAAGTACTGGACAGAGCCTGAGAAGTTCCTCCCTGAAAGATTCAGC
AAGAAGAACAAGGACAACATAGATCCTTACATATACACACCCTTTGGAAGTGGACCCAGA
AACTGCATTGGCATGAGGTTTGCTCTCATGAACATGAAACTTGCTCTAATCAGAGTCCTT
CAGAACTTCTCCTTCAAACCTTGTAAAGAAACACAGATCCCCCTGAAATTAAGCTTAGGA
GGACTTCTTCAACCAGAAAAACCCGTTGTTCTAAAGGTTGAGTCAAGGGATGGCACCGTA
AGTGGAGCCTGA
Enzyme 24 GenBank Gene ID AF182273 Link Image
Enzyme 24 GeneCard ID CYP3A4 Link Image
Enzyme 24 GenAtlas ID CYP3A4 Link Image
Enzyme 24 HGNC ID HGNC:2637 Link Image
Enzyme 24 Chromosome Location 7
Enzyme 24 Locus 7q21.1
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References
  1. Molowa DT, Schuetz EG, Wrighton SA, Watkins PB, Kremers P, Mendez-Picon G, Parker GA, Guzelian PS: Complete cDNA sequence of a cytochrome P-450 inducible by glucocorticoids in human liver. Proc Natl Acad Sci U S A. 1986 Jul;83(14):5311-5. [PubMed Link Image]
  2. Gonzalez FJ, Schmid BJ, Umeno M, Mcbride OW, Hardwick JP, Meyer UA, Gelboin HV, Idle JR: Human P450PCN1: sequence, chromosome localization, and direct evidence through cDNA expression that P450PCN1 is nifedipine oxidase. DNA. 1988 Mar;7(2):79-86. [PubMed Link Image]
  3. Beaune PH, Umbenhauer DR, Bork RW, Lloyd RS, Guengerich FP: Isolation and sequence determination of a cDNA clone related to human cytochrome P-450 nifedipine oxidase. Proc Natl Acad Sci U S A. 1986 Nov;83(21):8064-8. [PubMed Link Image]
  4. Spurr NK, Gough AC, Stevenson K, Wolf CR: The human cytochrome P450 CYP3 locus: assignment to chromosome 7q22-qter. Hum Genet. 1989 Jan;81(2):171-4. [PubMed Link Image]
  5. Bork RW, Muto T, Beaune PH, Srivastava PK, Lloyd RS, Guengerich FP: Characterization of mRNA species related to human liver cytochrome P-450 nifedipine oxidase and the regulation of catalytic activity. J Biol Chem. 1989 Jan 15;264(2):910-9. [PubMed Link Image]
  6. Chen Q, Wu J, Yu Y: [Establishment of transgenic cell line CHL-3A4 and its metabolic activation] Zhonghua Yu Fang Yi Xue Za Zhi. 1998 Sep;32(5):281-4. [PubMed Link Image]
  7. Gellner K, Eiselt R, Hustert E, Arnold H, Koch I, Haberl M, Deglmann CJ, Burk O, Buntefuss D, Escher S, Bishop C, Koebe HG, Brinkmann U, Klenk HP, Kleine K, Meyer UA, Wojnowski L: Genomic organization of the human CYP3A locus: identification of a new, inducible CYP3A gene. Pharmacogenetics. 2001 Mar;11(2):111-21. [PubMed Link Image]
  8. Hsieh KP, Lin YY, Cheng CL, Lai ML, Lin MS, Siest JP, Huang JD: Novel mutations of CYP3A4 in Chinese. Drug Metab Dispos. 2001 Mar;29(3):268-73. [PubMed Link Image]
  9. Komori M, Hashizume T, Ohi H, Miura T, Kitada M, Nagashima K, Kamataki T: Cytochrome P-450 in human liver microsomes: high-performance liquid chromatographic isolation of three forms and their characterization. J Biochem. 1988 Dec;104(6):912-6. [PubMed Link Image]
  10. Watkins PB, Wrighton SA, Maurel P, Schuetz EG, Mendez-Picon G, Parker GA, Guzelian PS: Identification of an inducible form of cytochrome P-450 in human liver. Proc Natl Acad Sci U S A. 1985 Sep;82(18):6310-4. [PubMed Link Image]
  11. Zhang H, Coville PF, Walker RJ, Miners JO, Birkett DJ, Wanwimolruk S: Evidence for involvement of human CYP3A in the 3-hydroxylation of quinine. Br J Clin Pharmacol. 1997 Mar;43(3):245-52. [PubMed Link Image]
  12. Zhao XJ, Kawashiro T, Ishizaki T: Mutual inhibition between quinine and etoposide by human liver microsomes. Evidence for cytochrome P4503A4 involvement in their major metabolic pathways. Drug Metab Dispos. 1998 Feb;26(2):188-91. [PubMed Link Image]
  13. Pabarcus MK, Hoe N, Sadeghi S, Patterson C, Wiertz E, Correia MA: CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases. Arch Biochem Biophys. 2009 Mar 1;483(1):66-74. Epub 2008 Dec 10. [PubMed Link Image]
  14. Yano JK, Wester MR, Schoch GA, Griffin KJ, Stout CD, Johnson EF: The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-A resolution. J Biol Chem. 2004 Sep 10;279(37):38091-4. Epub 2004 Jul 16. [PubMed Link Image]
  15. Williams PA, Cosme J, Vinkovic DM, Ward A, Angove HC, Day PJ, Vonrhein C, Tickle IJ, Jhoti H: Crystal structures of human cytochrome P450 3A4 bound to metyrapone and progesterone. Science. 2004 Jul 30;305(5684):683-6. Epub 2004 Jul 15. [PubMed Link Image]
  16. Sata F, Sapone A, Elizondo G, Stocker P, Miller VP, Zheng W, Raunio H, Crespi CL, Gonzalez FJ: CYP3A4 allelic variants with amino acid substitutions in exons 7 and 12: evidence for an allelic variant with altered catalytic activity. Clin Pharmacol Ther. 2000 Jan;67(1):48-56. [PubMed Link Image]
  17. Dai D, Tang J, Rose R, Hodgson E, Bienstock RJ, Mohrenweiser HW, Goldstein JA: Identification of variants of CYP3A4 and characterization of their abilities to metabolize testosterone and chlorpyrifos. J Pharmacol Exp Ther. 2001 Dec;299(3):825-31. [PubMed Link Image]
  18. Eiselt R, Domanski TL, Zibat A, Mueller R, Presecan-Siedel E, Hustert E, Zanger UM, Brockmoller J, Klenk HP, Meyer UA, Khan KK, He YA, Halpert JR, Wojnowski L: Identification and functional characterization of eight CYP3A4 protein variants. Pharmacogenetics. 2001 Jul;11(5):447-58. [PubMed Link Image]
  19. Lamba JK, Lin YS, Thummel K, Daly A, Watkins PB, Strom S, Zhang J, Schuetz EG: Common allelic variants of cytochrome P4503A4 and their prevalence in different populations. Pharmacogenetics. 2002 Mar;12(2):121-32. [PubMed Link Image]
  20. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 6324
Enzyme 25 Name Cytochrome P450 2C9
Enzyme 25 Synonyms
  1. (R)-limonene 6-monooxygenase
  2. (S)-limonene 6-monooxygenase
  3. (S)-limonene 7-monooxygenase
  4. CYPIIC9
  5. Cytochrome P-450MP
  6. Cytochrome P450 MP-4
  7. Cytochrome P450 MP-8
  8. Cytochrome P450 PB-1
  9. S-mephenytoin 4-hydroxylase
Enzyme 25 Gene Name CYP2C9
Enzyme 25 Protein Sequence >Cytochrome P450 2C9
MDSLVVLVLCLSCLLLLSLWRQSSGRGKLPPGPTPLPVIGNILQIGIKDISKSLTNLSKV
YGPVFTLYFGLKPIVVLHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKW
KEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICS
IIFHKRFDYKDQQFLNLMEKLNENIKILSSPWIQICNNFSPIIDYFPGTHNKLLKNVAFM
KSYILEKVKEHQESMDMNNPQDFIDCFLMKMEKEKHNQPSEFTIESLENTAVDLFGAGTE
TTSTTLRYALLLLLKHPEVTAKVQEEIERVIGRNRSPCMQDRSHMPYTDAVVHEVQRYID
LLPTSLPHAVTCDIKFRNYLIPKGTTILISLTSVLHDNKEFPNPEMFDPHHFLDEGGNFK
KSKYFMPFSAGKRICVGEALAGMELFLFLTSILQNFNLKSLVDPKNLDTTPVVNGFASVP
PFYQLCFIPV
Enzyme 25 Number of Residues 490
Enzyme 25 Molecular Weight 55627.4
Enzyme 25 Theoretical pI 7.99
Enzyme 25 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 25 General Function Involved in monooxygenase activity
Enzyme 25 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. This enzyme contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S- warfarin, diclofenac, phenytoin, tolbutamide and losartan
Enzyme 25 Pathways
Enzyme 25 Reactions
  • (R)-limonene + NADPH + H+ + O2 = (+)-trans-carveol + NADP+ + H2O [RN:R06119]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 32891803 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID P11712 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name CP2C9_HUMAN Link Image
Enzyme 25 PDB ID 1R9O Link Image
Enzyme 25 PDB File Show
Enzyme 25 3D Structure
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >1473 bp
ATGGATTCTCTTGTGGTCCTTGTGCTCTGTCTCTCATGTTTGCTTCTCCTTTCACTCTGG
AGACAGAGCTCTGGGAGAGGAAAACTCCCTCCTGGCCCCACTCCTCTCCCAGTGATTGGA
AATATCCTACAGATAGGTATTAAGGACATCAGCAAATCCTTAACCAATCTCTCAAAGGTC
TATGGCCCTGTGTTCACTCTGTATTTTGGCCTGAAACCCATAGTGGTGCTGCATGGATAT
GAAGCAGTGAAGGAAGCCCTGATTGATCTTGGAGAGGAGTTTTCTGGAAGAGGCATTTTC
CCACTGGCTGAAAGAGCTAACAGAGGATTTGGAATTGTTTTCAGCAATGGAAAGAAATGG
AAGGAGATCCGGCGTTTCTCCCTCATGACGCTGCGGAATTTTGGGATGGGGAAGAGGAGC
ATTGAGGACCGTGTTCAAGAGGAAGCCCGCTGCCTTGTGGAGGAGTTGAGAAAAACCAAG
GCCTCACCCTGTGATCCCACTTTCATCCTGGGCTGTGCTCCCTGCAATGTGATCTGCTCC
ATTATTTTCCATAAACGTTTTGATTATAAAGATCAGCAATTTCTTAACTTAATGGAAAAG
TTGAATGAAAACATCAAGATTTTGAGCAGCCCCTGGATCCAGATCTGCAATAATTTTTCT
CCTATCATTGATTACTTCCCGGGAACTCACAACAAATTACTTAAAAACGTTGCTTTTATG
AAAAGTTATATTTTGGAAAAAGTAAAAGAACACCAAGAATCAATGGACATGAACAACCCT
CAGGACTTTATTGATTGCTTCCTGATGAAAATGGAGAAGGAAAAGCACAACCAACCATCT
GAATTTACTATTGAAAGCTTGGAAAACACTGCAGTTGACTTGTTTGGAGCTGGGACAGAG
ACGACAAGCACAACCCTGAGATATGCTCTCCTTCTCCTGCTGAAGCACCCAGAGGTCACA
GCTAAAGTCCAGGAAGAGATTGAACGTGTGATTGGCAGAAACCGGAGCCCCTGCATGCAA
GACAGGAGCCACATGCCCTACACAGATGCTGTGGTGCACGAGGTCCAGAGATACATTGAC
CTTCTCCCCACCAGCCTGCCCCATGCAGTGACCTGTGACATTAAATTCAGAAACTATCTC
ATTCCCAAGGGCACAACCATATTAATTTCCCTGACTTCTGTGCTACATGACAACAAAGAA
TTTCCCAACCCAGAGATGTTTGACCCTCATCACTTTCTGGATGAAGGTGGCAATTTTAAG
AAAAGTAAATACTTCATGCCTTTCTCAGCAGGAAAACGGATTTGTGTGGGAGAAGCCCTG
GCCGGCATGGAGCTGTTTTTATTCCTGACCTCCATTTTACAGAACTTTAACCTGAAATCT
CTGGTTGACCCAAAGAACCTTGACACCACTCCAGTTGTCAATGGATTTGCCTCTGTGCCG
CCCTTCTACCAGCTGTGCTTCATTCCTGTCTGA
Enzyme 25 GenBank Gene ID AY341248 Link Image
Enzyme 25 GeneCard ID CYP2C9 Link Image
Enzyme 25 GenAtlas ID CYP2C9 Link Image
Enzyme 25 HGNC ID HGNC:2623 Link Image
Enzyme 25 Chromosome Location 1
Enzyme 25 Locus 10q24
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Meehan RR, Gosden JR, Rout D, Hastie ND, Friedberg T, Adesnik M, Buckland R, van Heyningen V, Fletcher J, Spurr NK, et al.: Human cytochrome P-450 PB-1: a multigene family involved in mephenytoin and steroid oxidations that maps to chromosome 10. Am J Hum Genet. 1988 Jan;42(1):26-37. [PubMed Link Image]
  2. Kimura S, Pastewka J, Gelboin HV, Gonzalez FJ: cDNA and amino acid sequences of two members of the human P450IIC gene subfamily. Nucleic Acids Res. 1987 Dec 10;15(23):10053-4. [PubMed Link Image]
  3. Yasumori T, Kawano S, Nagata K, Shimada M, Yamazoe Y, Kato R: Nucleotide sequence of a human liver cytochrome P-450 related to the rat male specific form. J Biochem (Tokyo). 1987 Nov;102(5):1075-82. [PubMed Link Image]
  4. Umbenhauer DR, Martin MV, Lloyd RS, Guengerich FP: Cloning and sequence determination of a complementary DNA related to human liver microsomal cytochrome P-450 S-mephenytoin 4-hydroxylase. Biochemistry. 1987 Feb 24;26(4):1094-9. [PubMed Link Image]
  5. Ged C, Umbenhauer DR, Bellew TM, Bork RW, Srivastava PK, Shinriki N, Lloyd RS, Guengerich FP: Characterization of cDNAs, mRNAs, and proteins related to human liver microsomal cytochrome P-450 (S)-mephenytoin 4'-hydroxylase. Biochemistry. 1988 Sep 6;27(18):6929-40. [PubMed Link Image]
  6. Ohgiya S, Komori M, Ohi H, Shiramatsu K, Shinriki N, Kamataki T: Six-base deletion occurring in messages of human cytochrome P-450 in the CYP2C subfamily results in reduction of tolbutamide hydroxylase activity. Biochem Int. 1992 Sep;27(6):1073-81. [PubMed Link Image]
  7. Shimada T, Misono KS, Guengerich FP: Human liver microsomal cytochrome P-450 mephenytoin 4-hydroxylase, a prototype of genetic polymorphism in oxidative drug metabolism. Purification and characterization of two similar forms involved in the reaction. J Biol Chem. 1986 Jan 15;261(2):909-21. [PubMed Link Image]
  8. Komori M, Hashizume T, Ohi H, Miura T, Kitada M, Nagashima K, Kamataki T: Cytochrome P-450 in human liver microsomes: high-performance liquid chromatographic isolation of three forms and their characterization. J Biochem. 1988 Dec;104(6):912-6. [PubMed Link Image]
  9. Srivastava PK, Yun CH, Beaune PH, Ged C, Guengerich FP: Separation of human liver microsomal tolbutamide hydroxylase and (S)-mephenytoin 4'-hydroxylase cytochrome P-450 enzymes. Mol Pharmacol. 1991 Jul;40(1):69-79. [PubMed Link Image]
  10. Haining RL, Hunter AP, Veronese ME, Trager WF, Rettie AE: Allelic variants of human cytochrome P450 2C9: baculovirus-mediated expression, purification, structural characterization, substrate stereoselectivity, and prochiral selectivity of the wild-type and I359L mutant forms. Arch Biochem Biophys. 1996 Sep 15;333(2):447-58. [PubMed Link Image]
  11. Sandhu P, Baba T, Guengerich FP: Expression of modified cytochrome P450 2C10 (2C9) in Escherichia coli, purification, and reconstitution of catalytic activity. Arch Biochem Biophys. 1993 Nov 1;306(2):443-50. [PubMed Link Image]
  12. Miyazawa M, Shindo M, Shimada T: Metabolism of (+)- and (-)-limonenes to respective carveols and perillyl alcohols by CYP2C9 and CYP2C19 in human liver microsomes. Drug Metab Dispos. 2002 May;30(5):602-7. [PubMed Link Image]
  13. Williams PA, Cosme J, Ward A, Angove HC, Matak Vinkovic D, Jhoti H: Crystal structure of human cytochrome P450 2C9 with bound warfarin. Nature. 2003 Jul 24;424(6947):464-8. Epub 2003 Jul 13. [PubMed Link Image]
  14. Stubbins MJ, Harries LW, Smith G, Tarbit MH, Wolf CR: Genetic analysis of the human cytochrome P450 CYP2C9 locus. Pharmacogenetics. 1996 Oct;6(5):429-39. [PubMed Link Image]
  15. Bhasker CR, Miners JO, Coulter S, Birkett DJ: Allelic and functional variability of cytochrome P4502C9. Pharmacogenetics. 1997 Feb;7(1):51-8. [PubMed Link Image]
  16. Imai J, Ieiri I, Mamiya K, Miyahara S, Furuumi H, Nanba E, Yamane M, Fukumaki Y, Ninomiya H, Tashiro N, Otsubo K, Higuchi S: Polymorphism of the cytochrome P450 (CYP) 2C9 gene in Japanese epileptic patients: genetic analysis of the CYP2C9 locus. Pharmacogenetics. 2000 Feb;10(1):85-9. [PubMed Link Image]
  17. Dickmann LJ, Rettie AE, Kneller MB, Kim RB, Wood AJ, Stein CM, Wilkinson GR, Schwarz UI: Identification and functional characterization of a new CYP2C9 variant (CYP2C9*5) expressed among African Americans. Mol Pharmacol. 2001 Aug;60(2):382-7. [PubMed Link Image]
  18. Higashi MK, Veenstra DL, Kondo LM, Wittkowsky AK, Srinouanprachanh SL, Farin FM, Rettie AE: Association between CYP2C9 genetic variants and anticoagulation-related outcomes during warfarin therapy. JAMA. 2002 Apr 3;287(13):1690-8. [PubMed Link Image]
  19. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 6326
Enzyme 26 Name Cytochrome P450 2C19
Enzyme 26 Synonyms
  1. (R)-limonene 6-monooxygenase
  2. (S)-limonene 6-monooxygenase
  3. (S)-limonene 7-monooxygenase
  4. CYPIIC17
  5. CYPIIC19
  6. Cytochrome P450-11A
  7. Cytochrome P450-254C
  8. Mephenytoin 4-hydroxylase
Enzyme 26 Gene Name CYP2C19
Enzyme 26 Protein Sequence >Cytochrome P450 2C19
MDPFVVLVLCLSCLLLLSIWRQSSGRGKLPPGPTPLPVIGNILQIDIKDVSKSLTNLSKI
YGPVFTLYFGLERMVVLHGYEVVKEALIDLGEEFSGRGHFPLAERANRGFGIVFSNGKRW
KEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICS
IIFQKRFDYKDQQFLNLMEKLNENIRIVSTPWIQICNNFPTIIDYFPGTHNKLLKNLAFM
ESDILEKVKEHQESMDINNPRDFIDCFLIKMEKEKQNQQSEFTIENLVITAADLLGAGTE
TTSTTLRYALLLLLKHPEVTAKVQEEIERVVGRNRSPCMQDRGHMPYTDAVVHEVQRYID
LIPTSLPHAVTCDVKFRNYLIPKGTTILTSLTSVLHDNKEFPNPEMFDPRHFLDEGGNFK
KSNYFMPFSAGKRICVGEGLARMELFLFLTFILQNFNLKSLIDPKDLDTTPVVNGFASVP
PFYQLCFIPV
Enzyme 26 Number of Residues 490
Enzyme 26 Molecular Weight 55930.5
Enzyme 26 Theoretical pI 7.42
Enzyme 26 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 26 General Function Involved in monooxygenase activity
Enzyme 26 Specific Function Responsible for the metabolism of a number of therapeutic agents such as the anticonvulsant drug S-mephenytoin, omeprazole, proguanil, certain barbiturates, diazepam, propranolol, citalopram and imipramine
Enzyme 26 Pathways
Enzyme 26 Reactions
  • (R)-limonene + NADPH + H+ + O2 = (+)-trans-carveol + NADP+ + H2O [RN:R06119]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 181344 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P33261 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name CP2CJ_HUMAN Link Image
Enzyme 26 PDB ID 1R9O Link Image
Enzyme 26 PDB File Show
Enzyme 26 3D Structure
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >1473 bp
ATGGATCCTTTTGTGGTCCTTGTGCTCTGTCTCTCATGTTTGCTTCTCCTTTCAATCTGG
AGACAGAGCTCTGGGAGAGGAAAACTCCCTCCTGGCCCCACTCCTCTCCCAGTGATTGGA
AATATCCTACAGATAGATATTAAGGATGTCAGCAAATCCTTAACCAATCTCTCAAAAATC
TATGGCCCTGTGTTCACTCTGTATTTTGGCCTGGAACGCATGGTGGTGCTGCATGGATAT
GAAGTGGTGAAGGAAGCCCTGATTGATCTTGGAGAGGAGTTTTCTGGAAGAGGCCATTTC
CCACTGGCTGAAAGAGCTAACAGAGGATTTGGAATCGTTTTCAGCAATGGAAAGAGATGG
AAGGAGATCCGGCGTTTCTCCCTCATGACGCTGCGGAATTTTGGGATGGGGAAGAGGAGC
ATTGAGGACCGTGTTCAAGAGGAAGCCCGCTGCCTTGTGGAGGAGTTGAGAAAAACCAAG
GCTTCACCCTGTGATCCCACTTTCATCCTGGGCTGTGCTCCCTGCAATGTGATCTGCTCC
ATTATTTTCCAGAAACGTTTCGATTATAAAGATCAGCAATTTCTTAACTTGATGGAAAAA
TTGAATGAAAACATCAGGATTGTAAGCACCCCCTGGATCCAGATATGCAATAATTTTCCC
ACTATCATTGATTATTTCCCGGGAACCCATAACAAATTACTTAAAAACCTTGCTTTTATG
GAAAGTGATATTTTGGAGAAAGTAAAAGAACACCAAGAATCGATGGACATCAACAACCCT
CGGGACTTTATTGATTGCTTCCTGATCAAAATGGAGAAGGAAAAGCAAAACCAACAGTCT
GAATTCACTATTGAAAACTTGGTAATCACTGCAGCTGACTTACTTGGAGCTGGGACAGAG
ACAACAAGCACAACCCTGAGATATGCTCTCCTTCTCCTGCTGAAGCACCCAGAGGTCACA
GCTAAAGTCCAGGAAGAGATTGAACGTGTCATTGGCAGAAACCGGAGCCCCTGCATGCAG
GACAGGGGCCACATGCCCTACACAGATGCTGTGGTGCACGAGGTCCAGAGATACATCGAC
CTCATCCCCACCAGCCTGCCCCATGCAGTGACCTGTGACGTTAAATTCAGAAACTACCTC
ATTCCCAAGGGCACAACCATATTAACTTCCCTCACTTCTGTGCTACATGACAACAAAGAA
TTTCCCAACCCAGAGATGTTTGACCCTCGTCACTTTCTGGATGAAGGTGGAAATTTTAAG
AAAAGTAACTACTTCATGCCTTTCTCAGCAGGAAAACGGATTTGTGTGGGAGAGGGCCTG
GCCCGCATGGAGCTGTTTTTATTCCTGACCTTCATTTTACAGAACTTTAACCTGAAATCT
CTGATTGACCCAAAGGACCTTGACACAACTCCTGTTGTCAATGGATTTGCTTCTGTCCCG
CCCTTCTATCAGCTGTGCTTCATTCCTGTCTGA
Enzyme 26 GenBank Gene ID M61854 Link Image
Enzyme 26 GeneCard ID CYP2C19 Link Image
Enzyme 26 GenAtlas ID CYP2C19 Link Image
Enzyme 26 HGNC ID HGNC:2621 Link Image
Enzyme 26 Chromosome Location 1
Enzyme 26 Locus 10q24.1-q24.3
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Romkes M, Faletto MB, Blaisdell JA, Raucy JL, Goldstein JA: Cloning and expression of complementary DNAs for multiple members of the human cytochrome P450IIC subfamily. Biochemistry. 1991 Apr 2;30(13):3247-55. [PubMed Link Image]
  2. Romkes M, Faletto MB, Blaisdell JA, Raucy JL, Goldstein JA: Cloning and expression of complementary DNAs for multiple members of the human cytochrome PH50IIC subfamily. Biochemistry. 1993 Feb 9;32(5):1390. [PubMed Link Image]
  3. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  4. Wrighton SA, Stevens JC, Becker GW, VandenBranden M: Isolation and characterization of human liver cytochrome P450 2C19: correlation between 2C19 and S-mephenytoin 4'-hydroxylation. Arch Biochem Biophys. 1993 Oct;306(1):240-5. [PubMed Link Image]
  5. Miyazawa M, Shindo M, Shimada T: Metabolism of (+)- and (-)-limonenes to respective carveols and perillyl alcohols by CYP2C9 and CYP2C19 in human liver microsomes. Drug Metab Dispos. 2002 May;30(5):602-7. [PubMed Link Image]
  6. de Morais SM, Wilkinson GR, Blaisdell J, Nakamura K, Meyer UA, Goldstein JA: The major genetic defect responsible for the polymorphism of S-mephenytoin metabolism in humans. J Biol Chem. 1994 Jun 3;269(22):15419-22. [PubMed Link Image]
  7. De Morais SM, Wilkinson GR, Blaisdell J, Meyer UA, Nakamura K, Goldstein JA: Identification of a new genetic defect responsible for the polymorphism of (S)-mephenytoin metabolism in Japanese. Mol Pharmacol. 1994 Oct;46(4):594-8. [PubMed Link Image]
  8. Xiao ZS, Goldstein JA, Xie HG, Blaisdell J, Wang W, Jiang CH, Yan FX, He N, Huang SL, Xu ZH, Zhou HH: Differences in the incidence of the CYP2C19 polymorphism affecting the S-mephenytoin phenotype in Chinese Han and Bai populations and identification of a new rare CYP2C19 mutant allele. J Pharmacol Exp Ther. 1997 Apr;281(1):604-9. [PubMed Link Image]
  9. Ibeanu GC, Goldstein JA, Meyer U, Benhamou S, Bouchardy C, Dayer P, Ghanayem BI, Blaisdell J: Identification of new human CYP2C19 alleles (CYP2C19*6 and CYP2C19*2B) in a Caucasian poor metabolizer of mephenytoin. J Pharmacol Exp Ther. 1998 Sep;286(3):1490-5. [PubMed Link Image]
  10. Ibeanu GC, Blaisdell J, Ghanayem BI, Beyeler C, Benhamou S, Bouchardy C, Wilkinson GR, Dayer P, Daly AK, Goldstein JA: An additional defective allele, CYP2C19*5, contributes to the S-mephenytoin poor metabolizer phenotype in Caucasians. Pharmacogenetics. 1998 Apr;8(2):129-35. [PubMed Link Image]
  11. Ibeanu GC, Blaisdell J, Ferguson RJ, Ghanayem BI, Brosen K, Benhamou S, Bouchardy C, Wilkinson GR, Dayer P, Goldstein JA: A novel transversion in the intron 5 donor splice junction of CYP2C19 and a sequence polymorphism in exon 3 contribute to the poor metabolizer phenotype for the anticonvulsant drug S-mephenytoin. J Pharmacol Exp Ther. 1999 Aug;290(2):635-40. [PubMed Link Image]
  12. Blaisdell J, Mohrenweiser H, Jackson J, Ferguson S, Coulter S, Chanas B, Xi T, Ghanayem B, Goldstein JA: Identification and functional characterization of new potentially defective alleles of human CYP2C19. Pharmacogenetics. 2002 Dec;12(9):703-11. [PubMed Link Image]
  13. Morita J, Kobayashi K, Wanibuchi A, Kimura M, Irie S, Ishizaki T, Chiba K: A novel single nucleotide polymorphism (SNP) of the CYP2C19 gene in a Japanese subject with lowered capacity of mephobarbital 4'-hydroxylation. Drug Metab Pharmacokinet. 2004 Jun;19(3):236-8. [PubMed Link Image]
  14. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
  15. Fukushima-Uesaka H, Saito Y, Maekawa K, Ozawa S, Hasegawa R, Kajio H, Kuzuya N, Yasuda K, Kawamoto M, Kamatani N, Suzuki K, Yanagawa T, Tohkin M, Sawada J: Genetic variations and haplotypes of CYP2C19 in a Japanese population. Drug Metab Pharmacokinet. 2005 Aug;20(4):300-7. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 6840
Enzyme 27 Name Cytochrome P450 2E1
Enzyme 27 Synonyms
  1. 4-nitrophenol 2-hydroxylase
  2. CYPIIE1
  3. Cytochrome P450-J
Enzyme 27 Gene Name CYP2E1
Enzyme 27 Protein Sequence >Cytochrome P450 2E1
MSALGVTVALLVWAAFLLLVSMWRQVHSSWNLPPGPFPLPIIGNLFQLELKNIPKSFTRL
AQRFGPVFTLYVGSQRMVVMHGYKAVKEALLDYKDEFSGRGDLPAFHAHRDRGIIFNNGP
TWKDIRRFSLTTLRNYGMGKQGNESRIQREAHFLLEALRKTQGQPFDPTFLIGCAPCNVI
ADILFRKHFDYNDEKFLRLMYLFNENFHLLSTPWLQLYNNFPSFLHYLPGSHRKVIKNVA
EVKEYVSERVKEHHQSLDPNCPRDLTDCLLVEMEKEKHSAERLYTMDGITVTVADLFFAG
TETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRIPAIKDRQEMPYMDAVVHEIQRF
ITLVPSNLPHEATRDTIFRGYLIPKGTVVVPTLDSVLYDNQEFPDPEKFKPEHFLNENGK
FKYSDYFKPFSTGKRVCAGEGLARMELFLLLCAILQHFNLKPLVDPKDIDLSPIHIGFGC
IPPRYKLCVIPRS
Enzyme 27 Number of Residues 493
Enzyme 27 Molecular Weight 56848.4
Enzyme 27 Theoretical pI 8.22
Enzyme 27 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 27 General Function Involved in monooxygenase activity
Enzyme 27 Specific Function Metabolizes several precarcinogens, drugs, and solvents to reactive metabolites. Inactivates a number of drugs and xenobiotics and also bioactivates many xenobiotic substrates to their hepatotoxic or carcinogenic forms
Enzyme 27 Pathways
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein Not Available
Enzyme 27 UniProtKB/Swiss-Prot ID P05181 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name CP2E1_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >1482 bp
ATGTCTGCCCTCGGAGTGACCGTGGCCCTGCTGGTGTGGGCGGCCTTCCTCCTGCTGGTG
TCCATGTGGAGGCAGGTGCACAGCAGCTGGAATCTGCCCCCAGGTCCTTTCCCGCTTCCC
ATCATCGGGAACCTCTTCCAGTTGGAATTGAAGAATATTCCCAAGTCCTTCACCCGGTTG
GCCCAGCGCTTCGGGCCGGTGTTCACGCTGTACGTGGGCTCGCAGCGCATGGTGGTGATG
CACGGCTACAAGGCGGTGAAGGAAGCGCTGCTGGACTACAAGGACGAGTTCTCGGGCAGA
GGCGACCTCCCCGCGTTCCATGCGCACAGGGACAGGGGAATCATTTTTAATAATGGACCT
ACCTGGAAGGACATCCGGCGGTTTTCCCTGACCACCCTCCGGAACTATGGGATGGGGAAA
CAGGGCAATGAGAGCCGGATCCAGAGGGAGGCCCACTTCCTGCTGGAAGCACTCAGGAAG
ACCCAAGGCCAGCCTTTCGACCCCACCTTCCTCATCGGCTGCGCGCCCTGCAACGTCATA
GCCGACATCCTCTTCCGCAAGCATTTTGACTACAATGATGAGAAGTTTCTAAGGCTGATG
TATTTGTTTAATGAGAACTTCCACCTACTCAGCACTCCCTGGCTCCAGCTTTACAATAAT
TTTCCCAGCTTTCTACACTACTTGCCTGGAAGCCACAGAAAAGTCATAAAAAATGTGGCT
GAAGTAAAAGAGTATGTGTCTGAAAGGGTGAAGGAGCACCATCAATCTCTGGACCCCAAC
TGTCCCCGGGACCTCACCGACTGCCTGCTCGTGGAAATGGAGAAGGAAAAGCACAGTGCA
GAGCGCTTGTACACAATGGACGGTATCACCGTGACTGTGGCCGACCTGTTCTTTGCGGGG
ACAGAGACCACCAGCACAACTCTGAGATATGGGCTCCTGATTCTCATGAAATACCCTGAG
ATCGAAGAGAAGCTCCATGAAGAAATTGACAGGGTGATTGGGCCAAGCCGAATCCCTGCC
ATCAAGGATAGGCAAGAGATGCCCTACATGGATGCTGTGGTGCATGAGATTCAGCGGTTC
ATCACCCTCGTGCCCTCCAACCTGCCCCATGAAGCAACCCGAGACACCATTTTCAGAGGA
TACCTCATCCCCAAGGGCACAGTCGTAGTGCCAACTCTGGACTCTGTTTTGTATGACAAC
CAAGAATTTCCTGATCCAGAAAAGTTTAAGCCAGAACACTTCCTGAATGAAAATGGAAAG
TTCAAGTACAGTGACTATTTCAAGCCATTTTCCACAGGAAAACGAGTGTGTGCTGGAGAA
GGCCTGGCTCGCATGGAGTTGTTTCTTTTGTTGTGTGCCATTTTGCAGCATTTTAATTTG
AAGCCTCTCGTTGACCCAAAGGATATCGACCTCAGCCCTATACATATTGGGTTTGGCTGT
ATCCCACCACGTTACAAACTCTGTGTCATTCCCCGCTCATGA
Enzyme 27 GenBank Gene ID J02625 Link Image
Enzyme 27 GeneCard ID CYP2E1 Link Image
Enzyme 27 GenAtlas ID CYP2E1 Link Image
Enzyme 27 HGNC ID HGNC:2631 Link Image
Enzyme 27 Chromosome Location 1
Enzyme 27 Locus 10q24.3-qter
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Song BJ, Gelboin HV, Park SS, Yang CS, Gonzalez FJ: Complementary DNA and protein sequences of ethanol-inducible rat and human cytochrome P-450s. Transcriptional and post-transcriptional regulation of the rat enzyme. J Biol Chem. 1986 Dec 15;261(35):16689-97. [PubMed Link Image]
  2. Umeno M, McBride OW, Yang CS, Gelboin HV, Gonzalez FJ: Human ethanol-inducible P450IIE1: complete gene sequence, promoter characterization, chromosome mapping, and cDNA-directed expression. Biochemistry. 1988 Dec 13;27(25):9006-13. [PubMed Link Image]
  3. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  4. Lasker JM, Raucy J, Kubota S, Bloswick BP, Black M, Lieber CS: Purification and characterization of human liver cytochrome P-450-ALC. Biochem Biophys Res Commun. 1987 Oct 14;148(1):232-8. [PubMed Link Image]
  5. Robinson RC, Shorr RG, Varrichio A, Park SS, Gelboin HV, Miller H, Friedman FK: Human liver cytochrome P-450 related to a rat acetone-inducible, nitrosamine-metabolizing cytochrome P-450: identification and isolation. Pharmacology. 1989;39(3):137-44. [PubMed Link Image]
  6. Gillam EM, Guo Z, Guengerich FP: Expression of modified human cytochrome P450 2E1 in Escherichia coli, purification, and spectral and catalytic properties. Arch Biochem Biophys. 1994 Jul;312(1):59-66. [PubMed Link Image]
  7. Zerilli A, Ratanasavanh D, Lucas D, Goasduff T, Dreano Y, Menard C, Picart D, Berthou F: Both cytochromes P450 2E1 and 3A are involved in the O-hydroxylation of p-nitrophenol, a catalytic activity known to be specific for P450 2E1. Chem Res Toxicol. 1997 Oct;10(10):1205-12. [PubMed Link Image]
  8. Porubsky PR, Meneely KM, Scott EE: Structures of human cytochrome P-450 2E1. Insights into the binding of inhibitors and both small molecular weight and fatty acid substrates. J Biol Chem. 2008 Nov 28;283(48):33698-707. Epub 2008 Sep 24. [PubMed Link Image]
  9. Hu Y, Oscarson M, Johansson I, Yue QY, Dahl ML, Tabone M, Arinco S, Albano E, Ingelman-Sundberg M: Genetic polymorphism of human CYP2E1: characterization of two variant alleles. Mol Pharmacol. 1997 Mar;51(3):370-6. [PubMed Link Image]
  10. Fairbrother KS, Grove J, de Waziers I, Steimel DT, Day CP, Crespi CL, Daly AK: Detection and characterization of novel polymorphisms in the CYP2E1 gene. Pharmacogenetics. 1998 Dec;8(6):543-52. [PubMed Link Image]
  11. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 6843
Enzyme 28 Name Cytochrome P450 1B1
Enzyme 28 Synonyms
  1. CYPIB1
Enzyme 28 Gene Name CYP1B1
Enzyme 28 Protein Sequence >Cytochrome P450 1B1
MGTSLSPNDPWPLNPLSIQQTTLLLLLSVLATVHVGQRLLRQRRRQLRSAPPGPFAWPLI
GNAAAVGQAAHLSFARLARRYGDVFQIRLGSCPIVVLNGERAIHQALVQQGSAFADRPAF
ASFRVVSGGRSMAFGHYSEHWKVQRRAAHSMMRNFFTRQPRSRQVLEGHVLSEARELVAL
LVRGSADGAFLDPRPLTVVAVANVMSAVCFGCRYSHDDPEFRELLSHNEEFGRTVGAGSL
VDVMPWLQYFPNPVRTVFREFEQLNRNFSNFILDKFLRHCESLRPGAAPRDMMDAFILSA
EKKAAGDSHGGGARLDLENVPATITDIFGASQDTLSTALQWLLLLFTRYPDVQTRVQAEL
DQVVGRDRLPCMGDQPNLPYVLAFLYEAMRFSSFVPVTIPHATTANTSVLGYHIPKDTVV
FVNQWSVNHDPLKWPNPENFDPARFLDKDGLINKDLTSRVMIFSVGKRRCIGEELSKMQL
FLFISILAHQCDFRANPNEPAKMNFSYGLTIKPKSFKVNVTLRESMELLDSAVQNLQAKE
TCQ
Enzyme 28 Number of Residues 543
Enzyme 28 Molecular Weight 60845.3
Enzyme 28 Theoretical pI 9.23
Enzyme 28 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 28 General Function Involved in monooxygenase activity
Enzyme 28 Specific Function Participates in the metabolism of an as-yet-unknown biologically active molecule that is a participant in eye development
Enzyme 28 Pathways
Enzyme 28 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 501031 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID Q16678 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name CP1B1_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >1632 bp
ATGGGCACCAGCCTCAGCCCGAACGACCCTTGGCCGCTAAACCCGCTGTCCATCCAGCAG
ACCACGCTCCTGCTACTCCTGTCGGTGCTGGCCACTGTGCATGTGGGCCAGCGGCTGCTG
AGGCAACGGAGGCGGCAGCTCCGGTCCGCGCCCCCGGGCCCGTTTGCGTGGCCACTGATC
GGAAACGCGGCGGCGGTGGGCCAGGCGGCTCACCTCTCGTTCGCTCGCCTGGCGCGGCGC
TACGGCGACGTTTTCCAGATCCGCCTGGGCAGCTGCCCCATAGTGGTGCTGAATGGCGAG
CGCGCCATCCACCAGGCCCTGGTGCAGCAGGGCTCGGCCTTCGCCGACCGGCCGGCCTTC
GCCTCCTTCCGTGTGGTGTCCGGCGGCCGCAGCATGGCTTTCGGCCACTACTCGGAGCAC
TGGAAGGTGCAGCGGCGCGCAGCCCACAGCATGATGCGCAACTTCTTCACGCGCCAGCCG
CGCAGCCGCCAAGTCCTCGAGGGCCACGTGCTGAGCGAGGCGCGCGAGCTGGTGGCGCTG
CTGGTGCGCGGCAGCGCGGACGGCGCCTTCCTCGACCCGAGGCCGCTGACCGTCGTGGCC
GTGGCCAACGTCATGAGTGCCGTGTGTTTCGGCTGCCGCTACAGCCACGACGACCCCGAG
TTCCGTGAGCTGCTCAGCCACAACGAAGAGTTCGGGCGCACGGTGGGCGCGGGCAGCCTG
GTGGACGTGATGCCCTGGCTGCAGTACTTCCCCAACCCGGTGCGCACCGTTTTCCGCGAA
TTCGAGCAGCTCAACCGCAACTTCAGCAACTTCATCCTGGACAAGTTCTTGAGGCACTGC
GAAAGCCTTCGGCCCGGGGCCGCCCCCCGCGACATGATGGACGCCTTTATCCTCTCTGCG
GAAAAGAAGGCGGCCGGGGACTCGCACGGTGGTGGCGCGCGGCTGGATTTGGAGAACGTA
CCGGCCACTATCACTGACATCTTCGGCGCCAGCCAGGACACCCTGTCCACCGCGCTGCAG
TGGCTGCTCCTCCTCTTCACCAGGTATCCTGATGTGCAGACTCGAGTGCAGGCAGAATTG
GATCAGGTCGTGGGGAGGGACCGTCTGCCTTGTATGGGTGACCAGCCCAACCTGCCCTAT
GTCCTGGCCTTCCTTTATGAAGCCATGCGCTTCTCCAGCTTTGTGCCTGTCACTATTCCT
CATGCCACCACTGCCAACACCTCTGTCTTGGGCTACCACATTCCCAAGGACACTGTGGTT
TTTGTCAACCAGTGGTCTGTGAATCATGACCCAGTGAAGTGGCCTAACCCGGAGAACTTT
GATCCAGCTCGATTCTTGGACAAGGATGGCCTCATCAACAAGGACCTGACCAGCAGAGTG
ATGATTTTTTCAGTGGGCAAAAGGCGGTGCATTGGCGAAGAACTTTCTAAGATGCAGCTT
TTTCTCTTCATCTCCATCCTGGCTCACCAGTGCGATTTCAGGGCCAACCCAAATGAGCCT
GCGAAAATGAATTTCAGTTATGGTCTAACCATTAAACCCAAGTCATTTAAAGTCAATGTC
ACTCTCAGAGAGTCCATGGAGCTCCTTGATAGTGCTGTCCAAAATTTACAAGCCAAGGAA
ACTTGCCAATAA
Enzyme 28 GenBank Gene ID U03688 Link Image
Enzyme 28 GeneCard ID CYP1B1 Link Image
Enzyme 28 GenAtlas ID CYP1B1 Link Image
Enzyme 28 HGNC ID HGNC:2597 Link Image
Enzyme 28 Chromosome Location 2
Enzyme 28 Locus 2p21
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Sutter TR, Tang YM, Hayes CL, Wo YY, Jabs EW, Li X, Yin H, Cody CW, Greenlee WF: Complete cDNA sequence of a human dioxin-inducible mRNA identifies a new gene subfamily of cytochrome P450 that maps to chromosome 2. J Biol Chem. 1994 May 6;269(18):13092-9. [PubMed Link Image]
  2. Tang YM, Wo YY, Stewart J, Hawkins AL, Griffin CA, Sutter TR, Greenlee WF: Isolation and characterization of the human cytochrome P450 CYP1B1 gene. J Biol Chem. 1996 Nov 8;271(45):28324-30. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Bejjani BA, Lewis RA, Tomey KF, Anderson KL, Dueker DK, Jabak M, Astle WF, Otterud B, Leppert M, Lupski JR: Mutations in CYP1B1, the gene for cytochrome P4501B1, are the predominant cause of primary congenital glaucoma in Saudi Arabia. Am J Hum Genet. 1998 Feb;62(2):325-33. [PubMed Link Image]
  5. Stoilov I, Akarsu AN, Alozie I, Child A, Barsoum-Homsy M, Turacli ME, Or M, Lewis RA, Ozdemir N, Brice G, Aktan SG, Chevrette L, Coca-Prados M, Sarfarazi M: Sequence analysis and homology modeling suggest that primary congenital glaucoma on 2p21 results from mutations disrupting either the hinge region or the conserved core structures of cytochrome P4501B1. Am J Hum Genet. 1998 Mar;62(3):573-84. [PubMed Link Image]
  6. Bailey LR, Roodi N, Dupont WD, Parl FF: Association of cytochrome P450 1B1 (CYP1B1) polymorphism with steroid receptor status in breast cancer. Cancer Res. 1998 Nov 15;58(22):5038-41. [PubMed Link Image]
  7. Shimada T, Watanabe J, Kawajiri K, Sutter TR, Guengerich FP, Gillam EM, Inoue K: Catalytic properties of polymorphic human cytochrome P450 1B1 variants. Carcinogenesis. 1999 Aug;20(8):1607-13. [PubMed Link Image]
  8. Plasilova M, Stoilov I, Sarfarazi M, Kadasi L, Ferakova E, Ferak V: Identification of a single ancestral CYP1B1 mutation in Slovak Gypsies (Roms) affected with primary congenital glaucoma. J Med Genet. 1999 Apr;36(4):290-4. [PubMed Link Image]
  9. Bejjani BA, Stockton DW, Lewis RA, Tomey KF, Dueker DK, Jabak M, Astle WF, Lupski JR: Multiple CYP1B1 mutations and incomplete penetrance in an inbred population segregating primary congenital glaucoma suggest frequent de novo events and a dominant modifier locus. Hum Mol Genet. 2000 Feb 12;9(3):367-74. [PubMed Link Image]
  10. Ohtake Y, Kubota R, Tanino T, Miyata H, Mashima Y: Novel compound heterozygous mutations in the cytochrome P4501B1 gene (CYP1B1) in a Japanese patient with primary congenital glaucoma. Ophthalmic Genet. 2000 Sep;21(3):191-3. [PubMed Link Image]
  11. Watanabe J, Shimada T, Gillam EM, Ikuta T, Suemasu K, Higashi Y, Gotoh O, Kawajiri K: Association of CYP1B1 genetic polymorphism with incidence to breast and lung cancer. Pharmacogenetics. 2000 Feb;10(1):25-33. [PubMed Link Image]
  12. Mashima Y, Suzuki Y, Sergeev Y, Ohtake Y, Tanino T, Kimura I, Miyata H, Aihara M, Tanihara H, Inatani M, Azuma N, Iwata T, Araie M: Novel cytochrome P4501B1 (CYP1B1) gene mutations in Japanese patients with primary congenital glaucoma. Invest Ophthalmol Vis Sci. 2001 Sep;42(10):2211-6. [PubMed Link Image]
  13. Vincent AL, Billingsley G, Buys Y, Levin AV, Priston M, Trope G, Williams-Lyn D, Heon E: Digenic inheritance of early-onset glaucoma: CYP1B1, a potential modifier gene. Am J Hum Genet. 2002 Feb;70(2):448-60. Epub 2002 Jan 3. [PubMed Link Image]
  14. Panicker SG, Reddy AB, Mandal AK, Ahmed N, Nagarajaram HA, Hasnain SE, Balasubramanian D: Identification of novel mutations causing familial primary congenital glaucoma in Indian pedigrees. Invest Ophthalmol Vis Sci. 2002 May;43(5):1358-66. [PubMed Link Image]
  15. Stoilov IR, Costa VP, Vasconcellos JP, Melo MB, Betinjane AJ, Carani JC, Oltrogge EV, Sarfarazi M: Molecular genetics of primary congenital glaucoma in Brazil. Invest Ophthalmol Vis Sci. 2002 Jun;43(6):1820-7. [PubMed Link Image]
  16. Aklillu E, Oscarson M, Hidestrand M, Leidvik B, Otter C, Ingelman-Sundberg M: Functional analysis of six different polymorphic CYP1B1 enzyme variants found in an Ethiopian population. Mol Pharmacol. 2002 Mar;61(3):586-94. [PubMed Link Image]
  17. Chakrabarti S, Komatireddy S, Mandal AK, Balasubramanian D: Gene symbol: CYP1B1. Disease: glaucoma, primary congenital. Hum Genet. 2003 Nov;113(6):556. [PubMed Link Image]
  18. Colomb E, Kaplan J, Garchon HJ: Novel cytochrome P450 1B1 (CYP1B1) mutations in patients with primary congenital glaucoma in France. Hum Mutat. 2003 Dec;22(6):496. [PubMed Link Image]
  19. Sitorus R, Ardjo SM, Lorenz B, Preising M: CYP1B1 gene analysis in primary congenital glaucoma in Indonesian and European patients. J Med Genet. 2003 Jan;40(1):e9. [PubMed Link Image]
  20. Melki R, Colomb E, Lefort N, Brezin AP, Garchon HJ: CYP1B1 mutations in French patients with early-onset primary open-angle glaucoma. J Med Genet. 2004 Sep;41(9):647-51. [PubMed Link Image]
  21. Reddy AB, Kaur K, Mandal AK, Panicker SG, Thomas R, Hasnain SE, Balasubramanian D, Chakrabarti S: Mutation spectrum of the CYP1B1 gene in Indian primary congenital glaucoma patients. Mol Vis. 2004 Sep 30;10:696-702. [PubMed Link Image]
  22. Curry SM, Daou AG, Hermanns P, Molinari A, Lewis RA, Bejjani BA: Cytochrome P4501B1 mutations cause only part of primary congenital glaucoma in Ecuador. Ophthalmic Genet. 2004 Mar;25(1):3-9. [PubMed Link Image]
  23. Alfadhli S, Behbehani A, Elshafey A, Abdelmoaty S, Al-Awadi S: Molecular and clinical evaluation of primary congenital glaucoma in Kuwait. Am J Ophthalmol. 2006 Mar;141(3):512-6. [PubMed Link Image]
  24. Acharya M, Mookherjee S, Bhattacharjee A, Bandyopadhyay AK, Daulat Thakur SK, Bhaduri G, Sen A, Ray K: Primary role of CYP1B1 in Indian juvenile-onset POAG patients. Mol Vis. 2006 Apr 20;12:399-404. [PubMed Link Image]
  25. Chavarria-Soley G, Michels-Rautenstrauss K, Pasutto F, Flikier D, Flikier P, Cirak S, Bejjani B, Winters DL, Lewis RA, Mardin C, Reis A, Rautenstrauss B: Primary congenital glaucoma and Rieger's anomaly: extended haplotypes reveal founder effects for eight distinct CYP1B1 mutations. Mol Vis. 2006 May 22;12:523-31. [PubMed Link Image]
  26. Lopez-Garrido MP, Sanchez-Sanchez F, Lopez-Martinez F, Aroca-Aguilar JD, Blanco-Marchite C, Coca-Prados M, Escribano J: Heterozygous CYP1B1 gene mutations in Spanish patients with primary open-angle glaucoma. Mol Vis. 2006 Jul 11;12:748-55. [PubMed Link Image]
  27. Chavarria-Soley G, Sticht H, Aklillu E, Ingelman-Sundberg M, Pasutto F, Reis A, Rautenstrauss B: Mutations in CYP1B1 cause primary congenital glaucoma by reduction of either activity or abundance of the enzyme. Hum Mutat. 2008 Sep;29(9):1147-53. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 6845
Enzyme 29 Name Cytochrome P450 2C18
Enzyme 29 Synonyms
  1. CYPIIC18
  2. Cytochrome P450-6b/29c
Enzyme 29 Gene Name CYP2C18
Enzyme 29 Protein Sequence >Cytochrome P450 2C18
MDPAVALVLCLSCLFLLSLWRQSSGRGRLPSGPTPLPIIGNILQLDVKDMSKSLTNFSKV
YGPVFTVYFGLKPIVVLHGYEAVKEALIDHGEEFSGRGSFPVAEKVNKGLGILFSNGKRW
KEIRRFCLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTNASPCDPTFILGCAPCNVICS
VIFHDRFDYKDQRFLNLMEKFNENLRILSSPWIQVCNNFPALIDYLPGSHNKIAENFAYI
KSYVLERIKEHQESLDMNSARDFIDCFLIKMEQEKHNQQSEFTVESLIATVTDMFGAGTE
TTSTTLRYGLLLLLKYPEVTAKVQEEIECVVGRNRSPCMQDRSHMPYTDAVVHEIQRYID
LLPTNLPHAVTCDVKFKNYLIPKGTTIITSLTSVLHNDKEFPNPEMFDPGHFLDKSGNFK
KSDYFMPFSAGKRMCMGEGLARMELFLFLTTILQNFNLKSQVDPKDIDITPIANAFGRVP
PLYQLCFIPV
Enzyme 29 Number of Residues 490
Enzyme 29 Molecular Weight 55710.1
Enzyme 29 Theoretical pI 7.22
Enzyme 29 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 29 General Function Involved in monooxygenase activity
Enzyme 29 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics
Enzyme 29 Pathways
Enzyme 29 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 189066652 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID P33260 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name CP2CI_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >1473 bp
ATGGATCCAGCTGTGGCTCTGGTGCTCTGTCTCTCCTGTTTGTTTCTCCTTTCACTCTGG
AGGCAGAGCTCTGGAAGAGGGAGGCTCCCGTCTGGCCCCACTCCTCTCCCGATTATTGGA
AATATCCTGCAGTTAGATGTTAAGGACATGAGCAAATCCTTAACCAATTTCTCAAAAGTC
TATGGCCCTGTGTTCACTGTGTATTTTGGCCTGAAGCCCATTGTGGTGTTGCATGGATAT
GAAGCAGTGAAGGAGGCCCTGATTGATCATGGAGAGGAGTTTTCTGGAAGAGGAAGTTTT
CCAGTGGCTGAAAAAGTTAACAAAGGACTTGGAATCCTTTTCAGCAATGGAAAGAGATGG
AAGGAGATCCGGCGTTTCTGCCTCATGACTCTGCGGAATTTTGGGATGGGGAAGAGGAGC
ATCGAGGACCGTGTTCAAGAGGAAGCCCGCTGCCTTGTGGAGGAGTTGAGAAAAACCAAT
GCCTCACCCTGTGATCCCACTTTCATCCTGGGCTGTGCTCCCTGCAATGTGATCTGCTCT
GTTATTTTCCATGATCGATTTGATTATAAAGATCAGAGGTTTCTTAACTTGATGGAAAAA
TTCAATGAAAACCTCAGGATTCTGAGCTCTCCATGGATCCAGGTCTGCAATAATTTCCCT
GCTCTCATCGATTATCTCCCAGGAAGTCATAATAAAATAGCTGAAAATTTTGCTTACATT
AAAAGTTATGTATTGGAGAGAATAAAAGAACATCAAGAATCCCTGGACATGAACAGTGCT
CGGGACTTTATTGATTGTTTCCTGATCAAAATGGAACAGGAAAAGCACAATCAACAGTCT
GAATTTACTGTTGAAAGCTTGATAGCCACTGTAACTGATATGTTTGGGGCTGGAACAGAG
ACAACGAGCACCACTCTGAGATATGGACTCCTGCTCCTGCTGAAGTACCCAGAGGTCACA
GCTAAAGTCCAGGAAGAGATTGAATGTGTAGTTGGCAGAAACCGGAGCCCCTGTATGCAG
GACAGGAGTCACATGCCCTACACAGATGCTGTGGTGCACGAGATCCAGAGATACATTGAC
CTCCTCCCCACCAACCTGCCCCATGCAGTGACCTGTGATGTTAAATTCAAAAACTACCTC
ATCCCCAAGGGCACGACCATAATAACATCCCTGACTTCTGTGCTGCACAATGACAAAGAA
TTCCCCAACCCAGAGATGTTTGACCCTGGCCACTTTCTGGATAAGAGTGGCAACTTTAAG
AAAAGTGACTACTTCATGCCTTTCTCAGCAGGAAAACGGATGTGTATGGGAGAGGGCCTG
GCCCGCATGGAGCTGTTTTTATTCCTGACCACCATTTTGCAGAACTTTAACCTGAAATCT
CAGGTTGACCCAAAGGATATTGACATCACCCCCATTGCCAATGCATTTGGTCGTGTGCCA
CCCTTGTACCAGCTCTGCTTCATTCCTGTCTGA
Enzyme 29 GenBank Gene ID AK313403 Link Image
Enzyme 29 GeneCard ID CYP2C18 Link Image
Enzyme 29 GenAtlas ID CYP2C18 Link Image
Enzyme 29 HGNC ID HGNC:2620 Link Image
Enzyme 29 Chromosome Location 1
Enzyme 29 Locus 10q24
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 General References
  1. Romkes M, Faletto MB, Blaisdell JA, Raucy JL, Goldstein JA: Cloning and expression of complementary DNAs for multiple members of the human cytochrome P450IIC subfamily. Biochemistry. 1991 Apr 2;30(13):3247-55. [PubMed Link Image]
  2. Romkes M, Faletto MB, Blaisdell JA, Raucy JL, Goldstein JA: Cloning and expression of complementary DNAs for multiple members of the human cytochrome PH50IIC subfamily. Biochemistry. 1993 Feb 9;32(5):1390. [PubMed Link Image]
  3. de Morais SM, Schweikl H, Blaisdell J, Goldstein JA: Gene structure and upstream regulatory regions of human CYP2C9 and CYP2C18. Biochem Biophys Res Commun. 1993 Jul 15;194(1):194-201. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  8. Archbold JK, Macdonald WA, Miles JJ, Brennan RM, Kjer-Nielsen L, McCluskey J, Burrows SR, Rossjohn J: Alloreactivity between disparate cognate and allogeneic pMHC-I complexes is the result of highly focused, peptide-dependent structural mimicry. J Biol Chem. 2006 Nov 10;281(45):34324-32. Epub 2006 Sep 8. [PubMed Link Image]
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 6847
Enzyme 30 Name Cytochrome P450 2F1
Enzyme 30 Synonyms
  1. CYPIIF1
Enzyme 30 Gene Name CYP2F1
Enzyme 30 Protein Sequence >Cytochrome P450 2F1
MDSISTAILLLLLALVCLLLTLSSRDKGKLPPGPRPLSILGNLLLLCSQDMLTSLTKLSK
EYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDR
WKVLRQFSIQILRNFGMGKRSIEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIIC
SVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFPSLLDWVPGPHQRIFQNFKC
LRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGT
KTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFA
DIIPMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSF
KKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQPLGAPEDIDLTPLSSGLGNL
PRPFQLCLRPR
Enzyme 30 Number of Residues 491
Enzyme 30 Molecular Weight 55500.6
Enzyme 30 Theoretical pI 7.40
Enzyme 30 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxygen binding
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 30 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 30 Specific Function May be involved in the metabolism of various pneumotoxicants including naphthalene. Is able to dealkylate ethoxycoumarin, propoxycoumarin, and pentoxyresorufin but possesses no activity toward ethoxyresorufin and only trace dearylation activity toward benzyloxyresorufin. Bioactivates 3- methylindole (3MI) by dehydrogenation to the putative electrophile 3-methylene-indolenine
Enzyme 30 Pathways
Enzyme 30 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 19743565 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID P24903 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name CP2F1_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >1476 bp
ATGGACAGCATAAGCACAGCCATCTTACTCCTGCTCCTGGCTCTCGTCTGTCTGCTCCTG
ACCCTAAGCTCAAGAGATAAGGGAAAGCTGCCTCCGGGACCCAGACCCCTCTCAATCCTG
GGAAACCTGCTGCTGCTTTGCTCCCAAGACATGCTGACTTCTCTCACTAAGCTGAGCAAG
GAGTATGGCTCCATGTACACAGTGCACCTGGGACCCAGGCGGGTGGTGGTCCTCAGCGGG
TACCAAGCTGTGAAGGAGGCCCTGGTGGACCAGGGAGAGGAGTTTAGTGGCCGCGGTGAC
TACCCTGCCTTTTTCAACTTTACCAAGGGCAATGGCATCGCCTTCTCCAGTGGGGATCGA
TGGAAGGTCCTGAGACAGTTCTCTATCCAGATTCTACGGAATTTCGGGATGGGGAAGAGA
AGCATTGAGGAGCGAATCCTAGAGGAGGGCAGCTTCCTGCTGGCGGAGCTGCGGAAAACT
GAAGGCGAGCCCTTTGACCCCACGTTTGTGCTGAGTCGCTCAGTGTCCAACATTATCTGT
TCCGTGCTCTTCGGCAGCCGCTTCGACTATGATGATGAGCGTCTGCTCACCATTATCCGC
CTTATCAATGACAACTTCCAAATCATGAGCAGCCCCTGGGGCGAGTTGTACGACATCTTC
CCGAGCCTCCTGGACTGGGTGCCTGGGCCGCACCAACGCATCTTCCAGAACTTCAAGTGC
CTGAGAGACCTCATCGCCCACAGCGTCCACGACCACCAGGCCTCGCTAGACCCCAGATCT
CCCCGGGACTTCATCCAGTGCTTCCTCACCAAGATGGCAGAGGAGAAGGAGGACCCACTG
AGCCACTTCCACATGGATACCCTGCTGATGACCACACATAACCTGCTCTTTGGCGGCACC
AAGACGGTGAGCACCACGCTGCACCACGCCTTCCTGGCACTCATGAAGTACCCAAAAGTT
CAAGCCCGCGTGCAGGAGGAGATCGACCTCGTGGTGGGACGCGCGCGGCTGCCGGCGCTG
AAGGACCGCGCGGCCATGCCTTACACAGACGCGGTGATCCACGAGGTGCAGCGCTTTGCA
GACATCATCCCCATGAACTTGCCGCACCGCGTCACTAGGGACACGGCCTTTCGCGGCTTC
CTGATACCCAAGGGCACCGATGTCATCACCCTCCTTAACACCGTCCACTACGACCCCAGC
CAGTTCCTGACGCCCCAGGAGTTCAACCCCGAGCATTTTTTGGATGCCAATCAGTCCTTC
AAGAAGAGTCCAGCCTTCATGCCCTTCTCAGCTGGGCGCCGTCTGTGCCTGGGAGAGTCG
CTGGCGCGCATGGAGCTCTTTCTGTACCTCACCGCCATCCTGCAGAGCTTTTCGCTGCAG
CCGCTGGGTGCGCCCGAGGACATCGACCTGACCCCACTCAGCTCAGGTCTTGGCAATTTG
CCGCGGCCTTTCCAGCTGTGCCTGCGCCCGCGCTAA
Enzyme 30 GenBank Gene ID NM_000774.3 Link Image
Enzyme 30 GeneCard ID CYP2F1 Link Image
Enzyme 30 GenAtlas ID Not Available
Enzyme 30 HGNC ID Not Available
Enzyme 30 Chromosome Location 1
Enzyme 30 Locus 19q13.2
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Nhamburo PT, Kimura S, McBride OW, Kozak CA, Gelboin HV, Gonzalez FJ: The human CYP2F gene subfamily: identification of a cDNA encoding a new cytochrome P450, cDNA-directed expression, and chromosome mapping. Biochemistry. 1990 Jun 12;29(23):5491-9. [PubMed Link Image]
  2. Chen N, Whitehead SE, Caillat AW, Gavit K, Isphording DR, Kovacevic D, McCreary MB, Hoffman SM: Identification and cross-species comparisons of CYP2F subfamily genes in mammals. Mutat Res. 2002 Feb 20;499(2):155-61. [PubMed Link Image]
  3. Tournel G, Cauffiez C, Billaut-Laden I, Allorge D, Chevalier D, Bonnifet F, Mensier E, Lafitte JJ, Lhermitte M, Broly F, Lo-Guidice JM: Molecular analysis of the CYP2F1 gene: identification of a frequent non-functional allelic variant. Mutat Res. 2007 Apr 1;617(1-2):79-89. Epub 2007 Jan 25. [PubMed Link Image]
  4. Hakkola J, Pasanen M, Hukkanen J, Pelkonen O, Maenpaa J, Edwards RJ, Boobis AR, Raunio H: Expression of xenobiotic-metabolizing cytochrome P450 forms in human full-term placenta. Biochem Pharmacol. 1996 Feb 23;51(4):403-11. [PubMed Link Image]
  5. Thornton-Manning J, Appleton ML, Gonzalez FJ, Yost GS: Metabolism of 3-methylindole by vaccinia-expressed P450 enzymes: correlation of 3-methyleneindolenine formation and protein-binding. J Pharmacol Exp Ther. 1996 Jan;276(1):21-9. [PubMed Link Image]
  6. Lanza DL, Code E, Crespi CL, Gonzalez FJ, Yost GS: Specific dehydrogenation of 3-methylindole and epoxidation of naphthalene by recombinant human CYP2F1 expressed in lymphoblastoid cells. Drug Metab Dispos. 1999 Jul;27(7):798-803. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 6849
Enzyme 31 Name Cytochrome P450 2B6
Enzyme 31 Synonyms
  1. CYPIIB6
  2. Cytochrome P450 IIB1
Enzyme 31 Gene Name CYP2B6
Enzyme 31 Protein Sequence >Cytochrome P450 2B6
MELSVLLFLALLTGLLLLLVQRHPNTHDRLPPGPRPLPLLGNLLQMDRRGLLKSFLRFRE
KYGDVFTVHLGPRPVVMLCGVEAIREALVDKAEAFSGRGKIAMVDPFFRGYGVIFANGNR
WKVLRRFSVTTMRDFGMGKRSVEERIQEEAQCLIEELRKSKGALMDPTFLFQSITANIIC
SIVFGKRFHYQDQEFLKMLNLFYQTFSLISSVFGQLFELFSGFLKYFPGAHRQVYKNLQE
INAYIGHSVEKHRETLDPSAPKDLIDTYLLHMEKEKSNAHSEFSHQNLNLNTLSLFFAGT
ETTSTTLRYGFLLMLKYPHVAERVYREIEQVIGPHRPPELHDRAKMPYTEAVIYEIQRFS
DLLPMGVPHIVTQHTSFRGYIIPKDTEVFLILSTALHDPHYFEKPDAFNPDHFLDANGAL
KKTEAFIPFSLGKRICLGEGIARAELFLFFTTILQNFSMASPVAPEDIDLTPQECGVGKI
PPTYQIRFLPR
Enzyme 31 Number of Residues 491
Enzyme 31 Molecular Weight 56277.8
Enzyme 31 Theoretical pI 8.44
Enzyme 31 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 31 General Function Involved in monooxygenase activity
Enzyme 31 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics
Enzyme 31 Pathways
Enzyme 31 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein Not Available
Enzyme 31 UniProtKB/Swiss-Prot ID P20813 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name CP2B6_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >1476 bp
ATGGAACTCAGCGTCCTCCTCTTCCTTGCACTCCTCACAGGACTCTTGCTACTCCTGGTT
CAGCGCCACCCTAACACCCATGACCGCCTCCCACCAGGGCCCCGCCCTCTGCCCCTTTTG
GGAAACCTTCTGCAGATGGATAGAAGAGGCCTACTCAAATCCTTTCTGAGGTTCCGAGAG
AAATATGGGGACGTCTTCACGGTACACCTGGGACCGAGGCCCGTGGTCATGCTGTGTGGA
GTAGAGGCCATACGGGAGGCCCTTGTGGACAAGGCTGAGGCCTTCTCTGGCCGGGGAAAA
ATCGCCATGGTCGACCCATTCTTCCGGGGATATGGTGTGATCTTTGCCAATGGAAACCGC
TGGAAGGTGCTTCGGCGATTCTCTGTGACCACTATGAGGGACTTCGGGATGGGAAAGCGG
AGTGTGGAGGAGCGGATTCAGGAGGAGGCTCAGTGTCTGATAGAGGAGCTTCGGAAATCC
AAGGGGGCCCTCATGGACCCCACCTTCCTCTTCCAGTCCATTACCGCCAACATCATCTGC
TCCATCGTCTTTGGAAAACGATTCCACTACCAAGATCAAGAGTTCCTGAAGATGCTGAAC
TTGTTCTACCAGACTTTTTCACTCATCAGCTCTGTATTCGGCCAGCTGTTTGAGCTCTTC
TCTGGCTTCTTGAAATACTTTCCTGGGGCACACAGGCAAGTTTACAAAAACCTGCAGGAA
ATCAATGCTTACATTGGCCACAGTGTGGAGAAGCACCGTGAAACCCTGGACCCCAGCGCC
CCCAAGGACCTCATCGACACCTACCTGCTCCACATGGAAAAAGAGAAATCCAACGCACAC
AGTGAATTCAGCCACCAGAACCTCAACCTCAACACGCTCTCGCTCTTCTTTGCTGGCACT
GAGACCACCAGCACCACTCTCCGCTACGGCTTCCTGCTCATGCTCAAATACCCTCATGTT
GCAGAGAGAGTCTACAGGGAGATTGAACAGGTGATTGGCCCACATCGCCCTCCAGAGCTT
CATGACCGAGCCAAAATGCCATACACAGAGGCAGTCATCTATGAGATTCAGAGATTTTCC
GACCTTCTCCCCATGGGTGTGCCCCACATTGTCACCCAACACACCAGCTTCCGAGGGTAC
ATCATCCCCAAGGACACAGAAGTATTTCTCATCCTGAGCACTGCTCTCCATGACCCACAC
TACTTTGAAAAACCAGACGCCTTCAATCCTGACCACTTTCTGGATGCCAATGGGGCACTG
AAAAAGACTGAAGCTTTTATCCCCTTCTCCTTAGGGAAGCGGATTTGTCTTGGTGAAGGC
ATCGCCCGTGCGGAATTGTTCCTCTTCTTCACCACCATCCTCCAGAACTTCTCCATGGCC
AGCCCCGTGGCCCCAGAAGACATCGATCTGACACCCCAGGAGTGTGGTGTGGGCAAAATA
CCCCCAACATACCAGATCCGCTTCCTGCCCCGCTGA
Enzyme 31 GenBank Gene ID M29874 Link Image
Enzyme 31 GeneCard ID CYP2B6 Link Image
Enzyme 31 GenAtlas ID CYP2B6 Link Image
Enzyme 31 HGNC ID HGNC:2615 Link Image
Enzyme 31 Chromosome Location 1
Enzyme 31 Locus 19q13.2
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 General References
  1. Yamano S, Nhamburo PT, Aoyama T, Meyer UA, Inaba T, Kalow W, Gelboin HV, McBride OW, Gonzalez FJ: cDNA cloning and sequence and cDNA-directed expression of human P450 IIB1: identification of a normal and two variant cDNAs derived from the CYP2B locus on chromosome 19 and differential expression of the IIB mRNAs in human liver. Biochemistry. 1989 Sep 5;28(18):7340-8. [PubMed Link Image]
  2. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  3. Miles JS, McLaren AW, Wolf CR: Alternative splicing in the human cytochrome P450IIB6 gene generates a high level of aberrant messages. Nucleic Acids Res. 1989 Oct 25;17(20):8241-55. [PubMed Link Image]
  4. Thum T, Borlak J: Gene expression in distinct regions of the heart. Lancet. 2000 Mar 18;355(9208):979-83. [PubMed Link Image]
  5. Ariyoshi N, Miyazaki M, Toide K, Sawamura Yi, Kamataki T: A single nucleotide polymorphism of CYP2b6 found in Japanese enhances catalytic activity by autoactivation. Biochem Biophys Res Commun. 2001 Mar;281(5):1256-60. [PubMed Link Image]
  6. Lang T, Klein K, Fischer J, Nussler AK, Neuhaus P, Hofmann U, Eichelbaum M, Schwab M, Zanger UM: Extensive genetic polymorphism in the human CYP2B6 gene with impact on expression and function in human liver. Pharmacogenetics. 2001 Jul;11(5):399-415. [PubMed Link Image]
  7. Jinno H, Tanaka-Kagawa T, Ohno A, Makino Y, Matsushima E, Hanioka N, Ando M: Functional characterization of cytochrome P450 2B6 allelic variants. Drug Metab Dispos. 2003 Apr;31(4):398-403. [PubMed Link Image]
  8. Saito S, Iida A, Sekine A, Kawauchi S, Higuchi S, Ogawa C, Nakamura Y: Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population. J Hum Genet. 2003;48(5):249-70. Epub 2003 Apr 29. [PubMed Link Image]
  9. Lamba V, Lamba J, Yasuda K, Strom S, Davila J, Hancock ML, Fackenthal JD, Rogan PK, Ring B, Wrighton SA, Schuetz EG: Hepatic CYP2B6 expression: gender and ethnic differences and relationship to CYP2B6 genotype and CAR (constitutive androstane receptor) expression. J Pharmacol Exp Ther. 2003 Dec;307(3):906-22. Epub 2003 Oct 9. [PubMed Link Image]
  10. Lang T, Klein K, Richter T, Zibat A, Kerb R, Eichelbaum M, Schwab M, Zanger UM: Multiple novel nonsynonymous CYP2B6 gene polymorphisms in Caucasians: demonstration of phenotypic null alleles. J Pharmacol Exp Ther. 2004 Oct;311(1):34-43. Epub 2004 Jun 9. [PubMed Link Image]
  11. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 6850
Enzyme 32 Name Cytochrome P450 3A5
Enzyme 32 Synonyms
  1. CYPIIIA5
  2. Cytochrome P450 HLp2
  3. Cytochrome P450-PCN3
Enzyme 32 Gene Name CYP3A5
Enzyme 32 Protein Sequence >Cytochrome P450 3A5
MDLIPNLAVETWLLLAVSLVLLYLYGTRTHGLFKRLGIPGPTPLPLLGNVLSYRQGLWKF
DTECYKKYGKMWGTYEGQLPVLAITDPDVIRTVLVKECYSVFTNRRSLGPVGFMKSAISL
AEDEEWKRIRSLLSPTFTSGKLKEMFPIIAQYGDVLVRNLRREAEKGKPVTLKDIFGAYS
MDVITGTSFGVNIDSLNNPQDPFVESTKKFLKFGFLDPLFLSIILFPFLTPVFEALNVSL
FPKDTINFLSKSVNRMKKSRLNDKQKHRLDFLQLMIDSQNSKETESHKALSDLELAAQSI
IFIFAGYETTSSVLSFTLYELATHPDVQQKLQKEIDAVLPNKAPPTYDAVVQMEYLDMVV
NETLRLFPVAIRLERTCKKDVEINGVFIPKGSMVVIPTYALHHDPKYWTEPEEFRPERFS
KKKDSIDPYIYTPFGTGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLDTQG
LLQPEKPIVLKVDSRDGTLSGE
Enzyme 32 Number of Residues 502
Enzyme 32 Molecular Weight 57108.1
Enzyme 32 Theoretical pI 9.09
Enzyme 32 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 32 General Function Involved in monooxygenase activity
Enzyme 32 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics
Enzyme 32 Pathways
Enzyme 32 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • None
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 41393491 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID P20815 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name CP3A5_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >1509 bp
ATGGACCTCATCCCAAATTTGGCGGTGGAAACCTGGCTTCTCCTGGCTGTCAGCCTGGTG
CTCCTCTATCTATATGGGACCCGTACACATGGACTTTTTAAGAGACTGGGAATTCCAGGG
CCCACACCTCTGCCTTTGTTGGGAAATGTTTTGTCCTATCGTCAGGGTCTCTGGAAATTT
GACACAGAGTGCTATAAAAAGTATGGAAAAATGTGGGGAACGTATGAAGGTCAACTCCCT
GTGCTGGCCATCACAGATCCCGACGTGATCAGAACAGTGCTAGTGAAAGAATGTTATTCT
GTCTTCACAAATCGAAGGTCTTTAGGCCCAGTGGGATTTATGAAAAGTGCCATCTCTTTA
GCTGAGGATGAAGAATGGAAGAGAATACGGTCATTGCTGTCTCCAACCTTCACCAGCGGA
AAACTCAAGGAGATGTTCCCCATCATTGCCCAGTATGGAGATGTATTGGTGAGAAACTTG
AGGCGGGAAGCAGAGAAAGGCAAGCCTGTCACCTTGAAAGACATCTTTGGGGCCTACAGC
ATGGATGTGATTACTGGCACATCATTTGGAGTGAACATCGACTCTCTCAACAATCCACAA
GACCCCTTTGTGGAGAGCACTAAGAAGTTCCTAAAATTTGGTTTCTTAGATCCATTATTT
CTCTCAATAATACTCTTTCCATTCCTTACCCCAGTTTTTGAAGCATTAAATGTCTCTCTG
TTTCCAAAAGATACCATAAATTTTTTAAGTAAATCTGTAAACAGAATGAAGAAAAGTCGC
CTCAACGACAAACAAAAGCACCGACTAGATTTCCTTCAGCTGATGATTGACTCCCAGAAT
TCGAAAGAAACTGAGTCCCACAAAGCTCTGTCTGATCTGGAGCTCGCAGCCCAGTCAATA
ATCTTCATTTTTGCTGGCTATGAAACCACCAGCAGTGTTCTTTCCTTCACTTTATATGAA
CTGGCCACTCACCCTGATGTCCAGCAGAAACTGCAAAAGGAGATTGATGCAGTTTTGCCC
AATAAGGCACCACCTACCTATGATGCCGTGGTACAGATGGAGTACCTTGACATGGTGGTG
AATGAAACACTCAGATTATTCCCAGTTGCTATTAGACTTGAGAGGACTTGCAAGAAAGAT
GTTGAAATCAATGGGGTATTCATTCCCAAAGGGTCAATGGTGGTGATTCCAACTTATGCT
CTTCACCATGACCCAAAGTACTGGACAGAGCCTGAGGAGTTCCGCCCTGAAAGGTTCAGT
AAGAAGAAGGACAGCATAGATCCTTACATATACACACCCTTTGGAACTGGACCCAGAAAC
TGCATTGGCATGAGGTTTGCTCTCATGAACATGAAACTTGCTCTAATCAGAGTCCTTCAG
AACTTCTCCTTCAAACCTTGTAAAGAAACACAGATCCCCTTGAAATTAGACACGCAAGGA
CTTCTTCAACCAGAAAAACCCATTGTTCTAAAGGTGGATTCAAGAGATGGAACCCTAAGT
GGAGAATGA
Enzyme 32 GenBank Gene ID AC005020 Link Image
Enzyme 32 GeneCard ID CYP3A5 Link Image
Enzyme 32 GenAtlas ID CYP3A5 Link Image
Enzyme 32 HGNC ID HGNC:2638 Link Image
Enzyme 32 Chromosome Location 7
Enzyme 32 Locus 7q21.1
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Aoyama T, Yamano S, Waxman DJ, Lapenson DP, Meyer UA, Fischer V, Tyndale R, Inaba T, Kalow W, Gelboin HV, et al.: Cytochrome P-450 hPCN3, a novel cytochrome P-450 IIIA gene product that is differentially expressed in adult human liver. cDNA and deduced amino acid sequence and distinct specificities of cDNA-expressed hPCN1 and hPCN3 for the metabolism of steroid hormones and cyclosporine. J Biol Chem. 1989 Jun 25;264(18):10388-95. [PubMed Link Image]
  2. Schuetz JD, Molowa DT, Guzelian PS: Characterization of a cDNA encoding a new member of the glucocorticoid-responsive cytochromes P450 in human liver. Arch Biochem Biophys. 1989 Nov 1;274(2):355-65. [PubMed Link Image]
  3. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  4. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Gellner K, Eiselt R, Hustert E, Arnold H, Koch I, Haberl M, Deglmann CJ, Burk O, Buntefuss D, Escher S, Bishop C, Koebe HG, Brinkmann U, Klenk HP, Kleine K, Meyer UA, Wojnowski L: Genomic organization of the human CYP3A locus: identification of a new, inducible CYP3A gene. Pharmacogenetics. 2001 Mar;11(2):111-21. [PubMed Link Image]
  7. Schuetz JD, Schuetz EG, Thottassery JV, Guzelian PS, Strom S, Sun D: Identification of a novel dexamethasone responsive enhancer in the human CYP3A5 gene and its activation in human and rat liver cells. Mol Pharmacol. 1996 Jan;49(1):63-72. [PubMed Link Image]
  8. Jounaidi Y, Guzelian PS, Maurel P, Vilarem MJ: Sequence of the 5'-flanking region of CYP3A5: comparative analysis with CYP3A4 and CYP3A7. Biochem Biophys Res Commun. 1994 Dec 30;205(3):1741-7. [PubMed Link Image]
  9. Jounaidi Y, Hyrailles V, Gervot L, Maurel P: Detection of CYP3A5 allelic variant: a candidate for the polymorphic expression of the protein? Biochem Biophys Res Commun. 1996 Apr 16;221(2):466-70. [PubMed Link Image]
  10. Chou FC, Tzeng SJ, Huang JD: Genetic polymorphism of cytochrome P450 3A5 in Chinese. Drug Metab Dispos. 2001 Sep;29(9):1205-9. [PubMed Link Image]
  11. Lee SJ, Usmani KA, Chanas B, Ghanayem B, Xi T, Hodgson E, Mohrenweiser HW, Goldstein JA: Genetic findings and functional studies of human CYP3A5 single nucleotide polymorphisms in different ethnic groups. Pharmacogenetics. 2003 Aug;13(8):461-72. [PubMed Link Image]
  12. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 6851
Enzyme 33 Name Cytochrome P450 1A1
Enzyme 33 Synonyms
  1. CYPIA1
  2. Cytochrome P450 form 6
  3. Cytochrome P450-C
  4. Cytochrome P450-P1
Enzyme 33 Gene Name CYP1A1
Enzyme 33 Protein Sequence >Cytochrome P450 1A1
MLFPISMSATEFLLASVIFCLVFWVIRASRPQVPKGLKNPPGPWGWPLIGHMLTLGKNPH
LALSRMSQQYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYTFTLISNGQS
MSFSPDSGPVWAARRRLAQNGLKSFSIASDPASSTSCYLEEHVSKEAEVLISTLQELMAG
PGHFNPYRYVVVSVTNVICAICFGRRYDHNHQELLSLVNLNNNFGEVVGSGNPADFIPIL
RYLPNPSLNAFKDLNEKFYSFMQKMVKEHYKTFEKGHIRDITDSLIEHCQEKQLDENANV
QLSDEKIINIVLDLFGAGFDTVTTAISWSLMYLVMNPRVQRKIQEELDTVIGRSRRPRLS
DRSHLPYMEAFILETFRHSSFVPFTIPHSTTRDTSLKGFYIPKGRCVFVNQWQINHDQKL
WVNPSEFLPERFLTPDGAIDKVLSEKVIIFGMGKRKCIGETIARWEVFLFLAILLQRVEF
SVPLGVKVDMTPIYGLTMKHACCEHFQMQLRS
Enzyme 33 Number of Residues 512
Enzyme 33 Molecular Weight 58164.8
Enzyme 33 Theoretical pI 8.47
Enzyme 33 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 33 General Function Involved in monooxygenase activity
Enzyme 33 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics
Enzyme 33 Pathways
Enzyme 33 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • None
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 181276 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID P04798 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name CP1A1_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >1539 bp
ATGCTTTTCCCAATCTCCATGTCGGCCACGGAGTTTCTTCTGGCCTCTGTCATCTTCTGT
CTGGTATTCTGGGTAATGAGGGCCTCAAGACCTCAGGTCCCCAAAGGCCTGAAGAATCCA
CCAGGGCCATGGGGCTGGCCTCTGATTGGGCACATGCTGACCCTGGGAAAGAACCCGCAC
CTGGCACTGTCAAGGATGAGCCAGCAGTATGGGGACGTGCTGCAGATCCGAATTGGCTCC
ACACCCGTGGTGGTGCTGAGCGGCCTGGACACCATCCGGCAGGCCCTGGTGCGGCAGGGC
GATGATTTCAAGGGCCGGCCCGACCTCTACACCTTCACCCTCATCAGTAATGGTCAGAGC
ATGTCCTTCAGCCCAGACTCTGGACCAGTGTGGGCTGCCCGCCGGCGCCTGGCCCAGAAT
GGCCTGAAAAGTTTCTCCATTGCCTCTGACCCAGCCTCCTCAACCTCCTGCTACCTGGAA
GAGCATGTGAGCAAGGAGGCTGAGGTCCTGATAAGCACGTTGCAGGAGCTGATGGCAGGG
CCTGGGCACTTTAACCCCTACAGGTATGTGGTGGTATCAGTGACCAATGTCATCTGTGCC
ATTTGCTTTGGCCGGCGCTATGACCACAACCACCAAGAACTGCTTAGCCTAGTCAACCTG
AATAATAATTTCGGGGAGGTGGTTGGCTCTGGAAACCCAGCTGAGTTCATCCCTATTCTT
CGCTACCTACCCAACCCTTCCCTGAATGCCTTCAAGGACCTGAATGAGAAGTTCTACAGC
TTCATGCAGAAGATGGTCAAGGAGCACTACAAAACCTTTGAGAAGGGCCACATCCGGGAC
ATCACAGACAGCCTGATTGAGCACTGTCAGGAGAAGCAGCTGGATGAGAACGCCAATGTC
CAGCTGTCAGATGAGAAGATCATTAACATCGTCTTGGACCTCTTTGGAGCTGGGTTTGAC
ACAGTCACAACTGCTATCTCCTGGAGCCTCATGTATTTGGTGATGAACCCCAGGGTACAG
AGAAAGATCCAAGAGGAGCTAGACACAGTGATTGGCAGGTCACGGCGGCCCCGGCTCTCT
GACAGATCCCATCTGCCCTATATGGAGGCCTTCATCCTGGAGACCTTCCGACACTCTTCC
TTCGTCCCCTTCACCATCCCCCACAGCACAACAAGAGACACAAGTTTGAAAGGCTTTTAC
ATCCCCAAGGGGCGTTGTGTCTTTGTAAACCAGTGGCAGATCAACCATGACCAGAAGCTA
TGGGTCAACCCATCTGAGTTCCTACCTGAACGGTTTCTCACCCCTGATGGTGCTATCGAC
AAGGTGTTAAGTGAGAAGGTGATTATCTTTGGCATGGGCAAGCGGAAGTGTATCGGTGAG
ACCGTTGCCCGCTGGGAGGTCTTTCTCTTCCTGGCTATCCTGCTGCAACGGGTGGAATTC
AGCGTGCCACTGGGCGTGAAGGTGGACATGACCCCCATCTATGGGCTAACCATGAAGCAT
GCCTGCTGTGAGCACTTCCAAATGCAGCTGCGCTCTTAG
Enzyme 33 GenBank Gene ID K03191 Link Image
Enzyme 33 GeneCard ID CYP1A1 Link Image
Enzyme 33 GenAtlas ID CYP1A1 Link Image
Enzyme 33 HGNC ID HGNC:2595 Link Image
Enzyme 33 Chromosome Location 1
Enzyme 33 Locus 15q24.1
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Jaiswal AK, Gonzalez FJ, Nebert DW: Human P1-450 gene sequence and correlation of mRNA with genetic differences in benzo[a]pyrene metabolism. Nucleic Acids Res. 1985 Jun 25;13(12):4503-20. [PubMed Link Image]
  2. Jaiswal AK, Gonzalez FJ, Nebert DW: Human dioxin-inducible cytochrome P1-450: complementary DNA and amino acid sequence. Science. 1985 Apr 5;228(4695):80-3. [PubMed Link Image]
  3. Kawajiri K, Watanabe J, Gotoh O, Tagashira Y, Sogawa K, Fujii-Kuriyama Y: Structure and drug inducibility of the human cytochrome P-450c gene. Eur J Biochem. 1986 Sep 1;159(2):219-25. [PubMed Link Image]
  4. Corchero J, Pimprale S, Kimura S, Gonzalez FJ: Organization of the CYP1A cluster on human chromosome 15: implications for gene regulation. Pharmacogenetics. 2001 Feb;11(1):1-6. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Yun CH, Park HJ, Kim SJ, Kim HK: Identification of cytochrome P450 1A1 in human brain. Biochem Biophys Res Commun. 1998 Feb 24;243(3):808-10. [PubMed Link Image]
  7. Quattrochi LC, Okino ST, Pendurthi UR, Tukey RH: Cloning and isolation of human cytochrome P-450 cDNAs homologous to dioxin-inducible rabbit mRNAs encoding P-450 4 and P-450 6. DNA. 1985 Oct;4(5):395-400. [PubMed Link Image]
  8. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  9. Hayashi S, Watanabe J, Nakachi K, Kawajiri K: Genetic linkage of lung cancer-associated MspI polymorphisms with amino acid replacement in the heme binding region of the human cytochrome P450IA1 gene. J Biochem (Tokyo). 1991 Sep;110(3):407-11. [PubMed Link Image]
  10. Cascorbi I, Brockmoller J, Roots I: A C4887A polymorphism in exon 7 of human CYP1A1: population frequency, mutation linkages, and impact on lung cancer susceptibility. Cancer Res. 1996 Nov 1;56(21):4965-9. [PubMed Link Image]
  11. Smart J, Daly AK: Variation in induced CYP1A1 levels: relationship to CYP1A1, Ah receptor and GSTM1 polymorphisms. Pharmacogenetics. 2000 Feb;10(1):11-24. [PubMed Link Image]
  12. Chevalier D, Allorge D, Lo-Guidice JM, Cauffiez C, Lhermitte M, Lafitte JJ, Broly F: Detection of known and two novel (M331I and R464S) missense mutations in the human CYP1A1 gene in a French Caucasian population. Hum Mutat. 2001 Apr;17(4):355. [PubMed Link Image]
  13. Saito T, Egashira M, Kiyotani K, Fujieda M, Yamazaki H, Kiyohara C, Kunitoh H, Kamataki T: Novel nonsynonymous polymorphisms of the CYP1A1 gene in Japanese. Drug Metab Pharmacokinet. 2003;18(3):218-21. [PubMed Link Image]
  14. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
  15. Jiang Z, Dalton TP, Jin L, Wang B, Tsuneoka Y, Shertzer HG, Deka R, Nebert DW: Toward the evaluation of function in genetic variability: characterizing human SNP frequencies and establishing BAC-transgenic mice carrying the human CYP1A1_CYP1A2 locus. Hum Mutat. 2005 Feb;25(2):196-206. [PubMed Link Image]
  16. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 6852
Enzyme 34 Name Cytochrome P450 2A13
Enzyme 34 Synonyms
  1. CYPIIA13
Enzyme 34 Gene Name CYP2A13
Enzyme 34 Protein Sequence >Cytochrome P450 2A13
MLASGLLLVTLLACLTVMVLMSVWRQRKSRGKLPPGPTPLPFIGNYLQLNTEQMYNSLMK
ISERYGPVFTIHLGPRRVVVLCGHDAVKEALVDQAEEFSGRGEQATFDWLFKGYGVAFSN
GERAKQLRRFSIATLRGFGVGKRGIEERIQEEAGFLIDALRGTHGANIDPTFFLSRTVSN
VISSIVFGDRFDYEDKEFLSLLRMMLGSFQFTATSTGQLYEMFSSVMKHLPGPQQQAFKE
LQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFF
AGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYTEAVIHEIQ
RFGDMLPMGLAHRVNKDTKFRDFFLPKGTEVFPMLGSVLRDPRFFSNPRDFNPQHFLDKK
GQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRFKSPQSPKDIDVSPKHVGF
ATIPRNYTMSFLPR
Enzyme 34 Number of Residues 494
Enzyme 34 Molecular Weight 56687.1
Enzyme 34 Theoretical pI 9.78
Enzyme 34 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 34 General Function Involved in monooxygenase activity
Enzyme 34 Specific Function Exhibits a coumarin 7-hydroxylase activity. Active in the metabolic activation of hexamethylphosphoramide, N,N- dimethylaniline, 2'-methoxyacetophenone, N- nitrosomethylphenylamine, and the tobacco-specific carcinogen, 4- (methylnitrosamino)-1-(3-pyridyl)-1-butanone. Possesses phenacetin O-deethylation activity
Enzyme 34 Pathways
Enzyme 34 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • None
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein Not Available
Enzyme 34 UniProtKB/Swiss-Prot ID Q16696 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name CP2AD_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >1485 bp
ATGCTGGCCTCAGGGCTGCTTCTGGTGACCTTGCTGGCCTGCCTGACTGTGATGGTCTTG
ATGTCAGTCTGGCGGCAGAGGAAGAGCAGGGGGAAGCTGCCTCCGGGACCCACCCCATTG
CCCTTCATTGGAAACTACCTGCAGCTGAACACAGAGCAGATGTACAACTCCCTCATGAAG
ATCAGTGAGCGCTATGGCCCTGTGTTCACCATTCACTTGGGGCCCCGGCGGGTCGTGGTG
CTGTGCGGACATGATGCCGTCAAGGAGGCTCTGGTGGACCAGGCTGAGGAGTTCAGCGGG
CGAGGCGAGCAGGCCACCTTCGACTGGCTCTTCAAAGGCTATGGCGTGGCGTTCAGCAAC
GGGGAGCGCGCCAAGCAGCTCCGGCGCTTCTCCATCGCCACCCTAAGGGGTTTTGGCGTG
GGCAAGCGCGGCATCGAGGAACGCATCCAGGAGGAGGCGGGCTTCCTCATCGACGCCCTC
CGGGGCACGCACGGCGCCAATATCGATCCCACCTTCTTCCTGAGCCGCACAGTCTCCAAT
GTCATCAGCTCCATTGTCTTTGGGGACCGCTTTGACTATGAGGACAAAGAGTTCCTGTCA
CTGTTGCGCATGATGCTGGGAAGCTTCCAGTTCACGGCAACCTCCACGGGGCAGCTCTAT
GAGATGTTCTCTTCGGTGATGAAACACCTGCCAGGACCACAGCAACAGGCCTTTAAGGAG
CTGCAAGGGCTGGAGGACTTCATCGCCAAGAAGGTGGAGCACAACCAGCGCACGCTGGAT
CCCAATTCCCCACGGGACTTCATCGACTCCTTTCTCATCCGCATGCAGGAGGAGGAGAAG
AACCCCAACACAGAGTTCTACTTGAAGAACCTGGTGATGACCACCCTGAACCTCTTCTTT
GCGGGCACTGAGACCGTGAGCACCACCCTGCGCTACGGTTTCCTGCTGCTCATGAAGCAC
CCAGAGGTGGAGGCCAAGGTCCATGAGGAGATTGACAGAGTGATCGGCAAGAACCGGCAG
CCCAAGTTTGAGGACCGGGCCAAGATGCCCTACACAGAGGCAGTGATCCACGAGATCCAA
AGATTTGGAGACATGCTCCCCATGGGTTTGGCCCACAGGGTCAACAAGGACACCAAGTTT
CGGGATTTCTTCCTCCCTAAGGGCACTGAAGTGTTCCCTATGCTGGGCTCCGTGCTGAGA
GACCCCAGGTTCTTCTCCAACCCCCGGGACTTCAATCCCCAGCACTTCCTGGATAAGAAG
GGGCAGTTTAAGAAGAGTGATGCTTTTGTGCCCTTTTCCATCGGAAAGCGGTACTGTTTT
GGAGAAGGCCTGGCCAGAATGGAGCTCTTTCTCTTCTTCACCACCATCATGCAGAACTTT
CGCTTCAAGTCCCCTCAGTCGCCTAAGGATATCGACGTGTCCCCCAAACACGTGGGCTTT
GCCACGATCCCACGAAACTACACCATGAGCTTCCTGCCCCGCTGA
Enzyme 34 GenBank Gene ID AF209774 Link Image
Enzyme 34 GeneCard ID CYP2A13 Link Image
Enzyme 34 GenAtlas ID CYP2A13 Link Image
Enzyme 34 HGNC ID HGNC:2608 Link Image
Enzyme 34 Chromosome Location 1
Enzyme 34 Locus 19q13.2
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Fernandez-Salguero P, Hoffman SM, Cholerton S, Mohrenweiser H, Raunio H, Rautio A, Pelkonen O, Huang JD, Evans WE, Idle JR, et al.: A genetic polymorphism in coumarin 7-hydroxylation: sequence of the human CYP2A genes and identification of variant CYP2A6 alleles. Am J Hum Genet. 1995 Sep;57(3):651-60. [PubMed Link Image]
  2. Su T, Bao Z, Zhang QY, Smith TJ, Hong JY, Ding X: Human cytochrome P450 CYP2A13: predominant expression in the respiratory tract and its high efficiency metabolic activation of a tobacco-specific carcinogen, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone. Cancer Res. 2000 Sep 15;60(18):5074-9. [PubMed Link Image]
  3. Cauffiez C, Lo-Guidice JM, Quaranta S, Allorge D, Chevalier D, Cenee S, Hamdan R, Lhermitte M, Lafitte JJ, Libersa C, Colombel JF, Stucker I, Broly F: Genetic polymorphism of the human cytochrome CYP2A13 in a French population: implication in lung cancer susceptibility. Biochem Biophys Res Commun. 2004 Apr 30;317(2):662-9. [PubMed Link Image]
  4. DeVore NM, Smith BD, Urban MJ, Scott EE: Key residues controlling phenacetin metabolism by human cytochrome P450 2A enzymes. Drug Metab Dispos. 2008 Dec;36(12):2582-90. Epub 2008 Sep 8. [PubMed Link Image]
  5. Sansen S, Hsu MH, Stout CD, Johnson EF: Structural insight into the altered substrate specificity of human cytochrome P450 2A6 mutants. Arch Biochem Biophys. 2007 Aug 15;464(2):197-206. Epub 2007 May 11. [PubMed Link Image]
  6. Smith BD, Sanders JL, Porubsky PR, Lushington GH, Stout CD, Scott EE: Structure of the human lung cytochrome P450 2A13. J Biol Chem. 2007 Jun 8;282(23):17306-13. Epub 2007 Apr 11. [PubMed Link Image]
  7. Zhang X, Su T, Zhang QY, Gu J, Caggana M, Li H, Ding X: Genetic polymorphisms of the human CYP2A13 gene: identification of single-nucleotide polymorphisms and functional characterization of an Arg257Cys variant. J Pharmacol Exp Ther. 2002 Aug;302(2):416-23. [PubMed Link Image]
  8. Fujieda M, Yamazaki H, Kiyotani K, Muroi A, Kunitoh H, Dosaka-Akita H, Sawamura Y, Kamataki T: Eighteen novel polymorphisms of the CYP2A13 gene in Japanese. Drug Metab Pharmacokinet. 2003;18(1):86-90. [PubMed Link Image]
  9. Saito S, Iida A, Sekine A, Kawauchi S, Higuchi S, Ogawa C, Nakamura Y: Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population. J Hum Genet. 2003;48(5):249-70. Epub 2003 Apr 29. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 6853
Enzyme 35 Name Cytochrome P450 3A7
Enzyme 35 Synonyms
  1. CYPIIIA7
  2. Cytochrome P450-HFLA
Enzyme 35 Gene Name CYP3A7
Enzyme 35 Protein Sequence >Cytochrome P450 3A7
MDLIPNLAVETWLLLAVSLILLYLYGTRTHGLFKKLGIPGPTPLPFLGNALSFRKGYWTF
DMECYKKYRKVWGIYDCQQPMLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKNAISI
AEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYS
MDVITSTSFGVSIDSLNNPQDPFVENTKKLLRFNPLDPFVLSIKVFPFLTPILEALNITV
FPRKVISFLTKSVKQIKEGRLKETQKHRVDFLQLMIDSQNSKDSETHKALSDLELMAQSI
IFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVV
NETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWREPEKFLPERFS
KKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKLRFG
GLLLTEKPIVLKAESRDETVSGA
Enzyme 35 Number of Residues 503
Enzyme 35 Molecular Weight 57525.0
Enzyme 35 Theoretical pI 9.59
Enzyme 35 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 35 General Function Involved in monooxygenase activity
Enzyme 35 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics
Enzyme 35 Pathways
Enzyme 35 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • None
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 11177455 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID P24462 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name CP3A7_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >1512 bp
ATGGCTCTCATCCCAGACTTGGCCATGGAAACCTGGCTTCTCCTGGCTGTCAGCCTGGTG
CTCCTCTATCTATATGGAACCCATTCACATGGACTTTTTAAGAAGCTTGGAATTCCAGGG
CCCACACCTCTGCCTTTTTTGGGAAATATTTTGTCCTACCATAAGGGCTTTTGTATGTTT
GACATGGAATGTCATAAAAAGTATGGAAAAGTGTGGGGCTTTTATGATGGTCAACAGCCT
GTGCTGGCTATCACAGATCCTGACATGATCAAAACAGTGCTAGTGAAAGAATGTTATTCT
GTCTTCACAAACCGGAGGCCTTTTGGTCCAGTGGGATTTATGAAAAGTGCCATCTCTATA
GCTGAGGATGAAGAATGGAAGAGATTACGATCATTGCTGTCTCCAACCTTCACCAGTGGA
AAACTCAAGGAGATGGTCCCTATCATTGCCCAGTATGGAGATGTGTTGGTGAGAAATCTG
AGGCGGGAAGCAGAGACAGGCAAGCCTGTCACCTTGAAAGACGTCTTTGGGGCCTACAGC
ATGGATGTGATCACTAGCACATCATTTGGAGTGAACATCGACTCTCTCAACAATCCACAA
GACCCCTTTGTGGAAAACACCAAGAAGCTTTTAAGATTTGATTTTTTGGATCCATTCTTT
CTCTCAATAACAGTCTTTCCATTCCTCATCCCAATTCTTGAAGTATTAAATATCTGTGTG
TTTCCAAGAGAAGTTACAAATTTTTTAAGAAAATCTGTAAAAAGGATGAAAGAAAGTCGC
CTCGAAGATACACAAAAGCACCGAGTGGATTTCCTTCAGCTGATGATTGACTCTCAGAAT
TCAAAAGAAACTGAGTCCCACAAAGCTCTGTCCGATCTGGAGCTCGTGGCCCAATCAATT
ATCTTTATTTTTGCTGGCTATGAAACCACGAGCAGTGTTCTCTCCTTCATTATGTATGAA
CTGGCCACTCACCCTGATGTCCAGCAGAAACTGCAGGAGGAAATTGATGCAGTTTTACCC
AATAAGGCACCACCCACCTATGATACTGTGCTACAGATGGAGTATCTTGACATGGTGGTG
AATGAAACGCTCAGATTATTCCCAATTGCTATGAGACTTGAGAGGGTCTGCAAAAAAGAT
GTTGAGATCAATGGGATGTTCATTCCCAAAGGGGTGGTGGTGATGATTCCAAGCTATGCT
CTTCACCGTGACCCAAAGTACTGGACAGAGCCTGAGAAGTTCCTCCCTGAAAGATTCAGC
AAGAAGAACAAGGACAACATAGATCCTTACATATACACACCCTTTGGAAGTGGACCCAGA
AACTGCATTGGCATGAGGTTTGCTCTCATGAACATGAAACTTGCTCTAATCAGAGTCCTT
CAGAACTTCTCCTTCAAACCTTGTAAAGAAACACAGATCCCCCTGAAATTAAGCTTAGGA
GGACTTCTTCAACCAGAAAAACCCGTTGTTCTAAAGGTTGAGTCAAGGGATGGCACCGTA
AGTGGAGCCTGA
Enzyme 35 GenBank Gene ID AF280107 Link Image
Enzyme 35 GeneCard ID CYP3A7 Link Image
Enzyme 35 GenAtlas ID CYP3A7 Link Image
Enzyme 35 HGNC ID HGNC:2640 Link Image
Enzyme 35 Chromosome Location 7
Enzyme 35 Locus 7q21-q22.1
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Komori M, Nishio K, Ohi H, Kitada M, Kamataki T: Molecular cloning and sequence analysis of cDNA containing the entire coding region for human fetal liver cytochrome P-450. J Biochem (Tokyo). 1989 Feb;105(2):161-3. [PubMed Link Image]
  2. Gellner K, Eiselt R, Hustert E, Arnold H, Koch I, Haberl M, Deglmann CJ, Burk O, Buntefuss D, Escher S, Bishop C, Koebe HG, Brinkmann U, Klenk HP, Kleine K, Meyer UA, Wojnowski L: Genomic organization of the human CYP3A locus: identification of a new, inducible CYP3A gene. Pharmacogenetics. 2001 Mar;11(2):111-21. [PubMed Link Image]
  3. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Wrighton SA, Vandenbranden M: Isolation and characterization of human fetal liver cytochrome P450HLp2: a third member of the P450III gene family. Arch Biochem Biophys. 1989 Jan;268(1):144-51. [PubMed Link Image]
  6. Komori M, Nishio K, Fujitani T, Ohi H, Kitada M, Mima S, Itahashi K, Kamataki T: Isolation of a new human fetal liver cytochrome P450 cDNA clone: evidence for expression of a limited number of forms of cytochrome P450 in human fetal livers. Arch Biochem Biophys. 1989 Jul;272(1):219-25. [PubMed Link Image]
Enzyme 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 6854
Enzyme 36 Name Cytochrome P450 4B1
Enzyme 36 Synonyms
  1. CYPIVB1
  2. Cytochrome P450-HP
Enzyme 36 Gene Name CYP4B1
Enzyme 36 Protein Sequence >Cytochrome P450 4B1
MVPSFLSLSFSSLGLWASGLILVLGFLKLIHLLLRRQTLAKAMDKFPGPPTHWLFGHALE
IQETGSLDKVVSWAHQFPYAHPLWFGQFIGFLNIYEPDYAKAVYSRGDPKAPDVYDFFLQ
WIGRGLLVLEGPKWLQHRKLLTPGFHYDVLKPYVAVFTESTRIMLDKWEEKAREGKSFDI
FCDVGHMALNTLMKCTFGRGDTGLGHRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYWLT
PHGRRFLRACQVAHDHTDQVIRERKAALQDEKVRKKIQNRRHLDFLDILLGARDEDDIKL
SDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDL
GKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWP
DPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDP
SRLPIKMPQLVLRSKNGFHLHLKPLGPGSGK
Enzyme 36 Number of Residues 511
Enzyme 36 Molecular Weight 58990.6
Enzyme 36 Theoretical pI 8.39
Enzyme 36 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 36 General Function Involved in monooxygenase activity
Enzyme 36 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics
Enzyme 36 Pathways
Enzyme 36 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • None
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 20067171 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID P13584 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name CP4B1_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >1536 bp
ATGGTGCCCAGCTTCCTCTCCCTGAGCTTCTCCTCCTTGGGCCTGTGGGCTTCTGGGCTG
ATCTTGGTCTTAGGCTTTCTCAAGCTCATCCACCTGCTGCTGCGGAGGCAGACGTTGGCT
AAGGCTATGGACAAATTCCCAGGGCCTCCCACCCACTGGCTTTTTGGACATGCCCTCGAG
ATCCAGGAGACGGGGAGCCTGGACAAAGTGGTGTCCTGGGCCCACCAGTTCCCGTATGCC
CACCCACTCTGGTTCGGACAGTTCATTGGCTTCCTGAACATCTATGAGCCTGACTATGCC
AAAGCTGTGTACAGCCGTGGGGACCCTAAGGCCCCTGATGTGTATGACTTCTTCCTCCAG
TGGATTGGGAGAGGCCTGCTGGTTCTTGAGGGGCCCAAGTGGTTGCAGCACCGCAAGCTG
CTCACACCTGGCTTTCATTATGATGTGCTGAAGCCCTATGTGGCCGTGTTCACTGAGTCT
ACACGTATCATGCTGGACAAGTGGGAAGAGAAAGCTCGGGAGGGTAAGTCCTTTGACATC
TTCTGCGATGTGGGTCACATGGCGCTGAACACACTCATGAAGTGCACCTTTGGAAGAGGA
GACACCGGCCTGGGCCACAGGGACAGCAGCTACTACCTTGCAGTCAGCGATCTCACTCTG
TTGATGCAGCAGCGCCTTGTGTCCTTCCAGTACCATAATGACTTCATCTACTGGCTCACC
CCACATGGCCGCCGCTTCCTGCGGGCCTGCCAGGTGGCCCATGACCATACAGACCAGGTC
ATCAGGGAGCGGAAGGCAGCCCTGCAGGATGAGAAGGTGCGGAAGAAGATCCAGAACCGG
AGGCACCTGGACTTCCTGGACATTCTCCTGGGTGCCCGGGATGAAGATGACATCAAACTG
TCAGATGCAGACCTCCGGGCTGAAGTGGACACATTCATGTTTGAAGGCCATGACACCACC
ACCAGTGGTATCTCCTGGTTTCTCTACTGCATAGCCCTGTACCCTGAGCACCAGCATCGT
TGTAGAGAGGAGGTCCGCGAGATCCTAGGGGACCAGGACTTCTTCCAGTGGGATGATCTG
GGCAAAATGACTTATCTGACCATGTGCATCAAGGAGAGCTTCCGCCTCTACCCACCTGTG
CCCCAGGTGTACCGCCAGCTCAGCAAGCCTGTCACCTTTGTGGATGGCCGGTCTCTACCT
GCAGGAAGCCTGATCTCTATGCATATCTATGCCCTCCATAGGAACAGTGCTGTATGGCCC
GACCCTGAGGTCTTTGACTCTCTGCGCTTTTCCACTGAGAATGCATCCAAACGCCATCCC
TTTGCCTTTATGCCCTTCTCTGCTGGGCCCAGGAACTGCATTGGGCAGCAGTTTGCCATG
AGTGAGATGAAGGTGGTCACAGCCATGTGCTTGCTCCGCTTTGAGTTCTCTCTGGACCCC
TCACGGCTGCCCATCAAGATGCCCCAGCTTGTCCTGCGCTCCAAGAATGGCTTTCACCTC
CACCTGAAGCCACTGGGCCCTGGGTCTGGGAAGTAG
Enzyme 36 GenBank Gene ID AF491285 Link Image
Enzyme 36 GeneCard ID CYP4B1 Link Image
Enzyme 36 GenAtlas ID CYP4B1 Link Image
Enzyme 36 HGNC ID HGNC:2644 Link Image
Enzyme 36 Chromosome Location 1
Enzyme 36 Locus 1p34-p12
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Nhamburo PT, Gonzalez FJ, McBride OW, Gelboin HV, Kimura S: Identification of a new P450 expressed in human lung: complete cDNA sequence, cDNA-directed expression, and chromosome mapping. Biochemistry. 1989 Oct 3;28(20):8060-6. [PubMed Link Image]
  2. Yokotani N, Sogawa K, Matsubara S, Gotoh O, Kusunose E, Kusunose M, Fujii-Kuriyama Y: cDNA cloning of cytochrome P-450 related to P-450p-2 from the cDNA library of human placenta. Gene structure and expression. Eur J Biochem. 1990 Jan 12;187(1):23-9. [PubMed Link Image]
  3. Lo-Guidice JM, Allorge D, Cauffiez C, Chevalier D, Lafitte JJ, Lhermitte M, Broly F: Genetic polymorphism of the human cytochrome P450 CYP4B1: evidence for a non-functional allelic variant. Pharmacogenetics. 2002 Jul;12(5):367-74. [PubMed Link Image]
  4. Carr BA, Ramakanth S, Dannan GA, Yost GS: Characterization of pulmonary CYP4B2, specific catalyst of methyl oxidation of 3-methylindole. Mol Pharmacol. 2003 May;63(5):1137-47. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 6855
Enzyme 37 Name Cytochrome P450 4Z1
Enzyme 37 Synonyms
  1. CYPIVZ1
Enzyme 37 Gene Name CYP4Z1
Enzyme 37 Protein Sequence >Cytochrome P450 4Z1
MEPSWLQELMAHPFLLLILLCMSLLLFQVIRLYQRRRWMIRALHLFPAPPAHWFYGHKEF
YPVKEFEVYHKLMEKYPCAVPLWVGPFTMFFSVHDPDYAKILLKRQDPKSAVSHKILESW
VGRGLVTLDGSKWKKHRQIVKPGFNISILKIFITMMSESVRMMLNKWEEHIAQNSRLELF
QHVSLMTLDSIMKCAFSHQGSIQLDSTLDSYLKAVFNLSKISNQRMNNFLHHNDLVFKFS
SQGQIFSKFNQELHQFTEKVIQDRKESLKDKLKQDTTQKRRWDFLDILLSAKSENTKDFS
EADLQAEVKTFMFAGHDTTSSAISWILYCLAKYPEHQQRCRDEIRELLGDGSSITWEHLS
QMPYTTMCIKECLRLYAPVVNISRLLDKPITFPDGRSLPAGITVFINIWALHHNPYFWED
PQVFNPLRFSRENSEKIHPYAFIPFSAGLRNCIGQHFAIIECKVAVALTLLRFKLAPDHS
RPPQPVRQVVLKSKNGIHVFAKKVC
Enzyme 37 Number of Residues 505
Enzyme 37 Molecular Weight 59085.4
Enzyme 37 Theoretical pI 9.63
Enzyme 37 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 37 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 37 Specific Function RH + reduced flavoprotein + O(2) = ROH + oxidized flavoprotein + H(2)O
Enzyme 37 Pathways
Enzyme 37 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • 10-30
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 158257782 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q86W10 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name CP4Z1_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >1518 bp
ATGGAGCCCTCCTGGCTTCAGGAACTCATGGCTCACCCCTTCTTGCTGCTGATCCTCCTC
TGCATGTCTCTGCTGCTGTTTCAGGTAATCAGGTTGTACCAGAGGAGGAGATGGATGATC
AGAGCCCTGCACCTGTTTCCTGCACCCCCTGCCCACTGGTTCTATGGCCACAAGGAGTTT
TACCCAGTAAAGGAGTTTGAGGTGTATCATAAGCTGATGGAAAAATACCCATGTGCTGTT
CCCTTGTGGGTTGGACCCTTTACGATGTTCTTCAGTGTCCATGACCCAGACTATGCCAAG
ATTCTCCTGAAAAGACAAGATCCCAAAAGTGCTGTTAGCCACAAAATCCTTGAATCCTGG
GTTGGTCGAGGACTTGTGACCCTGGATGGTTCTAAATGGAAAAAGCACCGCCAGATTGTG
AAACCTGGCTTCAACATCAGCATTCTGAAAATATTCATCACCATGATGTCTGAGAGTGTT
CGGATGATGCTGAACAAATGGGAGGAACACATTGCCCAAAACTCACGTCTGGAGCTCTTT
CAACATGTCTCCCTGATGACCCTGGACAGCATCATGAAGTGTGCCTTCAGCCACCAGGGC
AGCATCCAGTTGGACAGTACCCTGGACTCATACCTGAAAGCAGTGTTCAACCTTAGCAAA
ATCTCCAACCAGCGCATGAACAATTTTCTACATCACAACGACCTGGTTTTCAAATTCAGC
TCTCAAGGCCAAATCTTTTCTAAATTTAACCAAGAACTTCATCAGTTCACAGAGAAAGTA
ATCCAGGACCGGAAGGAGTCTCTTAAGGATAAGCTAAAACAAGATACTACTCAGAAAAGG
CGCTGGGATTTTCTGGACATACTTTTGAGTGCCAAAAGCGAAAACACCAAAGATTTCTCT
GAAGCAGATCTCCAGGCTGAAGTGAAAACGTTCATGTTTGCAGGACATGACACCACATCC
AGTGCTATCTCCTGGATCCTTTACTGCTTGGCAAAGTACCCTGAGCATCAGCAGAGATGC
CGAGATGAAATCAGGGAACTCCTAGGGGATGGGTCTTCTATTACCTGGGAACACCTGAGC
CAGATGCCTTACACCACGATGTGCATCAAGGAATGCCTCCGCCTCTACGCACCGGTAGTA
AACATATCCCGGTTACTCGACAAACCCATTACTTTTCCAGATGGACGCTCCTTACCTGCA
GGAATAACTGTGTTTATCAATATTTGGGCTCTTCACCACAACCCCTATTTCTGGGAAGAC
CCTCAGGTCTTTAACCCCTTGAGATTCTCCAGGGAAAATTCTGAAAAAATACATCCCTAT
GCCTTCATACCATTCTCAGCTGGATTAAGGAACTGCATTGGGCAGCATTTTGCCATAATT
GAGTGTAAAGTGGCAGTGGCATTAACTCTGCTCCGCTTCAAGCTGGCTCCAGACCACTCA
AGGCCTCCCCAGCCTGTTCGTCAAGTTGTCCTCAAGTCCAAGAATGGAATCCATGTGTTT
GCAAAAAAAGTTTGCTAA
Enzyme 37 GenBank Gene ID AK292175 Link Image
Enzyme 37 GeneCard ID CYP4Z1 Link Image
Enzyme 37 GenAtlas ID Not Available
Enzyme 37 HGNC ID Not Available
Enzyme 37 Chromosome Location 1
Enzyme 37 Locus 1p33
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References
  1. Rieger MA, Ebner R, Bell DR, Kiessling A, Rohayem J, Schmitz M, Temme A, Rieber EP, Weigle B: Identification of a novel mammary-restricted cytochrome P450, CYP4Z1, with overexpression in breast carcinoma. Cancer Res. 2004 Apr 1;64(7):2357-64. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 6856
Enzyme 38 Name Cytochrome P450 1A2
Enzyme 38 Synonyms
  1. CYPIA2
  2. Cytochrome P(3)450
  3. Cytochrome P450 4
  4. Cytochrome P450-P3
Enzyme 38 Gene Name CYP1A2
Enzyme 38 Protein Sequence >Cytochrome P450 1A2
MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKN
PHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDG
QSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELM
AGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFP
ILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGN
LIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLS
DRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPEL
WEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLE
FSVPPGVKVDLTPIYGLTMKHARCEHVQARRFSIN
Enzyme 38 Number of Residues 515
Enzyme 38 Molecular Weight 58293.8
Enzyme 38 Theoretical pI 9.43
Enzyme 38 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 38 General Function Involved in monooxygenase activity
Enzyme 38 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Most active in catalyzing 2-hydroxylation. Caffeine is metabolized primarily by cytochrome CYP1A2 in the liver through an initial N3-demethylation. Also acts in the metabolism of aflatoxin B1 and acetaminophen. Participates in the bioactivation of carcinogenic aromatic and heterocyclic amines. Catalizes the N-hydroxylation of heterocyclic amines and the O- deethylation of phenacetin
Enzyme 38 Pathways
Enzyme 38 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • None
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 30339 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID P05177 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name CP1A2_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >1548 bp
ATGGCATTGTCCCAGTCTGTTCCCTTCTCGGCCACAGAGCTTCTCCTGGCCTCTGCCATC
TTCTGCCTGGTATTCTGGGTGCTCAAGGGTTTGAGGCCTCGGGTCCCCAAAGGCCTGAAA
AGTCCACCAGAGCCATGGGGCTGGCCCTTGCTCGGGCATGTGCTGACCCTGGGGAAGAAC
CCGCACCTGGCACTGTCAAGGATGAGCCAGCGCTACGGGGACGTCCTGCAGATCCGCATT
GGCTCCACGCCCGTGCTGGTGCTGAGCCGCCTGGACACCATCCGGCAGGCCCTGGTGCGG
CAGGGCGACGATTTCAAGGGCCGGCCTGACCTCTACACCTCCACCCTCATCACTGATGGC
CAGAGCTTGACCTTCAGCACAGACTCTGGACCGGTGTGGGCTGCCCGCCGGCGCCTGGCC
CAGAATGCCCTCAACACCTTCTCCATCGCCTCTGACCCAGCTTCCTCATCCTCCTGCTAC
CTGGAGGAGCATGTGAGCAAGGAGGCTAAGGCCCTGATCAGCAGGTTGCAGGAGCTGATG
GCAGGGCCTGGGCACTTCGACCCTTACAATCAGGTGGTGGTGTCAGTGGCCAACGTCATT
GGTGCCATGTGCTTCGGACAGCACTTCCCTGAGAGTAGCGATGAGATGCTCAGCCTCGTG
AAGAACACTCATGAGTTCGTGGAGACTGCCTCCTCCGGGAACCCCCTGGACTTCTTCCCC
ATCCTTCGCTACCTGCCTAACCCTGCCCTGCAGAGGTTCAAGGCCTTCAACCAGAGGTTC
CTGTGGTTCCTGCAGAAAACAGTCCAGGAGCACTATCAGGACTTTGACAAGAACAGTGTC
CGGGACATCACGGGTGCCCTGTTCAAGCACAGCAAGAAGGGGCCTAGAGCCAGCGGCAAC
CTCATCCCACAGGAGAAGATTGTCAACCTTGTCAATGACATCTTTGGAGCAGGATTTGAC
ACAGTCACCACAGCCATCTCCTGGAGCCTCATGTACCTTGTGACCAAGCCTGAGATACAG
AGGAAGATCCAGAAGGAGCTGGACACTGTGATTGGCAGGGAGCGGCGGCCCCGGCTCTCT
GACAGACCCCAGCTGCCCTACTTGGAGGCCTTCATCCTGGAGACCTTCCGACACTCCTCC
TTCTTGCCCTTCACCATCCCCCACAGCACAACAAGGGACACAACGCTGAATGGCTTCTAC
ATCCCCAAGAAATGCTGTGTCTTCGTAAACCAGTGGCAGGTCAACCATGACCCAGAGCTG
TGGGAGGACCCCTCTGAGTTCCGGCCTGAGCGGTTCCTCACCGCCGATGGCACTGCCATT
AACAAGCCCTTGAGTGAGAAGATGATGCTGTTTGGCATGGGCAAGCGCCGGTGTATCGGG
GAAGTCCTGGCCAAGTGGGAGATCTTCCTCTTCCTGGCCATCCTGCTACAGCAACTGGAG
TTCAGCGTGCCGCCGGGCGTGAAAGTCGACCTGACCCCCATCTACGGGCTGACCATGAAG
CACGCCCGCTGTGAACATGTCCAGGCGCGGCGCTTCTCCATCAATTGA
Enzyme 38 GenBank Gene ID Z00036 Link Image
Enzyme 38 GeneCard ID CYP1A2 Link Image
Enzyme 38 GenAtlas ID CYP1A2 Link Image
Enzyme 38 HGNC ID HGNC:2596 Link Image
Enzyme 38 Chromosome Location 1
Enzyme 38 Locus 15q24.1
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Jaiswal AK, Nebert DW, Gonzalez FJ: Human P3(450): cDNA and complete amino acid sequence. Nucleic Acids Res. 1986 Aug 26;14(16):6773-4. [PubMed Link Image]
  2. Quattrochi LC, Pendurthi UR, Okino ST, Potenza C, Tukey RH: Human cytochrome P-450 4 mRNA and gene: part of a multigene family that contains Alu sequences in its mRNA. Proc Natl Acad Sci U S A. 1986 Sep;83(18):6731-5. [PubMed Link Image]
  3. Ikeya K, Jaiswal AK, Owens RA, Jones JE, Nebert DW, Kimura S: Human CYP1A2: sequence, gene structure, comparison with the mouse and rat orthologous gene, and differences in liver 1A2 mRNA expression. Mol Endocrinol. 1989 Sep;3(9):1399-408. [PubMed Link Image]
  4. Jaiswal AK, Nebert DW, McBride OW, Gonzalez FJ: Human P(3)450: cDNA and complete protein sequence, repetitive Alu sequences in the 3' nontranslated region, and localization of gene to chromosome 15. J Exp Pathol. 1987 Winter;3(1):1-17. [PubMed Link Image]
  5. Corchero J, Pimprale S, Kimura S, Gonzalez FJ: Organization of the CYP1A cluster on human chromosome 15: implications for gene regulation. Pharmacogenetics. 2001 Feb;11(1):1-6. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Wrighton SA, Campanile C, Thomas PE, Maines SL, Watkins PB, Parker G, Mendez-Picon G, Haniu M, Shively JE, Levin W, et al.: Identification of a human liver cytochrome P-450 homologous to the major isosafrole-inducible cytochrome P-450 in the rat. Mol Pharmacol. 1986 Apr;29(4):405-10. [PubMed Link Image]
  8. Quattrochi LC, Okino ST, Pendurthi UR, Tukey RH: Cloning and isolation of human cytochrome P-450 cDNAs homologous to dioxin-inducible rabbit mRNAs encoding P-450 4 and P-450 6. DNA. 1985 Oct;4(5):395-400. [PubMed Link Image]
  9. Zhou H, Josephy PD, Kim D, Guengerich FP: Functional characterization of four allelic variants of human cytochrome P450 1A2. Arch Biochem Biophys. 2004 Feb 1;422(1):23-30. [PubMed Link Image]
  10. Sansen S, Yano JK, Reynald RL, Schoch GA, Griffin KJ, Stout CD, Johnson EF: Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2. J Biol Chem. 2007 May 11;282(19):14348-55. Epub 2007 Feb 20. [PubMed Link Image]
  11. Huang JD, Guo WC, Lai MD, Guo YL, Lambert GH: Detection of a novel cytochrome P-450 1A2 polymorphism (F21L) in Chinese. Drug Metab Dispos. 1999 Jan;27(1):98-101. [PubMed Link Image]
  12. Chevalier D, Cauffiez C, Allorge D, Lo-Guidice JM, Lhermitte M, Lafitte JJ, Broly F: Five novel natural allelic variants-951A>C, 1042G>A (D348N), 1156A>T (I386F), 1217G>A (C406Y) and 1291C>T (C431Y)-of the human CYP1A2 gene in a French Caucasian population. Hum Mutat. 2001 Apr;17(4):355-6. [PubMed Link Image]
  13. Murayama N, Soyama A, Saito Y, Nakajima Y, Komamura K, Ueno K, Kamakura S, Kitakaze M, Kimura H, Goto Y, Saitoh O, Katoh M, Ohnuma T, Kawai M, Sugai K, Ohtsuki T, Suzuki C, Minami N, Ozawa S, Sawada J: Six novel nonsynonymous CYP1A2 gene polymorphisms: catalytic activities of the naturally occurring variant enzymes. J Pharmacol Exp Ther. 2004 Jan;308(1):300-6. Epub 2003 Oct 16. [PubMed Link Image]
  14. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
  15. Soyama A, Saito Y, Hanioka N, Maekawa K, Komamura K, Kamakura S, Kitakaze M, Tomoike H, Ueno K, Goto Y, Kimura H, Katoh M, Sugai K, Saitoh O, Kawai M, Ohnuma T, Ohtsuki T, Suzuki C, Minami N, Kamatani N, Ozawa S, Sawada J: Single nucleotide polymorphisms and haplotypes of CYP1A2 in a Japanese population. Drug Metab Pharmacokinet. 2005 Feb;20(1):24-33. [PubMed Link Image]
  16. Jiang Z, Dalton TP, Jin L, Wang B, Tsuneoka Y, Shertzer HG, Deka R, Nebert DW: Toward the evaluation of function in genetic variability: characterizing human SNP frequencies and establishing BAC-transgenic mice carrying the human CYP1A1_CYP1A2 locus. Hum Mutat. 2005 Feb;25(2):196-206. [PubMed Link Image]
  17. Cornelis MC, El-Sohemy A, Kabagambe EK, Campos H: Coffee, CYP1A2 genotype, and risk of myocardial infarction. JAMA. 2006 Mar 8;295(10):1135-41. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 6857
Enzyme 39 Name Cytochrome P450 19A1
Enzyme 39 Synonyms
  1. Aromatase
  2. CYPXIX
  3. Cytochrome P-450AROM
  4. Estrogen synthase
Enzyme 39 Gene Name CYP19A1
Enzyme 39 Protein Sequence >Cytochrome P450 19A1
MVLEMLNPIHYNITSIVPEAMPAATMPVLLLTGLFLLVWNYEGTSSIPGPGYCMGIGPLI
SHGRFLWMGIGSACNYYNRVYGEFMRVWISGEETLIISKSSSMFHIMKHNHYSSRFGSKL
GLQCIGMHEKGIIFNNNPELWKTTRPFFMKALSGPGLVRMVTVCAESLKTHLDRLEEVTN
ESGYVDVLTLLRRVMLDTSNTLFLRIPLDESAIVVKIQGYFDAWQALLIKPDIFFKISWL
YKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRGDLTRENVNQCI
LEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFI
YESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLEFFPKPNEFTLENFAK
NVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQKIHDLSLH
PDETKNMLEMIFTPRNSDRCLEH
Enzyme 39 Number of Residues 503
Enzyme 39 Molecular Weight 57882.5
Enzyme 39 Theoretical pI 7.56
Enzyme 39 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 39 General Function Involved in monooxygenase activity
Enzyme 39 Specific Function Catalyzes the formation of aromatic C18 estrogens from C19 androgens
Enzyme 39 Pathways
Enzyme 39 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • None
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 61354153 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID P11511 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name CP19A_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >1512 bp
ATGGTTTTGGAAATGCTGAACCCGATACATTATAACATCACCAGCATCGTGCCTGAAGCC
ATGCCTGCTGCCACCATGCCAGTCCTGCTCCTCACTGGCCTTTTTCTCTTGGTGTGGAAT
TATGAGGGCACATCCTCAATACCAGGTCCTGGCTACTGCATGGGAATTGGACCCCTCATC
TCCCACGGCAGATTCCTGTGGATGGGGATCGGCAGTGCCTGCAACTACTACAACCGGGTA
TATGGAGAATTCATGCGAGTCTGGATCTCTGGAGAGGAAACACTCATTATCAGCAAGTCC
TCAAGTATGTTCCACATAATGAAGCACAATCATTACAGCTCTCGATTCGGCAGCAAACTT
GGGCTGCAGTGCATCGGTATGCATGAGAAAGGCATCATATTTAACAACAATCCAGAGCTC
TGGAAAACAACTCGACCCTTCTTTATGAAAGCTCTGTCAGGCCCCGGCCTTGTTCGTATG
GTCACAGTCTGTGCTGAATCCCTCAAAACACATCTGGACAGGTTGGAGGAGGTGACCAAT
GAATCGGGCTATGTGGACGTGTTGACCCTTCTGCGTCGTGTCATGCTGGACACCTCTAAC
ACGCTCTTCTTGAGGATCCCTTTGGACGAAAGTGCTATCGTGGTTAAAATCCAAGGTTAT
TTTGATGCATGGCAAGCTCTCCTCATCAAACCAGACATCTTCTTTAAGATTTCTTGGCTA
TACAAAAAGTATGAGAAGTCTGTCAAGGATTTGAAAGATGCCATAGAAGTTCTGATAGCA
GAAAAAAGACGCAGGATTTCCACAGAAGAGAAACTGGAAGAATGTATGGACTTTGCCACT
GAGTTGATTTTAGCAGAGAAACGTGGTGACCTGACAAGAGAGAATGTGAACCAGTGCATA
TTGGAAATGCTGATCGCAGCTCCTGACACCATGTCTGTCTCTTTGTTCTTCATGCTATTT
CTCATTGCAAAGCACCCTAATGTTGAAGAGGCAATAATAAAGGAAATCCAGACTGTTATT
GGTGAGAGAGACATAAAGATTGATGATATACAAAAATTAAAAGTGATGGAAAACTTCATT
TATGAGAGCATGCGGTACCAGCCTGTCGTGGACTTGGTCATGCGCAAAGCCTTAGAAGAT
GATGTAATCGATGGCTACCCAGTGAAAAAGGGGACAAACATTATCCTGAATATTGGAAGG
ATGCACAGACTCGAGTTTTTCCCCAAACCCAATGAATTTACTCTTGAAAATTTTGCAAAG
AATGTTCCTTATAGGTACTTTCAGCCATTTGGCTTTGGGCCCCGTGGCTGTGCAGGAAAG
TACATCGCCATGGTGATGATGAAAGCCATCCTCGTTACACTTCTGAGACGATTCCACGTG
AAGACATTGCAAGGACAGTGTGTTGAGAGCATACAGAAGATACACGACTTGTCCTTGCAC
CCAGATGAGACTAAAAACATGCTGGAAATGATCTTTACCCCAAGAAACTCAGACAGGTGT
CTGGAACACTAG
Enzyme 39 GenBank Gene ID AY957953 Link Image
Enzyme 39 GeneCard ID CYP19A1 Link Image
Enzyme 39 GenAtlas ID CYP19A1 Link Image
Enzyme 39 HGNC ID HGNC:2594 Link Image
Enzyme 39 Chromosome Location 1
Enzyme 39 Locus 15q21.1
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Harada N: Cloning of a complete cDNA encoding human aromatase: immunochemical identification and sequence analysis. Biochem Biophys Res Commun. 1988 Oct 31;156(2):725-32. [PubMed Link Image]
  2. Chen SA, Besman MJ, Sparkes RS, Zollman S, Klisak I, Mohandas T, Hall PF, Shively JE: Human aromatase: cDNA cloning, Southern blot analysis, and assignment of the gene to chromosome 15. DNA. 1988 Jan-Feb;7(1):27-38. [PubMed Link Image]
  3. Corbin CJ, Graham-Lorence S, McPhaul M, Mason JI, Mendelson CR, Simpson ER: Isolation of a full-length cDNA insert encoding human aromatase system cytochrome P-450 and its expression in nonsteroidogenic cells. Proc Natl Acad Sci U S A. 1988 Dec;85(23):8948-52. [PubMed Link Image]
  4. Toda K, Terashima M, Mitsuuchi Y, Yamasaki Y, Yokoyama Y, Nojima S, Ushiro H, Maeda T, Yamamoto Y, Sagara Y, et al.: Alternative usage of different poly(A) addition signals for two major species of mRNA encoding human aromatase P-450. FEBS Lett. 1989 Apr 24;247(2):371-6. [PubMed Link Image]
  5. Means GD, Mahendroo MS, Corbin CJ, Mathis JM, Powell FE, Mendelson CR, Simpson ER: Structural analysis of the gene encoding human aromatase cytochrome P-450, the enzyme responsible for estrogen biosynthesis. J Biol Chem. 1989 Nov 15;264(32):19385-91. [PubMed Link Image]
  6. Pompon D, Liu RY, Besman MJ, Wang PL, Shively JE, Chen S: Expression of human placental aromatase in Saccharomyces cerevisiae. Mol Endocrinol. 1989 Sep;3(9):1477-87. [PubMed Link Image]
  7. Harada N, Ogawa H, Shozu M, Yamada K, Suhara K, Nishida E, Takagi Y: Biochemical and molecular genetic analyses on placental aromatase (P-450AROM) deficiency. J Biol Chem. 1992 Mar 5;267(7):4781-5. [PubMed Link Image]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. Evans CT, Ledesma DB, Schulz TZ, Simpson ER, Mendelson CR: Isolation and characterization of a complementary DNA specific for human aromatase-system cytochrome P-450 mRNA. Proc Natl Acad Sci U S A. 1986 Sep;83(17):6387-91. [PubMed Link Image]
  10. Simpson ER, Evans CT, Corbin CJ, Powell FE, Ledesma DB, Mendelson CR: Sequencing of cDNA inserts encoding aromatase cytochrome P-450 (P-450AROM). Mol Cell Endocrinol. 1987 Aug;52(3):267-72. [PubMed Link Image]
  11. Mahendroo MS, Means GD, Mendelson CR, Simpson ER: Tissue-specific expression of human P-450AROM. The promoter responsible for expression in adipose tissue is different from that utilized in placenta. J Biol Chem. 1991 Jun 15;266(17):11276-81. [PubMed Link Image]
  12. Mahendroo MS, Mendelson CR, Simpson ER: Tissue-specific and hormonally controlled alternative promoters regulate aromatase cytochrome P450 gene expression in human adipose tissue. J Biol Chem. 1993 Sep 15;268(26):19463-70. [PubMed Link Image]
  13. Chen S, Shively JE, Nakajin S, Shinoda M, Hall PF: Amino terminal sequence analysis of human placenta aromatase. Biochem Biophys Res Commun. 1986 Mar 28;135(3):713-9. [PubMed Link Image]
  14. Honda S, Harada N, Takagi Y: Novel exon 1 of the aromatase gene specific for aromatase transcripts in human brain. Biochem Biophys Res Commun. 1994 Feb 15;198(3):1153-60. [PubMed Link Image]
  15. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  16. Ghosh D, Griswold J, Erman M, Pangborn W: Structural basis for androgen specificity and oestrogen synthesis in human aromatase. Nature. 2009 Jan 8;457(7226):219-23. [PubMed Link Image]
  17. Ito Y, Fisher CR, Conte FA, Grumbach MM, Simpson ER: Molecular basis of aromatase deficiency in an adult female with sexual infantilism and polycystic ovaries. Proc Natl Acad Sci U S A. 1993 Dec 15;90(24):11673-7. [PubMed Link Image]
  18. Morishima A, Grumbach MM, Simpson ER, Fisher C, Qin K: Aromatase deficiency in male and female siblings caused by a novel mutation and the physiological role of estrogens. J Clin Endocrinol Metab. 1995 Dec;80(12):3689-98. [PubMed Link Image]
  19. Carani C, Qin K, Simoni M, Faustini-Fustini M, Serpente S, Boyd J, Korach KS, Simpson ER: Effect of testosterone and estradiol in a man with aromatase deficiency. N Engl J Med. 1997 Jul 10;337(2):91-5. [PubMed Link Image]
  20. Ley TJ, Mardis ER, Ding L, Fulton B, McLellan MD, Chen K, Dooling D, Dunford-Shore BH, McGrath S, Hickenbotham M, Cook L, Abbott R, Larson DE, Koboldt DC, Pohl C, Smith S, Hawkins A, Abbott S, Locke D, Hillier LW, Miner T, Fulton L, Magrini V, Wylie T, Glasscock J, Conyers J, Sander N, Shi X, Osborne JR, Minx P, Gordon D, Chinwalla A, Zhao Y, Ries RE, Payton JE, Westervelt P, Tomasson MH, Watson M, Baty J, Ivanovich J, Heath S, Shannon WD, Nagarajan R, Walter MJ, Link DC, Graubert TA, DiPersio JF, Wilson RK: DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome. Nature. 2008 Nov 6;456(7218):66-72. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 6858
Enzyme 40 Name Cytochrome P450 2C8
Enzyme 40 Synonyms
  1. CYPIIC8
  2. Cytochrome P450 IIC2
  3. Cytochrome P450 MP-12
  4. Cytochrome P450 MP-20
  5. Cytochrome P450 form 1
  6. S-mephenytoin 4-hydroxylase
Enzyme 40 Gene Name CYP2C8
Enzyme 40 Protein Sequence >Cytochrome P450 2C8
MEPFVVLVLCLSFMLLFSLWRQSCRRRKLPPGPTPLPIIGNMLQIDVKDICKSFTNFSKV
YGPVFTVYFGMNPIVVFHGYEAVKEALIDNGEEFSGRGNSPISQRITKGLGIISSNGKRW
KEIRRFSLTTLRNFGMGKRSIEDRVQEEAHCLVEELRKTKASPCDPTFILGCAPCNVICS
VVFQKRFDYKDQNFLTLMKRFNENFRILNSPWIQVCNNFPLLIDCFPGTHNKVLKNVALT
RSYIREKVKEHQASLDVNNPRDFIDCFLIKMEQEKDNQKSEFNIENLVGTVADLFVAGTE
TTSTTLRYGLLLLLKHPEVTAKVQEEIDHVIGRHRSPCMQDRSHMPYTDAVVHEIQRYSD
LVPTGVPHAVTTDTKFRNYLIPKGTTIMALLTSVLHDDKEFPNPNIFDPGHFLDKNGNFK
KSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNLKSVDDLKNLNTTAVTKGIVSLP
PSYQICFIPV
Enzyme 40 Number of Residues 490
Enzyme 40 Molecular Weight 55824.3
Enzyme 40 Theoretical pI 8.62
Enzyme 40 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 40 General Function Involved in monooxygenase activity
Enzyme 40 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. In the epoxidation of arachidonic acid it generates only 14,15- and 11,12-cis-epoxyeicosatrienoic acids. It is the principal enzyme responsible for the metabolism the anti- cancer drug paclitaxel (taxol)
Enzyme 40 Pathways
Enzyme 40 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • None
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 158258943 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID P10632 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name CP2C8_HUMAN Link Image
Enzyme 40 PDB ID 1PQ2 Link Image
Enzyme 40 PDB File Show
Enzyme 40 3D Structure
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >1473 bp
ATGGAACCTTTTGTGGTCCTGGTGCTGTGTCTCTCTTTTATGCTTCTCTTTTCACTCTGG
AGACAGAGCTGTAGGAGAAGGAAGCTCCCTCCTGGCCCCACTCCTCTTCCTATTATTGGA
AATATGCTACAGATAGATGTTAAGGACATCTGCAAATCTTTCACCAATTTCTCAAAAGTC
TATGGTCCTGTGTTCACCGTGTATTTTGGCATGAATCCCATAGTGGTGTTTCATGGATAT
GAGGCAGTGAAGGAAGCCCTGATTGATAATGGAGAGGAGTTTTCTGGAAGAGGCAATTCC
CCAATATCTCAAAGAATTACTAAAGGACTTGGAATCATTTCCAGCAATGGAAAGAGATGG
AAGGAGATCCGGCGTTTCTCCCTCACAACCTTGCGGAATTTTGGGATGGGGAAGAGGAGC
ATTGAGGACCGTGTTCAAGAGGAAGCTCACTGCCTTGTGGAGGAGTTGAGAAAAACCAAG
GCTTCACCCTGTGATCCCACTTTCATCCTGGGCTGTGCTCCCTGCAATGTGATCTGCTCC
GTTGTTTTCCAGAAACGATTTGATTATAAAGATCAGAATTTTCTCACCCTGATGAAAAGA
TTCAATGAAAACTTCAGGATTCTGAACTCCCCATGGATCCAGGTCTGCAATAATTTCCCT
CTACTCATTGATTGTTTCCCAGGAACTCACAACAAAGTGCTTAAAAATGTTGCTCTTACA
CGAAGTTACATTAGGGAGAAAGTAAAAGAACACCAAGCATCACTGGATGTTAACAATCCT
CGGGACTTTATCGATTGCTTCCTGATCAAAATGGAGCAGGAAAAGGACAACCAAAAGTCA
GAATTCAATATTGAAAACTTGGTTGGCACTGTAGCTGATCTATTTGTTGCTGGAACAGAG
ACAACAAGCACCACTCTGAGATATGGACTCCTGCTCCTGCTGAAGCACCCAGAGGTCACA
GCTAAAGTCCAGGAAGAGATTGATCATGTAATTGGCAGACACAGGAGCCCCTGCATGCAG
GATAGGAGCCACATGCCTTACACTGATGCTGTAGTGCACGAGATCCAGAGATACAGTGAC
CTTGTCCCCACCGGTGTGCCCCATGCAGTGACCACTGATACTAAGTTCAGAAACTACCTC
ATCCCCAAGGGCACAGCCATAATGGCATTACTGACTTCCGTGCTACATGATGACAAAGAA
TTTCCTAATCCAAATATCTTTGACCCTGGCCACTTTCTAGATAAGAATGGCAACTTTAAG
AAAAGTGACTACTTCATGCCTTTCTCAGCAGGAAAACGAATTTGTGCAGGAGAAGGACTT
GCCCGCATGGAGCTATTTTTATTTCTAACCACAATTTTACAGAACTTTAACCTGAAATCT
GTTGATGATTTAAAGAACCTCAATACTACTGCAGTTACCAAAGGGATTGTTTCTCTGCCA
CCCTCATACCAGATCTGCTTCATCCCTGTCTGA
Enzyme 40 GenBank Gene ID AK292753 Link Image
Enzyme 40 GeneCard ID CYP2C8 Link Image
Enzyme 40 GenAtlas ID CYP2C8 Link Image
Enzyme 40 HGNC ID HGNC:2622 Link Image
Enzyme 40 Chromosome Location 1
Enzyme 40 Locus 10q23.33
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. Okino ST, Quattrochi LC, Pendurthi UR, McBride OW, Tukey RH: Characterization of multiple human cytochrome P-450 1 cDNAs. The chromosomal localization of the gene and evidence for alternate RNA splicing. J Biol Chem. 1987 Nov 25;262(33):16072-9. [PubMed Link Image]
  2. Kimura S, Pastewka J, Gelboin HV, Gonzalez FJ: cDNA and amino acid sequences of two members of the human P450IIC gene subfamily. Nucleic Acids Res. 1987 Dec 10;15(23):10053-4. [PubMed Link Image]
  3. Romkes M, Faletto MB, Blaisdell JA, Raucy JL, Goldstein JA: Cloning and expression of complementary DNAs for multiple members of the human cytochrome P450IIC subfamily. Biochemistry. 1991 Apr 2;30(13):3247-55. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Ged C, Beaune P: Isolation of the human cytochrome P-450 IIC8 gene: multiple glucocorticoid responsive elements in the 5' region. Biochim Biophys Acta. 1991 Mar 26;1088(3):433-5. [PubMed Link Image]
  8. Zeldin DC, DuBois RN, Falck JR, Capdevila JH: Molecular cloning, expression and characterization of an endogenous human cytochrome P450 arachidonic acid epoxygenase isoform. Arch Biochem Biophys. 1995 Sep 10;322(1):76-86. [PubMed Link Image]
  9. Ged C, Umbenhauer DR, Bellew TM, Bork RW, Srivastava PK, Shinriki N, Lloyd RS, Guengerich FP: Characterization of cDNAs, mRNAs, and proteins related to human liver microsomal cytochrome P-450 (S)-mephenytoin 4'-hydroxylase. Biochemistry. 1988 Sep 6;27(18):6929-40. [PubMed Link Image]
  10. Shephard EA, Phillips IR, Santisteban I, Palmer CN, Povey S: Cloning, expression and chromosomal localization of a member of the human cytochrome P450IIC gene sub-family. Ann Hum Genet. 1989 Jan;53(Pt 1):23-31. [PubMed Link Image]
  11. Kolyada AY: Sequence of a human liver cytochrome P-450 cDNA clone. Nucleic Acids Res. 1990 Sep 25;18(18):5550. [PubMed Link Image]
  12. Schoch GA, Yano JK, Wester MR, Griffin KJ, Stout CD, Johnson EF: Structure of human microsomal cytochrome P450 2C8. Evidence for a peripheral fatty acid binding site. J Biol Chem. 2004 Mar 5;279(10):9497-503. Epub 2003 Dec 15. [PubMed Link Image]
  13. Dai D, Zeldin DC, Blaisdell JA, Chanas B, Coulter SJ, Ghanayem BI, Goldstein JA: Polymorphisms in human CYP2C8 decrease metabolism of the anticancer drug paclitaxel and arachidonic acid. Pharmacogenetics. 2001 Oct;11(7):597-607. [PubMed Link Image]
  14. Bahadur N, Leathart JB, Mutch E, Steimel-Crespi D, Dunn SA, Gilissen R, Houdt JV, Hendrickx J, Mannens G, Bohets H, Williams FM, Armstrong M, Crespi CL, Daly AK: CYP2C8 polymorphisms in Caucasians and their relationship with paclitaxel 6alpha-hydroxylase activity in human liver microsomes. Biochem Pharmacol. 2002 Dec 1;64(11):1579-89. [PubMed Link Image]
  15. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 6859
Enzyme 41 Name Cytochrome P450 2S1
Enzyme 41 Synonyms
  1. CYPIIS1
Enzyme 41 Gene Name CYP2S1
Enzyme 41 Protein Sequence >Cytochrome P450 2S1
MEATGTWALLLALALLLLLTLALSGTRARGHLPPGPTPLPLLGNLLQLRPGALYSGLMRL
SKKYGPVFTIYLGPWRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSN
GERWRQLRKFTMLALRDLGMGKREGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSN
VVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTYEMFSWFLRPLPGPHKQLLHH
VSTLAAFTVRQVQQHQGNLDASGPARDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYLL
FAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEA
QRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDA
DGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLESPCPPDTLSLKPTVSG
LFNIPPAFQLQVRPTDLHSTTQTR
Enzyme 41 Number of Residues 504
Enzyme 41 Molecular Weight 55816.2
Enzyme 41 Theoretical pI 8.84
Enzyme 41 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 41 General Function Involved in monooxygenase activity
Enzyme 41 Specific Function Has a potential importance for extrahepatic xenobiotic metabolism
Enzyme 41 Pathways
Enzyme 41 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • None
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 13161184 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID Q96SQ9 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name CP2S1_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >1515 bp
ATGGAGGCGACCGGCACCTGGGCGCTGCTGCTGGCGCTGGCGCTGCTCCTGCTGCTGACG
CTGGCGCTGTCCGGGACCAGGGCCCGAGGCCACCTGCCCCCCGGGCCCACGCCGCTACCA
CTGCTGGGAAACCTCCTGCAGCTACGGCCCGGGGCGCTGTATTCAGGGCTCATGCGGCTG
AGTAAGAAGTACGGACCGGTGTTCACCATCTACCTGGGACCCTGGCGGCCTGTGGTGGTC
CTGGTTGGGCAGGAGGCTGTGCGGGAGGCCCTGGGAGGTCAGGCTGAGGAGTTCAGCGGC
CGGGGAACCGTAGCGATGCTGGAAGGGACTTTTGATGGCCATGGGGTTTTCTTCTCCAAC
GGGGAGCGGTGGAGGCAGCTGAGGAAGTTTACCATGCTTGCTCTGCGGGACCTGGGCATG
GGGAAGCGAGAAGGCGAGGAGCTGATCCAGGCGGAGGCCCGGTGTCTGGTGGAGACATTC
CAGGGGACAGAAGGACGCCCATTCGATCCCTCCCTGCTGCTGGCCCAGGCCACCTCCAAC
GTAGTCTGCTCCCTCCTCTTTGGCCTCCGCTTCTCCTATGAGGATAAGGAGTTCCAGGCC
GTGGTCCGGGCAGCTGGTGGTACCCTGCTGGGAGTCAGCTCCCAGGGGGGTCAGACCTAC
GAGATGTTCTCCTGGTTCCTGCGGCCCCTGCCAGGCCCCCACAAGCAGCTCCTCCACCAC
GTCAGCACCTTGGCTGCCTTCACAGTCCGGCAGGTGCAGCAGCACCAGGGGAACCTGGAT
GCTTCGGGCCCCGCACGTGACCTTGTCGATGCCTTCCTGCTGAAGATGGCACAGGAGGAA
CAAAACCCAGGCACAGAATTCACCAACAAGAACATGCTGATGACAGTCATTTATTTGCTG
TTTGCTGGGACGATGACGGTCAGCACCACGGTCGGCTATACCCTCCTGCTCCTGATGAAA
TACCCTCATGTCCAAAAGTGGGTACGTGAGGAGCTGAATCGGGAGCTGGGGGCTGGCCAG
GCACCAAGCCTAGGGGACCGTACCCGCCTCCCTTACACCGACGCGGTTCTGCATGAGGCG
CAGCGGCTGCTGGCGCTGGTGCCCATGGGAATACCCCGCACCCTCATGCGGACCACCCGC
TTCCGAGGGTACACCCTGCCCCAGGGCACGGAGGTCTTCCCCCTCCTTGGCTCCATCCTG
CATGACCCCAACATCTTCAAGCACCCAGAAGAGTTCAACCCAGACCGTTTCCTGGATGCA
GATGGACGGTTCAGGAAGCATGAGGCGTTCCTGCCCTTCTCCTTAGGGAAGCGTGTCTGC
CTTGGAGAGGGCCTGGCAAAAGCGGAGCTCTTCCTCTTCTTCACCACCATCCTACAAGCC
TTCTCCCTGGAGAGCCCGTGCCCGCCGGACACCCTGAGCCTCAAGCCCACCGTCAGTGGC
CTTTTCAACATTCCCCCAGCCTTCCAGCTGCAAGTCCGTCCCACTGACCTTCACTCCACC
ACGCAGACCAGATGA
Enzyme 41 GenBank Gene ID AF335278 Link Image
Enzyme 41 GeneCard ID CYP2S1 Link Image
Enzyme 41 GenAtlas ID CYP2S1 Link Image
Enzyme 41 HGNC ID HGNC:15654 Link Image
Enzyme 41 Chromosome Location 1
Enzyme 41 Locus 19q13.1
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Rylander T, Neve EP, Ingelman-Sundberg M, Oscarson M: Identification and tissue distribution of the novel human cytochrome P450 2S1 (CYP2S1). Biochem Biophys Res Commun. 2001 Feb 23;281(2):529-35. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 6861
Enzyme 42 Name Cytochrome P450 2J2
Enzyme 42 Synonyms
  1. Arachidonic acid epoxygenase
  2. CYPIIJ2
Enzyme 42 Gene Name CYP2J2
Enzyme 42 Protein Sequence >Cytochrome P450 2J2
MLAAMGSLAAALWAVVHPRTLLLGTVAFLLAADFLKRRRPKNYPPGPWRLPFLGNFFLVD
FEQSHLEVQLFVKKYGNLFSLELGDISAVLITGLPLIKEALIHMDQNFGNRPVTPMREHI
FKKNGLIMSSGQAWKEQRRFTLTALRNFGLGKKSLEERIQEEAQHLTEAIKEENGQPFDP
HFKINNAVSNIICSITFGERFEYQDSWFQQLLKLLDEVTYLEASKTCQLYNVFPWIMKFL
PGPHQTLFSNWKKLKLFVSHMIDKHRKDWNPAETRDFIDAYLKEMSKHTGNPTSSFHEEN
LICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQGQQPSTAARESMP
YTNAVIHEVQRMGNIIPLNVPREVTVDTTLAGYHLPKGTMILTNLTALHRDPTEWATPDT
FNPDHFLENGQFKKREAFMPFSIGKRACLGEQLARTELFIFFTSLMQKFTFRPPNNEKLS
LKFRMGITISPVSHRLCAVPQV
Enzyme 42 Number of Residues 502
Enzyme 42 Molecular Weight 57610.2
Enzyme 42 Theoretical pI 8.87
Enzyme 42 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 42 General Function Involved in monooxygenase activity
Enzyme 42 Specific Function This enzyme metabolizes arachidonic acid predominantly via a NADPH-dependent olefin epoxidation to all four regioisomeric cis-epoxyeicosatrienoic acids. One of the predominant enzymes responsible for the epoxidation of endogenous cardiac arachidonic acid pools
Enzyme 42 Pathways
Enzyme 42 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • None
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein Not Available
Enzyme 42 UniProtKB/Swiss-Prot ID P51589 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name CP2J2_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >1509 bp
ATGCTCGCGGCGATGGGCTCTCTGGCGGCTGCCCTCTGGGCAGTGGTCCATCCTCGGACT
CTCCTACTGGGCACTGTCGCCTTTCTGCTCGCTGCTGACTTTCTCAAAAGACGGCGCCCA
AAGAACTACCCGCCGGGGCCCTGGCGCCTGCCCTTCCTTGGCAACTTCTTCCTTGTGGAC
TTCGAGCAGTCGCACCTGGAGGTTCAGCTGTTTGTGAAGAAATATGGGAACCTTTTTAGC
TTGGAGCTTGGTGACATATCTGCAGTTCTTATTACTGGCTTGCCCTTAATCAAAGAAGCC
CTTATCCACATGGACCAAAACTTTGGGAACCGCCCCGTGACCCCTATGCGAGAACATATC
TTTAAGAAAAATGGATTGATTATGTCAAGTGGCCAGGCATGGAAGGAGCAAAGAAGGTTC
ACTCTGACAGCACTAAGGAACTTTGGTTTAGGAAAGAAGAGCTTAGAGGAACGCATTCAG
GAGGAGGCCCAACACCTCACTGAAGCAATAAAAGAGGAGAACGGACAGCCTTTTGACCCT
CATTTCAAGATCAACAATGCAGTTTCCAATATCATTTGCTCCATCACCTTCGGAGAACGC
TTTGAGTACCAGGATAGTTGGTTTCAGCAGCTGCTGAAGTTACTAGATGAAGTCACATAC
TTGGAGGCTTCAAAGACATGCCAGCTCTACAATGTCTTTCCATGGATAATGAAATTCCTG
CCTGGACCCCACCAAACTCTCTTCAGCAACTGGAAAAAACTGAAATTGTTTGTTTCTCAT
ATGATTGACAAACACAGAAAGGATTGGAATCCTGCAGAAACAAGAGACTTTATTGATGCT
TACCTTAAAGAAATGTCAAAGCACACAGGCAATCCTACTTCAAGTTTCCATGAAGAAAAC
CTCATCTGCAGCACCCTGGACCTCTTCTTTGCCGGAACCGAGACAACTTCCACAACTCTG
CGATGGGCTCTGCTTTATATGGCCCTCTACCCAGAAATCCAAGAAAAAGTACAAGCTGAG
ATTGACAGAGTGATTGGCCAGGGGCAGCAGCCGAGCACAGCCGCCCGGGAGTCCATGCCC
TACACCAATGCTGTCATCCATGAGGTGCAGAGAATGGGCAACATCATCCCCCTGAACGTT
CCCAGGGAAGTGACAGTTGATACCACTTTGGCTGGGTACCACCTGCCCAAGGGTACCATG
ATCCTGACCAATTTGACGGCGCTGCACAGGGACCCCACAGAGTGGGCCACCCCTGACACA
TTCAATCCGGACCATTTTCTGGAGAATGGACAGTTTAAGAAAAGGGAAGCCTTTATGCCT
TTCTCAATAGGAAAGCGGGCATGCCTCGGAGAACAGTTGGCCAGGACTGAGCTGTTTATT
TTCTTCACTTCCCTTATGCAAAAATTTACCTTCAGGCCCCCAAACAATGAGAAGCTGAGC
CTGAAGTTTAGAATGGGTATCACCATTTCCCCAGTCAGTCACCGCCTCTGCGCTGTTCCT
CAGGTGTAA
Enzyme 42 GenBank Gene ID U37143 Link Image
Enzyme 42 GeneCard ID CYP2J2 Link Image
Enzyme 42 GenAtlas ID CYP2J2 Link Image
Enzyme 42 HGNC ID HGNC:2634 Link Image
Enzyme 42 Chromosome Location 1
Enzyme 42 Locus 1p31.3-p31.2
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Wu S, Moomaw CR, Tomer KB, Falck JR, Zeldin DC: Molecular cloning and expression of CYP2J2, a human cytochrome P450 arachidonic acid epoxygenase highly expressed in heart. J Biol Chem. 1996 Feb 16;271(7):3460-8. [PubMed Link Image]
  2. King LM, Ma J, Srettabunjong S, Graves J, Bradbury JA, Li L, Spiecker M, Liao JK, Mohrenweiser H, Zeldin DC: Cloning of CYP2J2 gene and identification of functional polymorphisms. Mol Pharmacol. 2002 Apr;61(4):840-52. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 6862
Enzyme 43 Name Cytochrome P450 2A7
Enzyme 43 Synonyms
  1. CYPIIA7
  2. Cytochrome P450 IIA4
Enzyme 43 Gene Name CYP2A7
Enzyme 43 Protein Sequence >Cytochrome P450 2A7
MLASGLLLVALLACLTVMVLMSVWQQRKSRGKLPPGPTPLPFIGNYLQLNTEHICDSIMK
FSECYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVAFSN
GERAKQLLRFAIATLRDFGVGKRGIEERIQEESGFLIEAIRSTHGANIDPTFFLSRTVSN
VISSIVFGDRFDYEDKEFLSLLSMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFKL
LQGLEDFIAKKVEHNQRTLDPNSPQDFIDSFLIHMQEEEKNPNTEFYLKNLMMSTLNLFI
AGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRTKMPYMEAVIHEIQ
RFGDVIPMSLARRVKKDTKFRDFFLPKGTEVFPMLGSVLRDPSFFSNPQDFNPQHFLDDK
GQFKKSDAFVPFSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVVF
ATIPRNYTMSFLPR
Enzyme 43 Number of Residues 494
Enzyme 43 Molecular Weight 56424.7
Enzyme 43 Theoretical pI 7.96
Enzyme 43 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 43 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 43 Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics
Enzyme 43 Pathways
Enzyme 43 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • None
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 15147330 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID P20853 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name CP2A7_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >1485 bp
ATGCTGGCCTCAGGGCTGCTTCTGGTGGCCTTGCTGGCCTGCCTGACTGTGATGGTCTTG
ATGTCTGTCTGGCAGCAGAGGAAGAGCAGGGGGAAGCTGCCTCCGGGACCCACCCCACTG
CCCTTCATTGGAAACTACCTCCAGCTGAACACAGAGCACATATGTGACTCCATCATGAAG
TTCAGTGAGTGCTATGGCCCCGTGTTCACCATTCACTTGGGGCCCCGGCGGGTCGTGGTG
CTGTGTGGACATGATGCCGTCAGGGAGGCTCTGGTGGACCAGGCTGAGGAGTTCAGCGGG
CGAGGCGAGCAAGCCACCTTCGACTGGGTCTTCAAAGGCTATGGCGTGGCGTTCAGCAAC
GGGGAGCGCGCCAAGCAGCTCCTGCGCTTTGCCATCGCCACCCTGAGGGACTTCGGGGTG
GGCAAGCGAGGCATCGAGGAGCGCATCCAGGAGGAGTCGGGCTTCCTCATCGAGGCCATC
CGGAGCACGCACGGCGCCAATATCGATCCCACCTTCTTCCTGAGCCGCACAGTCTCCAAT
GTCATCAGCTCCATTGTCTTTGGGGACCGCTTTGACTATGAGGACAAAGAGTTCCTGTCA
CTGCTGAGCATGATGCTAGGAATCTTCCAGTTCACGTCAACCTCCACGGGGCAGCTCTAT
GAGATGTTCTCTTCGGTGATGAAACACCTGCCAGGACCACAGCAACAGGCCTTTAAGTTG
CTGCAAGGGCTGGAGGACTTCATAGCCAAGAAGGTGGAGCACAACCAGCGCACGCTGGAT
CCCAATTCCCCACAGGACTTCATCGACTCCTTTCTCATCCACATGCAGGAGGAGGAGAAG
AACCCCAACACGGAGTTCTACTTGAAGAACCTGATGATGAGCACGTTGAACCTCTTCATT
GCAGGCACCGAGACGGTCAGCACCACCCTGCGCTATGGCTTCTTGCTGCTCATGAAGCAC
CCAGAGGTGGAGGCCAAGGTCCATGAGGAGATTGACAGAGTGATCGGCAAGAACCGGCAG
CCCAAGTTTGAGGACCGGACCAAGATGCCCTACATGGAGGCAGTGATCCACGAGATCCAA
AGATTTGGAGACGTGATCCCCATGAGTTTGGCCCGCAGGGTTAAAAAGGACACCAAGTTT
CGGGATTTTTTCCTCCCTAAGGGCACCGAAGTGTTCCCTATGCTGGGCTCCGTGCTGAGA
GACCCCAGCTTCTTCTCCAACCCTCAGGACTTCAATCCCCAGCATTTCCTGGATGACAAG
GGGCAGTTTAAGAAGAGTGATGCTTTTGTGCCCTTTTCCATCGGAAAGCGGAACTGTTTC
GGAGAAGGCCTGGCCAGAATGGAGCTCTTTCTCTTCTTCACCACCGTCATGCAGAACTTC
CGCCTCAAGTCCTCCCAGTCACCTAAGGACATTGACGTGTCCCCCAAACACGTGGTCTTT
GCCACGATCCCACGAAACTACACCATGAGCTTCCTGCCCCGCTGA
Enzyme 43 GenBank Gene ID NM_000764.2 Link Image
Enzyme 43 GeneCard ID CYP2A7 Link Image
Enzyme 43 GenAtlas ID Not Available
Enzyme 43 HGNC ID Not Available
Enzyme 43 Chromosome Location 1
Enzyme 43 Locus 19q13.2
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Yamano S, Tatsuno J, Gonzalez FJ: The CYP2A3 gene product catalyzes coumarin 7-hydroxylation in human liver microsomes. Biochemistry. 1990 Feb 6;29(5):1322-9. [PubMed Link Image]
  2. Fernandez-Salguero P, Hoffman SM, Cholerton S, Mohrenweiser H, Raunio H, Rautio A, Pelkonen O, Huang JD, Evans WE, Idle JR, et al.: A genetic polymorphism in coumarin 7-hydroxylation: sequence of the human CYP2A genes and identification of variant CYP2A6 alleles. Am J Hum Genet. 1995 Sep;57(3):651-60. [PubMed Link Image]
  3. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 6863
Enzyme 44 Name Cytochrome P450 2A6
Enzyme 44 Synonyms
  1. CYPIIA6
  2. Coumarin 7-hydroxylase
  3. Cytochrome P450 IIA3
  4. Cytochrome P450(I)
Enzyme 44 Gene Name CYP2A6
Enzyme 44 Protein Sequence >Cytochrome P450 2A6
MLASGMLLVALLVCLTVMVLMSVWQQRKSKGKLPPGPTPLPFIGNYLQLNTEQMYNSLMK
ISERYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVVFSN
GERAKQLRRFSIATLRDFGVGKRGIEERIQEEAGFLIDALRGTGGANIDPTFFLSRTVSN
VISSIVFGDRFDYKDKEFLSLLRMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFQL
LQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFI
GGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYMEAVIHEIQ
RFGDVIPMSLARRVKKDTKFRDFFLPKGTEVFPMLGSVLRDPSFFSNPQDFNPQHFLNEK
GQFKKSDAFVPFSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVGF
ATIPRNYTMSFLPR
Enzyme 44 Number of Residues 494
Enzyme 44 Molecular Weight 56501.0
Enzyme 44 Theoretical pI 9.72
Enzyme 44 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 44 General Function Involved in monooxygenase activity
Enzyme 44 Specific Function Exhibits a high coumarin 7-hydroxylase activity. Can act in the hydroxylation of the anti-cancer drugs cyclophosphamide and ifosphamide. Competent in the metabolic activation of aflatoxin B1. Constitutes the major nicotine C-oxidase. Possesses low phenacetin O-deethylation activity
Enzyme 44 Pathways
Enzyme 44 Reactions
  • RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O [RN:R04122]
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • None
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 189339233 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID P11509 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name CP2A6_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence >1485 bp
ATGCTGGCCTCAGGGATGCTTCTGGTGGCCTTGCTGGTCTGCCTGACTGTAATGGTCTTG
ATGTCTGTTTGGCAGCAGAGGAAGAGCAAGGGGAAGCTGCCTCCGGGACCCACCCCATTG
CCCTTCATTGGAAACTACCTGCAGCTGAACACAGAGCAGATGTACAACTCCCTCATGAAG
ATCAGTGAGCGCTATGGCCCCGTGTTCACCATTCACTTGGGGCCCCGGCGGGTCGTGGTG
CTGTGTGGACATGATGCCGTCAGGGAGGCTCTGGTGGACCAGGCTGAGGAGTTCAGCGGG
CGAGGCGAGCAAGCCACCTTCGACTGGGTCTTCAAAGGCTATGGCGTGGTATTCAGCAAC
GGGGAGCGCGCCAAGCAGCTCCGGCGCTTCTCCATCGCCACCCTGCGGGACTTCGGGGTG
GGCAAGCGAGGCATCGAGGAGCGCATCCAGGAGGAGGCGGGCTTCCTCATCGACGCCCTC
CGGGGCACTGGCGGCGCCAATATCGATCCCACCTTCTTCCTGAGCCGCACAGTCTCCAAT
GTCATCAGCTCCATTGTCTTTGGGGACCGCTTTGACTATAAGGACAAAGAGTTCCTGTCA
CTGTTGCGCATGATGCTAGGAATCTTCCAGTTCACGTCAACCTCCACGGGGCAGCTCTAT
GAGATGTTCTCTTCGGTGATGAAACACCTGCCAGGACCACAGCAACAGGCCTTTCAGTTG
CTGCAAGGGCTGGAGGACTTCATAGCCAAGAAGGTGGAGCACAACCAGCGCACGCTGGAT
CCCAATTCCCCACGGGACTTCATTGACTCCTTTCTCATCCGCATGCAGGAGGAGGAGAAG
AACCCCAACACGGAGTTCTACTTGAAAAACCTGGTGATGACCACGTTGAACCTCTTCATT
GGGGGCACCGAGACCGTCAGCACCACCCTGCGCTATGGCTTCTTGCTGCTCATGAAGCAC
CCAGAGGTGGAGGCCAAGGTCCATGAGGAGATTGACAGAGTGATCGGCAAGAACCGGCAG
CCCAAGTTTGAGGACCGGGCCAAGATGCCCTACATGGAGGCAGTGATCCACGAGATCCAA
AGATTTGGAGACGTGATCCCCATGAGTTTGGCCCGCAGAGTCAAAAAGGACACCAAGTTT
CGGGATTTCTTCCTCCCTAAGGGCACCGAAGTGTACCCTATGCTGGGCTCTGTGCTGAGA
GACCCCAGTTTCTTCTCCAACCCCCAGGACTTCAATCCCCAGCACTTCCTGAATGAGAAG
GGGCAGTTTAAGAAGAGTGATGCTTTTGTGCCCTTTTCCATCGGAAAGCGGAACTGTTTC
GGAGAAGGCCTGGCCAGAATGGAGCTCTTTCTCTTCTTCACCACCGTCATGCAGAACTTC
CGCCTCAAGTCCTCCCAGTCACCTAAGGACATTGACGTGTCCCCCAAACACGTGGGCTTT
GCCACGATCCCACGAAACTACACCATGAGCTTCCTGCCCCGCTGA
Enzyme 44 GenBank Gene ID NM_000762.5 Link Image
Enzyme 44 GeneCard ID CYP2A6 Link Image
Enzyme 44 GenAtlas ID CYP2A6 Link Image
Enzyme 44 HGNC ID HGNC:2610 Link Image
Enzyme 44 Chromosome Location 1
Enzyme 44 Locus 19q13.2
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References
  1. Miles JS, Bickmore W, Brook JD, McLaren AW, Meehan R, Wolf CR: Close linkage of the human cytochrome P450IIA and P450IIB gene subfamilies: implications for the assignment of substrate specificity. Nucleic Acids Res. 1989 Apr 25;17(8):2907-17. [PubMed Link Image]
  2. Yamano S, Nagata K, Yamazoe Y, Kato R, Gelboin HV, Gonzalez FJ: cDNA and deduced amino acid sequences of human P450 IIA3 (CYP2A3). Nucleic Acids Res. 1989 Jun 26;17(12):4888. [PubMed Link Image]
  3. Yamano S, Tatsuno J, Gonzalez FJ: The CYP2A3 gene product catalyzes coumarin 7-hydroxylation in human liver microsomes. Biochemistry. 1990 Feb 6;29(5):1322-9. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Maurice M, Emiliani S, Dalet-Beluche I, Derancourt J, Lange R: Isolation and characterization of a cytochrome P450 of the IIA subfamily from human liver microsomes. Eur J Biochem. 1991 Sep 1;200(2):511-7. [PubMed Link Image]
  8. Yun CH, Shimada T, Guengerich FP: Purification and characterization of human liver microsomal cytochrome P-450 2A6. Mol Pharmacol. 1991 Nov;40(5):679-85. [PubMed Link Image]
  9. Kitagawa K, Kunugita N, Kitagawa M, Kawamoto T: CYP2A6*6, a novel polymorphism in cytochrome p450 2A6, has a single amino acid substitution (R128Q) that inactivates enzymatic activity. J Biol Chem. 2001 May 25;276(21):17830-5. Epub 2001 Feb 16. [PubMed Link Image]
  10. Phillips IR, Shephard EA, Ashworth A, Rabin BR: Isolation and sequence of a human cytochrome P-450 cDNA clone. Proc Natl Acad Sci U S A. 1985 Feb;82(4):983-7. [PubMed Link Image]
  11. Yano JK, Hsu MH, Griffin KJ, Stout CD, Johnson EF: Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen. Nat Struct Mol Biol. 2005 Sep;12(9):822-3. Epub 2005 Aug 7. [PubMed Link Image]
  12. Yano JK, Denton TT, Cerny MA, Zhang X, Johnson EF, Cashman JR: Synthetic inhibitors of cytochrome P-450 2A6: inhibitory activity, difference spectra, mechanism of inhibition, and protein cocrystallization. J Med Chem. 2006 Nov 30;49(24):6987-7001. [PubMed Link Image]
  13. DeVore NM, Smith BD, Urban MJ, Scott EE: Key residues controlling phenacetin metabolism by human cytochrome P450 2A enzymes. Drug Metab Dispos. 2008 Dec;36(12):2582-90. Epub 2008 Sep 8. [PubMed Link Image]
  14. Hadidi H, Zahlsen K, Idle JR, Cholerton S: A single amino acid substitution (Leu160His) in cytochrome P450 CYP2A6 causes switching from 7-hydroxylation to 3-hydroxylation of coumarin. Food Chem Toxicol. 1997 Sep;35(9):903-7. [PubMed Link Image]
  15. Oscarson M, McLellan RA, Gullsten H, Agundez JA, Benitez J, Rautio A, Raunio H, Pelkonen O, Ingelman-Sundberg M: Identification and characterisation of novel polymorphisms in the CYP2A locus: implications for nicotine metabolism. FEBS Lett. 1999 Oct 29;460(2):321-7. [PubMed Link Image]
  16. Ariyoshi N, Sawamura Y, Kamataki T: A novel single nucleotide polymorphism altering stability and activity of CYP2a6. Biochem Biophys Res Commun. 2001 Mar 2;281(3):810-4. [PubMed Link Image]
  17. Kiyotani K, Fujieda M, Yamazaki H, Shimada T, Guengerich FP, Parkinson A, Nakagawa K, Ishizaki T, Kamataki T: Twenty one novel single nucleotide polymorphisms (SNPs) of the CYP2A6 gene in Japanese and Caucasians. Drug Metab Pharmacokinet. 2002;17(5):482-7. [PubMed Link Image]
  18. Saito S, Iida A, Sekine A, Kawauchi S, Higuchi S, Ogawa C, Nakamura Y: Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population. J Hum Genet. 2003;48(5):249-70. Epub 2003 Apr 29. [PubMed Link Image]
  19. Solus JF, Arietta BJ, Harris JR, Sexton DP, Steward JQ, McMunn C, Ihrie P, Mehall JM, Edwards TL, Dawson EP: Genetic variation in eleven phase I drug metabolism genes in an ethnically diverse population. Pharmacogenomics. 2004 Oct;5(7):895-931. [PubMed Link Image]
  20. Mwenifumbo JC, Al Koudsi N, Ho MK, Zhou Q, Hoffmann EB, Sellers EM, Tyndale RF: Novel and established CYP2A6 alleles impair in vivo nicotine metabolism in a population of Black African descent. Hum Mutat. 2008 May;29(5):679-88. [PubMed Link Image]
  21. Ho MK, Mwenifumbo JC, Zhao B, Gillam EM, Tyndale RF: A novel CYP2A6 allele, CYP2A6*23, impairs enzyme function in vitro and in vivo and decreases smoking in a population of Black-African descent. Pharmacogenet Genomics. 2008 Jan;18(1):67-75. [PubMed Link Image]
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 6946
Enzyme 45 Name Sex hormone-binding globulin
Enzyme 45 Synonyms
  1. SHBG
  2. Sex steroid-binding protein
  3. SBP
  4. Testis-specific androgen-binding protein
  5. ABP
  6. Testosterone-estradiol-binding globulin
  7. TeBG
  8. Testosterone-estrogen-binding globulin
Enzyme 45 Gene Name SHBG
Enzyme 45 Protein Sequence >Sex hormone-binding globulin
MESRGPLATSRLLLLLLLLLLRHTRQGWALRPVLPTQSAHDPPAVHLSNGPGQEPIAVMT
FDLTKITKTSSSFEVRTWDPEGVIFYGDTNPKDDWFMLGLRDGRPEIQLHNHWAQLTVGA
GPRLDDGRWHQVEVKMEGDSVLLEVDGEEVLRLRQVSGPLTSKRHPIMRIALGGLLFPAS
NLRLPLVPALDGCLRRDSWLDKQAEISASAPTSLRSCDVESNPGIFLPPGTQAEFNLRDI
PQPHAEPWAFSLDLGLKQAAGSGHLLALGTPENPSWLSLHLQDQKVVLSSGSGPGLDLPL
VLGLPLQLKLSMSRVVLSQGSKMKALALPPLGLAPLLNLWAKPQGRLFLGALPGEDSSTS
FCLNGLWAQGQRLDVDQALNRSHEIWTHSCPQSPGNGTDASH
Enzyme 45 Number of Residues 402
Enzyme 45 Molecular Weight 43778.8
Enzyme 45 Theoretical pI 6.70
Enzyme 45 GO Classification Not Available
Enzyme 45 General Function Involved in androgen binding
Enzyme 45 Specific Function Functions as an androgen transport protein, but may also be involved in receptor mediated processes. Each dimer binds one molecule of steroid. Specific for 5-alpha-dihydrotestosterone, testosterone, and 17-beta-estradiol. Regulates the plasma metabolic clearance rate of steroid hormones by controlling their plasma concentration
Enzyme 45 Pathways Not Available
Enzyme 45 Reactions Not Available
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • 1-29
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 7382460 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID P04278 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name SHBG_HUMAN Link Image
Enzyme 45 PDB ID 1F5F Link Image
Enzyme 45 PDB File Show
Enzyme 45 3D Structure
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >1209 bp
ATGGAGAGCAGAGGCCCACTGGCTACCTCGCGCCTGCTGCTGTTGCTGCTGTTGCTACTA
CTGCGTCACACCCGCCAGGGATGGGCCCTGAGACCTGTTCTCCCCACCCAGAGTGCCCAC
GACCCTCCGGCTGTCCACCTCAGCAATGGCCCAGGACAAGAGCCTATCGCTGTCATGACC
TTTGACCTCACCAAGATCACAAAAACCTCCTCCTCCTTTGAGGTTCGAACCTGGGACCCA
GAGGGAGTGATTTTTTATGGGGATACCAACCCTAAGGATGACTGGTTTATGCTGGGACTT
CGAGACGGCAGGCCTGAGATCCAACTGCACAATCACTGGGCCCAGCTTACGGTGGGTGCT
GGACCACGGCTGGATGATGGGAGATGGCACCAGGTGGAAGTCAAGATGGAGGGGGACTCT
GTGCTGCTGGAGGTGGATGGGGAGGAGGTGCTGCGCCTGAGACAGGTCTCTGGGCCCCTG
ACCAGCAAACGCCATCCCATCATGAGGATTGCGCTTGGGGGGCTGCTCTTCCCCGCTTCC
AACCTTCGGTTGCCGCTGGTTCCTGCCCTGGATGGCTGCCTGCGCCGGGATTCCTGGCTG
GACAAACAGGCCGAGATCTCAGCATCTGCCCCCACTAGCCTCAGAAGCTGTGATGTAGAA
TCAAATCCCGGGATATTTCTCCCTCCAGGGACTCAGGCAGAATTCAATCTCCGAGACATT
CCCCAGCCTCATGCAGAGCCCTGGGCCTTCTCTTTGGACCTGGGACTCAAGCAGGCAGCA
GGCTCAGGCCACCTCCTTGCTCTTGGGACACCAGAGAACCCATCTTGGCTCAGTCTCCAC
CTCCAAGATCAAAAGGTGGTGTTGTCTTCTGGGTCGGGGCCAGGGCTGGATCTGCCCCTG
GTCTTGGGACTCCCTCTTCAGCTGAAGCTGAGTATGTCCAGGGTGGTCTTGAGCCAAGGG
TCGAAGATGAAGGCCCTTGCCCTGCCTCCCTTAGGCCTGGCTCCCCTCCTTAACCTCTGG
GCCAAGCCTCAAGGGCGTCTCTTCCTGGGGGCTTTACCAGGAGAAGACTCTTCCACCTCT
TTTTGCCTGAATGGCCTTTGGGCACAAGGTCAGAGGCTGGATGTGGACCAGGCCCTGAAC
AGAAGCCATGAGATCTGGACTCACAGCTGCCCCCAGAGCCCAGGCAATGGCACTGACGCT
TCCCATTAA
Enzyme 45 GenBank Gene ID NM_001040.3 Link Image
Enzyme 45 GeneCard ID SHBG Link Image
Enzyme 45 GenAtlas ID SHBG Link Image
Enzyme 45 HGNC ID HGNC:10839 Link Image
Enzyme 45 Chromosome Location 1
Enzyme 45 Locus 17p13-p12
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References
  1. Gershagen S, Lundwall A, Fernlund P: Characterization of the human sex hormone binding globulin (SHBG) gene and demonstration of two transcripts in both liver and testis. Nucleic Acids Res. 1989 Nov 25;17(22):9245-58. [PubMed Link Image]
  2. Hammond GL, Underhill DA, Rykse HM, Smith CL: The human sex hormone-binding globulin gene contains exons for androgen-binding protein and two other testicular messenger RNAs. Mol Endocrinol. 1989 Nov;3(11):1869-76. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Hammond GL, Underhill DA, Smith CL, Goping IS, Harley MJ, Musto NA, Cheng CY, Bardin CW: The cDNA-deduced primary structure of human sex hormone-binding globulin and location of its steroid-binding domain. FEBS Lett. 1987 May 4;215(1):100-4. [PubMed Link Image]
  5. Gershagen S, Fernlund P, Lundwall A: A cDNA coding for human sex hormone binding globulin. Homology to vitamin K-dependent protein S. FEBS Lett. 1987 Aug 10;220(1):129-35. [PubMed Link Image]
  6. Que BG, Petra PH: Characterization of a cDNA coding for sex steroid-binding protein of human plasma. FEBS Lett. 1987 Jul 27;219(2):405-9. [PubMed Link Image]
  7. Hammond GL, Robinson PA, Sugino H, Ward DN, Finne J: Physicochemical characteristics of human sex hormone binding globulin: evidence for two identical subunits. J Steroid Biochem. 1986 Apr;24(4):815-24. [PubMed Link Image]
  8. Walsh KA, Titani K, Takio K, Kumar S, Hayes R, Petra PH: Amino acid sequence of the sex steroid binding protein of human blood plasma. Biochemistry. 1986 Nov 18;25(23):7584-90. [PubMed Link Image]
  9. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
  10. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  11. Power SG, Bocchinfuso WP, Pallesen M, Warmels-Rodenhiser S, Van Baelen H, Hammond GL: Molecular analyses of a human sex hormone-binding globulin variant: evidence for an additional carbohydrate chain. J Clin Endocrinol Metab. 1992 Oct;75(4):1066-70. [PubMed Link Image]
  12. Grishkovskaya I, Avvakumov GV, Sklenar G, Dales D, Hammond GL, Muller YA: Crystal structure of human sex hormone-binding globulin: steroid transport by a laminin G-like domain. EMBO J. 2000 Feb 15;19(4):504-12. [PubMed Link Image]
  13. Grishkovskaya I, Avvakumov GV, Hammond GL, Catalano MG, Muller YA: Steroid ligands bind human sex hormone-binding globulin in specific orientations and produce distinct changes in protein conformation. J Biol Chem. 2002 Aug 30;277(35):32086-93. Epub 2002 Jun 13. [PubMed Link Image]
  14. Hardy DO, Carino C, Catterall JF, Larrea F: Molecular characterization of a genetic variant of the steroid hormone-binding globulin gene in heterozygous subjects. J Clin Endocrinol Metab. 1995 Apr;80(4):1253-6. [PubMed Link Image]
  15. Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed Link Image]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 7556
Enzyme 46 Name Serum albumin
Enzyme 46 Synonyms Not Available
Enzyme 46 Gene Name ALB
Enzyme 46 Protein Sequence >Serum albumin
MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPF
EDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEP
ERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLF
FAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAV
ARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLK
ECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYAR
RHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFE
QLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVV
LNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTL
SEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLV
AASQAALGL
Enzyme 46 Number of Residues 609
Enzyme 46 Molecular Weight 69365.9
Enzyme 46 Theoretical pI 6.21
Enzyme 46 GO Classification
Function
Process
  • establishment of localization
  • transport
Component
  • extracellular region part
  • extracellular space
Enzyme 46 General Function Involved in transport
Enzyme 46 Specific Function Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • 1-18
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 28590 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID P02768 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name ALBU_HUMAN Link Image
Enzyme 46 PDB ID 1HA2 Link Image
Enzyme 46 PDB File Show
Enzyme 46 3D Structure
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >1830 bp
ATGAAGTGGGTAACCTTTATTTCCCTTCTTTTTCTCTTTAGCTCGGCTTATTCCAGGGGT
GTGTTTCGTCGAGATGCACACAAGAGTGAGGTTGCTCATCGGTTTAAAGATTTGGGAGAA
GAAAATTTCAAAGCCTTGGTGTTGATTGCCTTTGCTCAGTATCTTCAGCAGTGTCCATTT
GAAGATCATGTAAAATTAGTGAATGAAGTAACTGAATTTGCAAAAACATGTGTTGCTGAT
GAGTCAGCTGAAAATTGTGACAAATCACTTCATACCCTTTTTGGAGACAAATTATGCACA
GTTGCAACTCTTCGTGAAACCTATGGTGAAATGGCTGACTGCTGTGCAAAACAAGAACCT
GGGAGAAATGAATGCTTCTTGCAACACAAAGATGACAACCCAAACCTCCCCCGATTGGTG
AGACCAGAGGTTGATGTGATGTGCACTGCTTTTCATGACAATGAAGAGACATTTTTGAAA
AAATACTTATATGAAATTGCCAGAAGACATCCTTACTTTTATGCCCCGGAACTCCTTTTC
TTTGCTAAAAGGTATAAAGCTGCTTTTACAGAATGTTGCCAAGCTGCTGATAAAGCTGCC
TGCCTGTTGCCAAAGCTCGATGAACTTCGGGATGAAGGGAAGGCTTCGTCTGCCAAACAG
AGACTCAAGTGTGCCAGTCTCCAAAAATTTGGAGAAAGAGCTTTCAAAGCATGGGCAGTA
GCTCGCCTGAGCCAGAGATTTCCCAAAGCTGAGTTTGCAGAAGTTTCCAAGTTAGTGACA
GATCTTACCAAAGTCCACACGGAATGCTGCCATGGAGATCTGCTTGAATGTGCTGATGAC
AGGGCGGACCTTGCCAAGTATATCTGTGAAAATCAAGATTCGATCTCCAGTAAACTGAAG
GAATGCTGTGAAAAACCTCTGTTGGAAAAATCCCACTGCATTGCCGAAGTGGAAAATGAT
GAGATGCCTGCTGACTTGCCTTCATTAGCTGCTGATTTTGTTGAAAGTAAGGATGTTTGC
AAAAACTATGCTGAGGCAAAGGATGTCTTCTTGGGCATGTTTTTGTATGAATATGCAAGA
AGGCATCCTGATTACTCTGTCGTGCTGCTGCTGAGACTTGCCAAGACATATGAAACCACT
CTAGAGAAGTGCTGTGCCGCTGCAGATCCTCATGAATGCTATGCCAAAGTGTTCGATGAA
TTTAAACCTCTTGTGGAAGAGCCTCAGAATTTAATCAAACAAAATTGTGAGCTTTTTGAG
CAGCTTGGAGAGTACAAATTCCAGAATGCGCTGTTAGTTCGTTACACCAAGAAAGTACCC
GAAGTGTCAACTCCAACTCTTGTAGAGGTCTCAAGAAACCTAGGAAAAGTGGGCAGCAAA
TGTTGTAAACATCCTGAAGCAAAAAGAATGCCCTGTGCAGAAGACTATCTATCCGTGGTC
CTGAACCAGTTATGTGTGTTGCATGAGAAAACGCCAGTAAGTGACAGAGTCACCAAATGC
TGCACAGAATCCTTGGTGAACAGGCGACCATGCTTTTCAGCTCTGGAAGTCGATGAAACA
TACGTTCCCAAAGAGTTTAATGCTGAAACATTCACCTTCCATGCAGATATATGCACACTT
TCTGAGAAGGAGAGACAAATCAAGAAACAAACTGCACTTGTTGAGCTCGTGAAACACAAG
CCCAAGGCAACAAAAGAGCAACTGAAAGCTGTTATGGATGATTTCGCTGCTTTTGTAGAG
AAGTGCTGCAAGGCTGACGATAAGGAGACCTGCTTTGCCGAGGAGGGTAAAAAACTTGTT
GCTGCAAGTCAAGCTGCCTTAGGCTTATAA
Enzyme 46 GenBank Gene ID V00494 Link Image
Enzyme 46 GeneCard ID ALB Link Image
Enzyme 46 GenAtlas ID ALB Link Image
Enzyme 46 HGNC ID HGNC:399 Link Image
Enzyme 46 Chromosome Location 4
Enzyme 46 Locus 4q13.3
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Lawn RM, Adelman J, Bock SC, Franke AE, Houck CM, Najarian RC, Seeburg PH, Wion KL: The sequence of human serum albumin cDNA and its expression in E. coli. Nucleic Acids Res. 1981 Nov 25;9(22):6103-114. [PubMed Link Image]
  2. Dugaiczyk A, Law SW, Dennison OE: Nucleotide sequence and the encoded amino acids of human serum albumin mRNA. Proc Natl Acad Sci U S A. 1982 Jan;79(1):71-5. [PubMed Link Image]
  3. Minghetti PP, Ruffner DE, Kuang WJ, Dennison OE, Hawkins JW, Beattie WG, Dugaiczyk A: Molecular structure of the human albumin gene is revealed by nucleotide sequence within q11-22 of chromosome 4. J Biol Chem. 1986 May 25;261(15):6747-57. [PubMed Link Image]
  4. Yu Y, Zhang C, Zhou G, Wu S, Qu X, Wei H, Xing G, Dong C, Zhai Y, Wan J, Ouyang S, Li L, Zhang S, Zhou K, Zhang Y, Wu C, He F: Gene expression profiling in human fetal liver and identification of tissue- and developmental-stage-specific genes through compiled expression profiles and efficient cloning of full-length cDNAs. Genome Res. 2001 Aug;11(8):1392-403. [PubMed Link Image]
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  8. Urano Y, Watanabe K, Sakai M, Tamaoki T: The human albumin gene. Characterization of the 5' and 3' flanking regions and the polymorphic gene transcripts. J Biol Chem. 1986 Mar 5;261(7):3244-51. [PubMed Link Image]
  9. Meloun B, Moravek L, Kostka V: Complete amino acid sequence of human serum albumin. FEBS Lett. 1975 Oct 15;58(1):134-7. [PubMed Link Image]
  10. Corbett JM, Wheeler CH, Baker CS, Yacoub MH, Dunn MJ: The human myocardial two-dimensional gel protein database: update 1994. Electrophoresis. 1994 Nov;15(11):1459-65. [PubMed Link Image]
  11. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  12. Mogard MH, Kobayashi R, Chen CF, Lee TD, Reeve JR Jr, Shively JE, Walsh JH: The amino acid sequence of kinetensin, a novel peptide isolated from pepsin-treated human plasma: homology with human serum albumin, neurotensin and angiotensin. Biochem Biophys Res Commun. 1986 May 14;136(3):983-8. [PubMed Link Image]
  13. Carraway RE, Mitra SP, Cochrane DE: Structure of a biologically active neurotensin-related peptide obtained from pepsin-treated albumin(s). J Biol Chem. 1987 May 5;262(13):5968-73. [PubMed Link Image]
  14. Walker JE: Lysine residue 199 of human serum albumin is modified by acetylsalicyclic acid. FEBS Lett. 1976 Jul 15;66(2):173-5. [PubMed Link Image]
  15. Lapolla A, Fedele D, Reitano R, Arico NC, Seraglia R, Traldi P, Marotta E, Tonani R: Enzymatic digestion and mass spectrometry in the study of advanced glycation end products/peptides. J Am Soc Mass Spectrom. 2004 Apr;15(4):496-509. [PubMed Link Image]
  16. Jacobsen C: Lysine residue 240 of human serum albumin is involved in high-affinity binding of bilirubin. Biochem J. 1978 May 1;171(2):453-9. [PubMed Link Image]
  17. Garlick RL, Mazer JS: The principal site of nonenzymatic glycosylation of human serum albumin in vivo. J Biol Chem. 1983 May 25;258(10):6142-6. [PubMed Link Image]
  18. Shaklai N, Garlick RL, Bunn HF: Nonenzymatic glycosylation of human serum albumin alters its conformation and function. J Biol Chem. 1984 Mar 25;259(6):3812-7. [PubMed Link Image]
  19. Iberg N, Fluckiger R: Nonenzymatic glycosylation of albumin in vivo. Identification of multiple glycosylated sites. J Biol Chem. 1986 Oct 15;261(29):13542-5. [PubMed Link Image]
  20. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed Link Image]
  21. Lu J, Stewart AJ, Sadler PJ, Pinheiro TJ, Blindauer CA: Albumin as a zinc carrier: properties of its high-affinity zinc-binding site. Biochem Soc Trans. 2008 Dec;36(Pt 6):1317-21. [PubMed Link Image]
  22. Han G, Ye M, Zhou H, Jiang X, Feng S, Jiang X, Tian R, Wan D, Zou H, Gu J: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. Proteomics. 2008 Apr;8(7):1346-61. [PubMed Link Image]
  23. Zhou W, Ross MM, Tessitore A, Ornstein D, Vanmeter A, Liotta LA, Petricoin EF 3rd: An initial characterization of the serum phosphoproteome. J Proteome Res. 2009 Dec;8(12):5523-31. [PubMed Link Image]
  24. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  25. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  26. Carter DC, He XM, Munson SH, Twigg PD, Gernert KM, Broom MB, Miller TY: Three-dimensional structure of human serum albumin. Science. 1989 Jun 9;244(4909):1195-8. [PubMed Link Image]
  27. Carter DC, He XM: Structure of human serum albumin. Science. 1990 Jul 20;249(4966):302-3. [PubMed Link Image]
  28. He XM, Carter DC: Atomic structure and chemistry of human serum albumin. Nature. 1992 Jul 16;358(6383):209-15. [PubMed Link Image]
  29. Curry S, Mandelkow H, Brick P, Franks N: Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat Struct Biol. 1998 Sep;5(9):827-35. [PubMed Link Image]
  30. Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K: Crystal structure of human serum albumin at 2.5 A resolution. Protein Eng. 1999 Jun;12(6):439-46. [PubMed Link Image]
  31. Bhattacharya AA, Curry S, Franks NP: Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures. J Biol Chem. 2000 Dec 8;275(49):38731-8. [PubMed Link Image]
  32. Petitpas I, Grune T, Bhattacharya AA, Curry S: Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids. J Mol Biol. 2001 Dec 14;314(5):955-60. [PubMed Link Image]
  33. Brennan SO, Herbert P: Albumin Canterbury (313 Lys----Asn). A point mutation in the second domain of serum albumin. Biochim Biophys Acta. 1987 Apr 8;912(2):191-7. [PubMed Link Image]
  34. Takahashi N, Takahashi Y, Blumberg BS, Putnam FW: Amino acid substitutions in genetic variants of human serum albumin and in sequences inferred from molecular cloning. Proc Natl Acad Sci U S A. 1987 Jul;84(13):4413-7. [PubMed Link Image]
  35. Takahashi N, Takahashi Y, Isobe T, Putnam FW, Fujita M, Satoh C, Neel JV: Amino acid substitutions in inherited albumin variants from Amerindian and Japanese populations. Proc Natl Acad Sci U S A. 1987 Nov;84(22):8001-5. [PubMed Link Image]
  36. Arai K, Ishioka N, Huss K, Madison J, Putnam FW: Identical structural changes in inherited albumin variants from different populations. Proc Natl Acad Sci U S A. 1989 Jan;86(2):434-8. [PubMed Link Image]
  37. Arai K, Madison J, Huss K, Ishioka N, Satoh C, Fujita M, Neel JV, Sakurabayashi I, Putnam FW: Point substitutions in Japanese alloalbumins. Proc Natl Acad Sci U S A. 1989 Aug;86(16):6092-6. [PubMed Link Image]
  38. Arai K, Madison J, Shimizu A, Putnam FW: Point substitutions in albumin genetic variants from Asia. Proc Natl Acad Sci U S A. 1990 Jan;87(1):497-501. [PubMed Link Image]
  39. Brennan SO, Myles T, Peach RJ, Donaldson D, George PM: Albumin Redhill (-1 Arg, 320 Ala----Thr): a glycoprotein variant of human serum albumin whose precursor has an aberrant signal peptidase cleavage site. Proc Natl Acad Sci U S A. 1990 Jan;87(1):26-30. [PubMed Link Image]
  40. Galliano M, Minchiotti L, Porta F, Rossi A, Ferri G, Madison J, Watkins S, Putnam FW: Mutations in genetic variants of human serum albumin found in Italy. Proc Natl Acad Sci U S A. 1990 Nov;87(22):8721-5. [PubMed Link Image]
  41. Watkins S, Madison J, Davis E, Sakamoto Y, Galliano M, Minchiotti L, Putnam FW: A donor splice mutation and a single-base deletion produce two carboxyl-terminal variants of human serum albumin. Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):5959-63. [PubMed Link Image]
  42. Madison J, Arai K, Sakamoto Y, Feld RD, Kyle RA, Watkins S, Davis E, Matsuda Y, Amaki I, Putnam FW: Genetic variants of serum albumin in Americans and Japanese. Proc Natl Acad Sci U S A. 1991 Nov 1;88(21):9853-7. [PubMed Link Image]
  43. Peach RJ, Brennan SO: Structural characterization of a glycoprotein variant of human serum albumin: albumin Casebrook (494 Asp----Asn). Biochim Biophys Acta. 1991 Jul 26;1097(1):49-54. [PubMed Link Image]
  44. Minchiotti L, Galliano M, Stoppini M, Ferri G, Crespeau H, Rochu D, Porta F: Two alloalbumins with identical electrophoretic mobility are produced by differently charged amino acid substitutions. Biochim Biophys Acta. 1992 Mar 12;1119(3):232-8. [PubMed Link Image]
  45. Carlson J, Sakamoto Y, Laurell CB, Madison J, Watkins S, Putnam FW: Alloalbuminemia in Sweden: structural study and phenotypic distribution of nine albumin variants. Proc Natl Acad Sci U S A. 1992 Sep 1;89(17):8225-9. [PubMed Link Image]
  46. Minchiotti L, Galliano M, Zapponi MC, Tenni R: The structural characterization and bilirubin-binding properties of albumin Herborn, a [Lys240-->Glu] albumin mutant. Eur J Biochem. 1993 Jun 1;214(2):437-44. [PubMed Link Image]
  47. Brennan SO, Fellowes AP: Albumin Hawkes Bay; a low level variant caused by loss of a sulphydryl group at position 177. Biochim Biophys Acta. 1993 Aug 4;1182(1):46-50. [PubMed Link Image]
  48. Galliano M, Minchiotti L, Iadarola P, Stoppini M, Giagnoni P, Watkins S, Madison J, Putnam FW: Protein and DNA sequence analysis of a 'private' genetic variant: albumin Ortonovo (Glu-505-->Lys). Biochim Biophys Acta. 1993 Nov 25;1225(1):27-32. [PubMed Link Image]
  49. Madison J, Galliano M, Watkins S, Minchiotti L, Porta F, Rossi A, Putnam FW: Genetic variants of human serum albumin in Italy: point mutants and a carboxyl-terminal variant. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6476-80. [PubMed Link Image]
  50. Sunthornthepvarakul T, Angkeow P, Weiss RE, Hayashi Y, Refetoff S: An identical missense mutation in the albumin gene results in familial dysalbuminemic hyperthyroxinemia in 8 unrelated families. Biochem Biophys Res Commun. 1994 Jul 29;202(2):781-7. [PubMed Link Image]
  51. Rushbrook JI, Becker E, Schussler GC, Divino CM: Identification of a human serum albumin species associated with familial dysalbuminemic hyperthyroxinemia. J Clin Endocrinol Metab. 1995 Feb;80(2):461-7. [PubMed Link Image]
  52. Wada N, Chiba H, Shimizu C, Kijima H, Kubo M, Koike T: A novel missense mutation in codon 218 of the albumin gene in a distinct phenotype of familial dysalbuminemic hyperthyroxinemia in a Japanese kindred. J Clin Endocrinol Metab. 1997 Oct;82(10):3246-50. [PubMed Link Image]
  53. Sunthornthepvarakul T, Likitmaskul S, Ngowngarmratana S, Angsusingha K, Kitvitayasak S, Scherberg NH, Refetoff S: Familial dysalbuminemic hypertriiodothyroninemia: a new, dominantly inherited albumin defect. J Clin Endocrinol Metab. 1998 May;83(5):1448-54. [PubMed Link Image]
  54. Spahr CS, Davis MT, McGinley MD, Robinson JH, Bures EJ, Beierle J, Mort J, Courchesne PL, Chen K, Wahl RC, Yu W, Luethy R, Patterson SD: Towards defining the urinary proteome using liquid chromatography-tandem mass spectrometry. I. Profiling an unfractionated tryptic digest. Proteomics. 2001 Jan;1(1):93-107. [PubMed Link Image]
  55. Minchiotti L, Campagnoli M, Rossi A, Cosulich ME, Monti M, Pucci P, Kragh-Hansen U, Granel B, Disdier P, Weiller PJ, Galliano M: A nucleotide insertion and frameshift cause albumin Kenitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges. Eur J Biochem. 2001 Jan;268(2):344-52. [PubMed Link Image]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 7559
Enzyme 47 Name Estrogen receptor
Enzyme 47 Synonyms
  1. ER
  2. ER-alpha
  3. Estradiol receptor
  4. Nuclear receptor subfamily 3 group A member 1
Enzyme 47 Gene Name ESR1
Enzyme 47 Protein Sequence >Estrogen receptor
MTMTLHTKASGMALLHQIQGNELEPLNRPQLKIPLERPLGEVYLDSSKPAVYNYPEGAAY
EFNAAAAANAQVYGQTGLPYGPGSEAAAFGSNGLGGFPPLNSVSPSPLMLLHPPPQLSPF
LQPHGQQVPYYLENEPSGYTVREAGPPAFYRPNSDNRRQGGRERLASTNDKGSMAMESAK
ETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQAC
RLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDGEGRGEVGSAGDMRAANLWPSPLMIKR
SKKNSLALSLTADQMVSALLDAEPPILYSEYDPTRPFSEASMMGLLTNLADRELVHMINW
AKRVPGFVDLTLHDQVHLLECAWLEILMIGLVWRSMEHPGKLLFAPNLLLDRNQGKCVEG
MVEIFDMLLATSSRFRMMNLQGEEFVCLKSIILLNSGVYTFLSSTLKSLEEKDHIHRVLD
KITDTLIHLMAKAGLTLQQQHQRLAQLLLILSHIRHMSNKGMEHLYSMKCKNVVPLYDLL
LEMLDAHRLHAPTSRGGASVEETDQSHLATAGSTSSHSLQKYYITGEAEGFPATV
Enzyme 47 Number of Residues 595
Enzyme 47 Molecular Weight 66215.4
Enzyme 47 Theoretical pI 8.14
Enzyme 47 GO Classification
Function
  • DNA binding
  • binding
  • cation binding
  • ion binding
  • ligand-dependent nuclear receptor activity
  • lipid binding
  • metal ion binding
  • molecular transducer activity
  • nucleic acid binding
  • receptor activity
  • sequence-specific DNA binding
  • sequence-specific DNA binding transcription factor activity
  • signal transducer activity
  • steroid binding
  • steroid hormone receptor activity
  • transition metal ion binding
  • zinc ion binding
Process
  • biological regulation
  • regulation of biological process
  • regulation of gene expression
  • regulation of macromolecule metabolic process
  • regulation of metabolic process
  • regulation of transcription
  • regulation of transcription, DNA-dependent
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • nucleus
  • organelle
Enzyme 47 General Function Involved in sequence-specific DNA binding transcription factor activity
Enzyme 47 Specific Function Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Can activate the transcriptional activity of TFF1
Enzyme 47 Pathways Not Available
Enzyme 47 Reactions Not Available
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 31234 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID P03372 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name ESR1_HUMAN Link Image
Enzyme 47 PDB ID 1R5K Link Image
Enzyme 47 PDB File Show
Enzyme 47 3D Structure
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence >1788 bp
ATGACCATGACCCTCCACACCAAAGCATCTGGGATGGCCCTACTGCATCAGATCCAAGGG
AACGAGCTGGAGCCCCTGAACCGTCCGCAGCTCAAGATCCCCCTGGAGCGGCCCCTGGGC
GAGGTGTACCTGGACAGCAGCAAGCCCGCCGTGTACAACTACCCCGAGGGCGCCGCCTAC
GAGTTCAACGCCGCGGCCGCCGCCAACGCGCAGGTCTACGGTCAGACCGGCCTCCCCTAC
GGCCCCGGGTCTGAGGCTGCGGCGTTCGGCTCCAACGGCCTGGGGGGTTTCCCCCCACTC
AACAGCGTGTCTCCGAGCCCGCTGATGCTACTGCACCCGCCGCCGCAGCTGTCGCCTTTC
CTGCAGCCCCACGGCCAGCAGGTGCCCTACTACCTGGAGAACGAGCCCAGCGGCTACACG
GTGCGCGAGGCCGGCCCGCCGGCATTCTACAGGCCAAATTCAGATAATCGACGCCAGGGT
GGCAGAGAAAGATTGGCCAGTACCAATGACAAGGGAAGTATGGCTATGGAATCTGCCAAG
GAGACTCGCTACTGTGCAGTGTGCAATGACTATGCTTCAGGCTACCATTATGGAGTCTGG
TCCTGTGAGGGCTGCAAGGCCTTCTTCAAGAGAAGTATTCAAGGACATAACGACTATATG
TGTCCAGCCACCAACCAGTGCACCATTGATAAAAACAGGAGGAAGAGCTGCCAGGCCTGC
CGGCTCCGCAAATGCTACGAAGTGGGAATGATGAAAGGTGGGATACGAAAAGACCGAAGA
GGAGGGAGAATGTTGAAACACAAGCGCCAGAGAGATGATGGGGAGGGCAGGGGTGAAGTG
GGGTCTGCTGGAGACATGAGAGCTGCCAACCTTTGGCCAAGCCCGCTCATGATCAAACGC
TCTAAGAAGAACAGCCTGGCCTTGTCCCTGACGGCCGACCAGATGGTCAGTGCCTTGTTG
GATGCTGAGCCCCCCATACTCTATTCCGAGTATGATCCTACCAGACCCTTCAGTGAAGCT
TCGATGATGGGCTTACTGACCAACCTGGCAGACAGGGAGCTGGTTCACATGATCAACTGG
GCGAAGAGGGTGCCAGGCTTTGTGGATTTGACCCTCCATGATCAGGTCCACCTTCTAGAA
TGTGCCTGGCTAGAGATCCTGATGATTGGTCTCGTCTGGCGCTCCATGGAGCACCCAGTG
AAGCTACTGTTTGCTCCTAACTTGCTCTTGGACAGGAACCAGGGAAAATGTGTAGAGGGC
ATGGTGGAGATCTTCGACATGCTGCTGGCTACATCATCTCGGTTCCGCATGATGAATCTG
CAGGGAGAGGAGTTTGTGTGCCTCAAATCTATTATTTTGCTTAATTCTGGAGTGTACACA
TTTCTGTCCAGCACCCTGAAGTCTCTGGAAGAGAAGGACCATATCCACCGAGTCCTGGAC
AAGATCACAGACACTTTGATCCACCTGATGGCCAAGGCAGGCCTGACCCTGCAGCAGCAG
CACCAGCGGCTGGCCCAGCTCCTCCTCATCCTCTCCCACATCAGGCACATGAGTAACAAA
GGCATGGAGCATCTGTACAGCATGAAGTGCAAGAACGTGGTGCCCCTCTATGACCTGCTG
CTGGAGATGCTGGACGCCCACCGCCTACATGCGCCCACTAGCCGTGGAGGGGCATCCGTG
GAGGAGACGGACCAAAGCCACTTGGCCACTGCGGGCTCTACTTCATCGCATTCCTTGCAA
AAGTATTACATCACGGGGGAGGCAGAGGGTTTCCCTGCCACAGTCTGA
Enzyme 47 GenBank Gene ID X03635 Link Image
Enzyme 47 GeneCard ID ESR1 Link Image
Enzyme 47 GenAtlas ID ESR1 Link Image
Enzyme 47 HGNC ID HGNC:3467 Link Image
Enzyme 47 Chromosome Location 6
Enzyme 47 Locus 6q25.1
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References
  1. Green S, Walter P, Kumar V, Krust A, Bornert JM, Argos P, Chambon P: Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A. Nature. 1986 Mar 13-19;320(6058):134-9. [PubMed Link Image]
  2. Greene GL, Gilna P, Waterfield M, Baker A, Hort Y, Shine J: Sequence and expression of human estrogen receptor complementary DNA. Science. 1986 Mar 7;231(4742):1150-4. [PubMed Link Image]
  3. Pink JJ, Wu SQ, Wolf DM, Bilimoria MM, Jordan VC: A novel 80 kDa human estrogen receptor containing a duplication of exons 6 and 7. Nucleic Acids Res. 1996 Mar 1;24(5):962-9. [PubMed Link Image]
  4. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  5. Joel PB, Traish AM, Lannigan DA: Estradiol and phorbol ester cause phosphorylation of serine 118 in the human estrogen receptor. Mol Endocrinol. 1995 Aug;9(8):1041-52. [PubMed Link Image]
  6. Schubert EL, Lee MK, Newman B, King MC: Single nucleotide polymorphisms (SNPs) in the estrogen receptor gene and breast cancer susceptibility. J Steroid Biochem Mol Biol. 1999 Nov;71(1-2):21-7. [PubMed Link Image]
  7. Pfeffer U, Fecarotta E, Castagnetta L, Vidali G: Estrogen receptor variant messenger RNA lacking exon 4 in estrogen-responsive human breast cancer cell lines. Cancer Res. 1993 Feb 15;53(4):741-3. [PubMed Link Image]
  8. Arnold SF, Obourn JD, Jaffe H, Notides AC: Phosphorylation of the human estrogen receptor on tyrosine 537 in vivo and by src family tyrosine kinases in vitro. Mol Endocrinol. 1995 Jan;9(1):24-33. [PubMed Link Image]
  9. Reese JC, Katzenellenbogen BS: Characterization of a temperature-sensitive mutation in the hormone binding domain of the human estrogen receptor. Studies in cell extracts and intact cells and their implications for hormone-dependent transcriptional activation. J Biol Chem. 1992 May 15;267(14):9868-73. [PubMed Link Image]
  10. Arnold SF, Obourn JD, Jaffe H, Notides AC: Serine 167 is the major estradiol-induced phosphorylation site on the human estrogen receptor. Mol Endocrinol. 1994 Sep;8(9):1208-14. [PubMed Link Image]
  11. Jiang MS, Hart GW: A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine. J Biol Chem. 1997 Jan 24;272(4):2421-8. [PubMed Link Image]
  12. Rubino D, Driggers P, Arbit D, Kemp L, Miller B, Coso O, Pagliai K, Gray K, Gutkind S, Segars J: Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action. Oncogene. 1998 May 14;16(19):2513-26. [PubMed Link Image]
  13. Rogatsky I, Trowbridge JM, Garabedian MJ: Potentiation of human estrogen receptor alpha transcriptional activation through phosphorylation of serines 104 and 106 by the cyclin A-CDK2 complex. J Biol Chem. 1999 Aug 6;274(32):22296-302. [PubMed Link Image]
  14. Lee SK, Anzick SL, Choi JE, Bubendorf L, Guan XY, Jung YK, Kallioniemi OP, Kononen J, Trent JM, Azorsa D, Jhun BH, Cheong JH, Lee YC, Meltzer PS, Lee JW: A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo. J Biol Chem. 1999 Nov 26;274(48):34283-93. [PubMed Link Image]
  15. Montano MM, Ekena K, Delage-Mourroux R, Chang W, Martini P, Katzenellenbogen BS: An estrogen receptor-selective coregulator that potentiates the effectiveness of antiestrogens and represses the activity of estrogens. Proc Natl Acad Sci U S A. 1999 Jun 8;96(12):6947-52. [PubMed Link Image]
  16. Abramovich C, Shen WF, Pineault N, Imren S, Montpetit B, Largman C, Humphries RK: Functional cloning and characterization of a novel nonhomeodomain protein that inhibits the binding of PBX1-HOX complexes to DNA. J Biol Chem. 2000 Aug 25;275(34):26172-7. [PubMed Link Image]
  17. Chan SW, Hong W: Retinoblastoma-binding protein 2 (Rbp2) potentiates nuclear hormone receptor-mediated transcription. J Biol Chem. 2001 Jul 27;276(30):28402-12. Epub 2001 May 17. [PubMed Link Image]
  18. Sauve F, McBroom LD, Gallant J, Moraitis AN, Labrie F, Giguere V: CIA, a novel estrogen receptor coactivator with a bifunctional nuclear receptor interacting determinant. Mol Cell Biol. 2001 Jan;21(1):343-53. [PubMed Link Image]
  19. Shao W, Halachmi S, Brown M: ERAP140, a conserved tissue-specific nuclear receptor coactivator. Mol Cell Biol. 2002 May;22(10):3358-72. [PubMed Link Image]
  20. Wong CW, McNally C, Nickbarg E, Komm BS, Cheskis BJ: Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade. Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):14783-8. Epub 2002 Nov 1. [PubMed Link Image]
  21. Hsiao PW, Fryer CJ, Trotter KW, Wang W, Archer TK: BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation. Mol Cell Biol. 2003 Sep;23(17):6210-20. [PubMed Link Image]
  22. Bu H, Kashireddy P, Chang J, Zhu YT, Zhang Z, Zheng W, Rao SM, Zhu YJ: ERBP, a novel estrogen receptor binding protein enhancing the activity of estrogen receptor. Biochem Biophys Res Commun. 2004 Apr 23;317(1):54-9. [PubMed Link Image]
  23. Damdimopoulos AE, Miranda-Vizuete A, Treuter E, Gustafsson JA, Spyrou G: An alternative splicing variant of the selenoprotein thioredoxin reductase is a modulator of estrogen signaling. J Biol Chem. 2004 Sep 10;279(37):38721-9. Epub 2004 Jun 14. [PubMed Link Image]
  24. Rayala SK, den Hollander P, Balasenthil S, Yang Z, Broaddus RR, Kumar R: Functional regulation of oestrogen receptor pathway by the dynein light chain 1. EMBO Rep. 2005 Jun;6(6):538-44. [PubMed Link Image]
  25. Wittmann BM, Fujinaga K, Deng H, Ogba N, Montano MM: The breast cell growth inhibitor, estrogen down regulated gene 1, modulates a novel functional interaction between estrogen receptor alpha and transcriptional elongation factor cyclin T1. Oncogene. 2005 Aug 25;24(36):5576-88. [PubMed Link Image]
  26. Mo R, Rao SM, Zhu YJ: Identification of the MLL2 complex as a coactivator for estrogen receptor alpha. J Biol Chem. 2006 Jun 9;281(23):15714-20. Epub 2006 Apr 7. [PubMed Link Image]
  27. Rayala SK, den Hollander P, Manavathi B, Talukder AH, Song C, Peng S, Barnekow A, Kremerskothen J, Kumar R: Essential role of KIBRA in co-activator function of dynein light chain 1 in mammalian cells. J Biol Chem. 2006 Jul 14;281(28):19092-9. Epub 2006 May 9. [PubMed Link Image]
  28. Wei X, Xu H, Kufe D: MUC1 oncoprotein stabilizes and activates estrogen receptor alpha. Mol Cell. 2006 Jan 20;21(2):295-305. [PubMed Link Image]
  29. Eriksson M, Samuelsson H, Samuelsson EB, Liu L, McKeehan WL, Benedikz E, Sundstrom E: The NMDAR subunit NR3A interacts with microtubule-associated protein 1S in the brain. Biochem Biophys Res Commun. 2007 Sep 14;361(1):127-32. Epub 2007 Jul 16. [PubMed Link Image]
  30. Zhang PJ, Zhao J, Li HY, Man JH, He K, Zhou T, Pan X, Li AL, Gong WL, Jin BF, Xia Q, Yu M, Shen BF, Zhang XM: CUE domain containing 2 regulates degradation of progesterone receptor by ubiquitin-proteasome. EMBO J. 2007 Apr 4;26(7):1831-42. Epub 2007 Mar 8. [PubMed Link Image]
  31. Han WD, Zhao YL, Meng YG, Zang L, Wu ZQ, Li Q, Si YL, Huang K, Ba JM, Morinaga H, Nomura M, Mu YM: Estrogenically regulated LRP16 interacts with estrogen receptor alpha and enhances the receptor's transcriptional activity. Endocr Relat Cancer. 2007 Sep;14(3):741-53. [PubMed Link Image]
  32. Luboshits G, Benayahu D: MS-KIF18A, a kinesin, is associated with estrogen receptor. J Cell Biochem. 2007 Feb 15;100(3):693-702. [PubMed Link Image]
  33. Yan J, Kim YS, Yang XP, Albers M, Koegl M, Jetten AM: Ubiquitin-interaction motifs of RAP80 are critical in its regulation of estrogen receptor alpha. Nucleic Acids Res. 2007;35(5):1673-86. Epub 2007 Feb 20. [PubMed Link Image]
  34. Zou JX, Revenko AS, Li LB, Gemo AT, Chen HW: ANCCA, an estrogen-regulated AAA+ ATPase coactivator for ERalpha, is required for coregulator occupancy and chromatin modification. Proc Natl Acad Sci U S A. 2007 Nov 13;104(46):18067-72. Epub 2007 Nov 12. [PubMed Link Image]
  35. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  36. Li T, Li W, Lu J, Liu H, Li Y, Zhao Y: SH2D4A regulates cell proliferation via the ERalpha/PLC-gamma/PKC pathway. BMB Rep. 2009 Aug 31;42(8):516-22. [PubMed Link Image]
  37. Johnsen SA, Gungor C, Prenzel T, Riethdorf S, Riethdorf L, Taniguchi-Ishigaki N, Rau T, Tursun B, Furlow JD, Sauter G, Scheffner M, Pantel K, Gannon F, Bach I: Regulation of estrogen-dependent transcription by the LIM cofactors CLIM and RLIM in breast cancer. Cancer Res. 2009 Jan 1;69(1):128-36. [PubMed Link Image]
  38. Stanisic V, Malovannaya A, Qin J, Lonard DM, O'Malley BW: OTU Domain-containing ubiquitin aldehyde-binding protein 1 (OTUB1) deubiquitinates estrogen receptor (ER) alpha and affects ERalpha transcriptional activity. J Biol Chem. 2009 Jun 12;284(24):16135-45. Epub 2009 Apr 21. [PubMed Link Image]
  39. Zusev M, Benayahu D: The regulation of MS-KIF18A expression and cross talk with estrogen receptor. PLoS One. 2009 Jul 28;4(7):e6407. [PubMed Link Image]
  40. Schwabe JW, Neuhaus D, Rhodes D: Solution structure of the DNA-binding domain of the oestrogen receptor. Nature. 1990 Nov 29;348(6300):458-61. [PubMed Link Image]
  41. Schwabe JW, Chapman L, Finch JT, Rhodes D: The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements. Cell. 1993 Nov 5;75(3):567-78. [PubMed Link Image]
  42. Brzozowski AM, Pike AC, Dauter Z, Hubbard RE, Bonn T, Engstrom O, Ohman L, Greene GL, Gustafsson JA, Carlquist M: Molecular basis of agonism and antagonism in the oestrogen receptor. Nature. 1997 Oct 16;389(6652):753-8. [PubMed Link Image]
  43. Tanenbaum DM, Wang Y, Williams SP, Sigler PB: Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains. Proc Natl Acad Sci U S A. 1998 May 26;95(11):5998-6003. [PubMed Link Image]
  44. Shiau AK, Barstad D, Loria PM, Cheng L, Kushner PJ, Agard DA, Greene GL: The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell. 1998 Dec 23;95(7):927-37. [PubMed Link Image]
  45. Maalouf GJ, Xu W, Smith TF, Mohr SC: Homology model for the ligand-binding domain of the human estrogen receptor. J Biomol Struct Dyn. 1998 Apr;15(5):841-51. [PubMed Link Image]
  46. Tora L, Mullick A, Metzger D, Ponglikitmongkol M, Park I, Chambon P: The cloned human oestrogen receptor contains a mutation which alters its hormone binding properties. EMBO J. 1989 Jul;8(7):1981-6. [PubMed Link Image]
  47. McInerney EM, Ince BA, Shapiro DJ, Katzenellenbogen BS: A transcriptionally active estrogen receptor mutant is a novel type of dominant negative inhibitor of estrogen action. Mol Endocrinol. 1996 Dec;10(12):1519-26. [PubMed Link Image]
  48. Anderson TI, Wooster R, Laake K, Collins N, Warren W, Skrede M, Elles R, Tveit KM, Johnston SR, Dowsett M, Olsen AO, Moller P, Stratton MR, Borresen-Dale AL: Screening for ESR mutations in breast and ovarian cancer patients. Hum Mutat. 1997;9(6):531-6. [PubMed Link Image]
  49. Becherini L, Gennari L, Masi L, Mansani R, Massart F, Morelli A, Falchetti A, Gonnelli S, Fiorelli G, Tanini A, Brandi ML: Evidence of a linkage disequilibrium between polymorphisms in the human estrogen receptor alpha gene and their relationship to bone mass variation in postmenopausal Italian women. Hum Mol Genet. 2000 Aug 12;9(13):2043-50. [PubMed Link Image]
  50. Chanock SJ, Burdett L, Yeager M, Llaca V, Langerod A, Presswalla S, Kaaresen R, Strausberg RL, Gerhard DS, Kristensen V, Perou CM, Borresen-Dale AL: Somatic sequence alterations in twenty-one genes selected by expression profile analysis of breast carcinomas. Breast Cancer Res. 2007;9(1):R5. [PubMed Link Image]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 8369
Enzyme 48 Name 17-beta-hydroxysteroid dehydrogenase type 6
Enzyme 48 Synonyms
  1. 17-beta-HSD 6
  2. 17-beta-HSD6
  3. 3-alpha->beta-hydroxysteroid epimerase
  4. 3-alpha->beta-HSE
  5. Oxidative 3-alpha hydroxysteroid dehydrogenase
Enzyme 48 Gene Name HSD17B6
Enzyme 48 Protein Sequence >17-beta-hydroxysteroid dehydrogenase type 6
MWLYLAAFVGLYYLLHWYRERQVVSHLQDKYVFITGCDSGFGNLLARQLDARGLRVLAAC
LTEKGAEQLRGQTSDRLETVTLDVTKMESIAAATQWVKEHVGDRGLWGLVNNAGILTPIT
LCEWLNTEDSMNMLKVNLIGVIQVTLSMLPLVRRARGRIVNVSSILGRVAFFVGGYCVSK
YGVEAFSDILRREIQHFGVKISIVEPGYFRTGMTNMTQSLERMKQSWKEAPKHIKETYGQ
QYFDALYNIMKEGLLNCSTNLNLVTDCMEHALTSVHPRTRYSAGWDAKFFFIPLSYLPTS
LADYILTRSWPKPAQAV
Enzyme 48 Number of Residues 317
Enzyme 48 Molecular Weight 35965.4
Enzyme 48 Theoretical pI 8.91
Enzyme 48 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 48 General Function Involved in oxidoreductase activity
Enzyme 48 Specific Function NAD-dependent oxidoreductase with broad substrate specificity that shows both oxidative and reductive activity (in vitro). Has 17-beta-hydroxysteroid dehydrogenase activity towards various steroids (in vitro). Converts 5-alpha-androstan-3- alpha,17-beta-diol to androsterone and estradiol to estrone (in vitro). Has 3-alpha-hydroxysteroid dehydrogenase activity towards androsterone (in vitro). Has retinol dehydrogenase activity towards all-trans-retinol (in vitro). Can convert androsterone to epi-androsterone. Androsterone is first oxidized to 5-alpha- androstane-3,17-dione and then reduced to epi-andosterone. Can act on both C-19 and C-21 3-alpha-hydroxysteroids
Enzyme 48 Pathways Not Available
Enzyme 48 Reactions
  • retinol + NAD+ = retinal + NADH + H+ [RN:R02124]
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • 1-17
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 2338748 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID O14756 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name H17B6_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence >954 bp
ATGTGGCTCTACCTGGCAGCCTTCGTGGGCCTGTACTACCTTCTGCACTGGTACCGGGAG
AGGCAGGTGGTGAGCCACCTCCAAGACAAGTATGTCTTTATCACGGGCTGTGACTCGGGC
TTTGGGAACCTACTGGCCAGACAGCTGGATGCACGAGGCTTGAGAGTGCTGGCTGCGTGT
CTGACGGAGAAGGGGGCCGAGCAGCTGAGGGGCCAGACGTCTGACAGGCTGGAGACGGTG
ACCCTGGATGTTACCAAGATGGAGAGCATCGCTGCAGCTACTCAGTGGGTGAAGGAGCAT
GTGGGGGACAGAGGACTCTGGGGACTGGTGAACAATGCAGGCATTCTTACACCAATTACC
TTATGTGAGTGGCTGAACACTGAGGACTCTATGAATATGCTCAAAGTGAACCTCATTGGT
GTGATCCAGGTGACCTTGAGCATGCTTCCTTTGGTGAGGAGAGCACGGGGAAGAATTGTC
AATGTCTCCAGCATTCTGGGAAGAGTTGCTTTCTTTGTAGGAGGCTACTGTGTCTCCAAG
TATGGAGTGGAAGCCTTTTCAGATATTCTGAGGCGTGAGATTCAACATTTTGGGGTGAAA
ATCAGCATAGTTGAACCTGGCTACTTCAGAACGGGAATGACAAACATGACACAGTCCTTA
GAGCGAATGAAGCAAAGTTGGAAAGAAGCCCCCAAGCATATTAAGGAGACCTATGGACAG
CAGTATTTTGATGCCCTTTACAATATCATGAAGGAAGGGCTGTTGAATTGTAGCACAAAC
CTGAACCTGGTCACTGACTGCATGGAACATGCTCTGACATCGGTGCATCCGCGAACTCGA
TATTCAGCTGGCTGGGATGCTAAATTTTTCTTCATCCCTCTATCTTATTTACCTACATCA
CTGGCAGACTACATTTTGACTAGATCTTGGCCCAAACCAGCCCAGGCAGTCTAA
Enzyme 48 GenBank Gene ID AF016509 Link Image
Enzyme 48 GeneCard ID HSD17B6 Link Image
Enzyme 48 GenAtlas ID HSD17B6 Link Image
Enzyme 48 HGNC ID HGNC:23316 Link Image
Enzyme 48 Chromosome Location 1
Enzyme 48 Locus 12q13
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References
  1. Biswas MG, Russell DW: Expression cloning and characterization of oxidative 17beta- and 3alpha-hydroxysteroid dehydrogenases from rat and human prostate. J Biol Chem. 1997 Jun 20;272(25):15959-66. [PubMed Link Image]
  2. Huang XF, Luu-The V: Molecular characterization of a first human 3(alpha-->beta)-hydroxysteroid epimerase. J Biol Chem. 2000 Sep 22;275(38):29452-7. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Chetyrkin SV, Hu J, Gough WH, Dumaual N, Kedishvili NY: Further characterization of human microsomal 3alpha-hydroxysteroid dehydrogenase. Arch Biochem Biophys. 2001 Feb 1;386(1):1-10. [PubMed Link Image]
  5. Huang XF, Luu-The V: Gene structure, chromosomal localization and analysis of 3-ketosteroid reductase activity of the human 3(alpha-->beta)-hydroxysteroid epimerase. Biochim Biophys Acta. 2001 Aug 30;1520(2):124-30. [PubMed Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 12970
Enzyme 49 Name UDP-glucuronosyltransferase 2A3
Enzyme 49 Synonyms
  1. UDPGT 2A3
Enzyme 49 Gene Name UGT2A3
Enzyme 49 Protein Sequence >UDP-glucuronosyltransferase 2A3
MRSDKSALVFLLLQLFCVGCGFCGKVLVWPCDMSHWLNVKVILEELIVRGHEVTVLTHSK
PSLIDYRKPSALKFEVVHMPQDRTEENEIFVDLALNVLPGLSTWQSVIKLNDFFVEIRGT
LKMMCESFIYNQTLMKKLQETNYDVMLIDPVIPCGDLMAELLAVPFVLTLRISVGGNMER
SCGKLPAPLSYVPVPMTGLTDRMTFLERVKNSMLSVLFHFWIQDYDYHFWEEFYSKALGR
PTTLCETVGKAEIWLIRTYWDFEFPQPYQPNFEFVGGLHCKPAKALPKEMENFVQSSGED
GIVVFSLGSLFQNVTEEKANIIASALAQIPQKVLWRYKGKKPSTLGANTRLYDWIPQNDL
LGHPKTKAFITHGGMNGIYEAIYHGVPMVGVPIFGDQLDNIAHMKAKGAAVEINFKTMTS
EDLLRALRTVITDSSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRSAAHD
LTWFQHYSIDVIGFLLACVATAIFLFTKCFLFSCQKFNKTRKIEKRE
Enzyme 49 Number of Residues 527
Enzyme 49 Molecular Weight 60253.9
Enzyme 49 Theoretical pI 8.04
Enzyme 49 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 49 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 49 Specific Function UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds
Enzyme 49 Pathways
Enzyme 49 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • 1-23
Enzyme 49 Transmembrane Regions
  • 492-512
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 193211427 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID Q6UWM9 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name UD2A3_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >1584 bp
ATGAGGTCTGACAAGTCAGCTTTGGTATTTCTGCTCCTGCAGCTCTTCTGTGTTGGCTGT
GGATTCTGTGGGAAAGTCCTGGTGTGGCCCTGTGACATGAGCCATTGGCTTAATGTCAAG
GTCATTCTAGAAGAGCTCATAGTGAGAGGCCATGAGGTAACAGTATTGACTCACTCAAAG
CCTTCGTTAATTGACTACAGGAAGCCTTCTGCATTGAAATTTGAGGTGGTCCATATGCCA
CAGGACAGAACAGAAGAAAATGAAATATTTGTTGACCTAGCTCTGAATGTCTTGCCAGGC
TTATCAACCTGGCAATCAGTTATAAAATTAAATGATTTTTTTGTTGAAATAAGAGGAACT
TTAAAAATGATGTGTGAGAGCTTTATCTACAATCAGACGCTTATGAAGAAGCTACAGGAA
ACCAACTACGATGTAATGCTTATAGACCCTGTGATTCCCTGTGGAGACCTGATGGCTGAG
TTGCTTGCAGTCCCTTTTGTGCTCACACTTAGAATTTCTGTAGGAGGCAATATGGAGCGA
AGCTGTGGGAAACTTCCAGCTCCACTTTCCTATGTACCTGTGCCTATGACAGGACTAACA
GACAGAATGACCTTTCTGGAAAGAGTAAAAAATTCAATGCTTTCAGTTTTGTTCCACTTC
TGGATTCAGGATTACGACTATCATTTTTGGGAAGAGTTTTATAGTAAGGCATTAGGAAGG
CCCACTACATTATGTGAGACTGTGGGAAAAGCTGAGATATGGCTAATACGAACATATTGG
GATTTTGAATTTCCTCAACCATACCAACCTAACTTTGAGTTTGTTGGAGGATTGCACTGT
AAACCTGCCAAAGCTTTGCCTAAGGAAATGGAAAATTTTGTCCAGAGTTCAGGGGAAGAT
GGTATTGTGGTGTTTTCTCTGGGGTCACTGTTTCAAAATGTTACAGAAGAAAAGGCTAAT
ATCATTGCTTCAGCCCTTGCCCAGATCCCACAGAAGGTGTTATGGAGGTACAAAGGAAAA
AAACCATCCACATTAGGAGCCAATACTCGGCTGTATGATTGGATACCCCAGAATGATCTT
CTTGGTCATCCCAAAACCAAAGCTTTTATCACTCATGGTGGAATGAATGGGATCTATGAA
GCTATTTACCATGGGGTCCCTATGGTGGGAGTTCCCATATTTGGTGATCAGCTTGATAAC
ATAGCTCACATGAAGGCCAAAGGAGCAGCTGTAGAAATAAACTTCAAAACTATGACAAGC
GAAGATTTACTGAGGGCTTTGAGAACAGTCATTACCGATTCCTCTTATAAAGAGAATGCT
ATGAGATTATCAAGAATTCACCATGATCAACCTGTAAAGCCCCTAGATCGAGCAGTCTTC
TGGATCGAGTTTGTCATGCGCCACAAAGGAGCCAAGCACCTGCGATCAGCTGCCCATGAC
CTCACCTGGTTCCAGCACTACTCTATAGATGTGATTGGGTTCCTGCTGGCCTGTGTGGCA
ACTGCTATATTCTTGTTCACAAAATGTTTTTTATTTTCCTGTCAAAAATTTAATAAAACT
AGAAAGATAGAAAAGAGGGAATAG
Enzyme 49 GenBank Gene ID NM_024743.3 Link Image
Enzyme 49 GeneCard ID UGT2A3 Link Image
Enzyme 49 GenAtlas ID UGT2A3 Link Image
Enzyme 49 HGNC ID HGNC:28528 Link Image
Enzyme 49 Chromosome Location 4
Enzyme 49 Locus 4q13.2
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 13116
Enzyme 50 Name Cytochrome P450, family 1, subfamily A, polypeptide 1
Enzyme 50 Synonyms
  1. SubName: Cytochrome P450, family 1, subfamily A, polypeptide 1, isoform CRA_a
  2. SubName: cDNA, FLJ94514, Homo sapiens cytochrome P450, family 1, subfamily A, polypeptide 1(CYP1A1), mRNA
Enzyme 50 Gene Name CYP1A1
Enzyme 50 Protein Sequence >Cytochrome P450, family 1, subfamily A, polypeptide 1
MLFPISMSATEFLLASVIFCLVFWVIRASRPQVPKGLKNPPGPWGWPLIGHMLTLGKNPH
LALSRMSQQYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYTFTLISNGQS
MSFSPDSGPVWAARRRLAQNGLKSFSIASDPASSTSCYLEEHVSKEAEVLISTLQELMAG
PGHFNPYRYVVVSVTNVICAICFGRRYDHNHQELLSLVNLNNNFGEVVGSGNPADFIPIL
RYLPNPSLNAFKDLNEKFYSFMQKMVKEHYKTFEKGHIRDITDSLIEHCQEKQLDENANV
QLSDEKIINIVLDLFGAGFDTVTTAISWSLMYLVMNPRVQRKIQEELDTVIGRSRRPRLS
DRSHLPYMEAFILETFRHSSFVPFTIPHSTTRDTSLKGFYIPKGRCVFVNQWQINHDQKL
WVNPSEFLPERFLTPDGAIDKVLSEKVIIFGMGKRKCIGETIARWEVFLFLAILLQRVEF
SVPLGVKVDMTPIYGLTMKHACCEHFQMQLRS
Enzyme 50 Number of Residues 512
Enzyme 50 Molecular Weight 58164.8
Enzyme 50 Theoretical pI 8.47
Enzyme 50 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 50 General Function Involved in monooxygenase activity
Enzyme 50 Specific Function Not Available
Enzyme 50 Pathways Not Available
Enzyme 50 Reactions Not Available
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • None
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 189067013 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID A0N0X8 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name A0N0X8_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 Gene Sequence >1539 bp
ATGCTTTTCCCAATCTCCATGTCGGCCACGGAGTTTCTTCTGGCCTCTGTCATCTTCTGT
CTGGTATTCTGGGTAATCAGGGCCTCAAGACCTCAGGTCCCCAAAGGCCTGAAGAATCCA
CCAGGGCCATGGGGCTGGCCTCTGATTGGGCACATGCTGACCCTGGGAAAGAACCCGCAC
CTGGCACTGTCAAGGATGAGCCAGCAGTATGGGGACGTGCTGCAGATCCGAATTGGCTCC
ACACCCGTGGTGGTGCTGAGCGGCCTGGACACCATCCGGCAGGCCCTGGTGCGGCAGGGC
GATGATTTCAAGGGCCGGCCCGACCTCTACACCTTCACCCTCATCAGTAATGGTCAGAGC
ATGTCCTTCAGCCCAGACTCTGGACCAGTGTGGGCTGCCCGCCGGCGCCTGGCCCAGAAT
GGCCTGAAAAGTTTCTCCATTGCCTCTGACCCAGCCTCCTCAACCTCCTGCTACCTGGAA
GAGCATGTGAGCAAGGAGGCTGAGGTCCTGATAAGCACGTTGCAGGAGCTGATGGCAGGG
CCTGGGCACTTTAACCCCTACAGGTATGTGGTGGTATCAGTGACCAATGTCATCTGTGCC
ATTTGCTTTGGCCGGCGCTATGACCACAACCACCAAGAACTGCTTAGCCTAGTCAACCTG
AATAATAATTTCGGGGAGGTGGTTGGCTCTGGAAACCCAGCTGACTTCATCCCTATTCTT
CGCTACCTACCCAACCCTTCCCTGAATGCCTTCAAGGACCTGAATGAGAAGTTCTACAGC
TTCATGCAGAAGATGGTCAAGGAGCACTACAAAACCTTTGAGAAGGGCCACATCCGGGAC
ATCACAGACAGCCTGATTGAGCACTGTCAGGAGAAGCAGCTGGATGAGAACGCCAATGTC
CAGCTGTCAGATGAGAAGATCATTAACATCGTCTTGGACCTCTTTGGAGCTGGGTTTGAC
ACAGTCACAACTGCTATCTCCTGGAGCCTCATGTATTTGGTGATGAACCCCAGGGTACAG
AGAAAGATCCAAGAGGAGCTAGACACAGTGATTGGCAGGTCACGGCGGCCCCGGCTCTCT
GACAGATCCCATCTGCCCTATATGGAGGCCTTCATCCTGGAGACCTTCCGACACTCTTCC
TTCGTCCCCTTCACCATCCCCCACAGCACAACAAGAGACACAAGTTTGAAAGGCTTTTAC
ATCCCCAAGGGGCGTTGTGTCTTTGTAAACCAGTGGCAGATCAACCATGACCAGAAGCTA
TGGGTCAACCCATCTGAGTTCCTACCTGAACGGTTTCTCACCCCTGATGGTGCTATCGAC
AAGGTGTTAAGTGAGAAGGTGATTATCTTTGGCATGGGCAAGCGGAAGTGTATCGGTGAG
ACCATTGCCCGCTGGGAGGTCTTTCTCTTCCTGGCTATCCTGCTGCAACGGGTGGAATTC
AGCGTGCCACTGGGCGTGAAGGTGGACATGACCCCCATCTATGGGCTAACCATGAAGCAT
GCCTGCTGTGAGCACTTCCAAATGCAGCTGCGCTCTTAG
Enzyme 50 GenBank Gene ID AK313880 Link Image
Enzyme 50 GeneCard ID CYP1A1 Link Image
Enzyme 50 GenAtlas ID CYP1A1 Link Image
Enzyme 50 HGNC ID HGNC:2595 Link Image
Enzyme 50 Chromosome Location 1
Enzyme 50 Locus 15q24.1
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 General References
  1. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 14588
Enzyme 51 Name Estradiol 17-beta-dehydrogenase 12
Enzyme 51 Synonyms
  1. 17-beta-hydroxysteroid dehydrogenase 12
  2. 17-beta-HSD 12
  3. 3-ketoacyl-CoA reductase
  4. KAR
Enzyme 51 Gene Name HSD17B12
Enzyme 51 Protein Sequence >Estradiol 17-beta-dehydrogenase 12
MESALPAAGFLYWVGAGTVAYLALRISYSLFTALRVWGVGNEAGVGPGLGEWAVVTGSTD
GIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASEDIYDKIKT
GLAGLEIGILVNNVGMSYEYPEYFLDVPDLDNVIKKMININILSVCKMTQLVLPGMVERS
KGAILNISSGSGMLPVPLLTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLA
KIRKPTLDKPSPETFVKSAIKTVGLQSRTNGYLIHALMGSIISNLPSWIYLKIVMNMNKS
TRAHYLKKTKKN
Enzyme 51 Number of Residues 312
Enzyme 51 Molecular Weight 34323.9
Enzyme 51 Theoretical pI 9.79
Enzyme 51 GO Classification
Function
  • binding
  • catalytic activity
  • oxidoreductase activity
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 51 General Function Involved in oxidoreductase activity
Enzyme 51 Specific Function Catalyzes the transformation of estrone (E1) into estradiol (E2), suggesting a central role in estrogen formation. Its strong expression in ovary and mammary gland suggest that it may constitute the major enzyme responsible for the conversion of E1 to E2 in women. Also has 3-ketoacyl-CoA reductase activity, reducing both long chain 3-ketoacyl-CoAs and long chain fatty acyl-CoAs, suggesting a role in long fatty acid elongation
Enzyme 51 Pathways
  • Androgen and Estrogen Metabolism (map00150 Link Image)
Enzyme 51 Reactions
  • estradiol-17beta + NAD(P)+ = estrone + NAD(P)H + H+ [RN:R02352 R02353]
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • 4-24 182-202 271-291
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 5531815 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID Q53GQ0 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name DHB12_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 Gene Sequence >939 bp
ATGGAGAGCGCTCTCCCCGCCGCCGGCTTCCTGTACTGGGTCGGCGCGGGCACCGTGGCC
TACCTAGCCCTGCGTATTTCGTACTCGCTCTTCACGGCCCTCCGGGTCTGGGGAGTGGGG
AATGAGGCGGGGGTCGGCCCGGGGCTCGGAGAGTGGGCAGTTGTCACAGGTAGTACTGAT
GGAATTGGAAAATCATATGCAGAAGAGTTAGCAAAGCATGGAATGAAGGTTGTCCTTATC
AGCAGATCAAAGGATAAACTTGACCAGGTTTCCAGTGAAATAAAAGAAAAATTCAAAGTG
GAGACAAGAACCATTGCTGTTGACTTTGCATCAGAAGATATTTATGATAAAATTAAAACA
GGCTTGGCTGGTCTTGAAATCGGCATCTTAGTGAACAACGTGGGAATGTCGTATGAGTAT
CCTGAATACTTTTTGGATGTTCCTGACTTGGACAATGTGATCAAGAAAATGATAAATATT
AATATTCTTTCTGTTTGTAAGATGACACAATTGGTACTGCCTGGCATGGTGGAAAGATCC
AAAGGGGCTATTCTGAACATTTCATCTGGCAGTGGCATGCTCCCTGTCCCACTCTTGACC
ATCTATTCTGCAACCAAGACTTTTGTAGATTTCTTCTCTCAGTGCCTCCATGAGGAGTAT
AGGAGCAAGGGCGTCTTTGTGCAGAGTGTCCTGCCATACTTCGTAGCTACAAAACTGGCT
AAAATCCGGAAGCCAACTTTGGATAAGCCCTCTCCGGAGACGTTTGTGAAGTCTGCAATT
AAAACAGTCGGCCTGCAATCCCGAACCAATGGATACCTGATCCATGCTCTTATGGGCTCG
ATAATCTCAAACCTGCCTTCTTGGATTTATTTGAAAATAGTCATGAATATGAACAAGTCT
ACACGGGCTCACTATCTGAAGAAAACCAAGAAGAACTAA
Enzyme 51 GenBank Gene ID AF078850 Link Image
Enzyme 51 GeneCard ID HSD17B12 Link Image
Enzyme 51 GenAtlas ID HSD17B12 Link Image
Enzyme 51 HGNC ID HGNC:18646 Link Image
Enzyme 51 Chromosome Location 1
Enzyme 51 Locus 11p11.2
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Moon YA, Horton JD: Identification of two mammalian reductases involved in the two-carbon fatty acyl elongation cascade. J Biol Chem. 2003 Feb 28;278(9):7335-43. Epub 2002 Dec 13. [PubMed Link Image]
  4. Gnatenko DV, Cupit LD, Huang EC, Dhundale A, Perrotta PL, Bahou WF: Platelets express steroidogenic 17beta-hydroxysteroid dehydrogenases. Distinct profiles predict the essential thrombocythemic phenotype. Thromb Haemost. 2005 Aug;94(2):412-21. [PubMed Link Image]
  5. Luu-The V, Tremblay P, Labrie F: Characterization of type 12 17beta-hydroxysteroid dehydrogenase, an isoform of type 3 17beta-hydroxysteroid dehydrogenase responsible for estradiol formation in women. Mol Endocrinol. 2006 Feb;20(2):437-43. Epub 2005 Sep 15. [PubMed Link Image]
Enzyme 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 14810
Enzyme 52 Name Solute carrier family 22 member 7
Enzyme 52 Synonyms
  1. Novel liver transporter
  2. Organic anion transporter 2
  3. hOAT2
Enzyme 52 Gene Name SLC22A7
Enzyme 52 Protein Sequence >Solute carrier family 22 member 7
MGFEELLEQVGGFGPFQLRNVALLALPRVLLPLHFLLPIFLAAVPAHRCALPGAPANFSH
QDVWLEAHLPREPDGTLSSCLRFAYPQALPNTTLGEERQSRGELEDEPATVPCSQGWEYD
HSEFSSTIATESQWDLVCEQKGLNRAASTFFFAGVLVGAVAFGYLSDRFGRRRLLLVAYV
STLVLGLASAASVSYVMFAITRTLTGSALAGFTIIVMPLELEWLDVEHRTVAGVLSSTFW
TGGVMLLALVGYLIRDWRWLLLAVTLPCAPGILSLWWVPESARWLLTQGHVKEAHRYLLH
CARLNGRPVCEDSFSQEAVSKVAAGERVVRRPSYLDLFRTPRLRHISLCCVVVWFGVNFS
YYGLSLDVSGLGLNVYQTQLLFGAVELPSKLLVYLSVRYAGRRLTQAGTLLGTALAFGTR
LLVSSDMKSWSTVLAVMGKAFSEAAFTTAYLFTSELYPTVLRQTGMGLTALVGRLGGSLA
PLAALLDGVWLSLPKLTYGGIALLAAGTALLLPETRQAQLPETIQDVERKSAPTSLQEEE
MPMKQVQN
Enzyme 52 Number of Residues 548
Enzyme 52 Molecular Weight 60025.0
Enzyme 52 Theoretical pI 7.03
Enzyme 52 GO Classification
Function
  • ion transmembrane transporter activity
  • substrate-specific transmembrane transporter activity
  • transmembrane transporter activity
  • transporter activity
Process
  • establishment of localization
  • ion transport
  • transmembrane transport
  • transport
Component
  • cell part
  • integral to membrane
  • intrinsic to membrane
  • membrane part
Enzyme 52 General Function Involved in transmembrane transport
Enzyme 52 Specific Function Mediates sodium-independent multispecific organic anion transport. Transport of prostaglandin E2, prostaglandin F2, tetracycline, bumetanide, estrone sulfate, glutarate, dehydroepiandrosterone sulfate, allopurinol, 5-fluorouracil, paclitaxel, L-ascorbic acid, salicylate, ethotrexate, and alpha- ketoglutarate
Enzyme 52 Pathways Not Available
Enzyme 52 Reactions Not Available
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • 21-41 146-166 180-200 204-224 234-254 259-279 346-366 376-397 404-423 432-452 466-486 493-513
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein Not Available
Enzyme 52 UniProtKB/Swiss-Prot ID Q9Y694 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name S22A7_HUMAN Link Image
Enzyme 52 PDB ID Not Available
Enzyme 52 Cellular Location Not Available
Enzyme 52 Gene Sequence >1647 bp
ATGGGCTTTGAGGAGCTGCTGGAGCAGGTGGGCGGCTTTGGGCCCTTCCAACTGCGGAAT
GTGGCACTGCTGGCCCTGCCCCGAGTGCTGCTACCACTGCACTTCCTCCTGCCCATCTTC
CTGGCTGCCGTGCCTGCCCACCGATGTGCCCTGCCGGGTGCCCCTGCCAACTTCAGCCAT
CAGGATGTGTGGCTGGAGGCCCATCTTCCCCGGGAGCCTGATGGCACGCTCAGCTCCTGC
CTCCGCTTTGCCTATCCCCAGGCTCTCCCCAACACCACGTTGGGGGAAGAAAGGCAGAGC
CGTGGGGAGCTGGAGGATGAACCTGCCACAGTGCCCTGCTCTCAGGGCTGGGAGTACGAC
CACTCAGAATTCTCCTCTACCATTGCAACTGAGTCCCAGTGGGATCTGGTGTGTGAGCAG
AAAGGTCTGAACAGAGCTGCGTCCACTTTCTTCTTCGCCGGTGTGCTGGTGGGGGCTGTG
GCCTTTGGATATCTGTCCGACAGGTTTGGGCGGCGGCGTCTGCTGCTGGTAGCCTACGTG
AGTACCCTGGTGCTGGGCCTGGCATCTGCAGCCTCCGTCAGCTATGTAATGTTTGCCATC
ACCCGCACCCTTACTGGCTCAGCCCTGGCTGGTTTTACCATCATCGTGATGCCACTGGAG
CTGGAGTGGCTGGATGTGGAGCACCGCACCGTGGCTGGAGTCCTGAGCAGCACCTTCTGG
ACAGGGGGCGTGATGCTGCTGGCACTGGTTGGGTACCTGATACGGGACTGGCGATGGCTT
CTGCTAGCTGTCACCCTGCCTTGTGCCCCAGGCATCCTCAGCCTCTGGTGGGTGCCTGAG
TCTGCACGCTGGCTTCTGACCCAAGGCCATGTGAAAGAGGCCCACAGGTACTTGCTCCAC
TGTGCCAGGCTCAATGGGCGGCCAGTGTGTGAGGACAGCTTCAGCCAGGAGGCTGTGAGC
AAAGTGGCCGCCGGGGAACGGGTGGTCCGAAGACCTTCATACCTAGACCTGTTCCGCACA
CCACGGCTCCGACACATCTCACTGTGCTGCGTGGTGGTGTGGTTCGGAGTGAACTTCTCC
TATTACGGCCTGAGTCTGGATGTGTCGGGGCTGGGGCTGAACGTGTACCAGACACAGCTG
TTGTTCGGGGCTGTGGAACTGCCCTCCAAGCTGCTGGTCTACTTGTCGGTGCGCTACGCA
GGACGCCGCCTCACGCAAGCCGGGACACTGCTGGGCACGGCCCTGGCGTTCGGCACTAGA
CTGCTAGTGTCCTCCGATATGAAGTCCTGGAGCACTGTCCTGGCAGTGATGGGGAAAGCT
TTTTCTGAAGCTGCCTTCACCACTGCTTACCTGTTCACTTCAGAGTTGTACCCTACGGTG
CTCAGACAGACAGGGATGGGGCTGACTGCACTGGTGGGCCGGCTGGGGGGCTCTTTGGCC
CCACTGGCGGCCTTGCTAGATGGAGTGTGGCTGTCACTGCCCAAGCTTACTTATGGGGGG
ATCGCCCTGCTGGCTGCCGGCACCGCCCTCCTGCTGCCAGAGACGAGGCAGGCACAGCTG
CCAGAGACCATCCAGGACGTGGAGAGAAAGAGTGCCCCAACCAGTCTTCAGGAGGAAGAG
ATGCCCATGAAGCAGGTCCAGAACTAA
Enzyme 52 GenBank Gene ID AF097518 Link Image
Enzyme 52 GeneCard ID SLC22A7 Link Image
Enzyme 52 GenAtlas ID SLC22A7 Link Image
Enzyme 52 HGNC ID HGNC:10971 Link Image
Enzyme 52 Chromosome Location 6
Enzyme 52 Locus 6p21.1
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Sun W, Wu RR, van Poelje PD, Erion MD: Isolation of a family of organic anion transporters from human liver and kidney. Biochem Biophys Res Commun. 2001 May 4;283(2):417-22. [PubMed Link Image]
  5. Enomoto A, Takeda M, Shimoda M, Narikawa S, Kobayashi Y, Kobayashi Y, Yamamoto T, Sekine T, Cha SH, Niwa T, Endou H: Interaction of human organic anion transporters 2 and 4 with organic anion transport inhibitors. J Pharmacol Exp Ther. 2002 Jun;301(3):797-802. [PubMed Link Image]
  6. Kimura H, Takeda M, Narikawa S, Enomoto A, Ichida K, Endou H: Human organic anion transporters and human organic cation transporters mediate renal transport of prostaglandins. J Pharmacol Exp Ther. 2002 Apr;301(1):293-8. [PubMed Link Image]
  7. Babu E, Takeda M, Narikawa S, Kobayashi Y, Yamamoto T, Cha SH, Sekine T, Sakthisekaran D, Endou H: Human organic anion transporters mediate the transport of tetracycline. Jpn J Pharmacol. 2002 Jan;88(1):69-76. [PubMed Link Image]
  8. Kobayashi Y, Ohshiro N, Sakai R, Ohbayashi M, Kohyama N, Yamamoto T: Transport mechanism and substrate specificity of human organic anion transporter 2 (hOat2 [SLC22A7]). J Pharm Pharmacol. 2005 May;57(5):573-8. [PubMed Link Image]
  9. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
Enzyme 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 15056
Enzyme 53 Name HCG2039726, isoform CRA_f
Enzyme 53 Synonyms
  1. SubName: UDP glycosyltransferase 1 family polypeptide A10
Enzyme 53 Gene Name UGT1A10
Enzyme 53 Protein Sequence >HCG2039726, isoform CRA_f
MARAGWTSPVPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLERSLNCTVKTYSTSYTLEDQNREFMVFAHAQWKAQAQSIFSLLMSSSSGFLDLF
FSHCRSLFNDRKLVEYLKESSFDAVFLDPFDTCGLIVAKYFSLPSVVFTRGIFCHHLEEG
AQCPAPLSYVPNDLLGFSDAMTFKERVWNHIVHLEDHLFCQYLFRNALEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 53 Number of Residues 530
Enzyme 53 Molecular Weight 59809.1
Enzyme 53 Theoretical pI 7.31
Enzyme 53 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 53 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 53 Specific Function Not Available
Enzyme 53 Pathways Not Available
Enzyme 53 Reactions Not Available
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • None
Enzyme 53 Transmembrane Regions
  • None
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein 40849852 Link Image
Enzyme 53 UniProtKB/Swiss-Prot ID Q5DT02 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name Q5DT02_HUMAN Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence >1593 bp
ATGGCTCGCGCAGGGTGGACCAGCCCCGTTCCTTTATGTGTGTGTCTACTGCTGACCTGT
GGCTTTGCCGAGGCAGGGAAGCTGCTGGTAGTGCCCATGGATGGGAGTCACTGGTTCACC
ATGCAGTCGGTGGTGGAGAAACTTATCCTCAGGGGGCATGAGGTGGTTGTAGTCATGCCA
GAGGTGAGTTGGCAACTGGAAAGATCACTGAATTGCACAGTGAAGACTTACTCAACCTCG
TACACTCTGGAAGATCAGAACCGGGAATTCATGGTTTTCGCCCATGCTCAATGGAAAGCA
CAGGCACAAAGTATATTTTCTCTATTAATGAGTTCATCCAGTGGTTTTCTTGACTTATTT
TTTTCGCATTGCAGGAGTTTGTTTAATGACCGAAAATTAGTAGAATACTTAAAGGAGAGT
TCTTTTGATGCAGTGTTTCTGGATCCTTTTGATACCTGTGGCTTAATTGTTGCTAAATAT
TTCTCCCTCCCCTCTGTGGTCTTCACCAGGGGAATATTTTGCCACCATCTTGAAGAAGGT
GCACAGTGCCCTGCTCCTCTTTCCTATGTCCCCAATGATCTCTTAGGGTTCTCAGATGCC
ATGACTTTCAAGGAGAGAGTATGGAACCACATCGTGCACTTGGAGGACCATTTATTTTGC
CAGTATCTTTTTAGAAATGCCCTAGAAATAGCCTCTGAAATTCTCCAAACCCCTGTCACG
GCATATGATCTCTACAGTCACACATCAATTTGGTTGTTGCGAACGGACTTTGTTTTGGAC
TATCCCAAACCCGTGATGCCCAACATGATCTTCATTGGTGGTATCAACTGTCATCAGGGA
AAGCCATTGCCTATGGAATTTGAAGCCTACATTAATGCTTCTGGAGAACATGGAATTGTG
GTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCTATGGCAATTGCT
GATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGAACCCGACCATCG
AATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGATCTGCTTGGTCAC
CCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTATGAAAGCATATGC
AATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGACAATGCAAAGCGC
ATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACTTCTGAAGATTTA
GAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAACATCATGCGCCTC
TCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTGTTCTGGGTGGAG
TTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCACGACCTCACCTGG
TACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTGCTGACAGTGGCC
TTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGGAAAAAAGGGCGA
GTTAAGAAAGCCCACAAATCCAAGACCCATTGA
Enzyme 53 GenBank Gene ID AY435137 Link Image
Enzyme 53 GeneCard ID UGT1A10 Link Image
Enzyme 53 GenAtlas ID UGT1A10 Link Image
Enzyme 53 HGNC ID HGNC:12531 Link Image
Enzyme 53 Chromosome Location 2
Enzyme 53 Locus 2q37
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 General References
  1. Zhang T, Haws P, Wu Q: Multiple variable first exons: a mechanism for cell- and tissue-specific gene regulation. Genome Res. 2004 Jan;14(1):79-89. Epub 2003 Dec 12. [PubMed Link Image]
Enzyme 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 15057
Enzyme 54 Name HCG2039726, isoform CRA_e
Enzyme 54 Synonyms
  1. SubName: UDP glycosyltransferase 1 family polypeptide A8
Enzyme 54 Gene Name UGT1A8
Enzyme 54 Protein Sequence >HCG2039726, isoform CRA_e
MARTGWTSPIPLCVSLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLGKSLNCTVKTYSTSYTLEDLDREFMDFADAQWKAQVRSLFSLFLSSSNGFFNLF
FSHCRSLFNDRKLVEYLKESSFDAVFLDPFDACGLIVAKYFSLPSVVFARGIACHYLEEG
AQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLFCQYFSKNALEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 54 Number of Residues 530
Enzyme 54 Molecular Weight 59741.0
Enzyme 54 Theoretical pI 7.73
Enzyme 54 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 54 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 54 Specific Function Not Available
Enzyme 54 Pathways Not Available
Enzyme 54 Reactions Not Available
Enzyme 54 Pfam Domain Function
Enzyme 54 Signals
  • None
Enzyme 54 Transmembrane Regions
  • None
Enzyme 54 Essentiality Not Available
Enzyme 54 GenBank ID Protein 40849864 Link Image
Enzyme 54 UniProtKB/Swiss-Prot ID Q5DSZ6 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name Q5DSZ6_HUMAN Link Image
Enzyme 54 PDB ID Not Available
Enzyme 54 Cellular Location Not Available
Enzyme 54 Gene Sequence >1593 bp
ATGGCTCGCACAGGGTGGACCAGCCCCATTCCCCTATGTGTTTCTCTGCTGCTGACCTGT
GGCTTTGCTGAGGCAGGGAAGCTGCTGGTAGTGCCCATGGATGGGAGTCACTGGTTCACC
ATGCAGTCGGTGGTGGAGAAACTTATCCTCAGGGGGCATGAGGTGGTTGTAGTCATGCCA
GAGGTGAGTTGGCAACTGGGAAAATCACTGAATTGCACAGTGAAGACTTACTCAACCTCA
TACACTCTGGAGGATCTGGACCGGGAATTCATGGATTTCGCCGATGCTCAATGGAAAGCA
CAAGTACGAAGTTTGTTTTCTCTATTTCTGAGTTCATCCAATGGTTTTTTTAACTTATTT
TTTTCGCATTGCAGGAGTTTGTTTAATGACCGAAAATTAGTAGAATACTTAAAGGAGAGT
TCTTTTGATGCGGTGTTTCTTGATCCTTTTGATGCCTGTGGCTTAATTGTTGCCAAATAT
TTCTCCCTCCCCTCTGTGGTCTTCGCCAGGGGAATAGCTTGCCACTATCTTGAAGAAGGT
GCACAGTGCCCTGCTCCTCTTTCCTATGTCCCCAGAATTCTCTTAGGGTTCTCAGATGCC
ATGACTTTCAAGGAGAGAGTACGGAACCACATCATGCACTTGGAGGAACATTTATTTTGC
CAGTATTTTTCCAAAAATGCCCTAGAAATAGCCTCTGAAATTCTCCAAACACCTGTCACA
GCATATGATCTCTACAGCCACACATCAATTTGGTTGTTGCGAACAGACTTTGTTTTGGAC
TATCCCAAACCCGTGATGCCCAATATGATCTTCATTGGTGGTATCAACTGCCATCAGGGA
AAGCCATTGCCTATGGAATTTGAAGCCTACATTAATGCTTCTGGAGAACATGGAATTGTG
GTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCTATGGCAATTGCT
GATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGAACCCGACCATCG
AATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGATCTGCTTGGTCAC
CCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTATGAAAGCATATGC
AATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGACAATGCAAAGCGC
ATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACTTCTGAAGATTTA
GAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAACATCATGCGCCTC
TCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTGTTCTGGGTGGAG
TTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCACGACCTCACCTGG
TACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTGCTGACAGTGGCC
TTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGGAAAAAAGGGCGA
GTTAAGAAAGCCCACAAATCCAAGACCCATTGA
Enzyme 54 GenBank Gene ID AY435143 Link Image
Enzyme 54 GeneCard ID UGT1A8 Link Image
Enzyme 54 GenAtlas ID UGT1A8 Link Image
Enzyme 54 HGNC ID HGNC:12540 Link Image
Enzyme 54 Chromosome Location 2
Enzyme 54 Locus 2q37
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 General References
  1. Zhang T, Haws P, Wu Q: Multiple variable first exons: a mechanism for cell- and tissue-specific gene regulation. Genome Res. 2004 Jan;14(1):79-89. Epub 2003 Dec 12. [PubMed Link Image]
Enzyme 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 15058
Enzyme 55 Name UDP glycosyltransferase 1 family polypeptide A7
Enzyme 55 Synonyms Not Available
Enzyme 55 Gene Name UGT1A7
Enzyme 55 Protein Sequence >UDP glycosyltransferase 1 family polypeptide A7
MARAGWTGLLPLYVCLLLTCGFAKAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLGRSLNCTVKTYSTSYTLEDQDREFMVFADARWTAPLRSAFSLLTSSSNGIFDLF
FSNCRSLFNDRKLVEYLKESCFDAVFLDPFDACGLIVAKYFSLPSVVFARGIFCHYLEEG
AQCPAPLSYVPRLLLGFSDAMTFKERVWNHIMHLEEHLFCPYFFKNVLEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLEYPKPVMPNMIFIGGINCHQGKPVPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 55 Number of Residues 530
Enzyme 55 Molecular Weight 59818.3
Enzyme 55 Theoretical pI 7.85
Enzyme 55 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 55 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 55 Specific Function Not Available
Enzyme 55 Pathways Not Available
Enzyme 55 Reactions Not Available
Enzyme 55 Pfam Domain Function
Enzyme 55 Signals
  • None
Enzyme 55 Transmembrane Regions
  • None
Enzyme 55 Essentiality Not Available
Enzyme 55 GenBank ID Protein 40849862 Link Image
Enzyme 55 UniProtKB/Swiss-Prot ID Q5DSZ7 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name Q5DSZ7_HUMAN Link Image
Enzyme 55 PDB ID Not Available
Enzyme 55 Cellular Location Not Available
Enzyme 55 Gene Sequence >1593 bp
ATGGCTCGTGCAGGGTGGACTGGCCTCCTTCCCCTATATGTGTGTCTACTGCTGACCTGT
GGCTTTGCCAAGGCAGGGAAGCTGCTGGTAGTGCCCATGGATGGGAGCCACTGGTTCACC
ATGCAGTCGGTGGTGGAGAAACTCATCCTCAGGGGGCATGAGGTGGTCGTAGTCATGCCA
GAGGTGAGTTGGCAACTGGGAAGATCACTGAATTGCACAGTGAAGACTTACTCAACCTCA
TACACTCTGGAGGATCAGGACCGGGAGTTCATGGTTTTTGCCGATGCTCGCTGGACGGCA
CCATTGCGAAGTGCATTTTCTCTATTAACAAGTTCATCCAATGGTATTTTTGACTTATTT
TTTTCAAATTGCAGGAGTTTGTTTAATGACCGAAAATTAGTAGAATACTTAAAGGAGAGT
TGTTTTGATGCAGTGTTTCTCGATCCTTTTGATGCCTGTGGCTTAATTGTTGCCAAATAT
TTCTCCCTCCCCTCTGTGGTCTTCGCCAGGGGAATATTTTGCCACTATCTTGAAGAAGGT
GCACAGTGCCCTGCTCCTCTTTCCTATGTCCCCAGACTTCTCTTAGGGTTCTCAGACGCC
ATGACTTTCAAGGAGAGAGTATGGAACCACATCATGCACTTGGAGGAACATTTATTTTGC
CCCTATTTTTTCAAAAATGTCTTAGAAATAGCCTCTGAAATTCTCCAAACCCCTGTCACG
GCATATGATCTCTACAGCCACACATCAATTTGGTTGTTGCGAACTGACTTTGTTTTGGAG
TATCCCAAACCCGTGATGCCCAATATGATCTTCATTGGTGGTATCAACTGTCATCAGGGA
AAGCCAGTGCCTATGGAATTTGAAGCCTACATTAATGCTTCTGGAGAACATGGAATTGTG
GTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCTATGGCAATTGCT
GATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGAACCCGACCATCG
AATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGATCTGCTTGGTCAC
CCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTATGAAAGCATATGC
AATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGACAATGCAAAGCGC
ATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACTTCTGAAGATTTA
GAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAACATCATGCGCCTC
TCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTGTTCTGGGTGGAG
TTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCACGACCTCACCTGG
TACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTGCTGACAGTGGCC
TTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGGAAAAAAGGGCGA
GTTAAGAAAGCCCACAAATCCAAGACCCATTGA
Enzyme 55 GenBank Gene ID AY435142 Link Image
Enzyme 55 GeneCard ID UGT1A7 Link Image
Enzyme 55 GenAtlas ID UGT1A7 Link Image
Enzyme 55 HGNC ID HGNC:12539 Link Image
Enzyme 55 Chromosome Location 2
Enzyme 55 Locus 2q37
Enzyme 55 SNPs SNPJam Report Link Image
Enzyme 55 General References
  1. Zhang T, Haws P, Wu Q: Multiple variable first exons: a mechanism for cell- and tissue-specific gene regulation. Genome Res. 2004 Jan;14(1):79-89. Epub 2003 Dec 12. [PubMed Link Image]
Enzyme 55 Metabolite References Not Available
Enzyme 56 [top]
Enzyme 56 ID 15059
Enzyme 56 Name cDNA FLJ76966, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B10 (UGT2B10), mRNA (UDP glucuronosyltransferase 2 family, polypeptide B10, isoform CRA_b)
Enzyme 56 Synonyms Not Available
Enzyme 56 Gene Name UGT2B10
Enzyme 56 Protein Sequence >cDNA FLJ76966, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B10 (UGT2B10), mRNA (UDP glucuronosyltransferase 2 family, polypeptide B10, isoform CRA_b)
MALKWTTVLLIQLSFYFSSGSCGKVLVWAAEYSLWMNMKTILKELVQRGHEVTVLASSAS
ILFDPNDSSTLKLEVYPTSLTKTEFENIIMQLVKRLSEIQKDTFWLPFSQEQEILWAIND
IIRNFCKDVVSNKKLMKKLQESRFDIVFADAYLPCGELLAELFNIPFVYSHSFSPGYSFE
RHSGGFIFPPSYVPVVMSKLSDQMTFMERVKNMLYVLYFDFWFQIFNMKKWDQFYSEVLG
RPTTLSETMRKADIWLMRNSWNFKFPHPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGE
NGVVVFSLGSMVSNMTEERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQND
LLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFFDQPDNIAHMKAKGAAVRVDFNTMS
STDLLNALKTVINDPSYKENIMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAH
NLTWFQYHSLDVIGFLLACVATVLFIITKCCLFCFWKFARKGKKGKRD
Enzyme 56 Number of Residues 528
Enzyme 56 Molecular Weight 60775
Enzyme 56 Theoretical pI 9.40
Enzyme 56 GO Classification Not Available
Enzyme 56 General Function Carbohydrate transport and metabolism
Enzyme 56 Specific Function Not Available
Enzyme 56 Pathways Not Available
Enzyme 56 Reactions Not Available
Enzyme 56 Pfam Domain Function Not Available
Enzyme 56 Signals
  • None
Enzyme 56 Transmembrane Regions
  • None
Enzyme 56 Essentiality Not Available
Enzyme 56 GenBank ID Protein 158258913 Link Image
Enzyme 56 UniProtKB/Swiss-Prot ID A8K9M3 Link Image
Enzyme 56 UniProtKB/Swiss-Prot Entry Name A8K9M3_HUMAN Link Image
Enzyme 56 PDB ID Not Available
Enzyme 56 Cellular Location Not Available
Enzyme 56 Gene Sequence >1587 bp
ATGGCTCTGAAATGGACTACAGTTCTGCTGATACAACTCAGTTTTTACTTTAGCTCTGGG
AGTTGTGGAAAGGTGCTGGTATGGGCCGCAGAATACAGCCTTTGGATGAATATGAAGACA
ATCCTGAAAGAACTTGTTCAGAGAGGTCATGAGGTGACTGTACTGGCATCTTCAGCTTCC
ATTCTTTTTGATCCCAACGACTCATCCACTCTTAAACTTGAAGTTTATCCTACATCTTTA
ACTAAAACTGAATTTGAGAATATCATCATGCAATTGGTTAAGAGATTGTCAGAAATTCAA
AAAGATACATTTTGGTTACCTTTTTCACAAGAACAAGAAATCCTGTGGGCAATTAATGAC
ATAATTAGAAACTTCTGTAAAGATGTAGTTTCAAATAAGAAACTTATGAAAAAACTACAA
GAGTCAAGATTTGACATCGTTTTTGCAGATGCTTATTTACCCTGTGGTGAGCTGCTGGCT
GAGCTATTTAACATACCCTTTGTGTACAGTCACAGCTTCAGTCCTGGCTACTCATTTGAA
AGGCACAGTGGAGGATTTATTTTCCCTCCTTCCTACGTACCTGTTGTTATGTCAAAATTA
AGTGATCAAATGACTTTCATGGAGAGGGTAAAAAATATGCTCTATGTGCTTTATTTTGAC
TTTTGGTTCCAAATATTTAATATGAAGAAGTGGGATCAGTTTTACAGTGAAGTTTTAGGA
AGACCCACTACATTATCTGAGACAATGAGGAAAGCTGACATATGGCTTATGCGAAACTCC
TGGAATTTTAAATTTCCTCATCCATTCTTACCAAATGTTGATTTTGTTGGAGGACTCCAC
TGCAAACCTGCCAAACCCCTACCTAAGGAAATGGAGGAGTTTGTACAGAGCTCTGGAGAA
AATGGTGTTGTGGTGTTTTCTCTGGGGTCAATGGTCAGTAACATGACAGAAGAAAGGGCC
AACGTAATTGCAACAGCCCTTGCCAAGATCCCACAAAAGGTTCTTTGGAGATTTGATGGG
AATAAACCAGATGCCTTAGGTCTCAATACTCGACTGTACAAGTGGATACCCCAGAATGAC
CTTCTAGGTCATCCAAAAACCAGAGCTTTTATAACTCATGGTGGAGCCAATGGCATCTAT
GAGGCAATCTACCATGGGATCCCTATGGTGGGCATTCCATTGTTTTTTGATCAACCTGAT
AATATTGCTCACATGAAGGCCAAGGGAGCAGCTGTTAGAGTGGACTTCAACACAATGTCG
AGTACAGACCTGCTGAATGCACTGAAGACAGTAATTAATGATCCTTCATATAAAGAGAAT
ATTATGAAATTATCAAGAATTCAACATGATCAACCAGTGAAGCCCCTGGATCGAGCAGTC
TTCTGGATTGAATTTGTCATGCGCCACAAAGGAGCCAAACATCTTCGAGTTGCAGCCCAC
AACCTCACCTGGTTCCAGTACCACTCTTTGGATGTGATTGGGTTCCTGCTGGCTTGTGTG
GCAACCGTGCTATTTATCATCACAAAGTGTTGTCTGTTTTGTTTCTGGAAGTTTGCTAGA
AAAGGAAAGAAGGGAAAAAGGGATTAG
Enzyme 56 GenBank Gene ID AK292738 Link Image
Enzyme 56 GeneCard ID A8K9M3 Link Image
Enzyme 56 GenAtlas ID Not Available
Enzyme 56 HGNC ID Not Available
Enzyme 56 Chromosome Location Not Available
Enzyme 56 Locus Not Available
Enzyme 56 SNPs SNPJam Report Link Image
Enzyme 56 General References Not Available
Enzyme 56 Metabolite References Not Available
Enzyme 57 [top]
Enzyme 57 ID 15174
Enzyme 57 Name Cytochrome P450, family 3, subfamily A, polypeptide 7
Enzyme 57 Synonyms Not Available
Enzyme 57 Gene Name CYP3A7
Enzyme 57 Protein Sequence >Cytochrome P450, family 3, subfamily A, polypeptide 7
MDLIPNLAVETWLLLAVSLILLYLYGTRTHGLFKKLGIPGPTPLPFLGNALSFRKGYWTF
DMECYKKYRKVWGIYDCQQPMLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKNAISI
AEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYS
MDVITSTSFGVSIDSLNNPQDPFVENTKKLLRFNPLDPFVLSIKVFPFLTPILEALNITV
FPRKVISFLTKSVKQIKEGRLKETQKHRVDFLQLMIDSQNSKDSETHKALSDLELMAQSI
IFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVV
NETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFS
KKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKLRFG
GLLLTEKPIVLKAESRDETVSGA
Enzyme 57 Number of Residues 503
Enzyme 57 Molecular Weight 57471
Enzyme 57 Theoretical pI 9.52
Enzyme 57 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • tetrapyrrole binding
  • transition metal ion binding
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 57 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 57 Specific Function Not Available
Enzyme 57 Pathways Not Available
Enzyme 57 Reactions Not Available
Enzyme 57 Pfam Domain Function
Enzyme 57 Signals
  • None
Enzyme 57 Transmembrane Regions
  • None
Enzyme 57 Essentiality Not Available
Enzyme 57 GenBank ID Protein Not Available
Enzyme 57 UniProtKB/Swiss-Prot ID A4D288 Link Image
Enzyme 57 UniProtKB/Swiss-Prot Entry Name A4D288_HUMAN Link Image
Enzyme 57 PDB ID Not Available
Enzyme 57 Cellular Location Not Available
Enzyme 57 Gene Sequence Not Available
Enzyme 57 GenBank Gene ID CH236956 Link Image
Enzyme 57 GeneCard ID A4D288 Link Image
Enzyme 57 GenAtlas ID Not Available
Enzyme 57 HGNC ID Not Available
Enzyme 57 Chromosome Location Not Available
Enzyme 57 Locus Not Available
Enzyme 57 SNPs SNPJam Report Link Image
Enzyme 57 General References
  1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
Enzyme 57 Metabolite References Not Available
Enzyme 58 [top]
Enzyme 58 ID 15175
Enzyme 58 Name Cytochrome P450 2D6
Enzyme 58 Synonyms
  1. SubName: Cytochrome P450, family 2, subfamily D, polypeptide 6
Enzyme 58 Gene Name CYP2D6
Enzyme 58 Protein Sequence >Cytochrome P450 2D6
MGLEALVPLAVIVAIFLLLVDLMHRRQRWAARYPPGPLPLPGLGNLLHVDFQNTPYCFDQ
LRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVF
LARYGPAWREQRRFSVSTLRNLGLGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDK
AVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKV
LRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLCIVVA
DLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVI
HEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHF
LDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVPTGQPRPSHHGV
FAFLVTPSPYELCAVPR
Enzyme 58 Number of Residues 497
Enzyme 58 Molecular Weight 55729.9
Enzyme 58 Theoretical pI 7.09
Enzyme 58 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 58 General Function Involved in monooxygenase activity
Enzyme 58 Specific Function Not Available
Enzyme 58 Pathways Not Available
Enzyme 58 Reactions Not Available
Enzyme 58 Pfam Domain Function
Enzyme 58 Signals
  • None
Enzyme 58 Transmembrane Regions
  • None
Enzyme 58 Essentiality Not Available
Enzyme 58 GenBank ID Protein 45768272 Link Image
Enzyme 58 UniProtKB/Swiss-Prot ID Q6NWU0 Link Image
Enzyme 58 UniProtKB/Swiss-Prot Entry Name Q6NWU0_HUMAN Link Image
Enzyme 58 PDB ID Not Available
Enzyme 58 Cellular Location Not Available
Enzyme 58 Gene Sequence >1494 bp
ATGGGGCTAGAAGCACTGGTGCCCCTGGCCGTGATAGTGGCCATCTTCCTGCTCCTGGTG
GACCTGATGCACCGGCGCCAACGCTGGGCTGCACGCTACCCACCAGGCCCCCTGCCACTG
CCCGGGCTGGGCAACCTGCTGCATGTGGACTTCCAGAACACACCATACTGCTTCGACCAG
TTGCGGCGCCGCTTCGGGGACGTGTTCAGCCTGCAGCTGGCCTGGACGCCGGTGGTCGTG
CTCAATGGGCTGGCGGCCGTGCGCGAGGCGCTGGTGACCCACGGCGAGGACACCGCCGAC
CGCCCGCCTGTGCCCATCACCCAGATCCTGGGTTTCGGGCCGCGTTCCCAAGGGGTGTTC
CTGGCGCGCTATGGGCCCGCGTGGCGCGAGCAGAGGCGCTTCTCCGTCTCCACCTTGCGC
AACTTGGGCCTGGGCAAGAAGTCGCTGGAGCAGTGGGTGACCGAGGAGGCCGCCTGCCTT
TGTGCCGCCTTCGCCAACCACTCCGGACGCCCCTTTCGCCCCAACGGTCTCTTGGACAAA
GCCGTGAGCAACGTGATCGCCTCCCTCACCTGCGGGCGCCGCTTCGAGTACGACGACCCT
CGCTTCCTCAGGCTGCTGGACCTAGCTCAGGAGGGACTGAAGGAGGAGTCGGGCTTTCTG
CGCGAGGTGCTGAATGCTGTCCCCGTCCTCCTGCATATCCCAGCGCTGGCTGGCAAGGTC
CTACGCTTCCAAAAGGCTTTCCTGACCCAGCTGGATGAGCTGCTAACTGAGCACAGGATG
ACCTGGGACCCAGCCCAGCCCCCCCGAGACCTGACTGAGGCCTTCCTGGCAGAGATGGAG
AAGGCCAAGGGGAACCCTGAGAGCAGCTTCAATGATGAGAACCTGTGCATAGTGGTGGCT
GACCTGTTCTCTGCCGGGATGGTGACCACCTCGACCACGCTGGCCTGGGGCCTCCTGCTC
ATGATCCTACATCCGGATGTGCAGCGCCGTGTCCAACAGGAGATCGACGACGTGATAGGG
CAGGTGCGGCGACCAGAGATGGGTGACCAGGCTCACATGCCCTACACCACTGCCGTGATT
CATGAGGTGCAGCGCTTTGGGGACATCGTCCCCCTGGGTGTGACCCATATGACATCCCGT
GACATCGAAGTACAGGGCTTCCGCATCCCTAAGGGAACGACACTCATCACCAACCTGTCA
TCGGTGCTGAAGGATGAGGCCGTCTGGGAGAAGCCCTTCCGCTTCCACCCCGAACACTTC
CTGGATGCCCAGGGCCACTTTGTGAAGCCGGAGGCCTTCCTGCCTTTCTCAGCAGGCCGC
CGTGCATGCCTCGGGGAGCCCCTGGCCCGCATGGAGCTCTTCCTCTTCTTCACCTCCCTG
CTGCAGCACTTCAGCTTCTCGGTGCCCACTGGACAGCCCCGGCCCAGCCACCATGGTGTC
TTTGCTTTCCTGGTGACCCCATCCCCCTATGAGCTTTGTGCTGTGCCCCGCTAG
Enzyme 58 GenBank Gene ID BC067432 Link Image
Enzyme 58 GeneCard ID CYP2D6 Link Image
Enzyme 58 GenAtlas ID CYP2D6 Link Image
Enzyme 58 HGNC ID HGNC:2625 Link Image
Enzyme 58 Chromosome Location 2
Enzyme 58 Locus 22q13.1
Enzyme 58 SNPs SNPJam Report Link Image
Enzyme 58 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 58 Metabolite References Not Available
Enzyme 59 [top]
Enzyme 59 ID 15176
Enzyme 59 Name Cytochrome P450, family 3, subfamily A, polypeptide 5 (Cytochrome P450, family 3, subfamily A, polypeptide 5, isoform CRA_a)
Enzyme 59 Synonyms Not Available
Enzyme 59 Gene Name CYP3A5
Enzyme 59 Protein Sequence >Cytochrome P450, family 3, subfamily A, polypeptide 5 (Cytochrome P450, family 3, subfamily A, polypeptide 5, isoform CRA_a)
MDLIPNLAVETWLLLAVSLVLLYLYGTRTHGLFKRLGIPGPTPLPLLGNVLSYRQGLWKF
DTECYKKYGKMWGTYEGQLPVLAITDPDVIRTVLVKECYSVFTNRRSLGPVGFMKSAISL
AEDEEWKRIRSLLSPTFTSGKLKEMFPIIAQYGDVLVRNLRREAEKGKPVTLKDIFGAYS
MDVITGTSFGVNIDSLNNPQDPFVESTKKFLKFGFLDPLFLSIILFPFLTPVFEALNVSL
FPKDTINFLSKSVNRMKKSRLNDKQKHRLDFLQLMIDSQNSKETESHKALSDLELAAQSI
IFIFAGYETTSSVLSFTLYELATHPDVQQKLQKEIDAVLPNKAPPTYDAVVQMEYLDMVV
NETLRLFPVAIRLERTCKKDVEINGVFIPKGSMVVIPTYALHHDPKYWTEPEEFRPERFS
KKKDSIDPYIYTPFGTGPRNCIGMRFALMNMKLALIRVLQNFSFKPCKETQIPLKLDTQG
LLQPEKPIVLKVDSRDGTLSGE
Enzyme 59 Number of Residues 502
Enzyme 59 Molecular Weight 57109
Enzyme 59 Theoretical pI 9.09
Enzyme 59 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • tetrapyrrole binding
  • transition metal ion binding
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 59 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 59 Specific Function Not Available
Enzyme 59 Pathways Not Available
Enzyme 59 Reactions Not Available
Enzyme 59 Pfam Domain Function
Enzyme 59 Signals
  • None
Enzyme 59 Transmembrane Regions
  • None
Enzyme 59 Essentiality Not Available
Enzyme 59 GenBank ID Protein Not Available
Enzyme 59 UniProtKB/Swiss-Prot ID A4D289 Link Image
Enzyme 59 UniProtKB/Swiss-Prot Entry Name A4D289_HUMAN Link Image
Enzyme 59 PDB ID Not Available
Enzyme 59 Cellular Location Not Available
Enzyme 59 Gene Sequence Not Available
Enzyme 59 GenBank Gene ID CH236956 Link Image
Enzyme 59 GeneCard ID A4D289 Link Image
Enzyme 59 GenAtlas ID Not Available
Enzyme 59 HGNC ID Not Available
Enzyme 59 Chromosome Location Not Available
Enzyme 59 Locus Not Available
Enzyme 59 SNPs SNPJam Report Link Image
Enzyme 59 General References
  1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
Enzyme 59 Metabolite References Not Available
Enzyme 60 [top]
Enzyme 60 ID 15177
Enzyme 60 Name Cytochrome P450
Enzyme 60 Synonyms
  1. SubName: Cytochrome P450, family 4, subfamily X, polypeptide 1
  2. SubName: Cytochrome P450, family 4, subfamily X, polypeptide 1, isoform CRA_b
Enzyme 60 Gene Name CYP4X1
Enzyme 60 Protein Sequence >Cytochrome P450
MEFSWLETRWARPFYLAFVFCLALGLLQAIKLYLRRQRLLRDLRPFPAPPTHWFLGHQKF
IQDDNMEKLEEIIEKYPRAFPFWIGPFQAFFCIYDPDYAKTLLSRTDPKSQYLQKFSPPL
LGKGLAALDGPKWFQHRRLLTPGFHFNILKAYIEVMAHSVKMMLDKWEKICSTQDTSVEV
YEHINSMSLDIIMKCAFSKETNCQTNSTHDPYAKAIFELSKIIFHRLYSLLYHSDIIFKL
SPQGYRFQKLSRVLNQYTDTIIQERKKSLQAGVKQDNTPKRKYQDFLDIVLSAKDESGSS
FSDIDVHSEVSTFLLAGHDTLAASISWILYCLALNPEHQERCREEVRGILGDGSSITWDQ
LGEMSYTTMCIKETCRLIPAVPSISRDLSKPLTFPDGCTLPAGITVVLSIWGLHHNPAVW
KNPKVFDPLRFSQENSDQRHPYAYLPFSAGSRNCIGQEFAMIELKVTIALILLHFRVTPD
PTRPLTFPNHFILKPKNGMYLHLKKLSEC
Enzyme 60 Number of Residues 509
Enzyme 60 Molecular Weight 58874.6
Enzyme 60 Theoretical pI 8.62
Enzyme 60 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 60 General Function Involved in monooxygenase activity
Enzyme 60 Specific Function Not Available
Enzyme 60 Pathways Not Available
Enzyme 60 Reactions Not Available
Enzyme 60 Pfam Domain Function
Enzyme 60 Signals
  • None
Enzyme 60 Transmembrane Regions
  • None
Enzyme 60 Essentiality Not Available
Enzyme 60 GenBank ID Protein 55664877 Link Image
Enzyme 60 UniProtKB/Swiss-Prot ID Q5VVE5 Link Image
Enzyme 60 UniProtKB/Swiss-Prot Entry Name Q5VVE5_HUMAN Link Image
Enzyme 60 PDB ID Not Available
Enzyme 60 Cellular Location Not Available
Enzyme 60 Gene Sequence >1530 bp
ATGGAATTCTCCTGGCTGGAGACGCGCTGGGCGCGGCCCTTTTACCTGGCGTTCGTGTTC
TGCCTGGCCCTGGGGCTGCTGCAGGCCATTAAGCTGTACCTGCGGAGGCAGCGGCTGCTG
CGGGACCTGCGCCCCTTCCCAGCGCCCCCCACCCACTGGTTCCTTGGGCACCAGAAGTTT
ATTCAGGATGATAACATGGAGAAGCTTGAGGAAATTATTGAAAAATACCCTCGTGCCTTC
CCTTTCTGGATTGGGCCCTTTCAGGCATTTTTCTGTATCTATGACCCAGACTATGCAAAG
ACACTTCTGAGCAGAACAGATCCCAAGTCCCAGTACCTGCAGAAATTCTCACCTCCACTT
CTTGGAAAAGGACTAGCGGCTCTAGACGGACCCAAGTGGTTCCAGCATCGTCGCCTACTA
ACTCCTGGATTCCATTTTAACATCCTGAAAGCATACATTGAGGTGATGGCTCATTCTGTG
AAAATGATGCTGGATAAGTGGGAGAAGATTTGCAGCACTCAGGACACAAGCGTGGAGGTC
TATGAGCACATCAACTCGATGTCTCTGGATATAATCATGAAATGCGCTTTCAGCAAGGAG
ACCAACTGCCAGACAAACAGCACCCATGATCCTTATGCAAAAGCCATATTTGAACTCAGC
AAAATCATATTTCACCGCTTGTACAGTTTGTTGTATCACAGTGACATAATTTTCAAACTC
AGCCCTCAGGGCTACCGCTTCCAGAAGTTAAGCCGAGTGTTGAATCAGTACACAGATACA
ATAATCCAGGAAAGAAAGAAATCCCTCCAGGCTGGGGTAAAGCAGGATAACACTCCGAAG
AGGAAGTACCAGGATTTTCTGGATATTGTCCTTTCTGCCAAGGATGAAAGTGGTAGCAGC
TTCTCAGATATTGATGTACACTCTGAAGTGAGCACATTCCTGTTGGCAGGACATGACACC
TTGGCAGCAAGCATCTCCTGGATCCTTTACTGCCTGGCTCTGAACCCTGAGCATCAAGAG
AGATGCCGGGAGGAGGTCAGGGGCATCCTGGGGGATGGGTCTTCTATCACTTGGGACCAG
CTGGGTGAGATGTCGTACACCACAATGTGCATCAAGGAGACGTGCCGATTGATTCCTGCA
GTCCCGTCCATTTCCAGAGATCTCAGCAAGCCACTTACCTTCCCAGATGGATGCACATTG
CCTGCAGGGATCACCGTGGTTCTTAGTATTTGGGGTCTTCACCACAACCCTGCTGTCTGG
AAAAACCCAAAGGTCTTTGACCCCTTGAGGTTCTCTCAGGAGAATTCTGATCAGAGACAC
CCCTATGCCTACTTACCATTCTCAGCTGGATCAAGGAACTGCATTGGGCAGGAGTTTGCC
ATGATTGAGTTAAAGGTAACCATTGCCTTGATTCTGCTCCACTTCAGAGTGACTCCAGAC
CCCACCAGGCCTCTTACTTTCCCCAACCATTTTATCCTCAAGCCCAAGAATGGGATGTAT
TTGCACCTGAAGAAACTCTCTGAATGTTAG
Enzyme 60 GenBank Gene ID AL450996 Link Image
Enzyme 60 GeneCard ID CYP4X1 Link Image
Enzyme 60 GenAtlas ID CYP4X1 Link Image
Enzyme 60 HGNC ID HGNC:20244 Link Image
Enzyme 60 Chromosome Location 1
Enzyme 60 Locus 1p33
Enzyme 60 SNPs SNPJam Report Link Image
Enzyme 60 General References
  1. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 60 Metabolite References Not Available
Enzyme 61 [top]
Enzyme 61 ID 15178
Enzyme 61 Name Cytochrome P450, family 3, subfamily A, polypeptide 43, isoform CRA_e
Enzyme 61 Synonyms
  1. SubName: Putative uncharacterized protein CYP3A43
Enzyme 61 Gene Name CYP3A43
Enzyme 61 Protein Sequence >Cytochrome P450, family 3, subfamily A, polypeptide 43, isoform CRA_e
MDLIPNFAMETWVLVATSLVLLYIYGTHSHKLFKKLGIPGPTPLPFLGTILFYLRGLWNF
DRECNEKYGEMWGLYEGQQPMLVIMDPDMIKTVLVKECYSVFTNQMPLGPMGFLKSALSF
AEDEEWKRIRTLLSPAFTSVKFKEMVPIISQCGDMLVRSLRQEAENSKSINLKDFFGAYT
MDVITGTLFGVNLDSLNNPQDPFLKNMKKLLKLDFLDPFLLLISLFPFLTPVFEALNIGL
FPKDVTHFLKNSIERMKESRLKDKQKHRVDFFQQMIDSQNSKETKSHKALSDLELVAQSI
IIIFAAYDTTSTTLPFIMYELATHPDVQQKLQEEIDAVLPNKAPVTYDALVQMEYLDMVV
NETLRLFPVVSRVTRVCKKDIEINGVFIPKGLAVMVPIYALHHDPKYWTEPEKFCPESRF
SKKNKDSIDLYRYIPFGAGPRNCIGMRFALTNIKLAVIRALQNFSFKPCKETQIPLKLDN
LPILQPEKPIVLKVHLRDGITSGP
Enzyme 61 Number of Residues 504
Enzyme 61 Molecular Weight 57756.3
Enzyme 61 Theoretical pI 8.25
Enzyme 61 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • electron carrier activity
  • heme binding
  • ion binding
  • iron ion binding
  • metal ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • transition metal ion binding
Process
  • metabolic process
  • oxidation reduction
Component
Enzyme 61 General Function Involved in monooxygenase activity
Enzyme 61 Specific Function Not Available
Enzyme 61 Pathways Not Available
Enzyme 61 Reactions Not Available
Enzyme 61 Pfam Domain Function
Enzyme 61 Signals
  • None
Enzyme 61 Transmembrane Regions
  • None
Enzyme 61 Essentiality Not Available
Enzyme 61 GenBank ID Protein 41471310 Link Image
Enzyme 61 UniProtKB/Swiss-Prot ID Q75MK2 Link Image
Enzyme 61 UniProtKB/Swiss-Prot Entry Name Q75MK2_HUMAN Link Image
Enzyme 61 PDB ID Not Available
Enzyme 61 Cellular Location Not Available
Enzyme 61 Gene Sequence >1515 bp
ATGGATCTCATTCCAAACTTTGCCATGGAAACATGGGTTCTTGTGGCTACCAGCCTGGTA
CTCCTCTATATTTATGGGACCCATTCACATAAACTTTTTAAGAAGCTGGGAATTCCTGGG
CCAACCCCTCTGCCTTTTCTGGGAACTATTTTGTTCTACCTTAGGGGTCTTTGGAATTTT
GACAGAGAATGTAATGAAAAATACGGAGAAATGTGGGGGCTGTATGAGGGGCAACAGCCC
ATGCTGGTCATCATGGATCCCGACATGATCAAAACAGTGTTAGTGAAAGAATGTTACTCT
GTCTTCACAAACCAGATGCCTTTAGGTCCAATGGGATTTCTGAAAAGTGCCTTAAGTTTT
GCTGAAGATGAAGAATGGAAGAGAATACGAACATTGCTATCTCCAGCTTTCACCAGTGTA
AAATTCAAGGAAATGGTCCCCATCATTTCCCAATGTGGAGATATGTTGGTGAGAAGCCTG
AGGCAGGAAGCAGAGAACAGCAAGTCCATCAACTTGAAAGATTTCTTTGGGGCCTACACC
ATGGATGTAATCACTGGCACATTATTTGGAGTGAACTTGGATTCTCTCAACAATCCACAA
GATCCCTTTCTGAAAAATATGAAGAAGCTTTTAAAATTGGATTTTTTGGATCCCTTTTTA
CTCTTAATATCACTCTTTCCATTTCTTACCCCAGTTTTTGAAGCCCTAAATATCGGTTTG
TTTCCAAAAGATGTTACCCATTTTTTAAAAAATTCCATTGAAAGGATGAAAGAAAGTCGC
CTCAAAGATAAACAAAAGCATCGAGTAGATTTCTTTCAACAGATGATCGACTCCCAGAAT
TCCAAAGAAACAAAGTCCCATAAAGCTCTGTCTGATCTGGAGCTTGTGGCCCAGTCAATT
ATCATCATTTTTGCTGCCTATGACACAACTAGCACCACTCTCCCCTTCATTATGTATGAA
CTGGCCACTCACCCTGATGTCCAGCAGAAACTGCAGGAGGAGATTGACGCAGTTTTACCC
AATAAGGCACCTGTCACCTACGATGCCCTGGTACAGATGGAGTACCTTGACATGGTGGTG
AATGAAACGCTCAGATTATTCCCAGTTGTTAGTAGAGTTACGAGAGTCTGCAAGAAAGAT
ATTGAAATCAATGGAGTGTTCATTCCCAAAGGGTTAGCAGTGATGGTTCCAATCTATGCT
CTTCACCATGACCCAAAGTACTGGACAGAGCCTGAGAAGTTCTGCCCTGAAAGTAGGTTC
AGTAAGAAGAACAAGGACAGCATAGATCTTTACAGATACATACCTTTTGGAGCTGGACCC
CGAAACTGCATTGGCATGAGGTTTGCTCTCACAAACATAAAACTTGCTGTCATTAGAGCA
CTGCAGAACTTCTCCTTCAAACCTTGTAAAGAGACTCAGATCCCACTGAAATTAGACAAT
CTACCAATTCTTCAACCAGAAAAACCTATTGTTCTAAAAGTGCACTTAAGAGATGGGATT
ACAAGTGGACCCTGA
Enzyme 61 GenBank Gene ID AC011904 Link Image
Enzyme 61 GeneCard ID CYP3A43 Link Image
Enzyme 61 GenAtlas ID CYP3A43 Link Image
Enzyme 61 HGNC ID HGNC:17450 Link Image
Enzyme 61 Chromosome Location 7
Enzyme 61 Locus 7q21.1
Enzyme 61 SNPs SNPJam Report Link Image
Enzyme 61 General References
  1. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  2. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 61 Metabolite References Not Available
Enzyme 62 [top]
Enzyme 62 ID 15221
Enzyme 62 Name cDNA FLJ77672
Enzyme 62 Synonyms Not Available
Enzyme 62 Gene Name Not Available
Enzyme 62 Protein Sequence >cDNA FLJ77672
MESALPAAGFLYWVGAGTVAYLALRISYSLFTALRVWGVGNEAGVGPGLGEWAVVTGSTD
GIGKSYAEELAKHGMKVVLISRSKDKLDQVSSEIKEKFKVETRTIAVDFASEDIYDKIKT
GLAGLEIGILVNNVGMSYEYPEYFLDVPDLDNVIKKMININILSVCKMTQLVLPGMVERS
KGAILNISSGSGMLPVPLLTIYSATKTFVDFFSQCLHEEYRSKGVFVQSVLPYFVATKLA
KIRKPTLDKPSPETFVKSAIKTVGLQSRTNGYLIHALMGSIISNLPSWIYLKIVMNMNKS
TRAHYLKKTKKN
Enzyme 62 Number of Residues 312
Enzyme 62 Molecular Weight 34325
Enzyme 62 Theoretical pI 9.79
Enzyme 62 GO Classification Not Available
Enzyme 62 General Function Not Available
Enzyme 62 Specific Function Not Available
Enzyme 62 Pathways Not Available
Enzyme 62 Reactions Not Available
Enzyme 62 Pfam Domain Function Not Available
Enzyme 62 Signals
  • None
Enzyme 62 Transmembrane Regions
  • None
Enzyme 62 Essentiality Not Available
Enzyme 62 GenBank ID Protein 158258687 Link Image
Enzyme 62 UniProtKB/Swiss-Prot ID A8K9B0 Link Image
Enzyme 62 UniProtKB/Swiss-Prot Entry Name A8K9B0_HUMAN Link Image
Enzyme 62 PDB ID Not Available
Enzyme 62 Cellular Location Not Available
Enzyme 62 Gene Sequence >939 bp
ATGGAGAGCGCTCTCCCCGCCGCCGGCTTCCTGTACTGGGTCGGCGCGGGCACCGTGGCC
TACCTAGCCCTGCGTATTTCGTACTCGCTCTTCACGGCCCTCCGGGTCTGGGGAGTGGGG
AATGAGGCGGGGGTCGGCCCGGGGCTCGGAGAATGGGCAGTTGTCACAGGTAGTACTGAT
GGAATTGGAAAATCATATGCAGAGGAGTTAGCAAAGCATGGAATGAAGGTTGTCCTTATC
AGCAGATCAAAGGATAAACTTGACCAGGTTTCCAGTGAAATAAAAGAAAAATTCAAAGTG
GAGACAAGAACCATTGCTGTTGACTTTGCATCAGAAGATATTTATGATAAAATTAAAACA
GGCTTGGCTGGTCTTGAAATCGGCATCTTAGTGAACAACGTGGGAATGTCGTATGAGTAT
CCTGAATACTTTTTGGATGTTCCTGACTTGGACAATGTGATCAAGAAAATGATAAATATT
AATATTCTTTCTGTTTGTAAGATGACACAATTGGTACTGCCTGGCATGGTGGAAAGATCC
AAAGGGGCTATTCTGAACATTTCATCTGGCAGTGGCATGCTCCCTGTCCCACTCTTGACC
ATCTATTCTGCAACCAAGACTTTTGTAGATTTCTTCTCTCAGTGCCTCCATGAGGAGTAT
AGGAGCAAGGGCGTCTTTGTGCAGAGTGTCCTGCCATACTTCGTAGCTACAAAACTGGCT
AAAATCCGGAAGCCAACTTTGGATAAGCCCTCTCCGGAGACGTTTGTGAAGTCTGCAATT
AAAACAGTCGGCCTGCAATCCCGAACCAATGGATACCTGATCCATGCTCTTATGGGCTCG
ATAATCTCAAACCTGCCTTCTTGGATTTATTTGAAAATAGTCATGAATATGAACAAGTCT
ACACGGGCTCACTATCTGAAGAAAACCAAGAAGAACTAA
Enzyme 62 GenBank Gene ID AK292625 Link Image
Enzyme 62 GeneCard ID A8K9B0 Link Image
Enzyme 62 GenAtlas ID Not Available
Enzyme 62 HGNC ID Not Available
Enzyme 62 Chromosome Location Not Available
Enzyme 62 Locus Not Available
Enzyme 62 SNPs Not Available
Enzyme 62 General References Not Available
Enzyme 62 Metabolite References Not Available
Enzyme 63 [top]
Enzyme 63 ID 16420
Enzyme 63 Name cDNA, FLJ93689, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B7 (UGT2B7), mRNA
Enzyme 63 Synonyms Not Available
Enzyme 63 Gene Name Not Available
Enzyme 63 Protein Sequence >cDNA, FLJ93689, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B7 (UGT2B7), mRNA
MSVKWTSVILLIQLSFCFSSGNCGKVLVWAAEYSHWMNIKTILDELIQRGHEVTVLASSA
SILFDPNNSSALKIEIYPTSLTKTELENFIMQQIKRWSDLPKDTFWLYFSQVQEIMSIFG
DITRKFCKDVVSNKKFMKKVQESRFDVIFADAIFPCSELLAELFNIPFVYSLSFSPGYTF
EKHSGGFIFPPSYVPVVMSELTDQMTFMERVKNMIYVLYFDFWFEIFDMKKWDQFYSEVL
GRPTTLSETMGKADVWLIRNSWNFQFPYPLLPNVDFVGGLHCKPAKPLPKEMEDFVQSSG
ENGVVVFSLGSMVSNMTEERANVIASALAQIPQKVLWRFDGNKPDTLGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFADQPDNIAHMKARGAAVRVDFNTM
SSTDLLNALKRVINDPSYKENVMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAA
HDLTWFQYHSLDVIGFLLVCVATVIFIVTKCCLFCFWKFARKAKKGKND
Enzyme 63 Number of Residues 529
Enzyme 63 Molecular Weight 60721
Enzyme 63 Theoretical pI 8.45
Enzyme 63 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 63 General Function Carbohydrate transport and metabolism
Enzyme 63 Specific Function Not Available
Enzyme 63 Pathways Not Available
Enzyme 63 Reactions Not Available
Enzyme 63 Pfam Domain Function
Enzyme 63 Signals
  • None
Enzyme 63 Transmembrane Regions
  • None
Enzyme 63 Essentiality Not Available
Enzyme 63 GenBank ID Protein Not Available
Enzyme 63 UniProtKB/Swiss-Prot ID B2R810 Link Image
Enzyme 63 UniProtKB/Swiss-Prot Entry Name B2R810_HUMAN Link Image
Enzyme 63 PDB ID Not Available
Enzyme 63 Cellular Location Not Available
Enzyme 63 Gene Sequence Not Available
Enzyme 63 GenBank Gene ID AK313190 Link Image
Enzyme 63 GeneCard ID B2R810 Link Image
Enzyme 63 GenAtlas ID Not Available
Enzyme 63 HGNC ID Not Available
Enzyme 63 Chromosome Location Not Available
Enzyme 63 Locus Not Available
Enzyme 63 SNPs Not Available
Enzyme 63 General References Not Available
Enzyme 63 Metabolite References Not Available
Enzyme 64 [top]
Enzyme 64 ID 16465
Enzyme 64 Name cDNA, FLJ93424, highly similar to Homo sapiens cytochrome P450, family 2, subfamily A, polypeptide 6 (CYP2A6), mRNA (Cytochrome P450, family 2, subfamily A, polypeptide 6)
Enzyme 64 Synonyms Not Available
Enzyme 64 Gene Name CYP2A6
Enzyme 64 Protein Sequence >cDNA, FLJ93424, highly similar to Homo sapiens cytochrome P450, family 2, subfamily A, polypeptide 6 (CYP2A6), mRNA (Cytochrome P450, family 2, subfamily A, polypeptide 6)
MLASGMLLVALLVCLTVMVLMSVWQQRKSKGKLPPGPTPLPFIGNYLQLNTEQMYNSLMK
ISERYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVVFSN
GERAKQLRRFSIATLRDFGVGKRGIEERIQEEAGFLIDALRGTGGANIDPTFFLSRTVSN
VISSIVFGDRFDYKDKEFLSLLRMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFQL
LQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFI
GGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYMEAVIHEIQ
RFGDVIPMSLARRVKKDTKFRDFFLPKGTEVYPMLGSVLRDPSFFSNPQDFNPQHFLNEK
GQFKKSDAFVPFSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVGF
ATIPRNYTMSFLPR
Enzyme 64 Number of Residues 494
Enzyme 64 Molecular Weight 56518
Enzyme 64 Theoretical pI 9.69
Enzyme 64 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen
  • tetrapyrrole binding
  • transition metal ion binding
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 64 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 64 Specific Function Not Available
Enzyme 64 Pathways Not Available
Enzyme 64 Reactions Not Available
Enzyme 64 Pfam Domain Function
Enzyme 64 Signals
  • None
Enzyme 64 Transmembrane Regions
  • None
Enzyme 64 Essentiality Not Available
Enzyme 64 GenBank ID Protein Not Available
Enzyme 64 UniProtKB/Swiss-Prot ID B2R7F6 Link Image
Enzyme 64 UniProtKB/Swiss-Prot Entry Name B2R7F6_HUMAN Link Image
Enzyme 64 PDB ID Not Available
Enzyme 64 Cellular Location Not Available
Enzyme 64 Gene Sequence Not Available
Enzyme 64 GenBank Gene ID AK312964 Link Image
Enzyme 64 GeneCard ID B2R7F6 Link Image
Enzyme 64 GenAtlas ID Not Available
Enzyme 64 HGNC ID Not Available
Enzyme 64 Chromosome Location 19
Enzyme 64 Locus 19q13.2
Enzyme 64 SNPs SNPJam Report Link Image
Enzyme 64 General References Not Available
Enzyme 64 Metabolite References Not Available
Enzyme 65 [top]
Enzyme 65 ID 16466
Enzyme 65 Name cDNA, FLJ93938, Homo sapiens cytochrome P450, family 2, subfamily C, polypeptide 18(CYP2C18), mRNA (HCG39167, isoform CRA_b)
Enzyme 65 Synonyms Not Available
Enzyme 65 Gene Name Not Available
Enzyme 65 Protein Sequence >cDNA, FLJ93938, Homo sapiens cytochrome P450, family 2, subfamily C, polypeptide 18(CYP2C18), mRNA (HCG39167, isoform CRA_b)
MDPAVALVLCLSCLFLLSLWRQSSGRGRLPSGPTPLPIIGNILQLDVKDMSKSLTNFSKV
YGPVFTVYFGLKPIVVLHGYEAVKEALIDHGEEFSGRGSFPVAEKVNKGLGILFSNGKRW
KEIRRFCLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTNASPCDPTFILGCAPCNVICS
VIFHDRFDYKDQRFLNLMEKFNENLRILSSPWIQVCNNFPALIDYLPGSHNKIAENFAYI
KSYVLERIKEHQESLDMNSARDFIDCFLIKMEQEKHNQQSEFTVESLIATVTDMFGAGTE
TTSTTLRYGLLLLLKYPEVTAKVQEEIECVVGRNRSPCMQDRSHMPYTDAVVHEIQRYID
LLPTNLPHAVTCDVKFKNYLIPKGTTIITSLTSVLHNDKEFPNPEMFDPGHFLDKSGNFK
KSDYFMPFSAGKRMCMGEGLARMELFLFLTTILQNFNLKSQVDPKDIDITPIANAFGRVP
PLYQLCFIPV
Enzyme 65 Number of Residues 490
Enzyme 65 Molecular Weight 55711
Enzyme 65 Theoretical pI 7.22
Enzyme 65 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • heme binding
  • ion binding
  • iron ion binding
  • monooxygenase activity
  • oxidoreductase activity
  • tetrapyrrole binding
  • transition metal ion binding
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 65 General Function Secondary metabolites biosynthesis, transport and catabolism
Enzyme 65 Specific Function Not Available
Enzyme 65 Pathways Not Available
Enzyme 65 Reactions Not Available
Enzyme 65 Pfam Domain Function
Enzyme 65 Signals
  • None
Enzyme 65 Transmembrane Regions
  • None
Enzyme 65 Essentiality Not Available
Enzyme 65 GenBank ID Protein Not Available
Enzyme 65 UniProtKB/Swiss-Prot ID B2R8K2 Link Image
Enzyme 65 UniProtKB/Swiss-Prot Entry Name B2R8K2_HUMAN Link Image
Enzyme 65 PDB ID Not Available
Enzyme 65 Cellular Location Not Available
Enzyme 65 Gene Sequence Not Available
Enzyme 65 GenBank Gene ID AK313403 Link Image
Enzyme 65 GeneCard ID B2R8K2 Link Image
Enzyme 65 GenAtlas ID Not Available
Enzyme 65 HGNC ID Not Available
Enzyme 65 Chromosome Location Not Available
Enzyme 65 Locus Not Available
Enzyme 65 SNPs Not Available
Enzyme 65 General References Not Available
Enzyme 65 Metabolite References Not Available
Enzyme 66 [top]
Enzyme 66 ID 16500
Enzyme 66 Name cDNA FLJ45935 fis, clone PLACE7003985, highly similar to Estradiol 17-beta-dehydrogenase 1 (Hydroxysteroid (17-beta) dehydrogenase 1)
Enzyme 66 Synonyms Not Available
Enzyme 66 Gene Name HSD17B1
Enzyme 66 Protein Sequence >cDNA FLJ45935 fis, clone PLACE7003985, highly similar to Estradiol 17-beta-dehydrogenase 1 (Hydroxysteroid (17-beta) dehydrogenase 1)
MARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSL
ETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTV
RMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVH
LSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEV
FLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGG
GAGPGAEDEAGRSAVGDPELGDPPAAPQ
Enzyme 66 Number of Residues 328
Enzyme 66 Molecular Weight 34980
Enzyme 66 Theoretical pI 5.42
Enzyme 66 GO Classification
Function
  • catalytic activity
  • estradiol 17-beta-dehydrogenase activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH-OH group of donors
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
  • steroid dehydrogenase activity
Process
  • cellular lipid metabolism
  • estrogen biosynthesis
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
  • steroid biosynthesis
  • steroid metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 66 General Function Lipid transport and metabolism
Enzyme 66 Specific Function Not Available
Enzyme 66 Pathways Not Available
Enzyme 66 Reactions Not Available
Enzyme 66 Pfam Domain Function
Enzyme 66 Signals
  • None
Enzyme 66 Transmembrane Regions
  • None
Enzyme 66 Essentiality Not Available
Enzyme 66 GenBank ID Protein Not Available
Enzyme 66 UniProtKB/Swiss-Prot ID B3KXS1 Link Image
Enzyme 66 UniProtKB/Swiss-Prot Entry Name B3KXS1_HUMAN Link Image
Enzyme 66 PDB ID 1QYX Link Image
Enzyme 66 PDB File Show
Enzyme 66 3D Structure
Enzyme 66 Cellular Location Not Available
Enzyme 66 Gene Sequence Not Available
Enzyme 66 GenBank Gene ID AK127832 Link Image
Enzyme 66 GeneCard ID B3KXS1 Link Image
Enzyme 66 GenAtlas ID Not Available
Enzyme 66 HGNC ID Not Available
Enzyme 66 Chromosome Location 17
Enzyme 66 Locus 17q11-q21
Enzyme 66 SNPs SNPJam Report Link Image
Enzyme 66 General References Not Available
Enzyme 66 Metabolite References Not Available
Enzyme 67 [top]
Enzyme 67 ID 16501
Enzyme 67 Name cDNA, FLJ93594, Homo sapiens hydroxysteroid (17-beta) dehydrogenase 2 (HSD17B2),mRNA (Hydroxysteroid (17-beta) dehydrogenase 2)
Enzyme 67 Synonyms Not Available
Enzyme 67 Gene Name HSD17B2
Enzyme 67 Protein Sequence >cDNA, FLJ93594, Homo sapiens hydroxysteroid (17-beta) dehydrogenase 2 (HSD17B2),mRNA (Hydroxysteroid (17-beta) dehydrogenase 2)
MSTFFSDTAWICLAVPTVLCGTVFCKYKKSSGQLWSWMVCLAGLCAVCLLILSPFWGLIL
FSVSCFLMYTYLSGQELLPVDQKAVLVTGGDCGLGHALCKYLDELGFTVFAGVLNENGPG
AEELRRTCSPRLSVLQMDITKPVQIKDAYSKVAAMLQDRGLWAVINNAGVLGFPTDGELL
LMTDYKQCMAVNFFGTVEVTKTFLPLLRKSKGRLVNVSSMGGGAPMERLASYGSSKAAVT
MFSSVMRLELSKWGIKVASIQPGGFLTNIAGTSDKWEKLEKDILDHLPAEVQEDYGQDYI
LAQRNFLLLINSLASKDFSPVLRDIQHAILAKSPFAYYTPGKGAYLWICLAHYLPIGIYD
YFAKRHFGQDKPMPRALRMPNYKKKAT
Enzyme 67 Number of Residues 387
Enzyme 67 Molecular Weight 42786
Enzyme 67 Theoretical pI 8.62
Enzyme 67 GO Classification
Function
  • catalytic activity
  • electron transporter activity
  • oxidoreductase activity
  • transporter activity
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 67 General Function Lipid transport and metabolism
Enzyme 67 Specific Function Not Available
Enzyme 67 Pathways Not Available
Enzyme 67 Reactions Not Available
Enzyme 67 Pfam Domain Function
Enzyme 67 Signals
  • None
Enzyme 67 Transmembrane Regions
  • None
Enzyme 67 Essentiality Not Available
Enzyme 67 GenBank ID Protein Not Available
Enzyme 67 UniProtKB/Swiss-Prot ID B2R7T4 Link Image
Enzyme 67 UniProtKB/Swiss-Prot Entry Name B2R7T4_HUMAN Link Image
Enzyme 67 PDB ID Not Available
Enzyme 67 Cellular Location Not Available
Enzyme 67 Gene Sequence Not Available
Enzyme 67 GenBank Gene ID AK313109 Link Image
Enzyme 67 GeneCard ID B2R7T4 Link Image
Enzyme 67 GenAtlas ID Not Available
Enzyme 67 HGNC ID Not Available
Enzyme 67 Chromosome Location 16
Enzyme 67 Locus 16q24.1-q24.2
Enzyme 67 SNPs SNPJam Report Link Image
Enzyme 67 General References Not Available
Enzyme 67 Metabolite References Not Available